diff --git "a/data/SwissProtV3/valid_set.jsonl" "b/data/SwissProtV3/valid_set.jsonl"
new file mode 100644--- /dev/null
+++ "b/data/SwissProtV3/valid_set.jsonl"
@@ -0,0 +1,10000 @@
+{"protein": "MSFVNIRSSRGPVVKVCGLQSLKAAQCALDSDADLLGIICVPGRERTVDPVVAMEISALVRACRTSMSTPKYLVGVFRNQSKEDVLRIANDYGIDIVQLHGDEPWQEYQKFLGLPVIKRLVFPRDCDILLSTPSEKTHLFMPLFDSEAGGTGELLDWNSISDWFAEQGNPECLQFMLAGGLTPENVSDALQLHGVIGVDVSGGVETNGMKDMDKITNFVRNAKKES", "text": "SIMILARITY: Belongs to the TrpF family."}
+{"protein": "MKKFMNFFSSNEFLKMIMSTIYLPTPVNINYMWNFGSILGIFLMIQIISGFILSMHYCPNIDIAFWSITNIMKDMNSGWLFRLIHMNGASFYFLMMYIHISRNLFYCSYKLNNVWGIGIMILLMSMAAAFMGYVLPWGQMSYWGATVITNLLSAIPYIGDTIVLWIWGGFSINNATLNRFFSLHFILPLLILFMVILHLFALHLTGSSNPLGSNFNNYKISFHPYFSIKDLLGFYIILFIFMFINFQFPYHLGDPDNFKIANPMNTPTHIKPEWYFLFAYSILRAIPNKLGGVIGLVMSILILYIMIFYNNKMMNNKFNMLNKIYYWMFINNFILLTWLGKQLIEYPFTNINMLFTTTYFLYFFLNFYLSKLWDNLIWNSPLN", "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": "MVMIRLARMGARKQPYYRIVVIEKRSARNGRSLEVVGTYNPRTNPASVELKRDRIDYWTGKGAQMSDRVAKLVQQNPAPAAA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
+{"protein": "MTRSAPAASATSRTAIGSAGAPAADARRALGARAEDAVVAHLAAQGVEIVARNARVGRLEIDVVARDGPVIAIIEVRTRGAGSYVRALDSIDARKRARVRRAGERLWRATFSRVRGVERMRFDAASVTFLPSGEATVEIIKAAF", "text": "SIMILARITY: Belongs to the UPF0102 family."}
+{"protein": "MSRQILVTSALPYANGSIHLGHLVEYIQTDIWVRFQKMRGTNCRYMCADDTHGTAIMLRAEKEAITPEALIQRVWAEHTRDFAGFHIGFDHYYSTHSDENREHASKIYLALKDAGLIEVKTIAQLYDPVKNLFLPDRFIKGECPKCGAADQYGDNCEVCGATYSPTELKNPVSAVSGATPVHKDSEHYFFKLGDCEAFLREWTTSGTLQAEAANKMQEWFAAGLNNWDISRDAPYFGFEIPDAPGKYFYVWLDAPVGYMASFARYAKDHGLDFDAWWGKDSKTELVHFIGKDILYFHALFWPAMLKFSGHRLPTAVYAHGFLTVNGQKMSKSRGTFITASSYLDQGLNPEWLRYYYAAKLNGTMEDIDLNLDDFVARVNSDLVGKFINIASRTAGFIHKKFDGKLADGVGNIELIGEFQAAADTIAAHYEARDYAKALREIMALADRANQYVADEKPWELAKDDAAVYRLHEVCTVALNLFRLLTLYLKPVLPKLAGEVERFLDIPALTWKDARSLFIRQAINAYSHLMTRIDPKSIEAMVDANKQNLEPTPAPAPARHAEAQAHAAQAVEAPKTETISIDDFAKVDLRIARIANAEHVEGADKLLRLTLDVGELGPRQVFAGIKSAYAPEALVGRLTVMVANLAPRKMKFGMSEGMVLAASNPDGHKDDVPGLFILSPDSGAEPGMKVK", "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": "MTRQYFGTDGVRGKVGTSPITPDFVMRLGYAAGTVLTKSRKASSRPVVLIGKDTRISGYMLEAALEAGFSAAGVDVMLAGPMPTPAIAYLTRALRLSAGVVISASHNPYEDNGIKFFSASGNKLPDAIELEIEAALNEPMSCVASEKLGRAKRLDDARGRYIEFCKSTFPNELDLRGTKLVVDCAHGAAYHIAPDVFHELGAEVIAIGNQPNGFNINEGYGATAPAALVEAVRANQAHLGIALDGDADRLLVVDAAGRVYNGDELLYIMVKDRMRVRPIEGAVGTLMTNMALEVAFKEMGVGFARANVGDRYVLEVLRERGWQVGGEGSGHMLCLDKHTTGDGIVSALQILSALKRSGLSLAELTQDIEMFPQTLINVKVEPGFDWKKNKELLAEKEAVEAELGDKGRVLIRASGTEPLIRVMVEAKDADIADKMARRIAAKLSK", "text": "FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family."}
+{"protein": "MRYLPKSPADREAMLREIGAASIDELFAIIPEEFRLTRDLAIPRQMGESEIVDHFQAAAARNANGYASFLGAGAYRHYRPVLIDTIVQRGEFLTSYTPYQAEITQGTLQAIFEFQTMICELTGMDIANASMYDGSTGAAEAVMMAIRVTGRDKVLVSRSVHPEYREVMHTYAQHQGHDAAEVEYIREGAQAGRVDLAALEAAVTEETACVLVQSPNFFGVIEDIPAIAEIAHKKGALLIVSIAEALSLGAVRPPVEADIVSLEAQSFGVALSYGGPYCGVLAAKEKYLRQMPGRLVGETKDSQGRRGFVLTLSTREQHIRREKATSNICTNQALVALMATVYMTIYGKQGIKDLALQNLAKADYAAKTLGQSGKLLFAGSPRFHEFVLETSETPAQVNERLLEEKIIGGLPLGKWYPELGHAALWCATEVTTREQIDRAAQVLAHAPALAAR", "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": "MMMSNRVLVAMSGGVDSSVAALMLKEQGYEVIGAHMRIWYREEDEELYEQNVKGCCSLAAVHDAKRVADKIGIPFYVLNFKEPFYDWVVKNFIDEYLQGRTPNPCIACNRFIKWEEFLKRAMALECDYIATGHYSKIVYDNLKNRYLLYRGKDKTKDQSYMLSQLTQEQLARTLFPLGDYYKEDVRNIAEQNELGVADKPDSQEICFVPNNDYGEFLQSVVPEHINPGPILDAQGNKLGEHKGIAFYTIGQRRGLGISLGRPVYVIDIDADNNALIVGDKEELYSDGLIAEEINLIPYEQIENSIDIECKIRYNSRNVSSTLQPYGNDQLLVKFNQPVEAVTPGQGVTFYQDDLVIGGGTILKATTKK", "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": "MEAKAIARHLRVTPMKARRVVDLVRGKQATEALAILKFAQQGASEPVYKLVTSAVANARVKADREGQAFDEDALYITEAFVDEGPTMKRFQPRAQGRAYRINKRTSHVTVVVASKDEKGGN", "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": "MSTIRSIHAREILDSRGNPTLEAEVILEDGSFGRAAVPSGASTGTKEAVELRDGDKTRYLGKGVRKAVDNVNTTIAAALKGFEATDQAGLDRRLIDLDGTENKGRLGANALLGVSMAAAHAAAASNKQALWQYLAARTGVTPSLPVPMMNIINGGAHADNNVDFQEFMVLPVGFTSFSEALRAGTEIFHSLKSVLKGHGLSTAVGDEGGFAPDFRSNVEALDTILEAIGKAGYTAGEDVLLGLDVASSEFFENGKYNLVGENKRLTSEQFVDFLADWAAQYPIITIEDGLAENDWAGWKLLTDRIGKKVQLVGDDLFVTNPKIFQEGIDSGTANAILIKVNQIGTLSETLEAIAMADRAGYAAVVSHRSGETEDTTIADIAVATTATQIKTGSLCRSDRVAKYNQLLRIEEALGAGARYAGRDAFVSLKR", "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": "MGRYIGPLTKVSRRLGVFVGGDIESFQKRNFPPGQHGRTQGRKKLSDYGVRLQEKQKLRFLYGGIREGQFKRYFERASKAAGNTGTVLLQLLERRLDNVVYRLGFAKTRLQARQLVKHGHFLVNGKKVDIPSYELDKGDIIEVREKSKKLEVFKENLESRDPRSVPRWLEIDKDNFRGKVVEIPEEIELEIPVNVQYIIEYYSM", "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": "MAAWDLLFRRVHLATFAGDEPYGALRDGALAVRTGRIEWLGAERDLPREARAAQEIDGAGGWLLPGLIDCHTHLVHAGNRAREFELRMQGANYEEIARAGGGIRVTVIATRAADEAALVVASRPRLARLIAEGVTTVEIKSGYGLELSAERRMLRAARALGDTAPVRVTTTFLGAHALPPEYDGRADDYIAEVCDVMLPALYREGLVDAVDAFCERIAFSPAQTEAVFRAARALGLPVRLHAEQLSDSGGAALAARYGALCADHLEHLSEAGAAALAAAGSVAVLLPGAFYFLRETHLPPAARLRALGVPVAIATDCNPGTSPLSSLLLALNMACVLFRLSPAAALAGVTRNAARALGRGDDLGTLEAGKLADLGLWNVDTPAELCYHLGYNPLALRVFGGQISGAGDVAQG", "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": "MRTEGDSWDITTSVGSTALFVATARALEAQKSDPLVVDPYAEAFCRAVGGSWADVLDGKLPDHKLKSTDFGEHFVNFQGARTKYFDEYFRRAAAAGARQVVILAAGLDSRAYRLPWPDGTTVFELDRPQVLDFKREVLASHGAQPRALRREIAVDLRDDWPQALRDSGFDAAAPSAWIAEGLLIYLPATAQERLFTGIDALAGRRSHVAVEDGAPMGPDEYAAKVEEERAAIAEGAEEHPFFQLVYNERCAPAAEWFGERGWTAVATLLNDYLEAVGRPVPGPESEAGPMFARNTLVSAARV", "text": "FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. SIMILARITY: Belongs to the UPF0677 family."}
+{"protein": "MTSQDALKKQAAEKAVEYLESGMVVGLGSGSTATFAIHAIARLMKEGKLKDIVGIPSSTPTEEVARSLGIPLVGFEEHAVIDVTIDGADEVDPDLNLIKGGGGALLREKVVAQATKKNIIIVDESKISDKLGTIFALPVEVVPFATASETRFLESLGAKVTVRENQLGKAFKTDNHNRILDADFGPMDDAVKIGMALSQRAGVVEHGLFLGTTALVIVAGADGIREMKAA", "text": "FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. SIMILARITY: Belongs to the ribose 5-phosphate isomerase family."}
+{"protein": "MSLLQFSGLFVVWLLCTLFIATLTWFEFRRVRFNFNVFFSLLFLLTFFFGFPLTSVLVFRFDVGVAPPEILLQALLSAGCFYAVYYVTYKTRLRKRTTDVPRRPLFTMNRVETNLTWVILMGIALVSVGIFFMHNGFLLFRLNSYSQIFSSEVSGVALKRFFYFFIPAMLVVYFLRQDSKAWLFFLVSTVAFGLLTYMIVGGTRANIIIAFAIFLFIGIIRGWISLWMLAAAGVLGIVGMFWLALKRYGMNVSGDEAFYTFLYLTRDTFSPWENLALLLQNYDNIDFQGLAPIVRDFYVFIPSWLWPGRPSMVLNSANYFTWEVLNNHSGLAISPTLIGSLVVMGGALFIPLGAIVVGLIIKWFDWLYELGNRETNRYKAAILHSFCFGAIFNMIVLAREGLDSFVSRVVFFIVVFGACLMIAKLLYWLFESAGLIHKRTKSSLRTQVEG", "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": "MKTLLLTLVVVTIVCLDLGYTLKCNQLIPIASKTCPAGKNLCYKMFMMSDLTIPVKRGCIDVCPKNSLLVKYVCCNTDRCN", "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": "MAKKVVAEVKLQLPAGKATPAPPVGPALGQRGVNIMEFCKRFNAETADKAGMILPVIITVYEDRSFSFVVKTPPASFLLKRAAGLEKGSGEPKRKNVGKVTRKQLEEIAKIKMPDITANDLEAAVKIVEGTAKSMGIEIVD", "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": "MSDRIRVRYAPSPTGYLHIGNARTALFNYLYAKHYNGDFVIRIEDTDKKRNLEDGETSQFDNLKWLGLDWDESVDKDNGYGPYRQSERQHIYQPLIDQLLAEDKAYKCYMTEEELEAEREAQIARGEMPRYGGQHAHLTEEQRQQFEAEGRQPSIRFRVPQNQTYSFDDMVKGNISFDSNGIGDWVIVKKDGIPTYNFAVAIDDHYMQISDVIRGDDHISNTPKQIMIYEAFGWEPPRFGHMSLIVNEERKKLSKRDGQILQFIEQYRDLGYLPEALFNFIALLGWSPEGEEEIFSKEEFIKIFDEKRLSKSPAFFDKQKLAWVNNQYMKQKDTETVFQLALPHLIKANLIPEVPSEEDLSWGRKLIALYQKEMSYAGEIVPLSEMFFKEMPALGEEEQQVINGEQVPELMTHLFSKLEALEPFESAEIKKTIKEVQKETGIKGKQLFMPIRVAVTGQMHGPELPNTIEVLGKEKVLNRLKQYK", "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": "MNLYDVIKKPVITEGSMAQYEAGKYVFEVDTRAHKLLIKQAVEAAFEGVKVANVNTINVKPKAKRVGRYTGFTNKTKKAIVTLTADSKAIELFGAEEE", "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": "MQEFKQHTGLAVPLDSANVDTDQIIPKQFLQRVSKLGFGQNLFHDWRFLDEAGTQPNPEFVLNFPRYKGASILLARENFGNGSSREHAPWALADYGLKAVIAPSFADIFYGNSLNNGLLVVRLKDDEVDALFKLVEANEGQNITVDLEAKEVRAADYCFKFEIDDFRRYCIMNGLDNIGLTLQHADAIDAYEAKQPVWL", "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": "MAGKGKTAARTLEDLTLDSGYGGAADSFRSSSVSLCCSDTHLSYAHGGNCWHLTESMHSRHNSLDTVNTVLAEDTEILECSGQCAKLPELEEDVPWSLGEVEGALRKDEELCVGNASREILAKLSALVSRALVRIAREAQRMSLRYARCTKHEIQSAIKMVLSWTISVNCITAALSALSLYNMSTGDKFSRGKSTRCGLIFSVGKFFRWMVDSRVALRIHEHAAIYLSACMESLFREVFTRVQRSALVEKENGVPKFSVESLEQAINNDSELWGLLQPYQHLICGKNASGVLSLPDSLNLHRDQQRAGKTGEGHAYSQAELRTIEQSLLATRVGSIAELSDLVSRAMHHLQPLHIKNPSNGTPVHQNRTGSVHWEPEALYTLCYFMHCPQMEWENPNVEPSKITLHTERPFLVLPPLMEWIRVAVAHTEHRRSFSVDSDDVRQAARLLLPGVDCEPRQLKADDCFCATRKLDAASTEAKFLQDLGFRMLNCGRTDLVKQAVNLLGPDGINSMSEQGMTPLMYSCVRGDEAMVQMLLDAGADINSEVPSSLHKHPSVYPDTRQGTPLTFAVLHGHVPVVQLLLDARANVEGAIQESTENYTETPLQLASAAGNFELVSLLLERGADPLIGTTYRNGISSGPLGEMNSYSLAAAHGHRNVFRKLLSQVEKDKGDVLSLEEMLAEGSEAVERRAPQNEGTLRTGKAKLRALREAMYHSAEHGHVDITIDIRSLGVPWTLHTWLESLRTCFVQQRRPLIQGLLKDFSCIKEDEYTEELITHGLPLMFQILRASKNEVISQQLSVIFTQCYGPFPIPKLTEIKKKQTSRLDPHFLNNKEMSDVTFLVEGKPFYAHKVLLFTASPRFKSLLSNRPAAENTCIEISHVKYNIFQLVMQYLYCGGTESLHIRNTEIMELLSAAKFFQLDALQRHCEIICSKNITNDSCVDIYKHARFLGALELAGFIEGFFLKNMVLLIELENFKQLLYEVPADSPGPGPSYDVLHDLEQTLALRIRSIHLSTSKGSIV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
+{"protein": "MAKVLVLYYSMYGHIETMAHAIAEGANKVDGVEVVIKRVPETMNAEAFLKAGGKTQNAPQATPQELADYDAIIFGTPTRFGNMSGQMRTFLDQTGGLWATGALYGKLASVFSSTGTGGGQEQTITSTWTTLAHHGMVIVPIGYGAQELFDVSAVRGGTPYGATTIAGGDGSRQPSQEELAIARFQGEHVAGLAKKLNG", "text": "SIMILARITY: Belongs to the WrbA family."}
+{"protein": "MLGLKEKICLYGFNNLTKTLSFNIYDICYAKTEREKEDYIKYIDEQYNSERLTKILCDVTEMIGAHVLNISKQDYEPQGASVNVLITEEALPVALIDPSCNKGELSYLELRDSVVGHLDKSHLTVHTYPEFHPNNDIISFRVDIDVSTCGKISPLNALDYLIGSFDSDVITIDYRVRGFTRDVDGRKCYIDHDIKSIQDYIDEETLKKYDAMDVNVYQSNIFHTKMMLKDIGLNNYLFNSDPYELSPNDRREIRDRISKEMIEIYGGVNIY", "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": "MRIINAEGLILGRLASRVAKMLLEGEEVVIVNAEKAVITGNREVIFSKYKQRTGLRTLTNPRRGPFYPKRSDEIVRRTIRGMLPWKTDRGRKAFKRLKVYVGIPKEFKDKQLETIVEAHVSRLSRPKYVTVGEVAKFLGGKF", "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": "MSKRTTYCGLVTEELLNQKVTLKGWVHNRRDLGGLIFVDLRDREGIVQIVFNPDFSEEALSVAETVRSEYVVEVEGTVTKRDPDTVNSKIKTGQVEVQVSNISIINKSETPPFSINEENQNVDENIRLKYRYLDLRRPELAQTFKMRHQTTRAIREYLDNNGFFDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVIQMGEEMLRKVVKDVKGIDVSGPFPRMTYEEAMRRYGSDKPDTRFEMELKDVSQLGREMDFKVFKDTVENNGEVKAIVAKGAADNYTRKDMDALTEFVNIYGAKGLAWVKVVDDGLSGPIARFFEDSNVATLKDLTQAESGDLVMFVADKPNVVAQSLGALRIKIAKELGLIDENKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKQEDISKLDSEPQNAQANAYDIVLNGYELGGGSIRIADGELQEKMFEVLGFTKEQAREQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTDAPGEVSDKQLEELSLRIRH", "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": "MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLVDILGASGAENVQGEVQQKLDLFANEKLKAALRARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRVTPVGTPVTEEDFLQPGNKQVAAGYVVYGSSTMLVYTTGCGVHAFTYDPSLGVFCLCQERMRFPEKGNTYSINEGNYIKFPQGVKKYIKYCQEEDKATQRPYTSRYIGSLVADFHRNLLKGGIYLYPSTASHPEGKLRLLYECNPMAFLAEQAGGKASDGKERILDIIPESLHQRRSFFVGNNHMVEDVENFIKAFPDA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family."}
+{"protein": "MQSFEKEFLKPRSINIEKISEIHSKITLEPLERGFGHTLGNALRRILLSSMPGCAITEVEIEGVLHEYGTKEGVREDVLEILLNLKTLAINMYVKDSIVLTLKKTGIGPVIASDIEYDSSIISIVNPNHIICCITDQDTSIIMRIKVQRGRGYVPAFSRFSSDDQHDLPIGRLLLDACYSPVERISYTVEAARVEKRTDLDKLIIDMETNGTIDPEEAIRRAATILSDQLSSFIDLKDVHQPEVKEEKPEFDPSLLNLVDDLELTVRSANCLKAESIHYIGDLVQKTEVELLKTPNLGKKSLTEIKDVLASRGLSLGMRLDNWPPKHLSEQ", "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": "MTNPTKPIPLNFDKPRRFMPPKHFADLSADERIDALKELGLPKFRANQIARHYYGRLEADPSTMTDLPAAAREKVKDALFPQLMQPVRAVQADDGETQKTLWKLHDGTLLESVLMRYPNRATLCISSQAGCGMACPFCATGQGGLDRNLSTGEIVDQVRAASATMQAEGGRLSNIVFMGMGEPLANYKRVVSAVRQITAPVPEGFGISQRNVTVSTVGLAPAIRKLADEDLSVTLAVSLHTPDDELRNTLVPTNNRWEVAEVLDAARYYADRSGRRVSIEYALIRDVNDQGWRADMLGKKLHKALGPLVHVNLIPLNPTPGSKWDASPMDRQKEFVQRVIAQGVTCTVRDTRGQEIAAACGQLAAEER", "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": "MTVSREEISTILDDALFLPVKLYSLKVNQRPNHSLIEVVLDNLEHPYGSVSLLECEQVSRKLKEELERISPDLDFTLKVSSAGAERKLHLPEDIDRFRGIPVRLVFRSGESEKNQEGIFRIVNRDGDQVFLEKFQKGKKSAVKKQTTLNLKDILKGNLYVSI", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family."}
+{"protein": "MISLKNFGLLFWKRFSENKLNQVAGALTYSTMLAIVPLVMVIFSIFSAFPVFNEVTGELKEMIFTNFAPSASDMVGEYIDQFVSNSKKMSAVGIVSLIAVALMLINNIDRTLNSIWHNSQSRSPLSSFAIYWMILTLGPLIIGVSIGISSYIKIMFEQSEHLSLGLKLLSFVPFLFTWFIFTLIYTVVPNKKVKIKHSAYGAFLAAIFFTLGKQAFTWYVVTFPSYQLIYGAMATLPIMLLWIQISWLVVLVGAQLASTLDEIGEQIEQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0761 family."}
+{"protein": "MNRSEKAAIIEQLKARAEGASIAVVTDFKGMSVEELTRLRVKLRENGAEYHVVKNTLARIAFTDGAHDVIKDVFKENCAVALGFADPVAVAKAVTDFAKTSKIFTVRHGSLEGKFLSGEQVSDLAKLPSKPELIARALGTMNAVPTNFVSLFANIIRGLLYALKGIEEKKAAA", "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": "FIGDIWSGIQG", "text": "SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MPLRVIFMGTPEFSVPTLRAIAKAGHEISAVYTQPPRAAGRRGLELTPSPVQREAERLGIEVRTPTSLKGEAEQAAFNALRADIAVVVAYGLLLPKVILDAPRLGCINGHASLLPRWRGAAPIQRAIMAGDLESGMMVMRMEEGLDTGPVGLLEKCAIDPDMTAGDLHDRLMRVGAALMVEALARLAKNTLTFTAQAAEGVTYARKIDKSETRVDWTRPAAEVHNHLRGLSPFPGAWSEIDIGGRMERLKLLRSTLSDGLSPSEDLGESGGILDDRLTVACGAGAIRLVEVQRAGGKPAAASEFLRGAKIVKGMKFS", "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": "MRHRNGLRKLNRTSSHRLAMFRNLTNSLLEHEIIKTTLPKAKELRRVVEPVITLGKNPTLASKRLAFDRLRNRENVVKIFSELGPRYQNRNGGYLRILKCGFRKGDNAPMAIVELLDRSEANNDIVNIAE", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
+{"protein": "MAVTYNYGTGRRKTAVARVFIKPGSGNIVVNGKPVDEFFSRETGRMIVRQPLVLTGNEGRFDIMVNVTGGGESGQAGAVRHGITRALIDYSAELKSELRAAGFVTRDAREVERKKVGLRKARRAKQFSKR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
+{"protein": "MISAGDFRNGVTIEFEGNIYQIIEFQHVKPGKGAAFVRTKLKNIISGGVVEKTFRPTEKCPTAHIDRKDMQYLYADDDFYHFMDVETYDQIDLPKDEVGDALKFVKENEMCKVCSHKGNVFAVEPPLFVELTVTETEPGFKGDTATGATKPATVETGATVYVPLFVETDDVIKIDTRTGEYLSRV", "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": "MKAIVLLNMGGPNNLEEVELFLRNMFNDKNILPIRNDLLRKFVAYMITQGRKKEARSNYEKLGGKSPLNFYTDRLIAKLQKRLPDVYVTKAMRYTPPFAKEAIKELMYHNVREVFLIPLYPHYSTTTTKSSLEDFYNMAKGVGYHARFHDIANFYENRLYNQAIIERIEEALDGEDTKEYELVFSAHSLPQKIIEKGDPYLQEVQEHVKILTSILEEKFSGYHLAFQSKLGPVKWLEPGLDEKLEELKGKKILVYPISFTLDNSETEFELHIEYAQIAQKIGVKKYKVARCPNESDRFVDALVDIYQRM", "text": "FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferrochelatase family."}
+{"protein": "MEYTHQSSWIIPFIPLPVPILIGVGLLFFPTATKNIRRMWVFPSIFLLTIVMIFSIDLSIHQINNSSIYQYVWSWTINNDLSLEFGYLIDSLTSIMSILITTVGILVLIYSDSYMSHDQSYLRFFTYLSFFNTSMLGLVTSSNLIQVYIFWELVGMCSYLLIGFWFTRPIAANACQKAFVTNRVGDFGLLLGILGFYWITGSLEFRDLFQIFNNLIYKNEVNIFFVTLCALLLFCGSVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLLPLFIVIPSIMSGIALIGIITVVLGATLAIAQKDIKKNLAYSTMSQLGYMILALGMGSYRAALFHLITHAYSKALLFLGSGSIIHSMEAIVGYSPDKSQNMVLMGGLTKHAPITKNAFLIGTLSLCGIPPFACFWSKDGILNDSWLYSPIFAIIACSTAGLTAFYMFRIYLLVFEGYLNVHFQHFNGKKNSSFYSISLWGKEEKKKLKKKIHLLALLTMNNNERTSFFQKRAYSHRINRNVKSIRRLFLDSTHFGIKNIGFFYPQESDNTMLFSMLVLVLFTFFVGSVGISFSQEGIDLDILSKLLIPSIDLLHQNSKNSVDWYEFFTNATFSVSIAFFGILIASFFYKPVFSSLQNLNLCNLFQKGLPKKIIADKIINIIYDWSYNRGYIDAFLEVSLIASVKKLAKFNYFFDRQIIDGIPNGVGISSFFMGEAIKYVGGGRISSYIFFFLLIFLVICYSIFI", "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": "MTNVVVVGSQWGDEGKGKIVDWLSERADIVVRFQGGHNAGHTLVIDGVSYKLSLLPSGVVRPGKLAVIGNGVVIDPHALIAEIDKLGKQGVQITPDNLRIADNATLILSLHRELDGFREDAASNSGTKIGTTRRGIGPAYEDKVGRRAIRVMDLADLDTLPAKVDRLLTHHNALRRGLGEAEISHQAIMDELSSVAARVLPFMDTVWLLLDKERRKGARILFEGAQGTLLDIDHGTYPFVTSSNTVAGQAAAGSGMGPGALGYILGITKAYTTRVGEGPFPTELHDEVGQFLGERGHEFGTVTGRKRRCGWFDAALVRQSVAANGITGIALTKLDVLDGLDELKICVGYTLDGQEIDHLPASQAQQASVKPVYITLEGWKESTVGARSWADLPAQAIKYVRQVEELIGAPVALLSTSPERDDTILVTDPFED", "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": "MRKPVIAGNWKLYKTTSEALELVNELIPLVKNASGVEIVVAPVFTVLSTVKNALKGTNINLAAQDCFWDEQGAYTGEVSSTMLLDAGCSHVIIGHSERRQFFGETDETVNKKNIAALRAGLTILFCIGETLHEREENQTFTVLERQISGGISGITKDELKNVIIAYEPVWAIGTGKTATDDQAQEAHKFIRGVVAKLCDSESAENIRILYGGSVKPENVKGLMAQKDIDGALVGGASLKADSFAHIVRFSE", "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": "MALWGGRFSQGADSRFKQFNDSLRFDYRLAEQDIQGSMAWAKALVKVGVLTADEQGKLQQAMEVLLASVQQDPQQILISDAEDIHSWVESALIAAVGDLGKKLHTGRSRNDQVATDLKLWCKAQGELLLGSITALQQGLVASARANQAAVLPGYTHLQRAQPVTYAHWALAYVEMLERDYSRLQDALKRLDTSPLGCGALAGTAYAIDREALALDMGFAGATRNSLDSVSDRDHVVELMHVASLSMTHLSRFAEDLIFYNTGEAGFVELSDAVTSGSSLMPQKKNPDALELIRGKTGRVVGAQMGMLMSLKALPLAYNKDMQEDKEGLFDALDTWHDCLDMAALVLIDLKVNGERTMAAAQGGYANATELADYLVAKGIPFREAHHIVGETVVYAIQVKKPLEELTIGEFQRFSPVIEFDVYPNLELEATLAKRVAKGGVAREQVEAALIAAETWLAKRAG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
+{"protein": "MHRYRSHTCGALRDSHIDQTVRLSGWCHRIRDHGGVLFIDLRDHYGLTQCVADPDSPAFAQAEKLRSEWVVRIDGKARLRPAGTENPELPTGQIEIYINEIEVLGPADELPLPVFGEQEYPEDIRLKYRFLDLRREKLHQNIMTRGAIVDSMRKRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVEQDDVFAAVEPVVTGVFEEFAKGKPVTKNWPRIPFAESLRKYGTDKPDLRNPLLMQDVSQHFRGSGFKVFARMLEDSKNQVWAIPGPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTEAIRQQLGLKAGDAAFFVAGDPAKFWKFAGLARTKLGEELNVIDKDRFELAWIVDFPMYEYNEDEKKVDFSHNPFSMPQGGLDALNNQDPLTIKAFQYDITCNGYEIASGGIRNHRPEAMVKAFEIAGYGENDVVERFGGMYRAFQYGAPPHGGMAAGVDRVVMLLCGTTNLREISLFPMNQRAEDLLMGAPSDVTPKQLRELHIRLNLPQD", "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": "MKSKSSRTRVAILGSGSIGLDLMFKVKASEQFDLKFVVGRNANSDGLRLARSCNVETSSDGLDFLKAHEDAYDLVFDATSAAAHKVNNRFFSDAGKFVIDLTPAKVGRLCVPCINLDDMGAEQNVNLITCGGQASLPLAYALKQAVDEIDYLEVVSAIASRSAGIATRENIDEYMTTTEYALAKFSDAKKTKAILNINPAEPGVRMQTTLYAYARYRDFDRVRASVADMVEKVREYVPGYRLVVEPLESQGRITIGLTVRGRGDYLPEYAGNLDIINCAALAVASHRHATARLGATQ", "text": "SIMILARITY: Belongs to the acetaldehyde dehydrogenase family."}
+{"protein": "MKREDVLMEALPYIQKFHGRSMVIKLGGHAMVDTCIMDTVIRDVVLLQLVGIKCVIVHGGGPEITEKMKAMGKQPRFVSGLRITDDDTLEVAQMVLVGKINSKIVSLVSRAGGRAVGISGNDANLIIARKMDRQKVRVENREEEVDLGHVGEIEEIRPALLHTLLDNQFIPVISPLAIDRNGNDLNINADTAAGELAIALGAHKLISMTDVDGIMNRERTEVYRRMTPQDAEELIASGVVSEGMIPKVLAVLRALHGGVPYAHIINGNLAHNLIMELFTAEGVGTMITDRIDEV", "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": "MQSLISFAHSRLSWGILALSALALESAALYFQHIMKLDPCVMCIYQRVAVFGLLGAGLFGFMAPANRVIRALGALLWGISAAWGLKLALELVDMQNNPNPFSTCSFLPEFPSWLQLHEWLPSVFMPTGMCTDIPWEFAGVTMGEWMIVAFSVYLLAWLAFIVPMLKKSA", "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": "MARECYITGRKARSGNKRSHAMNKSKRRFGANVQKVRILVDGKPKRVYVSARALKSGKVERV", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
+{"protein": "MDRIVVKGSGPLSGQIPIAGAKNTCLKLMCAALLSDEPLTLTNVPRLSDVATLSELLESLGVQIGRLDDGQTLAFSANTLTSQLAHYDIVRKLRASFNVLGPLLGRTGQAVVSLPGGCAIGARAVDFHITGLEAMGAKIELKDGYVHAAGDLKGAEIEFPFPSVGATENVMCAAVRAKGTTVIKNAAREPDTKALADCLIAMGADIEGAGTETMIVRGVDRLHGATHRVIADRIEMGTYMCAPGIAGGEVECLGGTRALVASLCDKMEAAGLEITETDAGLKVRHPGGRLKAVDVATAPFPGFPTDLQAQFMAMMCFADGTSVLEETIFENRFMHAPELIRMGASIDVQGNTARVTGVDRLRGAPVMATDLRASVSLILAGLAADGETTVNRVYHLDRGYEHLVRKLRGVGANVERLSDG", "text": "FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily."}
+{"protein": "MATPLKLYRNIGIAAHVDAGKTTTTERVLYYTGMSHKIGEVHDGAATMDWMVQEQERGITITSAATTCYWSGMDKQFESHRINIIDTPGHVDFMIEVERSLRVLDGAVVVFDSVAGVEPQSETVWRQANKYGVPRIVFVNKMDRMGANFLRVVSQIKQRLGSTPVVLQLPIGAEEEFKGVIDLIKMKAIHWDEENKGMTFKYVDIPADLKSTCEEYRAHIIEAAAEYSEELMEKYLEGEEFTEAEIKKALRHLTITNKVVPVFCGSAFKNKGVQAVLDGVIEYLPSPTDIPDIQGVDEHGDVIHRKTSYDEPFSALAFKIATDPFVGTLTYFRAYSGILKSGDTVYNSVKGKKERIGRLLQMHANSREEIKEVRAGDIAAAVGLKTVTTGDTLCDQDKVVILERMDFPDPVIAVAVEPKTKADQEKMGIALGKLAQEDPSFRVHTDEESGQTIIQGMGELHLEIIVDRMKREFNVEANVGKPQVAYRETLKQAVEQEGKFVRQSGGRGQYGHVWLKIEPQEPGKGYEFINAIVGGVIPKEYIPAVDKGIQEQMQNGVIAGYPVVDVKVTLFDGSFHEVDSSEMAFKIAGSQCFKQGALKAKPVLLEPIMSVEVVTPEDYMGDVMGDLNRRRGLVQGMEDSPAGKIVRAEVPLAEMFGYSTDLRSATQGRATYTMEFCKYAEAPTNIAEAIIKKQ", "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": "MAKAKFERSKPHVNIGTIGHVDHGKTTLTAAITTVLAKAGGAEARGYDQIDAAPEERERGITISTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRQVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYGFPGDDIPVIKGSALKALQGEADWEAKIIELMAEVDAYIPTPERETDKPFLMPVEDVFSITGRGTVATGRVERGIVKVGDVVEIIGLAEENASTTVTGVEMFRKLLDQAQAGDNIGALLRGVAREDIQRGQVLAKSGSVKAHAKFKAEVFVLSKEEGGRHTPFFANYRPQFYFRTTDVTGIIQLPEGTEMVMPGDNVEMTIELIAPIAIEEGTKFSIREGGRTVGYGVVATIVE", "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": "MSDSKNLNQERQKALDSAISQIEKAFGRGAIMKLKQGAIEKIDSISTGSIALDTALGIGGFPKGRIVEIFGPESSGKTTLALHVIAESQKKGGNCAFIDAEHALDIMYARKLGVNTGDLIVSQPDTGEQALHIVEYLVCSGAIDVIVVDSVAALTPRAEIEGDMGDQHMGLQARLLSHALRKLTSIVSKANCVLIFINQIRMKIGVVYGNPETTTGGNALKFYSSVRLDIRKVSAIKDKDVIIGNQTKVKVVKNKVAPPFKQVDFDIMYNEGISKVGEIIDMGVKLNIIEKAGSYYSYNSVRLGQGKENAKSYLKANCDTAHEIEQKIRSILASDNEVSCFNAEVNDNLHEVEETVF", "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": "MVESVVKNWQGEQVGQKTFELRVAKETTAAHIVHRALVRQQTNARQGTASTKTRAEVRGGGRKPWRQKGTGRARAGSIRSPLWRGGGVIFGPKPRDFDLKMNRKERRLALRTALVSRIDDLILVEEFSNELSRPKTKDLVAAFTRWGAEPESKILLILSEFPENVYLSARNIENLKLIAADQLNVYDLLHADKIVVTTSALEKIQEVYNG", "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": "MSNIGKVVQVIGPVVDIKFDEENLPDIYNAISIESGNAKIITEVAQHLGDDIVRTISMESTDGLMRGMDALDIGAPISVPVGKPVLGRLFNMLGQPIDENGEVEADEYSPIHRPAPSFEDQSVKPEMFETGIKVIDLIAPYQKGGKIGLFGGAGVGKTVIIQELINNIAKEHGGLSVFTGVGERTREGNDLYYEMQESGVINKTALVFGQMNEPPGARMRVALTGLTMAEHFRDEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKHGSITSVQAVYVPADDLTDPAPATTFTHLDATTVLSRSISEIGIYPAVDPLASTSRILDPRVVGEEHYKVASDVKHILERYSELQDIIAILGVDELSEEDRLVVIRARRIQRFLSQPFSVAEQFTGYEGKYVPIKETIRGFKEILEGKYDDLPETAFLFKGSIDEVIESAKNMVKS", "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": "MANTPSAKKRAKQAEKRRSHNASLRSMVRTYIKNVVKAIDAKDLEKAQAAFTAAVPVIDRMADKGIIHKNKAARHKSRLSGHIKALSTAAA", "text": "FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family."}
+{"protein": "MSFDLPDIILRPASLLYKNIIRIRNRLYDQQIFHTWHSPLPIVSIGNISAGGTGKTPLVDWIVKYYLSLGCKPAIVSRGYGRNTKGVQLVSDGKTVLMKSNACGDETAMLAWNNRDAIVIVAEKRKDAVTFIIRRFAEAMPDVIILDDAFQHRQIARNLDIVVINEKEPYFRADMIPKGRLREPLINLARADLLVLSKITGGSTTAAISMDLEQTGKPVIKAGIAAGNLVCLSGMFNTAKESPVHAGIKALAFAGIGSPQSFIDTLEGQGIQIVSHRFFRDHESYTAKKIAALRLEADEKKLTLVTTEKDYFRMLGQPELQEILHTLSCCYLKIRPEFTEGEKLLKTMLNAVINR", "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": "MSRRRRVSRRPVVSDGGPGGVLLARFINVVMSRGKKALAERIVSGALKMAESKSTGETGVSIFNTAVSNVMPRMEVRSRRVGGVTYQIPVEVREDRSTSLALRWIVKAARTNRKRTNKTYMSCLCNELLEAYNKRGSACKMKEEKFRMAEANKAFSHFRF", "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": "MKLHEYQAKGLFRDYGVSVPDGIVAETVDAAVDAARRLEEENDATLFIVKAQIHAGGRGKGGGVKLAHSVEEVREHADNILGMDLVTHQTGPEGQTVRKILVTEGVDIDQEYYLGVTLDRETSMNAIMVSTEGGVDIETVAEESPEKIQRVWVDPSIGLRPFQTRQLAFAMGLEGDAFKQAVASIQGLYEAFEENDCTLAEINPLVQTPGGDIEAVDAKVNLDDNALFRHPDLEEMRDLHEEDPTEVKAGEHGLSYITLDGNVGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGAASAETVEAGFRIILEDPNVEALLLNIFGGIVRCDRVAQGVIEAAKNIDIDVPLIVRLQGTNAEEGKRLLDESDLSLRSAVLLKEAADEVTAALGED", "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": "MNDMSRVERAVESKQTKMECRDCHVYYGDTHAIKNVNVDIADKTVTAFIGPSGCGKSTFLRCLNRMNDTIAGARVQGSFQLDGEDIYDKRVDPVQLRAKVGMVFQKPNPFPKSIYDNVAYGPRIHGLARNRAEMDEIVEKALRRGAIWDEVKDRLDAPGTGLSGGQQQRLCIARAIATEPEVLLMDEPCSALDPIATAQVEELIDELRQNYSVVIVTHSMQQAARVSQKTAFFHLGQLVEYGETGQIFTNPEDPRTESYITGRIG", "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": "MKSVTSLGVFGNPIAHSLSPRIHALFAQTRQDSINYQRYLSTPGHFPRRVAEFFRHGGQGANVTLPFKQQAASLVTKLSDRARLAGAVNTLIPYGNGLLLGDNTDGEGLIIDLKNKGLNVSERSLAVFGAGGSARGIIPLLLEQKPRCLYLVNRTAKKAEMLKSQLETLGLVAANRIQVRSSASEIDEPIDLLINATSSSLNGQRLTLPPLLSENASGYDLMYADQPTVFMEQLTQAGCKNVSDGFGMLIEQAASSYQLWMGDERPDTAFVMAEMRTPS", "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": "MFLMNMLCLIIPILLAMAFLTLVERKILGYMQLRKGPNIVGPYGLLQPIADAIKLFIKEPLRPLTSSKLMFTLAPMLAFSLALSMWIPMPMPHPLIHLNLGVLFILALSSLAVYSILWSGWASNSKYALIGALRAVAQTISYEVTLAIILLSTMMMNGSFTLSTLTTTQEHMWLIFPLWPLAMMWFISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFALFFMAEYTNIIMMKALTTTLFLGALHNPLLPELFTANFVTKTLALTMAFLWIRASYPRFRYDQLMHLLWKSFLPLTLALCMLHVSLPTVSAGIPPHM", "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": "MLTNRQLLILQVIVNDFIRSAQPVGSRTLSKKEDITFSSATIRNEMADLEELGFIEKTHSSSGRIPSEKGYRYYVDHLLSPGKLSKTDLNIIHSIFKEKIFELEKAVQKSAQVLSDLTNYTSIVLGPRLSENHLKQIQIVPIQPKKAVAILVTNTGHVENKTINFPAEVDLSDLEKLVNILNERLRGVPISELKDRIFKEVVIFLKSHIQNYDTILHALGATLDSSVQTDRLFFGGKINMLNQPEFHDIDRVKSLLSLIEKEQEILRLFQSTESGITIKIGKENDYEEMENCSLITATYTVGSKQIGSIAVIGPTRMDYSRVVGLLQHVSSDLSKALTSLYDG", "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": "MTSTTSFTRADGRAQDQMRTVKITRGFTTNPAGSVLIEFGNTRVMCTASVELGVPRFKRDSGEGWLTAEYAMLPAATAERNRRESMAGKVKGRTHEISRLIGRSLRAAVDLSQLGENTIAIDCDVLQADGGTRTAAITGAYVALADAIRVLKEQGVVPGDPLLPPVAAVSVGLIDGQPCLDLPYEEDVRADVDMNVVMTESGEFVEIQGTGEETTFTRAQLNEMLDIAEKGCRELVHAQKAALGI", "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": "MAELATIARPYAEALFRVAKAADLNGWSELVSEMAQVAAHPDVYALAHNPKISDDVISSAFISALKSPVGAEAKNFINMLVQNDRLTLLPEIATQFHALKNAQEGAADAEIVSAFELSAAQLTELVATLEKKFGRKLNPTVAVDSALIGGVRVVVGDEVLDTSVRAKLQQMQVALTA", "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": "MAGQKIRIRLKAYDHEAIDASARKIVETVVRTGANVVGPVPLPTEKNVYCVIRSPHKYKDSREHFEMRTHKRLIDILDPTPKTVDALMRIDLPASVDVNIQ", "text": "FUNCTION: Involved in the binding of tRNA to the ribosomes. SIMILARITY: Belongs to the universal ribosomal protein uS10 family."}
+{"protein": "MALNKKGAKRRRKKVCAFCADKSSSIDYKDVNKLRKYVTERGKILPRRISGNCAKHQRELTLAIKRARNVALLPFTTD", "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": "MRNKYIESFEKAQLENRNIPEFRAGDTVKVAVRIKEGSKERVQNYEGLCIAIRGQGTGRTFMVRKMGANSVGVERIFPLYSDSIESIEVLRKGRVRRAKLFYLRELKGKAARIKELRRK", "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": "MFNLRNFDVIVVGAGHAGTEAAMASSRMGCKTLLLTQKISDLGALSCNPAIGGIGKSHLVKEIDALGGMMAKAIDYSGIQFRILNSSKGPAVRSTRAQADKILYHETVKKILKKQNNLLILEAEVKDLIFKNYSVVGVLTQNEINFYSRSVVLAAGTFLGGKIHIGLKSYSAGRIGDKSAIDLSVRLRELSLRVNRLKTGTPPRIDINTVNFNNLLIQNSDTPVPVFSFMGNVSHHPKQIPCYLTHTNEKTHEIIRKNLDKSPIYTGFLKGLGPRYCPSIEDKIVRFPDRKSHQVFLEPEGLSSIKVYPNGISTSLPIEVQEQIVASIKGLEKSKIIRPGYAIEYDFFDPKDLNLTLESKLIKGLFFAGQINGTTGYEEAASQGLLAGLNAALSSKNTEGWFPRRDQAYLGVLIDDLTTQGTEEPYRMFTSRAEYRLSLREDNADLRLTEIGRKLGLVNDSRWIRYNQKVLNIQTEMNRLKKNKISPISPDADILKKLYNINLIKEISMSELLKRPQIRYQDLQSLESFRTGIVDLEAIGQIENEIKYAGYIKRQSEEIERHLKNENTFLSSIYDYNKIRGLSSEVVKKLNDYKPISIGQASRISGITPAAISILLIHLKKESYKHTL", "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": "MPRYALRIEYDGGPFAGWQRQAAQASVQGAIETALGRLEPGPHTIAAAGRTDTGVHASGQVAHCDLVREWDPFRLAGALNAHLKPLPVAIVAAARVPEEFHARFSAVERRYLFRLLARRAPEVHDRGRVWRVPHPLDPEAMRAGAAHLVGRHDFTTFRAAGCQAASPVKTLDALTLETVEGMNGTEYRFHLRARSFLHNQVRSIVGTLERVGAGAWTPDQVREALDARDRAACGPVSPPQGLYLTGVGYPADPFA", "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": "MDLKLKDCEFWYSLHGQVPGLLDWDMRNELFLPCTTDQCSLAEQILAKYRVGVMKPPEMPQKRRPSPDGDGPPCEPNLWMWVDPNILCPLGSQEAPKPSGKEDLTNISPFPQPPQKDEGSNCSEDKVVESLPSSSSEQSPLQKQGIHSPSDFELTEEEAEEPDDNSLQSPEMKCYQSQKLWQINNQEKSWQRPPLNCSHLIALALRNNPHCGLSVQEIYNFTRQHFPFFWTAPDGWKSTIHYNLCFLDSFEKVPDSLKDEDNARPRSCLWKLTKEGHRRFWEETRVLAFAQRERIQECMSQPELLTSLFDL", "text": "SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MNIIDQVKQTLIEEITASVKAAGLAEEVPEVKVEIPKDPKNGDYSTNIAMVLTKIAKRNPHEIAQAIVDHLDKSKANVEKIEIAGPGFINFYLNNQYLTAVIPEALEKDKDFGRNEDPKHQKVLVEYVSANPTGDLHIGHARNAAVGDTLSNILDAAGYDVTREYYINDAGNQITNLAHSIEARYDQAMGKETELPADGYYGKDIINIGKDLAEKRPELKDLPEDERLKVFRQLGVDYEMEKLKKDLADFNTHFDGWFSETTLYDKGEIKKVLELMKENGYTYEADGATWLRTTDFNDDKDRVIIKKDGSYTYFLPDVAYHYDKFHRDGGQDILINLFGADHHGYINRLKASVETYGIDADRLEIQIMQMVRLMQDGEEVKMSKRTGNAITLREIMDEVGIDAARYFLTMRSPDTHFDFDMELAKENSAENPVYYAQYAHARISSILKQAGERGITPSENADFSVITNDKAIDLLKKVAEFEPMIESAAEHRAPHRVTNYIQELASAFHKFYNADKVLTDDEKKTQAYVSMIAAVQITLRNALALVGVSAPHNM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
+{"protein": "MTEKEHFFWNKLLELAKEELTQATFDYYVLDTKLIKIQDNVATILLEEVKKLFWEKNMQSFILMTGFEVYNSEIKVEYVFDEALVSETKPTLANNDFSNKREQQTPDLPTLNSDLNSKYTFDNFIQGDENRWSVAASLAVADSPGATYNPLFIYGGPGLGKTHLLNAIGNKVLHDNPQARIKYITAENFINEFVLHIRLDKMDELKLKYRHLDVLLIDDIQSLAKKSTQATQEEFFNTFNVLHDNNKQIVLTSDRNPDQLNEMEERLVTRFKWGLTVNITPPDFETRVAILTNKIMDYDYHFPPETIEYLAGQFDSNVRDLEGALKDISLVANVRQLDTITVEVAAEAIRARKIDGPKLTLIPIEDIQSEVGKFYNVTVKEIKATKRTQNIVLARQVAMYLAREMTDNSLPKIGKEFGGRDHSTVLHAYNKIKNMLAQDDSLRIEIDTIKNKIK", "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": "MPSFDIVSEVDKQEVRNAIDQVNKEVSTRFDFKGSDARVEQSDYALTVYADTDFQLDQVQDILSQKLSKRGVDVKCLDTGNVEKVSGNKVKRSVTVKTGVGTELAKKIVKCIKDSKLKVQASIQGETVRVSGAKRDVLQETIALVKKSVSDFPLQYQNFRD", "text": "SIMILARITY: Belongs to the UPF0234 family."}
+{"protein": "MLVIVGGTTTGILFLGPRYLPRYLPILGINGASAMKKSYFLANFLACLGLLAISSSSALLITSSPSLLAASATAPSAMTAIFTSFPLPWGSTTSSLNLFSGRLRSISLRFTATSTLCVKLRGLARALASFTASTIFCLSKAILDIPP", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MIKGINHITYSVSNIAKSIEFYRDILGADILVESETSAYFNLGGIWLALNEEKNIPRSEIKYSYTHIAFTISDNDFEDWYNWLKENEVNILEGRDRDIRDKKSIYFTDLDGHKLELHTGSLEDRLSYYKEAKPHMNFYI", "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": "MSAKFNVKTFQGMILALQDYWAQQGCTIVQPFDMEVGAGTSHPMTALRALGPEPMAFAYVQPSRRPTDGRYGENPNRLQHYYQFQVVIKPSPDNIQELYLGSLKMLGFDPTQHDIRFVEDNWENPTLGAWGLGWEVWLNGMEVTQFTYFQQVGGLECKPVTGEVTYGLERLAMYIQGVDSVYDLVYSDGPLGKTTYGDVFHQNEVEQSTYNFEYADVDFLFECFNKYEQEAKFLLKQEPRMENDKEIWVETALPLPAYERILKAAHSFNLLDARKAISVTERQRYILRIRALTKGVAEAYYASREALGFPGCK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
+{"protein": "MSLELQEHCSLKPYNTFGIDVRARLLAHARDEADVREALALARERGLPLLVIGGGSNLLLTRDVEALVLRMASQGRRIVSDAADSVLVEAEAGEAWDPFVQWSLERGLAGLENLSLIPGTVGAAPMQNIGAYGVELKDVFDSLTALDRQDGTLREFDRQACRFGYRDSLFKQEPDRWLILRVRLRLTRRERLHLDYGPVRQRLEEEGIASPTARDVSRVICAIRREKLPDPAVLGNAGSFFKNPLVDATQAERLRQAFPDLVGYPQADGRLKLAAGWLIDKGGWKGFRDGPVGVHAQQALVLVNHGGATGAQVRALAERIQEDVRRRFGVELEPEPNLY", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurB family."}
+{"protein": "MAIQIVLIVGPTASGKSKLAVDVAKEFNGEIISADSMQVYKYMDVGTAKITKEEMQGIPHYLIDIVEPDQEFSVAEYEKRAKEIIKDIYKRGKLPIIVGGTGLYINSIIYIMHFSDFEGSKEFREKMKELANTYGSQYLYEKLKSVDPEAAKKIHPNDIRRIIRALEVYEFTGKPISYYQKMSGMRLNPEYQPIMIGLNFRDRQILYDRINQRVDEMIKNNLVEEVVNLLKIGYNKDSTAMQALGYKEIVEYLKGEISLEEAIEKIKKGTRRYAKRQITWFKGYDFIKWFFVDDYKNYEELKKNIIKYLAGKLNF", "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": "MTAKLERLQRALGYTFKEPALLTLALTHRSFGGRNNERLEFLGDSVLNFIIADYLFGRFEEAREGQLSRLRARMVKGVTLAEIAREFDLGEYLRLGSGEMKSGGFRRESILADALESIIGAIYLDAGFEVCADRVLNWFEARLQKLNLKDTQKDSKTRLQEYLQARQLNLPRYEVISVQGEAHAQTFHVRCEIDGLSDATEGTGSSRRVAEQKAAKQALLALGVDQ", "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": "MRIALTNDDGIQAPGLRAIYKALIEAGHTVDVVAPVTEQSAVGHAVTIAMPLRVKVFHENGFRGHGVYGTPTDCMKLGLSSLLEHKPELVVSGINAGANVGPDILYSGTVSAATEAAHMGYRAVALSYDSFRPEDISAHARHAAALLPHIEWAGLPERCVVNINYPAVPVESIKGVRVCPQTRAVWHDWYEHRTDPRGGSYWWLNGVIPPETVAPGTDRALLTEGYITVTPLRFDFTDSETLTRLASLEE", "text": "FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SurE nucleotidase family."}
+{"protein": "MFAESPIKRRKSTRINVGNVPIGDGAPIAVQSMTNTRTTDVAATVDQINRIVAVGGEIVRVSVPTMEAAEAFKEIKKQVSVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGNMERVRSVVDCAKDKNIPIRIGVNGGSLEKDLQEKYGEPTPEALVESAMRHVDILDKLNFDQFKVSVKASDVFLAVGAYRLLAQKIDQPLHLGITEAGGQRAGAVKSAVGLGMLLAEGIGDTVRVSLAADPVEEIKVGFDILKSLRIRSRGINFIACPSCSRQEFDVIGTVNALEQRLEDILTPMDVSIIGCVVNGPGEAEVSDLGLTGARNMSGLYEDGKRVKERLPNDDLVDKLEAKIRAKAARLSEQNKIQVSVKD", "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": "MDIKIIKDKKNPLLNRRELDFIVKYEGSTPSRNDVRNKLAAMLNAPLELLVIQRIKTEYGMQESKGYAKLYEDADRMKQVEQEYVLKRNAVPGSETEGEEA", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS24 family."}
+{"protein": "MKINVINQQELREINSKKIKDIAKKVLLNEVGKGNFELNILITDDKSITEFNKYRGKSTPTDVLSFSYGLSEPVIGDIVISVESIEKQAPDFGNSFEEEFYYILIHGLLHIVGYDHENSEEDAKKMFEVQDQYFHQLIKDRRR", "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": "MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLSLMARKMKDTDTEEELIEAFKVFDRDGNGLISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGHINYEEFVRMMMAK", "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": "MASLRDIKSRITSTKKTSQITKAMQMVSAAKLNRAETNAKSFAPYMDKIQEVVFNVGKGAKNAKHPMLVSREVKKTAYLVITSDRGLAGAFNSSVLRNAYRTIQERHQSKDEYTVIAIGRVGRDFFKKREMPILSELVGLGDEVTFAQIKDLTRQTVQMFIDGAFDELHLVYNHFVSAISQEVTEKKVLPLTDFGTSGGKRTASYEFEPDEEEVLEVLLPQYAESLIYGALLDSKASEHAARMTAMKNATDNAKELIDSLSLSYNRARQAAITQEITEIVGGAAALE", "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": "MRIVITIGGSILLKEYDNKKFEDYAKIIRQINEDHEIFIVVGGGRPARDYISVVRDMGETESICDEIGIQVTRINARLLQLALKDVSYPAIPVNFQQALEFSATGKIVVMGGTEPAHSTDAVGSILAEYVGADLVINATSVDGLYDKDPNKYNDAQMFSEVSADKLMEIVSDNDTKAGTYEFIDKTAIQIIKRSKIKTVIVNGNTPENVKTAITQPIGTLITE", "text": "FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UMP kinase family."}
+{"protein": "AALPPGDAAAAQGGSNGVGPNLYGIVGRKSGTVEGFTYSKANQDSGVMWTPQVLDVYLENPKKFMPGTKMSFAGLKKPQERADLIAYLETLKD", "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": "MSQTRHVPVMLQRCLDLLAPALQDPAHPEPVVVDCTLGLGGHSEALLASFPTARLIALDRDKEALRLSGERLAPYGDRATLVHAVYDELPEVLARLGIPKVQGVLFDLGVSSMQLDEADRGFAYAQDAPLDMRMDQSTGMGAAEVLNTYPPGELVRILRAYGEEKQAKRIVSAVVREREKEPFSNSARLVELIRDALPQAAKRTGGNPAKRTFQALRIEVNGELSVLERAIPAAVDSLDVGGRIAVLSYHSLEDRLVKQVFAAGAANTAPPGLPVVPERYQPRLKQLTRGAELPTEQEVAENRRAAPARLRGAQRIRAEER", "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": "MGPPKIGQTVVVEVPSTTANIGPGFDCLGAALDLSNQFTIKRIEGNAERFELIMESTEGNHLRGGPENLFYRAAQRVWRTAGIEPVALEARVKLAVPPARGLGSSATAIVAGLVGANALAGYPLPKEKLLELAIDIEGHPDNVVPSLIGGLCVTAKTASDRWRVVRCDWDKSIKAVVAIPSIRLSTSEARRVMPENIPVNDAVINLGALTLLLQGLRTGNEDLITDGMHDKLHEPYRWGLIKGGLEVREAAKAAGALGCAISGAGPSILALCKATKGREVSVAMVKAWEAAGVASRAPLMSLQLTGSECISNTFG", "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": "PNTVIYNCSECHKRFRSKSGFVKHQKTHTGETPFVCFVCEQRFVCHSALIGHQRIHTGEKPFSCTECGKCFSRRSHLNSHHKTHTGEKSFLCFACGKCFASRSHLTAHHRTH", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MTEFDNLTWLHGKPQGSGLLKANPEDFVVVEDLGFTPDGEGEHILLRILKNGCNTRFVADVLAKFLKIHAREVSFAGQKDKHAVTEQWLCARVPGKEMPDFSAFQLEGCKVLEYARHKRKLRLGALKGNAFTLVLREISDRRDVETRLQAIRDGGVPNYFGAQRFGIGGSNLQGALRWAQSNAPVRDRNKRSFWLSAARSALFNQIVHQRLKKPDFNQVVDGDALQLAGRGSWFVATSEELPELQRRVDEKELMITASLPGSGEWGTQRAALAFEQDAIAQETVLQSLLLREKVEASRRAMLLYPQQLSWNWWDDVTVELRFWLPAGSFATSVVRELINTMGDYAHIAE", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family."}
+{"protein": "MIETDRIISANTAQTNDENVIDRAIRPKTLAEYEGQPAVREQMEIFIQAAKARKDALDHTLIFGPPGLGKTTLSNIIANEMGVELKQTSGPVLEKAGDLAALLTNLEENDVLFIDEIHRLSPVVEEILYPAMEDYQLDIMIGEGPAARSIKIDLPPFTLVGATTRAGLLTSPLRDRFGIIQRLEFYSIDDLSKIVYRSAKLLNLDITTDGAMEIAKRSRGTPRIANRLLRRVRDYAQVKGSGVICFEIADKALSMLKVDPVGFDHMDHRYLLTLMEKFAGGPVGLDTMSAALSEEKGTIEDVIEPYLIQQGYIMRTARGRIATLLAYNHFKLKIPDNLSADQQQTLSI", "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": "MFVINLLLYIVPILLAVAFLTLVERKVLGYMQFRKGPNIVGPYGLLQPIADAVKLFTKEPLRPLTSSVSMFIIAPILALTLALTIWTPLPMPHALIDLNLGLLFILSLSGLSVYSILWSGWASNSKYALIGALRAVAQTISYEVTLAIILLSIMLINGSFTLKNLIITQENMWLIVATWPLAMMWYISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFAMFFLAEYANIMAMNAMTAILFLGSSLNHNLSHLNTLSFMLKTLFLTFMFLWIRASYPRFRYDQLMHLLWKNFLPLTLALCLWFISIPIALSCIPPQI", "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": "MAAKGARMIIHLECTECKNRNYTTEKNKKNDPDRLELKKYCKFCRRHTIHRETK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
+{"protein": "MNWREIAVTVSSVGEEAVADLFYQLGCPGVSVEDPELLQSYVESGNWDYHDFGEIALTGTSVVKGYICEDHELQPKLRQLDEGLKELLQRFPEWVLQVKGLTVQEEDWATSWKAYFKPVRIGRHFLIKPSWEEVTPLPEDIILELDPGMAFGTGTHATTSLCLETLEETVKPDMRIFDLGTGSGILAIAAAKLGAQVEAIDLDSVAVKVAQENVELNQVADRISVRQGDLGTVLQGQADLVVANIIADVILMLIPDLKRIMKEDGEFLASGIIGHRSSDVEAGLGEHGLEVLEKKEDSGWVLLRARWQRASL", "text": "FUNCTION: Methylates ribosomal protein L11. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family."}
+{"protein": "MKDEHNQEHDHLSPKEPESYQKAYACKEQQGEEKQEASEKEGEIKEDFELKYQEMREQYLRVHADFENVKKRLERDKSMALEYAYEKIALDLLPVIDALLGAHKSAVEVDKESALTKGLELTMEKLHEVLARHGIEGIECLEEFDPNFHNAIMQVKSEEKENGKIVQVLQQGYKYKGRVLRPAMVSIAKND", "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": "MAQKIKKGDTVQVISGKDKGKRGEVIQVLPKEEKLIVRGVNIVKRHQRPTGQMRQGGIIEKEAPLYWSKVMLVCPSCDKATRVGFRVLEDGSKVRYCKKCGEIIDKK", "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": "MFAKLEDIERSFMDLEQELADPEVYNNQERYRKVTMAHAELGDVVAAFREYKQLSADLEDNKEMAKDSDPEIREMAEMEIAEIKDRLPKLEEELKLLLLPKDPMDGKNIILEIRAGTGGEEAALFAADLFRMYSRFAESNGWKVEVMNSNPTGTGGFKEIIAAISGSRIYSMMKYESGTHRVQRVPATETQGRIHTSAATVAIMPEAEEVDVQVRNEDLRIDVFRASGPGGQSVNTTDSAIRITHLPTGLVVICQDEKSQHKNKAKAMKVLCSRLLQAEQDKQHAEMAEQRRAQVGSGDRSERIRTYNFPQGRVTDHRINLTLYKLDAVIEGDMQELVESLISHYQSEALKQQAQDG", "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": "MSTPENPDPVDTTTQDAAAAIVAEEGTPPSESLRDEYEQLADLVRKYRYAYYQEDSPTVSDAEFDELYRRLEELEALHPELVSNDSPTQEVGGEVSSAFAAVEHLQRMYSLDDVFSLDELEAWVRKAEASVAKLGDSVPPIAWLTELKIDGLAVNLLYRDGKLVRAATRGDGTTGEDITHNVLTIKEIPRQLSGSGYPSEVEIRGEVFIPSKAFLEFNESLVAAGKAPLANPRNAAAGSLRQKDPAETAKRPLSMFVHGIGAREGLDAKSQSESYKLLEEWGLPVSPYLKVLETFDDVLKFIADYGERRHKLVHEIDGIVVKIDDFATQRALGYTSRVPRWAAAYKYPPEEVHTKLLDIAVNVGRTGRVTPFGLMEPVKVAGSTVGMATLHNQDVVKAKGVMIGDIVILRKAGDVIPEIVGPVLALRDKQEPPVREFVMPTECPSCGTPLAPAKESDVDIRCPNAKSCPSQLRERVFHVASRGAFDIEALGWEAAVALTQPAEPETPPLTSEARLFSLTREDLADVLIRREKRSKGVGTGEYELVPYFYTKGTAKSPSKPTATTEKLFAELEKAKQQPLWRVLVALSIRHVGPTASRALATAFGSMDAIRNATEEQMAHVDGVGPTIAVALKEWFAVDWHNEIVDSWAAAGVRMEDERDASVPRTLEGLTVVVTGTLPNFSRDEAKEAIIIRGGKASGSVSKNTSYLVAGESAGTKLDKAEQLGVPVLDEDGFRELLANGPAQTGTEAEAATDEATVVDETAAEAATE", "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": "MPTFRTLDEADLAGKRVLVRVDLNVPMDEGRVTDDTRIQAILPTIRAITEKGGKAILLSHFGRPKGRDASQSLAPVAAAVGERLGAPVAFAGDCIGSDAEAAVSTLAPGAVLVLENTRFHAGEEKNAADFVQQLAALGDIYVNDAFSAAHRAHASTEGLAHKLPAFAGRSMQKELEALAKALEAPQRPVLAVVGGAKVSSKLELLGNLTAKVDILVIGGGMANTFLAAKGVKVGKSLCEHDLADTARQIIATAASHGCEIVLPVDAVVTKTFAAHADHRVVPVDQVAEDEMILDAGPATVALVREKLKGAKTVVWNGPFGAFELPPFDAATVAVAKAVAEATKAGALLSVAGGGDTVAALNHAGAAGDFSYVSTAGGAFLEWLEGKQLPGVEALRR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
+{"protein": "MTIIRVKENEPFEVAMRRFKRTIEKNGLLTELRAREFYEKPTAERKRKKAAAVKRHYKRIRGQMLPKKLY", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family."}
+{"protein": "MAKKSSSRLPKRKGEYTYRGKTVSELQELSLEEFAELLPSRERRSLKRGFTDGQKKVLHEFKEGKKIRTHHRDMIILPEMIGKTIEIHNGKGFVSVDLQPEMVGHRFGEFAPTRSRVSHGSAGVGATRSSKFVPLK", "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": "MDDDLKSIASKYYIGGHISVSGGLHLAPERASIFGFRTFQFFSKNQMRWNSTPISEEEALRFISEVSSHSISSTMVHASYLINLASSSNELHQKSFNAFVEEIQRAERIDATFLTFHPGSNGNKDEGIRKIKEAIEKVETHKVKLLVENTAGQGNVIGSTIYEIGQIIDGFDSSVGVCIDTCHAWAAGYDITNKYDEFIDELDSAIGLDRIYAFHLNDAMKDLGSNIDRHELIGRGKIGEGLIKLISDVRLFGKPKIMETPYGEAKFEENLKYIRKKLGE", "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": "MRYEYVPLKDQYEKEIVPALMKEFNYKNIHQVPKLVKIVINMGIGEGSRNYDLIERHANELAKITGQKPIVTRARKSISNFKIRKGMPIGLKVTLRGARMYNFLYKLINIVLPKVRDFRGLDPNSFDGRGNYSFGLSEQLVFPELSPDEVRRIQGMDITIVTTAKTDQEARRLLELFGMPFKRG", "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": "MNIVILAGGRSAERQVSLVTGKACKRALEDLGHRAKLIDPEEDLPLRLWQERQAGCDFVWIALHGPGGEDGVVQGMLEWLGLPYQGSGPLASALAMDKLVSKQIFRAEGIPTPEWLVWDEAQPLSWAECVARLGSPLVVKPSNSGSTVGISLARDEVSLAQGLALASSVSSRVFLERYIPGKEITLSILSGQVLPAIEIIPAQGDFYDYEAKYAPGGSRHLIPCSLSAAGLARCEAAGLRAYRVLGCEGLARVDLRVDADENPWVLEVNTLPGMTPTSLCPEAAAALGWTFTELVERMLQDALQRAALTRSAPSGSRPSPQPA", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
+{"protein": "MIFDKGNVEDFDKELWDAIHAEEERQEHHIELIASENMVSKAVMAAQGSVLTNKYAEGYPGNRYYGGTECVDIVETLAIERAKKLFGAAFANVQAHSGSQANAAAYMALIEAGDTVLGMDLAAGGHLTHGSPVNFSGKTYHFVGYSVDADTEMLNYEAILEQAKAVQPKLIVAGASAYSRSIDFEKFRAIADHVGAYLMVDMAHIAGLVAAGVHPSPVPYAHIVTSTTHKTLRGPRGGLILTNDEALAKKINSAIFPGLQGGPLEHVIAAKAVAFKEALDPAFKDYAQAIIDNTAAMAAVFAQDDRFRLISGGTDNHVFLVDVTKVIANGKLAQNLLDEVNITLNKNAIPFETLSPFKTSGIRIGCAAITSRGMGVKESQTIARLIIKALVNHDQETILEEVRQEVRQLTDAFPLYKK", "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": "MAKTIAFDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNMAAGANPLGLKRGIEKAVEAVTEHLLKEAKEVETKEQIAATAGISAGDPAIGELIAEAMDKVGKEGVITVEESNTFGLQLELTEGMRFDKGFISGYFATDAERQEAVLEDAYILLVSSKISTVKDLLPLLEKVIQSGKPLAIIAEDVEGEALSTLIVNKIRGTFKSVAIKAPGFGDRRKAMLQDMAILTGGQVISEEVGLSLETAGLELLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIESSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGKVFETLNLEGDEATGANIVKVALDAPVKQIAINAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNASSIAALFLTTEAVVADKPEKAGAPVDPTGGMGGMDF", "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": "MSKFIVIEGLDGAGKSTAIGFIKKYLDSKSLAAVYTREPGGTKVAEELRSIVLHNDYDEEIHPDSELLMIYAGRIQHYRNLIAPALTKGVNVVSDRFYWSSIAYQGGGRELGVDKLNVLNETFLKDCQPDLIIYLDIDPAIGLARAGKVGSPDRIEKAGLAFFDRTRAVFKSLVAANHNAYEIDASQSIDVIEKEIYAILDKYF", "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": "MAYAVVRIRGSVGVRGSIADTLKMLRLHKVNHCVIIPNTETYNGMINKAKDFITYGEIDKDTLIKMILKRGRLSGNRRIDQETVKELMGMSVEELAEKIVNEEILLKDTPIKPVFRLHPPRKGHNKAGIKKSFTVGGALGYRGEKISELLKKMI", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
+{"protein": "MLQPKRTKFRKVQKGRNTGLAHRGSTVSFGSIAIKATERGRMTARQIEAARRTISRRIKRGGKIFIRVFPDKPITEKPLEVRMGNGKGNVEYWVCEIKPGKILYEIEGVNDELATQAFKLAAAKLPFKTTIVTRTVM", "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": "MELTPREKDKLLIFTAGLLAERRKARGLKLNYPEAVAFITCAILEGARDGRSVAELMSYGATLLSREDVMDGIAEMIPEIQVEATFPDGTKLVTVHNPIV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urease gamma subunit family."}
+{"protein": "MQKYFVEARQLLALAIPVILAQVAQTAMGFVDTVMAGGYSATDMAAVAIGTSIWLPAILFGHGLLLALTPVVAQLNGSGRRDRIAQQVRQGFWLAGFVSVLIMVVLWNAGYIISSMHNIDPLLAEKAVGYLRALLWGAPGYLFFQVARNQCEGLAKTKPGMVMGFIGLLVNIPVNYIFIYGHFGMPELGGVGCGVATASVYWVMFASMLWWVRRARSMRDIRCAERFSRPDVAVLLRLVQLGLPIALALFFEVTLFAVVALLVSPLGIIDVAGHQIALNFSSLMFVLPLSLAAAVTIRVGFRLGQGSTIDAQVSARTGVGVGVCLAVFTAIFTVLMREQIALLYNDNPEVVLLASHLMLLAAIYQISDSIQVIGSGILRGYKDTRSIFFITFTAYWVLGLPSGYLLALTDMVVPRMGPAGFWCGFIIGLTSAAIMMMLRMRFLQRQPSSIILQRAAR", "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": "MKKVGVIPNINKDKDLEVTKSVVNWLLDHGSEPYLNEIVAARIGYEKHGKKANEIYSKSDFLIALGGDGTILNVARLCAPFGTPILAVNLGHLGFLTEIDASELFPSLEKIYKGEYAIEKRMMLEANVVKNDMEVINFRALNDIVITRGAFSRMARIKAYVNDNYVDTYLADGVIVATPTGSTAYSLSAGGPIVYPTVEVIIITPICPHTLYSRSIVVSPDDVIRLEIAEENQDLMITTDGQQGYKIDYRDVIYIKKSNEYTNLIKVKNSNFFDLLRDKLTER", "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": "MILAVIGINHETASVETREQLAFSSKQVKELVQKLIEGQPIKEASVLSTCNRTEVHFTVNTGQIEAGKNHIMTYLSDFSDLDPREYVDHLYFITDQEAVSHIFKVTAGLNSLVTGETEILGQVKKAYQLSDEAGGVDSIFHGLYQQALRTGKRVHRETGINDNAASVSYASVELATKIFGSLQNRRALIIGAGKMSELAARHLYSNGVKDVIVINRTIERAKNLADKFGGLYASYDQLSEWLNEIDIVITSTGAPHFVIKEEQIKRAMKSRKYSPMFLIDIAVPRDVEPSVNNQDNAYLYTIDDLEAVVESNMQERQEEARNAELIISEEVAEFMVWYKTRDVVPLISALREKAEDVRKMELEKYHKKLKNLSPKEQEAVDKLTKSIVNKILKEPVLRIKEFAVEDKSELYMATLAQLFDLEDEVIPKDGEEHSSSKEVESVTQSSTERGHHESDFHN", "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": "QTTEILLCLSPVEVASLKEGINFFRNKSTGKDYILYKNKSRLRACKNMCKHQGGLFIKDIEDLAGRSVRCTKHNWKLDVSTMKYINPPESFCQDELVVEMDENNRLLLLELNPPNPWDLQPRSPEELAFGEVQITYLTHACMDLKLGDKRMVFDPWLIGPAFARGWWLLHEPPSDWLERLCQADLIYISHLHSDHLSYPTLKKLAGRRPDIPIYVGNTERPVFWNLNQSGVQLTNINVMPFGIWQQVDKNLRFMILMDGVHPEMDTCIIVEYKGHKILNTVDCTRPNGGRLPMKVALMMSDFAGGASGFPMTFSGGKFTEEWKAQFIKTERKKLLNYKARLVKNLQPRIYCPFAGYFVESHPSDKYIKETNTKNDPNELNNLIKKNSDVITWTPRPGATLDLGRMLKDPTDSKGIIEPPEGTKIYKDSWDFEPYLEILNAAVGDEIFLHSSWIKEYFTWAGFKDYNLVVRMIETDEDFNPFPGGYDYLVDFLDLSFPKERPQREHPYEEIHSRVDVIRHVVKNGLLWDELYIGFQTRLQRDPDIYHHLFWNHFQIKLPLTPPNWKSFLMCCEQNGPGILQFSTERTNEPNRNKFSVENKA", "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": "MIELNPVRQRITDLTDRVLSLRGYLDYDAKKERLEEVTRELESPDVWNNAEYAQNLGRERSSLEKTVGGIASVLDGLADATELLELAESEQDEDTALAVVADLDKHQAHVEKLEFQRMFSGEMDNAAAFVDIQAGAGGTEAQDWAEILLRMYLRWCESRGWKTELMEVSGGDVAGIKSATLRVEGDYAYGWLKTETGVHRLVRKSPFDSDNRRHTSFTSVFVSPEIDDNIDITINPADLRTDVYRSSGAGGQHVNKTESAVRITHIPTNIVVACQTGRSQHQNRDNAMKMLAAKLYELEIQKRNAEKDAVEATKSDIGWGSQIRNYVLDQSRIKDLRTGIERSDTQKVLDGDLDEFVEASLKAGLAVGSKRVDA", "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": "MTDLTDLTLAAALDGLKSKQFSSAEITGAFLQAMEKSRVLNAYVVETPEKAMEMARASDARIAKGEGGRLEGAPLGIKDLYCTKGVRTTACSNILGEFTPTYESTVTQNLWDEGAVMLGKLNMDEFAMGSSNETSRFGPPINPWRRKGDNAGLTPGGSSGGSAAAVSGNLCLAATASDTGGSIRQPASFTGTVGIKPTYGRASRYGMVAFASSLDQAGPIAKTVEDSALLLEIMCSHDPKDSTSLKVETPDWRSDVRKGVKGMKIGIPKEYRIEGLSEEIEALWQQGIAWLKAAGAEIVEISLPHTKYALPAYYIVAPAEASSNLARYDGMRYGARVEGNNLTQTYEASRASGFGKEVQRRLMIGTYVLSSGYYDAYYLRAQKVRAKIFQDFVGAFEQCDAILTPACPSTAFAFGEKSGDPLEMYLMDVFTVTANLAGLPGISVPAGLSASGLPLGLQVIGKALDESACFRVGGVLEDAASFVAKPDRWW", "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": "MAGNRNEEMVYCSFCGKNQEEVKKIIAGNGVFICNECVALSQEIIREETAEEVLADLAETPKPKELLDILNNYVVGQDRVKRALAVAVYNHYKRINFTESREDNDVDLQKSNILMIGPTGSGKTYLAQTLARSLNVPFAIADATSLTEAGYVGEDVENILLKLIQAADFNIERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPNQEMIQIDTKNILFIVGGAFDGIEDIVKQRLGEKIIGFGQNNKAIDDESSYMKEIVAEDIQKFGLIPEFIGRLPVLATLEQLTVDDLVRILTEPRNALVKQYQTLLSYDGVELEFDQDALEAIASKAIERKTGARGLRSIIEEVMMDVMFEIPSLEDVTKVRITKEAVDGKAAPVLETA", "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": "MQQLQSIIESAFENRATLTPATVNHETRDAVTQVINLLDSGKLRVAEKIDGQWVTHQWLKMAVLLSFRINENQIIDGTESRYFDKVPMKFSDYDQTRFEKEGFRVVPPAAARQGAFIARNCVLMPSYVNIGAYVDEGTMVDTWTTVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIIEEGSVISMGVYIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPSKDGSYSLYCAVIVKKVDAKTQGKVGINELLRSID", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
+{"protein": "MIRYFTAGESHGPALSAIVEGMPAGISIAPEDINDELARRQRGYGRGGRMNIETDTAAVLSGIRFGKTIGSPITLQIENRDWKNWTVKMAQFEQPEENIPAITIPRPGHADLTGMIKYGFQDIRPVIERASARETAARVAACSLAKVFLRHAGIQIGSYVSAIGPAGEIAPSPKMQELLSQGAASLSRAADASCVRMLDKENEEAAIAAIDKAKEDGDTLGGIIEVFITGVPLGLGTYVQHDRRLDAALAAALLSIQAVKGVEIGSAFDNARRPGSQVHDEMYVEDGSAPVRKTNRAGGIEGSMSNGQVIHLRAAMKPIATLMSPLHSFDLSSMEAHLSHIERSDTCAVPACSVIAEAVVAPILANALLEKTGGDHLEEILERLNAYKASIAKQFQT", "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": "MDVILLERVAKLGHMGDIVRVKNGYARNFLLPGGKALRATEANKKHFESQRAHLETRNQELRDQAAAIGEKLDGQTFVIIRQAGETGQLYGSVSPRDIAEAAIAAGFDVHRNQIALTTPIKTIGLHEVPVVLHPEVSVNVTVNIARSPVEAERQAKGEEINVVEETNLDELGLEIGAALADAGGSLGDR", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
+{"protein": "MDIDQARLTHLQQLEAESIHIIREVAAEFENPVMLYSIGKDSAVMLHLAKKAFYPGKPPFPLMHVDTTWKFRDMIALRDKQAKENGWDLIVHVNQDGVEAGINPFTAGSAKHTDVMKTEGLKQALNRHKFDAAFGGARRDEEKSRAKERVYSFRDKNHRWDPKNQRPELWNIYNGRIDKGESIRVFPLSNWTELDIWQYIYLENIEIVPLYFAAERPVVERDGMLIMIDDERILEYLTPEEKASIQTRKVRFRTLGCYPLTGAVESEAATLPEIIQEMLLTRTSERQGRLIDHDSAGSMEKKKMEGYF", "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": "MYFYLKYNINNMIMRRVRSFVSRNRKLTQNKRQFLKNYLLKYGIDFSCSYVNFNFIFNNEYPVILEIGFGTGEFLINMARKNLFSNFLGIEVYIPSILSCLRYIHKYNLPNVKVIFYDAVEVISYMISNNSLSEVYILFPDPWPKRRHHKRRIITKELLEVILKKLVFGGYLNIATDCQIYAKSILNIIENIKGYINLSNTGDYVIRSDYRLVTKFEKKGLVLGNKIFNLKFKSIFNNSNFL", "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": "MTGNELEIELKEPLLPVEEYLAAGVHIGTQQKSKDMMKFIYRVRGDGLYILDIQATDERIKTAAKFLSQYEPSKILVVTSRQYGQYPAKKFADAIGGMAVVGRFIPGMLTNQRLHGLNKYIEPDVVVVTDPIGDSQTIAEAVQVGIPIVALCDTNNMTKYVDVVIPTNNKGRKALSVIYYLLTKELLRLRGVATSLTPEDFETEL", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
+{"protein": "MAKKSMIAKAQRKPKFQVRAYTRCRICGRPHSVYRDFGLCRVCLRKMGSEGLIPGLRKASW", "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": "MQIKAEEISQIIEQQIQHYESRVEMSETGTVLSVGDQIARVYGVQNAMAMELLEFPGGVMGLVLNLEEDNVGVALLGEDTHIKEGDPVKRTGKIFSVPVGDAVTGRVIDPLGNPIDGLGPVEAKETRNVEIKAPGIIARKSVHEPMYTGLKAVDAMTPIGRGQRELIIGDRQTGKTAVCIDAILAQKGQGVFCFYVAIGQKKSTVALVAETLRRHGAMEYTTIISATASEPASLQFMSAYSGCTMAEYHRDNGRAALIIYDDLSKQAVSYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGAGSLTALPIIETQAGDVSAYIPTNVISITDGQVYLEPNLFNAGIRPAINVGLSVSRVGGAAQVKAMKQVAGTLRLDLAQYRELAAFAQFGSDLDKATQLKLSRGMRMVELLKQPQYKPMNVAEQVISLFAGTRGFMDDVPVEAVRKFEEGLQEYFHNAKSDILNEIQEKKALDEGLIAKLGAAIDEFKKGFKA", "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": "MLTIGVLGLQGAVREHIRSIEACGSKGVVIKRPEQLDDIDGLILPGGESTTMRRLMDTYHFMEPLREFAAQGKPMFGTCAGLIILAKEIAGTDNAHLGLLNVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAGEDVEVLCEHNGRIVAAKQGNFLGCSFHPELTDDHRVTELFVKMAEKHKQETAV", "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": "MKIGIIGATGYGGAELVRILNHHPYAEDCILYSSSDEGKEYAASYPHLRNIASQSLQPLHIETIRNEIDVMFIAAPPGVSGEWSPKLAEAGIPVIDLSGDLRIQNPAVYEKWYKRKAAPKGTIQSAVYGLAELQKEEIQTAKLIANPGCFPTAVLLGLAPLAKNGLLQDSFLIVDAKTGVSGAGRKASMGTHYSELNDNFKIYKVNEHQHTPEIEQQLAAWQPGTGPITFSAHLAPMTRGIMATMYTEAPPGMSAAQVRELYSEFYKDSYFVRIRPEGEFPATKEVYGSNFCDISVTVDERTNRATIVSVIDNLMKGAAGQAVQNLNIMNGWQEETGLTMTPVYP", "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": "MDYLDLGPYSSASGTVRLPGSKSISNRVLLLAALAEGDTTITNLLDSDDTRVMLDALGKLGVKLARDGDTCVVTGTRGAFTAKTADLFLGNAGTAVRPLTAALAINGGDYRVHGVPRMHERPIGDLVDGLRQIGAQIDYEQNEGFPPLRIRPATISVDAPIRVRGDVSSQFLTALLMTLPLVKAKDGRSIVEIDGELISKPYIDITIRLMARFGVNVEREGWQRFTVPAGVRYRSPGRIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFAHALMQMGANVTMGDDWIEVRGIGHDHGKLEPIDMDFNLIPDAAMTIAVAALFANGTSTLRNIASWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAALTPNAAIDTYDDHRMAMCFSLVSLGGVPVRINDPKCVGKTFPDYFDRFAALAKA", "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": "MTQPIVVAALYKFVTLSDYVELREPLLQAMVDNGIKGTLLIADEGINGTVSGSREGIDGLMAWLKSDPRLIDIDHKESYCDEQPFYRTKVKLKKEIVTLGVEGVDPNKSVGTYVEPKDWNDLISDPEVLLIDTRNDYEVSIGTFEGAIDPKTTSFREFPEYIKAHFDPAVHKKVAMFCTGGIRCEKASSYMLGEGFEEVYHLKGGILKYLEEVPEQESHWRGECFVFDNRVTVRHDLTEGDYDQCHACRTPISAEDRASEHYSPGVSCPHCWDSLSEKTRRSAIDRQKQIELAKARNQPHPIGRNYRLPSEA", "text": "FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. SIMILARITY: Belongs to the TrhO family."}
+{"protein": "MAKATVVKKHNGGTIAQNKRARHDYFIEEKFEAGMSLLGWEVKSLRAGRMSLTESYVIFKNGEAFLFGAQIQPLLSASTHIVPEATRTRKLLLSRRELEKLMGAVNQKGYSCVPLACYWKGHLVKLEIALVKGKQLHDKRATEKERDWQRDKARIFHK", "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": "MTDQPAKKVHSAPTLKVQLRSENAIAPTKGSAAAAGYDIYASQDCVIPGRGQGLVATDVSFTVPVGTYGRIAPRSGLAVKHGIQTGAGVVDRDYTGEVKIVLFNHSDRDYAVKRGDRVAQLVLERIVDDAEVVVVESLDESSRGEGGFGSTGN", "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": "MDIKTLHPAIAAAYRVLETGEPISLEEAELLASLPGEFSLDLASLANKVRNRWGKGGIHACSIMNAKSGVCGENCRFCAQSRHNHADIEVYPLVDEDAVLFEARSCAEHGVSHFGLVTSGYGYRTMNAEFKRILAMIDRLHEELPELNVCASIGILGPETAAALARHGIAHYNINLQVAPEKYAGLIADTHGIEERMETVRLLRREGVNVCCGGIIGVGESMEDRVAMLFALRDLDVSVIPINVLVPIEGTPLQAAESVPLADIVKVFALARLVHPHSIIKFAAGRETLMKDFQGLLMLSGADGYLTGGYLTTRGRDLADDQRFSERLASFS", "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": "MAKVFEGHLIGEGLRFGIVVARFNEFITHKLLSGAQDALIRHGVAENDIEVAWVPGAFEIPLVARRMLARNRYDAVLCLGTVIRGGTPHFEYVASEVAKGVAKVGLETGTPVIFGVITADTIEQAIERAGTKAGNKGWQAAVSGIEMANLVRRLESSS", "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": "MKLVIVSGRSGSGKSVALRVLEDLGYYCVDNLPLPLIGSLLAQLKSSNDLVAISVDVRNIAEQGKVLEQQLALLPPETEISSFFLNSSDKVLLKRFSETRRLHPLSRSQMSLQEAIKLEGRLLEPIAKMVDHHIDTSLLNVYELSDQVRQILLGSVDKELVINIESFGFKHGMPTEADFMFDVRFLPNPHWETELRPLTGLDVPVQEFLARQPLVHKLIWQIENLFETWMPHLERNNRSYLTIAIGCTGGQHRSVYIADQLAKRFANGKHVVNARHRELGDVKA", "text": "FUNCTION: Displays ATPase and GTPase activities. SIMILARITY: Belongs to the RapZ-like family."}
+{"protein": "MAYQDEESKEYSEKVVKIDRVAKVVKGGRRFSFNALSVVGDQKGKVGIGFGKANEVPDAIRKSIEAAKKHLVKINFKGHTIPHEVVGKFKSARVILKPSTAGTGIIAGASVRSIVEKAGIQDVLTKSWGSSNPVNIVKATLDALEQLETPILAAKKRGISLNQLFGKD", "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": "MAFGYDTITPEPVAKLIDEFNRLPGIGPKSASRLVFYLLRAKREQSERLANAIMAMKDSTIFCNRCFNITVEDPCTICTNANRNERQVCVVEEPLDVVALERTGEFKGLYHVLHGAISPVEGINPEDLRIRELLARLRVEPIEEVILSTNPNLEGDATAAYLAREIIPLGIRVTRLARGLPMGSDLEYADEVTLGRALQGRREM", "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": "MLIIPAIDLKDGACVRLRQGRMEDSTVFSDDPVSMAAKWVEGGCRRLHLVDLNGAFEGQPVNGEVVTAIAKRYPNLPIQIGGGIRSLETIEHYVKAGVSHVIIGTKAVKQPEFVAEACKAFPGRVIVGLDAKDGFVATDGWAEVSAVQVIDLAKRFEADGVSAIVYTDIAKDGMMQGCNVPFTKALAEATSIPVIASGGIHNLGDIKALLDAKAPGIIGAITGRAIYEGTLDVAEAQAFCDNYQG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
+{"protein": "MELKKLLECLTFYNVNGEVENCEITSLEMDSRKITSGSAFVCITGFTVDGHDYVDQAVKNGASAIFTSKPLMKEYGVPIIQVEDTNRALAMLAVKYYDYPTKHFPLIGVTGTNGKTTVTYLLDKIFEYHQKKAGVIGTIQVKIGEETFPIVNTTPNALELQKTFHVMREKDVKQGIMEVSSHALDMGRVYGCDYDIAVFTNLSQDHLDYHQDIQDYLRAKSLLFAQLGNGYDSEKEKYAIINDDDSSSHLLKRSTAQHVITYSCKKEATIMAKDIELTASGIRFKLHSPLGNITIQSRLMGMFNVYNMLAASAAAIASKVPLNVIQQALESIEGVNGRFEPIVEGQNYSVIVDFAHTPDSLENVLQTIKDFAKRNVYVVVGCGGDRDRKKRPLMAEVALNYADHAVFTSDNPRTEDPQAILDDMTAELDANSGSYEVVVDRKEGIAKAIQSAQKDDIVLIAGKGHETYQIIGHTKYDFDDRDVARNAIKQKGE", "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": "MARVKFGKVTRARRKRWIKRAKGYYGTKHSSYKKAHEQVVRSMAYAFIGRKQKKRDFRKLWIVRINAAVRPYGLSYSKFMNGLKLANIDVNRKMLSELAISNPEQFKLLVDASNKALTSK", "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": "MNNRVHQGHLARKRFGQNFLNDRFVIDSIVSAINPQKGQAMVEIGPGLAALTEPVGERLDKLTVIELDRDLAARLQTHPFLGPKLTIYQQDAMTMNFGELSTQLGQPLRVFGNLPYNISTPLMFHLFSYTDAIADMHFMLQKEVVNRLVAGPNSKAYGRLSVMAQYYCQVIPVLEVPPSAFTPPPKVDSAVVRLVPHATMPYPVKDIRVLSRITTEAFNQRRKTIRNSLGNLFSVETLTEMGIDPAMRAENISVAQYCQMANYLSENAPLKES", "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": "MTEHIQFSPEKDALVLLDQRYLPTREDWFDCKTTDDIVEALVVMVVRGAPAIGVTAAYGCYLAGREVAGSADWKAELEKNLDKIENARPTAVNLRWAVREMKRIWAEAGDVSLDELCAIWLKRAKEIHVDDIRMCEDIGKFGGELMDDGDTIMTHCNAGALATAGYGTALGVVRGAVDQGKKVSVIANETRPFLQGARLTAYELHRDGIPVKVACDNACALLMKKGLVQKVVVGADRVTANGDAVNKIGTYGVALLAREFGIPFYVAAPVYTIDPETPTGDDVPIEDRTPTEVTHVGDHRITPEGVEVFNFAFDPTPNELIAGIITEKGVLRPPYTEAIKKLFEDN", "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": "MVKYISILGSTGSIGTSALDVVSAHPEHFKIVGLTANYNIELLEQQIKTFQPRIVSVATKELADTLRTRISTNTKITYGTDGLIAVATHPNSNLVLSSVVGVSGLLPTIEALKAKKDIAIANKETLVAAGHIVTELAKQNGCRLIPVDSEHSAIFQCLNGENNKEIDKLIVTASGGAFRDKTREEMKTLQAKDALKHPNWLMGAKLTIDSATLMNKGFEVMEARWLFDIPYEKINVMIHKESIIHSLVEFIDGSVIAQLGAPDMRMPIQYAFHYPTRLPSSYEKLNLLEIGSLHFEKPDLEKFPCLQYAYECGKIGGITPAVLNAANEIANALFLKNEIAFFDIEKTIYKTVEAHHNVKDPSLDAILEADQWARQYANQLLIKKS", "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": "MNGIKYAVFTDKSIRLLGKNQYTSNVESGSTRTEIKHWVELFFGVKVKAMNSHRLPAKGRKVRLIMGHTMHYRRMIITLQPGYSIPPLRKKRT", "text": "FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL23 family."}
+{"protein": "MAITKDDILEAVGAMSVMELNDLVKAFEEKFGVSAAAMAVAAAPGAGGAAAAEEKTEFNVILAEVGSNKVGVIKAVREITGLGLKEAKDLVDGAPKPVKEGVDKATADDAKKKLEDAGAKVDVK", "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": "MRLMGLDVGSKTVGISVSDPLGWTAQAVEIIPIDEENEIFGIDRVAELVKKEQVAGFVIGLPKNMNNTEGPRVEASQHYGKLLQQRFPDIPIDFQDERLTTVEAHRMLVEEADISRAKQKKVIDEVAATFILQSYLDRHGRLVNKLK", "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": "MFRGSHVAIVTPMLEDGALDLDRFCALIDFHIEQGTDGIVVVGTTGESPTVDFDEHDLLIRTAVSYADGRIPIIAGTGANSTREAIELTVFSKNAGADACLSVAPYYNKPTQEGLYQHFKAIAEAVDIPMILYNVPGRTVADISNETTLRLAQIPGIVGIKDATGNIARGCDLVQRVPDNFAVYSGDDATALALLLLGGHGIISVTANVAPRLMHEMCTAALSGDLAQARAINARLFKLHIDLFVEANPIPVKWAVAKMGLINENIRLPLTALSSQHHELIRKAMLQAGITV", "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": "MLTLPAPAKLNLMLHIVGRRADGYHELQTLFQFLDHGDELSFSPREDGEIRLHTELPGVDHDSNLIVRAARLLQHESGCPQGADIHLLKRLPMGGGIGGGSSDAATALLGLNHLWQLHLEEDQLAELGLTLGADVPVFVRGRAAFAEGVGERLQPVELPEPWFLVIAPQVSVSTAEIFADPELTRNTPAITVRSLLAGGGHNDCQPIVEKRYPEVRNALSLLNKFVPASMTGTGACVFGSFPNEGEADKVRRQLPDTLPSFVARGRNVSMLHRCLEKLAQEVSA", "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": "MTITPQNLIALLPLLIVGLTVVVVMLSIAWRRNHFLNATLSVIGLNAALVSLWFVGQAGAMDVTPLMRVDGFAMLYTGLVLLASLATCTFAYPWLEGYNDNKDEFYLLVLIAALGGILLANANHLASLFLGIELISLPLFGLVGYAFRQKRSLEASIKYTILSAAASSFLLFGMALVYAQSGDLSFVALGKNLGDGMLNEPLLLAGFGLMIVGLGFKLSLVPFHLWTPDVYQGAPAPVSTFLATASKIAIFGVVMRLFLYAPMGDSEAIRVVLAIIAFASIIFGNLMALSQTNIKRLLGYSSISHLGYLLVALIALQTGEMSMEAVGVYLAGYLFSSLGAFGVVSLMSSPYRGPDADSLYSYRGLFWHRPILAAVMTVMMLSLAGIPMTLGFIGKFYVLAVGVQAHLWWLVGAVVVGSASGLYYYLRVAVSLYLHAPEQPGRDAPSNWQYSAGGIVVLISALLVLVLGVWPQPLISIVRLAMPLM", "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": "MARTVNCVYLNKEADGLDFQLYPGDLGKRIFDNVSKEAWGLWQKKQTMLINEKKLNMMNVDDRKFLEEQMTSFLFEGKDVEIEGFVPEKGQE", "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": "MQNKKLIIVESPTKAKTIKKFLDESFLVEACIGHVVDLPNNAKEIPKEYKKYEWANISIDYNNGFNPIYIIPSNKKPIVSKLKKLVKTINEIYLATDQDREGETIAFHLKEVLKIKNYKRMIFHEITETAITESLKNTRNIDMNLVNAGEARRILDRLYGYTISPLLWKKVAYGLSAGRVQSVGLKLLIEKEKTRINFKKANYYSILLQCKHEKKNLLLEAKLEEIDGKNIAEGKDFVNETGKLKNIAKTTIITQDLMIELEKELKNGQKIELISIETKKIKIPPPKPFTTSTLQQEINKRLKIGTKQIMQHAQKLYEHGYITYMRTDSHNIAKIAKDKITKIIKNKYGKEYIEEKDRIYEKEKMAQNAHEAIRPSEIFIPNETIEIESKTAKEIYKIIWDRTIISGMKDAIKENIKLTFKYKNLIFRSSFTKIIFDGFLKHTKEQDEHLNINFDLIKKGDTFSIVKMKTSEHETKAPFRYTEASLVQKMEKEGIGRPSTYSTIISTLLEREYAFKLNNTLMPTIKGAAVINLLEKYFPVLIELNFTSNMEEKLDKIAIGKLDKIKYLSKFYNGKKGLKDTVMQLEPKIDSSEFRTVIESQKIENKNSINYTINIGKYGPYLIFKGHNYSINAKTPLENLYKKDEIEKIINEKELKPNILGVDPLTGLNVIFKNTIYGNIVQLGEDTHAPQEYTKKGKPKKLKIIKAKKASTKKIDPENITLELALKLLSLPKPIGKHPQTNEQIIAATGVFGDYIKTESGSIACSLKKDLKAYDITLDKAISLLNERANKVGIIVKTITFSKNKIGNKIYIYKKNDKFYAKIKRKKIDLPDNINLEEINEKYVFSLL", "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": "MTYELLNTIDDPADLRRLDRRQLGPLANELRAFVLDSVSQTGGHLSSNLGTVELTIALHYVFNTPEDRIVWDVGHQSYPHKILTGRRDQMGSLRQLDGISGFPRRSESPYDTFGTAHSSTSISAALGMALGAKTKGEDRVAIAVIGDGAMSAGMAFEAMNNAGVYKDLPLVVVLNDNDMSISPPVGALNRYLARLMSGQFYAATKKGVEKLLSVAPPVLEFAKRFEEHTKGMFVPATMFEEFGFNYIGPIDGHDLESLVPTLQNIRQRAREGGGPQFLHVVTKKGQGYKLAEADPILYHGPGKFNPQEGIKPSGRPAKVTYTQVFGQWLCDMAAADKRLVGITPAMREGSGMVEFEQRFPDRYYDVGIAEQHAVTFAGGLACEGLKPVVAIYSTFLQRGYDQLIHDVALQNLPVVFALDRAGLVGADGATHAGAYDIAYLRCIPNMMVMTPADENECRQLLSTAFAQDCPTAVRYPRGAGTGVTVQPTLEPLPVGKAEVRRTSTAPAGQRVAILAFGSMVAPASAAAERLDATVVNMRFVKPLDVACVLEMARTHDFVVTAEEGCVMGGAGSACLEALAAAGVATPVLQLGLPDRFVDHGDHAALLAQCGLDANGILASIRERFAVQPRAAAPRVA", "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": "MSLMLEPNPTQIKEERIYAEMGLTDEEFAMVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGERVLQGPGEGAGIVDIGDNQAVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSPRVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEGNPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSEAKRPAVQVGDPFMEKLLIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGREQEIVDLFEKYGLAAVTMGKVTEDKMLRLFHKGEMVAEVPADALAEEAPIYHKPSQEAAYFAEFQQMKMETPKVENYKETLFALLQQPTIASKEWVYDQYDYQVRTSTVVTPGSDAAVVRVRGTEKGLAMTTDCNSRYIYLDPEMGGKIAVAEAARNIVCSGGEPLAITDCLNFGNPEKPEIFWQIEKSVDGMSEACRTLQTPVIGGNVSMYNERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKQAGDLVYVIGETKAEFGGSELQKMLHGKIFGQSPSIDLDVELKRQKQVLAAIQAGLVQSAHDVAEGGLAVAISESAIGANGLGATVKLDGEATAALFAESQSRFVITVKRENKEAFEKAVEAIQVGEVTNTNEVTIHNEENEVLLTANVDEMRKAWKGAIPCLLK", "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": "MKQYLELLNDVVTNGLTKGDRTGTGTKAVFARQYRHNLADGFPLLTTKKLHFKSIANELIWMLSGNTNIKWLNENGVKIWDEWATEDGDLGPVYGEQWTAWPTKDGGTINQIDYMVHTLKTNPNSRRILFHGWNVEYLPDETKSPQENARNGKQALPPCHLLYQAFVHDGHLSMQLYIRSSDVFLGLPYNTAALALLTHMLAQQCDLIPHEIIVTTGDTHAYSNHMEQIRTQLARTPKKLPELVIKRKPASIYDYKFEDFEIVGYDADPSIKADVAI", "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": "MIGKLTGTLLEKNPPEVLVDCHGVGYEVLVSMSTFYNLPAVGERVSLLTQFIVREDAQLLYGFGTAQERQAFRELIKISGVGPRTALSILSGMGVADLAQAVSLQEAGRLVKVPGIGKKTAERLLLELKGKLGADVGVRAHAANDNQADILQALLALGYNDKEAAAALKALPADVGVSEGIKLALKSLSK", "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": "MVNSFEKSRFLLVKKLLEGEPLTPGEAAQLAQAMLDPSFDNSLKAAALAALRVRGEQPGEVVGFARALRDRAVRVEYGGEVLLDTAGTGGDGLSTLNASTAAALVAASLGVPTAKHGNRSFSSKSGSADVMEMLGYNINHRADRAVRMLSTLGFTFLYAPNYHPAMKAVVPVRRKLATRTIFNLVGPLANPAFNNVQVIGVARRSLMPVIASAASLLGYDAVLVVHGDPGMDEVSVTGETKILEVRRGRIEEYSITPEDLGLPITGLKELRVANAVESAERVRRALSGRGRRSDEAFIAANAAAALYVAGFEKDLKGAAEAAVQAIREGRPAALLEKAVKASLGM", "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": "MIIWLSNFLEQYFPFFRLFEYLSFRAILSIITALTISLWMGPKLIAWLQNLQIGQVVRDDGPESHFSKRGTPTMGGIMILTAISVTVFLWADLTNPYVWAVMFVLLGYGAVGFVDDYRKVVRKNTDGLIARWKYFWQSSIALVVAFALYAYGKDTAATQLVVPFFKEVMPQLGLAYILLTYFVIVGTSNAVNLTDGLDGLAIMPTVFVAAGFAFIAWATGNVQFANYLHIPHIPLASELVVVCAAIVGAGFGFLWFNTYPAQVFMGDVGSLALGGALGTIAVLVRQEFLLVIMGGVFVVETLSVILQVGSYKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISMLLVLIALATLKVR", "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": "MNVQIGIDLMGGDHSPLVIWEVLIDVLNSTASNSHFSFTAFASHEVQEQILSSCTYKECPKIIASDSFVTMDDSPLSAIRKKSSSMALGLDYLKEDKIDAFISTGNTAALITLSRTKIPVFPTVRRPALLVRVPTMRGCAVILDVGANVSVNPEEMLGFARMGLAYRQCIGEKEHPTIGLLNIGSEERKGTEAHRQTFRILRETFQDSFLGNIESGDVFSGSVDIVVADGFTGNIFLKTAEGVFDFLRHILGDKLESDVKRQLDYTIYPGSMVCGLSKLVIKCHGKACGRSLFNGISGSIDLARARVCQRILSSLS", "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": "MGILGLSKLIADLAPLAIRESEIKNFFGRKVAIDASMCLYQFLIAVRSEGAQLATVNGDPTSHLMGMFYRTIRLLDNGIKPVYVFDGKPPDLKAGELAKRAERREEAEKALKVATDAGDEAEIEKFNRRLVRVTKEHSNEAKELLKLMGVPYVDAPCEAEAQCAALVKAGKVYATATEDMDALTFGSCKLLRYLTYSEARKMPVKEFSYDKVLQGLELTSKEFIDLCILMGCDYCDSIKGIGPKRAIELIKTYRDIETILENIDTSKYIVPENWNYQRARELFVEPEVTDASTIDLKWTAPDEDGLVQFLCGDRQFNEERVRNGARKLLKSKQSQTQVRLDSFFKALPSSPNATAAAKRKAEEIKKSANNKKAKTSGGSGAARGRRPK", "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": "MGEIWSELKAHHSAKSRRKMLDLFEKGNRVQAFSATVDGLYFDFSKTNLDDGALSLLLELARVKGVESRRAAMFAGDKINETEGRAVLHTALRAPAGPIKVDGQDIMPGVLETRARCFTFAQQVRDGSFTAQGGRITDVVNIGIGGSDLGPAMATLALAPYHDGPRLHYVSNVDGADMNGALQGIDPKTTLVIVASKTFTTIETMTNAQTARDWMAQDVADPSAQFVALSSSTEKAGAFGIPPERTFGFEDWVGGRYSLWGPIGLGLMIAIGPEAFQQFLDGAATMDRHFQEADLADNLPVLLALVGMWHNQVEGHATRAVLPYDNRLSRLPAYLQQLEMESNGKSVAMDGSALQQNSGPVVWGEPGTNGQHAFYQLIHQGTRVVPCEFLVAAKGHEPDLTHHHRLLVANCLAQSEALMRGRSMEEARALMAAKGLEGAELERQAAHRVFPGNRPSTTLLYDQLTPFTLGQIIALYEHRVFVEGVILGINSFDQWGVELGKELATALEPVLTGKDDGAGKDGSTLALVDAVKAVGGI", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
+{"protein": "MAHKKAGGSTRNGRDSESKRLGVKRFGGESVLAGNIIVRQRGTKFHAGVNVGIGRDHTLFALSDGKVKFEVKGPNNRKFISIEA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
+{"protein": "MDAPLGFVVIDKPSGLTSHACVSRMRRVLQTKRVGHGGTLDPAVTGVLPIAVGQATRLLPYLPGEKTYRGVIQLGTSTSTDDLQGEIVAVQNWPDLSVEEMDQALNPFRGTIEQCPPQVSAVHVNGERAYARARRGEVIDLPARPVTIHSLSLEHWDFEQGKLTLEVHCSAGTYIRSLARDLGQALGCGGCLDSLRRTQALGFVEAHAIALPVHPNEQSGPSLEPLTLIPPQLALKHLPIRTLSELERDDWSCGRTIPHQNGDGPTVVLSEDNIMLGIGLANSEAQLRPKVVFEARG", "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": "MSKQNELNARRKQRVRARIKKYGSGRPRLSVFRSSKHIYAQIIDDTAGHTLAAASSLDKDLREGLKTGADIDAAKAVGKLIAERATAKGVTAVVFDRGAYLFHGRVKALADAAREAGLQF", "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": "MLNIAIAVFIGGGLGSVLRWLISYRLNSLFPHFATGTLVANCIGAFIIAFGIAWFSKAPNIDPIWKIMLTTGFCGGLTTFSTFSVEVVALFNEGRIGWALGTMGANLAGSFLMTAFAFWLLREM", "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": "MDNVFDYEDIQLIPAKCIVESRSECDTSVTLGGHTFKLPVVPANMQTIIDETLAKKLAENGYFYIMHRFQPEARVNFIQDMHGSGLIASISVGVKEEEYAFIEELAATNLVPEFITIDIAHGHSNAVIRMIQHIKKHLPNSFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAATKPIIADGGIRTHGDIAKSVRFGASMVMIGSLFAGHEESPGQTIEVEGKKVKEYFGSASEFQKGERKNVEGKKMFVEHKGSIKDTLIEMQQDLQSSISYAGGTKLDAIRNVDYVIVKNSIFNGDKVY", "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": "MTDIRITEVPREAGFGDYFALLKPRVMSLVVFTALVGLLVAPATVHPMIALTGILFIALGAGASGALNMWWDADIDRVMKRTRNRPVPAGVVQPGEALGLGLALSGIAVVMLGLATNLFAAGLLAFTIFFYAVVYSMWLKRTTPQNIVIGGAAGAFPPMIGWAVATGGVSLESLFMFALIFMWTPPHFWSLALFMKTDYSDAGVPMLTVTHGRRVTRGHVLAYALLLAPLAVAGAFTGIGGPLYLVVALALNGWLLRGAVRIWRRDEAEAEADRYRTEKGFFRFSLYYLFLHFGAILAEAALKPYGLGGW", "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": "MLTGQFLTPLMSGFVITVIFMPLFIGYLRFKKEGQTIRDEGPKWHAKKNGTPTMGGLVFIVAAVISSIWVAIWLQQLTNSLWIALFILVLYGLLGFSDDFIKVFKKQNLGLRAWQKLAGQILGGAVFLAVYFHEGFSHALNIPLIGTISSSWFFSLFVIVWLVGFSNAVNLADGIDGLVAGLAIVSFATYTIIAFRQNRIDVAIFGLTIIGGLIGFLIFNHKPAQIFMGDVGSLALGGALAAMSILLHREFSLLLIGLVYVIETASVMLQVASFKLFHKRIFKMSPIHHHFEMSGWSEWRIDISFWVFSIICSAIYLLIF", "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": "MSKFWSPFVKDLVPYVPGEQPKLSRLVKLNTNENPYGPSPQALAAMQAELNDDLRLYPDPNGERLKQAVAAHYGVQANQVFVGNGSDEVLAHIFHGLFQHDLPLLFPDVTYSFYPVYCGLYGIAHEKIALDERFRIRVEDYARPNGGIIFPNPNAPTGCLLPLDAIEAMLKASPDSVVVVDEAYVDFGGESAIALVDRYPNLLVTQTLSKSRSLAGLRVGLAVGHADLVEALERIKNSFNSYPLDRLAIAGAAAAFEDDAYFRRTCQAVIDSREALSASLQALGFEVLPSAANFVFARHPRHDAGQIASTLREQGVIVRHFKQARIDQFLRITIGSPEQNQALLDALHFLK", "text": "SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily."}
+{"protein": "NTDITSNGERVKCMQVWPPIGKKKFETLSYLPPLTRDQLLKEVEYLLRKGWVPCLEFELLKGFVYGEHNKSPRYYDGRYWTMWKLPMFGTTDPAQVVKEVDEVVAAYPEAFVRVIGFNNVRQVQCISFIAHTPESY", "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": "MSFRERLEQTIAQNHSLLCIGLDPDLERFPTGIPRDPEGIVVFNRAIIEATADLVCAYKPNLAFYLQYGAAGIAALATTRQLIPPHIPVILDAKLGDIASTSAAYARAVFETLGFDALTVHPYLGSEALEPFLSTSDRGVFVLVRTSNPGASEIQDLPVGEAGEPLYLWLAERARAWNQRSGNVGLVVGATYPVDLALVRQRCPDLPILAPGIGAQGGDLERAVCAGLTEATAPLLVTVSRSILYADASARFAESARAAARRVRDTIERIRKEVAGQAGHR", "text": "SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily."}
+{"protein": "MSKGHSLQDPYLNTLRKERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVRLPTASEGEQPEPGNA", "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": "MHKKSSTLIRKREISDVTKESKVVLKSDQQWREQLSEQEYHVCREQGTEPPFSGKLLHNKDSGEYACTCCHAPLFSSVNKYDSGCGWPSFDAPINETAVLYLDDFSHGMKRVEIRCARCDSHLGHVFPDGPKTTGERFCVNSVSLIFNKIETNE", "text": "SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family."}
+{"protein": "MLKKIFIKTFGCQMNEYDSNRIFDTVKKIGFEKTEKYEDANCYLLNTCHIRDKAKEKVYHEIGRVKKIFREKKKPIVVVAGCVAQAENQEMLKREPYIDIVIGPQSYHKINEAILNHLKNKKKEEETEFDTISKFNYLSQIKNKDSKVSSFLTIQEGCDKFCHFCVVPYTRGPEYSRPFDQIINEAKELVQSGAKEIILLGQNVNAYSYDEEGKKYRLSDLLIKLDSFDKLERIRYTTSHPKDMTDDLINVYKTSSKLMPLVHLPVQSGSNKILNLMNRKHTIEEYLLVYEKLRKINPKIEFSSDFIIGYPEEDEQDFKMTMELIEKVKFINSYSFIFSPRPGTVAANLTLVDQKKSKQRLEIIQEKLFNNQIKKNKSLENKILNVLVENKMKDGIKLFGRTEYMTSVIFDGNIENIGKLVQVEIISSNQNSLFGKLTESSKKKVA", "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": "MSHTSRVFFPPAFVEQMQQLLPDADEFQRFITSSQLPLRRSLRVNTLKISVDDFLTLVEPYQWALTPIPWCQEGFWISRDDADTLPLGSTAEHLAGLFYIQEASSMLPVSALFDGGDMPQRVMDMAAAPGSKTTQIAAHMGNRGAILANEYSASRVKVLHANLSRCGVSNTAMTHFDGRVFGPALPECFDAVLLDAPCSGEGVVRKDADALRNWSQSSTEEIAATQQALINSAFHALRPGGTLVYSTCTLNTRENQQVVNGLLEQYPDAVKVEPLDTLFMGAERATTAEGYLHVFPHIFDSEGFFVARLRKVASVPPMPQPGYKVGKPPFTPLNRVQQQEVIAAAASVGLRWDTELKLWQRDKELWLFPSEIEPLLGRVRFSRIGLKLAETFPKGFRWQHHAAVALADAASANAFELNSNEAEEWYRGRDIYPERDLPASELIICYQQRPIGIAKKVGSRIKNNYPRELVRDGKLFTL", "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": "MSKIIGIDLGTTNSAVAVLEGTEPKIIANPEGNRTTPSVVSFKNGEIIVGDAAKRQAVTNPDTVISIKSKMGTSEKVSANGKEYTPQEISAMILQYLKGYAEEYLGEKVTKAVITVPAYFNDAQRQATKDAGKIAGLEVERIVNEPTAAALAYGLDKTDKEEKILVFDLGGGTFDVSILELGDGVFDVLATAGDNKLGGDDFDQKIIDYMVEEFKKENGIDLSTDKMALQRLKDAAEKAKKDLSGVTSTQISLPFITAGEAGPLHLEMTLTRAKFDDLTRDLVERTKTPVRQALSDAGLSLSDIDEVILVGGSTRIPAVVEAVKAETGKEPNKSVNPDEVVAMGAAIQGGVISGDVKDVVLLDVTPLSLGIETMGGVFTKLIERNTTIPTSKSQVFSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPAAPRGVPQIEVTFDIDKNGIVSVKAKDLGTQKEQTIVIQSNSGLTDEEIERMMKDAEANAEADAKRKAEVELRNEVDQAIFATEKTIKETEGKGFDTERDAAQSALDELKKAQESGNLDDMKAKLEALNEKAQALAVKLYEQAAAAQQAQAGAEGAQATDNSGDDVVDGEFTEK", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MKKLKASEIRQKYLDFFVEKGHMVEPSAPLVPIDDDTLLWINSGVATLKKYFDGRETPKKPRIVNSQKAIRTNDIENVGFTARHHTFFEMLGNFSIGDYFKQEAIEFAWEFLTSDKWMGMEPDKLYVTIHPEDMEAYNIWHKDIGLEESRIIRIEGNFWDIGEGPSGPNTEIFYDRGEAYGQDDPAEEMYPGGENERYLEVWNLVFSEFNHNKDHSYTPLPNKNIDTGMGLERMASVSQNVRTNYETDLFMPIMNEIEKVSGKQYLVNNEQDVAFKVIADHIRTIAFAISDGALPANEGRGYVLRRLLRRAVRFSQTLGINEPFMYKLVDIVADIMEPYYPNVKEKADFIKRVIKSEEERFHETLEDGLAILNELIKKAKATTNEINGKDAFKLYDTYGFPIELTEEIAVQAGLKVDMTTFESEMQQQRDRARQARQNSQSMQVQSEVLKNITSASTFVGYDTATAQTTLTHLIYNGEEVSQVEAGETVYFMLTETPFYAVSGGQVADTGIVYNDNFEIAVSEVTKAPNGQNLHKGVVQFGQVNVGATVSAEVNQNDRRDIQKNHSATHLLHAALKSVLGDHVNQAGSLVEADRLRFDFSHFGPMTNDEIDQVERLVNEEIWKGIDVNIQEMDIVSAKEMGAMALFGEKYGDVVRVVNMAPFSIELCGGIHVRNTSEIGLFKIVSESGTGAGVRRIEALTGKAAFLYLEDIQEKFNTMKSQLKVKSDNQVVDKLTQLQDEEKALLKQLEQRDKEITSLKMGNIEDQVEEINGYKVLVTEVDVPNAKAIRSTMDDFKSKLQDTIIILASNVDDKVSMVATVPKSLTNNVKAGDLIKQMAPIVGGKGGGRPDMAQGGGTQPENISKSLSFIKDYIKNL", "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": "MSERLLVLVRHGQSEWNLKNLFTGWKDPDLTAQGVSEAKDAGRKLKAHGLSFDVAFTSELTRAQHTLKLILDELGQPGLPTSKNLALNERDYGDLSGLNKDDARAKWGEEQVHVWRRSYDVPPPGGESLKDTLARALPYYVQEILPGVLNGQRTLVAAHGNSLRALIMVLEKLTPEGILKRELATGVPIIYRLKADSTVESKLDLAG", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
+{"protein": "MKRTYQPSKTKRVRRFGFRALMKTKGGRAVLSRRRAKGRRKLSASDEKKPF", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family."}
+{"protein": "MEALVYTFLLVSTLGIIFFAIFFREPPXILTKKTK", "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": "MAEITAALVKELREKSGVGMMDCKKALAENNGDIEASIDWLRAKGLSKAAKKADRAAAEGLVAIATAEQGAGETATAVEVNAETDFVSRNDLFQGAARQIAGAALGTDGSVDAITAAKLAGGETVQDHLTNLIATIGENMMVRRAAKWTVENGVVASYIHNATAPDLGRIGVLVAVESTGDKAALRELGRKIAMHVAATSPLSLSPDDLDPAAIEREKAVFTEQALESGKPAAVVEKMIEGRIRKFLEEVVLLKQAFVMNPDQTVEQLVAETAKTLGAPVAVKGFTRLALGEGVEKKQDDFAAEVASMTGQA", "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": "MAPARPFALLFLAVTVGFVLLTAADDSANATATTTTAMAPSSSTDDAAPPVWLKAHATFYGGADASGTMGGACGYGDLYSQGYGTRNAALSTALFNDGASCGQCYKIACDRKRAPQWCRPGVTVTITATNFCPPNWDLPSDNGGWCNPPRPHFDMAQPAWEKIGIYRAGIIPVIYQRVPCVKKGGVRFTINGHDYFNLVLVTNVATTGLIKSMDVMGSNSTDWLPMVRNWGANWHSLSYLTGQMLSFRVTNMDGQTLVFRNIVPSGWKFGQTFASKLQFK", "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": "MDIFSIANQHIRFAVKLATAIVLALFVGFHFQLETPRWAVLTAAIVAAGPAFAAGGEPYSGAIRYRGFLRIIGTFIGCIAGLVIIIAMIRAPLLMILVCCIWAGFCTWISSLVRIENSYAWGLAGYTALIIVITIQPEPLLTPQFAVERCSEIVIGIVCAIMADLLFSPRSIKQEVDRELESLLVAQYQLMQLCIKHGDGEVVDKAWGDLVRRTTALQGMRSNLNMESSRWARANRRLKAINTLSLTLITQSCETYLIQNTRPELITDTFREFFDTPVETAQDVHKQLKRLRRVIAWTGERETPVTIYSWVAAATRYQLLKRGVISNTKINATEEEILQGEPEVKVESAERHHAMVNFWRTTLSCILGTLFWLWTGWTSGSGAMVMIAVVTSLAMRLPNPRMVAIDFIYGTLAALPLGLLYFLVIIPNTQQSMLLLCISLAVLGFFLGIEVQKRRLGSMGALASTINIIVLDNPMTFHFSQFLDSALGQIVGCVLAFTVILLVRDKSRDRTGRVLLNQFVSAAVSAMTTNVARRKENHLPALYQQLFLLMNKFPGDLPKFRLALTMIIAHQRLRDAPIPVNEDLSAFHRQMRRTADHVISARSDDKRRRYFGQLLEELEIYQEKLCIWQAPPQVTEPVHRLAGMLHKYQHALTDS", "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": "MNERKIIHIDMDAFYASVEQRDHPELRGKPLAVGHAEERGVVAAASYEARRYGVRSAMSSQKAKRLCPQLIFVPGRMEVYKSVSRQVHEIFHEYTDLIEPLSLDEAFLDVTENKQGILLAVDIAKAIKQRIREELSLVASAGVSYNKFLAKIASDFRKPDGLCTIHPDQAIDFIARLPIESFWGVGPVTARKMHLLGIHNGLQLRECSSEMLVRQFGKVGLLYYDFARGVDLRPVEAVRIRKSIGCEHTLEKDIHVRSSVIIELYHVATELVERLQQKEFRGNTLTLKIKFHDFSQITRSMTQAQELTNLERILPLAKQLLKEVEYEQHPIRLIGLSVSNPREEADEHRGVWEQLSFEFSDWGK", "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": "MEPLVIAGKSYSSRLLLGTGKYRDFAETRAAVDASGAQIITVAIRRTNIGQNPDEPNLLDILPPSQFTLLPNTAGCYTAEDAVRTLRLARELLDGHALVKLEVLGDQKTLFPDVVATIEAAKILVKEGFQVMVYTSDDPIVARQLEDIGCAAIMPLASLIGSGMGILNPWNLQIIIDKATVPVIVDAGVGTASDAAIAMELGCDGVLMNTAVASARNPILMASAMRKAVEAGREAYLAGRMPRKIYQASPSSPAEGMFTGTQHPAANS", "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": "MTQTSSLWVGVISLFPDMFDAITDQGVTGRAVKSGLIDFNCWNPRDYALDKHRTVDDRPYGGGPGMLMMVEPLKKAIAEAKKAAGDGAKVIYMSPQGRKLDQQGASELASSKKLILIAGRYEGIDERIIESYVDEEWSIGDFILSGGELPAMTLIDAVARLVPGVLGHNQSAEQDSFSDGLLDCPHYTRPETLDDKQVPAVLLSGNHQEIAKWRLMQSLGRTWLRRPDLLHNLALTEEQAVLLAKFQQEYQKACG", "text": "FUNCTION: Specifically methylates guanosine-37 in various tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase TrmD family."}
+{"protein": "IVFRAAQKRSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKKIRVTAERDPANLKWDEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDNTPMFVRGANFDTYAGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAASEGAMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLV", "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": "MLIIIRPSGEIALKSPRSRRNFEHTLANNIRSVIKEGKIWRSQGVLFLEVNDNNKNIEELSKVFGIASFSPVMSIKSYNNNLEDIINKAKEVFAEIVKGKIFSVRAKRIGSHNFTSLDVQRKVGEALYPFSRGVNLENPEVEVFIEIRNDVAYFYYKIIKGPRGLPVGVAGKTVVLFSGGIDSPVATWMMMKRGSIPVILNFNLGGSVHRKFVLEELSVLRKWSGGHKLKLFIVNGTDVLIKLSQIEKRNRVVMLKRVMYKVAERLCDKANAKSITTGESLSQVSSQTMTNLYVTEYGIKYPIFRPLIGFDKEEIVELARKIGTYEYSIKLPEYCAISTKARTSVELNEVLKDEENLNIDYEKVLENSEVIEI", "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": "MINEIKKDTQQRMEKSLEALKSHISKIRTGRAQPSLLDGIQVEYYGSATPLRQVANVVAEDARTLAVNVFDRSLISAVEKAILTSDLGLNPSSAGATIRVPLPALTEERRRDLIKIVKNEGEQGKIAIRNVRRDANDQIKALLKDKEISEDEERKAQDEIQKITDGYVKKVDEVLMAKEKELLDF", "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": "MFLKDIHQFFLGFVITNTIIVIIGQINLQFKNSYNIVSGLKVQQLDSIKYYCKVLTHDSSCLFFRNCLAVIDSIIVNIDEYLSLSPFKRREKFLQDVESLNNPSVPARLFINPKKDFILIHRKGVSLKIRSTFQMYSIYKFNVSVSKNAAIFNTLRPSDFISFLEYYSDMNINEILINVLNNYGLNDISLFLVKKIFYLFDSDKIFFNEFIGVDSVPLEYFLLFLSKKYIIRARKESPLKIYTDFEDFYIHGSFKNILKMQQQKIKQNLGFKTKSNFFTGI", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast."}
+{"protein": "MRKIQAKKGLSIECKGWEQEAVLRMLYNNLDTEVAERPEDLVVYGGIGKAARNWEAFEAIEKTLRELESDETMLVQSGKPVAVFKTHEEAPRVLISNSVLVPEWANWDHFNELDKKGLIMYGQMTAGSWIYIGSQGIVQGTYETFAELGNQHFNGDLAGTVTLTAGLGGMGGAQPLAITMNHGVAICVDVDETRVDKRIATKYCDIKTANLDEALKLAEEAKERGEGLSIGLVGNAVDLHQAILEKGFKIDIITDQTSAHDPLNGYVPQGYSVEEAKVLREKDPKKYVELSQASMAKHVELMLEFHKRGAVAFDYGNNIRQVAFNNGVRNAFDFPGFVPAYIRPLFCEGKGPFRFAALSGDPKDIERADEEMRKLFPENEKLLRWLDLAEEKISYQGLPSRIAWLGYGERAKMGLALNRLVRDGEISAPIVIGRDHLDAGSVASPNRETESMKDGSDAVGDWAVLNALINTAAGGSWISFHHGGGVGMGYSLHAGMVVVADGSERAERRLERVLTTDPGMGVARHVDAGYDIAIQTAKEKGIHIPMIDKAGDK", "text": "FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5- propionate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urocanase family."}
+{"protein": "MKKVRKLYEGKAKIVYETDEKDKLILEFKDVATAFDGVKKEEIKGKGSLNNEISSLIFEILEDHGIKTHYIKKLSDREMLVWRAERFPVEVVVRNYAAGSFVKRYGVKEGTKLEQPLVEFFMKSDELHDPMVCINHIKVLKLAPAELVPEMEKIALKVNEILKKIFEEKGILLVDFKLEFGRLPSGELAIVDEISPDSMRLWDKSTGENWIKTDSV", "text": "SIMILARITY: Belongs to the SAICAR synthetase family."}
+{"protein": "MSITYMNMFMAFTISLLGLLMYRSHMMSSLLCLEGMMLSLFVMMTMAILNTHLTLASMIPIILLVFAACEAALGLSLLVMVSTTYGMDYVQNLNLLQC", "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": "MAVIKLKPTTPGQRGTVKVTRDHLHKGAGFAPLLEPQHQKSGRNNNGHITTRHKGGGHKHHYRVVDFKRTKDGIPAKVERIEYDPNRTAHIALVCYADGERRYIIAPRNLEVGATIVSGSEAPIRVGNTLPIRNIPVGSTIHCIELKIGAGAQIARSAGTSATLLAREGIYAQVRMRSGEVRKVHIECRATIGEVANEEHSLRRLGKAGVKRWMGIRPTVRGVVMNPVDHPHGGGEGKTGEGRHAVDPWGNLTKGYRTRNNKRTQSMIVSRRKK", "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": "MTAILERRESQSLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAIEAPSTNG", "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": "MGKKRSASSSRWLNEHFKDPFVQKAHKQKLRSRAYFKLDEIQQSDRLFKPGMTVVDLGAAPGGWSQYVVTQIGDKGRIIACDILDMDPIVGVDFLQGDFRDENVLAALLDRVGEDQVDVVMSDMAPNFSGMPSVDIPRAMYLVELALDMCKQVLAKKGSFVVKVFQGEGFDEYLREIRSLFTTVKVRKPEASRDRSREVYIVATGYRG", "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": "MYAVIRTGGKQYRVAQGDRVKIEKLAGDVGGKVNFDVLLVGGEGEAKVGKPTLAGVTVEGEIVAQGKHKKVIHFRKKKEGWTKKRGHRQPYTEVLITTVRA", "text": "FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
+{"protein": "MKIKVVLPDGSEREYEKGTKPMEIAREVGIKKVIGAVVDEELWDLKRPLERDCRIRFVTLEDPEAPEFYRHTMAHILAQAVMRLYGKENVKLGIGPTIENGFYYDFDIRNGKLTEEDLPRIEQEMKKIIKENLPIEREEISKDEAKEIFKDQPYKLELIEEIEGDTVTIYRQGEFVDLCRGPHLPSTGVVKHFKLLSVSGAYWRGSEKNPMLTRVYGTAFAKKEDLENYLKFLEEAQKRDHRKLGPQLELFMLNTDYAPGMPFFLPRGVIVLNELMNFSRELHRERGYQEIFTPLIMNEQLWRISGHWDHYAENMYFIEKGEERYAVKPMNCPGHILVYKSRAVSYRDLPLRFFEFGRVHRYERSGVLHGLMRVRSFTQDDAHIFCTPDQIEDEILGVLELINTIYSQFGFTYRVELSTMPEDHMGDEAIWEKATNALKKALDRAGLPYRVNEGEGAFYGPKIDFHIKDSLGREWQCATIQLDFMMPEKFNVTYIGPDNREHTAVMIHRAIYGSLERFFGILIEHFAGAFPTWIAPVQVAVIPISDKHSEGAKKVATMLSREGFRVFLDDRRETLGYRIRQAQIQKIPYMVVLGDRELESGKLSVRTRSGKEIKDVEMDHFIDTLKKEVRDRKLELTLEG", "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": "MMSFEEEQLRDHAVVNLYRIGAIRFGDFILSDGKKTPIYVDMRLVISCPDVLQTIASLIWRLRPSFNSSLLCGVPYTALTLATCISLKYNISMVLRRKELKHPNQEDKIKVEGLFSPGQTCLVINDVIASGRSILDTAKALEDEGLNIRESLVFLDRQVGGADALKEAGIKLRSVFTLEELVKALLSKCQLSETDAAIARTLLETF", "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": "MSAIQGIEGVISQLQTTAMSARAQESLPQPTISFAGQLHAALDRISDTQTAARTQAEKFTLGEPGVALNDVMTDMQKASVSMQMGIQVRNKLVAAYQEVMSMQV", "text": "SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the FliE family."}
+{"protein": "MNFEVLYQDNNARCGVFNFNQEIIETPVFMPVGTYGAVKSISTEEIKNTGSRIILSNAFHLYFRPGLEIIKLHGNLHNFMNWSGPILTDSGGFQVFSLSRFCKVNEEGVIFQNHIDGKKTFLTPKISMKIQSDLGSNIVMIFDQCIEYNQNWEKTKNAMERSLYWAKKSRIYFDSYKNKNSLFGIIHGGIYPSLRDISLQELIKIDFDGYALGGLAVGEPKIEMYKLLDHICPQIPKNKPRYLMGVGKPEDLIEGVRRGVDMFDCVIPTRNARNGHLFVTNGVIKIRNKKYKKDLSCLDKTCVCYTCRYYSRSYLHHLDACNEILGARLNTIHNLHYYQTLMSNIRNSIKNNTFEQFSLNFYKQKNKIDF", "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": "MNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKMKKLADAGFPQAVIPPHERPFIPVLRQLGFRGSDEQVLEKVARQAPHWLSSVSSASPMWVANAATIAPSADTLDGKVHLTVANLNNKFHRSLEAPVTESLLKAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGMQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNPQQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFMAIEVPATQVFVSDAVSTYLFNSQLLSRDDGSMVLVLPQECREHAGVWRYLNELLAADNPISELKVFDLRESMANGGGPACLRLRVVLTEEERRAVNPAVMMNDTLFNALNDWVDRYYRDRLTAADLADPQLLREGREALDTLTQLLDLGSVYPFQREGGGNG", "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": "MSGKTLYDKLWDSHLVQQRDDGSALIYIDLQLLHEVTSPQAFEGLRLAGRKPWRVSSSLATPDHNVPTTKKERISGVDGIEDPVSKIQVTTLDDNCNEFGITEFNMKDIRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVQKKSRNMLVRVDGELSPWVSAKDVVLAIIGAIGTAGGTGYAIEFGGTGIQSLSMEGRMTVCNMAIEAGARVGLIAVDDTTIEYVKGRPYAPKGEHWEMAVEAWKDLVSDKDAQFDEVVVIKAEDIKPQVTWGTSPEMVIAIDEPIPRAEDQKDPVKKEGYARAWKYMGLEGKSMLSDIVLDRVFIGSCTNSRIEDLRIAAQVVKGRKVASTLKQAIVVPGSGLVKAQAEKEGLHEIFEAAGLEWREPGCSMCLAMNADKLGAGEHSASTSNRNFEGRQGFGGRTHLVSPAMAAAAAIAGHFVDVNEFVKH", "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": "MPIDPVALTADLVRCPSVTPEEGGALDLIERILSGAGFDCTRVDRNGVPNLFARWGRKGANRTFGFNGHTDVVPVGDAAAWTRDPFGGEIADGWLWGRGATDMKSGVAAFVAAAVDFVQETPPDGAVVLTITGDEEGDATDGTVALLDWMAAEGEAMSVCLVGEPTCPERLGEMMKIGRRGSMTAFFTARGVQGHSAYPHRAKNPVAALARLIDRLSSHDLDQGTEHFDASTLAVTTFDTGNPATNVIPALCRATVNIRFNDAHSGASLASWLEEEAARVTAETGVEIALSAKISGESFLTPPGELSELVARAVEAETGLRPEPSTSGGTSDARFVRAHCPVVEFGLVGKTMHQVDERVEVAQIEPLKAIYLRILKDYFA", "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": "MDEDTRAEYESTSQQLRIDLKTWETDWAKSHEGKKPGRGDIKANEDIAAKYKQYNKVRDILSGKISPPSKHAPKSTKRKSDGLSAQTPIKQNKHIETPAKNRTQNHDEDLMNTPAISRKLFSPTSVTSVGPTPQRDGQVLGLFDLLVEKELGTPSKKDSATKTGSARKVDATPSKRSAATDDDEDERLGRTPMSSSKRQRLDHFLTPLKNKDGNKDAATPSSVSKLQFDTPAFLKRNTLPVLEENGDFDAPAPLRLPRKPFARGLSEIVASLRKVEEESLDDDLDALRDIEDGGMGEPKPKTLFPSKPKDDILVDDNEARQLPLGGFDDEGVYDSPVEGDNPTRVYKKKGQKRTTRMAKMRPVRVNRPENMAANPQSDVENDEIQAGGEDAGSDFDDIVEKKPAQKKEGTVKKAARKVNELAHANFQRLKLRNHGAKGGPGINSRFRRRK", "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": "MKKKKIFIGTIISCVMLALSACGSSDNVVTSKVGNVTEKELSKELRQQYGESTLYQMMLSKALLDKYKVSDEEAKKKVEEAKDKMGENFKSTLEQLGLKNEDELKEKMKPEIAFEKAIKATVTDKDVKNNYKPEMKVSHILVKDEKTAKEIKEKVNNGEDFAALANQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSDPVKTTYGYHIIKVTDKKELKPFDEVKDKIRKDIEQQRLQDTTGKWKQQVVNDLLKDADIKVNNKEFKDTFKFLEKK", "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": "MIQRRRPVPFELGPVHFIGIGGIGMSGIAEIMIRIGYTVQGSDAKASANTERLEKLGARIFIGHDAAHVEGASAIVYSTAVKADNPEMVAGRDKRLPLVRRAEMLAELMRLQFSVAVGGTHGKTTTTSMVAALLDAGGLDPTVVNGGIINAYGTNAKVGEGDWIVVEADESDGSFLKLKSTVAIVTNIDAEHLDHWGDFDAVKKGFQDFIQNIPFYGFAAVCTDHPEVQALTSRIENRRLVTYGTNPQAEVRVSNIEMGPEGATFDIIVSPRAGEAVRYDGLKMPMAGHHNVLNATAAVAVARELGVDAEAIAKGLAGFGGVKRRFTTTGVANGIRVVDDYGHHPVEIAAVLKAARAVTPNGKVIAVVQPHRFTRLRDLMTEFSSCFNDADTVIVADVYTAGEQPIPGVDRDALVAGLKKFGHRRALPLENPTALPRLIAAEATSGDLVVLLGAGDITTWSYALPGQLEALTK", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family."}
+{"protein": "MKHELVLVIDFGGQYNQLIARRVRENNVYCEILPCTASIERIKEKNPKGIIFTGGPNSAYLEDSPTISKEIFELGVPILGICYGIQIMSHVLGGVVRKGNKQEKEYGKTAITYGKSSLFEGITTNSVWMSHTDLIEKVPEGFTIVANTNDCPVAAMENVERNLYGVQFHPEVEHCLEGDKILTNFLYNICKVKGDWTTDSFIEDKIKELKEKIGDKKALCALSGGVDSSVAAVLIHKAIGDNLTCIFVDHGLLRKNEGNDVERIFREKFDINLIRVNAEDRFLSKLKGVSEPEAKRKIIGEEFIRVFEEESNKLGKMDFLVQGTIYPDVIESGHGNAATIKSHHNVGGIPEDVDFQEIVEPLRELFKDEVRKIGLELGIEEGLIFRHPFPGPGLGIRVIGDVTKEKCDILREADAVYMDELRKAGLYREIWQAFATLPDVKTVGVMGDERTYAYLVGLRAVTSSDGMTSDWYKMPYDVLERISNRIINEVDGVNRVVYDITSKPPGTIEWE", "text": "FUNCTION: Catalyzes the synthesis of GMP from XMP."}
+{"protein": "MQLMEYTQLALFLGLLALMSPVLGRFIGRAVLRGEQTWLHSVLGPVERLIYRASGIRPEARQSWRQYAASLCAFSAAGFLMTFGVLMLQDKLPLNPQGFPGLSWHLAFNTAVSFLTNTNWQSYAGESTVSHFSQLVGLAYHNFVSAAAGLAVAVAVMRGLASQESKTIGNFWADLVRSVLYVLLPISLVLAVVLVGQGVVQTMSAGTEVATLEGGHQFIAMGPTASQVAIKMLGTNGGGFFNANAAHPLENPTALSNLLQMLAIFIIPSSLVFTLGEAVSNRRHAWTVWFVMACLFMVGTLSLYKAETLGTPLLTEVAQAPVTNMEGKEVRFGIFGSAMFATVTTDASCGAVNAMHDSLTPLGGLVTLVNMQMGEVIFGGVGSGLYGMVLFILLTVFLAGLMVGRTPDYLGKRIEGREVTLAMLALIIAATPPLLFSAVAAVSGWGQAALNNAGAHGFSEILYAYTSGVQNNGSAFAGLNANSPAWNVTLALAMLIGRFGVMLPMLGVAGSMASRKARPIGEFSFPVSGFTFGLLLTLVIVIVGALTYLPALALGPVVEHFQMLDGLLH", "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": "MIKKSAAILAGGKSSRMNYINKAFLKYEENYFIERIIKALEDYEEIIIISNNPEEYTEFGLKVFKDIYPSQGPLSGIHSALNYIKNDYCLVVACDMPFINKEVVNYLGNIKEDYEILIPKFQERLQPLCAIYKKSCKDIMEKELINNSNKLIKTCFKFSMKVVEEFPFIEKIHKKEIKNFYNINTVHEYEDLIRKKEI", "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": "MQSELQRGFVLHRRPYSETSLLVDLFTEESGRLTVIAKGARAKRSSWKSVLQPFTPLLLRWTGKSTLKTLTKAEPAAITLPLQQITLYSGFYVNELLTRVIESETPNPALFQHYLKCLTGLATETNVEPTLRLFEFQLLQILGYGVDFLHCAGSGEPVDFSMTYRYREEKGFVASLVKDNLTFYGRDLLAFEALDFSDDAVRQAAKRFTRIALKPYLGDKPLKSRELFTQNILLLK", "text": "FUNCTION: Involved in DNA repair and RecF pathway recombination. SIMILARITY: Belongs to the RecO family."}
+{"protein": "MFNKHSVEIDWGGRPLKLETGKVARQADGAVVATYGETIVLATVVAAKTPREGVDFLPLTVDYQEKTYAAGRIPGGYFKREGRPTEKETLVSRLIDRPIRPLFADGWRNETQVIVTVLSHDMENDPDILAMVAASAALTLSGAPFKGPIGAARVGFINDEYVLNPVLDEMPETQLELVVAGTADAVLMVESEAKELSEEIMLGAVMFGHRHFQPVIDAIIELAEKAAKEPRELVVIDDSAIEKEMLGLVEQELRAAYAIPVKQERYAAVGKVKEKAIAHFFPEGEEPKYDKLRIAGVFKELEAKIVRWNILDTGKRIDGRDSKTVRSIIAEAGVLPRAHGSALFTRGETQALVVTTLGTGEDEQYVDSLAGTYKETFLLHYNFPPYSVGETGRLGGTKRREIGHGKLAWRAIRPVLPPHHEFPYTIRVVSEITESNGSSSMASVCGASLALMDAGVPLKRPTAGIAMGLILEGERFAVLSDILGDEDHLGDMDFKVAGTEQGITSLQMDIKIAGITEEIMKVALGQAKDGRIHILGEMSKALDRARAELGEHAPRIETFKIPTDKIREVIGTGGKVIREIVEKTGAKVNIEDDGTVKVASSDGESIKAAIKWIKSIASDPEVGEIYEGTVVKVMEFGAFVNFFGAKDGLVHISQLASGRVQKTSDVVKEGDKVKVKLLGFDDRGKTRLSMRVVDQETGEDLEAKQKAEGEAPAQATGE", "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": "MAATRIAILYGSETGTAQDFANILSHQLRRFHYKHTVCSIGEYSAQNILACQYLFVICSTTGQGALPQNARQSPQGKVEGTLWSVLKRSSLPPTLLDHLQVAFLGLGDSSYSKFNFAIRKLHNRIVGQLGAREIFPRLEADAIGLAGSNAGNGNGIELVYSEFEKRVLSFLNDQFPFMTVNGEQVPREPIATDIYLKPEYYLEASGNDKGTASVPCTFEGDSSVKYGTVVTNKRITATDHFQDVRQLVFSSQDGENYYPGDTVSIYPYNTDADVQAFIDTQQHWASIADVPLQIKTPTSARGICDGGLVSPLTLRNLLKYHCDIVSIPMRSFFMKTWTFAVDHERLPDGKDQLQQQRDKLREFAESEDMQDIYDYCNRPRRSILEVVQDFMSLRLPWEYILDYLPHIKPRFFSISSQPCNKDIELTIAIVRYKTILRRIRRGLCTNYISDLSEGSIIRYKVQYNDLLPAGKQDRPVIMISPGVGLAPMKCLIYAQLFNPMLLFFGNRYKDKDFLYADTLQKWADENRIKLFVCFSRSPDDSPGLKYVQDAVWENAREVARLITEENAVVYVCGSSGKMPVQVRLTLCEVLKKWGNFPDDKASEEYLKDMENSDRYLQETW", "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": "MTTITQKYEEAKEKYASIDVDTEAVLEKMADVKISMHVWQGDDVRGFLSEDELSGGISVTGNYPGVARSPQQLRQDLEKAFSLIPGKHKLNLHAIYLDTEERVDLNELEPKHFEPWVTWAKENGLGLDFNPTFFSHPMYRDGFTLAHPNPQVRDFWIEHGKRSRRIAEYFGRELGQVAVNNFWVPDGFKDNPVDRLTPRKRLMASLDEIFSEEIDPAYTVDAMESKLFGIGSEAYTVGSHEFYMGYGLTRNKLICLDAGHFHPTEVISNKLSSLSLFGEGMLLHVSRPVRWDSDHVVIMDDELQEIAKELVRNDLLGKTHVGLDFFDATINRVAAWVIGTRNTQKALMKAMLEPTNVLKEAELIGDFTTRLALTEELKDFPFADIWNYYCQENHVPIGLDWLTDVQEYEKVILPTRQLPTGKDSCRFS", "text": "FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose isomerase family."}
+{"protein": "MTTRITARFTELAAEGRPGLVTFITAGDPDYDTALSILRGLPEAGADVIEVGIPFTDPMADGPAIQAAGLRALKGGQTLAKTLDMVRAFRDENDTTPVVLMGYYNPIYIYGVPRFIADAKAAGVDGLIVVDLPPEEDNELCLPALDAGLDFIRLATPTTDEKRLPAVLAHTAGFVYYVSITGITGSATPDANAVAGAVARIKQHTTLPVAVGFGVKTPAQAAAIAAGADGVVVGSALVEAVRKTLDEDGKATVNTVPAVTALVQELAEAVRGVNRAAAE", "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": "MVGFKTLALHLAAVLPALAAPVDKQATQVVPNSYIITLKQGASAASFHNHLSWVGDVHRRSVSKRDTTGVDKVFDLDGFTAYSGSFDAATLQEIKKSDEVAFVEPDQVWDLYTLSTQSGAPWGLGSISHRKPNSTDYVYDPAGLGADHYAYIIDTGLDTEHVEFEGRGTLGYNAYPNSQFIDKIGHGTHVAGTIAGKTYGVAKKASIVSVRVFDTGSVTRQSTTAIVLDGFSWAVKDITAKGRQAKSVISMSLGGGRSEAFNAAVEAAYQANILTVAAAGNSAWDASQYSPASAPNAITVGAIDVDNVMAWFSNYGPVVDVFAPGVAVESAWIGSSHAEHDVLDGTSMATPHVSGLVLYLKSLEGFASAAAVTDRIKALGTNDVVTGLEGTDSPNLIAFNGVTA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
+{"protein": "MAIRRILTVDNAADLAVLKQVSKDVPAVDDALRGLMDDMLETMYDAPGIGLAAVQVGELVNVIVMDLAREGEEPAPRYFVNPKITWASEELFEYEEGCLSVPEVYDAVERPAKVKISYLNYQGEAVEEDAEELFAVCIQHEMDHLKGVLFIDHLSRLKRDRAISKVKKARRAA", "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": "MKISLKWLHDYVDVTEFFQKPEVLAEALTRGGLEVEEITNRAKDFNHVVIGHILEKDKHPNADKLSLCRVSTGEGVVHQIVCGAQNHKAGDRVIVALPGAVLPGNFAIKKSAVRGVDSAGMLCSLKELGLATESEGIAILPADAPVGKAYAEYGGYDDVTFELKVTANRADCLSHFGLAREVSTLFGKELKVPSSELKTNGKSSKSEIALDVKAFDLCPRYAGRFLKGVKVGPSPAWLKARLESVGMNSINNIVDVTNYVMLELGQPLHAFDAAFINGKKIIVDRAVAGEKFITLDGTEIALNGAELTIRDVNHPVCLAGVVGGKNSGVSDSTTEVFLEAAYFLPMSARKTSRSHGIDTDSSYRFARGVDPDGTLRGLNRAAALILEVAGGEAYADHHDFYPNPVKKAPVDITIKTVSDRLGYEAEEHKFVDFMKRLGCEINKKGETFTVLPPTFRFDIEQDMDLVEEYARLNGYEHIPEALPALAAAPSFQDKTFMLNRTTSELLRGEGFQQAVNFAFVGSKAQKAFLGSLEALKATGLAATEKEIRILNPLNEEMDVMRSSLSFGLFKNLNHNFHSGNMQGRLFEIGSTFFVKDDGSFAEGSRAGMAIWGRASNLWNKSLDYPVVYELKAAVEVLLKSLNISSYTWVTPANKSEVPEFLHQGQFAQLLVEGKKVGFIGTLHPLLLEDNKIRVPAALAELDLDQLYKGQPRPYRIQSVSKFPIVERDFAFVMPKALKVGDVLKDIRKAGAGLLLNVDVFDLYEGEKMEAGKKSVAIRIWLQDKNATLQETQINETTTKILESLKKNFDLSVR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily."}
+{"protein": "MIRRGTYLNTADNSGAKKVQCIGIPKKVNFGKQTDFATLGDVITVTVKDALPNGAAKKGKVYKAVVVRTAKEVSREDGSYIKFDDNAVVLLNNNLEPIGTRILGPVAREIRAKGFYRIVSLAPEVI", "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": "MSNWTPAADQKNQGTLEFEISRAQVEEGLEKAFQRNKNQVSIPGFRKGKVTKALFFSKFGEEALYQEAMDIVLPAAYEAAVEEAGITPVGRPNIEPVSMNKGEAWTLKAEVTTAPAIKLGEYLNLEVAAEDTAVSDADVDAEIKRLQDGQAELVLQEESVKAEDGDTVVIDFDGSVDGDHFDGGQANDFSLALGSGQFIPGFEEQLVGHTAGEDVEVKVTFPEDYQAADLAGKEALFEVKIHELKRKELPELDDEFAKDVDEEVETLAELKEKTAKKLADDKEAAAKSAFEDAVITKAVDNASVDGDAIPDAMIEEDVHRQVDQYLGQLQQQGISREMFFQISGQTEEDLHKQFEEGAATRVKTNLVLEAIVKAEGIEPSAEQVTEEINNLATQYNMDAEQVRSSLSDSLLKHDIAMREVIKKITDSAKAK", "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": "MKILGIDPGSRNCGYAIIEKNVRKTALIEAGLIKIKPNTLQYQITELCEGLDVIFKNHKFDEVAIEDIFFAYNPKTVLKLAQFRGALSLKILQLHGDFAEYTPLQVKKAVTGKAKAQKEQVAFMVKKILGITKEIKPLDITDAIAVALTHANNLCLR", "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": "MLTLTRIRTVSYEVRSTFLFISVLEFAVGFLTNAFVFLVNFWDVVKRQALSNSDCVLLCLSISRLFLHGLLFLSAIQLTHFQKLSEPLNHSYQAIIMLWMIANQANLWLAACLSLLYCSKLIRFSHTFLICLASWVSRKISQMLLGIILCSCICTVLCVWCFFSRPHFTVTTVLFMNNNTRLNWQIKDLNLFYSFLFCYLWSVPPFLLFLVSSGMLTVSLGRHMRTMKVYTRNSRDPSLEAHIKALKSLVSFFCFFVISSCAAFISVPLLILWRDKIGVMVCVGIMAACPSGHAAILISGNAKLRRAVMTILLWAQSSLKVRADHKADSRTLC", "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": "MKSTAPSYLKHHFLIAMPQMADPNFAQTLIYLIEHGPEGAMGLIVNRPSGLSLADVLEQLRPDEPIPALCQSLPIFAGGPVQTDRGFVLHSAEQQFQATLMLGPLGMSTSQDVLFAIADGQGPQRHFVALGYAGWEAGQLEAELADNTWLSCPADPQILFDLPHDQRLQAAAASLGVDLRLLSTQVGHA", "text": "SIMILARITY: Belongs to the UPF0301 (AlgH) family."}
+{"protein": "MLILVSPAKTLDFEQPPLTQIHTRPDFLAQSQELIQVCQQLTPSDIATLMKVSDSIAGLNAARFGEWKPDYSIDNAKQAIFAFRGDVYTGFDADTLTAAQLERTQSQLRILSGLYGLLRPLDLILPYRLEMGTALTNQKGKNLYEFWGNTLTDAVNSAVAAQGDGIIINLASNEYFKAIKPKFLNGQLITPVFKDFKNGQYKVISFFAKRARGMMARYIIDQQVSSIDGLKAFEVDGYYYSEELSKPNEPTFLREAQ", "text": "SIMILARITY: Belongs to the UPF0246 family."}
+{"protein": "MKIINEDLASLKRLVQTKTQQLTDLKVESAVREIIANVIKNGDAAVKDYETQFDKVTLTDFKLSQTVIDDAYNNLDPQVKDALLLAKRNITSFHEKEKATGFIDAEQPGVLRGQKLMPLNRVGLYVPGGTAAYPSTLLMSALPAKIAGVNEVIMVTPPQVDGINPAVLAAAKIAGVDAIYQVGGAQAIAALAYGTESIPAVDKIIGPGNIFVATAKKQVFGQVAIDMVAGPSEIGILADDSADPRQLAADLLSQAEHDRRARPILITDSADLAQAVSDNVTSQLKVLPREAIATDAVNEKGFIAVVAKIEEMFDLMNTVAPEHLEVQLKNPTQYLNLIKNAGSVFLGRYASEPLGDYVAGPNHILPTSGTARFSSPLGVYDFVKRTSFIQYTKDALAKEAPAITTLARVEGLEGHARAIESRFDTYYD", "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": "MEDIKHYMQQLGSEARTASRAMARADTETKNKALRAIATAIRRERDTLLAANAADLEAARRHGLEPAMLDRLVLSEKGIDTMAEGLEQIAGLPDPIGEMSDFKYRPSGIQIGKMRVPLGVIGIIYEARPNVTVDAAGLCIKSGNAAILRGGSEAIQCNRALAAIVHEGLAAAALPASAVQVVATTDRAAVGELITMKDYVDVIVPRGGKGLIERISNEARIPVIKHLDGNCHVYIDESADLAKALRILENSKTQRLGTCNTAESLLVARSIAQEALPPLTAMLISKGVEIRGCSETRALVPQAKPATEEDYYTEYLAAIISVKVVADVDEAIAHINQYSSQHTEAIVTENYTNARRFLREVDSSSVIVNASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSLKYIVLGDGEVRA", "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": "MLAVFLQGFALSAAMILPLGPQNVFVMNQGIRRQYHLMVASLCALSDIVLICGGIFGGSALLSRSPLLLALVTWGGVAFLLWYGWGAFRTAFSRQLALATAEELKQSRWRLVVTMLAVTWLNPHVYLDTFVVLGSLGGQLTPDVRSWFALGAVSASVVWFFALALLASWLAPWLKTQMAQRIINTLVGVVMWGIALQLAWQGASL", "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": "MKKVVAIDGPSGAGKSTVSKEIAKALGFQYLDTGALYRAVAYYFSIKFNYIDDFSLLTEQEIEEELKNIKIHYKNGRVFLSGEDVSDFIRDPKIGEITSQLSTQKVVRDFLMPLQRSFAEKVDIVAEGRDMTTVVFPDAWKKFYLDASPQVRAKRRFEQLIQSGKKISFEEALRDVIERDKRDCSRENAPLRLSKDAFYIDTSELTLQEVISIVLKKVAEDA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily."}
+{"protein": "MRKILLPYPAGCATGTFVRRVKRFSVEMTRDGESVWVHSNNSGSMLGLLRPGATMLASPAANPDRKLAWTHEAMRCHGDGPQGFWVGVNTSVPNRMVEAAFHAGRLPWAQGYDTFRRERKRGDSRLDARLDGPGLPTLWVECKNVTMVEDDVACFPDAVTERGSKHLREMMDIVSRGERAAMFYLVQRPDGLCFGPADVIDPQYAALFWEAVDAGVEMYPHRGIVSPVGIDLSGVLPLTRCR", "text": "SIMILARITY: Belongs to the SfsA family."}
+{"protein": "MSEQKKVVLAYSGGLDTSVAIKWLQEQGYNVIACCLDVGEGKDLAFVQQKALEVGATNSYVIDAKEEFAQDYALISLQAHTMYEGKYPLVSALSRPLIAKKLVEIAEKEDAQAIAHGCTGKGNDQVRFEVSIKSLNPDLEVIAPVREWQWSREEEIEYAASRGIPIPINLDSPYSIDQNLWGRANECGILEDPWAAPPEGAYDLTAPLEKTPDTPEVIEIAFEQGVPVSIDGVSYSLSELILKLNEMAGAHGVGRIDHVENRLVGIKSREVYECPGAMTLIKAHKELEDLTLVKEVAHFKPIIEQKMSEIIYNGLWFSPLKDALHAFLKETQKHVTGIVRVKLFKGHAIVEGRKSEYSLYDEKLATYTKDDAFDHHAAIGFIELWGLPTKVNSIVKKKEQIKA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily."}
+{"protein": "MGAKSKQYFNIFVFVISLIFFDQLSKYLVVKYVKLGSIYFSFFDNFFRIIHVRNTGILFSMGSDIHYSLKKIFFIAMPIFILIFVFSLALKEKNCITRISLLLIFSGGVGNIIDRLFRPSGVVDFLDFKFYGIFGLDRWPTFNFADSYVVIGMILFLVYDFFIKRKVLNT", "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": "MKDFYARVTVMVTGLCFVGTVTNPSRKSSLSLHQQDGDLLANWSSTRHTSQKTDTVDRNSYFFRVLFQPHTKERHTNHLDRTNHRLSKVTLSCLAHLRALEMLNLGDDVIHSLCLDLSLPSSSRQKRHRSRFRGRHPRLKVLLLQRNQLGPTPKGLWKLKPLCSLDLSFNRRVGIGLSGFHGCLQLKSIYLKNNKILTIHPEAFKGLKKLQVVDLRSSALTMLVPIVTIALEWPNLELGLADNQWQCNESDANFQNIASVSWGEIWKAVCNTPVENEKPYVEASQIRISRDIHLPRSPSSDLQSLIQSKAEKPRAGMDVHLSALEKKAQVGYGDLKGIWLQSPMELRDSQGGPVTDRKDDKPPDLALAVCLSVFITFVVAFCLGAFARPYIDRLRQQRCLNKRPGSENAYSNEGFHDDVEAAQHVQHQGTDLCQTTHHLNLFENQDPSWGTEAIPHGAVLSERMLGSNGMDPSSQQSPGQFEDSGEARSGDGNMFPNGRVVHPAVHGLPSADAQKPISPGQHHYDVPEESLYDTVAQEYSLLDNAMDRSSVAGCLGTFPNSINSGRDELCPSQPRDVVASFSKTLAHMSTREAEESVERGFPEPLGAMGSQIESSEERQVSNSIRELATQQASFQEVDVEERLAHVYSEALYNDTPSHMPRHSSGHDVASATEEAVQRDASFDPHDDLVTNYESDSDEGSLFTLSSEGSQDTRSLTEEQAFVESGGDSQPLPSRNLGEYKDSVTSAESVEDITSQQTLEKREAQEAHLGNTLISGPDSCVHETHLENDSSPLDPENVPTWTQPPDHKLAHHETLGTFVYGDIGPQSEAVDWLYSLRDLEFPNIDSSPSPPCSDQDPSDPEEHDTK", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
+{"protein": "MKQFAFPKYERLLKRSEFVQFTNARQRIHTAHFILLWTHTEDSTLKIGITVSRKVGNSVIRNRVKRLVREFYRLNKSRFVMAHYNIIAKKGAEQLDFQRLSRELANVLERLHK", "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": "MAKEELIEMQGSVTEVLPDSRFRVTLDNGHQLIAYTGGKMRKHHIRILAGDKVSLEMSPYDLTKGRITFRHLAGRGPGPGTGSSSGNR", "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": "MSYKQVIIIGAGLAGSEAAWQVASSGVPVKLVEMRPIKSTPAHHTSEFGELVCSNSFGALSPDRAAGLLQKELRIFNSLIVQTADKFAVPAGGALAVDRSKFSIALTEALSNHPLIEIKRFEQLDLPSKENITILATGPLTADELSYKIQAFTGIDACHFFDAASPIIYGDTIDQEIVFKASRYDKGDPAYFNCPMGKNDYINFRNELIKGEQVNLKDFEKESANFFEACLPIEEIARRGVDTMRYGPLKSIGLWNPKWGDLFDRENRLKKRPHAVVQLRKEDLEGKLLNMVGFQTNLKWSEQKRIFRLIPGLEKAEFVRFGVMHRNTFLESPKLLLPTLQFLKRENLFAAGQITGTEGYAAAAAGGLLAGINASLLAKGKKTVSFPDQSMIGSLMNFISNKNQILSNQQKNKFQPMPASFGLVPELIKRIKDKRLRYKAYQERSTEALNDFKNQLDSCFDKDHLLSKIY", "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": "MSRIGRLPIDVPAGVDVAVDGQHVTVKGPKGELSLTIAQPIRAEVQDGQVLVTRPDDERESRSLHGLTRSLIANNIVGVTTGYTKGLEIVGTGYRVAIKDKGVEFALGFSHPVYVEAPAGISFTVEGVNKMTVVGIDKQLVGETAANIRKIRKPEPYKGKGVRYAGENVRRKAGKSGK", "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": "MKRIFLLIATNLAVLLVASIVMSILGVNTSTMGGLLVFAAIFGFGGAFISLAISKWMAKKTMGCEVITTPRDSTERWLVETVARQAKQAGIKMPEVAIYQSSDMNAFATGPSKDNSLVAVSTGLLYGMSQDEIEGVLAHEVSHVANGDMVTLTLIQGVVNTFVIFAARVVAGIINNFVSSNDEEGEGLGMFAYMAVVFVLDMLFGILASIIVAYFSRIREYKADEGAARLAGKGKMIAALERLRQGPESTAMPAQMSAFGINGKRSMAEMMMSHPPLEKRIAALRAS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family."}
+{"protein": "MHGKLLPLAGLYLVQGLPYGLQSSLLPILLRARGLSLTRVGLTKGLYAPWLLKLAWAPLVDRRGTPRVWLTLSTLSLGLVCGLLAVLPPPQAGQTGLPTTVMGLLLLLNLGAAVQDVALDTLAVQLLEPKELGPGNTVQVVAYKLGSALAGGGLLVLFPTLSWPLLFLLLAATYWLAAALAWAAPALGRLPWPQASEHTPHSSYLLQDLLAVPGTLWTAGFVLTYKLGEQGAGSLFPLLLLDHGASASDLGLWSGLGAVTCSIAGSSLGGALLARHWQPLKLLKTVLQLRLGSLACQTALLFHLNSPGASVDPGTVMRGAVLLSLCLQQFFGGVVTTATFTVMMHCSQLAPRALQATHYSFLATLELLGKLLLGTLAGVLADSLGPHLCFAVFLVLSALPVLDLRLAPSNLT", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MARGPKKHLKRVAAPKHWMLDKLTGVFAPRPSTGPHKLRECLPLIIFLRNRLKYALTGDEVKKICMQRFIKIDGKVRVDVTYPAGFMDVISIEKTGEHFRLVYDTKGRFAVHRITAEEAKYKLCKVRKITVGTKGIPHLVTHDARTIRYPDPVIKVNDTVRIDLGSGKITSFIKFDTGNVCMVIGGANLGRVGVITNRERHPGSFDVVHVKDASGNSFATRISNIFVIGNGNKPWISLPRGKGIRLTIAEERDKRLAAKQSSG", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family."}
+{"protein": "MEIFQAAILGIIEGLTEFLPISSTGHLIVVSDWLGIEQTKQNTAFEVIIQVAAILAIFSHYKEKFSLQHLRLWNNVLIAFLPIAIIGFIFQDTVKAFFTIETVAWFFIIGGLIFLIMEKLYVDGKHRTQDIEDLTMRQAFWIGIIQVFALIPGTSRAGASIVGGVMMGLDRKTAAEFSFLLALPVLMAASGLDLLKHYEDFNNTSWTPLMVGFLMAFLAAWLTIKVFIKFLQTFTFNAFGVYRIVFGIVLLIWFV", "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": "MEKHIILLPGDGIGREIIDSAKQVLTAIASEYNHRFTFEEHAIGGSAIDEYGTPLPDKTVDACSKADAILLGAVGGPKWDANPSHLRPEKGLLGIRKQLGLFANLRPVKTISSLLYASPLKEEIVSQADMLIIRELTGGIYFGTPSERTTNGVVDTLQYSREEIERIVERGFEAARIRKKHLTSVDKANVLESSKLWREIVEEKSKDYPDVAVNHLLVDAAAMKLVTQPSFFDVIVTENLFGDILSDEASVLTGSLGMLPSASLRADGLGLYEPVHGSAPDIAGKGIANPLAMILSAALMLEHSFGLVDEAKEIERAVNDCLLQGFHTADIHIPGGVQVGTKQMTDAVLENVTTKSISDSICSSYV", "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": "MIDRFGRPLEDLRITLTHVCNFECFFCHMEGEEGDNYILSKEDILLVAKVAKNFDINSVKLTGGEPTLRRDLVEIVRGLKQLGYRDVSMTTNGFLLKDLAYKLKLAGLDRINVSLHAISRETFKKITGVDAFDRVIEGIKSAIDVGLVPVKLNFVVNRRNREEVFKFIELSQNLGVNEIHLIELHPVGLGKLAFKEHDDLREIEEYIEKISIKKQIRKKHFRPRYVLPSGLIVEVIKPYANPIFCAGCNRIRLSVDGKLKTCLYREDNVIDILDILKGEYSEDVKEELLGRAFMIAIAIREPNFKYKI", "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": "SVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEESQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPNAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGEREITLGFVDLLRDDFVEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLASEGNQIIREASKWSPELAAACEVWKE", "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": "MISGDSIVALSSGRLPAGVAVLRISGPQTRFVVETIAGGMVKDRVAVLRRFKAPDGTVLDSGLVIFFPGPASFTGEDVAEFHVHGGRAVVARMLEIISGFDGVRHAEPGEFTRRAFLNGKVDLVETEALADLVNAETEAQRRFAVRNAEGVQSELYLSWRRRLIHARAMIEAEIDFADEDDVPGSVSDTVWSDVRAMIGEIDRHIAGFHAAEIIREGFEVVILGAPNAGKSSLFNALARRDAAIVTDEPGTTRDLLEVTLDLGGLRVRLTDTAGLREAPGKVEAIGIEKARAKADRADLLLLLEDILAPGVLGPLPGKAPLLRVGTKLDLLDEGSAREAAGRYDVAISVVGGTGVEALLAEIGRRAADAAGDVGDVLPSRLRHVELLGEANRHLLRAAAEDAAGQELRAEELRLAADSLGRIVGAIDVEDMLDVIFSQFCIGK", "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": "MLEILWIALAYVLGSAPWGLVIARTFCGIDPRESGSRNTGATNVARLCGFGWGVATLLCDVLKGAVPVWLAFRINASPVFVSMVALACVLGHVFSCFMKFRGGKAVATSIGIFLPLAFWQLLASSLLCMLVIWRSGFVSLGSLTLVTALPVALAVSGQWGWLPLSLAVWAVVVWKHRENIVRLRSGTEKSWLKSKNKGAAAGNAAEGDDTQNMNPQDAGRKDG", "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": "MRVTDFSFELPESLIAHYPQPERSRCRLLSLEGPTGALTHGTFTDLLDKLNPGDLLVFNNTRVIPARLFGRKASGGKIEVLVERMLDDKRILAHIRASKAPKPGTELLLGDDESIHATMTARHGALFEVEFNDPRPVLDILNAIGHMPLPPYIDRPDEDADRELYQTVYSEKPGAVAAPTAGLHFDEPLLAALREKGVEMAFVTLHVGAGTFQPVRVDTIEDHIMHSEYAEVPQEVVDAVLVAKVRGNRVIAVGTTSVRSLESAAQAAKSDLIEPFFGDTQIFIYPGYQYKVIDALITNFHLPESTLIMLVSAFAGYQHTMNAYKTAVEQKYRFFSYGDAMFITYNPQAIFERP", "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": "MSGLRLEGKIVIITGGASGIGADAARLFTDHGAKVVIVDVQEELGQNVAVLIGKDKASFYRCDVTNETEVEDAVKFTVEKHGKLDVLFSNAGVLEPLESFLDFDLERFDRIMAVNVRGAAAFIKHAARAMVEKGTRGSIVCTTSVSAEIGGGHHGYTASKHGLVGLIRSACGDLGKYGIRVNGVAPYAVATPMTSHDEVTGKQLEDYFDAKGILKGMVLKASHVAQVALFLASDDSAYISGQNLAVDGGYTVVKPSRD", "text": "SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MALHSLIADARRLVVKVGSSLVTNDGRGLDQAAIARWAAQIAALRAAGKEVVLVSSGAIAEGMQRLGWAKRPKEIHELQAAAAVGQMGLAQVYESEFARHSIRTAQVLLTHGDLADRERYLNARSTLLTLLSLGVVPIINENDTVVTDEIKFGDNDTLGALVTNLIEGDALIILTDQRGLYTADPRKDPGARFVDEAQAGTPDLEQMAGGAGSSIGKGGMLTKILAAKRAAKSGAHTIIASGREADVLARLASGEAIGTQLRAPTGRMAARKQWMIDHLQLRGRVVLDAGAVEKLTAGGKSLLPIGVTEVQGEFARGEVISCVDAAGLEVARGLTNYSSAEARLIARKASSEIEAVLGYVSAAELVHRDNLVLL", "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": "MENIVLIGMPLSGKSTLGRELSKILKYDLIDTDTLIEEMEDKSIKEIFKIYGEDYFREKELKIINKLKKESNKVISTGGGLPIYNKNIYELKKIGFTVYLKVPLEELIKRMVKKEYDTRPLLKNNDTKFLEEMYKNRIEIYEKAHTIICNTNYKESLITIVRAYKKWKGI", "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": "MFENMDFSKMGELLTKAQEKANELEQEALKKEFSAKSGGGLVKVSANGKGEIIDINIDDSLLEDKESMQILLIAAINDVMKMVEQNKKSMASNLFSGMGVL", "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": "METTKPSFQDVLEFVRLFRRKNKLQREIQDVEKKIRDNQKRVLLLDNLSDYIKPGMSVEAIQGIIASMKSDYEDRVDDYIIKNAELSKERRDISKKLKVMGEIKNGEAKSE", "text": "SIMILARITY: Belongs to the UPF0265 family."}
+{"protein": "MLFITSNRHKYEEAAEFLGNYNIDIKWKNMKYEEIQGDTNKEISMDSCRKLMYKIKDDFFIDDTGLYIDDLNGFPGPYASYVNKTLGNKNIIRLASGSRAHFETVISLFYSGKIYQFSGILNGTISDHESGSMNFGYDPIFIPDGYDKSLAELSISEKNRISHRSKALEIMVEFLKKQ", "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": "MKQAIGFIDSGVGGLTVVREVLKQLPHEQVYYLGDTARCPYGPRDKEEVAQFTWEMTNFLVDRGIKMLVIACNTATAAALYDIREKLDIPVIGVIQPGSRAALKATRNNKIGVLGTLGTVESMAYPTALKGLNRRVEVDSLACPKFVSVVESGEYKSAIAKKVVAESLLPLKSTKIDTVILGCTHYPLLKPIIENFMGDGVAVINSGEETASEVSALLDYHNLLDATDDEIEHRFFTTGSTQIFKDIAKDWLNMPDMTVEHIKLGK", "text": "FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. SIMILARITY: Belongs to the aspartate/glutamate racemases family."}
+{"protein": "MSVATNPNHAGADREVGTQALNRELQDKGFLVTSSEDIINWARTGSLHWMTFGLACCAVEMMHTSMPRYDAERFGIAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQRKIRRTGTIAR", "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": "MTAPTPPVTPPLVLTVAGSDSGGGAGIQADLKTMLALGTHGMSVLTAVTAQNSRGVQGAWELPVEAVRAQYRSVVDDIGVQAVKTGMLSSAELVETVAELLAGTDAPAVVDPVGVSKHGDALLASSALESVRTRLLPVATVATPNLDEVAQLTGVRVDDETDLRRAAAAVLAFGPRWALIKGGHLAGDAVDLLTDGSEEHWLRAPRLDNRHTHGTGCTLASAVACGLAKGQSVPVAVRAAKEYVTGAITAGFPLGGGIGPVDHGWALGE", "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": "MELPPQIQAQLMQLQQLQQQLQMILMQKQSVETELKECKKALEELEKSSSDEVYKLVGGLFVKRKKEDVKKELEEKVETLELRVKTLEKQEEKLQSRLKELQEKIQKMIPTAQ", "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": "MAEEKYIMAIDQGTTSSRAIIFDKKGNKIGSSQKEFTQYFPNAGWVEHNANEIWNSVQSVIAGSLIESGVKPTDIAGIGITNQRETTVVWDKATGLPIYNAIVWQSRQTTPIADQLKEDGYSEMIHEKTGLIIDAYFSATKVRWILDHVEGAQERAENGELMFGTIDTWLVWKLTGDTHVTDYSNASRTMLFNIHDLDWDQEILDLLNIPRVMLPKVVSNSEVYGLTKNYHFYGSEVPIAGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGEEPQLSKNNLLTTIGYGINGKVYYALEGSIFVAGSAIQWLRDGLKMLQTAAESEAVAKASTGHNEVYVVPAFTGLGAPYWDSQARGAVFGLTRGTTREDFVKATLQAVAYQVRDIIDTMKEDTGIDIPVLKVDGGAANNDFLMQFQADILNTAVQRAHNLETTALGAAFLAGLAVGFWKDLEEIKAFQEEGQQFEPIMAEEEREDLYEGWQQAVAATQQFKRKNK", "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": "MNKSYSLREIVSTLGGELLGKDDVLISRVASLANAQPGQISFLTDSKYRSVLATTNASAVILTPQNRDITALPRILTDNPYAYFAKVSDLLNPKPEYVAGVDDTAVIAPSAQVPASCTIMAKAVVGANVVLGEHVVVHPGCVIGEGVEIGAHSVLHANVTIYHHCMIGERCNIFSGSVIGGDGFGYAPEEGRWVKIPQVGRVVIEHDVDIGANTTIDRGAIDDTIIHEGCKIDNLVQIGHNCRIGAHSVIAGCVGIAGSAVLGKHCRIGGAAMILGHLEIADGVTVSPGSMITRSLMKAGTYTALMPFQSHDEWLRTAAGIRRLGELAERVKQLEKQLAPQQVSGIQRDK", "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": "MRHYEIVFLVHPDQSEQVPGMIERYTGILTQAGGQIHRLEDWGRRQLAYPIIELHKAHYVLMNVETTAEAVEELETAFRFNDAVLRSMVMRTKAAITEASPMAKAKDERDTRRSSEERAPRAEATEEAEESAENTAE", "text": "FUNCTION: Binds together with bS18 to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family."}
+{"protein": "MFVDIAKIYVKAGDGGDGIVAFRREKYVPAGGPAGGDGGKGGDVIFVADRELNTLLDFKYKRHYKAQNGERGGPNNMHGKDGEDLIIKVPVGTVIKDAETGEIIADLSREGDRAIVAHGGRGGRGNAHFATATRQVPRFAEVGEKGDELWVILELKVLADVGLIGYPNVGKSTFLSVATNARPEIANYPFTTKYPNLGIVYISEGESFVLADIPGLIEGASEGAGLGHQFLRHVERTKVLIHIVDVSGSEGREPVEDFIKINEELKKYSPELAQKPQIVAANKMDLPDAQAYFELFKEEIEKMGYEVYPISAATGMGIREVLKRAYELLKQQKAAENIEEDAKPRTFVYYKKKDVKPLTVRKENGVYVVEGTVVEKVARNIVLNDHDSFRYFQNFLNKLGVFDKLREMGIQDGDIVRILDVEFEYYE", "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": "MSMSDPLGDMLTRIRNALGRKKDKVVTPASKLRAHVLDVLQSEGYIRGYNQVDLGDGKAELEIELKYFEGMAAIRDISRVSKPGRRVYVSAKSLPQVANGLGISVLSTPKGVMADHEAREQNVGGELLCRVF", "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": "MKETRSKQPDITPDMLLRAYSIGLFPMADSADDPELFWVEPEIRGIIPLDRFHVSRSLAKAIRRRPFDIRFDTAFAEVMEGCAQPAPDRPTTWINDTIRSLYAALHNMGHAHSVEAWEGDALVGGLYGVSLGAAFFGESMFSRRTGASKICLVHLVERLRSKGFQLLDTQFTTEHLKSFGAVDVPKAQYEVLLAKAIASPNLEF", "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": "MKVLSSLASAKTRYPDCQVVRRRGRVYVICKSNPRFKAVQGRKKRR", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
+{"protein": "MGSTRLRNASVWLCGLLCLLQVVPSINADVSGCKPGFSSAEYIFSVNRRELERGRKLGKVNFSDCTTRKHGLYDVGDSRFRVLPDGTVLVKRHVKLHKDTKFTISTWDARGIKHSTNIAVASKRHRSGEEAHSRSSKLPVLTFPETHTGLKRKKRDWVIPPIKVSENERGPFPKRLVQIKSNKDRFNKVYYSITGQGADNPPQGVFRIEWETGWMLVTRPLDREEYDKYVLSSHAVSENGSPVEEPMEITINVIDQNDNRPKFTQDVFRGSVREGVQPGTQVMAVSATDEDDNIDSLNGVLSYSILKQDPEEPIPNLFTINRETGVISLIGTGLDREKFPEYTLTVQATDLEGAGLSVEGKAIIQITDANDNAPIFDPKTYTALVPENEIGFEVQRLSVTDLDMPGTPAWQAVYKIRVNEGGFFNITTDPESNQGILTTAKGLDFELRKQYVLQITVENAEPFSVPLPTSTATVTVTVEDVNEAPFFVPAVSRVDVSEDLSRGEKIISLVAQDPDKQQIQKLSYFIGNDPARWLTVNKDNGIVTGNGNLDRESEYVKNNTYTVIMLVTDDGVSVGTGTGTLILHVLDVNDNGPVPSPRVFTMCDQNPEPQVLTISDADIPPNTYPYKVSLSHGSDLTWKAELDSKGTSMLLSPTQQLKKGDYSIYVLLSDAQNNPQLTVVNATVCSCEGKAIKCQEKLVGGFDLPIILVILGSVLALLILFLLLLLFLKRKKVVKEPLLLPEDDTRDNIFYYGEEGGGEEDQDYDLSQLHRGLDSRPDIMRNDVVPTLMPAPHYRPRPSNPDEIGNFIDENLDAADNDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSNSNDEHDYNYLSDWGSRFRKLADMYGGDDDEE", "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": "MNIKFVVVGKLKEKYFKQGIAEYAKRLSRFCKFSIVEVPDEKAPENLSQAEMDRVMAEEGERILAKIKDREYVYALAILGKERSSEAFAKEIKDLTTYGHSDITFVIGGSLGLTPAVLKRADTQISFGKFTLPHQLMRLVLTEQVYRAFMINEGSPYHK", "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": "MSKETKLQVEAIKNGTVIDHIPAKVGIKVLKLFDMHNSTQRVTIGLNLPSSALGSKDLLKIENVFISEAQASKLALYAPHATVNQIENYEVVKKLALQLPERINNVFACPNSNCISHNEPVESSFKLSEKNNDIRLKCKYCEKVFARDVVTEIEA", "text": "FUNCTION: Involved in allosteric regulation of aspartate carbamoyltransferase. SIMILARITY: Belongs to the PyrI family."}
+{"protein": "MFLKHLTLQNFRSYEELSLDFNSRLIFFVGDNGEGKTNLLEAICMLSWLKSFRESEDSNLIRWGSENYFLRGKIKGDQKESVLEVGFTAKPTVKRKLKFNQEEVKKRTDLIGKFITVLLTPMDLKIIEGGPAERRKFIDAFISSFDPFYLECLLEYNKILKHRNALLKTGISDASHLSIWDRKLIEKGVLILNKRKEIVFGLNSFYQPNLNKLSGGKDELEMIYGPNVKDKDEFVEKLGRNLGKDLRLGYTSVGIHRDDLFIGADKRDITEFGSQGQKRSTVIALKAATFNYYRNVLDTMPVLLIDDVIRELDVKRREYFVDLVINAGQAFFTTTDLEGIQDYVGKLKDQKQIFLIQQGNIQFAK", "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": "MKKVHERFLEYVKVDTKSDETTRVTPSTKGQLELGKMLAEELKEIGVDEVRISEEGYVYACLKSNCNKDIPKIGFISHMDTAPDMSGKNVNPKIVENYDGKDIELGNGYTLSPSFSPELPMYKGQTLITTDGTTLLGADDKAGIAEIVTAIEYLINHPEIKHGDIKIGFTPDEEIGEGADHFDVEGFGADFAYTLDGGRIGELEYENFNAASAKVEIIGKNVHPGSAKGKMINSILVAHEFVSMLPLDEVPEKTEGYEGFSFLLDIQGEVEKTSLSFIIRDFDKEGFKNRKERFNEIAKELNKKYGEGTVTVTLKDQYMNMKEMIEPRMHIVETAEKAMKQCGIEPIKNPIRGGTDGARLSFMGLPTPNLFTGGENFHGRYEYISINSMEKAVEVILNIIKIYAEK", "text": "FUNCTION: Cleaves the N-terminal amino acid of tripeptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20B family."}
+{"protein": "MSSPTTPVPVISWTADEAIKFLKEWNFSLGIIVLFITIILQFGYTSRSMFVYVIKMVILWLMWPLTIILTIFNCVYALNNVYLGFSIVFTIVAIIMWVVYFVNSIRLFIRTGSWWSFNPETNNLMCIDMKGRMYVRPIIEDYHTLTATIIRGHLYIQGIKLGTGYSLSDLPAYVTVAKVTHLCTYKRGFLDRIGDTSGFAVYVKSKVGNYRLPSTHKGSGMDTALLRNNI", "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": "MAKQSMKARDVKRAKLAEKFFTKRVELKAVISDVNASDEERWNAVLKLQTLPRDSSPSRQRNRCRQTGRPHAFLRKFGLSRIKVREAAMRGEIPGLKKASW", "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": "MSWQTYVDDHLMCDIEGHEGHRLTAAAIVGHDGSVWAQSATFPQFKPEEMNGIMTDFNEPGHLAPTGLHLGGTKYMVIQGEAGAVIRGKKGSGGITIKKTGQALVCGIYEEPVTPGQCNMVVERLGDYLLEQGL", "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": "MPEQQRLASLDSSTASRLPAYSQTLFEAKTEKGLTFEAIAQHLGRSEVAVAGLFYGQVQASAEDVDKLSELLSVPKEAIAKQMMGFPDRGRAGPMPPVEPLIYRLYEIVQNYGYAFKAVMNEKFGDGIMSAICFNTTVDKEVDETGASWVVITLKGKWLPFARF", "text": "FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. SIMILARITY: Belongs to the cyanase family."}
+{"protein": "MAIYRRKASPIKIGDAIDYKDVELLSNFLTEQGKILPKRLTGLTNKQQNKVTKAIKRARMLSLLPFVNREGSL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family."}
+{"protein": "MAEAAPEIPPENENPQREPWEEWIGEILEEIKQEALKHFDPRLLTALGNFIYSRHGDTLAGAGELIKILQRALFLHFRAGCQHSRIGQSGGGNPLSTIPPP", "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": "MKFTKMHGCGNDYVYVNLFEEKLDDPARVSIYVSDRHFGIGSDGLITIGPSDKADFRMRIYNADGSEAEMCGNGIRCVAKYVYDHKLTDKTEISVETGAGIKYLTLYVEENKVSQVRVDMGEPILTPGDIPVVKADGSAYSDDYRVIDEPISAGNREWHMTCVSMGNPHAVVFVDDVAGFELEKYGPLFENHKMFPKRTNTEFVEILSRNEAKMRVWERGSAETWACGTGTCATVMACILNKKTDNKVLVHLRGGDLTIEYIPETNHVFMTGPATEVFSGEIDII", "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": "MQIYMVGGAVRDRLLGRPVNDHDWVVVGATPDDMVARGYLPVGRDFPVFLHPETREEYALARTERKSGRGYRGFVVQTSPDVTLEEDLSRRDLTINAIAASAAWTGAEDLFDPYGGARDLQARVLRHVTDSFREDPVRILRVARFAARFTDFTVAPETMQLMREMVHDGEADHLVPERVWQELARGLMEPQPSRMFDVLRDCGALAVVLPEVERLWGVPQRPEYHPEVDTGVHLMMVLDMAAHLQAPLTVRFACLTHDLGKGTTPHDVLPRHIGHEQRSARLLKAVCERLRVPVECRELADVVAREHGNIHRSGDLGAAALVRLLERCDAIRKPARLDEILLACECDARGRLGFADRPYPQRARINAALAAVQSVTTSSVAAHAAQLGLSGPKVGEMIHAARVQAVADWLHATAQPAPEPQGNAG", "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": "MTDPNSKGSTSKEGFGDWCLLEADCSDVENDLGQLFERDTDSDISDLLDDTELEQGNSLELFHQQECEQSEEQLQKLKRKYLSPKAVAQLSPRLESISLSPQQKSKRRLFAEQDSGLELTLNNEAEDVTPEVEVPAIDSRPDDEGGSGDVDIHYTALLRSSNKKATLMAKFKESFGVGFNELTRQFKSHKTCCKDWVVSVYAVHDDLFESSKQLLQQHCDYIWVRGIGAMSLYLLCFKAGKNRGTVHKLITSMLNVHEQQILSEPPKLRNTAAALFWYKGCMGSGAFSHGPYPDWIAQQTILGHKSAEASTFDFSAMVQWAFHNHLLDEADIAYQYARLAPEDANAVAWLAHNNQAKFVRECAYMVRFYKKGQMRDMSISEWIYTKINEVEGEGHWSDIVKFIRYQNINFIVFLTALKEFLHSVPKKNCILIYGPPNSGKSSFAMSLIRVLKGRVLSFVNSKSQFWLQPLSECKIALLDDVTDPCWIYMDTYLRNGLDGHYVSLDCKYRAPTQMKFPPLLLTSNINVHGETNYRYLHTTIKGFEFPNPFPMKADNTPQFELTDQSWKSFFTRLWTQLDLSDQEEEGEDGESQRAFQCSARSANEHL", "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": "MTRASLEKQPHEVASMFDGVAANYDLTNDVISLGQARLWRRAVAAAVDARPAQKILDLAAGTATSSQPFVKAGAYVVPCDFSLGMLKVGKERHPWMPFTAGDGMRLPFKDETFDTVTISFGLRNIQDTEVALRELYRVTKPGGRVVICEFSQPTWTPFRTVYTEYLMRAIPPAARAVSSNPDAYVYLAESIRDWPDQPALAALLQKAGWSKVAWRNLTGGVVALHRATRA", "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": "SVPVGETTLGRIFNVLGEPVDNLGPVQNSTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVSGGVGERTREGNDLYMETKESKVINEQNIAESKVALVYGQMNEPPGARMRVGLTASTMAEYFRDINKRDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLPETIKGFQMILPGELDNLPEQASYLVGNIDEAAAKAAALQAGG", "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": "MASLKDLRDRIASVKATQKITKAMQMVAAARLHRAQEAAQSARPYAKRMADILTSVAADVDGVDAPALMRGTGRDDVHLLVVCTAERGLCGAFNVQIARRAREQIKALLAAGKIVKIITVGKKGADILSRDYKSLMIDHIDLHAVKRIGFAEALVISQRIVDLFNEGAFDVCTLFYSEFVSVINQRPTAFGLIPMGAPKAAVEATDVVEQKETSKDSQSIVHEAIVYEYEPDAASLLEALVPRNLSVQIFRALLENVAGEMGAKMTAMDNASRNAGEMINKLTVAYNRQRQAQITTELIEIIAGAEAL", "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": "MNKQNLIDVEGSVTESLPNGMFRVRLDNGCQVPTHISGKIRRNHVRILPGDRVKVELSPYDLTKGRIIYRLRNKSSNDWITS", "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": "MTLQCTKSAGHWRMVVWDEEGFQGRRHEFTAECPSVLELGFETVRSLKVLSGAWVGFEHAGFQGQQYVLERGDYPGWDAWGGNTAYPAERLTSFRPVACANHRDSRLTIFEQENFLGRKGELNDDYPSLQAMGWDGTEVGSFHVQSGAWVCSQFPGYRGFQYILESDHHSGDYKHFREWGSHAHTFQVQSVRRIQQ", "text": "FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SIMILARITY: Belongs to the beta/gamma-crystallin family."}
+{"protein": "MILVYSTFPNEEKALEIGRKLLEKRLIACFNAFEIRSGYWWKGEIVQDKEWAAIFKTTEEKEKELYEELRKLHPYETPAIFTLKVENVLTEYMNWLRESVL", "text": "FUNCTION: Involved in resistance toward heavy metals. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CutA family."}
+{"protein": "MIAEIICVGTELLLGDILNSNAQFLAKQLANLGIAHYYQTVVGDNPDRIKQVLAIATDRSQILIFTGGLGPTPDDLTVATIADFFETPLIERPEIIEDITKKFARRGRIMTASNRKQALIPQGANILPNPIGTAPGIIWQPVQNITIMTFPGVPTEMKSMWQETAIPYMQSQGWCEQTIYSRTLKFWGITESSLAEKVAPFLEKENPTVAPYANYGEVKLRISARATSLELANKLIIPVEEEIKDIAGIDFYGINDESLASVVGKLLLESGETLAVAESCTGGSLGSMLTSIPGSSEYFYGGVISYENQVKITLLDVNLEDLMAEGSVSHVVAKQMASGVVKKLGTNWGISITGIAGPGGGSDTKPVGLVYIGIARYDDIVESFEYRFSNLRDRNWIRRVSVSTALDLLRRKLYLSKQRPQHHQA", "text": "SIMILARITY: Belongs to the CinA family."}
+{"protein": "MDDSNDSSSAGPDGRLHAVDPSLTERQRTILNVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGVDDDVAAPATEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGDGTLFLLKVVGDSMVEAAICDGDWVVVRQQHVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV", "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": "MAGKARVHELAKELGVTSKEVLARLSEQGEFVKSASSTVEAPVARRLRESYGGSKSDKTKAAPSGNGAAGATVKPSAPQSRPGPKPGPPVAQQPAAPAAPPAAPPAPPTPAAAPPSPAPAAPAAATPAEPAAPSARPGPTPGPRPGPSAPKPGAPKPAARTPRVGNNPFSSQQPVERPAPRPQGPGGPRPGPGAGGPRPGGGPRPGASPGSMPPRPQGARPGGGPRPGGGPRPGGGPRPTPGGAGRPGGGGGGGGNYRGGGAGGGAPAAGGGGFRGRPGGGGGGGRPGQRGGAAGAFGRPGGAPKRGRKSKRAKRAEYENMQAPVVGGVRLPHGNGETIRLARGASLSDFAEKINANPASLVQALFNLGEMVTATQSVGDETLELLGGEMNYVVQVVSPEDEDRELLESFDLTYGEDEGGEEDLEIRPPVVTVMGHVDHGKTRLLDTIRNATVREGEAGGITQHIGAYQVTVDLDGTERPITFIDTPGHEAFTAMRARGAKATDIAILVVAADDGVMPQTVEAINHAQAADVPIVVAVNKIDKEGADPAKIRGQLTEYGLVPEEYGGDAMFVDISAKQGTNIEALLEAVILTADASLDLRANPDMEAQGVAIEAHLDRGRGPVATVLIQRGTLRVGDSVVAGDAYGRVRRMVDEHGEDVEEALPSRPVQVIGFTSVPGAGDNFLVVDEDRIARQIADRRSARKRNALAARTRKRISLEDLDSALKETSQLNLILKGDNSGTVEALEEALLGIQVDDEVELRVIDRGVGGVTETNVNLASASDAIIIGFNVRAEGKATELANREGVEIRYYSIIYQAIDEIESALKGMLKPVYEEKELGRAEIRAIFRSSKVGNIAGCLVQSGIMRRNAKARLLRDNVVVAENLTISSLKREKDDVTEVRDGYECGLTLTYSDIKEGDVIETYELVEKART", "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": "MGNIRTSFVKRIAKEMIETHPGKFTDDFDTNKKLVEEFSTVSTKHLRNKIAGYITRIISQQK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS17 family."}
+{"protein": "MGRRRRRLPREPFEIAITGLSHEGRGIAHHDERTLFVHGALPGERVRAVYTKRRRSVAEARVVEVVSPAPERIAPHCPHFGVCGGCSLQHLTPERQVELKQSVLMEQFHHMGGVQPERVLAPLTGAPWGYRRKARLAVKHVPRKGGVLVGFREKHSPFVAEMDRCPVLDPRVGERLTELGRLIEGLSIPDRVPQIEVALGDETGALVFRNLAPLTAADLNRLAGFARDSGLAVYQQPGNEATMALVHDPVGRRLDYALPGHGVRLGFRPGDFTQVNAEINRAMVDQALDLLAVEPGQRVLDLFCGLGNFTLPLARRASEVVGVEGAEALVERGRENALRNGLDNVRFYGADLTLAAADQPWATGGFDRVLLDPPRSGAFEVLGLVAALGPKRIVYVSCGPATLARDAGELVHRHGYRLTAAGVMDMFPHTAHVESMAVFQREAQD", "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": "MTIKILPARLANQIAAGEVVERPASVIKELVENSLDSGATRIDIDIEKGGAKLIRVRDNGKGIAKDELGLALSRHATSKIHTLDDLEAIMSLGFRGEALASISSVSRLTLTSRPAAQEEAWSAYSEGRDMQVKLQPAAHPIGTTVEVLDLFFNTPARRKFLRTEKTEFAHIDELLKRIALSRFDVSINVRHNGKVIRQYRAAKNQLQTEKRIAAVCGNAFVRNMLRIELEHQGLKLHGWITTPDGARQQSDLQYCYVNGRMMRDKLINHAIRQSYEMSLKPDQFAAYVLFIELDPHQVDVNVHPAKHEVRFHQARLVHDFIYQALADALAQSSVIDKPQVNESAFHRAEPEERESQPETTPQYSPQSVSTTVPERVYQAIDKTPTYPGRTDYEIKPRDRAPSDSSVREARIADSFKRTDWIESKLAPKPNVGKERHAEPAPSKREVHAYHELLKTPDFESQQAEQPTSIESVREVSLPQVTALGKALVVVDEQFVLMSSDSGVALVSLPRSEFYRTKGQLTPSEGALKAQPLLVPLSMKLDTDLVRLAQDYQQDFAQLGIQLKARNDKALMVMGVPAPLRQQNLQNLVPDLLSYAQTWMKGEKASTQMLPALIDWLAVQVTTVKSHYTLSEAIQIIAELEQLRHGQLPLDDKTFVSAVDFSATIAKLKP", "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": "MELDIKGIMDRLPHRYPMLLIDRVLEMVPGKSIVAIKNVSINEPFFTGHFPHHPVMPGVLIVEAMAQASALFSFTDENGGLKCDGAKTAYYLVGIDGARFRKPVVPGDQLRLEVEAERLSCTICKYQGRALVDGQLVAEAKLMCAIRSLEE", "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": "MTPVQLSFNTAFTLGLMGVTFHRAHLLSALLCLEGMMLSLYMGLSLWPMQLESTTYMTTPLLLLAFSACEAGAGLALMVATSRTHGTDHLQNLNLLQC", "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": "MPVVSFSRREMERLWRSLSEEELTDLLDFTKMNLESFGEEVGFEVTSDRMDLVTLEGIVRCLKGISNEELGLPKYRVRRKAFEVRVGEGVAKVRPYVVAALVRDVDLRTEESLVALIEAQEKIHDTLGRKRRRVAIGLHDFSKVKPPIIYDARRAEEVHFVPLGEYAEMSAKEILEQTEKGKIYSHLIANPENLVPLIMDSREEVLSMPPIINSELTRLTPGVRDIFIDVTGTDLKAIWYALEIISSALAERGGEISTLDILYPDGRNIETPRHEPEEMEVDLDFIRSILGLNLSEDDVVMQLLRARLDAECSDGKVRVLIPGYRSDFLHPIDVAEEVSITLGLNKIGYELPKNVMTVGRPHPVEKVSRKVRTVMIGLGYQEVLNYIMTSRASLFHAVGREEREVVEISNPVSESYSVLRDALFPGLLAFLANNTHVRYPQKVFEIGDVVLIDERLENKTRDERRVAAAYADDSVGFEDIYSHLKVLFENLSYRIELEPRKERPFIEGRCASVLREGEEVGVIGEIDPEVLLNLGITVPVAIFEVALKVPGKEPLT", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily."}
+{"protein": "MLDLKRIRTDFDTVAAKLKNRGVSEDTLTHLKELDEKRRALLVQSEELKAERNIASAAIAQAKRQKEDATQQIADMQKVSADIKTIDNQLVAIDQQVTDIITVLPNTPHDSVPVGADEEDNVEIRRWGTPRDFDFEVKAHWDLGEDLDILDWERGAKVTGARFLFYKNLGARLERALYNFMLDEHIKEGYQEIITPYMVNHDSMFGTGQYPKFKEDTFELADTNFVLIPTAEVPLTNYYRGEILDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPEESYQELEKMTANAENILQKLGLPYRVISLCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEADGKVKLLHTLNGSGLAVGRTVAAILENYQNEDGSVTIPEVLRPYMGGETVISPK", "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": "MPRFPDQLLYIGGRYVPARGGHTFEVVNPATGEVLANVHNADADDLDAAVDSAKAGQRHWAALTVVERSRILLRAVALLRERNDALAELETLNTGKPLSETRSVDIVTGADVLEYYAGVAQALQGVQVPLREGSFFYTRHEPLGVVGAIGAWNYPIQIALWKAAPALAAGNAMIFKPSEVTPLTALKLAEIFTEAGLPDGVFNVLPGDGASVGHALTEHPEIEKISFTGGTATGRKVMASASSSSLKDVTMELGGKSPLIVCADADLDLAADIAMMANFYSSGQVCTNGTRVFVPRALRTAFEARLLARVQRIHIGDPLDERTTFGPMVSAAHMQRVLEHIEQGKAEGARLLCGGERLRDGALAQGCYVAPTIFSDCTDVMTIVREEIFGPVLSLLTYDDEDEAITRANATSYGLAAGVVTPDLSRAHRLIHRLEAGICWINTWGESPAPMPVGGYKQSGVGRENGLATLQAYTRTKSVQVELERYASVF", "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": "MGKLTLLLLALLGWLQYSLWLGKNGVHDYVRVNDDVAVQQGSNAKLKARNDQLFAEIDDLNGGQEAIEERARNELSMIKPGETFYRLVPDQSRRNAASSSQNNLQK", "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": "MPKMKSHRGACKRFKATASGKIKRERMNGSHNLEKKNRKRTRRLHQSTMLDNATKEKQIKRMILA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
+{"protein": "MFPGARILATLTLALHLLHGAHAAIGPAGNMYIVNEDVSPDGFARSAVVARSVPATDPTPATASIPGVLVQGNKGDNFQLNVVNQLSDTTMLKTTSIHWHGFFQAGSSWADGPAFVTQCPVASGDSFLYNFNVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPSDPHLSLYDIDNADTVITLEDWYHIVAPQNAAIPTPDSTLINGKGRYAGGPTSPLAIINVESNKRYRFRLVSMSCDPNFTFSIDGHSLLVIEADAVNIVPITVDSIQIFAGQRYSFVLTANQAVDNYWIRANPNLGSTGFVGGINSAILRYAGATEDDPTTTSSTSTPLLETNLVPLENPGAPGPPVPGGADININLAMAFDFTTFELTINGVPFLPPTAPVLLQILSGASTAASLLPSGSIYELEANKVVEISMPALAVGGPHPFHLHGHTFDVIRSAGSTTYNFDTPARRDVVNTGTGANDNVTIRFVTDNPGPWFLHCHIDWHLEIGLAVVFAEDVTSISAPPAAWDDLCPIYNALSDNDKGGIVPS", "text": "FUNCTION: Lignin degradation and detoxification of lignin-derived products. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "MLQEFKTFIMKGNVLDLAVGVIIGAAFGKIVNSAVNDLIMPVVGLALGKVDFSNLFISLKGGEYATVAAAKAAGAPTLNYGIFLNTTLDFLIMALVIFMIIKAANKVRKTEEPAPAPVPRECPFCKSAVHDEASRCPHCTSQLNATA", "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": "MNQSILSPFGNTAEERVLNAINAFKHGTGVLVLDDEDRENEGDLIFPAETITSEQMAKLIRYGSGIVCLCITDERCQQLDLPPMVEHNNSVNKTAFTVTIEAAKGVSTGVSAADRVTTIQTAIADNAVPTDLHRPGHVFPLRAANGGVLTRRGHTEASVDLARLAGFKEAGVICEITNDDGTMARTPEIVEFAKKFGYSVLTIEDLVEYRLAHNI", "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": "MRNNKTPFLSAIFTASIRGYQRFFSAFTPSSCRFYPTCSNYALWLLYFESPLSAMGKIAIRILSCNPFCSGGIAYPVTRLKRPSLLQSHKDFNRNFKTITFWLVPTAKSRTTYYIIKV", "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": "MGRDTIAEIITSIRNADMDRKRVVRIASTNITENIVQILLREGFIENVRKHRENNKYFLVLTLRYRRNRKRPYRNILNLKRISRPGLRIYSNYQRIPRILGGMGIVILSTSRGIMTDREARLEGIGGEILCYIW", "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": "MALSKDEKAATLKEFGLHETDTGSPEAQVALLSARINQLTEHLKDHKHDHHSRRGLLLLVGRRKGLLKYLASTDIERYRSLIERLGLRR", "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": "MTKFKLKIASRRSKLAMVQTLWVKEQLEKNIPDLEVSIEAMATQGDKILDVALAKIGDKGLFTKELEAQMLVGHADIAVHSLKDLPTNLPDGLTLGCITKREDPSDALVVNKKNKIYQLESLPPGSIVGTSSLRRLAQLRYKFPHLDFKDIRGNVITRIEKLDSGEFDCIILAAAGLKRLGFESRVHQIIPNEISLHAVGQGALGIECKSDDKEVLKIISVLEDKVSSQRCLAERSFLRELEGGCQVPIGVNSSIQNDEIALIGMVASIDGKRLIKNESIGNIKYPEEVGKKLAEKLKLQGADKILSEIFEQFRDK", "text": "FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. SIMILARITY: Belongs to the HMBS family."}
+{"protein": "MSVESFTPTALEFTPGAAHKVKTLVSEEGNDRLKLRVFVTGGGCSGFQYGFTFDEDVAEDDTIVEREGVALVVDPMSFQYLAGAEVDYQEGLEGSRFVIKNPNATTTCGCGSSFSI", "text": "FUNCTION: Required for insertion of 4Fe-4S clusters for at least IspG. SIMILARITY: Belongs to the HesB/IscA family."}
+{"protein": "MTPGELFTDGPDHVLNAGRRTLTLVVQNTADRPIQVGSHYHFAETNAALGFDRQAAHGMRLNIASGTAVRFEPGQQRTVELVDYAGERKVFGFRGLVQGGLDASGQSHKETT", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urease beta subunit family."}
+{"protein": "MVNPEENNRNLVVKPITEILQDDDKRSRKFGVEMKRQNRRALGVINHNLVGAKAYPCVVNKRRGLSQRKQESCDKKKLDSLHPSISRSQEETKKLKPSGNEFGDCIFIDEEEEKNEEVTLDQPMPMSLEEPYIEFDPMEEEVEMEDMEEEQEEPVLDIDEYDANNSLAAVEYVQDLYDFYRKTERFSCVPLDYMAQQFDISDKMRAILIDWLIEVHDKFELMNETLFLTVNLIDRFLSKQAVARKKLQLVGLVALLLACKYEEVSVPIVEDLVVISDKAYTRTDVLEMEKIMLSTLQFNMSLPTQYPFLKRFLKAAQSDKKLEILASFLIELALVDYEMVRYPPSLLAATAVYTAQCTIHGFSEWNSTCEFHCHYSENQLLECCRRMVRLHQKAGTDKLTGVHRKYSSSKFGYIATKYEAAHFLVSDSH", "text": "SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily."}
+{"protein": "MTRCDDSPSASQISITHVTQGSCVASSSPNEVYATILGSCICTCMCDPVAGVGGMNHFLLPSADVEDAQHLRYGSHAMELLINALLKLGAARQRIEAKIFGGAMMTPQLGAIGQANAAFARRYLKDEGIRCTAHSLGGNRARRIRFWPKTGRVQQMFLGSEDVVPNEQPQFRLQGGAGDVTFFDRHNNAEMPDPIKEPR", "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": "MTELSIRPEEIRDALREYVDSFQATSAGREEVGRVVVTGDGIARVEGLPHTMTNELLEFHGGVLGLALNLEVGEIGTVILGESENIEEGQEVRRTGQILSAPVGDGFLGRVVDPLGRPIDGLGEIVAEGSRELELQAPTVVQRQPVKEPLQTGIKAIDAMTAIGRGQRQLIIGDRQTGKTTVAIDAIINQRDNWTSGDPSKQVKCVYVAIGQKKSTIREVVNSLEEAGALAYTTIVAAPADEPAGFKYIAPYTGSAIAQHWMYNGQHALIVFDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGGGSLTGLPIIETKANDISAYIPTNVISITDGQVFLESDLFNQGVRPAINVGTSVSRVGGSAQVKAMKSVAGRLRLDLAQYRELEAFSAFGSDLDKASRDQLARGARLVELLKQPQGQPFPVERQVVSIWAGTTGKLDDVPVADIRRFESEFLDFVGRSYPGVYDAIVTTGKLSDDTIAMLESAVAEFKKQFTLSDGKPLVNEPAPSPLDPGLVRQESIPVHRPAARKDDEG", "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": "MISFEFPVTERTRILLRLEYLYGRLAYFIGKDHPHDHHAALQVLFELMETASRADLKADLLQELERQKQMLEALRDNPNVAEETLEGVLEEIERASSQLLALTGKFGQNLRENEWLMAIKQRAGIPGGTCQFDLPSYHLWQQRSAEVRRQDLRRWAAPLMPTADAAEILLHLLRDSGKTYHYVARKGAFQQMSGGKVVQLIQVAYDDNLELLPELSANKYALNIRFVSAVTGEARPRQTEQDVEFQLTNCKF", "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": "MNICLIDETGAGDGALSVLAARWGLTHDADNPMALVMTSARLELRKRDEPKLGGIFVDFVEGAMAHRRKFGGGRGEAVAKAVGIKGSYLPQVVDATAGLGRDAFVLASVGCHVRMLERNPVVAALLDDGLARGYQDAEIGPWLRERLQLIHASSLTALEAITPRPDVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLAPARRLAIKRVVVKRPDYAPPLGDVATPNAVVTKGHRFDIYTGTPA", "text": "FUNCTION: Specifically methylates the guanosine in position 1516 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family."}
+{"protein": "MAQKIIRTGSIEIANDKPMVVFGGMNVLESRDMAMQVCEEYVRVTEKLGIPYVFKASFDKANRSSVNSYRGPGLEEGMRIFEEIKRTFNVPLITDVHEPHQAAVVAEVCDIIQLPAFLSRQTDLVVAMAKTGAIINIKKAQFLAPQEMKHILTKCEEAGNDQLILCERGSSFGYNNLVVDMLGFGIMKQFEYPVLFDVTHALQMPGGRSDSAGGRRAQVLDLAKAGISQNLAGLFLEAHPDPDNAKCDGPCALRLDKLEPFLAQLKSLDELVKSFPIVETA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsA family."}
+{"protein": "MPTINQLVRKPRKPRTFKSKVPALNFGYNSMSRKQTNNTAPQKRGVATRVGTMTPKKPNSALRKYARVRLSNQYEVTAYIPGIGHNLQEHSVVLIRGGRVKDLPGVRYHIIRGALDTAGVEGRMNGRSKYGAKRPKK", "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": "MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPIQQPPEAQVPPQHAPRPAQPMQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA", "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": "MSWIERIKSNIAPTRKASIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMSARNRLHSLLDEGTMVELGSELEPKDLLKFRDSKKYKDRIASAQKETGEKDALVVMKGTLHEMPVVAAAFEFSFMGGSMGSVVGARFIRAVEQALEDNCPLICFSASGGARMQEALMSLMQMAKTSAALGKMQERGLPYISVLTDPTMGGVSASFAMLGDLNIAEPKALIGFAGPRVIEQTVREKLPPGFQRSEFLIQKGAIDMIVRRPEMRLKLASVLAKLMNLPAPSPDEPRESVVVPDQEPEA", "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": "MTSTCTNSTRESNSSHTCMPLSKMPISLAHGIIRSTVLVIFLAASFVGNIVLALVLQRKPQLLQVTNRFIFNLLVTDLLQISLVAPWVVATSVPLFWPLNSHFCTALVSLTHLFAFASVNTIVVVSVDRYLSIIHPLSYPSKMTQRRGYLLLYGTWIVAILQSTPPLYGWGQAAFDERNALCSMIWGASPSYTILSVVSFIVIPLIVMIACYSVVFCAARRQHALLYNVKRHSLEVRVKDCVENEDEEGAEKKEEFQDESEFRRQHEGEVKAKEGRMEAKDGSLKAKEGSTGTSESSVEARGSEEVRESSTVASDGSMEGKEGSTKVEENSMKADKGRTEVNQCSIDLGEDDMEFGEDDINFSEDDVEAVNIPESLPPSRRNSNSNPPLPRCYQCKAAKVIFIIIFSYVLSLGPYCFLAVLAVWVDVETQVPQWVITIIIWLFFLQCCIHPYVYGYMHKTIKKEIQDMLKKFFCKEKPPKEDSHPDLPGTEGGTEGKIVPSYDSATFP", "text": "FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MSNSPESSTPKQSIPARFPKWLRQKLPLGKVFSRTDGTIKNKGLPTVCEEASCPNRTHCWSRHTATYLALGDACTRRCGFCDIDFTKKPLPPDPQEGEKIAASAKALGLKHIVITMVSRDDLEDGGADALARIITTLHIELPEATIEVLASDFEGNIDALHHLLDARIAIYNHNVETVERLSPLVRHKATYRRSLMMLEQAAQYLPDLMIKSGIMVGLGEQESEIKQTLKDLADHGVKIVTIGQYLRPSRRHIPVKSYVSPETFDYYRSVGEALGLFIYAGPFVRSSFNADAVFEAMSQRERLSASIQ", "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": "MATQSVEGSSRSGPRRTIVGDLLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISMN", "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": "MAVQQNKPTRSKRGMRRSHDALTAVTSLSVDKTSGEKHLRHHITADGFYRGRKVIAK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
+{"protein": "MATLGVNIDHIATIRQARRTVEPDPVAAAVLAELGGADGITVHLREDRRHIQDRDVQLLRQTVRTHLNLEMAATDEMVGIALDIKPDYVTLVPEKREEVTTEGGLDIVGQIARIGEVVSKLQNAAIPVSLFIDAEPAQIEASVKVQAKFIELHTGRYAEATDETSRQQELAFLATGCEQAIKAGLRVNAGHGLTYWNVYPVAALPGMEELNIGHTIISRAALVGIERAVREMKQAIRGE", "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": "MFLGEYQHSLDEKGRITIPAKFREEIGYKFVATKGLDNCIFLYPQDEWQLIEKKLRSLPFTRADVRSFVRFFFSGAAELDLDRQGRSVLPLNLREYAGIDRDVIIIGVGTRVEIWSTEKWTDYNENAQSSYEEIAENLVDLGI", "text": "SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the MraZ family."}
+{"protein": "MAQIIDGRGLAEKLQKKLAEKTARLKEKTGQVPGLVVIVVGNNPASQIYVRNKERSALAAGFRSKVERLPEETSQEELLSLIETYNQNPDWHGILVQLPLPEHIDDEAVLLAIDPDKDVDGFHPLNMGKLWSGHPVMIPATPAGIMAMFHEYGIELEGKRAVVIGRSNIVGKPMAQLLLAKNATVTLTHSRTHNLAKTAKRADILVVAIGRGHFVTKNFVKEGAVVIDVGMNRDENGKLIGDVKFDEVAEIASLITPVPGGVGPMTITMLMEQTYQAFKRSLES", "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": "MQAELVIKNGLVILETGEVITDVAVQGGKIVAIGQDLSGERVIDATGLVVSPGMVDAHVHITDPGGGYRDEWEGYVTGTAACAKGGVTTFMEMPLNQIPATVDKTSLEIKYKAGENKLKVDVGSFGGVVPTNLADGIQELDEGGVSGYKCFLGTCGDRSIEGDFQNVDDYSLYEGMKQVAKTGKVLAIHAENAPITDKLGAVAYQNGETTLAAYVATRPVFTEVEAIQKAILFAKETGCRIHICHVACQEGVEEVLKAQAEGVDVTCETCTHYLYFTTDELDAIGPVVKCSPPIRDADQQAALWNHVQTGGIAFVTSDHSPCTPDLKDTTNAFEAWGGISGVQNNVDVLFDEAVQKRGLSLKQFADMIAANPADRYHLAQKGRISIGKDADFVLIKPNAPYILKAEDLEYRNKISPYIGREIGAQVIQTILRGETIYAQETGVTEAFNGVFIKN", "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": "MKLHELRPAEGSKKAPKRVGRGNGSGLGKTAGKGHKGQNARSGGGVRPGFEGGQMPLYRRLPKRGFTNIFAKEYVEVNVSRLNIFEDGTEVTPEVLKANGVISKVKDGVKILGNGTLEKKLTIKATKFTKGAVEKIESIGGKAEVI", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
+{"protein": "MEGAELIIQEIHREAEQKIQYILSEAQREAEKLKEEARKRAQSQAEWILRKAKTQAEIEKQRIIANAKLEVRRKKLAVQEELIGEVLSAMREKLAALPDDEYFEALVSLTKEAIEELGTKKIVLRSNERTLKLIDSRMEEFSEKVGVEVSLGEPIECIGGVLVESPDGTVRVDNTFDARIERLESELRATVAKALFG", "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": "MRLIPLRNTAEVGKWAARHIVNRINAFKPTAERPFILGLPTGGTPMEAYKYLIAMHKAGEVSFKHVVTFNMDEYVGLPKEHPESYYTFMHTNFFDHVDIPAENINLLNGNAADIDAECRRYEEKIKSYGKIHLFMGGVGVDGHIAFNEPASSLASRTRIKTLTQETRIANSRFFGGDANLVPKYALTVGVGTLLDAEEVMILVTGHGKAQALQAAVEGSINHMWTISCLQLHAKAIMVCDEPSTMELKVKTVKYFRELEAENVKDL", "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": "MAGRLRVALVAGEASGDILGSGLMQALRARHPEIEFIGVGGPRMEAEGLSSYFPMERLSVMGLVEVLGRLPELLRRRKRLIRTLIDARPDVMIGIDAPDFTLGVEHRLRQAGLRTVHYVSPSVWAWRQKRVLKIREACDLMLALFPFEARFYEEHGVPVRFVGHPLANTIPLQADRVAARERLGLPLDGQVVALMPGSRGGEVGKLGELFLDTAQRLLGERPGLRFVLPCASAARREQIERMLQGREPLPLTLLDGASHEALAACDAVLIASGTATLEALLYKRPMVVAYRVAGLTYRILKRLVKSPYISLPNLLAGRLLVPELIQDAATPRALATTLSPLLDDGSQQVEFFDAIHRALRQDASAQAAEAVLQLVERR", "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": "MTHFTVSCLLVALFLCQSLVHAAYNGYYGYSPAAAPYPAEEPQNIMNPVDSCWRLKSDWDVNREDLADCAVGFGSSTLGGKKGNIYVVTNPYDNAQNPHPGSLRYGVIQAKPLWITFAKDMVITLANELMVNSYKTIDGRGAKVEIAYGPCITIQDVTNVIVHGISIHDCKPGKSGKVRSSPTHVGHRKGSDGDAITIFGSSNVWIDHCYLASCTDGLIDVIHASTAITISNNYFTQHDKVMLLGHNDNFVKDVKMKVTVAFNHFGPGLVERMPRVRRGYAHVANNRYDKWIMYAIGGSADPTIFSEGNYFIASDKSYSKEVTKREVKGGWNNWRWRTSNDVFKNGAFFVPSGYGSIPLPYSSAQRFTVAPGNLVPSLTADAGPLNCNRNGPCY", "text": "SIMILARITY: Belongs to the polysaccharide lyase 1 family."}
+{"protein": "MIRSELIQIVADENPHLYQRDVERIVNTVFEEIIEAMSNGDRVELRGFGAFSVKHRDARTGRNPRTGEAVAVEAKSVPFFKTGKLLRDRLNGKED", "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": "MARKGILGTKLGMTQVFDENNKVVPVTVVKAGPNVVTRIRTPERDGYSAVQLAYGEISPRKVNKPVTGQYTAAGVNPRRHLAELRLDDAEAVTEYEVGQELTAEIFADGSYVDVTGTSKGKGFAGTMKRHGFSGQGASHGAQAVHRRPGSIGGCATPARVFKGTRMAGRMGNDRVTVQNLLVHKVDAEQGVLLIKGAVPGRTGGLVMVRSAIKRGEK", "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": "MIDAEGYRANVGIVIINDMGQVFWARRYGQHSWQYPQGGVDEGETAEQTMYRELHEEVGLKPEHVKIVASTKHWLKYKLPKRYIRHDSKPVCIGQKQKWFLLKLTAAESSVDLLHSSHPEFDDWRWVSYWYPVRQVVSFKRDVYRMVMKEFANFALPLTYERRPDRRKRRA", "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": "MNTLDETLLKEIISSNKKYTNYGQVASYIPELKNARRNDLGICIIDSENNLYSAGNCSTKFTIQSISKPIVLAMALMDNDWEDVFSNVGMEPSGDPFNSIMKLEINDTKKPCNPMINAGAIVTTSLINGSCLEEKEERMLSFFRKLAKNDNIGINYDVYKSEKMTGDRNRAMAYLLKSDGFIRGNVEDVLDLYFKQCSIEIDSVDLARIGINLANYGVDIENGEHLMSEMVSRIVKTFMMTCGMYDASGEFAIKVGIPAKSGVGGGIMASVPGRMGIGVYGPALDKKGNSVAGVKVLEELSNKLKLNIF", "text": "SIMILARITY: Belongs to the glutaminase family."}
+{"protein": "MTMRIFNFSPGPATLPEPVLRQAQAEMLEWNAVGASVMEISHRSAEFIALAKGIESDLRCLLGVPDDYAVLFLSGGATTQQALLPLNFAAPGQTADYVVTGHWSKTALKQASPYVNINVVADGERDGFQDIPNRAGWRLSKDAAYVHMTANETIHGVEFRQTPDVGDVPLFADFSSSIAADLIDVSKYDLIYAGAQKNLGPVGICVVIVRRTLLERTGQPRADIFTYASHAERDSMLNTPPTFNWYLLGLTVKWMLAEGGVQEFARRNQAKAQLVYQTIDQSGGFYRNGVAAAVRSRMNIPFFLPNVEQDARFAAEAKAAGLLSLKGHKAVGGIRASLYNAMPLAGVQALVAFMHDFQQRYG", "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": "MTNPSPKLTPMFEQYLRIKEDYPDALLFYRMGDFYELFFDDAETTARELQIALTCRNPNAELKAPMCGVPYHAVEGYISQLLDKGYRVAICEQIEDPKEAKGLVKRAVTRVLTPGTVIDDANLDAKEHNYLGALFWNQDAEAGAFAWVDVSTGEWSGLYSRKLAELWQWAQKMAPRELLLPEGVDTPAMATLGTTQTVRVPARSHFDLKSGTERVMRAQGVADLGSLGLEGKPELVRACAALLAYLAQTQKQELSHLAPFKPLNLGRHLIIDEVTERNLELFHRLDGRKGPGTLWHILDRTLTPMGGRLLEERMHHPWREASPIRETQQVVEWLFQDDVRREALRTALDLVYDLERLSTRIFLNRATPKDFIALRQSLSALPAVRATLERPANPEGTYPTDAETSGDTLPKPLSDMLSAWDDLADYADLLRRALTDNPPHLVTEGGLFRPGFDPDLDELLDLAEHGEARLQELLAEEQTVSGLPKLKLGYNRVFGYFFELSRAGADSVPEHFVRRQTLANAERFTTERLKELEEKLVSATDRRKTLEYRLFQSLRDTVAEARPRVLFMADMLAHLDFWQSLADVARRNGWVRPDVHTGHDIVIREGRHPVVEAMQGSASFVPNDLRMDEKRRLLLITGPNMAGKSTVLRQTAIICLLAQMGAFVPAREASIGIADRIFSRVGASDNLAQGQSTFMVEMMETARILRQASKRSLVILDEIGRGTSTFDGMALAWAVVEELTRRAGGGIRTLFATHYHEITSLEGRIPGVHNMNIAIREWNGDIVFLRRLVPGPADKSYGIEVARLAGVPHSVVQRARELLADLERTRDAARGTNSAPSRQTLPGLDLPSKQEQVDTIVAPPPCSGVEHPLLVALRDIDTDDMTPLEALKRITEWKQLWGTTREDRS", "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": "MKCIVGLGNPGKKFEMTRHNVGFLAIDRLAEKHGISLNEAKFNALMGTGRINGERVVLVKPLTYMNLSGEAVRPILDYYKIEIDDLLVIYDDLDMVPGKLRFRPKGSAGGHNGIKSLIQHLGTAEFKRLKLGIGRPPHPIKVVDWVLMNYRKDELPELNETLDNAVTAATDFVDTDWLALMNRYN", "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": "MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHALEMQHILGALSLDAYLITGNGTRVHSLEGELLHRDDLPADVAELVLYQQWDTRASMHIFNDDGWFTGKEIPALLQAFVYSGFRYQIIDVKKMPLGSVTKICFCGDHDDLTRLQIQLYEALGERAHLCFSATDCLEVLPVGCNKGAALTVLTQHLGLSLRDCMAFGDAMNDREMLGSVGSGFIMGNAMPQLRAELPHLPVIGHCRNQAVSHYLTH", "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": "MRRTVIGDETTARDVARADWVAGAGGVVRVGLTGGIASGKSTVSQMLGERGAVIIDYDRLSRDVVAVGTQGLAQVVEAFGREVLVADGSLNRSALGSIVFADLQARRRLEAIIHPLVEEAAHRVDEEARAADGLVVVVHDIPLLVETGRADEFDVVMVTDVDPAEQVRRVVERDGCSQADAWARIHAQASREEHLAVADVIIDTSVPLEDLPEQIDRVWSRIAGALRFDRR", "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": "MARIAGINIPDQKHTVIALTAIFGIGRTRARAICASTSIAEDAKIKELSEAQIDILREEVAKYTVEGDLRREISMNIKRLMDLGCYRGLRHRRSLPLRGQRTKTNARTRKGPRKPIRK", "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": "MGPQTGKRLLVMAGGTGGHVFPALAVARRLASEGWQIRWLGTADRMEARLVPQHGFDIDFIDIQGVRGNGLLRKLAAPFKVLRSVMQARKVIREFKPDVVLGMGGFASGPGGVAAKLCGIPLVLHEQNAIPGMTNKLLSRIATRVLCAFEGAFGSLGTTVGNPIREELVALGAKPRESRTEALKVLVVGGSLGAKVFNDLMPSVTARIAQLQPVTVWHQTGKNNLSTVQAEYQLQGQDGGVKIAEFIDDMEAAYRWADVVLCRAGALTVSELAAVGLPSILVPYPHAVDDHQTMNARVLVDAGAAFLVPQPIATTELLADKLQLLAGDRDELTRMGERARAAAVLDATERVAEVCRELAK", "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": "MIIIDTGCANLSSVKFAFDRLNIKAEISRDIATIKSADKLLLPGVGTAMAAMKILQDRNLIETIQNATQPMLGICLGMQLMTEYSSEGNVPTLSLMSGHTDLIPNTGLPLPHMGWNKVRYEQDHPLFAGIEQDSHFYFVHSYAVLPNEHTIATSDYGVPFSAALGCKNFYGVQFHPERSGKNGAQLLKNFVENL", "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": "MLDFLNRMFSRDGGNSKNIAKERLRLVLVHDRSSVSPEIVEALKEDLIKVISSYMEIDERSLEVNLNNDEASVALVANIPVLGLKRRNV", "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": "MSKSENLYSAARELIPGGVNSPVRAFTGVGGTPLFIEKADGAYLYDVDGKAYIDYVGSWGPMVLGHNHPAIRNAVIEAAERGLSFGAPTEMEVKMAQLVTELVPTMDMVRMVNSGTEATMSAIRLARGFTGRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKHTLTCTYNDLASVRAAFEQYPQEIACIIVEPVAGNMNCVPPLPEFLPGLRALCDEFGALLIIDEVMTGFRVALAGAQDYYGVEPDLTCLGKIIGGGMPVGAFGGRRDVMDALAPTGPVYQAGTLSGNPIAMAAGFACLNEVAQPGVHETLDELTSRLAEGLLEAAEEAGIPLVVNHVGGMFGIFFTDAESVTCYQDVMACDVERFKRFFHMMLDEGVYLAPSAFEAGFMSVAHSMEDINNTIDAARRVFAKL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
+{"protein": "MATTERKPLLLDFEKPLAELANRIDQIRQLAEENGVDVSGEIRKLETRAMQLREEIFSTLSPSQRLQVARHPRRPSTLDYIQAISDEWMELHGDRCGGDDPALIGGVARLGGKPVVILGHQKGRDTKDNIARNFGMATPGGYRKAMRLMEHANKFSMPILTFIDTPGALPTVVAERQGAGEAIAYNLREMFSLDVPIICTVIGEGGSGGALGIGVGDRLLMFEHSVYTVATPEACAAILWKDASKSPQAAVALKIVSHDLKNLGIIDQILPEPTGGAHSDPLTAATTLKQALLDNLDELDRLTSQERRQLRYDKFRKIGVFTEVAH", "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": "MATKYPKFSRDLAQDPTTRRIWYAIATGNDFESHDGITEENLYQKIFATHFGHVAIIFLWASSLLFHVAWQGNFEQWIKDPLHIRPIAHAIWDPHFGEPAIEAFSQGGANYPVNIAYSGVYHWWYTIGMRTNNDLYQGSIFLLLLAALFLFAGWLHLQPKFRPSLTWFKSAEPRLNHHLAGLFGVSSLAWAGHLIHVAIPESRGVHVGWRNFLTTLPHPAGLTPFWMGNWGVYAENADTTGHIFGTSQGAGTAILTFLGGFHPQTESLWLTDMAHHHLAIAVIFIIAGHMYRTNFGIGHSIKEMLNARQFFGIRTEGQFNLPHQGLYDTYNNSLHFQLSIHLAALGTALSLVAQHMYSLPPYAFIAKDFTTQAALYTHHQYIAGFLMVGAFAHAGIFWVRDYDPEQNQGNVLDRVLKHKEAIISHLSWVSLFLGFHTLGLYVHNDVVVAFGTPEKQILIEPVFAQFIQAAHGKLLYGMDTLLSNPDSIAYTAWPNHANVWLPNWLEAINSGTNSLFLTIGPGDFLVHHAIALGLHTTTLICVKGALDARGTKLMPDKKDFGFTFPCDGPGRGGTCQTSSWEQSFYLALFWMLNLLGWVTFYWHWKHLGVWQGNVAQFNENSTYLMGWFRDYLWANSAQLINGYNPYGTNNLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLVWAHERTPLANLVRWKDKPVALSIVQGWLVGLAHFTVGYILTYAAFLIASTAGKFG", "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": "MQITVREALRDAMQEEMLRDEKVFVIGEEVAEYQGAYKVTQGLLEQFGSKRVIDTPITEYGFAGLAVGAAFAGLRPIVEFMTFNFAMQAFDHIVNSAAKTHYMSGGQVKCPIVFRGPNGAASRVAAQHSQNYTACYSHIPGLKVVAPYSAEDHKGLMLTAIRDDNPVIFLENEILYGHSFDVPDIIEPIPFSKAKILKEGSNVTIVTFSIQVKLALDVVNILQNDNIDCELIDLRTIKPLDTDSIIESVKKTNRLVIVEEGWFFAGVGASIASIVMKEAFDYLDAPIEIVSGKDVPLPYAVNLEKLAMPSANDLIEAVKKVCYYSI", "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": "MSKQLILALSKGRILQETLPLLADAGIEPAEDFGKSRKLLFDTNLPDVKLVVIRAVDVPTYVQMGAADVGVAGKDTLLEHGAEGLYEPLDLEISRCKLMTAGIVGAEPTHARRRVATKFVNVARRYYAQQGIQAEVIKLYGAMELAPLMNLADEIVDIVDTGNTLRANGMEPRELIDEVSSRLVVNKASMTMKHDRLKPLIERLGQAVASRRETQA", "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": "MKVIDQFKNKKVLVLGLAKSGESAARLLDKLGAIVTVNDGKPFEDNPAAQSLLEEGIKVITGGHPLELLDEEFALMVKNPGIPYNNPMIEKALAKGIPVLTEVELAYLISEAPIIGITGSNGKTTTTTMIGEVLTAAGQHGLLSGNIGYPASQVAQTASDKDTLVMELSSFQLMGVQEFHPEIAVITNLMPTHIDYHGSFSEYVAAKWNIQNKMTAADFLVLNFNQDLAKDLTSKTEATVVPFSTLEKVDGAYLEDGQLYFRGEVVMAANEIGVPGSHNVENALATIAVAKLRDVDNQTIKETLSAFGGVKHRLQFVDDIKGVKFYNDSKSTNILATQKALSGFDNSKVVLIAGGLDRGNEFDELVPDITGLKKMVILGQSAERVKRAADKAGVAYVEATDIADATRKAYELATQGDVVLLSPANASWDMYANFEVRGDLFIDTVAELKE", "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": "MQSADNLIWIDLEMTGLDVDSCKIIEIAAIITDKDLNIIAEAEPIAIHQSDEILNSMNEWCIKVHCETGLTQRVKDSKISTEAAEQQILEFIRKFVPYQSSPLCGNSIWQDRRFLAKYMPKIDEYCHYRMLDVTTLKLLNQYWGDGKGFEKKNTHKALDDIRESIAELKFYRQKLLSI", "text": "FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the oligoribonuclease family."}
+{"protein": "MRALFSSPAADTAGQQEALAVPLARLRFAAPLAALLGVMHTLAFAPNRWWWLQILSLAGLAALVRQAPRLRDVAWVGYAFGLGWFLSGIWWLYISMHVYGDMPAWMAAAAVLLFSAYLALHPALAAWLWQRLARGRQLSGAASALVFGAAWLVSEWLRGTEWTGFPWLNGGYAHTDGPLAGYAPLVGVYGVVAIAATLAGLLCAAAERRLHWLAGLAGVAVLAAGWPLHTIAWTQPVGKPITVRLLQGNVPQDVKFQQTGIDHSLALYTKMVTEQPAQLVVTPETAFPILLQDMPQEIALAIRTYVDTTGSSVLFGAANADSAVDYTNSAFGVGPWFKGVYRYDKHHLVPFGEFIPFGFHWFVHMMNMPLGDFRRGLPVQPPMPVAGQRVAPNICYEDLFGEEIAASLRQAERPATMLANVTNLAWFGDTIALDQHLQISRMRALESGRPMLRATNTGATAVVRPDGSVQARLPVFTLGTLQADVQGMQGLTPFVRTGNAPALGAGVLVLLAALARRRRAGAA", "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": "MLNPVWLKSLVAIVQTGSFQSAARALGLAQPTVSQHLQKLEEQVGVTLVQRSRSGCQPTTRALAFMPHATALLDMHARALEALHGNRERVGASSNIGTYLLQPFVRNYLTTANERGEVDLRIAANPDVADQLLAGQLDAAIMEWWLPHPDFEYRLWRVEPLVLIVSPDHALAEAGCIERDRLVDLPMLGGEPGSGT", "text": "SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MRVLGIETSCDETGIAVYDDKKGLLSHALYSQVKLHADYGGVVPELASRDHVRKIVPLIRQALADAGMTIEDIDGIAYTKGPGLIGALLVGACVGRALAFSWDKPAIGVHHMEGHLLAPMLEDDVPEFPFLALLVSGGHSMIVGVEGIGRYTVLGESVDDAAGEAFDKTAKLMGLDYPGGPRLSKLAAKGVPNSYRFPRPMTDKPGLNMSFSGLKTFAANTIAAEPKDEQTRANIACAFEEAVVDTLAIKCKRALKQTGYKNLVIAGGVSANTRLRSSLAEMMQGLGGKVYYPRGEFCTDNGAMIAYAGLQRLKAGQVEGLEVKGQPRWPLDTLEPVD", "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": "MADSVHLNRRGVLFVLSSPSGAGKTTISRMMLEEDKDIALSVSATTRPPRPGEIDGVHYHFVDTDTFKKMAADGAFLEWAHVFGHRYGTPRAPVEELLAAGKDVLFDIDWQGAQQLYQEAGPDVVRVFVLPPTMEELERRLRARGTDSDEVIAARMARAANEISHWDGYDYVLINDHVGECYGEVMAILRAERLKRRRQIGLIGFARDLIRSVPDADTKL", "text": "FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the guanylate kinase family."}
+{"protein": "MVLRLSQLFLRTLREDPVDAEVDSHKLLVRAGYIRRAAPGIYTWLPLGLSVLRKVEDIIRQEMSAIGAQEVHFPALLPREPYEATNRWTEYGEGLFRLQDRKGADYLLAPTHEEMFTLLVKDLYSSYKDLPLSLYQIQNKYRDEARPRAGLLRGREFIMKDSYSFDIDDAGLDASYAAHRAAYLKIFERLGLEVIPVAATAGAMGGSKSEEFLFPTEIGEDTFVRSAGGYYANVEAVTTVVPDEIDFSNAPAAEVLDTPNTPTIDTLVDAANQLAPRSESDGGAWTAADTLKNVVLAVTLPTGERQIVVIGVPGDRGVDLKRVEANIGSHLPIAGEIGLEAANEEDLKKLPWLVKGYIGPGLSLDEPVLGLEGSSKVLFLVDPRVVSGTTWVTGANAEGKHVFGLVAGRDFVWDGVIESTEVRAGDPAPDGSGPLETARGIEMGHIFQLGRKYAEALDLKVLDQNGKQQVVTMGSYGVGVTRAVAALAEANNDDRGLVWPRSVAPADVHVVAVGRGDEIFEAAEKLSLELEAAGLDVIFDDRPKVSPGVKFGDAELVGVPTILAVGRGLVDGVVEIKDRRSGEAENISVDKAVDYVVNAVRTR", "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": "MATERTLSIIKPDATRRNLTGKINAVFEDAGLRIVAQKRVQLSEAEAGAFYAVHKDRPFYGELVSFMVSGPVVLQVLEGENAVLKHRDVMGATDPKKAAPGTVRAQFAESIEANSVHGSDSLENANTEIAFFFAQTEILP", "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": "MSRISKEQVKHVAHLARLAITEEEAETFRNQLEDIITAAEQLNEVDTEGVVPTTHVLQMHNVLREDKPEKGLEVKEVLKNAPDHEDGQIRVPSVF", "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": "MNRIHAVILDWAGTTVDFGSFAPTQIFVEAFRQAFDVEITLAEARVPMGLGKWQHIEALGKLPAVDARWQAKFGRSMSAADIDAIYAAFMPLQIAKVVDFSSPIAGVIDTIAALRAEGIKIGSCSGYPRAVMERLVPAAAEHGYRPDHWVATDDLAAGGRPGPWMALQNVIALGIDAVAHCVKVDDAAPGISEGLNAGMWTVGLAVSGNEFGATWDAYQTMSKEDVAVRREHAASKLYAAGAHYVVDSLADLPEVIAHINARLAQGERP", "text": "FUNCTION: Involved in phosphonate degradation. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family."}
+{"protein": "MEYGSVEKDGSPDLDVDWLDDGWVALLRKWIDDAERAGVAEPNAMVLATVTPDGRPASRTVLCKSLDETGITFFTNYDSAKADDLAATPYAAVTFPWYQLGRQVHLRGPVSKVTAQVTEDYWSKRPRGSQLGAWASQQSRPIASRAALLEQLAQVTARFADHERVPVPPGWGGYLIAADVVEFWQGRENRLHNRIRVTGNRVERLQP", "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": "MIWHVQNENFILDSTRIFMKAFHLLLFDGSFIFPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSLVMSITALLFRWREEPMISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATMKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSLAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNGGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRKQEITPHVRNYRGSPLRSNNSIELSMIVCVIASTILGISMNPIIAIAQDTLF", "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": "MALWMRLLPLLAFLILWEPSPAHAFVNQHLCGSHLVEALYLVCGERGFFYTPKFRRGVDDPQMPQLELGGSPGAGDLRALALEVARQKRGIVEQCCTGICSLYQLENYCN", "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": "MDGVTVIDHPLVQHKLTIMRRKETSTGSFRRLLREISTLLCYEVTRDLELTMETIETPLQTMESPILEGKKLVFASILRAGNGLLEGMLDLVPSARVSHIGVYRDHETLQPVEYYFKAPEDVAERLIIVVDPMLATGNSSIAAIDKLKERGAHNIRFLCLLAAPEGIQNFRAAHPDVPVFTASIDSHLNEKGYIVPGLGDAGDRMYGTK", "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": "MCVRLAGNLFKTSDFIQCQKLILAVSGGSDSLALLFLVKDHLKTLSVPPEIIVVTVDHQLRQESAREASIVAEICRAHHIQHRIVRWEGKKPKTHIASSARVARYDLLFQEAQKQGATLIMTGHTLNDQVETYQMRYQRLQKSADVLQQEAFAEMGGGVHADVLQQEAFAERCERMGVGGHGGDIAEKSDGLIYERGLSCIPREALLRGTVRLIRPLLGVKRETLRTYLRLKEKTWIEDPTNEDCNFERVRVRQSLQPKKFTCIARKVHEAALQRRQQAKNIADLILALDITVEYGRCFIAKPALFLQKHPGFPFVVGLFAVLMGGGFYLLPHKKLSTLVQKLSLHSSEKRRFTYAGSVIEYNRSGIAFWREARNIKEAIVEKGQTFLWDGRYQITNHSHEPIKVGAAGLQQLKSLFKNNNFNLENTHFPSLKSLLMISNDKGYDIPELAYHAAMQHTITIRRIMAPFDWLLSSQDAAFVNVVQPFFDIKVKG", "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": "MSGFSLSDLESIVAERSKAPPEQSWTAKLVAGGQPKAAKKLGEEAIEAVMAAVTGDRDNLTYEAADVLYHLLVVLKIAEIPLENVMAELERRTAQSGLKEKASRQSS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family."}
+{"protein": "MEEFQGYLEFDGARQHNFLYPFFFRESIYVLAYDHGLNRLNRNRSIFLENAGYDTKYSSLIVKRLIFRIYEQNHLIISTNDFSQNPFFGHTNHFYYQTISALFAVIVEIPFSLRLVSSFGGKQLAKSYNLQSIHSIFPFLEDKLSHLNYVLDVLIPYPIHLEILVQTLRYRVKDASSLHLLRFCLYEYWNWKNFYTQKKSILNTKFFLFLYNCHVCEYESIFFFLRKRSSHLRSTSSGVLFERIFFYRKIEHLLKVFVNNFQDILGLFKDPFIHYVRYHGKCILAAKDTPLLMNKWKYYFVNLWQWHFSVWFQWQKVHINKLSKDNLDFLGYLSSLRLNPLVVRSQMLENSFLIDNVRKEFDTKIPICSIIGSFAKEKFCNVLGYPISKSTWMDSSDSDILDRFVRICRNLSHYHSGSSKKKNLYRIKYILRLSCVKTLARKHKSTVRAFLKRLGSVLLEEFLTGEEQVLSLIFSRGYSPSQRFYRVRIWYLDIIYLNDLVNHE", "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": "MVGSGGTGAPPPRSSPMTTLYVTQPGSVVRSEGGSLTVWVETEADDPGPNDSPVRRKRLASVEPHRLESLVLLGFTTITANAMRLCMANKIAVSLLDGGGGLAARVVPPEARSADLRLHQYALHLDPPERLIRARAVVTAKLRNAAAVLRGIRSNQASSAALASAITQTEASAEAAAAAVSAESLLGIEGNGAHQYFAGLRTAFVGGIPFLGRAQRPPPDPANSLLSFGYVLLGNRLTGLLEARGVDPCLGFFHDLRPGRPSLALDLLEELRHPVVDRLALRICNLRKIQPQHFEPDAERPGGVKLTVDGRKIFLEEWEGHLARPLREPGVAAEHRLDVHRLLQRQVDRLVSDLRGGEPYRPFRFGTSRPG", "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": "MTDQTTRLPVRRALISVSDKTGILEFARELQQLGVEILSTGGTYKLLKDNGVNAVEVADYTGFAEMMDGRVKTLHPKIHGGILGRRGVDDAIMNEHGIKPIDLVAVNLYPFEATIAKPGCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNASDYASVLEGLKAGGLTYAQRFDLMLKAFEHTAAYDGMIANYMGTIDQAKDTLSTEARSEFPRTFNSQFVKAQEMRYGENPHQSAAFYVEAKKGEASVSTAIQLQGKELSFNNVADTDAALECVKSFVKPACVIVKHANPCGVAVVPEDEGGIRKAYDLAYATDTESAFGGIIAFNRELDGETAKAIVERQFVEVIIAPKISQAARDVVAAKQNVRLLECGEWPAERAAGWDFKRVNGGLLVQSRDNGMITAEDLKIVTKRAPTEQEIHDLVFAWKVAKFVKSNAIVYAKQRQTIGVGAGQMSRVNSARIAAIKAEHAGLQVQGAVMASDAFFPFRDGIDNAAKVGISAVIQPGGSMRDAEVIAAADEAGIAMVFTGMRHFRH", "text": "SIMILARITY: Belongs to the PurH family."}
+{"protein": "MAILGLGTDIVEIDRIEAVISRSGDRLAKRVLSANEWAQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDELGKPKLRLWDEAERLAARMGVTSVHVTLADERHYACATVIIES", "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": "MTAIVEPSVTTGPIAGSSKVYRELDGVPGARVPFRRVHLSTGDHFDLYDTSGPYTDPDATIDLTAGLPARPGRVRDRGTQLQRARAGEITAEMAFIAAREGMPAELVRDEVARGRAVIPANHNHPEIEPMIIGKAFATKVNANIGNSAVTSSIAEEVDKMVWATRWGADTIMDLSTGKNIHETREWILRNSPVPVGTVPIYQALEKVKGDPTLLTWEIYRDTVIEQCEQGVDYMTVHAGVLLRYVPLTAKRVTGIVSRGGSIMAAWCLAHHRESFLYTNFDELCEIFARYDVTFSLGDGLRPGSIADANDAAQFAELRTLGELTKIAKSHGVQVMIEGPGHVPMHKIVENVRLEEEWCEEAPFYTLGPLATDIAPAYDHITSAIGAAIIAQAGTAMLCYVTPKEHLGLPDRKDVKDGVIAYKIAAHAGDLAKGHPHAQERDNALSQARFEFRWNDQFALSLDPDTAREYHDETLPAEPAKTAHFCSMCGPKFCSMRITQDVRDYAAKHGLDSEEAIEAAMADKSREFAEHGNRVYLPLAQ", "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": "MMNQDSLALIKQSIKTIPDYPIPGIMFRDVTSLLENAEAYKATIAILVAHYQSKGFTKVVGTEARGFLFGAPLALELGVGFVPVRKPGKLPRKTISQTYDLEYGKDTLEIHVDAINANDKVLVIDDLLATGGTIEATVKLIRELGGEVSHAAFVISLPEIGGEKRLQGMGIEVLSLCEFDGE", "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": "MAKKDYYEVLGLQKGATEKDIKRAYKRLAAKYHPDKNQGSKDSEEKFKQITEAYEILTDDQKRAAYDQYGHAAFEQGSSNGGFNGFGGGFGGFEDIFSEMFGGGFGGGSRRQHVVRGQDLRYDIEISLEEAVKGCKKDIRLSTLAECDNCHGTGAEAGTKVENCPHCHGAGRIRRQQGFFVTEAVCPSCHGTGKKIEKPCHSCHGDGRVQKAKNLSVTIPAGVDTGNQLRLSGEGEAGENGAPAGDLYVVIHVREHNIFTRDGANLYCEVPISFSMAALGGEIEVPTLDGKLKLKIPTETQTGKLFRVRGKGVVSPRGGYAGDLICKVVVETPVQLNEEQKELLRQLEISLDGKANHRPQQAGFLDSVKNFFTHLGK", "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": "MKRVLYPGTFDPITLGHVDVISKAARLFDEVVVGVAAQTPKETLFELEERMELVERTLKHFSFSNAIALPYTGLTVDFAKELNCCAIIRGLRAVSDFETEFQLALMNRRLKPEIETLFLMPEDNHIYLSSSLVKEISRLGGEISAFVPTVVMEALKQKIGKRNSNPVAISRPR", "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": "MYHIELKKEALLPRERLVDLGADRLSNQELLAILLRTGIKEKPVLEISTQILENISSLADFGQLSLQELQSIKGIGQVKSVEIKAMLELAKRIHKAEYDRKEQILSSEQLARKMMLELGDKKQEHLVAIYMDTQNRIIEQRTIFIGTVRRSVAEPREILHYACKNMATSLIIIHNHPSGSPNPSESDLSFTKKIKRSCDHLGIVCLDHIIVGKNKYYSFREEADIL", "text": "SIMILARITY: Belongs to the UPF0758 family."}
+{"protein": "MLECLSALLVLFAGGGGSVLAAVQSKTVADPNLCPGYNSQLISPFLSSCKRNLSECVSRYFDEQYAFCRSCVTVNNETMEDLDNCKCLQCALSSLNNSCFHDYCTSKDEYDKLQIVVEQFQLTNGVLDDGEILKPRGNKFSSRKLSYFVGQNNTLFRNPLQFEKNQLISALLTSLTNNQKTISSVDMFEVVDANNEVQYLRERTISGKTLSPATGYEEENDGDCSVKDKKWEGKIEYHENKKVSSENCSKDTDDKSGSKKERNTKAPLFHTATEIHMTRWSSWRPKKIFTRYLVNEYQSPKIITTVNRFYRTKTDTETGTTLITSTKAKRRWFPRTKIVTSTATSTFLSITTTTTTNAIATKSLVAVLNPDGLNKKAGINFGLFSANGELASPDEGGTPTVVRRDKISDPGAANEQATLFSTTFSQVPHLPELDSGEFISAASQLDKRIFIFTAITVSITTLMMLGFSYRSRVSFRDHSIDDSDDDNDWSDDEVEFDEEYFYSLPVSIPEKGISLDKMAQQLGVE", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MSQTVHFQGNPVTVANVIPQAGSKAQAFTLVAKDLSDVSLSQYAGKRKVLNIFPSIDTGVCAASVRKFNQLATEVENTVVLCVSADLPFAQSRFCGAEGLSNVITLSTLRNNEFLKNYGVEIVDGPLKGLAARAVIVLDENDNVIFSQLVDEITHEPDYDAALNVLKA", "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": "MSNDLPTKKDLVKWDQEDALNWTRGEYEIPNSKACGGEADGKAIYFCGNSLGLLNKKARQHIMEELDVWSTSSVTGHFNHPYQRPWKHVDEPLTPHLAKLVGAREEEVAHTSTLTSNMHNLFTSFYQPTEKRWKIVIEKGSFPSDWYAVHSHPRLHDKVLRPEQIDNAIIALVPREGEDTLRTEDILKVLDDNKDSIAIVWLPLVQYYTGQLFDISSISPKVHEIGALLGLDMAHGIGNVECKLNEWNVDFAVWCTYKYLNAGPAAIGGFYIRSGLEDGGRRLAGWWGNDARTRFHMSPNFQPTPGAKGYQHSCTPVFSSIPLLATLQLIEAVGFSNMVEKARRLTGTLEALLKASRYYVHPADPKGKIGFKIITPAAPYRGTQLSLVILPEEEHVMPKVFDRMLRKGLVGDERKPSVIRLSPVVLYNTFEEVGRAVEIVEEALEEEEEERKR", "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": "MTFLAIDVGNTRLKWAMYDAPKPGAAVLAHGAEFLDHIERLADSAWAGLPAPTRMLGCVVAGDAVRRRVMEQMEWWDVPSHWVVPSAEEAGLVNGYDHPTRLGSDRWVAMIGARHRLLRQGPARPLVVVMVGTAVTVEAIDAEGRFLGGLILPGHGIMLRALESGTAGLHVPTGEVKLFPTNTSDALTSGGTYAIAGAVERMVQHVIQHCGEEPACMMTGGAGWKMAPSMTRPFDLIENLIFEGLLAIAAERFR", "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": "MERAIFAGGCFWCMVQPFEEQDGILSVRSGYTGGHVVNPTYEQVCSKMTGHTEAVEIIFDESKISYADLVEIYWRQTDPTDSFGQFEDRGDNYRPVIFYFDEQQRKIAEQSKANLQASGHFNRPIVTTIEAAQPFYEAEKDHQAFYRKNPERYARSSAIRHHFLKENWS", "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": "MADDGMLLNFDLGSGPVKPQVKFKGGRWRDRKQAEKSARIASGKQSQPKSSTDGPDDGRSSKRQRTDDGDFDNGFDYKSANRFGSRPKHFDNDGHGGASGQSRSHQSDGKSKQVISRLFSFNPAQKTEADEKQGEWTAPEATNAPLSDVANFGTLTISARLVDELGKMGLERPTGIQNKVIPHMLTSSSDAFVQAETGSGKTLAYLLPILHRVLLLSVKGGAQIHRDSGAFAIIVAPTRELAKQVHTVLEKLIRPFPWLVSTAITGGESKKAEKARIRKGVNFLVATPGRLADHIDNTKALNLSIVRWLILDEGDRLMDLGFEDDLKKVITALKAVDVSDTLPDGTPLKALPERRVTVLCSATMKMNVQKLGEMSLADATFLAAKKEDMELDVQKSEMKAPAQLHQYYSVVPAKLRLVTLISYLKSTFSRRGKTMKAIIFISCADSVDFHYELLRDPNTTEAPVAASKEAESISKTVSKAAYITSPASPEVVLHRMHGSLSQPIRTATLKSFSACKSPSLLITTDVSSRGLDIPSVDLVIEYDPAFSFADHIHRVGRTARAGKPGDALLFLLPGTEEGYIELMKGSTTPTSQSYDSILQKGMMTKLEFPVETTAKPEDGHSFHDKAESLQLHIEQRLLEDTKRLELARNGFKSHIRAYATHTKEERKHFDISELHLGHTAKSYGLREAPGGIGQGVERKTKKRTNKGVEKDPEQAAGDERQNQNIIRKKSMMLMNSAADEFNIG", "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": "MLKPLGDRVVLKVEEKEQKVGGFVIAGNGQAATKTAEVVAVGQGIRTLNGELVSLSVKEGEKVLVENHAGVEVKDGDEAYLLVSEANILAVVE", "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": "MSDYKNTLNLPETGFPMRGDLAKREPGMLQRWYEQDLYGMIRTAKKGKKSFILHDGPPYANGSIHIGHSVNKILKDIIIKSKGMSGFDSPYIPGWDCHGLPIELKVEQLYGKPGEKLTAAEFRIKCREYAAEQVEGQKKDFIRLGVLGDWDRPYLTMDFKTEANIIRALGKIISNGHLLKGAKPVHWCTDCRSSLAEAEVEYYDKTSPSIDVAFHAVDAAAVATKFGVTRFNGPVSLVIWTTTPWTLPANRAISLHPEFAYQLVQVEGQCLILAAELVESVMKRAGITHWEVLGSCKGADLELMRFEHPFMGFDVPAIMGEHVTLDAGTGAVHTAGGHGPDDFVISQKYGLEIANPVGPNGCYLTGTHPLLDGKFVFKANDLIVDLLREKDALLHVEKLVHSYPCCWRHKTPIIFRATPQWFISMDQKGLRKQSLEEIKGVQWIPEWGQARIETMVANRPDWCISRQRTWGVPMSLFVHKDTEQLHPRSVELMEEVAKRVEQDGIQAWWDLDAADILGADAADYVKVPDTLDVWFDSGSTHSSVVDVRPEFNGHGADMYLEGSDQHRGWFMSSLMISTAMKGKAPYKEVLTHGFTVDGQGRKMSKSIGNTISPQDVMNKLGGDILRLWVASTDYTGEIAVSDEILKRSADSYRRIRNTARFLLANLNGFEPSTDCVAPEEMVVLDRWAVGRALAAQQDIEKAYANYDFHEVVQRLMQFCSVEMGSFYLDIIKDRQYTAKSDSVARRSCQTALFHIAEALVRWMAPIMSFTADEIWAFLPGKRAQYVFTEEWYDGLFGLAEGEGMNDSFWAELLKVRGEVNKVLEQARADKRLGGSLEAAVTLYADSELAERLNSLQDELRFVLLTSGARVAPLADAPADAQAAELVKGLKIAFSTAEGEKCPRCWHYTTDIGLVAEHADLCGRCVVNVAGDGEKRKFA", "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": "MPQWDLYVVITTKLGGGRPTLELVRGALAGGATAIQLREKELPARELVELGRAIRELTRDAGATFIVNDRLDIALAVEADGLHIGQEDLPAPVARKLLGPEKILGVSAGTTDEARQAEVDGADYLGVGSIFATGSKGDAGSPIGLEGLRAIRAAVKIPIVGIGGINPDNAAGVIAAGADGVSVISAVIGAADVAAAARRLREVVTRARGK", "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": "MAETLKEDSIMIREVWDYNLVEEFALIREIVDKFSYIAMDTEFPGVVLKPVATFKYNNDLNYRTLKENVDLLKLIQVGLTFSDENGNLPTCGTDKFCIWQFNFREFNIGEDIYASESIELLRQCGIDFKKNIEKGIDVVRFGELMMSSGIVLNDAISWVTFHGGYDFGYLVKLLTCKELPLKQADFFKLLYVYFPTVYDIKHLMTFCNGLFGGLNRLAELMGVERVGICHQAGSDSLLTLGSFRKLKERYFPGSTEKYTGVLYGLGVEDGTTTTVAN", "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": "MSAHDPHASLARPAAKAWHARLELGFERQPGGRTALAHRRHVGPLRVQRALYPEGDAICHAVIVHPPGGVAGGDRLEIDVKLDAGTHAVLTTPGATKWYKSNGLDARQRIDIDVGARAKLDWLPQNNLFFDATHASLEFVLKLGDGASVLGWDAAQLGRQAAGEAWSTGSVASFSKIVGPSGRALWVERARLDARDPLRAAPQGLGGFPVYGTLWALGPACTNALAESIAPALPFDDALRAGVTCIAPGTMLIRALAHSMEALQHLFAEQWLALRPIVHGIDAKPLRLWQT", "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": "MNGYSVFCVSDHTGLTIEAVAKSVLAQFPRIEFSLITLPFIDDAAKARAAAGRVAVTARALVFSSLTDPALRAHFKDAGLHVFDLFEHVSPAVERVLGEPATPSGGHTHGMASDYEARMDAVNFALRLDDGLSPEHLGQADLILVGVSRVGKTPTALYLALHYGLRAANYPLTPDDLANDGLPRALQPHLPRLRGLTLAPERLAAIREARLPGSRYASVAQCRSELDAAERLLAAHAIPLIDTSRMSVEEIAARLRAS", "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": "MDKIYTVSEVTYYIEALIDQDQYLSDIQVVGEIADLKERNGHLFFYLKDEFTTIGCVFFGGAYRSFGLSDGRIAQVAGQIKVYAPRGQYRLICRQAKILPERGTLFLRMKESYERLVAEGIFDKPKRPLPEYPSKIGLITSRNSAAYQDVLRTISDRYPLVEIFLYHTGVQGEDAKGSLLRALKDVNESDVDVVIITRGGGSRDDLWLFNDEDIVRAVYKLRHPVITGVGHQIDTVFIDLVADYSAHTPTAAAQAAVPNLSEIRMHFLELMQRMNLSIRKKIESFSQQIESSNKSLFQSMMSQILRTHSSIDSMKEKAFALMQRQMFSYEKKLSSAGTKLFSLNPVELLKKGYVIVEKDGKWVKSSSILREKDEISMRFFDGVVKVVVK", "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": "MTDKIRSVQGRVVSDKMEKSFVVAIERKVKHPLYGKFIRRTTKLHVHDENNEAKLGDLVEVRECRPISKTKSWTLVRVVEKAVIA", "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": "MNKKNLLSFNQNALNDFFVGLGEKPYRTKQIMQWIYKDHEFDFEKMLNFSKSLRDELSKVVCVELLRVVKQNFILDGVIKWVLALDKNNHIEMIYIPEKNRGTLCISSQVGCGLACTFCSTGMQGFNKNLTTAEIIAQVLIASRYLNSKTKRISNVVFMGMGEPLLNEHAVYNACDLLLDDLAFGLSRRKVTISTSGVVPAMLRMSERTPVSLAVSLHASDDHLRNELVPINQKYSLEELLKACKVYLQAGTQKRHILFEYVMLKGVNDSIEHANKLVKLLKGISAKINLIPFNSFEKTQYQTSSAQTIEKFQNILYHQGIRTMTRRTRGEDIGGACGQLAGKVLDKTKRTYDRRH", "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": "MPMQGAQRKLLGSLNSTPTATSNLGLAANHTGAPCLEVSIPDGLFLSLGLVSLVENVLVVAAIAKNRNLHSSMYCFICCLALSDLLVSGSNMLETAIILLLEAGTLATRASVVQQLHNTIDVLTCSSMLCSLCFLGAIAVDRYISIFYALRYHSIMTLPRAQRAIAAIWVASVLSSTLFITYYDHAAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIIRLHNRQLPAHKGFGLRGAATLTILLGIFFLCWGPFFLHLTLVVFCPQHLTCNCIFKNFKVFLTLIICNTIIDPLIYAFRSQELRRTLKEVLLCSWWPGCWAEGGGDSVWPGSCVTLRGPLPP", "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": "MYHVVAATINPAKIKAISQAFSDIFGAGSCHIEGVEVDSGVAAQPISNTETRTGARQRVMNARRVRPEADFWVAIEAGIEEDTAFAWMVVENQKLRGESRSASFTLPAIVMKGIHQGRELGDEMARLTGIDNIKHKGGAIGAFTAGHLTRSSVYHQALILALCPFHNDIYQRKADDEDSDLI", "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": "MGAVSCRQGQHTRVSAPQKGDNIQGHWVQGWKSLWCGMGTIRSGLEELWGLQRHQCLHQELLQPAPLLLEKPQSEWPVPQFISLFLPEFPVRPVREQQELKILGLVAKGSFGTVLKVLDCAQKAVFAVKVVPKVKVLQRDTLRQCKEEVSIQRQINHPFVHSLGDSWQGKQHLFIMCSYCSMDLYSLWSTVGWFPEDSIRLFAAELVLVLCYLHDLGIIHRDVKMENILLDERGHLKVTDFGLSRHLSQGARAYTICGTLQYMGEREAKVGREGDLRM", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MAYPAQMGFQDATSPIMEELLYFHDHTLMIVFMISSLVLYTISLMLTTSLTHTNTMNAQEVETVWTILPAIICILIALPSLRILYMMDEINNPSLTIKTMGHQWYWTYEYTDYENMTFDSYMTSTNDLTPGELRLLEVDNRMVLPTELPIRVLVSSEDVLHSWTVPSLGLKTDAIPGRLNQTTLMASRPGLYYGQCSEICGANHSFMPIVLELIPLKYFEKWLLTML", "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": "MITISDAAQAHFVTLLADQPEGTHIRVFVISPGTATAECGVSYCPPDAVEADDMEFEFNGFNAMVDEKSAPFLEEASIDFVTDQLGSQLTLKAPNAKMRKVASDAPLSERIDYVIQSEINPQLASHGGNIMLVEVTEEGTAILQFGGGCNGCSMVDVTLKDGIETQLLEKFPGELTGVKDVTEHQHGDHSYQ", "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": "MRVAFIYRWLLCGAAIVNVLVAQRHTASDNPSTYNIGGVLSNSDSEEHFRTTIAHLNFDQQYVPRKVTYYDKTIRMDKNPIKTVFNVCDKLIEKRVYAVVVSHEQTSGDLSPAAVSYTSGFYSIPVIGISSRDAAFSDKNIHVSFLRTVPPYYHQADVWLEMLSHFLYTKVIIIHSSDTDGRAILGRFQTTSQTYYDDVDVRATVELIVEFEPKLESFTEHLIDMKTAQSRVYLMYASTEDAQVIFRDAGEYNMTGEGHVWIVTEQALHANNTPDGVLGLQLEHAHSDKGHIRDSVYVLASAIKEMISNETIAEAPKDCGDSAVNWESGKRLFQYLKSRNITGETGQVAFDDNGDRIYAGYDVINIREHQKQHVVGKFSYDSPRGKMRMRINDSEIIWGGKQKRKPEGIMIPTHLKLLTIEEKPFVYVRRMGDDEFRCEPDERPCPLFNASGATANEFCCRGYCIDLLIELSKRINFTYDLALSPDGQFGHYILRNNSGAMTLRKEWTGLIGELVNERADMIVAPLTINPERAEYIEFSKPFKYQGITILEKKPSRSSTLVSFLQPFSNTLWILVMVSVHVVALVLYLLDRFSPFGRFKLSHSDSNEEKALNLSSAVWFAWGVLLNSGIGEGTPRSFSARVLGMVWAGFAMIIVASYTANLAAFLVLERPKTKLSGINDARLRNTMENLTCATVKGSSVDMYFRRQVELSNMYRTMESNNYVTAEQAIQDVKKGKLMAFIWDSSRLEYEASKDCELVTAGELFGRSGYGIGLQKGSPWTDAVTLAILEFHESGFMEKLDKQWIFHGHVQQNCELFEKTPNTLGLKNMAGVFILVGVGIAGGVGLIIIEVIYKKHQVKKQKRLDIARHAADKWRGTIEKRKTIRASLAMQRQYNVGLMATHAPGTISLAVDKRRYPRLGQRLGPERAWPGDGADVLRIRRPYDLGKGGLTASQLGLGKTRPQQNPLPPRYSPGYTSDVSHLVV", "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": "MNIVILAAGMGKRMQSALPKVLHPLAGKPLLSHVIDTARQLSPSRLCVIYGHGGEQVPQLLQAKDLSFAKQEPQLGTGHAVMQAVPQLDDHTPTLILYGDVPLTTAASLQRLLDSAGNDKLGILTVNLGNPTGYGRIVRENGAITRIVEQKDAKPAELEINEINTGIMVAPTAALKRWLAKLSNNNAQGEYYLTDIVASAVADGVAVVSAQPDHEWETHGVNSKVQLAELERIHQRNIAHALLEQGVTLADPARIDVRGTLTCGRDVTIDVGCVFEGDVSLADGVRIDANCVIHNSTIGARSHVRPYSHFENAVVGAECIIGPYARLRPGTVLAEDVHIGNFVEVKNSDIAAHSKANHLTYVGDSTVGSRVNIGAGTITCNYDGVNKSRTIIEDDVFVGSATQLIAPIRVGKGATLGAGTTLTKDAPADKLTVSRAKQITVDNWQRPVKIKK", "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": "MRAFKVTRDTNETKIHLELNIDGTGKYAITTGIAFFDHVLSSFAKHGAFDLKLDVLGDLEIDDHHTVEDVGIVLGKAFENMEKKNIKRFGWAIIPMDEAKASVSVDIGGRPYVVGDYTPSTEKIGNFSTENVVHFFESFSNNAKINLHFEVTGENEHHKVEALFKAFGVAMDMATQIDERKGIVSTKGVI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
+{"protein": "MSSYLFTSESVSEGHPDKIADQISDAVLDEILKQDPKARVACETYVKTGMALVGGEITTSAWVDIENLTRKVICDIGYEHSEMGFDGHSCAVLNAIGKQSADINQGVDRENPLDQGAGDQGIMFGYATNETDVLMPAAITYAHRLMEKQAEVRKSGKLAWLRPDAKSQVTLKYEDNKIVGVDAVVLSTQHSEEVSQKDLHEGVMEEIIKPVLPTEWLSKETKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGAARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQLSYAIGVADPTSIMVETFGTGKVANELLVSLVREFFDLRPYGLIKMLDLIQPIYRETAAYGHFGREQFPWEKVDHAEDLRIAAGLK", "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": "MSTDNKQSLPAITLAAIGVVYGDIGTSPLYTLRECLSGQFGFGVERDAVFGFLSLIFWLLIFVVSIKYLTFVMRADNAGEGGILTLMSLAGRNTSARTTSMLVIMGLIGGSFFYGEVVITPAISVMSAIEGLEIVAPQLDTWIVPLSIVVLTLLFMIQKHGTGMVGKLFAPIMLTWFLILAVLGLRSIIANPEVLHALNPVWAVRFFLEYKTVSFIALGAVVLSITGVEALYADMGHFGKFPIRLAWFTVVLPSLVLNYFGQGALLLKHPEAIKNPFFLLAPDWALIPLLILAALATVIASQAVISGVFSLTRQAVRLGYLSPMRIIHTSEMESGQIYIPFVNWLLYFAVVVVIVSFEHSSNLAAAYGIAVTGTMVLTSILSTTVARKNWHWNKYLVALILVAFLCVDIPLFSANLDKLLSGGWLPLSLGLIMFTIMTTWKSERFRLLRRMHEHGNSLEAMIASLEKSPPVRVPGTAVYMSRVLNVIPFALLHNLKHNKVLHERVILLTLRTEDAPYVHNVRRVQIEQLSPTFWRVVASYGWRETPNVEEVFHRCGLEGLSCRMMETSFFMSHESLIVGKRPWYLRLRGKLYLLLQRNALRAPDQFEIPPNRVIELGTQVEI", "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": "MALATLDWMSKDAERLAQCNHDHPQAVLGPQQLEDGRWVVRVWMPEASRVVLLHQGHEHALENPHHAWIFEGELSSNPGSQYRLRVERAGITHEQHDPYAFRQEWMGAMDRHLFAEGNHHHIWQRMGAHPHLQDGVAGVQFCLWAPNARSVSVIGDCTNWDGRHLPMQQRIGGIWELFVPGLGAGAHYKYEIHTQQGHCYEKADPYGFQHEVRPAQASVVASLKGYQWGDDAWLKQRDNRNPLEQPVSVYEMHMGSWMHGSWDEPYIEADGTPRAPVPAADLKPGARLLTYPELADRVIPYVKARGFTHIELMPMAEHPFDGSWGYQVTGFYAPTSRFGTLDEFRAFVDRCHAEGIGVILDWVPGHFPKDAHGLAFFDGSHLYEHGDPRIGEHKEWGTLIFNYSRNEVRNFLVANLVFWFEELHIDGIRVDAVASMLYRDYLRPDGEWIANEHGGRENLEAVRFLQQANSVLFHYFPGALSIAEESTTWPLVTMPTSMGGLGFNLKWNMGWMHDMLDYFELDHWFRQFHQNNITFSIWYAHTENFMLALSHDEVVHGKSHLLHKMPGSDELKFANVRALLTYMWTHPGKKTIFMGMEFAQRGEWNVWGDLEWDKLQFPEHQGVVNLVDDLNALYKSEPALWRNDFDSFGFQWIDCDDTNHSVVSFMRRDEKEGNWVVVVCNFTPEGHGNYRIGVPVDGFYTELFNSDGARYGGSNQGNLGGKFSDDWGMHSYGQSLDLCLPPLTVMVFKHDPNRQREAAKDEAAAKLGGSLG", "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": "MSTIRCDIVSAEKEIFHGEATLVVATGELGELGIAPKHAPLITRLKPGKVVVTTANGEHLDFAISGGILEVQPQVVTILVDTAVRAQDIEEAAVRKVKEEAERLLANRGNTVDVAEAQRRLTEATVQLQALERLRRNLKH", "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": "MAKVYYEKDVTVNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDKAKEDGFSVYTVAEAAKKADVVMILLPDELQPEVYEAEIAPNLQAGNSLVFAHGFNVHFDQVKPPVNVDVFLVAPKGPGHLVRRTFVEGGAVPALFAVYQDATGVATEKALSYADGIGATRAGVLETTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMYEGGLENMRYSVSDTAQWGDFVSGPRVVTEDTKKAMDTVLAEIQDGTFARGWIAEHKAGRPNFHATNEKENEHEIEVVGRKLREMMPFVQPRVKAGVK", "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": "MNNLAEKKCIPCSLGTPPLSSDEIKRYISQLHEEWKVINDHHLEREFKFKNFKEALSYTNVIGQLAEKEGHHPDMLLSWGKVKITLFTHKIDGLSESDFVFAAKVDKQQSE", "text": "SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family."}
+{"protein": "MKIGRQSKIVELISKHNIETQEELADLLVKAGYRVTQATISRDIRELKLTKVATDNGKQKYIVLTNQESGMSEKYIRILRDGFVSMDMAQNIIIVKTVSGMAMAVAAALDALHIEGIVGCIAGDDTIMCAIRTVPDTISVMEKLSKLINGNK", "text": "FUNCTION: Regulates arginine biosynthesis genes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ArgR family."}
+{"protein": "MMPNTDVSSLSMLGQQTETAKSPEEAVLEKVPSNHAGTDYVVRFTAPEFTSLCPMTGQPDFAHIVIDYIPSEWLVESKSLKLFLHSFRNHGAFHEDCSIYIAKRIVELLDPKWLRIGAYWYPRGGIPIDVFWQTGKPPEGVWLPEQGVATYRGRG", "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": "MSNRGRLGDAFLRPGSSSFLDFLSDHAPELLPGRSAAAGNAPLAPHATTIVALTFQDGVVMAGDRRATAGTMIASREIEKVFPADDYSVIGISGSAGIGVDLARLFQLELEHYEKIEGSLLSLDGKANRLGTLLRGNLPLAMQGFVVVPLFGGYDLDRGAGRIFSYDATGGRYEEHEHHGTGSGAIFARGALKKLWRPGMDAAEAVKVAVEALYDAADDDAATGGPDPVRRIWPVVTTVTAAGYRRVPEDELATLVDALLAVRTERGRLA", "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": "MAKVSKRVAANKAKIERTKFYPIDEALGLVKGCASAKFDESIDVAVQLGIDAKKSDQVVRGSVVLPAGTGKSVRVAVFAQGDKAEAAKAAGADIVGMEDLAEQVKAGNLNFDVVIASPDTMRIVGTLGQILGPRGLMPNPKVGTVTPDVAQAVKNAKAGQVQFRVDKAGIIHATIGRRSFEDTALKSNLAALLDALVKAKPATSKGVYLRKIAVSSTMGVGVRVEQASLSA", "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": "MIDPLAALVPVVVEQTSRGERSFDIFSRLLRERIVFVTGEVEDNMASLIVAQLLFLESENPKKDIYMYINSPGGVVTAGMAIHDTMQYIRPRVGTVCIGQAASMGSFLLAAGEPGMRVALTNARVMVHQPSGGARGMASDIEIQAKEILRIRKRMNDLYVKYTGKSLKDIEKAMDRDTFLEADEAKEFGIVDHVYDRRPALPGDDAPRDVSEGPTP", "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": "MLRYSVIFLIIAIIAAVFGFGGIAAGAAEIAKILFYLFLVIFLVSLVLGMIRR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0391 family."}
+{"protein": "MTHSIWHEKIKSFLPEHYYGRINHFLDEAYASGLVYPQRENVFKALQVTPLEETKVLILGQDPYHGPKQAQGLSFSVPEEISAPPSLINILKELADDIGPRDHHDLSTWASQGVLLLNACLTVPAGQANGHAGLIWEPFTDAVIKVLNEKDSPVVFILWGAYARKKKAFITNSKHHIIESPHPSPLSSYRGFFGSKPFSRTNAILEKEGMTGVDWLK", "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": "MSDIADRVKKIVVEHLGVEEEKVTETTSFIDDLGADSLDTVELVMAFEEEFGIEIPDDAAETIQTFGDAP", "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": "MKFAVIVLPGSNCDIDMFHAVKDELGEEVEYVWHEETSLDGFDGVLIPGGFSYGDYLRCGAIARFANIMPAVKKAAAEGKPVLGVCNGFQILQELGLLPGAMRRNKDLKFICRPVELIVQNGGTLFTSSYEKGQSITIPVAHGEGNFYCDDETLERLKENNQIAFTYGGDINGSVSGIAGVVNEKGNVLGMMPHPERAVDELLGSADGLTLFRSIVKNWRETHVATA", "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": "MTGKTQTSNVTNKNDPKSINSRVFIGNLNTAIVKKVDIEAIFSKYGKIVGCSVHKGYAFVQYMSERHARAAVAGENARVIAGQPLDINMAGEPKPYRPKPGNKRPLSALYRLESKEPFLSVGGYVFDYDYYRDDFYNRLFDYHGRVPPPPRAVIPLKRPRVAVTTTRRGKGVFSMKGGSRSTASGSTGSKLKSDELQTIKKELTQIKTKIDSLLGRLEKIEKQQKAEAEAQKKQLEESLVLIQEECVSEIADHSTEEPAEGGPDADGEEMTDGIEEDFDEDGGHELFLQIK", "text": "SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily."}
+{"protein": "MAKEAARVRRRERKNISSGVAHVNSTFNNTMITITDAQGNSIAWSSAGAQGFKGSRKSTPFAAQMAAEDVAKKAQEHGMRMLEVEVCGPGSGRESALRALQAAGFTITSIRDVTPIPHNGCRPRKKRRV", "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": "MTSDDTVWPGAGRSIETLAALSPGQAEAVLALLDEAARVDGQPAVSEQGRLQLRGGEREGVRHLLLSAGDTLVGYAQLEDTDPVEAPAAELVVHPAHRGRGHGRALGTALLAATGKRLRAWAHGGHSAARHLAQVLGLTLFRELRQMRRPLAGLDLAEPKLPDGVTVRAFVPGQDDAAWLAVNAAAFAHHPEQGSLTQRDLDDRKAEPWFDPAGFFLAERDGELIGFHWTKVHAQEGIGEVYVLGVRPGAQGGGLGKALTTIGLRHLEAQGLPTAMLYVDADNKAAVSVYERLGFATHETDLMYRTES", "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": "MRDETGETQDLEAEEIHPLFHGAPGSTEFRKLRKRLVRETRAAIETYDMIRPGDRWLVCLSGGKDSYTLLAVLHELKWRGLLPVELLACNLDQGQPGFPATVLPEFLTQRQVPHRIEYQDTYSIVKEKVPEGRTYCSLCSRLRRGNLYRIAREEGCQAVVLGHHRDDILETFFMNLFHGGRLASMPPKLLNEEGDLNVLRPLAFVAEADCDRFARAMNYPVIPCDLCGSQEGLQRMQVKRLLDEWESRSPGRRRVMFRALMNVRPSHLPDPKLFDFTALMPDMSDFREKDVPILREH", "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": "MNALGDVSPHTGPTQLAAGHAPPTPPHEDPLDDIYGSAPGSPSLLGVDPLNLDHPRERTHEILSDLPSRQRALDTDAYREGLSNSKGQYVQEGFDEGYSLGANLGIRVGYILGVLQGFVAAWRGSNDNLFKDTKKVYDTAQKELAIQELLSQQWVTEEGIWNWEVHGVEDDPTFREVAEQHPVVRKWTATVESMAAQWGVDLQAVEKVHGSNEEEQS", "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": "MSETLPLLLRAARGETVERPPVWMMRQAGRYMKVYRDLRDRHPSFRERSENPDLSYEISMQPFKAFQPDGVILFSDILTPLPGMGIEFDIVESKGPQIGDPIRSLSQVEALRPLQPEESMPFVGEVLGRLRSSVGNQAAVLGFVGAPWTLAAYVVEGKSSKNYAVIKKMAFQEPELLHKLLDHFATSIATYLRYQIDSGAQVVQMFDSWAGQLSPADYDTFAAPYQKKVVDLVKQTHPDTPFILYISGSAGVLERMGRTGVDIISLDWTVDMAEGLARLPDHIGVQGNVDPGLLFGTPEAIRDRIDDCVRKARGRRHILNLGHGILPGTPEENGRAFFEAGKTVMDRIGGA", "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": "MKAVIQRVCSASVVVEGEVVGEIGQGILVLLGVEKGDDEAKASWLAEKIISLRIFGDDSDKMNLSLRDVGGSLLAVSQFTLAGNCAKGRRPSFDSAAPPEEGRRLYDHFVQAVRAKGVATATGIFQADMRVSLVNDGPVTFILER", "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": "MNEHSLIEIEGLNKTFDDGYVSIRDISLNIKKGEFITILGPSGCGKTTLLRLLAGFEDPTYGKIKVNGIDIKDMAIHKRPFATVFQDYALFSHLTVYKNIAYGLKVMWTKLDEIPKLVSDYQKQLALKHLKLERKIEQLQKNNSNAQRIKKLKEKLQKLLEINKQKVIEFENKEKLRREDIYKNLEQLTKEWDLLSQKKLKEVEQQKQAIDKSFEKVENKYKKDPWFFQHSEIRLKQYQKKKTELKADIKATKNKEQIQKLTKELQTLKQKYANKKAIDKEYDKLVVAYNKKDYWTSYWETYTLQQKEAFEKRYLSRKLTKAEQNKKVSDVIEMVGLKGKEDRLPDELSGGMKQRVALARSLVVEPEILLLDEPLSALDAKVRKNLQKELQQIHKKSGLTFILVTHDQEEALVLSDRIVVMNEGNILQVGNPVDIYDSPKTEWIANFIGQANIFKGTYLGEKKIQLQSGEIIQTDVDNNYVVGKQYKILIRPEDFDLVPENKGFFNVRVIDKNYKGLLWKITTQLKDNTIVDLESVNEVDVNKTFGVLFDPIDVHLMEV", "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": "MTSILTNIAAMAALQTLRTIGSNMEETQAHVSSGLRVGQAADNAAYWSIATTMRSDNMALSAVQDALGLGAAKVDTAYSGMESAIEVVKEIKKKLVAATEDGVDKAKIQEEIDQLKDQLTSISEAASFSGENWLQADLSGGAVTKSVVGSFVRDASGAVSVKKVDYSLNTNSVLFDTVGNTGILDKVYNVSQASVTLTINTNGVASQHTVAAYSLESLTQAGAEFQGNYALQGGNSYVKVDNVWVRAETAATGATGQELAATTTAAGTITADSWVVDVGNAPAANVSAGQSVAGINIVGMGAAALDALISGVDAALTDMTSAAADLGSIAMRIDLQSDFVNKLSDSIDSGVGRLVDADMNEESTRLKALQTQQQLAIQSLSIANSASENVLTLFR", "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": "MNIPQDLKYTKTHEWVKIDGNKAKVGITDFAQYEITDVVHVELPEIGKQVKKAQPAAVVESVKSAFDIYSPLSGKILEVNDSVLRSPEVINQSPYENGYLFIIEFTDEKEIADLLEADSYKNLI", "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": "MMQPDHDLPYDLEGEILSHLPIQILARFRCVCKRWNTLFKERRFFNSDLGLARPQFILLAESKICSVDVNLDGPSIEVHNLPSDIPGYKLYMPMHVEYCDGLFLYATCYGIGICNPWLRQIRWFKSSYEGYDFSGMGYDNSRQDKHYKILGSYCTNTTMNASVTELGSDAWKSYEFAFHSWNLSMSPYSVSLNGNLYWVAYNHESRDYFIQSFDFSTVSFKHYCILPTKNGHRQCDGRSLAIFREDRFSFLEQEIYNTRNIEIWVTKETIKNGDGEAVEWVNLMSVLVPEWSSLSVNYYPPSYFVDEDKVGLTLVICCYNKEGKAYIYIAKGDKFHEIEIKDLVEYNPRHRTYFPNLIQVPTFTMSGRSITQHQVESRFAPLRGIQVSVGVGGDEWDDGFFDNVKEIIIHTNSLGIIFVKFYYRNGNVRVAGAAHGDSTETRGLMVPDDDYIEAVQGTYTESHITSMAFRLHKGNRSLRFGFFEGMSFVLGGARGSKIIGFYGRSSDLYLTAFGVHFSPLP", "text": "SIMILARITY: Belongs to the jacalin lectin family."}
+{"protein": "MSAVLSTENGLILKLYIQPKASRDQIVGLHGDELKVAITAPPVDGQANTHLVKFIAKQFRVAKSQVIIEKGELGRHKQIKVINPQQIPPEVTILLE", "text": "SIMILARITY: Belongs to the UPF0235 family."}
+{"protein": "MRQKFRFAAYVLAGFGLIFLALTIAGARLYTDWLWFQSVNYQRVFATIIISDLGLRLAVGLTFFVLLFLNLMLTRRPLLKVSQNSAIIREKDVLTIQSSPLSQLITPKLLLLAFIALSALMAFLFNFTVAGDWITFQKFLHPTSFGIKDPVFNLDIGFYVFKLPFYIFIYKVINWVILVSAFWVLAAYFVVYFIQGNPGAIFRNISARYHFSFLAAIFFGLKAAGYQLEQYSLLFSHHGAVWGPGYTATHATLLAYKVLTYIALLCALAILINLFLRRFKLVIYSIGVLLIASVLLGGIYPAAVQKFMVTPNEIAMERPYLERNINFTRLAYNLDEIEKRYFPAGRVLTAEDIRANQDTISNIRLWDWEPLQQTYGQLQEMRLYYEFKDIDVDRYIVNGRYRQVMVAARELNQEHLPAQAKTWVNQRLKFTHGYGIAMSPVNELTGEGLPAFFLKDIPPTGPTDLQVTRPEIYYGEASDQYVIVNTRSQEFDYPKGEENVFSTYEGDGGVRVANFLRRLMFAFSLGDYKLLLSSEVDNNSRVLYYRNIRQRVPKIAPFLQYDNDPYIILSEGKLYWMWDAYTTTDKFPYSEPYNKNDNYIRNAVKVVVDAYTGKVDFYISDSSDPLVLTYSKIFPGMFKPLDSMPEDLRRHIRYPVDLFKTQAKMYAVYHMEDPQVFYNKEDKWNLPTEIYASEEKPMEPYYTVIKLPGENKPEYVLILPFTPQNKKNMIAWLAARSDGENYGKLISYSFPKQELVYGPMQVEARINQDTTISQQLTLWDQGGSRVIRGNLFAVPIKDALLYVEPLYLQAEQSRMPELRRVIVAHGEKVVMEPTLDKALEKIFGEGATVQKSVQQPVDVTQPQPEKSIAELANTANQIYDEAMKKIKAGDWAGYGEDLSRLKQVLAELAERAGK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0182 family."}
+{"protein": "MALQPAAGAKDLNPRQVETNRQLTERLASVYRLWGYDEVSPPRVERLATLMAGGAIDSSDIVRLVADDPLGLRPEMTASIARAACTRFADRQRPLRLWASGTVFRTRSADEGGQCIEENLQSGVELFGVSGSEAEMELLSLLMASVQTLGLQTSQKPRLLLGHTALMDLVLRPFNGAVRDQIRTALIDFDRLAIESFDLAYAEKTRLLSLMDCRGTPDQVLAQLSSLYGEQPVFDELRRLCTHLASAAQAQAVTIQLDPTFQPHFELYTGLVFQLVCDGRSSPVVFARGGRYDDLVRRCGATDDRAFGAGFSLAIDPIRELISDLDAAEQQQSDVLIAFSTASNLESAMERQRSWHEQGRTAVMALEPLSSMQEAELQAKAQGGLQLDWVDP", "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": "MTDLFDYKEFLKTVTSQPGVYRMYDTAGTVIYVGKAKDLKKRLTSYFRAQVANRKTETLVKNIAQIDVTVTHTETEALLLEHNYIKLYQPRYNVLLRDDKSYPLIFLSADEHPRLAVHRGAKHEKGEYFGPFPNSYAVRETLALLQKLFPVRQCENSVYRNRSRPCLQYQIGRCSGPCVEGLVSEEEYQRQVDYVRLFLSGKDQQVLTQLITRMEEASQQLHFEDAARIRDQIQAVRRVTEQQFVSGDSEDLDVIGVAFDAGLACVHVLFIRLGKVLGSRSYFPKVPAGTELSEVVQTFVGQFYLQGSQGRTLPGEILLDFTLTEKDLLASSLSELAGRKIQIQSRPRGDRARYLKLARTNASTALITRLSQQSTIHQRMKELAKVLKLDEINRMECFDISHTMGEQTVASCVVFDANGPVRSEYRRYNISGITPGDDYAAMAQVLKRRYGKALDDQKIPDVIFIDGGKGQLSQAFDVFASLNVPWDKQKPLLVGVAKGSDRKAGLETLFLASEGEGFSLPPDSPALHLIQHIRDDSHNHAITGHRQRRSKVKNTSALEMIEGVGPKRRQALLKYMGGLQPLFNASVEEIAKVPGISQALAEKIHNALKH", "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": "MEQHNLTTVNEFILTGITDIAELQAPLFALFLMIYVISVMGNLGMIVLTKLDSRLQTPMYFFLRHLAFMDLGYSTTVGPKMLVNFVVDKNIISYYFCATQLAFFLVFIGSELFILSAMSYDLYVAICNPLLYTVIMSRRVCQVLVAIPYLYCTFISLLVTIKIFTLSFCGYNVISHFYCDSLPLLPLLCSNTHEIELIILIFAAIDLISSLLIVLLSYLLILVAILRMNSAGRQKAFSTCGAHLTVVIVFYGTLLFMYVQPKSSHSFDTDKVASIFYTLVIPMLNPLIYSLRNKDVKYALRRTWNNLCNIFV", "text": "FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MSHQGKIVQCIGAVIDVEFTPGEIPKVYDALVMEGSELTLEVQQQLGDGVVRTIALGSSDGLRRGMMVTNTQKQISVPVGTKTLGRIMDVLGRPIDEMGEIGANSLMPIHRAAPAFDELSASTELLETGIKVIDLVCPFAKGGKIGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEAFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGRLQERITSSKTGSITSIQAVYVPADDLTDPSPATTFGHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPLIIGEDHYNTAREVQQTLQRYKELRDIIAILGMDELSPEDKLSVSRARKIQRFLSQPFFVAEVFTGSPGKYVPLKETIKGFKGIVSGEYDDIPEQAFYMVGGIEEVLEKAKSIQ", "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": "MNLILFGPPAAGKGTQAKRLVEQRGMVQLSTGDMLRAAIASGSELGQKVKGVLDRGELVTDEIVIALIEDRLPEAEAAGGAIFDGFPRTVPQAQALDAMLARRGQKIDSVLRLKVDEPALIERISKRFAEQGRPDDNPEVFVTRLAAYNAQTAPLLPYYREQGKLTELDGMASVETVAGSIDAALSVVA", "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": "MRRAVIIPARLGSTRLKEKPLKNLLGKPLIRWVVEGLVKTGERVILATDSERVKEVVEDLCEVFLTPSDLPSGSDRVLYVVRDLDVDLIINYQGDEPFVYEEDIKLIFRELEKGERVVTLARKDKEAYERPEDVKVVLDREGYALYFSRSPIPYFRKNDTFYPLKHVGIYGFRKETLMEFGAMPPSKLEQIEGLEQLRLLENGIKIKVLITENYYHGVDTEEDLKIVEEKLKNL", "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": "MNLETIIGLEVHVELKTNSKIFSASPTEFGAEPNTQTSVIDLGYPGVLPTLNKEAVNFAMKAAMALNCEIATETKFDRKNYFYPDNPKAYQISQFDKPIGENGWIEIEVDGKKKRIGITRLHLEEDAGKSTHTADGSLVDYNRQGMPLIEIVSEPDMRTPEEAYAYLEKLKSIIQYTGVSDCKMEEGSLRCDANISLRPVGQEKFGTKAELKNLNSFTYVQKGLEHEQVRQEKELLSGGIIQQETRRYDEATKKTILMRVKEGSDDYRYFPEPDLVELYIDDEWKEAVRASIPELPDARKARYVAEIGLPAYDAHVLTLTKEMSDFFEATVADGADAKLTSNWLMGEVLAYLNKQQKELKDVALTPAGLSKMVQLIEKGTISSKIAKKVFNELIEKGGDPEEIVKAKGLVQISDEGTLRKVVTEILDNNGQSIEDFKNGKDRAIGFLVGQIMKATKGQANPPLVNKILLEEINKR", "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": "MSPNISLDNTYITLPEEFYTEQLPSKVPSPKLVKWNSTLAKELGLDSDFFQSEEGALVLSGNQILEDTTPIAEAYAGHQFGYFTMLGDGRAVLLGEIVTNDEERYDIQLKGSGRTPYSRGGDGKATLGPMLREYIISEGMKGLGIPSTRSLAVLTTGETILRETALPGAILVRVAKSHIRVGTFQFANQFLDTKELKALADYTIKRHYKEIFTKEDRYRHFLHEVVKNQARLIAQWQLVGFIHGVMNTDNMVISGETIDYGPCAFMDTYHPETVFSSIDTEGRYAYQNQPKMASWDLARLAEALVPLLNDNTEKAIEIAQEEINQFSKLYLTFWYEGMRKKLGLFHENDMDEDLIEALLGLMVKYEADYTNTFRDLTLNQTTQPNLKGSAEYQQWLDLWQDRRKKQEESLEDSIKLMESVNPTVIPRNHRVEEALERAVNYHDYNAMDSLVSVLQHPYDYKNQNDYYATPPGKTACGYRTFCGT", "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": "MHISKPAGPLPASVPFYRQLYFQVVVAIVLGALLGHFEPAFAESLKPLGDAFIKLVKMIIAPVIFLTIVTGIAGMTHLKTVGRVFGKAMAYFLFFSTLALVVGLVVAHVVQPGAGMNINPADLDQSAVKSYVEKSHDLTLVGFLMDIIPNSLIGAFTGDQVVNGKLTGPNILQVLFVAVLFGVSLALVGERGKPVLNLLEALIAPVFKLVHILMRAAPIGAFGAIAFTIGKYGVESLVNLAWLVGSFYLTSLLFVLVILGLVSRLCGFSVLKLIRYLKAELLLVLGTSSSESALPSLMEKMEKAGCEKSVVGLVVPTGYSFNLDGTNIYMTLAALFIAQATNTELTLGHQIALLAVAMLSSKGAAGVTGAGFITLAATLAVVPEVPVAGMALILGVDRFMSECRSLTNFIGNAVATVVVSRWENALDRDRLKLVLDGGEPPLLAPVGQPGVAPASLR", "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": "MISVVVVDDSAFMRKALSTMLEKDPEIRVVATARDGEEGLQVIRQHNPDVVTLDIEMPRMDGLTTLRHIMMEMPRPVLMVSSLTTEGAEATLKALELGAVDFIPKQLSKVSLDIVRIENDLREKVKEVSKRRMLRTPRPVRPAPTASAPAQTAQVASAAPATAPSRPAMPATRASRPVRDVVAIGVSTGGPPAVQKVLSQLPADFPASILIAQHMPAAFTGPFAKRLDGVCAISVKEAESGEKLKPGTAYIAPGGKHLRVEQRVSHMEVVVTTDPADALYKPSANVLMESVGQSMGRRALGVILTGMGSDGMEGMKVLKQKGGRSIAQSDATCVVYGMPKAIVDAGLADEIVDIDDMAAAIMNGLYK", "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": "MNSENALLQSDILAYLEQHEQKDMLRFLTCGSVDDGKSTLIGRLLHDSKMIYEDQLAAITKDSKKSGTTGDKVDLALLVDGLASEREQGITIDVAYRYFSTDKRKFIIADTPGHEQYTRNMVTGASTCDLAIILVDARAGVKTQTRRHSFLVSLLGIKHVIVAINKMDLMEFSEEVYENIKKDYLVFSEQLDIPDIQFVPISALDGDNVVNKSENTPWFEGSTLMKTLENIEIGNDANIDDFRFPVQYVNRPNLNFRGFAGTVVSGQIKKGDKITALPSGKQSTVRSIVGFEGEQEVAYTPLTTTITLEDEIDISRGDMIVKSDNLPLQSSAYEVNLVWMDETPLMPNKQYGFKFATKFVPGSVTDIEHQIDVNTMEHKEAVRLNLNEIGVGKIKLTQSVACDPYTKNRETGAFIIIDRLTNSTVGAGMVIDAIQDSGTKTEYSEFELEFNTLVRKHFPHWNATDITKL", "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": "MAVPKKRTSVSKKHIRRNIWKRKGYRAASKALSLAKSISTGHSKSFFVRQTSNKALE", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
+{"protein": "MSDKLIIFDTTLRDGEQSPGASMTREEKIRIARQLERLKVDVIEAGFAASSNGDFEAIRSIAQVVKDSTICSLARANDKDIARAAEALKPANSFRIHTFIATSALHMEKKLRMTPDQVYEQARLAVRFARQFTDDIEFSPEDGSRSDMDFLCRVLEGVIAEGATTINLPDTVGYAVPEGYAELIRSVRERIPNSDKAVWSVHCHNDLGMAVANSLAAVKLGGARQIECTINGLGERAGNTSLEEVVMAVKTRRDYFNMDVGIDTTQIVPASKLVSQITGFVVQPNKAVVGANAFAHASGIHQDGVLKARDTYEIMRAEDVGWTANKIVLGKLSGRNAFKQRLQELGVQLESEAEINAAFARFKELADQKAEIFDEDIMAIVSDEEQEHANEHYRFISLSQRSETGERPHARVVFNIDGSEQTGEAEGNGPVDATLHAIEGKVNSGAELVLYSVNAITAGTQAQGEVTVRLSKAGRIVNGVGTDPDIVAASAKAYLAALNKLHDKAVQKINPQI", "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": "MGQKVHPKGLRLGIIRDWDSRWYAGKEYKTLLHEDLKIREFIKKRLYQAGIASVEIERAANRIKVIVNTAKPGIVIGRGGAEVEALRKDLERLTGKQVNLNIAEIKKPELNAQLVAENVAAQLEKRIAFRRAMKQAVGRAMRLGAQGIKIACGGRLAGAEIARTEWYSEGKVPLHTLRADIDYGFAEANTTYGKIGVKVWIYKGEVLPERARVREGGSK", "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": "VLSPADKTNVKSTWDKIGGHAGEYGGEALERTFASFPTTKTYFPHFDLSHGSAQVKAHGKKVADALTNAVAHMDDLPGAMSALSDLHAYKLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFFSAVSTVLTSKYR", "text": "FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SIMILARITY: Belongs to the globin family."}
+{"protein": "MSDYFLLFIGTVLVNNFVLVKFLGLCPFMGVSNKIETAVGMSFATTFVLTLTAAVSYIVNKYILLPLDLVYLQTIGFILVIAVVVQFTEMVMHKTSPTLYRLLGIFLPLITTNCAILGLALLNINEDHDFVESIIYGFSAGVGFSLVLVVFSSMRERLAASDIPLPFKGGSIAMITAGLMSLAFMGFTGLIK", "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": "MNLLSLLLILLGIILGVVGGYVVARNLLLQKQSQARQTAEDIVNQAHKEADNIKKEKLLEAKEENQILREQTEAELRERRSELQRQETRLLQKEENLERKSDLLDKKDEILEQKESKIEEKQQQVDAKESSVQTLIMKHEQELERISGLTQEEAINEQLQRVEEELSQDIAVLVKEKEKEAKEKVDKTAKELLATAVQRLAADHTSESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRREIARTALVNLVSDGRIHPGRIEDMVEKARKEVDYIIREAGEQATFEVNAHNMHPDLVKIVGRLNYRTSYGQNVLKHSIEVAHLASMLAAELGEDETLAKRAGLLHDVGKAIDHEVEGSHVEIGVELAKKYGENETVINAIHSHHGDVEPTSIISILVAAADALSAARPGARKETLENYIRRLERLETLSESYDGVEKAFAIQAGREIRVIVSPEEIDDLKSYRLARDIKNQIEDELQYPGHIKVTVVRETRAVEYAK", "text": "FUNCTION: Endoribonuclease that initiates mRNA decay. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RNase Y family."}
+{"protein": "MAIAMAVVSFPSLLNKTTLSSSLFTPTFLPAKSSSLLIKSSPKTRFVVSSSMEAGIGVMGSKLGMMSFFEEDGTVVPVTVVGFREGNIVTQIKTLATDGYDAVQIGYRRVRDKKLTKPETGHLQKAGTIPMRHLQEFRLTNIEGFEPNQKLVFDEIFKEGDLVDVAGTTIGKGFQGGIKRHHFKRGQMTHGSKSHRALGSIGAGTTPGRVYKGKKMPGRMGGTRTKIRKLKIVKVDKELNVVMIKGALPGKPGNLLRITPAKIVGVNIPKN", "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": "MIQPQTHLNVADNSGARKLMCIRIIGASNRRYAHIGDVIVAVIKEAVPHMSLEKSEVVRAVIVRTCKELKRDCGMIIRYDDNAAIVIDQKGNPKGSRVFGAIPEELRQFGFTKILSIAPEVL", "text": "FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
+{"protein": "MDVLGIDEAGRGSVLGPLVIAGVIVPEKMDIVLERMGVKDSKRLTPNRRTILSRKLKKMFEYDLVVISAQDIDNMRADGINLNEIERIGMEKILSNLNPEKAIVDAVDIKAERFQNKLANDTGVNVVAEHKADDNYIEVSAASIIAKQERDAHIAEINKDYIKMGGIGSGYPSDPITKKFLTNFTYDEMPDFVRKSWATVEKMKNSQ", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
+{"protein": "MRVLGFMTGTSLDAVDMAVLETDGEGISAFGPAGERKLTDATREILLEATEAALKWERGEPEPQIFAKAAVTVAEEHFAAAEAFLAEHGLVWSEFDLLGMHGQTVLHERPQDGVPGRTVQLGDAGLLASLTGRPVAHDFRSADVAAGGEGAPLAPIYHLARARASGLEPPLAVLNVGGVANVTFWSGPGDFAAFDTGPGNGMIDLLVQARKAGRYDAGGRYASVGRVDEAVVRALLAHPYFEAPAPKSLDRYDFSLEPLEPLQLEDACATLVAFTAEAVGRGFELMGEVPREVVVTGGGRHNPEIMKALAARLPAPVKTAEDHGWRGDSIEAEAFAYLAARCARGQPISFPKTTGVARPMTGGRIVQPE", "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": "MARIIALDGAQGEGGGQILRSALSLSMITGQPFEMSGIRAGRAKPGLLRQHLTAVRAATEICGAQVNGDELGSQQLRFTPGPIRGGEYRFAIGSAGSCMLVLQTVLPALWFADGSSRVEVHGGTHNQAAPSADFICRVWEPLLARMGISQRTTLIKHGFYPAGGGAAATVVEPAASLRGLTLISRGETLRTTAEALLAAVPYHVGEREVATLEAHFPQAEKNVVALEGGCGPGNALSLMIQSEQLTELFAAFGVKGTSAEAVANQVAHEARRYLASPAAVGEHLADQLILPLALAGEGAFTVARASAHLLTNIAVVERFLPVRFSCEATESGYLVRVSD", "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": "MFEATTILGYRGEMGGKKFALIGGDGQVTLGNCVVKANATKIRSLYHNQVLSGFAGSTADAFSLFDMFERILESKKGDLFKSVVDFSKEWRKDKYLRRLEAMMIVLNLDHIFILSGTGDVLEAEDNKIAAIGSGGNYALSAARALDSFAHLEPRKLVEESLKIAGDLCIYTNTNIKILEL", "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": "MAKKQRYNTTQRKELRKKEVDYIKELETKIDEYDASINKPVFFKDLPISNSTLKGLNDSAFLKLTDIQRDSIPMSLKGYDILGAAKTGSGKTLAFLIPVLEKLYRERWTEFDGLGALIISPTRELAMQIYEVLLKIGTSTSFSAGLVIGGKDVKFEMERISKINILIGTPGRILQHMDQAIGLNTSNLQMLVLDEADRCLDMGFKKTLDAIVSNLPPTRQTLLFSATQSQSLEDLARLSLTDYKTIGNPDILNPSNGKVLGPSTPETLQQSYINVELPDKLDMLYSFIKSHLKSKMIVFLSSSKQVHFVYETFRKMQPGISLMHLHGRQKQKARTETLDKFNRAQHVCLFATDVVARGIDFPAIDWVVQVDCPEDVDTYIHRVGRCARYGKQGKSMIMLTPQEEEGFLKRLASRKIEPSKLTIKQSKKKSIKPQLQSLLFKDPELKYLGQKAFISYIRSVFIQKDKEVFKFEELPTDEFANSLGLPGAPKIKMKGTKSVEQIKQMKNASRQLLSLAKTNEDGELVEEKSKQPVRTKYDKMFERKNQTVLSEHYLNITKAQAQEDEDDDFISIKRTDHALNEEELPQLSLPSSRRAQKRALSKKASLSTKGNATRVVFDDDGAAHPVYELQGEEDFIKAGAAEDQKLEYLQKEKDVMNEVDVEDKQVAKQKKQEKKRKRLEAIRREMEADMDNESSGEEKVPFLGTGNLSDDMQDPDSDDEEGSRLRKRSRFETNNNYNDNDSDDGVIQVEEPQTLEDLESLTARLIDN", "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": "MHPAAEHSPLGKSSEYIATYMPSLLFPIPRTAKWAELGVTAQTLPWHGVDYWNCFELSWLLPSGKPVVAIGEFAIPADSPNIIESKSFKLYLNSLNQTVFATIGELQACLEKDLSAAAGKPVSVQVRTLAEVEAQGVVALPGQCIDALDVTISNYEQPQPELLRCNPERVVEETLHSHLLKSNCPVTGQPDWGSVVVEYKGRALDHASLLTYLISFRQHADFHEQCVERIYLDLKNLLQPEHLTVYARYVRRGGLDINPYRSTGAISPENVRLVRQ", "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": "MADPSAFYEPEEDELLSQLAIPIQNYQPLSEGDEYRRLQQLEQHAYAQQTAMAQEQEMEQLAVLELIPEDVKRFLVMFHQAILENDLPTITSMYESGWNKLTQAHYLNNEWPEAELIAPLVGNDQVFLTLYRELYFRHVYARLQPTIDDRFQSYENICELFNYLLNSEGPVPLDLPIQWLWDMLDEFVYQFTSFSHWRSSPKAKTEEELEMLAESPNIWSSYSVLNVLYSLVQKSQINEQLKAERAGKSVEEVTEVAGEYGSKPLYKNLGYFSLICLLHVHVLLGDPTLALQTMENVDLGNAAFLTRITACHVTTYYHVGCAYMALGRWPDAIKTFVSVLIFFIRMKQYHTRSYQYGSIAKTCERMYALLAICTTLSPGPSDENIMTIVKEHYGDQLAILQRGGPEALEAFKDLYLQACPKYLNVNPPPYEDASALEAWLANPPADATQRHLELFLSDVQAVQGVNGMRNLLKLYTSIDAAKLAAFSVSGEEEGEEEVLQQLMVLKSASSTYGRGQAETTLLDGERKVTNNLDFTIDGTMVHVEETTSHRRYAGFFIRNAEHAQRALTSIKSAPLPVRKPASSSAPAPATTAAPISKSGESAAPAPAEAPAAPEKKAGTWVPKSRQARIAA", "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": "MRSDTIKSGFEKAPHRSLLKATGAIRSSSDYRKPFIGICNSYNELIPGHTHLQELGRIAKEAVREAGGVPFEFNTIGVCDGIAMGHIGMRYSLASRELIADSVETVAEAHRLDGLVCIPNCDKITPGMMMAALRINIPVIFVSGGPMKAGHTPEGKTVDLISVFEAVGQCSNGSITEGELQNIEEHACPGCGSCSGMFTANSMNCLSEALGFALPGNGTIVAEDPRRLELVKAASRRIVDLVENNVRPRDILTRQALLNAFALDFAMGGSTNTILHTLAIANEAGLSFDFSELNALSAKTPYICQVSPATMAVHIEDVDRAGGISAILKELSSIDGLLDLSAITVTGKTLGENIANAEVLDRSVIRSISDPYSATGGLAVLYGNLAPQGAVVKTGAVSPQMMQHSGPAKVYNAQDDAIKGIMEGDVKAGDVVVIRYEGPKGGPGMPEMLSPTSAIMGRGLGDSVALITDGRFSGGSRGACIGHVSPEAAERGPIAALQNGDIITIDIPARTMSVALSESTIKERLAQLPPFEPKIKRGYLARYAQLVTSANTGAILGHL", "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": "MSLQPQSETLSFEAEVKQLLHLVAHSLYSNKEIFLRELISNSSDAADKLRYQALSDAALYENDADLKIWIDFDKDNRTITIRDNGIGMSREEVIENLGTIAKSGTRAFRELLAEKKAEDSQLIGQFGVGFYSAFIVADRVVVRTRRAGMKADQGVEWESTGEGEYTLKNIDKPTRGTEVVLHLKESEEEFLDPLRLRAIITKYSDHILLPIVMKKIKTSGADDEDKNETPEEEVVNRANALWVLPKDKIKDEEYKELYKHIAHDFEDPLAWVHNKVEGKLEYTTLLYIPARAPFDIWNREGQRGLKLYVKRIFIMDDAEHFMPMYLRFVKGIVDSNDLPLNISRELLQSNEVINKIKAGCVKRILSLLEDLAKNDKEKYASFWKAFGQVLKEGPAEDFANRDRIANLLRFASTHNDTDEQNVSLQDYISRMKPEQNRIYYIVADTYTSAKNSPLLEVFRKKDIEVLLMSDRVDEWLVAHLNEFEGKSLQSIAKGTLDLGDLEKEEKVETEKFEKDFDELLKQFKEVLGEKIKDVRITHRLTDSPTCVVFDENEMSGHLQRLLIQTGQDFMQAKPILEINPSHPLILRVKNESDKTRFNRWADLLLNQALLAEGEQLKDPASFVKGLNELLLDS", "text": "FUNCTION: Molecular chaperone. Has ATPase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family."}
+{"protein": "MTDHDNQRWLQLWRERRTDFHQHGVNLLLSRFWPAFAPATPSRVFVPLCGKSLDMLWLAEQGHDVIGVELSPLAIEAFFRENHLPPSKRRQGRFTLWRHGRIGILCGDYFALSEADLGPVDSVYDRAALTALPPILRSRYVAQLRRIVPDTARVFLLTLEDAEADATLQQALGVDEELAALYTAGFEIALAHVESLFEPDPQNGAPRRVEHKVYQLTGKRPASPEADGRAAETED", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TPMT family."}
+{"protein": "MALNDFHVSEPYTLGIELEMQVINPPSYDLSQDSSTLIDAVKSRLTAGEIKHDITESMLEMATGVCRDIDQAAAQLSAMQHVILQAASEHHLGICGGGTHPFQKWQRQEVCDNERYQRTLENFGYLIQQATVFGQHVHVGCANGDDAIYLLHGLSHFVPHFIALSAASPYMQGSDTRFACARLNIFSAFPDNGPMPWVSNWQEFAGLFRRLSYTTMIDSIKDLHWDIRPSPAFGTVEVRVMDTPLTLDHAINMAGLIQATAHWLLTERPFKPQEQDYLLYKFNRFQACRYGLEGVLTDAYTGDRRRLADDTLRLLDNVTPSARKLGADSAIDALRLQVKKGGNEAQYMREFIADGGSLIGLVQKHCEIWAGQ", "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": "MPFRIEAPYQPTGDQPQAIEKLVAGLRAGYRHQTLLGATGTGKTFVMAHIFAQIQRPTLVLAHNKTLVSQLWAEFREFLPDAAVEMFISYYDEYTPEAYVPSKDLYIEKEASINEEIDRLRHAATQALLTRRDVLIVASVSAIFGLGSPHDYGQEKIHLRTGEVRNRDKLLRQLIDLQFERNDVDFQRGTFRVRGDTLDIIPANAETAIRVEFWGDEIERIVELDPLTGEVLLKHTAVEIYPAKHFVTTKEKLQLAIVSIQAELNERLQELEAAGKLLEAQRLKQRTLYDLEMLSEVGYCSGIENYSRHLDGRAPGQTPWTLLDYFPDDFLMFIDESHITIPQLRGMYNGDRQRKQTLVDYGFRLPSALDNRPLKFEEFEQHVYQVIYVSATPGPYEREKSEQIVEQIIRPTGLLDPEIEVRPTRGQIDDLLGEIRRRVERKQRVLVTTLTKRMAEDLADYLKEMGVRTMYLHADIDTIERVEILRDLRLGVYDVVVGINLLREGLDLPEVSLVAILDADKEGYLRSETSLIQIIGRAARHIEGKVIMYADTITRSMEVAIRETQRRREIQMAHNVRHGITPQGIAKGVRDLTDRIRKVAEERGEYVTTPETAVPVDLPRDEVLKLIKDLEKQMKQAAKALAFEKAAALRDQIVELRQALALSE", "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": "MSSFDKTMKFNFSDDSAETNVEEVLNTVYDALQEKGYNPINQIVGYLLSGDPAYIPRHRDARNLIRKLERDELIEELVKSYLEQHKEA", "text": "SIMILARITY: Belongs to the UPF0297 family."}
+{"protein": "MNKELISEIPLLEDKAVSEIENAASLKDLEKVRLSYLGRKGVVKAYFDDLKNIDDAGEKRDLGAVINVLRNKIDQLITSKENELKDKEVKLKLQNEAVDITLPVRPERIGKIHPLSKVISEVKLIFAHMGFKAVDGPDIEDEFHVFDALNTPSHHPAREEQDTFYLRNKINDKRMVLRTHTSSVQIRTMEKTKTFPIKIVAAGRVYRNDFDATHTPMFHQIEGLYVNENVNMGQLKFTIHCFLSKFFGDKGLRIRFRNSFFPFTEPSAEVDISYKDSKWIEVLGCGMVHPNVFKNVGIDHTKYSGFAFGIGIERLAMLKYQISDLRSFYDNRVSWLNHYGFHFSSLR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily."}
+{"protein": "MSVTIHTKPFGTIQVDSKQILKFPQGLLGFEEFDEYALIEESAESPFKWLQSTKESGLAFIVIQPELFMNQYKPAISDEELHDIGLTSWKDGIIFLIVTIPHDNPKGMTANLQGPIILNGKEGKGKQCISRDENHSIRKNIIESMEEMSSEKV", "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": "MNFVLALTINTLLALLLMILTFWLPQLNPYMEKSDPYECGFDPAYPARIPFSMKFFLVAITFLLFDLEIALLLPLPWALQTTNLPLMTTSSLMLIIILALGLTYEWSQKGLDWTE", "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": "MIEQNKHQQLRIGLASPEQICAWSEKILPNGEIVGQVTKPYTLHYETNKPERDGSFCERIFGPIKSRVCACGNSPGIGNEKIDSKFCTQCGVEFVDSRIRRYQMGYIKLACPVVHVWYLKRLPSYIANLLAKTRKELEGPVYCDLFLARPIAKKPTLLRSRGTFNYEIQSWKDIIPHYLSARPHYLFARGSGTFKEREIATGGDAIGEQLTGLDLQMIIDRSHMEWKNLVELKWNRLEENQESTVDRWEDEKIRRRKDFLVGRIKLAKHFLRTNIEPKWMVLCLLPVLPPEPRPIVQLGEGGLITSSDLNELYRRVINRNNTLTNLLARSGSESFVICQKKLIQEAVDALLDNGICGQPMRDSHDRPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPFLSLYQCGLPSEIAIELFQAFVIRSLIGRHIAPNLRAAKSMIRDKGPIVWEVLQEVMQGHPVLLNRAPTLHKLGIQAFQPILVEGRAIRLHPSVCGGFNADFDGDQMAVHVPLSLEARAEARLLMFSETNLLSPAIGDPISIPTQDMLLGLYISTVENSQGIYGNRYHPYHSEKKSFSCKKPSFYSYDDVLRAYRQKRIDLYSPLWLRWGELDLRIITSVNQEAPIEVQYESLGTFHEIHEHYRIRKGRMGEILNIYIRTTVGRTRFNREMEEAIQGFACFEHPKKSLPALRI", "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": "MALHDTPSARKVTTTPDGPARLYVCGITPYDATHLGHASTYVAFDLLNRAWRNAGHDVTYVQNVTDVDDPLLERAAKVHVDWVELAERETELFRQDMAALRVIPPDHYVGAVESIPLVIELIGRLETAGAIYRVEDDLYFSVTADPAFGAESGWDRERMLEIYPERGGDPDRPGKKDPLDCVVWRGRREGEPSWESPWGPGRPGWHVECTAIAQRHLGGAFDVQGGGSDLVFPHHEMCAGHAQVAVPGTPFAQVYSHGGMVGYDGEKMSKSRGNLVFVSALRNSDVDPMAIRLALLRHHFRSDWEWTDDQLWVAVDDIARWRKALSLGAGAPAAPVIDEVLAALADDLDAPRATAAIDRWVAATLGTAGLADTTDPDAAARLLAALDAALGLALWLS", "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": "MPKKIDTKKIEECIREIIVALGDDPNREGLLDTPKRVSKMYEEVFQGMTLSNREIAEAFGTTFENEDYDSETHNNMVVVKDIPIHSYCEHHLALMYNMKVTVVYIPKDKIIGLSKISRIADMVGRRLQLQERIGTDIAEIVSMVTKSSDVGVLITGEHGCMTSRGIKKPGTLTTTTTFTGKFQTNDLLRQEALLIMK", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I family."}
+{"protein": "MERKHMNVASFNLDHNAVKAPYVRLADKKIGSHGDVIYKYDIRVCQPNREQMLMPALHSLEHLLAELMRNHSDKILDISPMGCQTGFYISLLNEPDYQVMLHLLETTLNDILAAEAVPACCEEQCGFAANHSLSGAQEIARYLLAHRNKWEQVF", "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": "MGDDQSLRSTVAENDISANLSFTQGFLLGQLSVVLLIGAFIKFFIFGEAPPPPSRGLSHRASTHRRSNSIYTINPNEGTSRSLREKPSTSNVLRPVPSSATNTRSILRKTYYSAIPTNPSGKHGRHRIHHSSHQPESLDWFNVLIAQTIAQYRQTAYLLKDDPTSSILSSLTAALNNPEKKPSFIDKIAVTDISLGEEFPIFSNCRIIAVDDPNSDGGRLQALLDVDLSDDNLSIAVETSLLLNYPKPCSAILPVALSISVVRFSGTLCISLVPASTPPLHTPSPSPSPPTADGAVNAGTHPTNGSREPTQEAPNAQEESPPKTSPKSNVAFSFLPDYRLDLSVRSLIGSRSRLQDVPKVAQLVEARVHSWFEERVVEPRVQVVGLPDLWPRMGRTGVRTGEDSETGSNAASRSAMSADMGNSLRADDIGREPDGLRFRGLGARPPFDSVSRTSSFNVETGGFRSHSMTREGSGGGMSDDFHMPGTLPGGAAAN", "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": "MKVTFEQLKAAFNRVLISRGVDSETADACAEMFARTTESGVYSHGVNRFPRFIQQLDNGDIIPDAEAKRITTLGAIEQWDAQRSIGNLTAKKMMDRAIELAADHGIGLVALRNANHWMRGGSYGWQAAEKGYIGICWTNSIAVMPPWGAKECRIGTNPLIVAIPSTPITMVDMSMSMFSYGMLEVNRLAGRQLPVDGGFDDEGNLTKEPGVIEKNRRILPMGYWKGSGMSIVLDMIATLLSDGASVAEVTQDNSDEYGVSQIFIAIEVDKLIDGATRDAKLQRIMDYITTAERADENQAIRLPGHEFTTLLAENRRNGITVDDSVWAKIQAL", "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": "MYSSRILKYEGRSKFGSSCARILRAKSEIPAVVYGKESDVLHIKINSNEFDKKFAKFTDNTVLLLNDGMVEKCVFIKDVSENLTKKFIYHIDFYEVDRTREIERDISIKFIGASVGVKEGGTLSVLRNTVKVKALPLNLPEFVEVDLTPVKKGDQITLKDIVLSDNVKLSETDENLAVLFVK", "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": "MTFTIMTDSTADLNQTWAEDHDIVLIGLTILCDGEVYETVGPNRISSDYLLKKMKAGSHPQTSQINVGEFEKVFREHARNNKALLYLAFSSVLSGTYQSALMARDLVREDYPDAVIEIVDTLAAAGGEGYLTILAAEARDSGKNLLETKDIVEAVIPRLRTYFLVDDLFHLMRGGRLSKGSAFLGSLASIKPLLWIDEEGKLVPIAKIRGRQKAIKEMVAQVEKDIADSTVIVSYTSDQGSAEKLREELLAHENISDVLMMPLGPVISAHVGPNTLAVFVIGQNSR", "text": "FUNCTION: May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism."}
+{"protein": "MVRYVKFSRTANRGVHISAEARINERIRVPEVRLVGPNGEQVGIVRIEDARKLAFDADLDLVEVAPNAKPPVCKIMDYGKFKYEAAQKARESRKNQQQTVVKEQKLRPKIDDHDYETKKNNVIRFLEKGSKVKVTIMFRGREQARPELGYRLLERLANDVVDFGIVETRAKQDGRNMTMVLGPVRKGKK", "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": "MPSEGTWVYVVNLRRVYWGRRTRRAIRAVRMVREFVRRHTKADEVVIDNELNNYIWSRSREKPPARVKIIVSIREEEPEEGGERIRKAVVRLAGRKLRPGRYKG", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL31 family."}
+{"protein": "MTEPLKPRIDFDGPLEVDQNPKFRAQQTFDENQAQNFAPATLDEAPEEEGQVEAVMDAALRPKRSLWRKMVMGGLALFGASVVGQGVQWTMNAWQTQDWVALGGCAAGALIIGAGVGSVVTEWRRLWRLRQRAHERDEARDLLHSHGTGKGRAFCEKLAQQAGIDQSHPALQRWYASIHETQNDREVVSLYAHLVQPVLDAQARREISRSAAESTLMIAVSPLALVDMAFIAWRNLRLINRIATLYGIELGYYSRLRLFKLVLLNIAFAGASELVREVGMDWMSQDLAARLSTRAAQGIGAGLLTARLGIKAMELCRPLPWIDDDKPRLGDFRRQLIGQVKETLQKGKTPSEK", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0283 family."}
+{"protein": "MSTHANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNVITILTMYQWWRDISREGTFQGLHTFPVTIGLRWGMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPVGIAAFNPFQIPLLNTAILLASGVTVTWAHHALMEGNHSQATQGLFFTIVLGVYFTILQAYEYIEAPFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINYHFSKNHHFGFEAAAWYWHFVDVVWLFLYITIYWWGS", "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": "MEWTETQFDRQRREMVDSLRRNGIQNPWVLEAFQEVRRHLFVPEEGRAHAYDDAAWPIGYGQTISQPFTVAYMTSLLADHVPGGSGRPFGRVLEIGTGSGYQAAILEAIGYSVFSVERLPVLYHQAKAKFHRFGLPITCRLGDGTLGWPEEAPFDGILVSAGAPSEPKALKEQLAENGSMVIPVGNRGMQVMTLVTRKGARFEREQYQNFAFVPLVGREGWDDKNTLLY", "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": "MTLRIGIIGTGAIGTDHARRINRVLSGAEVTAVTDVNRDNAEACVAGVAPGAQILGSAEEVIAASDAVLVCSWGAAHEAQVLAAIAAGKPCFCEKPLATEAYGARRIVEAEEAMGRRLVQVGFMRRYDRGYVALKETVRTRLGPPLMIHAAHRNPTVPGRYRTPMAIHDTLIHEIDVLRWLLDDEYVSAQVIFPRATRHTHAGLRDPQIVLLETAKGVRIDVEIFVNCRYGYDIQCEVVGEEGTARLPEPTAIPTRLGAVFGQPILMDWKDRFIDSYDVELQDFLKAAAQGTAAGPSAWDGYVAAITADVCAQAQERPGAILPVTLPARPALYA", "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": "MAVFLIAYDLVNERRGTHDYQPLWDELKRLGAHRTQFSLWLVSANNTTAEVRQHFQQFVDSNDRIWVTRLRKSQYDYANAIGGTNNWLSNNPPEA", "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": "MGASVKPAARRNARQFALQAIYSWQITKDNVATIEEQFLSGDKYDEEELHASEPALAAPETDVAYFRELLSGVVLSHSELDSKIRPYVSRPMQDLDMMELALLRLAMYEMTRREDVPYKVVINEAIELAKVFAAEDSHKFVNGVLDKAAPHVRKK", "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": "MRRVLKELCRNATALSASSNASTTALSQRFRSTLSFFRYHSSVPLKNADDAPTADRLTAVPLERTRNFSIIAHVDHGKSTLADRLLELTGAIRRASGGARNEQVLDTLPVERRRGITVKAQAVSILHRDESDGEEYLLNLIDTPGHADFSFEVARSLSACDGAVLLVDATQGVEAQTIATFYLALDRNLVIIPAANKVDMSSADVERVANQMVRVFGVERDEVLEVSGKTGLNAEKVLSAVVQRVPPPRGNPDGSLRALLLDCRYDDFRGAVNLVQVVDGVLHKGDKITSLASGQHFEVLELGFNTPTPIATNVLSAGQVGYMITNVRDVRSSKVGDTLHMRGLTTIEPLAGFRPAKPMVFQGLFPVNSDDFEKLRAAVSKLTLNDASVTAQAENSSALGAGFRCGFLGLLHADVFHQRLQEEFGAEIIATAPTVPYRIKHQSDDTYIDCTSPLSVPSGGFPSKSTEIEEPLVEATIICPSNVVGTILELCADRRGEQLEQSFLDDSRVILRYKLPLGEVAADFADELKSRSSGYATFDYEEAGMRKSDIVRMDVLVNGVIVDALATLVHRTKAQRHGKDIVARLKDALPRQLYEIAIQASLGSKIIAREDIRAFRKQVTSKCYGGDITRKKKLLEKQKEGKRRMRRIGNVDIPNDTFAGILSTKRD", "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": "MSEEELNNRDTESKQEHDENNSNFEAGSAHMNLPVLPLREVIFFPGDYLPIFIGRKGSIQAMDKALAETSENTGRMLLIAQKNPKKEIPEGKDLYEVGVIAKIAEPKINLQDGGVKLMVIVECRARAVNFRKSEGVLEADVLPIEEEESDNVDIEAYRRAVVQNFEKCVKLSETIPDEIIGLLSQIDSTSRIADLVTASINLKLSVKQEILETVDLLERIKKVHALLEKELGVLQVKQQIKEKTESQIKKSHKVYLLNEQLKAITKELYDKEGEEYDELVDLEKKIGNGKLSAEAKEKVSKELKKLKNMVPMSAEATVVRNYVDWIISLPWKKKGKMITDIAASERILKASHYGIEKVKERIIEYLAVQNRTKSFKGSILCLLGPPGVGKTSLASAIAEATGRPFVRMSLGGIKDESEIKGHRRTYIGAMPGKIIQHMKKAKLSNPVFLLDEIDKMSSDFRSDPAFALLEVLDPEQNAHFVDHYLEVEYDLSDVMFVATANSLNMIPALLDRLEIIRLEAYSEEEKLQIAEHYLIGKLQREHGLKKSEWSISKEALKLLIRRYTRESGVRNLKRELANLMRKAVKKLGVQSGLKSIEVSVKNLKKYAGVEKYTFGTAEPENLVGMTTGLAYTQTGGDLIMIEAVLLPGKGEIRSTGKLGEVMQESVQAAYSFVCSNCNKFGFTSKFFKSKDVHLHVPEGATSKDGPSAGVAICTSIVSVMTGIPVRSNVAMTGEVSLRGKVMEIGGLKEKLLAAVRGGIKIVLIPASNEKDLENIPKSVKNAVRIIPVSTVSEALTFTLAEQPTPLAVDVWPDIPLSSTQQSEQRV", "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": "MAQKINPLGFRLGVTQNDRSHWFAQQRNYSKDLREDQKIRTCIENYVRTHIKSSSNYGGIARVEISRKIDLIQVKIYIGFPNLLLIEGRGFQGIEKLKNDVLNMLDSVDRKLHIAIEKVAKPYRKPNILAEYIALQLEKRVPFRKTMKKAIELAEREEVEGIQIQIAGRLDGKEIARVEWDRGGRVPLQTIRARIDYCYYPVQTIYGVLGIKIWILEE", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
+{"protein": "MQQEIRNSNTPNTGSGNPVSNLSSALRQVHLGNSNTTTDQSNISIDYTSRAPQQQPLDELSRGAAGGPAAGGGPEGSNMVGASSAAQVTAFGGPSVVDSSRITKFFQNQPMEGYTLFSHRSAPNGFKVAIVLSEMGLNYNTIFLDFNLGEHRAPEFVAINPNARVPALIDHSLDNLSLWESGAIILHLANKYYRETGTPLLWSDNLAEQAQINSWLFFQTSGHAPMIGQALHFRYFHSQKVPSAVERYTDEVRRVYGVVEMALAERREALIMDLDSENAAAYSAGTTPLTQSRFFDYPVWLVGDHITIADLSFVPWNNVVDRIGINIKVEFPEVYKWTKHMMRRPAVIKALRGE", "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": "MNNEERLERQKNIRNFSIIAHIDHGKSTLADRILENTKSVETRDMQAQLLDSMDLERERGITIKLNAVKLKYEAKNGESYIFHLIDTPGHVDFSYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLELLPVVNKIDLPAAEPERVKQELEDVIGIDQDDVVLASAKSNIGIDEILEKIVETIPAPSGDPSAPLKALIFDSEYDPYRGVISSIRIVDGVVKAGDKIKMMASGKEFEVTEVGINTPKQLPVDELTVGDVGYITASIKNVDDSRVGDTITHADQPAEQPLKGYKKMNPMVYCGLFPIDNKKYNDLREALEKLQLNDASLEFEPETSQALGFGFRTGFLGMLHMEIIQERIEREFGIELIATAPSVIYECILKNGDKVIVDNPSKMPERDQIEEIYEPYVRATIMVPNDYVGAVMELCQRKRGQFINMDYLDDIRVNIIYDIPLSEVVFDFFDQIKSNTKGYASFDYELTGYKESNLVKMDILLNGDKVDALSFIVHKEFAYERGKALVERLKTLIPRQQFEVPVQAAVGQKIVARTNIKSMGKNVLSKCYGGDISRKRKLLEKQKAGKAKMKAVGNVEIPQDAFLAVLKMDED", "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": "MPSSAHLQDPPPLLSRTLTQNEGQTSLRQSSSCGPSAASASESLSGSTESRIPHSKMLQGKLPRNIPLEYPAGLYCCYVVIIVLSVAVVALSVALSVKKTAQISTINTYAACPRNWIGVGNKCFYFNEIPSNWTLSQTLCKEQGAELARFDTEEELNFLRRYKGSSGYWFGLHRESSAHPWKWTDNTEYNNSVSIGGDEKHGFLSDNGFSSGRGYIVRKSICRKPNSYTSQCL", "text": "FUNCTION: Lectin-type cell surface receptor. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
+{"protein": "MSLVFIIMAIAGYLVGAIPMAYLLSRWRRGIDIRRYGSGNVGASNVVKTAGKRLGLAVFIFDVSKGAVMILLSGALGLALWQQIVVGLFTIAGHNWPVFLRFNGGRGIATSLGVALVMAPVPALIALGTAIAFGLFKKMAPGVFLGVAALPFMSGYFHGFFGIREYQTISWGFIGIFLIMVTRRLMAPDNEYAHTVSKAELIFNRMFLDRDIRSRSVWINRNSAPAEESPNIL", "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": "MDAVNACGAVAPWHVGRAALLRMLGAQPYVPVWHAMQRFTDVRDATAVDELWVVEHEPVFTLGQAGKLEHVLAPGEIPVVHVDRGGQVTYHGPGQLVVYPLLDLSRLGLGVRDYVYGIEQAVINTLAQWNILGERREHAPGVYVGDAKIAALGIRVRRGCSFHGVAFNVAMDLEPFHRIHPCGYRGLQVTSVLDLGGPSEMDTVAAALLAELARQFGFVLHPTSGWLSS", "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": "MSPPAAVSPPARSAELASAPAVKLPVGLSKNSAAATTVEEMEGKWDDFKFAPIRESQVSRAMTRRYFQDLDNYAESDIVIVGAGSCGLSTRYILGKKRPDLKIAIIEASVSPGGGAWLGGQLFSAMVMRKPADAFLREVGVPYEDEGNYVVVKHAALFTSTIMSKVLQLPNCKLFNATCVEDLITRPSKEGVRISGVVTNWTLVSMHHDDQSCMDPNTINAPLVISTTGHDAPMGAFCVKRLVSMGRIEKLGGMRGLDMNVAEDAIVKGTREIVPGLIVGGMELSEVDGANRMGPTFGAMVLSGLKAAEEALKVIDIRQKQNSF", "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": "MLAKRIIPCLDVRNGQVVKGVQFRNHEIIGDIVPLAQRYAQEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGGIKSVEEAGQILSFGADKISINSPALADPELITRLADRYGVQCIVVGIDTWHDATTGRYHVNQYTGDEARTKVTTWETLDWVEEVQKRGAGEIVLNMMNQDGVRNGYDLHQLNLVRDVCNVPLIASGGAGTMEHFLDAFQTAHVDGALAASVFHKQIINIGELKQYLKQQGVEIRVC", "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": "DQGAGVTYLEPSASQIGHKESIKDTARVLGRMYDGIEYRGFGQDVVEELAKYAGVPVFNGLTNEFHPTQMLADALTMREHSGKPLSQTAFAYVGDARYNMANSLLVLGAKLGMDVRIGAPKTLWPSEHIVARARAVAKETGGRILLTENAEEAVKGVDFIHTDVWVSMGEPKEAWQERIDLLKDYRVTPELMAASGNPQVKFMHCLPAFHNRETKVGEWIYETFGLNGVEVT", "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": "MAAETFLFTSESVNEGHPDKLCDQVSDAVLDACLAQDADSKVACETCTKTNMVMVFGEITTKATVDYEKIVRDTCRNIGFISDDVGLDADRCKVLVNIEQQSPDIAQGVHGHFTKRPEDIGAGDQGIMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCAWLRPDGKTQVTVEYLNEGGAMVPVRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIARQAAKSIIASGLARRCIVQISYAIGVPEPLSVFVDSYGTGKIPDKEILKIVKENFDFRPGMISINLDLKKGGNRFIKTAAYGHFGREDADFTWEVVKPLKFDKASA", "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": "MVTVEDIRRAQRAEGPATVMAIGTATPENCVDQSTYPDYYFRITNSEHRTDLKEKFKRMCEKSMIRKRYMHLTEEFLKENPNMTAYMAPSLDARQDIVVVEVPKLGKEAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRFMMYQQGCFAGGTVLRMAKDLAENNAGARVLVVCSEITAVTFRGPSESHLDSLVGQALFGDGAAAVIVGSDPVVGVERPLFQLVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLKEAFGPLGISDWNSVFWIAHPGGPAILDQVEAKLGLKPEKLRSTRHVLGEYGNMSSACVLFILDEMRKSSAKEGMSSTGEGLDWGVLFGFGPGLTVETVVLHSVPINN", "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": "MSNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQPDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTLNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTHGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINASIPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVVKGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRYFLF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family."}
+{"protein": "MLRALLPSTTLALILAGGGHAAVGDAFPAFAVLCAAWDAATNKQIKPWSEDRELPELNDIYNMNMSIASEEWQTIFDGQAEQQTWSQFAQANAGKYKGIDWKQNWDRWRKQRQQTKDAGGAWQTKNHRPEWAATPRDVRPVILAIAEEATELSRKLEPPRTADGKDLIAEINSKLASARCSGELKAAAGNIGCTGPEGTPDKTTTCTTAKAGGSIGHDMLCLCSVAEATDKCSSTGVGDAVPNSGEKLRSNGFQHIVARCPKGPESGTLPQAIDLALAMLATALGTQQPGSNNMILGKSGGGTCTATNSACVDYHEKFSKQQAGITGIPWVALLQQARALYGTYVDAKLAAQTARQQIVMLAGQAKREYRRPAGSLKDPAGVIQEQATNRRRHGADDTNQCTSNNATADECPETRCEYDSEKNECRPKKGTETTATGPGERTTPADGKANNTVSDSLLIKTSPLWLAFLLF", "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": "MLGILNKVFDPTKRTISKYEKKANEIEALAQDFEKLSDEALRNKTIEFKEKLEKGQSVDDLLVEAFATVREASRRVTGMFPFKVQLMGGIALHEGNISEMKTGEGKTLTSTMPVYLNALSGKGVHIVTVNEYLASRDAEEMGKIFEFLGLTVGLNLNSLDKDEKREAYAADITYSTNNELGFDYLRDNMVLYKEQMVQRPLHYAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAFVRTLKIEDDFTYDIKTKSVQLTESGMTKAEKAFGIENLFDVKHVALNHHIAQALKAHVAMQKDVDYVVEEGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEVQNESMTLATITFQNYFRMYEKLSGMTGTAKTEEEEFRNIYNMQVVTIPTNQPVVRDDRPDLIYRTMEGKFKAVAEDVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAVTIATNMAGRGTDIKLGEGVKELGGLAVIGTERHESRRIDNQLRGRSGRQGDPGITQFYLSMEDELMRRFGAERTMAMLDRFGMDDTTPIQSKMVSKAVESSQKRVEGNNFDSRKQLLQYDDVLRQQREVIYKQRFEVIDSDNLKSIVINMIQSSIERAVGSYTPKEELPEEWKLDGLVELINTNYLDEGAISVKDIYGKEADEITSFIMDRIKEKYDAKEETYGDEQMREFEKVIVLRAVDSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMVASIEDDVAKYVLKSEIQNNLEREEVVQGQTTAHQPQEGDEEKTVKKKPVRKVVDIGRNSPCHCGSGKKYKNCHGKTE", "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": "MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTLHAGGVHINCPFAEPLYGEMDDTGISWQQRLGDWWQDDKPWLREAPRRESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDVLSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKRQPWCVEIPRLAEQAMQAVIARRDAFGEAQLAHRISDYLPEQGQLFVGNSLVVRLIDALSQLPAGYPVYSNRGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNGGQIFSLLPTPKSERERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETTLVDAWRTPTTTVIEMVVNDTDGAQTLQQLLAQVSHL", "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": "MTTRIVVAQILGAHGVHGRVKLKSFTADETAVFGYAPLTDESGRREFKLRRTGTGKDHFLAEVDGITGKEAADALRGTRLYIERDRLPAPEDEDEFYHADLIGLDTVTADDQPFGTIKAIYDFGAGDMLEIRHVSEKTVFLPFTKACVPVIEIAAGRVVVEPPANFFAPAGPQPAEGEEMPDGALEALEGEEAGAGTAPQP", "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": "MTALNHTPLNAAHRALNARMVDFGGWDMPVNYGSQIEEHEAVRTDAGMFDVSHMCVVDFTGSRVRAFFEHAIANNVGKLKTPGKALYSCLLNPQGGVIDDLIVYYFTEEFFRVVVNAGTAEKDIAWFNQLNEQGGFGVTITPRRDFAIVAVQGPNAREKAWSTVPAARAATSELKPFNAAQVAGTPFGDLTVARTGYTGEDGFEVIVPAVHVEALWNALQQNGVRPCGLGARDTLRLEAGMNLYGQDMDDTVSPLDAGLAWTVDLTAPRDFVGRAALEANGTRAAFVGLILQKENGKAGGVLRAHQKVVTPHGEGEITSGTFSPSMQESIAFARVPAAVQIGDLVQVQIRDKNLPARVVKLPFVRNGKVLAA", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. SIMILARITY: Belongs to the GcvT family."}
+{"protein": "MKLPIIAVIGRPNVGKSTLVNRIAGDQQAIVHDQPGITRDRTYRPGFWQDRNFQIVDTGGIVFDDHEEFLPLIREQAAIALAEAAVALFVVDGQAGLNAADQEIADWLRQQNVPVVLAVNKCESLEQGYTQAAEFWELGMEEPFPISAIHGSGTGDLLDKVIEYLPTITDVEEDTTINVAIIGRPNVGKSSLLNALTGEQRAIVSPISGTTRDAIDTIIERNGQQYRLIDTAGIRRKKNVDYGAEFFSINRAFKAIRRADVVLFVIDVLDGVTEQDLKLAGRIIDEGRAVIIVANKWDAVEKDTYTINQYRKELQARLFFMEWAEMLFISAQTGQRVNKILDLVDQAAESHRRRVSTAVINEVIQEAVSWHSPPTSRQGKQGRIYYGTQVRSQPPTISLFVNDPKRFNDSYRRYIEKQFRQDLGFAGTPIRLVWRGKRVRDAERGTPNRATKV", "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": "MREIVHIQIGQCGNQIGAKFWEMIGEEHGIDLAGSDRGASALQLERISVYYNEAYGRKYVPRAVLVDLEPGTMDSIRSSKLGALFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVLEVVRHESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRIMNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENADACFCIDNEALYDICFRTLKLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNTMAACDLRRGRYLTVACIFRGKMSTKEVDQQLLSVQTRNSSCFVEWIPNNVKVAVCDIPPRGLSMAATFIGNNTAIQEIFNRVSEHFSAMFKRKAFVHWYTSEGMDINEFGEAENNIHDLVSEYQQFQDAKAVLEEDEEVTEEAEMEPEDKGH", "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": "MSNGSVPVSGIGGRGDGEGSSQVHMESTGGMDRAKVFAVYGKGGIGKSTTSSNLAVAFSQLGKRVLQIGCDPKHDSTFTLTKRLVPTVIDSLEEVDFHMEELRPEDYVYEGYNGVLCVEAGGPPAGTGCGGYVVGQTVKLLKQHHLLEETDVVIFDVLGDVVCGGFAAPLQHADQALIVTANDFDSIFAMNRIAGAIQAKAKNYKVRLGGVIANRSERTDQIDRINERIGLRTLAHVPNYDVVRRSRLHKSTLFELEEQSEELERVRDEYLSLAAALWNGVDPLSPSPLKDREVFDLLGFD", "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": "MIKVDKLPDVFIKAMPVLQTLEDAGFEAYFVGGSVRDLLLDRHVHDVDITTSAYPEEVKELFAKSIDTGIRHGTVTVLYGGESYEITTFRTESGYQDYRRPDHVTFVQNLDEDLKRRDFTINALAMDLHGQIVDLFNGVEDLKNHIIRAVGDPEKRFHEDALRMMRAVRFTSQLKFNLEEKTEQAIKDNHELLKKISVERIREEFVKMGIGPHSRQAFQIFLDTQLSEDVPDFAGKKELLQIYPQLQFSPTLETSLWSLIIILLKLPDEDISKFMRDWKNSNAMTEQVERIIKFFDLISDHTPNDYELFQAGERTIINTIDVAHILGQPVASEALVDRYLALPIKKPAELAIDGRFLIKHGMRPGAELGHTLNKIRELVVSSRLENSPDAIEKYLEDLD", "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": "MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGQAVA", "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": "MPELPEVETVKRGLIKTIIDKKIFDIEINTDKLRYPIDKDQLVKIKNKVVKEIQRRGKHLIIFIEDDLQLIIHLGMSGIIKVIDSTNYNKIKHDHIVVTLSDNLSLVYNDPRKFGYWLVNTNHTPLEHRVLVSHGVEPLTADFNSDYLVSKLKQTSRKIKQTIMDNNIVVGVGNIYASEALFDSNILPTRASNTITKKEAANLVSSIKKILEKAITQGGTTLKDYKNTEGKPGYFTQQLNVYGRNEQQCYVCNTKIQSLVIAQRNTFFCKKCQK", "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": "MNNFLSCPAIPFPNFLDPIIIQLGPIALHWYGLGYVVGILFSWWYVQKLSHKKSLWYANYPPLNAEKASDFVVWAALGIVVGGRLGQVLIWDPTYYFNHPSSIIAVWDGGMSFHGGLIGTTIAIIWFARKHNINIWAMFDTIAAGAPFGIGVVRICNFINQELWGSVTNVPWAVCFSLDPQYLPRHPSQLYEALMEGFLLFIVLAFIIFAFKAFKRPGTVAGTFIISYGIARTISEIFRVPQEDPEWFSALFHGSGFTYGMALSLPMILFGFYAIFRAFRNHFIK", "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": "MSETQRAFVKRITHETQVQIALALNGGPLEIGQSILGGAKTTVAHQASSSQVINVQTGVGFLDHMIHALAKHSGWSLIVECVGDLHIDDHHTTEDCGLALGQALREAIGQVRGVKRFGTGFAPLDEALSRAVVDLSNRPYAVVDLGLRREKIGDLSTEMIPHFLQSFAESARVTLHVDCLRGTNDHHRSESAFKAVAVALRDALTRTGTDDVPSTKGVLM", "text": "SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
+{"protein": "MIHLEGITKSFGSLQVLKGIDLEITQGEVVSIVGPSGAGKTTLLQIMGTLDSPDAGMINIDGTNVSRMKEKELSAFRNKHIGFVFQFHQLLPEFTALENVMIPAFIAGVPTKEASMRAMEILDFMGLKERASHKPNELSGGEKQRVAVARALINQPAVILADEPSGSLDSHNKEELHQLFFDLRNRFGQTFVIVTHDEALAKITDRTIHMVDGNII", "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": "MKILVDENMPYVEPLFGDLGDIIPVNGRTLTAEQVGEADVLLVRSVTKVNAELLSGNNKLKFVGSATIGTDHVDLTYLAERNIPFSNAPGCNATAVGEFAFIAMLELAQRFNSPLKGKVVGIVGAGNTGTATAKCLQAYGIKVLLNDPIKAAEGDPRSFVSLETIMAQADIISLHVPITRTGEHKTKYLFDEARLKALKPNTWLVNCCRGDVIDNQALIKVKQQRDDLKLVLDVWEGEPTPLPELVPLAEFATPHIAGYSLEGKARGTFMLYQKLCQLLNITADKSLLDLLPTFNIKAVELATAPNEKALLQLARFVYDLRDDDKMFRNTFLNENGFDTMRKNHQHRREFSALALAYDGQSEVDWLSNLGFSGVGQ", "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": "MSIKSDKWIRRMSEEFGMIDPFEPNQIKEADGKRIISYGTSSYGYDIRCANEFKIFTNINSTIVDPKNFDPKNFVTVEDDCCIIPPNSFALARTVEYFRIPRNVLTVCLGKSTYARCGIIVNVTPFEPEWEGYVTLEFSNTTPLPAKIYAGEGVAQVLFFESDEICETSYKDRNGKYMGQTGVTLPKA", "text": "FUNCTION: Catalyzes the deamination of dCTP to dUTP. SIMILARITY: Belongs to the dCTP deaminase family."}
+{"protein": "MKIEKMNFYSPKKYKWKGIKITEQAIEQILFLINKNPKNKGIRIGTKKSGCAGFRYTMELVKNNTIEKENKNDIVFYYNNILVYISLKEAPFLNGIKIDFVKDSINEVFKYCNPRIKTFCGCGESFSID", "text": "SIMILARITY: Belongs to the HesB/IscA family."}
+{"protein": "MKISFHGQSCIKIITGNTTILVDPFISGNEKCDLKAEEQMPDFIVLSHGHDDHVGDTVEIAKNSGATVICNADLASFLAVEDGLENIAAMHIGGKRQFEFGQVKLTQAFHGSQTVRNGRIINLGFPTGVVFTIENKNIYFAGDTGLFSDMKLIGELNPLDVAFLPIGDNFTMGPEDAAIAARFLQTKLVIPMHYNTFPLIEQDPHKFVASLDEGISGKVLEIGESIEI", "text": "SIMILARITY: Belongs to the UPF0173 family."}
+{"protein": "MDRPKPQTVRELADTLCIPLVDILLPCRFCNRFLAYIELVAFDLKGLQLIWTEEDFVFACCSSCAYATAQYEFSKFYEQSVSGRELEEIEHKPIGEIPIRCKFCLKKLDLLEKLDTCYRHQQFHKVRRNWKGLCRHCGSIG", "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": "MKKPVDFFAMKENGEKITMITAYDYPSAKNVEQAEADMILVGDSLGMVVLGYDSTVPVTMNDMIHHTKAVKRGAPNTFVVTDMPFMTYHGSVDETIQNARKIIQESGAHAVKLEGAGEVVNKIARLTEAGAPVVAHLGLTPQSVGLTGSYKVRAKSVQEAQELIDNALAVEAAGAIAIVLEAIPRQLAEKVTKALTIPTIGIGAGLETDGQVLVYHDIIGYGINRRAKFVKAYADIDETIEPALKNYVNDVKELAFPEVKHSFTMAEEDLKGLYGRE", "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": "MSHYGSYYGGLGYSCGGFGGLGYGYGCGCGSFCRRGSGCGYGGYGYGSGFGSYGYGSGFGGYGYGSGFGGYGYGCCRPSYNGGYGFSGFY", "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": "MSQILHPDAALVLFSGGQDSATCLAWALDRFARVETIGFDYGQRHLVELDSRAKLLDGLKTLKPEWVAKLGETHTLAIPTLAQVSDTALTRDVAIAMGADGLPNTFVPGRNLIFLTFAAALAYRRGIGAIIGGMCETDYSGYPDCRDATIKALGEAINLGMATQFELHTPLMWLDKAATWGLAQTLGGERLVDLIREHSHTCYLGERGARHDWGFGCGECPACQLRAKGWREFSAQRDARQG", "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": "MKKIEFELHYQAQKALHACIDKANRYFQHQFPMPLLSYQLRGKAAGKAYLQLNQIRLNPILFKENKTAFLEEVIPHEVAHLLTYQLYGRVKPHGAEWQSIMQGVFLLPANTTHQFAVASVQGKTFQYRCQCREFPLTIRRHNKVLRNEASYTCQKCRQTLIFTGIQLS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SprT family."}
+{"protein": "MSDILNKIIATKREEVAAARLAKPLAIVEAEAIAQPAPRDFVGAIRNKIANDRPAVIAEIKKASPSKGIIRPDFQPADIARSYEQHGAACLSVLTDRQYFQGCPEYLQSARAACALPVLRKDFMVDAYQVAEARAMGADAILLIAAALTLEEMQALETQASAYGMAVLVEVHNGEELDAALQLKTPLLGINNRNLRTFAVTLETTLGLLSRIPAGRIVVTESGILKPEEVALMRTNKVNAFLVGEAFMRVPEPGAELARLFA", "text": "SIMILARITY: Belongs to the TrpC family."}
+{"protein": "MALRRTSDSKVYLPPTPVSRVVRRMNMYTHRIYYYAGSSRLLTLGHPYFPIPKSGSTAEIPKVSAYQYRVFRVHLPDPNKFGLPDPQLYNPETERLVWACVGVEVGRGQPLGVGLSGHPLFNKLDDTENSHLATANADTDNRDNVCVDNKQTQLCIIGCTPPLGEHWGVGTVCKNAQSQVQRGDCPPLELISSVIEDGDMIDTGFGAMDFTALQATKCDVPLDINQSICKYPDYLKMSADTYGNSMFFFLRREQLFARHFFNKAGTIGDSVPVSMYIKGAGQGREPPTTSIYSRTPSGSMVTSDAQLFNKPYWLQRAQGHNNGICWGNQLFVTCVDTTRSTNLTISTVSAQSASATFKPSDYKQFIRHGEEYELQFIFQLCKITLTTDVMAYIHTMNSTILENWNFGLTLPPTASLEDAYRFIKNSATTCQRDAPAQPKEDPFSKLKFWDVDLKEKFSIDLDQFPLGRKFMLQAGIQRRPKLGTKRPASSLSASSSSTTRKKRKLTK", "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": "MAKKKAFTPLLYLVSIVFLPWWISLLFQKSLESWVTNWWNTRQSETFLNDIEEKSILEKFIELEELLFLEEMIKEYSETHLQNLRIGIHKETIQLIKIQNEGRIHTILHFSTNIICFIILSGYSILGNKELVILNSWAQEFLYNLSDTIKAFSLLLLTDLCIGFHSPHGWELMIGFVYKDFGFVHNDQIISGLVSTFPVILDTILKYWIFRYLNRVSPSLVVIYHSMND", "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": "MESVRSLVEDKPVVIFSKSSCCMSHSIQTLISGFGAKMTVYELDQFSNGQEIEKALVQMGCKPSVPAVFIGQQFIGGANQVMTLQVKNQLAAMLRRAGAIWV", "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": "MGMSFSHLLIVLLIIFVLFGAGKLPQVMSDLAKGLKAFKEGMKDDGNDNDKTNN", "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": "MSTILESLPTGQKVGIAFSGGLDTSAALHWMKLKGAVPYAYTANLGQPDEDDYDAIPKRAIEYGAAGARLIDCRAQLVAEGIAALQSGAFHITTAGVTYFNTTPIGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERFYRYGLLVNPDLKIYKPWLDQTFIDELGGRAEMSEFMNQAGFAYRMSAEKAYSTDSNLLGATHEAKDLESLESGIKIVNPIMGVAFWRDDVKIAAEEVTVRFEAGQPVALNGVEFKDQVELLLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGLALLYIAYERLVTGIHNEDTIEQYRENGRRLGRLLYQGRWFDPQAIMLRETAQRWVARAITGEVKIELRRGNDYSILSTKSPNLTYQPERLSMEKVASTFSPRDRIGQLTMRNLDITDTRDKLRVYAQVGLLTPGESSALPQIKSDSGE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2 subfamily."}
+{"protein": "MSTTKSDNYISELRKVIWPIERYENKKFLPMAFMMFCILLNYSTLRSIKDGFVVTDIGAEAISFLKTYIVLPSAVIAMIVYVKLCDILKQENVFYVITSFFLAYFALFAFVLYPNPDLVHPNPEAIESLSLAYPNFKWFIRIVGKWSFASFYTMAELWGTLMLSLLFWQFANQITKTDEAKRFYSMFGLLANLALPVTSLIIGYFLHEKTQIVAEHLKFTPLFVIMIISSLAVILTYRWMNKNVLTDPKLYDPALVKGKKAKAKMSLIESFKMIFTSKYVGYIALLLIAYGISVNLVEGVWKSKLKELHPTKEAYTMYMGQFQAYQGWVAIAFMIIGSNILRKVSWLTAAMITPLMMLITGIAFFAFIFFDSVIAMYLTGILASGPLALAVMIGTIQNVLSKGVKYSLFDATKNMAYIPLDKDLRVKGQAAVEVIGGRFGKSGGAIIQSTFFIIFPALGFVEATPYFASIFFVIVILWIYAVKGLNKEYQVLVNNTEK", "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": "MKAFDRPALTVLLVQGARDLSLNLSEAQITKLIDYLALMAKWNSVYNLTAVRDPVQMVTQHLLDSLAAVSAFSNAKNVLDVGAGGGLPGIVLAIWAAEAHPEMRISMIDTVHKKTAFLTQVKAELNLSNVSVYTARVEQWQAPQKFDVITSRAFADLSDFVNWSEHLLADGGQYIALKGVAPDTEVAGLPAGWQVREVRALQVPTLQAERHLVFIERTVL", "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": "MKIGIINTKIRTVFSAFACMIAASLVCTMPARAVVEININKGVIEPLPIAITDFLSADQLGSNITSVIAADLERSGLFAPIDKGAFIEKISNPDAAPRFEDWKVINAQALVTGRITKQPDGRLKAEFHLWDTFGGQQMIGQQFFTTPDNWRRVAHIIADAIYERLTGDKGYFDTRVVFVDESGPAQKRVKRLAIMDQDGANVRFISDGRALSLTPRFSPNRQEVTYMSFEGGSPKVYLLQLETGQRELVGNFPGMTIAPRFSPDGQKVVMSLLQDDGSANIYTMDLRNRTTTRLTSSQAIDTGASYSPDGSQIVFTSDRGGRPQLYVMGADGSNPRRISMGDGSYSTPVWSPRGDLIAFTKQSQGQFSIGVTKTDGSGERLLTSGFHNEGPTWAPNGRVLMFFRKAAGAGGPKLFTIDLTGRNERQIQTPNFASDPAWSPLLE", "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": "MENLSERFNVLQDQLMNIYEAAEHTLETQIAHWTLLRREAVLLYYARQKGITRLGYQPVPTLAVSEAKAKEAIGIMLQLQSLQKSEYASENWTLVDTSAETYNNVPEHHFKKGPVPVEVIYDKEPENANVYTMWKYVYYMDPEDVWHKTTSGVNQTGIYYLHGDFKHYYVLFADGARMYSKTGQWEVKVNKETVFAPVTSSTPPGSPGQRDPDATSKTPATSSDSTTRSSDKQSQQADPRRKGYGRRPSSRTRRQETQQRRSRSRYRSQSNSRSRSQSQTRALGATSVSRSSRSPSVTQIRNRRSRSQSRGRGGRGSSTDTTTKRRRSRSSSSNTRKRSQRGERGRGERGGRGKRRDRSSSTSPTPKRSRAGSRSSRQRGVSPEQVGRSLQSVSSKHRGRLGRLLEEALDPPVIICKGGANTLKCFRNRARHKYTGLFKAFSTTWSWVAGDSTERLGRPRMLISFTSTNQRKDFDETVKYPKGVETAYGNLDSL", "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": "MKAVIFAYHDMGCQGVQAVLDAGYEIAAIFTHADNPAENTFFGSVSRLAAELGIPVYAPDNVNHPIWVDRIAELAPDIIFSFYYRNLLSEEILHLAPAGAFNLHGSLLPAYRGRAPLNWVLVNGESETGVTLHRMVKRADAGEIVASQRVAIAQDDVALTLHHKLCQAARQLLNSILPTMKCGDIPSVPQRESDATYYGRRRPEDGLIDWHKPVSTVHNLVRAVAAPWPGAFSYNGSQKFTIWSSRICPDAQGALPGSVISVSPLRVACADGALEIITGQAGDGITVQGSQLAQTLGLVAGARLNRPPATSGKRRIRVLILGVNGFIGNHLTERLLNEENYEVYGMDIGSNAISRFLLHPRFHFVEGDISIHSEWIEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYCVKYRKRVVFPSTSEVYGMCTDASFDEDKSNLIVGPVNKPRWIYSVSKQLLDRVIWAYGEKEGLRFTLFRPFNWMGPRLDSLNAARIGSSRAITQLILNLVEGTPIKLIDGGQQKRCFTDIRDGIEALFRIIVNDGDRCDGKIINIGNPDNEASIQELATLLLDSFDKHPLRCHFPPFAGFQVVESRSYYGKGYQDVAHRKPSIDNARRCLGWEPSIAMRDTVEETLDFFLRSVDVAERAS", "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": "MTIKAISVDIDGTITYPDRRLHEKALEAIRLAESLGVPVMLVTGNTVQFGEAAAILIGTSGPVVGEDGGALSIKEGKLRKRVYLTNMDEEWILWGELKKRYPEALLSFSMPERKAGLVVLRTVPVKAVRELIKELGLNLIAVDSGFAIHIKKPWINKGTGIEKACEYLGISPKEVAHIGDGENDLDAFGVVGYRVAVAQAPESLKEKADYVTTKPYGEGGAEAIEHILRKFGYLPEEKT", "text": "FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate. SIMILARITY: Belongs to the archaeal SPP-like hydrolase family."}
+{"protein": "MSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQSVLLPKKTESAKSAKSK", "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": "MTNAPPATPKIGFVSLGCPKALVDSEQILTQLRAEGYDTAKSYDGADLVIVNTCGFIDAAVQESLDAIGEALHENGRVIVTGCLGAKKDANGDDIIQKVHPKVLAVTGPHALGEVMDAVHLHMPKPHAPFLDLLPPQGIKLTPKHFAYLKISEGCNHRCSFCIIPSMRGDLVSRPIADVMMEAENLFKAGVKELLVISQDTSAYGVDIKFRMGFWNGKPVKTHMTQLVEALGELAAPYGAWVRLHYVYPYPHVDAIIPMMAEGKILPYLDVPLQHAHPDVLKRMKRPASGEKNIERIQAWRAMCPDLTIRSTFIAGFPGETEAEFEYLLDFLKEAEIDRLGCFAYSPVEGATANDLPNAVPEEVREERRGRVMLLQEEISKKRLQAKVGKTMRVLIDEVNRTGAATARSGADAPEIDGVVYVKAPYEPHIKYKVGEFVDVKITGADAHDLWAEA", "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": "MPTNSQDTTVLHALFGGTFDPIHYGHLRPVEALAAEAGLNRVTLLPNHVPPHRPQPEANAQQRLKMVELAIAGNPLFAVDDRELHRTTPSYTIETLEAIRKERGAALPLAFIIGQDSLLTLHKWHRWQSLLDTCHLLVLARPGYNDRMDTPELQQWLEQHQVTDAALLSRQPQGYIYLADTPQLEISATEIRQRRHQGLNCDDLLPRSVQRYIELQGLYR", "text": "FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). SIMILARITY: Belongs to the NadD family."}
+{"protein": "MDTQAVRAYLLDLQDRITTAVGTLDGGTFVTDTWDKPPTERLRGSGRTCILENGAVLERGGVGFSHVMGDTLPPSATANRPELAGRGFEAMGVSLVFHPRNPYAPTVHMNVRCFVAQRPDAEPVWWFGGGMDLTPYYGFAEDAAHFHRTCKQALEPFGEELYPRFKQWCDDYFYLKHRKEARGVGGIFFDDFAELGFERSFEMMRAVGDALLPAWLPIAEQRHATPYGERERAFQAYRRGRYVEFNLVFDRGTLFGLQSGGRTESILMSMPPVANWRYDWQPEPGSPEAALYTDFLPARDWV", "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": "MQRHPMTKEGADALQEELQHLKKVERPAVSNAIAEAREHGDLKENAEYHAAREQQGLMEARIKQIESLLGSVQIIDVTKLNPNGKVVFGSTVTILNVDTEEEVTYKIVGEEEADIKHNKISVNSPIARALIAKEEGEEITVKAPSGNIEYEIVEIQYV", "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": "MIVKTKEEVVGTPREIFAPNGHWISRRYLLAGEGMGFSFHETIILAGTKTHIHYQNHLEAVFCVQGRGEVELIPSGERFLIEEGVMYALDKHDEHYLSASEEMRLICVFNPPLQGNEVHDEKGVYPLKKGQ", "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": "MSEMTPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLDEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAIKLVRETEMEKMKYRAEEAAEERILDALLPNPRNSWGEEEKADNSNTRQIFRKKLREGQLDDKEIELELAASPMGVEIMTPPGMEEMANQLQGLFQNLGQNQKKKRKIKVKEAMKALIEEEAARLVNPEELKQKAIAAVENNGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGAFQIAKPSDLIPELQGRLPIRVELTALTTDDFERILTEPNASLTDQYQALMATEGVKIEFTKDGIRRLAEAAWQVNERTENIGARRLHTVMERLMEDISYDASEKSGETFVIDTDYVNAHLGKLIEDEDLSRFIL", "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": "MAIQTSNLGYPRIGLQREWKKTLEAFWSNKIDEEQFLTTMKEIRLQHVKVQQEKGIELIPIGDFTYYDHVLDTAYMLGFIPSRFSEFTSYLDVYFAMARGSKDHVASEMTKWFNTNYHYIVPEYEEGLQISLKDNRPLRLYEEAKQELGVDGKPVILGPYTFLKLAKGYTQEQFATILKQLVAPYVQLLSELHAAGAQVIQVDEPIFASLTKEEVQQAKEIYEAIRKEVPNANLLLQTYFDSVEENYEEIITFPVSGIGLDFVHGKEGNLHAISKYGFPADKTLAVGCIDGRNIWRADLDEVLTLFTTLQKQVQTKDFIVQPSCSLLHTPIDKTEETHLSTELFDALAFANQKLEELVLIHSALTKGTESISNELETYRNVHHTIRSSAVRNREDVKAARTALKEEDFSRPLPFEKRYELQQVALELPLLPTTTIGSFPQTTEVRQTRKEWRNGVISNEQYEKFIEKETEKWIRYQEEIGLDVLVHGEFERTDMVEYFGERLAGFSFTKNGWVQSYGSRCVKPPVIYGDVAFINGMTIKETVYAQSLTEKVVKGMLTGPVTILNWSFVRNDIPRKEVSYQIALALRHEIELLESSGIRVIQVDEPALREGMPLKEKDWDAYITWAVQSFLLATSSVANETQIHTHMCYSNFEDIVDAIRALDADVISIETSRSHGEFIDTLKHTTYEKGIGLGVYDIHSPRVPSKDEMYKIVEQSLEVCDPKYFWINPDCGLKTRRTEEVIPALEHMVQAAKDARSLLKTNA", "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": "MKEKAVVLDDQMIRRALTRISHEIVEHNKGVDQCVLVGIKTRGIFLAKRLAEKIGQIEGKEIEVGELDITLYRDDLTLQSKDKEPLVKGSDIPVDITKKKVILVDDVLYTGRTVRAAMDALMDLGRPSQIQLAVLVDRGHRELPIRADYVGKNIPTSSEERIEVDLQETDQKDRVSIYEK", "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": "MARYRGPKLRIVRRLGELPGLTQKNCTRDFPPGQHGPKKKGGGNQKTKESQYAVRLKEKQKLRFNYGISERQLMSYVREARKRKGSTGEILLQILEMRLDTIIFRLGFAPTIAAARQLINHGHIVVNGRRVDIPSSLCKVNDSISVALNSQNFVKNLLQSFTKTLDAPYLEVNQEKLSAVVRDNIPREAVSLQINELLVVEFYSRKV", "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": "MGGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGANSHNPDWDFNPNKDHWPEANQVGAGAFGPGFTPPHGGLLGWSPQAQGVLTTVPVAPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTTFHQALLDPRVRGLYFPAGGSSSGTVNPVPTTASPISSISSRTGDPAPNMENTTSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGAPTCPGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPGTSTTSTGPCKTCTIPAQGTSMFPSCCCTKPSDGNCTCIPIPSSWAFARFLWEGASVRFSWLSLLVPFVQWFVGLSPTVWLSVIWMMWYWGPSLYNILSPFLPLLPIFFCLWVYI", "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": "MSRDIIKLDQIDVTFHQKKRTITAVKDVTIHIQEGDIYGIVGYSGAGKSTLVRVINLLQKPSAGKITIDDDVIFDGKVTLTAEQLRRKRQDIGMIFQHFNLMSQKTAEENVAFALKHSGLSKEEKKAKVAKLLDLVGLADRAENYPSQLSGGQKQRVAIARALANDPKILISDESTSALDPKTTKQILALLQDLNQKLGLTVVLITHEMQIVKDIANRVAVMQDGHLIEEGSVLEIFSNPKQPLTQDFISTATGIDEAMVKIEKQEIVEHLSENSLLVQLKYAGASTDEPLLNELYKHYQVMANILYGNIEILDGTPVGELVVVLSGEKAALAGAQEAIRQAGVQLKVLKGVQ", "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": "ELTTGPEIVEQFEGKQIDAFLAGVGTGGTLSGAGKVLKEKYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFVPDTLNTDIYDSIIQVGNDIAMETSRRVAKEEGILAGISSGAAIHAAIQKAKELGKGKTVLTVLPSNGERYLSTPLYSFDD", "text": "SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family."}
+{"protein": "MGRKWANIVAKKTAKDGANSKVYAKFGVEIYVAAKKGDPDPETNTALKFVIDRAKQAQVPKHVIDKAIDKAKGNTDETFTEGRYEGFGPNGSMLIVDTLTSNVNRTAANVRAAFGKNGGNMGASGSVSYLFDNKGVVVFAGDDADSIFELLLEADVDVDDVEAEEGTITVYTAPTDLHKAIVALRESGIEEFQVTELEMIPQSEVELSGDDLATFEKLVDVLEDDEDVQKVYTNVEGF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TACO1 family. YeeN subfamily."}
+{"protein": "MNTITGKVWNFGANIDTDVIIAARYLNSSDPEHLAKYVMEDADPEFPKKLKKGDIIVAGENFGCGSSREHAPIALKAAGIAAVVAPSFARIFYRNAFNMGLPIFELPESLEIKEGEEISINLDKGEITNNTTKKTYKFIPIPPFMQELIATGGLINYAKAEMKKAI", "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": "MSLLTEVETPIRSEWECRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE", "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": "MTESHIDFRRAKFLISAPDIAHLDQYLPGDVGVEIAFAGRSNAGKSSALNALTEQKNLARTSKTPGRTQLINVFELDAQRRLVDLPGYGFAQVPLAMKLKWQQSLGEYLQKRACLSGVVVLMDIRHPLKDLDMQMIEWAVASEIPVLALLTKSDKLAQSAKMKTVNEVRKALVEFGDWVQVEPFSALKGTGKPKVLSILNEWCHPQWLADELENQEDAE", "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": "MTVAKELRQKSSEELVKLVIKLKGELLEYRFKLAHGELDKPHLINQTRRLLATILTILTERKLNWQEEQAKYKLLTKKTNEAAVNAWKQHLEANKAKLLKSRAKREDASKK", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
+{"protein": "MNILDDLKARGLVYQTTDEEALYKRLESPMTLYCGFDPTADSLHIGHLLPVLMLRRFQLAGHCPIALVGGGTGLIGDPSGKTSERTLNPTEVVQEWANRIKEQLSCFLDFEGVGNPAIMANNYEWLGTINVIEFLRDIGKNFSLGSMLAKESVESRMSRGISFTEFSYQILQSYDFLKLNELYGCEMQIGGSDQWGNITSGTDLIRRMSVGEDRQVHGLTVPLVTKSDGTKFGKTEGGAVWLDQDKTSPYKFYQFWINTDDRDVVKYLNFFTFLSIEEIQGLAQEVESQPEKRNAQRMLAKEVTELVHGVEARERAEKISQALFTGGIANLTAKEVEEGFSDVPSADVEDQEMLLVDALIKVGAVSSRRQARESMESGAVYVNGIRQTDTTLTVAQLDKIESRFIVIRRGKKNYYLVKLV", "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": "MMQPSIKPADEHSAADIIARIGSLTRMLRDSLRELGLDRAIAEAAEAIPDARDRLDYVVQMTAQAAERALNSVEASQPHQEEMEKGAKSLSQRWDAWFDDPIELAQARELVTDTRRFLAEVPDHTRFTNAQLLDIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQDARPKRENESLLNGPQVDTSKAGVVASQDQVDDLLDSLGF", "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": "MGDIIEGTKPTLDDLWAGDEDQKPQTPPVSPPRSPSFKHEHKSPFPGSTSPPPASPIGEEDLKPRTARASSSTSKVKSRKASPEEFKPVLIDDLPTAWDEAHETFEALEKCVYERKDIGLSKENDEMMVCECVYNRHDPDADPCGPDSDCINRALYIECIAGECRAGKHCHNQQFSKRQYANVDVVLTEKKGYGLRASSTIPANTLIYEYIGEVVAEKTFRKRMQQYADEGIRHFYFMMLQKEEYIDATKKGGIGRFANHSCNPNCEVQKWVVGRRLRMGIFTKRDVIKGEEITFNYNVDRYGHDAQTCYCGEPNCVGTIGGKTQTDIGTMNDLFLDALGITDEVEAMGMKGSKKKKSRQLDEDFVPILRPISAHEVQKVAAAIRQSMENKKMMSRLLQRIQMTDDGAMHRQLMRMHGFSLMYMVLTELADDNEIVLLALESMNKWKLQIRNKIEDSKIEEPVKALSQSGDEKICGLAKQLIEYWSTLELSYKIPRVSKIASLDADDEAGTQTIAEANVVSAARRPDAWENTQEIQIDIAPVRPRTLPVSRPRPPPPPPPLPVKKPALNSMSSTDRLKLDAIIAMAEQTVQAQAAAAAVEATASPQAGSSRSGSRPAEDEERRKRQKRTHMTEEELAEQKERRLRKLIGAVVVKSMNKYKDMMEHDTFKKYARECTDTLVKKEKKRNPSYQDVKHPSLSDDKKAKIKSFTKDYTHKILKHLKEKGKLRNPKSSSSLRTNSNDPRQAASSSTNGDTPSISTTPSQGATQRLRDGELVDDIFGADEDMVMDLDEDTPEMQNDHPAPPSVPPATPPLPPVHVEVVDNVSTPTSQWET", "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": "MNPLTLSLVLTTMMAGTLIVMTSSHWFMIWVGFEMNMLAIIPLLTKEHNPRSTEAATKYFLTQATASMLLMMAAITNLLYTGHWSIMKLINPTASIMMTMALTMKLGLSPFHFWVPEVTQGIPLMSGLILLTWQKLAPLSGLYMIMPLINTDILLIMSLMSIAIGGWGGLNQTQLRKIMAYSSIAHMGWMMAVLAYNPTMTLLNLYIYIPMTITTFMLLMINSTTTTTSLSQTWNKLPLITTLILITMLSLGGLPPLTGFLPKWAIIQEMTKNSSIIMPTLMTLLALLNLYFYTRITYTTSLTMFPTANNMKIKWQFKNPKQMMSLPLMIMISTLVPPLAPMMPILT", "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": "MQAATSRESYRIAGDRLDAYVRGAEPSAVAATADELLSVADLIRREPRLRRALADPARSGADRAALLTGILSGKVGADALDLSTTLVAGRWSAPSELLDGAERLGVAALLAAADKAGDLGEVEDELFRFGQVVAGQSALSNALSDPAAPVEQRATLAGELLTGKARPVTVRLVEVALGGFGGRSFVGALTRLVELAADRRDRQVAYVTVAAPLGEEEERRLGASLSAIYGREVSVKQSVDPEVLGGVSVRVGSDLYDGTVLRRLNETRNALAKR", "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": "MEIILAKRAGFCFGVKRATQMAFEAAEKEGKTYSLGPIIHSPQVVHRLEEMGVKVLKGLGEITDGTIIVRSHGVTSEELEEAVRKELEVVDATCPFVKKAQENVQNLSEAGYEVVVVGDADHPEVQGIVSYAKGKVCVVGSEEEAARLPKMKKIGIVAQTTQSFDNLKHVVLECLRKGAEIRIFNTICDATAVRQQEATALARTVDCMIVIGGYNSANTKRLAEVCAELQPRTHQIETAQEINPAWFEGVAKVGVTAGASTPKWLIDEVIERIREIDSAKTS", "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": "MIVQPKVRGFICTTAHPEGCARHVGEWINYAKQQPSLTGGPQKVLIIGASTGFGLASRIVAAFGAGAKTIGVFFERPASGKRTASPGWYNTAAFEKTALAAGLYAKSISGDAFSDEIKQQTIDLIQKDWQGGVDLVIYSIASPRRVHPRTGEIFNSVLKPIGQTYHNKTVDVMTGEVSPVSIEPATEKEIRDTEAVMGGDDWALWINALFKYNCLAEGVKTVAFTYIGPELTHAVYRNGTIGRAKLHLEKTARELDTQLESALSGQALISVNKALVTQASAAIPVVPLYISLLYKIMKEKNIHEGCIEQMWRLFKERLYSNQNIPTDSEGRIRIDDWEMREDVQAEIKRLWESINTGNVETLSDIAGYREDFYKLFGFGLNGIDYERGVEIEKAIPSITVTPENPE", "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": "MGFLEDKKRTLMNLELAIREGLVDEEIIPILNKINEIDNYYTTSSCIGRVGIMEIPKDKNPKLYSRWLGKWHHYASYDELFNALKNKKEGYIVFVMNSPILHIACKDIESAKKMLELAIHSGLKASSIKSISDKRVIVEILTTYKVDTPIGEDGEIFVDNNYLKFLLDYSNSKLKRAREILMRWANRLDELKK", "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": "MRNSLYKKNIISINDLQRNELELVLNKSAMLKRTPQPNLLKNKVIASCFFEASTRTRLSFETAIYRLGASIVGFSDGNNISLEKKGETLTDTISVISSYVDAIIIRHPQEGSARLAAEFSNKKPIFNAGDGANQHPTQTLLDLFTIQETQNRLTQLNIAIVGDLKYGRTVHSLTQALAKFKHNKFYFISPDALKMPNYINNMLDKKEIYWKRHNNIEEIISEIDILYMTRIQKERLDSTEYANAKSKFVLRAAILKNARNNMKILHPLPRIDEIDRDVDYTPYAWYFKQAANGIYARQAILSLVLIEKHL", "text": "SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family."}
+{"protein": "MKYTLTKANPDADVYPAQTSQTVNDPMEDEVNKNVFMGRLEDLVHSTANWGRKHSLWPFNFGTSCCYVEYATTLTAVHDLSRFGAEVIRASPRQADVMIVAGTCFVKMAPVIQRLYEQMLEPKWVISMGACANSGGMYDIYSVVQGVDKIIPVDVYVPGCPPRPEALIQGLMLLQESITKERRPLGIHVNDQGIYQPQMTPERDRKQADRIAVKNLRSPDSI", "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": "MKCLCFIVLLAIVIAQSYVGVEAAPSDGFVSRNGVQFILNGKPFYANGFNAYWLAYEATDPTTRFKITNVFQNATSLGLTIARTWGFRDGAIYRALQTAPGSYDEQTFQGLDFVIAEAKRIGIKLIILLVNNWDDYGGKKQYVDWARSKGEVVSSNDDFYRNPVIKDFYKNHVKTVLNRVNTFTKVAYKDEPAIMAWQLMNEPRCGVDKSGKTLMDWINEMAPFVKSVDPNHLLSTGHEGFYGDSSPERKNSLNPVSANTVGADFIANHNIDAIDFASMHCGSDLWFQRLDQNSRLAFIKRWLEGHIEDAQNILKKPVILAEFGLGSDTPRYTLANRDGVFTTTYDIIYASAQKGGSAAGALFWEVISEGMSNFAGPSSIILSDKSSTVNIISEHARKMGLLGETTRK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
+{"protein": "MSTFGELANEVVNNSYHKDLLRLSWGVLSDDMEGTGLMLMANLFNMSPESRLKFGRLGHLSTGRDNSKLRGHSITLMYALKNFVDALDDVDRLKCVVEKFAVNHINRQISAEEFGKIVGPFRAVLRIRMGDYFDEEIVAAWAALIAVVQAAL", "text": "SIMILARITY: Belongs to the globin family."}
+{"protein": "MMLRGGCQRVGARLRGLRRGPRGPADGARRGVVSCIDPSMGLSEEQKEFQKVAFNFAAREMAPHMAEWDQKELFPVDTMRKAAQLGFGGVYVQTDVGGAGLSRLDTSIIFEALATGCTSTTAYMSIHNMCVWIIDRFGSEEQRHRLCPPLCTMEKFASYCLTEPGSGSDAASLMTSAVRQHDHYILNGSKAFISGGGEADIYVVMCRTGGPGPRGISCVVVEKGTPGLSFGKKEKKVGWNSQPTQAVIFEDCAVPVANRIGDEGQGFLIAMKGLNGGRINVASCSLGAAHASIVLARDYLKVRKQFGEPLANSQYLQFQLADMAARLVASRLMIRTAATALQEEREDAIVLCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRMLISRSLLQE", "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": "MNQKVLFIDRDGTLINEPPADFQVDRMDKLALEPGVIPVLLALQKAGFRLVMITNQDGLGTTSFPQADFDGPHDLMMAIFTSQGIVFDEVLICPHLPTDGCACRKPQTGIVTPWLKEHALDSAHSYVIGDRETDMALAANMGITGLRYQRASLNWPAIGEQLTRSDRHARVNRVTRETAIDVEVWLDREGDSRINTGIGFFDHMLDQIATHGGLRINIAVKGDLHIDDHHTVEDTALALGEALNKALGDKRGIGRFGFVLPMDECLARCALDISGRPHLEYKAKYSFQRVGDLSTEMVEHFFRSLSYAMACTLHLRTKGKNDHHRVESLFKAFGRTLRQAIRVEGDTLPSSKGVL", "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": "MKQGIHPEYKEITATCSCGNIIKTKSTLCENIHIDVCSSCHPFYTGKQKVLDTGGRIDRFKKRFGGRMGRSS", "text": "FUNCTION: Binds the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily."}
+{"protein": "MARYRHSRSRSRSRYRRRRRRRRSRYRGRRRRYRRSRRRRRRGRRRGNCLGRRGYRRRRYSRRRRRRYY", "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": "MTWQQRITTALEKRRATDAFRVRTVVEGGAGRFLIRDQCQFCNFSSNDYLGLSQHPAIVRAWQDGAERYGVGSGGSGHVSGYTTAHHALEESLADWLGYSRALLFISGFAANQALIAALMEKDDRIVADRLSHASLLEAANLSPAQLRRFAHNDASQLNTLLEKPCDGQQLVVTEGVFSMDGDSAPLGDVQATAQRHSAWLLVDDAHGIGVLGDEGRGSAFSQHVQPEVLVVTFGKGFGVSGAAVLCSDSVADYLLQFARHLIYSTSMPPAQAVALQAALKVIRSDDGEQRRQTLAALIQRFRAGVRDLPYQTTDSHSAIQPLIVGENSRALTLAEQLRERNMWVTAIRPPTVPAGTARLRLTLTAAHQTQDIDNVLEALYAAG", "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": "MKKSFILQQQEISFAKNTFTEKLAEHLGIVEVQGPILSQVGNGIQDNLSGAEKAVQVNVKQITDATFEVVHSLAKWKRHTLARFNFAQGEGLFVHMTALRPDEDSLDQTHSVYVDQWDWEKVISAEQRNLAYLKETVRAIYAAILETEEAVSKKFGLATFLPKDIQFVHSEELVQRFPNMNDKERENAICKEYGAVFLIGIGGKLSDGKPHDVRAPDYDDWTTPSEGEYKGLNGDILVWNPILERAFELSSMGIRVDETALRKQLALTNNEDRLKFDWHQDLVNGRLPLSIGGGIGRSRLVMLLLQKKHIGEVQSSVWPKWVMEQFDNIL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily."}
+{"protein": "MSGTAEENTREVEAGVVTDFTREMSYGEYLHLDELLAAQHPLSTPEHHDELLFIVQHQTSELWLKLVLHELRSAMRAIAADDLKTALKNIARVKHIQRTLTEQWSVLATLTPTEYAQFRGFLANSSGFQSQQYRAVEFALGNKNAKMLDVFAHDGPGHAQLTELLEAPSLYDEFLRHLARRGHDVPAELLERDVTKAHVHTPALVATFRVIYEDAQRYWTEYEACEELVDLEENFQLWRFRHLKTVERTIGFKRGTGGSSGVGFLARALDLTFFPELYAVRTEIGS", "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": "MYPAHLLVLLAVCVSLLGAASVPPQPLNLVQFGYLIQCANHGSRATWHYMDYGCYCGAGGSGTPVDDLDRCCKIHDDCYGDAEKKGCSPKMLAYDYYCGENGPYCKNIKKECQRFVCDCDVKAAKCFAGAPYNDANWNIDTTKHCQ", "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": "MNSIEFPLLDRTTQNSVISTTSNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTISGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKISREIYEDRIKSQRENRCFTTNHKFQVGRSIHTGNYDRGFLYQPPFTSEIPSETFFKYKSSVSSHELVN", "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": "MTNTKTLEENISFEEALKELEEIVKKIDNGQESLETAVNSFERGILLKNHCEKKLKEARLKIEKITKLADSTGVLEETEV", "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": "MSEELSHGKDYTLESDSELRFEIEQKDAKVLVTLISGFAELFGTELVKKKKYEFGVGAKVAIFTYQGCVLHVSGKMDVCYISKETPMVQYLNCHAALEQFRTDAEDKDQRGPVAMVVGPMDVGKSTLCRILLNYAVRVGRRPLYADLDVGQGAIAISGNVATILIERPASVEDGFPKTAPLVYHFGHKSPGGNSVLYNSVVSKMAEVTLQSLNSNKRTKSSGIIINTCGWVKGSGYAHLLHAAQAYGACAIFVLDQERLYNELLRDVPQGVNVVLLPKSGGVVERSKELRHESRDLRMKEYFYGNPRAPFYPFSFEVKFQDLRLYKIGAPPLPDSCMPIGMKAEDNKTKVVAVTPTPALIHHILALSFAESVEDDVIGSNVAGFCCVTEVDMERQAVMVLSPQPRPLPPNSLLLWSELQFMDNHT", "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": "MTAAAGNKDHQKVILVGDGAVGSSYAFALVTQNIAQEVGIIDINVPKTEGDALDLSHALAFTSPKKIYAATYDDCHDADLVVLTAGAPQKPGETRLDLVHKNLKINKEIVTTIVDSGFNGIFLVAANPVDILTYSTWKFSGFPKERVIGSGTSLDSARFRQAIAELVDVDARNVHAYILGEHGDTEFPVWSHANVAGLQIYEWVKNNPDVDEEAMVNLFFNVRDAAYTIIEKKGATFYGIAVALARITKAILNDENSVLPLSVYLEGEYGQNDIYIGAPAIINRQGVKQVIEIPLTDAEQEKMEASASALKEVIETAFAKFEAEEAK", "text": "FUNCTION: Catalyzes the conversion of lactate to pyruvate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family."}
+{"protein": "MACGLVASNLNLKPGECLRVRGEVAPDAKSFLLNLGKDDNNLCLHFNPRFNAHGDINTIVCNSKDGGAWGAEQREVAFPFQPGSVVEVCISFNQADLTVKLPDGHEFKFPNRLNLEAINYMSAGGDFKIKCVAFD", "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": "MLTYETWEENVVSFSEEDETKGALSVLNWAYEEYKDEIVYACSFGVEGMVLLHLINQVNPSAKVVFLDTNVHFQETYELIQRVRERFPSLNIIEKQPELTLDEQAKLHGEKLWESNPNLCCKIRKILPLEKSLVVEKAWISGLRREQSETRKHTKFINQDHRFQSIKVCPLIHWTWKEVWRYVYKHSLPYNPLHDVGYPSIGCEKCTLPVGDGGDSRDGRWAGKMKTECGLHYQ", "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": "MNPRPLIGITMGDPVGIGPEIILTALAGTSVYEKCRPLVIGDPGVLGQAMAVAGYAPVIHMTDTPETGVYRPGTISMFSPAPPLSPVTWGEPTPETGGAMEAWITTAVDMAMAGAISAMVTCPINKEALKMAGSAFAGHTEMLAMRTGTNRYAMMLAGNRLRVVLVTIHTALQNVPGLLSVDAIADTILLTVESLKQRFGMNAPRVAVAGLNPHAGEGGLFGDEEARLITPAIEAARRKTEAAITGPWPPDTVFVKAAAGDFDAVVCMYHDQGLIPFKLLHFEDGVNTTLGLPIIRTSVDHGTAYDIAGTGRADCRSLTAAIDMAIDQAACLGKRPAA", "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": "MASQGTKRSYEQMETGGERQNATEIRASVGRMVGGIGRFYIQMCTELKLSDYEGRLIQNSITIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRRDGKWMRELILYDKEEIRRIWRQANNGEDATAGLTHLMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQRAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGLSVASGYDFEREGYSLVGIDPFRLLQNSQVFSLIRPNENPAHKSQLVWMACHSAAFEDLRVSSFIRGARVVPRGQLSTRGVQIASNENMETMDSSTLELRSRYWAIRTRSGGNTNQQRASAGQISVQPTFSVQRNLPFERATIMAAFTGNTEGRTSDMRTEIIRMMENARPEDVSFQGRGVFELSDEKATNPIVPSFDMNNEGSYFFGDNAEEYNN", "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": "MDSNTITSFQDILQRMSKMQLESSSADLNGMITQFERLKIYRDSLGESVMRMGDLHSLQNRNATWRDELSQKFEEIRWLIAECRNILTRTENSFEQITFLQALQLLLEVESEIRTFSFQLI", "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": "MVTILQLLVSILILLSFALVVGVPVILVSPGEWERSKNLVYASAGLWFGLVIVTAAFNSFVI", "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": "MSPFSIVLIGFAMSTDAFAAAIGKGAAMRKPQWRDALRAGLIFGCIEAITPVIGWVLGRAASSYLSAYDHWIAFVLLGALGTHMMIAGLRNGPDDANDAEAKTPKRHGLLGLATTGFATSIDAMAVGVSLAFLDVHIGVVAVVVGLCTFSMVTAGVMLGRALGNLIGKRAEILGGLILVIVGSVILYEHLGAAT", "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": "MFPARRGLHTTSRACARTRFTKPKPKPAKRENVRLPTQRTHHDNDLKITAPIPPAAANLTCPDDHPLWQFFSEKKFLRTPEELDTLSRPWTIPELRRKSFTDLHSLWYTCLKERNVLARENHLVQFNFEAQTEAYQDISEKIRTTMWRIRHVLSERDWAFKIANEKFAVEKQVFIESFEKDFLEAPANEDEEIFESLQRFQYAIYGISEYIDENKVDRTFVDGLKAVATLKLKKFALRNEDIKNFLEESNNTIVDAGESFLLYTSENTESAIAEACQAVRELRENGSSVSRYDELETVQEYVNKLAEAQMAKVTEAEIQLQEEDAKNNANTL", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
+{"protein": "MRVLVLPEELRDELKEPLGVLYRCHGVECVERMSDHLRAAERVIAVGDITTFYLLKASFIPDLMIVDHKTKRSPVEDSIKRRHLEGSYRVVNVENPAGTLTEELLDAVRESLNGCTPTEIIVDGEEDLAALPAILYAPLGSAVVYGQPSVGSVLVMVTPEKKREIEGILRRMTVKEKV", "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": "MMSKLGALLTICLLLFPLTAVPLDGDQPLDRHAERMHDGISPKRHPWFDPVKRCCKVQCESCTPCC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily."}
+{"protein": "MRRHKSKSIPGRNLRLADQIQKDLAGIIQREIDMTRAGLITLSGVELSADYAHAKVYFTVLGAEPDTAAALLNEKAGWLHSQLYKLLHIHTVPTLRFVHDLQITRGIEMSVLIDRANRPGPHSGVPDEPEDQS", "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": "MPTRLTKTRKHRGNVSAGKGRIGKHRKHPGGRGKAGGQHHHRTNLDKYHPGYFGKVGMRYFHKQQNHFWRPEINLDKLWTLVDSEKKDEYLSKSSASAAPVIDTLAHGYGKVLGKGRLPEVPVIVKARFVSKLAEEKIRAVGGVVELVA", "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": "MDSLAALYKNHIVTLQERTRDVLTRFKLDALLIHSGELLNVFLDDHAYPFKVNPQFKAWVPVTQVPNCWLLVDGVNKPKLWFYLPVDYWHNVEPLPTTFWTEEVDVIALPKADGIGSQLPAARGNIAYIGPVPERALGLDIPADKINPKGVIDYLHYYRAYKTDYELSCMREAQKTAVNGHQAAHEAFLSGMSEFDINQAYLTATGHRDTDVPYGNIVALNEHASVLHYTKLDHRAPSEIRSFLLDAGAEYNGYAADLTRTWAANSDTDFAHLIKDVNDEQLALISTMKAGTSYVDYHIQFHQRIAKLLRKHQIVTDMSEEAMVENDLTGPFMPHGIGHPLGLQVHDVAGFMQDDTGTHLAAPSKYPYLRCTRVLEPRMVLTIEPGIYFIDSLLNPWREGQFSKHFNWQKIDALKPFGGIRIEDNVVVHENNIENMTRDQKLA", "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": "MENLTNIFLFLSNENEGIQLNTDIFEANIINLALLIVLVINVAKDVLGSILSARKASILDKIEEADKKLNEADKRFTEARLQWSQANIFGEDLEKKTYQRINAFHESQNLKNKDALLREYFSTLVVLDLKNEQVQKQVRNYVMELALIEVYGVFTKLVANKKFQENYSNYSVLLLEKLIGEK", "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": "MSERLFVLSQHILPKLALTRLAGRFADWKGGGITTAAIRRFIARYNVDMGEAADSDPAAYATFNDFFTRALKPGVRPVADARLVCPVDGAVSQLGAIDSGRIFQAKGRDYSATALLAGDADLAARFADGHFATIYLSPRDYHRIHMPCAGRLLEMTYVPGDLYSVNPATARGVDRLFARNERVVCVFEDEQSQPFVMVLVGATIVGSMATVWHGVVNPPRRPAVEKWDYRGQDIRLAKGEEMGRFLLGSTVVLLYPAGPLKFNPQWQAASPVRMGEAMAS", "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": "MALSMYHYIENTWNSEEWKKSVLRQRLIKWRKEPSIVRLAKPTRLNRARSLGYKAKQGFVIVRVRVRRGGLNKPRPNKGRRPKRMGVYGYSPAKGYRWIAEERAARKYPNLEVLGSYYVGEDGLYKYYEIVMVDPSHPVIKSDPKHKWLQDPSNRNRVFRGLTSAGKKVRGLRKSRGLKGTVRYKWNRKQKEREEKKRHEASKYYKLQEYDKIPGK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family."}
+{"protein": "MSQFDNVSVVKKANLYFDGKCVSHTVTFADGTRKTLGVIFPAALTFNTGAPEIMEINAGVCRVRLAGSDEWKTYGAGQQFDVPGNSSFDIEVTETLDYVCHFG", "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": "MANRGGRHARNEDSENTINYVQCDGLAVMKMIKHCHEESSNMDLAQGALLGLVVDKCLEITNCFPFPKSGDETMDEEMYQLTVMRRLRRVNVDHLHVGWYQSSDVGNSLSLALLESQYHYQTSIEESVVVVYDTQKSSRGFLCLKAYRLTPQAIQMYKDGDFTPEAFRTLKVGYESLFAEIPIVIKNSPLTNIMMSELNELLPEDKGHNFLDLGTASVLENHMRSLIERVDELYQEAVRYNKYQQVVFKQDTEKHRALAKLAAENAVRTSKGEPTVPEEEVIKQFRPMPVPARLTATITSGQINTHAQHIAQFCSQSLAKLFITESLQNAKETKEIK", "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": "MARLSEPSPYVEFDRTQWRALRMSTPLKLTEDELKKLRGLGEKLDLLEVEEVYLPLARLIHLQVAARQRLFAATSEFLGEPQQNPDRPVPFIIGVAGSVAVGKSTTARVLQALLARWGNHARVDLVTTDGFLYPNAELGRRNIMHRKGFPESYDRRALMRFVTAVKSGADYACAPVYSHLLYDIVPGEKQVIRHPDILILEGLNVLQTGPALMVSDLFDFSVYVDARLEDIEGWYISRFLTMRSTAFADPASHFHHYATLTDEQAVFAARDIWHSINRPNLIENILPTRPRATLVLRKDADHAINRLRLRKL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic pantothenate kinase family."}
+{"protein": "MHRKRLRVVLSATLLDLITCVQLMLDPLVRSHVIARLVRWRHHRLLLAELVLSETRVRILRLALEQGALESGAMSSRALARIVIPRSSSRPNWKLSRVVSELSDNSKTNVYKNQLFIHCARYLLHVLP", "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": "MEQAGTRPAATEHPRLRRPMPWLLLLPLLLLLLLLLPGPAASQLRYSVPEEQAPGALVGNVARALGLELRRLGPGCLRINHLGAPSPRYLELDLTSGALFVNERIDREALCEQRPRCLLSLEVLAHNPVAVSAVEVEILDINDNSPRFPRPNYQLQVSESVAPGARFHIESAQDPDVGANSVQTYELSPSEHFELDLKPLQENSKVLELVLRKGLDREQAALHHLVLTAVDGGIPARSGTAQISVRVLDTNDNSPAFDQSTYRVQLREDSPPGTLVVKLNASDPDEGSNGELRYSLSSYTSDRERQLFSIDASTGEVRVIGGLDYEEASSYQIYVQATDRGPVPMAGHCKVLVDIVDVNDNAPEVVLTDLYSPVPENATPNTIVAVLSVNDQDSGPNRKVSLGLEATLPFRLNGFGNSYTLVVSGPLDRERVAVYNITVTATDGGIPQLTSLRTLKVEISDINDNPPSFLEDSYSIYIQENNLPGVLLCTVQATDPDEKENAEVTYSLLEREIQGLPVTSYVSINSASGSLYAVNSFDYEKFREFFVTVEAQDKGNPPLSSTGTANVYVVDMNDHAPHILYPSSTNSSAAFEMGPRTAPAGYLVTKVIAMDSDSGQNAWLFYHLAQTSDLDLFKVELHTGEIRTTRKMGDESGSTFNLTVVVRDNGEPSLSASVAITVAVVDRVSKILPDTQRHVKSPRTYSEITLYLIIALSTVSFIFLLTIIILSIIKCYRYTAYGTACCGGFCGVRERSPAELYKQANNNIDARIPHGLKVQPHFIEVRGNGSLTKTYCYKACLTAGSGSDTFMFYNTGAQTGPGPSGAQAAVTDSRNLTGQSGQNAGNLIILKNEAVSQNEPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ", "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": "MSAQKPGLHPRNRHHSRYDLATLCQVNPELRQFLTLTPAGEQSVDFANPLAVKALNKALLTHFYAVANWDIPDGFLCPPVPGRADYIHYLADLLAEATGSIPANASILDIGVGANCIYPLIGVHEYGWRFTGSETSSQALSSAQAIISANPGLNRAIRLRRQKESGAIFNGIIHKNEQYDATLCNPPFHDSAAAARAGSERKRRNLGLNKDDALNFGGQQQELWCEGGEVAFIKKMIEESKGFAKQVMWFTSLVSRGENLPPLYRALTDVGAVKVVKKEMAQGQKQSRFIAWTFMNDEQRRRFVNRQR", "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": "MIIFEKSVPGRKAYRLPDEELQRIDPVFPEHLKRTRPLRLPELSEPDVVRHYTALAEKNYSVDKGFYPLGSCTMKYNPKLNEYVAGLEGFTDIHPYQPWESVQGALQVMYELKEFLCEITGMDEMTLQPAAGAHGELTGMLIVRAYHLSRNDKKRHVALVPDSAHGTNPASAAMAGFDVVEIKSTEDGLVDLEQLENHLNDEIAVLMLTNPNTLGLFEKDIVKIAEKVHQAGALLYYDGANLNAIMGKIKPGEMGFDIVHLNLHKTFSAPHGMGGPGSGPVGVKAFLSEFLPIPIIRKDGDKYYPDFKLPNSIGRTRSFYGNFLVLLKAYVYILSMGKDGLTRASEMAVLNANYLRSLISKFLKIASPGICMHEFVVDGSQFVKETGVKILDVAKRILDYGLHAPTVYFPLIVHEDMMIEPTETENKNTLDYFAKVLEKIVEEAKKTPEVVKTAPHTTPVKRLDDITATKKPVYRYRLS", "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": "MKTPTKYFIIFILLAALAVFVSEATSKVGQQTTTTTQQVKCSGLQCTLNKLIVAVGKFTIKQILVGIVIVLATIALHQQYVITQKKGSLPGPSFVPPFFGMLFQLIFTPFSFYEKQEKYGPISWTSIMNKFVLFVTDAEINRQVFKEENAKLYLSLGAKKILTEKAIPFIEGAPHRQLRKQLLPLFTIRALSSYLPIQESIVDEHIAMWIKNGKADINARNNCRDLNMAISTGVFVGNNTPESVRDDIAKNFFVMNEGFLCLPIDLPGTTLRKAINARVRLVEIFTDIIAKSRKRMGDGEKPQSLIDLWVEHFLNCPEEERDELSNDTIIFTLLSFMFASQDALTSSLVWTVQLMAEHPDILAKVRAEQASLRPNNEKLDLDTMRQATYTRMVVSEILRFRPPAVMVPHENIEDIVIGDNVHVPKGTMILPSIWSAHFQEGGYSDPYKFDPQRFDSVRKEDVTCAKNSLVFGAGPHFCIGKELAKNQIEVFLTKLAMSTEWTHNKTPGGDEIIFGPTIFPKDGCNITIKARN", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MGFITKAIPIVLAALSTVNGARILEAGPHAETIPNKYIVVMKKDVSEEAFSAHTTWLSQTLNSRLMRRAGSSKPMAGMQDKYSLGNVFRAYSGEFDEAMIKDISGHDDVDFIEPDFVVRTTTNGTNLTHQDNVPSWGLARVGSKQAGGTTYYYDPSAGKGVRAYIIDTGIDTDHKDFGGRAKWGKNFADDMDQDCNGHGTHVAGTVGGTQYGLAKSVSLIAVKVLDCEGSGSNSGVIKGMEWAMRDASGGGNGTAKAAGKTVMNMSLGGPRSEATNQAAKAISDAGIFLAVAAGNENMDAQHSSPASEPSVCTVAASTKDDGKASFSNYGSAVDVYAPGKDITSLKPGGSTDTLSGTSMASPHVCGLGAYLIGLGKQGGPGLCDTIKEMANDAIQSPGEDTTSKLIYNGSGK", "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": "MKVAVLGAAGGIGQALALLLKLQLPAGTNLALYDIAPVTPGVAVDVSHIPTAVKVVGYAGEDPTPALEGANLVLISAGVARKPGMDRSDLFNINAGIVRNLIEKVATVCPTACVGIITNPVNTTVAIAAEVLKKAGVYDKRKLFGVTSLDVLRSETFVAELKGKDVNDVKVPVIGGHSGVTILPLLSQAFEEDKIDFTAEEVAALTKRIQNAGTEVVEAKAGGGSATLSMAQAAARFARSVLKGLTGEQVVEYAYVEGNGEYARFFAQPVRLGLNGVEELLPIGTLSAYEEEAVQAMIPTLKADIELGEKFVNG", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family."}
+{"protein": "MKCPFCNASDTKVVDTRASEDDKIVRRRRECISCHKRFTTYERYDFNNLTVVKKDKNREAFDRDKVYRGMKKSCEKRPVPDSVLLEATKEIEVELTHSNKREVDSSEIGELIMKKLKKIDKVAYIRFASVYREFTDVKSFNEEISKLDNE", "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": "MSSGGLLLLLGLLTLWEALTPVSSTDRPEFCELPEDSGPCKGLFHVFYYNSDQNQRLEFIYGGCYGNANNFKTIEECKRTCAA", "text": "FUNCTION: Serine protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family."}
+{"protein": "MITEIMKQVEIFTDGSCLGNPGPGGYGIVMRYKGTEKTFSEGFNKTTNNRMEMLAAVVALRKLKEPCSVILTTDSQYVRQGITQWIHGWKKRDWKKADKKPVVNADLWKQLDAESERHKIDWRWVKGHAGHRENEMCDELARTAAENPTQDDTGYPG", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase H family."}
+{"protein": "MSHPPIQTATLSWNEQGTPVSEQFGDIYFSNEDGLEETHYVFLKGNGFPERFALHPRDNCVFAETGFGTGLNFLTLWRDFAQFRQLHPAAKLQRLHYISFEKYPLQVADLAAAHQRWPELACFAEQLRAQWPLPLAGCHRILLAEGAITLDLWFGDVNTLLPQLDSSLNNQVDAWFLDGFAPAKNPDMWNDVLFNAMARMARPGGTFATFTAAGFVRRGLQQAGFDVAKIKGFGQKREMLTGILPQRLNTQSEPWYHRPLATRCDDIAIIGGGIVSALTALALLRRSAKVTLYCADALPAQGASGNRQGALYPLLNGKNDALEIFFTSAFTFARRQYSQLLEQGIRFDHQWCGVSQLAFDEKSRGKINKMLQTDWPPQLAAAMSREQLSALAGLDCAHDGIHYPAGGWLCPSDLTTALMALAQQLGMTCHYGHELCQLERVDGLWQLIFTSPQVNRQHTTVVLATGHRLPEWQQTQHLPLSAVRGQVSHIPTTPVLSQLRQVLCYDGYLTPVNPANQHHCIGASYQRGDVTTDFRADEQQENRDRLLRCLPDVSWPQQVDISDNQARCGVRCAIRDHLPMVGAVPDYSATLAQYQDLPRKIQHGEDIPLAPVWPELFMVGALGSRGLCSAPLVAEILAAQMFGEPQPLDTTTLAALNPNRFWIRKLLKGRPVQQRVSVLS", "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": "MPIKAILTDIEGTTSAVSFVFDVLFPFARKHLPAFVREHAEQPAVAQQLQAVRDLAGEPDADVERVIALLLEWIAEDRKATPLKALQGMVWEQGYNAGQLKGHVYPDAVDALKHWHQQGYRLYVYSSGSIQAQQLIFGCSEAGDLSGLFSGYFDTTSGPKREAQSYRTIAQAMDCPAGDILFLSDIVEELDAAQAAGMATCGLARDGGALAGHRYVTSFALIDPASF", "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": "MDSLTSAASVLAAALAVGLAAIGPGIGQGSAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALVLLFANPFA", "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": "MASEIFGIAAVFWVLIPVGLAGGALLLKLQGD", "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": "MPLNRTLSMSSLPGLEDWEDEFDLENTVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYYLVGPYTEQGVRTQVELLEAPTPALKKTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAGIGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQTVVALFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKYLGRYYMSARHMALSKAFPEHFTYEPSEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDEEDPRNGPLEEDSERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLSTPSEPLSPTSSLGEERN", "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": "MTTTSAFMLNVRLDNVAVVAIDVPGEKVNTLKAEFAAQVRAILKQIRENKALQGVVFISAKADNFIAGADINMIGHCQNAQEAETLARQGQQLMAEIQALPVPVIAAIHGACLGGGLEMALACHRRICTDDVKTVLGLPEVQLGLLPGSGGTQRLPRLVGVSTALDMILTGKQLRARQALKAGLVDDVVPQTILLEAAVELAKKERLAQRTLPVRERILAGPLGRALLFRLVRKKTAQKTQGNYPATERIIDVIETGLAQGSSSGYDAEARAFGELAMTPQSQALRAVFFASTEVKKDPGSDAPPGPLNSVGILGGGLMGGGIAWVTACKGGLPVRIKDINTQGINHALKYSWDLLETKVRRRHIKASERDKQLALISGSTDYRGFSHRDLVIEAVFEDLPLKQQMVAEVEQNCAAHTIFASNTSSLPIGDIAANAARPEQVIGLHFFSPVEKMPLVEVIPHASTSAQTIATTVKLAKKQGKTPIVVSDKAGFYVNRILAPYINEAIRMLTEGERVEHIDAALVKFGFPVGPIQLLDEVGIDTGTKIIPVLEAAYGERFSAPANVVASILNDDRKGRKNGRGFYLYGEKGRKSKKQVDPAIYKLIGVQGQSRLSAQQVAERCVMLMLNEAARCFDEKVIRSARDGDIGAVFGIGFPPFLGGPFRYMDALGPGEMVATLQRLAALYGPRYAPCEQLVRMAERREHFWTNGETDQGN", "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": "MELIEKHASFGGWQNVYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDTSPRGSHVADADRYDLGQGAGFYLNATQAPWNEHYKMYDYIRNELPDLVMQHFPATTRKSISGHSMGGLGALVLALRNPDEYVSVSAFSPIVSPSQVPWGQQAFAAYLGENKDAWLDYDPVSLISQGQRVAEIMVDQGLSDDFYAEQLRTPNLEKICQEMNIKTLIRYHEGYDHSYYFVSSFIGEHIAYHANKLNMR", "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": "MTDPRRTEQVHPDYADLDTLAPDALIAALADDQLGAVRAVQAAAPQLTAALNAAVPQLERGGRLVYVGAGTSGRLGVLDATELTPTFSWPPERAVPLIAGGERAIRQAVEGAEDDEAAGERDVQAVNIGPDDVLIAVAASGTTPYVLGAARSGRAAGALTVGLANNPGAPLLAAVDCPVLLDTGPEIISGSTRLKAGTAQKIALNTLSSALMVRLGKLYGNLMVDVRATNAKLEDRARRLVQHATGADADAAQAALSECGGSVKTALVMLKLGLGAQEAAQRLEGAGGHARQVLGEGEALGTSAS", "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": "MSLCTVEINLSTIKNNYLLLQDICKTSLVGAAVKANGYGLGAVQISKALIEENCRHFFVASSEEGVNLRNALGLDVNILVLNGVFEHDALELIEYNLTPVLNNLKQIEIWQKFSNLKNRLLSCYLHFNTGINRLGLSSDEIEQLINDRDLLKGLDLQYIISHLAISEEIDNPYNLEQLNRFKAYLQYFPNVKASLANSGGIFLGQDYHFDLARPGAALYGLNPLTKNPVTLKAPIIHLQNLTLDSHIGYNMTFTTKRDSVIATLPLGYADGFSRNFSNQGEVFINSRSVPIVGRVSMDLINIDVTDLPPSEIFLGQEAEIIGNYCTPDKIASIIGTIGYEVLTNLGSRYKRKYIG", "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": "MYHVYLLSDATGETVERVARAALTQFRDVDIRLRRMGQIRNREDILRALDEVDRAPGIIFYTLVNTELAQFVRNEVEARQLEAVDLITPLLYKLAEFLEMRPQKLPGLQYEMNSEYYRRMEAVDFTVKQDDGQEPRNLHKADIVLIGVSRSSKTPLSMYLAHKGYKVANVPIIQGIDPPGELEEVEPERVVGLIIDTQRLVDIRSARLRNLRQSPRGSYADYRQVEEELAYCRRFYRAHPAWLVIDVTNKSVEESAAEILSRLHGDIRHD", "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": "MNYFPWLTLIVVLPISAGSLIFFLPHRGNKVIRWYTIFICMLELLLTTYVFCYHFQLDDPLIQLVEDYKWINFFDFDWRLGIDGLSIGPILLTGFITTLATLAAWPVTRDSRLFHFLMLAMYSGQIGSFSSRDLLLFFIMWELELIPVYLLLSMWGGKKRLYSATKFILYTAGGSIFLLLGVLGIGLYGSNEPTLNFETSANQSYPVALEIIFYIGFFIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELLPHAHSIFSPWLVVVGTMQIIYAASTSSGQRNLKKRIAYSSVSHMGFIIIGIGSITDTGLNGAILQIISHGFLGAALFFLAGTSYDRIRLIYLDEMGGIAIPMPKIFTMFSILSMASLALPGMSGFVAELIVFFGIITSQKFLLMPKILITFVMAIGMILTPIYSLSMSRQMFYGYKLFNAPNSYFFDSGPRELFVLISIFLPVIGIGIYPDFVLSLSVDKVEAILSNFFYR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family."}
+{"protein": "MITYDDEVVCAPRAGTLYDVLELILDRGMVIDVFVRVSLVGIEILKVDARIVVASVDTYLRFAEACNRLDLEHDVRSKTVPEMFGSPMAKTVGRAGARRTARSLTDKVRDVLTPEHEHEEEPEEAEDRPRAGAERGRSTQRPRSRPAARPRDEDDRPRSRPRRRTEEEDR", "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": "MIDAGTDRGDIAITVRDAYKRYGDFVALDHVDFVVPTGSLTALLGPSGSGKSTLLRTIAGLDQPDTGTVTIYGRDVTRVPPQRRGIGFVFQHYAAFKHLTVRDNVAYGLKVRKRPKAEIKAKVDNLLEVVGLSGFQGRYPNQLAGGQRQRMALARALAVDPQVLLLDEPFGALDAKVREDLRAWLRRLHDEVHVTTVLVTHDQAEALDVADRIAVLNQGRIEQIGSPTEVYDAPTNAFVMSFLGAVSTLNGTLVRPHDIRVGRTPEMAVAAEDGTAESTGVARAIVDRVVKLGFEVRVELTSAATGGPFTAQITRGDAEALALREGDTVYVRATRVPPITAGATTVPALSRDGADEATLTSA", "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": "MSLLSKTRELNTLLQKHKGIAVDFKDVAQTISSVTVTNVFIVSRKGKILGSNLNELLKNERIIQMLENRHIPVEYTDQLMDVKETQSNIGIDNVLTVFPPENNDLFGDSRTTIFPILGGGERLGTLVLGRVTEDFSENDLVLGEYAATVIGMEILREKHNEVEQEARDKAAISMAINSLSYSESEAIEHIFEELGGKEGLLIASKVADRVGITRSVIVNALRKLESAGVIESRSLGMKGTFIKVKKDKFLDELERIK", "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": "MADDPGSSFTTVWNAVVSELNGEPVADGGAANRTTLVTPLTPQQRAWLNLVRPLTIVEGFALLSVPSSFVQNEIERHLRAPITDALSRRLGQQIQLGVRIAPPPDDVEDAPIPPAEPFPDTDAALSADDGADGEPVENGEPVTDTQPGWPNYFTERPHAIDPAVAAGTSLNRRYTFDTFVIGASNRFAHAAALAIAEAPARAYNPLFIWGESGLGKTHLLHAAGNYAQRLFPGMRVKYVSTEEFTNDFINSLRDDRKVAFKRSYRDVDVLLVDDIQFIEGKEGIQEEFFHTFNTLHNANKQIVISSDRPPKQLATLEDRLRTRFEWGLITDVQPPELETRIAILRKKAQMERLAVPDDVLELIASSIERNIRELEGALIRVTAFASLNKTPIDKSLAEIVLRDLIADASTMQISAATIMAATAEYFDTTVEELRGPGKTRALAQSRQIAMYLCRELTDLSLPKIGQAFGRDHTTVMYAQRKILSEMAERREVFDHVKELTTRIRQRSKR", "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": "MKDVVIVGALRTPIGCFRGALAGHSAVELGSLVVKALIERTGVPAYAVDEVILGQVLTAGAGQNPARQSAIKGGLPNSVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLTDSRTGAQLGNSQLVDSLVHDGLWDAFNDYHIGVTAENLAREYGISRQLQDAYALSSQQKARAAIDAGRFKDEIVPVMTQSNGQTLVVDTDEQPRTDASAEGLARLNPSFDSLGSVTAGNASSINDGAAAVMMMSEAKARALNLPVLARIRAFASVGVDPALMGIAPVYATRRCLERVGWQLAEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRNARKGLATLCIGGGQGVALTIERDE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
+{"protein": "MNEQYSAMRSNVSMLGTLLGDTIKEALGEHILDRVETIRKLSKSSRAGNEASRQELLTTLQNLSNDELLPVARAFSQFLNLTNTAEQYHSISPHGEAASNPEALAQLFTRLKDKKLSDQDMRSAVDDLSIELVLTAHPTEITRRTLIHKLVEVNTCLSQLDHNDLADYERNKIMRRLRQLVAQSWHTDEIRKLRPSPVDEAKWGFAVVENSLWEGVPAFLREFNEQLENSLDYRLPVEAVPIRFTSWMGGDRDGNPNVTAEITRHVLLLSRWKATDLFLRDIQVLVSELSMSECTPELRELAGGEEVLEPYRQLMKNVRTQLTNTQAYLEARLKGERVLPPHDLLVSNDQLWEPLYACYQSLKACGMEIIANGQLLDTLRRVRCFGVPLVRIDVRQESTRHTDAIAELTRYLGLGDYESWSESDKQAFLVRELNSKRPLVPLKWEPSAETQEVLETCRVIAEAPQGSIAAYVISMAKVPSDVLAVHLLLKEAGCPFTLPVAPLFETLDDLNNADDVMTQLLGIDWYRGLIQGKQMVMIGYSDSAKDAGVMAASWAQYRAQDALIKTCEKAGITLTLFHGRGGSIGRGGAPAHAALLSQPPGSLKGGLRVTEQGEMIRFKFGLPEVTISSLALYAGAILEANLLPPPEPKKEWIEVMDLLSDASCDMYRSYVRENPEFVRYFRAATPELELGKLPLGSRPAKRRPDGGVESLRAIPWIFAWTQNRLMLPAWLGAGAGLQRAIDAGKRDVLATMCRDWPFFSTRIGMLEMVFAKADLWLAEYYDQRLVDKSLWPLGQQLRDQLAADIKVVLAIANDDHLMADLPWIAESIALRNVYTDPLNVLQAELLHRSRQQEHPDACVEQALMVTIAGVAAGMRNTG", "text": "FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. SIMILARITY: Belongs to the PEPCase type 1 family."}
+{"protein": "MTNKLRSEETITSLSSFMASTLSIASPSPCSIPLSVTKVSPLKRKRPTHLNIPDLNPQQPISTDYFRFREGDAKVSPLKRKRPAHLNIPDLNPQQPIRTDYFSFTDFAHQNGTVSFGGNGFGVVSRNGKKKFMEDTHRIVPCLVGNSKKSFFGVYDGHGGAKAAEFVAENLHKYVVEMMENCKGKEEKVEAFKAAFLRTDRDFLEKGVVSGACCVTAVIQDQEMIVSNLGDCRAVLCRAGVAEALTDDHKPGRDDEKERIESQGGYVDNHQGAWRVQGILAVSRSIGDAHLKKWVVAEPETRVLELEQDMEFLVLASDGLWDVVSNQEAVYTVLHVLAQRKTPKESEEENLVQGFVNMSPSSKLRRASLVKSPRCAKSQSYYYNSENESPSLNREIGSSPSKSPITPWKSLWAKAACKELANLAAKRGSMDDITVVIIDLNHYKG", "text": "SIMILARITY: Belongs to the PP2C family."}
+{"protein": "MSAKTYPVLKAAKAQALIDNDKYLKWYEESIEEPEKFWSKHGKRIDWFKPYTKAKNTSFKGKVPIKWFEDGLTNVSYNCIDRHLKTHGERTAIIWEGDNPYIDKRITYNQLYDNVCRLANVLKAHGVKKGDRVTIYMPMVPEATYAMLACSRIGAVHSVVFGGFSPEALAGRIVDCESTFVITCDEGVRGGKPVALKENTDVAIDIAAKQYVIVNKVLVVRRTGGKVGWAPGRDLWYHQEIAKVKPDCPPVKMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTHEYVFDYKDGEIFWCSADVGWVTGHSYIVYGPLANCATTVMFEGVPNFPDQGRFWEIIDKHKVNIFYTAPTAIRSLMGAGDDFVKRSSRSSLRLLGSVGEPINPEAWEWYYNVVGDQRCPIVDTWWQTETGGILISPLPGATDLKPGSATRPFFGVKPELVDNEGKVLEGAADGNLCLIDSWPGQARTIYGDHNRFVQTYFSTYKGKYFTGDGCRRDEDGYYWITGRVDDVLNVSGHRLGTAEVESALVSHHLVSEAAVVGYPHGIKGQGIYCYVTLMAGHEGNEELRQTLIKHVRSEIGPIASPDKVQFAPGLPKTRSGKIMRRILRKIAEDDFGALGDTSTLADPGVVDDLIANRQNKASA", "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": "MIGRTPKLSELVLGETAEALSLHCDEALENLSDDDEEDHQDRQVHRERPYAVSVPCKRCRQTISFVCVCDPEAIRTLNRLLSASLSLVCPECCN", "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": "MRSPQSLRNGETPSPSPRPPRFPTPHFHSTVSLQKLKRFNLLILVFRLSTFCFSLASSVFMLTNPTWYHFDAFRYVFAANAIVAIYSLFEMAASVWEISRGNTLFPEILQVWFDFGHDQVFAYLLLSADSAATALAKTLKGGDTCAASNAFCVQSYIAIALGFAGFLFLGLSSLLSGFRVVCFLINGSRFYV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP) family."}
+{"protein": "MDRSFIRNFAIIAHIDHGKSTLSDRLLELTGSLTAREMQAQVLDAMDLERERGITIKAHSVRMMYKAHDDVVYQLNLIDTPGHVDFSYEVSRSLASCEGALLVVDASQGVEAQTLANAYLAINNGLEIIPVINKIDLPSADVERAKEMIEGAVGLDASHALPISAKTGMGVEDILESIVHLVPPPKGNPDHPLQALIFDSWFDSYRGVVILARIKEGTVRKGDKIMLWSNKHQFLVEEMGVLTPKPVAIEQLEAGEVGFIVANIKTVADVGIGDTITHVERPCLEALPGFEELKPMVFAGIYTVDAHEHTLLREALEKLRLNDSSFFFEPESSVALGFGFRCGFLGLLHMEIIQERLEREYDLDLITTAPGVRYKITLTDNSVIEVDNPSKWPDSTLIEKIEEPIITAMILTNEEYVGGILKLVEEKRGRQKNFEYVTGSRVMLTYELPLNEIVLDFYDRLKSVSRGYASLDYHLAGAWESPMVKLDIMVAGESVDALSTIVHKDFAYDRGRALVSKMRELIPRQMFEVPIQAAIGAKIIARETVAAMRKNVLAKCYGGDISRKRKLLEKQKEGKKRMKRIGKVDIPQEAFLAVLKVGENS", "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": "MQGTVYKSTGSWYQVKAEDGKFYECRIKGKFRIQGIKSTNPVAVGDEVSFDLEEGVEEKTGVIKKIKERENYIIRKSVNLSKQTHIIASNIDQVFLLITLNNPPTLTTFIDRFLVTAEAYDITAVLLFNKVDTYSIEELAEVKYLAELYRSAGYECIGISAKNGKNVDKVKDKMIGNTSMISGHSGTGKSTLINAIEPALDLKTSEISRQHSQGQHTTTFAEMFDLSFNARIIDTPGIKGFGVVDMDREEIGDYFPEFFERKQDCKFHNCLHIEEPKCAIKDSLEEGEIAWSRYKSYLQIMEGEEDNYRVDQYQK", "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": "MSQTITQSRLRIDANFKRFVDEEVLPGTGLDAAAFWRNFDEIVHDLAPENRQLLAERDRIQAALDEWHRSNPGPVKDKAAYKSFLRELGYLVPQPERVTVETTGIDSEITSQAGPQLVVPAMNARYALNAANARWGSLYDALYGSDIIPQEGAMVSGYDPQRGEQVIAWVRRFLDESLPLENGSYQDVVAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKNNGLHIELQIDANGRIGKDDPAHINDVIVEAAISTILDCEDSVAAVDAEDKILLYRNLLGLMQGTLQEKMEKNGRQIVRKLNDDRHYTAADGSEISLHGRSLLFIRNVGHLMTIPVIWDSEGNEIPEGILDGVMTGAIALYDLKVQKNSRTGSVYIVKPKMHGPQEVAFANKLFTRIETMLGMAPNTLKMGIMDEERRTSLNLRSCIAQARNRVAFINTGFLDRTGDEMHSVMEAGPMLRKNQMKSTPWIKAYERNNVLSGLFCGLRGKAQIGKGMWAMPDLMADMYSQKGDQLRAGANTAWVPSPTAATLHALHYHQTNVQSVQANIAQTEFNAEFEPLLDDLLTIPVAENANWSAQEIQQELDNNVQGILGYVVRWVEQGIGCSKVPDIHNVALMEDRATLRISSQHIANWLRHGILTKEQVQASLENMAKVVDQQNAGDPAYRPMAGNFANSCAFKAASDLIFLGVKQPNGYTEPLLHAWRLREKESH", "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": "MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISALIYEETRSVLKTFLESVIRDAVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG", "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": "MADNLLSEQLLQRLQDGDNKGVDTLELAAVLSVDHQQVVGAVKSLQCLGEIIEAEQRSSKKWELSSEGEEIAQVGSHEARVFQSLPKEGLLQAELMKLPFAKVGFSKAMSNKWIRLDKAAAGGPCVYRVVETIEDTVKEKLQLILKGRADDVNEKDKNELKKRKLVNEVTVKSYWVTKGSGFSTSITKQETDLTPEMIASGSWREKQFKGYNFNALGVMPECGHLHPLLKVRTQFRQIFLEMGFTEMPTNNFIESSFWNFDALFQPQQHPARDQHDTFFLQDPALATEFPMEYLERVKKVHSEGGYGSQGYKYDWSIHEAQKNILRTHTTAVSARMLYKLAHQKEFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADRGLTLGNLMGVLKEFFHKLGITKLRFKPAYNPYTEPSMEVFSYHEGLKKWVEVGNSGLFRPELLLPMGLPGDVNVLGWGLSLERPTMIRYGIKNIRELVGHKVNLQMVYDSPICRLDAC", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily."}
+{"protein": "MAAPGEALTQSGYIEHHLSNLSLAKLGMVADETSFWNVHIDSLFFSVLTGMLFLWVFRSVAKKATTGVPGKLQCFVEMVVEFVADNVKETFHGRNPLVAPLALTIFCWVILMNLMDLIPIDFLPYSAAHWLGIPYLKVVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFNHPIMIPFNLLLEVISLLAKPLSLGMRLFGNMFAGEVVFILIAAMLPWYLQWVGALPWAIFHILVILIQAFVFMMLTIVYLSMAHEDPDH", "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": "MEFVFLGTGAGVPSKGRNVSAIALQLLEERGQTWLFDCGEATQHQILHTSVRPRRIEKIFITHLHGDHIFGLPGLLGSRSFQGGTTPLTVYGPKGIKQFIEVALSVSTTHVKYPLEIVEITEEGTVFEDNEFHVETKRLSHGIECFGYRIIEKDIQGALLVDKLLEMGVKPGPLFKRLKDGEVVELENGTILNGQDFIGPPQKGRIITILGDTRFCEASRELAQDADVLVHEATFAAEDEQQAYDYFHSTSKQAASIALQANAKRLILTHISSRYQGDTYKELLKEARELFSNTEIATDLKSFPVER", "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": "MTSDIEIARAATLKPMAAIAARLGIPDEAIIPFGRSKAKLSGDFIATLKDRPRGKLILVTAISPTPAGEGKTTTTVGLGDGLSRIGKKVAICLREPSLGPCFGMKGGAAGGGMAQVVPMEDINLHFTGDFHAITSAHNLLAALIDNHVHWGNEQQIDSRRIALRRVLDMNDRSLRNLVTGLGGPAHGTPREGGFDITVASEVMAILCLARDLADLEERLGDIVIAERADRSRVTARDIGAAGAMTVLLKDAFQPNLVQTLEHTPTFIHGGPFANIAHGCNTLVATDTALRLADYVVTEAGFGADLGAEKFFDIKCRKGGLEPSAAVLVATIRALKMNGGVPKDQLGAENVAAVEAGCANLGRHIENLAKFGVPVVVAINHFTADSEAEVAAVEAFCEARGVKAVLATHWAEGGQGTQKLAEAVSELVEGGSSRFAPLYPDDMPLVDKIETVAQSIYRAGSVVFERSARLQLERWQEAGYGHLPVCMAKTQYSFSADPALTGAPEGHELPVREVRLSAGAGFVVAVCGAIMTMPGLPRKPAALDIHLNAEGEVEGLF", "text": "SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family."}
+{"protein": "MIIPNLPFNLPFNLPFNLPFNLPSILPSILVPLVGLLLPAITMVLSHLYIQNDEIL", "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": "MGKFEDDGNSESVPLTRQRSESLASQTSTDSGLSIASESFMKNHKGGNTMPTDGGDGDRYLDVEDGGETGLDEPLISSGTKTGSSSRLRKIVWLLVLLCVGGWVLSFVLFLTQKRPDTAALSSASTVEIHEPGPATGGTSHGKPVTLEQVLSGTWSPKSHAISWIAGPDGEDGLLVEQGEKQDAFLRVKDIRSSEDGVDNLETRVLMKKGYIWFDGEAMLSAKTWPSPDMNRVLVMTDIQSNWRHSYFGKYWILDVATQKAEPLDPGNLSGRVQLAAWSPTSDAVVFVRENNLYLRKLTSLEVTPITKDGDENLFYGVPDWVYEEEVFSGNTGTWWSDDGKFVAFLRTNETAVPEYPIQYFRSRPSGKQPPPGLENYPEVRQIKYPKPGSPNPIVNLQFYDVEKNEVFSFEMPEDFVDDERIIIEVVWASEGKVLIRETNRESDVVKIFVMDTKARTGKLVRSDDIAALDGGWVEPTQSTRVIPADPKNGRPHDGYVDTVIYEGYDHLAYFTPFDNPEPVMLTKGNWEVVNAPSAVDLKKGLVYFVATKEAPTQRHVYSVKLDGSDLRPLTDTSAPGFFDVSFSHGAGYGLLSYKGPAVPWQAVINTQGDEIDFINLIEENVELAKMVEESAIPTEVYSNVTIDGYTLQVLERRPPNFNPEKKYPVLFFLYGGPGSQTVDRKFTIDFQTYVASNLGYIVVTVDGRGTGFIGREARCLVRGNIGHYEAIDQIETAKIWASKSYVDESRMAVWGWSYGGYMTLKVLEQDAGETFQYGMAVAPVTDWRFYDSIYTERYMHTPEHNPSGYANASIDDVMALGHSVRFLIMHGVADDNVHLQNTLVLIDKLDLKNIDNYDMQVFPDSDHSIQFHMAHALVYERLSSWLINAFNGEWHRTANPKPQEST", "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": "MSELLSIALFLASVLIYAWKAGRNTWWFAAILAVLGLFVVLNITLYASDYFTGDGINDAVLYTLTNSLTGAGVSKYILPGAGIVLALAAVFSALGWVLRRRRHHPHHFGYSLLALLLALGSVDASPAFRQISELVKSQSRDGDPDFPAYYKEPSKTIPNPQLNLVYIYGESLERTYFDNDAFPDLTPELGALKNEGLDFSHTMQLPGTDYTIAGMVASQCGIPLFAPFEGNASASVSSFFPQNICLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDHLYGAEELKTVVADPSYRNDWGFYDDTVLDEAWKKFEELSRSGQRFSLFTLTVDTHHPDGFISRTCNRKRYDFDGKPNQSFSAVSCSQENIAEFINKIKASPWFKNTVIVVSSDHLAMNNTAWKYLNKQDRNNLFFVLRGDQPQQDTLAVKRNTMDNGATVLDILGGDNFIGLGRSSLSGQSLSEVFLNSKEKILAMKPDIIRLWNFPKEMKDFTVDRDKDMIAFSGSHFRLPLLLRVSDKRVEPLPESEYSAPLRFQLANFAPRDNFVWVDRCYKMAQLWAPELALSTDWCVSQGQLGGQQSIQHVDKAQWKGKTAFKDTVIDMERYKGNVDTLKIVDNDIRYKADSFIFNVAGAPEEVKQFSGISRPESWGRWSNAQLGDEVKIEYNTPLPKKFDLVITAKAFGANANRPIPVRVGKEEQTLVLENEVTTTTLHFDNPSNASTLVIVPPDPVSTNEGNILGHSPRKLGIGMVEIKVVNAEG", "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": "MEQQKIPQATAKRLPLYYRFIQNLSLSGKQRVSSAELSEAVKVDSATIRRDFSYFGALGKKGYGYNVNYLLSFFRETLDQDDITRVALIGVGNLGTAFLHYNFTKNNNTKIEMAFDVSEEKVGTEIGGIPVYHLDELEERLSNDIQVAILTVPATVAQSVADRLAETNVHGILNFTPARLNVSENIRIHHIDLAVELQTLVYFLKNYPQ", "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": "MTAREVGRIGLRKLLQRIGIVAESMTPLATDPVEVTQLLDARWYDERLRALADELGRDPDSVRAEAAGYLREMAASLDERAVQAWRGFSRWLMRAYDVLVDEDQITQLRKLDRKATLAFAFSHRSYLDGMLLPEAILANRLSPALTFGGANLNFFPMGAWAKRTGAIFIRRQTKDIPVYRFVLRAYAAQLVQNHVNLTWSIEGGRTRTGKLRPPVFGILRYITDAVDEIDGPEVYLVPTSIVYDQLHEVEAMTTEAYGAVKRPEDLRFLVRLARQQGERLGRAYLDFGEPLPLRKRLQEMRADKSGTGSEIERIALDVEHRINRATPVTPTAVVSLALLGADRSLSISEVLATVRPLASYIAARNWAVAGAADLTNRSTIRWTLHQMVASGVVSVYDAGTEAVWGIGEDQHLVAAFYRNTAIHILVDRAVAELALLAAAETTTNGSVSPATVRDEALSLRDLLKFEFLFSGRAQFEKDLANEVLLIGSVVDTSKPAAAADVWRLLESADVLLAHLVLRPFLDAYHIVADRLAAHEDDSFDEEGFLAECLQVGKQWELQRNIASAESRSMELFKTALRLARHRELVDGADATDIAKRRQQFADEIATATRRVNTIAELARRQ", "text": "SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family."}
+{"protein": "MAVSAIFSQDSNSKRLLIAFAITTLFMVTEAIGGWLSGSLALLADTGHMLTDSAALFIALMAVHFSQRKPDPRHTFGYLRLTTLAAFVNAAALLLIVILIVWEAVHRFFSPHEVMGTPMLIIAIAGLLANIFCFWILHKGEEEKNINVRAAALHVLSDLLGSVGAMIAAIVILTTGWTPIDPILSVLVSVLILRNAWRLLKESFHELLEGAPQEIDINKLRKDLCTNIYEVRNIHHVHLWQVGEQRLMTLHAQVIPPLDHDALLQRIQDYLLHHYRISHATVQMEYQHCGTPDCGINQAAPADGHHRHHHHE", "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": "MSSAQNIKKSIMAPVLDNNPIALQVLGVCSALAVTTKLETAFVMTLAVTFVTALSNFSVSLIRNHIPNSVRIIVQMAIIASLVIVVDQVLKAYLYDISKQLSVFVGLIITNCIVMGRAEAFAMKSAPVPSLIDGIGNGLGYGFVLITVGFFRELFGSGKLFGMEVLPLVSNGGWYQPNGLMLLAPSAFFLIGFLIWVIRVFKPEQVEAKE", "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": "MRTLVIEPLSKEAFAPFGDVIETDGSDHFMINNGSTMRFHRLATVETAQPEDQAIISIFRADALDMPLTIRMLERHPLGSQAFIPLLGNPFLIVVAPLGDEPVSGLVRAFVSNGRQGINYHRGVWHHPVLTIEKRDDFLVVDRSGTGNNCDEHFFKEDERLILAPHQ", "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": "MGKLELLQTLTGHAGRVWSAAWHPGGKLFASCGEDKTIRVWNKSDTDRWVAQTVLTDGHTRTIRELAWSCCGHYLASASFDTTVAVWDKKSGEFECNATLEGHDNEVKSVTWSRSGNLLATCSRDKSVWIWEIHHAPDQEDEYECVAVLNGHTQDVKKVCWHPQEDLLASASYDNTIRMYRQDLADSEWEMLEPLESHSSTVWSISFDATGQRLASCSEDTTVKVWQQYGPDNALGIPCPDRGTIWKCVCTLSGYHSRSVYDIDWCKQTGLLATACGDDTVRIFREASDSDRNEPTFELVVTVEAHSQDANKVAWHPTVPGLLLTASDDGEIKLWQYVDAD", "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": "MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINIDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFIDINLNKYSNVTTGKIYSEVLKKERRGEYLGATVQVIPHVTDALKEKIKRAATTTDSDVIITEVGGTVGDIESLPFLEALRQMKADVGSDNVMYIHTTLLPYLKAAGEMKTKPTQHSVKELRGLGIQPNMLVIRTEQPAGQSIKNKLAQFCDVAPEAVIESLDVDHIYQIPLNMQAQNMDQIVCDHLKLETPAADMTEWSAMVDKVMNLEKKVKIALVGKYVELPDAYLSVVEALKHSGYVNDVAIDLKWVNAAEVTEDNIKELVGDADGIIVPGGFGQRGSEGKIEAIRYARENDVPMLGVCLGMQLTCVEFARNVLNLHGANSAELDPKTPFPIIDIMRDQIDIEDMGGTLRLGLYPCKLKSGSRAAAAYNNQEVVQRRHRHRYEFNTKFREQFEAAGFVFSGVSPDNRLMEVVELPEKKFFVAAQYHPELQSRPNHAEELYTAFVTAAVENMK", "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": "MSDQKLSVNEYLKTDSNYLRGTIEEGLDTSLTGAFNDADQQLIKFHGFYQQDDRDLRNERKEQKLEPLYSFMLRARVAGGVCTPKQWLGVDKIASTLTSSNSIRLTTRQTFQYHGIPKRNLKTLIQDLDREALDSIAACGDVNRNVMCNPNPVESKLHQQAYYWAKKLSDNYLPRTKAYAEIWLGDDKVAVSESEEVEPVYGKTYLPRKFKMAVAVPPDNDVDVYTNDLGFIAVAEDGELVGFNMVAGGGMGSTHGEVATFPRLGDDFGFIKAEDCLKFAEAVLKVQRDWGNRSDRKQSRLKYTIVKHGFEAFKAEVEQRAGVKFEPKREVVIGDRGDRYGWIKGVDNNWHLTLFIEGGRIKDLPGQPLQTGLREIALVHKGDFRMTANQNIIIAGVAEEDKAQIEALARSHGLMGKLISPTRGHSIACVALPTCALAMAEAERYFPDFMTKVEALQEKHGFLEQPIVIRMTGCPNGCARPFAAEIGLVGKAPGRYNLYLGASFEGTRLNKLYRENIQEAEILAALDELFARYVKEREAGETFGNFTVRVGVVKAVIDAAKDFHG", "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": "MLKASLLFFVTALAEIIGCFLPYLWLRKGASMWLLLPAAASLALFVWLLTLHPAASGRVYAAYGGVYVATALIWLRVVDDVKLSLFDWVGAAVALVGMLIIVAGWRVN", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0060 family."}
+{"protein": "MLKTRIIPCLDVADGRVVKGVNFVDLRDAGDPVEAARAYDAAGADELCFLDIHATHENRGTMYDLVTRTAEQCFMPLTVGGGVRTHQDVRALLLAGADKVSFNSAAVADPGVVAEAADRFGSQCIVVAIDAKTVAPGRWEIFTHGGRRATGIDAVAFACEMASRGAGEILLTSMDRDGTRAGFNLPLTRAISDAVPIPVIASGGVGTLDHLVEGVTEGGASAVLAASIFHFGEFTIGEAKAHMAAAGIPVRLA", "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": "MQAYFDQLDRVRYEGSKSSNPLAFRHYNPDELVLGKRMEEHLRFAACYWHTFCWNGADMFGVGAFNRPWQQPGEALALAKRKADVAFEFFHKLHVPFYCFHDVDVSPEGASLKEYINNFAQMVDVLAGKQEESGVKLLWGTANCFTNPRYGAGAATNPDPEVFSWAATQVVTAMEATHKLGGENYVLWGGREGYETLLNTDLRQEREQLGRFMQMVVEHKHKIGFQGTLLIEPKPQEPTKHQYDYDAATVYGFLKQFGLEKEIKLNIEANHATLAGHSFHHEIATAIALGLFGSVDANRGDAQLGWDTDQFPNSVEENALVMYEILKAGGFTTGGLNFDAKVRRQSTDKYDLFYGHIGAMDTMALALKIAACMIEDGELDKRIAQRYSGWNSELGQQILKGQMSLADLAKYAQEHNLSPVHQSGRQEQLENLVNHYLFDK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the xylose isomerase family."}
+{"protein": "MKLIVSVMPRSLEEAQALSATRYLDADIIEWRADYLPKEAILQVAPAIFEKFAGRELVFTLRTRSEGGEIDLSPEEYIHLIKEVAQFYQPDYIDFEYYSYKDVFEEMLDFPNLVLSYHNFQETPENMMEILSELTILNPKLVKVAVMAHTEQDVLDLMNYTRGFKTLNPEQEYVTISMGKVGKVSRITADVTGSSWSFASLDEVSAPGQISLASMKKIREILDEA", "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": "MSTARFIKCVTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGSTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLLSRASYENISKKWIPELRHYAPTVPIVLVGTKLDLREDRQYLIDHPGATPITTAQGEELKKAIGAAVYLECSSKTQQNVKAVFDAAIKVVLQPPKPKKKRKKTRPCVFL", "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": "MKSLLPLAILAALAVAALCYESHESMESYEVSPFTTRRNANTFISPQQRWHAKAQERVRELNKPAQEINREACDDYKLCERYALIYGYNAAYNRYFRQRRGAK", "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": "MKMEQALNITSEIGKLQTVLVKRPGSELENITPEYLESLLFDDIPYLKMMQKEHDFFAKTMKDSNIEVLYLEKLAAEALREANNKESFLTKMIKESNQMDESALYVRDYLMSFDEEEMIRKLMSGLKKSEIPERKKKHLNEMMDEQYPFFLDPLPNLYFTRDPAAVIGNGVTINRMFQPARRRESMFIELILKHHPRFSNQEIPVWSGRGEPFSLEGGDELVLNEETVLVGVSERTDARAVERLAESLFSRSPKIKRVLAVEIPETRSFMHLDTVFTMVNFAQFTIHPAIQNQQGELNIYILEKSENGLEITPRRDFQRVIAEVLDEPEIDFIPCGGEDVIVSAREQWNDGANTLAIAPGEVITYDRNQVSNDLLRSAGIKVHEVISSELSRGRGGPRCMTMPLVRENLK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the arginine deiminase family."}
+{"protein": "MAPVRDPNTLSNYNEWRTKHTTADFKVDFTAKCLRGSVVLELESQTDKASKEIILDSSYVDVSAITLNSTPSQWEVRDRTGPSGSPVRVAVPNGAGKGEVVKLEIELATTDKCTALQWLTPAQTSNKKAPFMFSQCQAIHARSIFPCQDTPDVKSTYDFIIRSPHVVVASGVPVPGEPESVGEDKVYKFHQKVPIPSYLFAVASGDIASAKIGRCSSVATGPNELKASQWELEDDMDKFLDAAEKIVFPYQWGEYNVLVLPPSFPYGGMENPIFTFATPTIISGDRQNIDVIAHELAHSWSGNLVTSCSWEHFWLNEGWTVYLERRILASIHKNDSYFDFSAIIGWKHLEEAIEEFGKDHEYTKLSIKHDGIDPDDAFSSVPYEKGFHFIWSLDRLVGRENFDKFIPHYFSKWQNKSLDSFEFKDTFLEFFSAPEYSKLKDKISQIDWEGRFFNPGLPPKPEFDTTLVDGCFQLANKWKSKDFSPSPSDTSSWTGNQLLVFLNVVQDFEEPLTAEQSQNMGKIYALADSKNVELKAAYYQIAMKAKDTTSYPGVAELLGNVGRMKFVRTLFRTLNKVDRDLAVKTFQKNRDFYHPICRQLVEKDLGLGESK", "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": "MSRAPLPLAAHERLIFALDVPSHDEAIAWVDRLGDSVAFYKIGMELLASGEYFHVLDALAKRDKRVFVDLKFFDIPATVAGTIRRLAQWPVSYCTVHGWHAGMLQAAADANHGAMRLLAVTVLTSMGRPDLAAMGIDREPVDVVVERALAAEAAGIDGVIASGQEAGPIRRATGPAFSIVCPGIRPGGPVADDQQRIVGVAQAFTDGADAIVVGRPIRLAADPAAAAAAIQAEILAAVGQDRS", "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": "MKKTKRIFTALSHLFSPKWWKKNWQRVVLLFFFAVFALLLIFRFVPIPFSAYMVQQKIANLLQGDFRYQIQYDWVSLENISPNIQLAVISSEDQRFPEHLGFDFEAIQRAIRYNEKSNKGIRGASTISQQTAKNLMLWHGQNWLRKGLEVPATMLLELTWSKKRILEVYLNIAEFGNGIFGVEAASRYYFKKSAKNLSQNEAALLVAVLPNPIIYKVNKPSLLVRKKTSLDFETNGKFRY", "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": "MKGSVRALCAFLGVGALGSALCVSCTTVCPHAGKAKAEKVECALKGGIFRGTLPAADCPGIDTTVTFNADGTAQKVELALEKKSAPSPLTYRGTWMVREDGIVELSLVSSEQSKAPHEKELYELIDSNSVRYMGAPGAGKPSKEMAPFYVLKKTKK", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
+{"protein": "MIGALARKIFGSANDRRVKGYQARVDAINAMEPEIAALSDEALKARTAEFKQQLASGKTLDDILVPAFATVREAAKRTLGQRHFDVQLIGGMVLHEGDIAEMKTGEGKTLVATLAVYLNALTGRGVHVVTVNDYLAKRDAEWMSQVYSFLGLTTGIIIHGLDDPERQAAYACDITYGTNNEFGFDYLRDNMKYRLEDMVQRDHVFAIVDEVDSILIDEARTPLIISGPLDDRSEFYNTIDTFIPKLEPADYEIDEKQRTVTLTEGGMEKLEQMLREAGLLKGESLYDIENVSVVHHVNQALRAHRLFTRDKDYIVRDGEVVIIDEFTGRMMPGRRYSEGLHQALEAKEHQPVQPENQTLASITFQNYFRMYEKLGGMTGTAATEADEFFDIYKLEVLEIPTNLPIARLDEDDEVYRSSREKYAAILAEIERANGRMQPVLVGTASIEKSEVLADFLKEHGYKQIDFANPKSMAKLYDAARAGKPSKLFAVLNARFHEQEAYIVAEAGVPGAITIATNMAGRGTDIKLGGSLEMRAAAATAGIEDEAEKQKIVEGIKADIEKFKEMVLAAEETVELEPGKPGGKTIKKPGGLYIIGSERHESRRIDNQLRGRAGRQGDPGRTKFYLSLDDDLMRIFGSDRLEGMLQRLGLKEGEAIIHPWINKALEKAQQKVEARNFDIRKNLLKYDDVQNDQRKVIFEQRIDLMRDQNVSETVTDMRHTLIEGLVAKHIPEHAYPEQWDVSGLREELQRVIGLDLPVEDWAKEEGIADEEMLSRLQQRVDEHMAAKSAQWGPEVMRYVEKTILLQTLDHLWREHLIMLDHLRQVIGLRGYGQRDPLQEYKSEAFELFESLISHMREAVTAQLMRVEIVPPDEQPPMPAMEAHKLDPNTGEDQVAQAQSGLAPVAPAKRDPANPATWGKVGRNEDCPCGSGRKFKHCHGRYA", "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": "MKPLSSPLQQYWQTVVERLPEPLAEKSLSAQAKSVLTFSDFVQDSVIAHPEWLTELESQSPQADEWQHYAAWLQEALSNVSDEAGLMRELRLFRRRIMVRIAWAQTLALVTEESILQQLSHLAETLIVAARDWLYDACCREWGTPCNAQGEAQPLLILGMGKLGGGELNFSSDIDLIFAWPEHGCTQGGRRELDNAQFFTRMGQRLIKVLDQPTQDGFVYRVDMRLRPFGESGPLVLSFAALEDYYQEQGRDWERYAMVKARIMGDSEGVYANELRAMLRPFVFRRYIDFSVIQSLRNMKGMIAREVRRRGLTDNIKLGAGGIREIEFIVQVFQLIRGGREPSLQSRSLLPTLSAIAALHLLSENDAEQLRVAYLFLRRLENLLQSINDEQTQTLPSDELNRARLAWAMDFADWPQLTGALTAHMTNVRRVFNELIGDDESETQEESLSEQWRELWQDALQEDDTTPVLAHLSEDDRKQVLTLIADFRKELDKRTIGPRGRQVLDHLMPHLLSDVCAREDAAVTLSRITALLVGIVTRTTYLELLSEFRAALKHLISLCAASPMIASQLARYPLLLDELLDPNTLYQPTATDAYRDELRQYLLRVPEDDEEQQLEALRQFKQAQLLRIAAADIAGTLPVMKVSDHLTWLAEAMIDAVVQQAWVQMVARYGKPNHLNDREGRGFAVVGYGKLGGWELGYSSDLDLIFLHDCPMDAMTDGEREIDGRQFYLRLAQRIMHLFSTRTSSGILYEVDARLRPSGAAGMLVTSAEAFADYQKNEAWTWEHQALVRARVVYGDPQLTAHFDAVRREIMTLPREGKTLQTEVREMREKMRAHLGNKHRNRFDIKADEGGITDIEFITQYLVLRYAHEKPKLTRWSDNVRILELLAQNDIMEEQEAMALTRAYTTLRDELHHLALQELPGHVPEDCFTAERELVRASWQKWLVEE", "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": "MSAGLETFALKEEDAIKLLACQTHVGAANCDFQMEQYVWKRRADGIHIIHLRKTWEKLLLAARAIAAIDNPGDVCVVSARPYAQRALLKFAAHTGSTPIFGRFTPGCLTNQIQKQFKEPRLLIVSDPRVDHQAVTEASYVGVPVISFCNTDSPLKFIDIAIPCNNKGVQSIGLMWWLLAREVLLIKGKMTRQTGFVLDDKEIMPDLYFYRNPEEQEKEELAEPREVKEPWPGVPPPEVAKIDEVVRSIGMYQTIGGVEPAKKLDFSMVEPVSDWAQETERAVQLDAAQQQEWGASTQNSNW", "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": "MLEGIIDINHIFDEEGIKTLKRFGWDGSVAVQNHNEYSEEIINSTVEYGEKHDFKVFSGVKISTKNQNEMEKAIKKYRNKVDILLVEGGDIKINRRVLEMNDVDILSTPELNRMDNGLDHILARLGSTNRVAIELNFGNLLKSRNYDRSKILWAFQRNLKLAKKYDTPVVISSGASDIYGIKAPGDLRGFLNTITDPLYSKKIMETTSKIIDYRLYLKKDTVLTLGIEIVEE", "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": "MTHKQRAIFEPALVRTALLDAVKKLDPRVQWRNPVMFVVYLGSWLTTLIWLDILSGHTTGSAMFTGSIALWLWFTVLFANMAEALAEGRSKAQAASLRGVKKTSWAKKLSEARVDAPQEKVSADSLRKGDLVLIEAGDTVPCDGEVLEGGASVDESAITGESAPVIRESGGDFSSVTGGTRVLSDWLVVECRVNPGETFLDRMIAMVEGAKRRKTPNEVALTILLVALTIVFLLATATLYPFSVFSVEASQAGSPVTITVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQASEFLPAPGVTEQQLADAAQLSSLADETPEGRSIVVLAKQRFNLRERDLHSLNATFIPFSAQTRMSGVNVQERMIRKGAVDAIRRHVESNQGHFPPAVDDLVASVARTGGTPLVVAEGSRVLGVVALKDIVKGGIKERFAELRKMGIKTVMITGDNRLTAAAIAAEAGVDDFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAKEAGNMVDLDSNPTKLIEVVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAATYPQLNALNIMQLHSPSSAILSAVIFNALVIVFLIPLALKGVSYKAMSAAALLRRNLWIYGLGGLLVPFVGIKLIDLLLTALNMG", "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": "MSSFQLPKLSYDYDELEPYIDSNTLSIHHGKHHATYVNNLNAALENYSELHNKSLEELLCNLETLPKEIVTAVRNNGGGHYCHSLFWEVMSPRGGGEPNGDVAKVIDYYFNTFDNLKDQLSKAAISRFGSGYGWLVLDGEELSVMSTPNQDTPLQEGKIPLLVIDVWEHAYYLKYQNRRPEFVTNWWHTVNWDRVNEKYLQAIQSQKH", "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": "MNITPCSIKTLKGLYDISGVEVGQHFYWQIGGFQIHAQVLITSWFVITILLGSVIIAVRNPQTIPTDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPWKIIELPHGELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEKYIKPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH", "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": "MDIEKLTLKVQQTINDSQKIAVKYNHQQLEPFHLFAALVFQEDGLIPNILGKMNINIKVLRDEIKRELNEMPKVLGDGAQNSGVYATRSFEEIFIRAESIAKDFKDSYISVEHIMLSLMQGRSTSIKKILDKFNIRKDKFLNVLQQVRGNQRVDTQDPEGTYEALVKYGRNLIEDAKKHKLDPVIGRDEEIRRIVRILSRRTKNNPVLIGDPGVGKTAIIEGLAERIVRGDVPEGLKNKIIFSLDMGALIAGAKFRGEFEERLKAVLKEVENSQGKIILFIDEIHNIVGAGKTEGSMDAGNLIKPMLARGELNCIGATTFDEYRKYIEKDKALERRFQPVIIDEPTVEDTISIIRGLKERFEIHHGIRIHDSAIVAAAKLSQRYITDRYLPDKAIDLIDEAGAMIRTEIDSLPTELDSIKRKIFQMEIEKEALAKEKDSRSKERLEDLEKELSNLKEKDKEMTAKYEKEKEQIINMRNLKQKLDEVKGQLEKAEREYDLNKVAELKYGIIPGIKSQIEEKEILIKENSQGNMLKEEVTENEISKIISHWTGIPVTKLIEGEKDKLLRLEDELKSRVIGQDEAVEAVSNAVLRARAGMKDPQKPIGSFIFLGPTGVGKTELAKTLCKNLFDSEENIIRIDMSEYMEKYSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSVILFDEIEKAHDDVFNIFLQILDDGRLTDNKGKTVDFKNCIIIMTSNIGSSYLLENKKEDGIDETVKNKVSNALKDRFKPEFLNRLDDIIMFKPLTNREITKIIDIFLQDIENRLKDRNITLIVTENAKELMAKEGYDAIYGARPLKRYIENILETKIAKQIIKGDIYEGCKIGVDIKGEEIIIGKI", "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": "MYTKILGTGSYLPVQVRSNADLEKMVDTSDEWIVTRTGIRERRIAGLDETVATMGFQAAEKALEMAGIDKDDIGLIIVATTSSSHAFPSSACQVQRMLGIKDAASFDLAAACAGFTYALSVADQYVKSGAVKHAIVIGSDVLSRALDPEDRGTIILFGDGAGAVVLGASEQPGIMSTHLHADGRYGELLALPYPDRQQDQPAYVTMAGNEVFKVAVTELAHIVDETLQANNLDRTALDWLVPHQANLRIISATAKKLGMGMDKVVITLDRHGNTSAASVPSAFDEAVRDGRIQRGQLVLLEAFGGGFTWGSALVRF", "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": "MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIVPEIEAIATDMLIQLEEEGLNVVPCARATKLTMNREGIRRLAAEELQLPTSTYRFSDSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDGVHFCAPVGHRQEDGDYRESWQPQQMSPLALERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASAVILPQLTSQNVTFDNVQNAVGADLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQG", "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": "MERIKELRDLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRIMEMIPERNEQGQTLWSKTNDAGSDRVMVSPLAVTWWNRNGPTTSTVHYPKVYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKIAPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVKNDDVDQSLIIAARNIVRRATVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSVKKEEEVLTGNLQTLKIRVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQSWGIEPIDNVMGMIGILPDMTPSTEMSLRGVRVSKMGVDEYSSTERVVVSIDRFLRVRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQDPTMLYNKMEFEPFQSLVPKAARGQYSGFVRTLFQQMRDVLGTFDTVQIIKLLPFAAAPPEQSRMQFSSLTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGALREDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN", "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": "MTQQSKETTDFGFQTVDKDEKQTMVAKVFHSVASKYDLMNDLMSFGIHRVWKRYTIEASGVRRNQRVLDLAGGTGDLTAKFSRLVGENGEVVLADINDSMLKMGREKLRDHGIVGNVSYVQANAEELPFPDDYFDCITISFGLRNVTDKAKALRSMFRVLKPGGRLLVLEFSKPVLDPLSKIYDAYSFHILPRIGQVIVNDADSYRYLTESIRMHPDQETLKGMMEEAGFDQVSYTNMTGGIVALHKGFKF", "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": "MERSFMKNNSSVNMTSWMGRVDHEDGELGLRWHQKVKVTNSTNQDGIMLLGFACDEGVIRNKGRKGAYAAPQVIRRALANLAWHHQSDVYDGGDIQCNDGDLELAQKQLGIKIKSALANRHQVIVLGGGHEVAWGSFQGIARYLQSRAVLTSPTPPPRIGIINFDAHFDLRNLSQSPSSSASQSSKQYGNSGTPFHQISEFCHVQHWPFHYACLGLNKGSNTQALYHKAKQLGVLHFDDIEMNLLNLPQIKQALSEFIEQNDFLYLTIDIDVFPASCAPGVSAPAVRGVSLDIIESLLPDILKAKNQHGESKLLLADLAEFNPTFDIDNQTARLVARLVWTIAHGMKSNM", "text": "FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L- glutamate and formamide. SIMILARITY: Belongs to the arginase family."}
+{"protein": "MLKRSKFETTQSQIMHRAEDLISAASNRYRITVQVANRAKRRRYEEFESAEDSMMKPVLRAIIEMSDELTQPEIIGEI", "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": "MPNKVYDVTIIGGGPIGLFSAFYSGLRSMKTKIIDAEPAVGGKVRYFFPEKIIRDIGGIPAITGENLVANLKQQAETFHPTIVCSERVVDVTKLSDGTFQLTSHNGSIHFSKTIVIATGSGTFEVNKLEALHAEDFPFAIHYDVKNIEQFRDKVVVVSGGGNSAIDWAQTLEPIAKQVHLIYRGEDFKAHEESVRELQNSRVEIHIHHEINELIGTNNQLTKINVCCNKTQATKTIQTDALFINHGVKVDLGTMAEWGFEQADFGIVVDDEMKTTVPGIFACGDSATYPRKIRIIAAGLHEGPIAINSAKKYLEPTAADEAMISTHHESFIG", "text": "SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family."}
+{"protein": "MLTKQTTGQAWKQIKGSITDVKGFTTAGAHCGLKRKRLDIGAIFCDVPANAAGVFTLNQIQAAPLKVTKESLAHSNGKLQAVLVNSGNANACTGASGLVDAYEMRALAAAKFAVPEEMVAVTSTGVIGEKMPMEKVRSGIEDLVLSKESTPFAEAILTTDTGTKEVCVEVVIDQKTVRIAGVAKGSGMIHPNMATMLGFITTDANIETAALKRALAKATDETFNRITVDGDTSTNDMVLVLASGLADNQPLDETHPDWANFYGALSACAESLAKKIAKDGEGATKLIEVQVAGAVSDEEAGKVAKAIVGSDLVKTAAYGKDGNWGRIICAIGYSGCTLDPDTIDIAIGPYETLVQSEPVVVDDAAISKYMEAETIVIKADLHQGQGVGKAWGCDLTYDYVRINAGYRT", "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": "FFPILGKLLSGIL", "text": "FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily."}
+{"protein": "MTLWINGDWITGQGERRRKTNPVSAEILWQGNDANAAQVAEACQAARAAFPRWARQPFTARQAIVQKFAALLEAHKADLTEVIARETGKPRWEAATEVTAMINKIAISIKAYHARTGEQKSELVDGAATLRHRPHGVLAVFGPYNFPGHLPNGHIVSALLAGNTLIFKPSELTPWTGETVIKLWERAGLPAGVLNLVQGGRETGQALSSLDDLDGLLFTGSASTGYQLHRQLSGQPEKILALEMGGNNPLIIEDVANIDAAVHLTLQSAFITAGQRCTCARRLLVKQGAQVDAFLARLVDVAGRLQPGRWDDDPQSFIGGLISAQAAQHVMEAWRQREALGGRTLLASRKVKEGTSLLTPGIIELTGVADVPDEEVFGPLLNVWRYAHFDEAIRLANNTRFGLSCGLVSTDRAQFEQLLLEARAGIVNWNKPLTGAASTAPFGGVGASGNHRPSAWYAADYCAWPMASLESPELTLPATLSPGLDFSRREAV", "text": "FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD subfamily."}
+{"protein": "VQPSLGKESAAMKFERQHMDSTVATSSSPTYCNQMMKRRNMTQGQCKPVNTFVHESLADVHAVCSQENVKCKNGKSNCYKSHSALHITDCRLKGNAKYPNCDYQTSQHQKHIIVACEGNPFVPVHFDATV", "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": "MTKLLAYFPSPPQGVWHLGPVPIRAYALFIIAGIVAALLIGDRRWEARGGERGVIYDIALWTVPFGLVGGRLYHLATDWRTYWGPGGAGFGAAVRIWDGGLGIWGAVALGAVGAWIGCRRHGIPLPAFADALAPGIILAQAIGRLGNYFNQELYGRETTLPWGLEIFYRRDPSGYIDPHSLDGVSTGQVALVVQPTFLYELLWNLLIFVALLYADRRLTLGHGRLFALYVAGYCVGRFCVELLRDDTATHIAGIRINSFTSTFVFIGAVVYLMAAPKGREDPESLRGNQYVEEEPAEPEPATVAATTEAATEGVAAPADGAEAAGADATAQRPEESAEPDVEKPESEETEAEAAEEPESEETEAAEEPGEPEAEEPEEPEAEEPEEPETEEPEADSDEEPEEESGEAPEQPVAEEPEPAPQQPETKRRWGARLRDRLSGR", "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": "MSTRTASAGDIKEGSYIMIDNMPCRVVEVEKSKTGKHGSAKARIVGIGVIDGVKRTIVVPTDAAVEVPVIEKFTAQVISISGDSVQLMDLRNYQTFEIPSSYIEDEAKGKLEPGVQVEVWDVAGYKKIMRTR", "text": "FUNCTION: Functions by promoting the formation of the first peptide bond. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-5A family."}
+{"protein": "MIYKVFYQETKERNPRREQTKTLYVTIDAANELEGRIAARKLVEENTAYNIEFIELLSDKHLEYEKETGVFELTEF", "text": "FUNCTION: A non-essential component of RNA polymerase (RNAP). SIMILARITY: Belongs to the RNA polymerase subunit epsilon family."}
+{"protein": "MDKKEIFQSVTSMEEQLSHLYRQLVQLKEHVVQLLEENHHLQIENDHLRRRLEQVTSELAEEKQKEKDHKHGHERKLVDIGEGYDNLARLYQEGFHICHVHYGSVRKEGDCLFCLSFLNKK", "text": "FUNCTION: Involved in initiation control of chromosome replication. SIMILARITY: Belongs to the YabA family."}
+{"protein": "MEINPYLMFLNNDVTSLISTTYPYTGPPPMSHGSSTKYTLETIKRTYDYSRTSVEKTSKVFNIPRRKFCNCLEDKDELVKPTGNVDISSLLGLAEMMEKRMGEGFFKHCVMEAETEILKMHFSRLTEGRQTYDWTSERNMPAATALQLTVDAIKETEGPFKGTTMLEYCNKMIEMLDWKEVKFRKVKTMVRREKDKRSGKEIKTKVPVMGIDSIKHDEFLIRALTINTMAKDGERGKLQRRAIATPGMIVRPFSKIVETVAQKICEKLKESGLPVGGNEKKAKLKTTVTSLNARMNSDQFAVNITGDNSKWNECQQPEAYLALLAYITKDSSDLMKDLCSVAPVLFCNKFVKLGQGIRLSNKRKTKEVIIKAEKMGKYKNLMREEYKNLFEPLEKYIQKDVCFLPGGMLMGMFNMLSTVLGVSTLCYMDEELKAKGCFWTGLQSSDDFVLFAVASNWSNIHWTIRRFNAVCKLIGINMSLEKSYGSLPELFEFTSMFFDGEFVSNLAMELPAFTTAGVNEGVDFTAAMSIIKTNMINNSLSPSTALMALRICLQEFRATYRVHPWDSRVKGGRMKIINEFIKTIENKDGLLIADGGKLMNNISTLHIPEEVLKFEKMDEQYRNRVFNPKNPFTNFDKTIDIFRAHGPIRVEENEAVVSTHSFRTRANRTLLNTDMRAMMAEEKRYQMVCDMFKSVFESADINPPIGAMSIGEAIEEKLLERAKMKRDIGAIEDSEYEEIKDIIRDAKKARIESR", "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": "MSYHKLTRDQIAQRVAQDIPEGSYVNLGIGLPTKIASYLPADKDVFLHSENGLLAFGPPPAAGEEDPELINAGKEYVTMLEGGCFFHHGDSFAMMRGGHLDICVLGAFQIAANGDLANWHTGAPDAIPSVGGAMDLAVGAKKVFVTTDHVTKKGEPKIVAELTYPATGQKCVDRIYTDLCIIDVVPEGLKVIEKVEGLSFEELQRLTGATLIDATQG", "text": "SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit B family."}
+{"protein": "MNNILVINGPNLNLLGKREPDMYGNITLENINQKIKLHFKNEDLKIDFFQSNEEGKIIDKIIESQKKYNAIVINPAAYSHYSIAILDAMRSINIPAVEVHLSNIYKREEYRKKSVTAEASLGVISGFGYYGYIMAIEFILNNLVREK", "text": "FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. SIMILARITY: Belongs to the type-II 3-dehydroquinase family."}
+{"protein": "MAATATSKITLTSSDGVEITIERQVAERSILIKNMLEDLGDSGEAIPIPNVNESVLKKVIEWCKHHKGDPPSTGDDDVDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEDR", "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": "MQQHYDYIIVGAGSAGCVLADRLSESGDHSVLLLEAGGSDKSIFIQMPTALSYPMNSEKYAWQFETDAEADLDGRRLHCPRGKVLGGSSSINGMVYVRGHACDFDEWEEQGAKGWNYQACLPYFRRAENWIDGEDEYRGGDGPLSTCAGNKMTLNPLYRAFIDAGKEAGYPETSDYNGYQQEGFGPMHMTVKNGVRASTSNAYLSRAKKRSNFKLIKGVVVQRILLEEKRAVGVEFELAGELRTCFAKNEVISSAGSIGSVQLLQLSGIGPKTVLEKAGVTPVHHLPGVGQNLQDHLEVYFQYHCQKPITLNGKLDWFSKGLIGAEWILTRKGLGATNHFESCAFIRSRAGLKWPNIQYHFLPAAMRYDGQAAFDGHGFQVHVGPNKPESRGRVEIVSANPSDKPKIQFNYLSTERDRQDWRDCIRLTREILAQPAMDEFRGEEIQPGINVATDAEIDQWVKENVESAYHPSCSCKMGADDDPMAVLDEECRVRGITNLRVVDSSVFPTIPNGNLNAPTIMVAERAADLILHKQPLPPQRSKVWLAPSWETQQRTGEPMR", "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": "MPIIIDKDLPARKVLQEENIFVMTKERAETQDIRALKIAILNLMPTKQETEAQLLRLIGNTPLQLDVHLLHMESHLSRNVAQEHLTSFYKTFRDIENEKFDGLIITGAPVETLSFEEVDYWEELKRIMEYSKTNVTSTLHICWGAQAGLYYHYGVPKYPLKEKMFGVFEHEVREQHVKLLQGFDELFFAPHSRHTEVRENDIRGVKELTLLANSEEAGVHLVIGPEGRQVFALGHSEYSCDTLKQEYERDRQKGLNIDVPKNYFKHNNPNEKPLVRWRSHGNLLFSNWLNYYVYQETPYVL", "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": "MENIQKLIARYPLVEDLVALKETTWFNPGTTSLAQGLPYVGLTEQDVNAAHDRLARFAPYLAKAFPQTAAAGGMIESDVVAIPAMQKRLEKEYGQTIDGEMLLKKDSHLAISGSIKARGGIYEVLTHAEKLALEAGLLTTDDDYSVLLSPEFKQFFSQHSIAVGSTGNLGLSIGIMSACIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEDDYGVAVEQGRKAAQSDPNCFFIDDENSRTLFLGYAVAGQRLKAQFAQQGRVVDASHPLFVYLPCGVGGGPGGVAFGLKLAFGDNVHCFFAEPTHSPCMLLGVYTGLHDAISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGLYTLDDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRICAATEYQQRHGFSQTQLGNATHLVWATGGGMVPEDEMEQYLAKGR", "text": "SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA subfamily."}
+{"protein": "MNKIALYCRPGFEKECAAEITDKAGQKEIYGFARVKDNSGYVLFECYQHEDADRLIREIPFRELIFARQMLVVGELLRDLPPEDRVSPIVGMLHGVIERAGDLRVEVPDTNESKELLKFCRKFTVPLRNAMRQEKILQIRENTKRPVIHVFFIAPGCCYVGYSYSHNNSPFYMGIPRLKFPSDAPSRSTLKLEEAFHVFIPYDEWEERLASGLYAVDLGACPGGWTYQLVKRSMMVHAVDNGPMSQSLMDTGQVRHHKVDGFKFEPLVKNIYWLVCDMVEKPAKVTQLMADWLVNGWCREAIFNLKLPMKKRYEEVAHNLQKMNLQLKENGINAQIQAKHLYHDREEITVHVRRIWSAYAASRNND", "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": "MIPAYLSNPFAAVFGGGKPIDGGRTYKDGRRILGDGKTYRGLFSGIFCGFLAGCVEVWLSFRGFEILGIEMPGFGPDYTSSLIVVLALASGALFGDMFKSFFKRRMGLKRGASLPLVDQLDFVVGAWVFTYLAAPEWFVSNFTPGIMLTVIIITPLLHLTTNIIGYFIGVKKEPW", "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": "MKTLLLTLVVVTIMCLDLGYTTKCYKTGERIISETCPPGQDLCYMKTWCDVFCGSRGRVVELGCTATCPTVKPHEQITCCSTDNCNPHPKMKQR", "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": "MNADTAPFWRRKTLDQLDSKEWESLCDGCGLCCLQKLEDEEDNSVYYTSIACKLLDLQTCQCSDYPNRFKHVPDCIQLTPGKADQFKWLPPTCGYRLVSEGQDLPAWHHLVSGDRTQVHEQRISRSGRMLSENDVDEDDWEDHLIFRAG", "text": "SIMILARITY: Belongs to the UPF0260 family."}
+{"protein": "MVQEQDTPWILSTGHINTQKGEDGQQTPKLEHRNSTRLMGHCQKTMNQVVMPKQIVYWKQWLSLRNPILVSLKTRVLKRWRLFSKHEWTS", "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": "WIMGHMVNNIKQIDEFVNLGSNAIETDVSFDKKANPEYTYHGTPCDCGRDCLRWEYFNDFVKALRTATTPGNSKYDKLFLVVFDLKTSSLYDYRASEAGTKLAKNLLQHYWNNGNNGGRAYIILSIPNLKHYKLITGFQQTLKDEGHAELLDKVGYDFSGNDDIGDVQKTYEKAGVTGHVWQSDGITNCLLRGFTRINAAVANRDSANGIINKVYYWTVDKRQATRDTLDANVDGIMTNYPDITVEILNEDAYKTKFRIATYEDNPWETFKE", "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": "MLDAMREKPPLVHCITNYVAMNIAANVLLASGASPAMVHAPEEAGEFAGIASALTVNIGTLSTQWIDGMQAAAKAAASAGKPWVLDPVAHYATTFRRQAVADLLALKPTIIRGNASEIIALAGGESRGQGVDSRDPVEQAEDSARRLAERQQAIVAVTGAVDFVTDGERAVRIKGGSVLMPEVTALGCSLTCLIGAFAATAPEDLFGATVAALATFAVAGEDAALGAAGPGSFAWRFLDALAALDGEALDARARVSLA", "text": "FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ). SIMILARITY: Belongs to the Thz kinase family."}
+{"protein": "MAKATSSLVVPIIFLVIFALVEQNTGCFDYDVYQPCDHCRERCLKYYPVTRKAICRKNHCVCIGPCPDDKAIPDVKLFKNVKEQILS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family."}
+{"protein": "MSRYDLVERLNGTFRQIEQHLAALSDNLQQHSLLIASVFSLPQVTKEAEHAPLDTIEVTQHLGKEAEALALRHYRHLFIQQQSENRSSKAAVRLPGVLCYQVDNATQLDLENQVQRINQLKTTFEQMVTVESGLPSAARFEWVHRHLPGLITLNAYRTLTLINNPATIRFGWANKHIIKNLSRDEVLSQLKKSLASPRSVPPWTREQWQFKLEREYQDIAALPQQAKLKIKRPVKVQPIARIWYKGQQKQVQHACPSPIIALINTDNGAGVPDIGGLENYDADNIQHRFKPQAQPLRLIIPRLHLYVAD", "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": "MEEKITYKNAGVDTEKGREFIQKIKRNVESTHGPRVIGGLGGFAGAYDVSVLKKYKHPILLSGTDGVGTKIELARLLKIYNTIGIDLVAMCVNDILVCGGEPLFFLDYIACGKLDPEKMDQIVSGIVQGCKMSNASLLGGETAEHPGTMKEDEFDLAGFVVGAVEKDSMIDGSTIRSGDKILGLESSGPHSNGFSLIRKLLLKEGKYLPTDPQQVKFLKDYALKPTRIYVSSILKLLQQVSVKGMVHITGGGYQENVPRILPQGTQSKFFKEKIPSGYFFEKIKKDHKIEELELFATFNMGIGYMVIVSEENAELAKKIMESSGEVVHEIGEIVSGNKEEVQFV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AIR synthase family."}
+{"protein": "MSFNLRGAVLANVSGNSQDQLQETIVDAIQSGEEKMLPGLGVLFEVIWKNADENEKHEMLETLEQGLKK", "text": "SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspI family."}
+{"protein": "MSVLVKEVIEKLRLDIVYGEPELLEKEINTADITRPGLEMTGYFDYYTPERIQLLGMKEWSYLISMPSNSRYEVLKKMFLPETPAVIVARGLVVPEEMLKAARECKIAILTSRAATSRLSGKLSSYLDSRLAERTSVHGVLMDIYGMGVLIQGDSGIGKSETGLELVKRGHRLVADDRVDIFAKDEITLWGEPAEILKHLIEIRGVGIIDVMSLYGASAVKDSSQVQLAVYLENYDTHKTFDRLGNNAEELEVSGVAIPRIRIPVKTGRNISVVIEAAAMNYRAKEMGFDATRLFDERLTSLIARNEVQNA", "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": "MAMYPRELKWGVAHIYSSFNNTHVHITDLTGAETVARVTGGMVVKADREKPSPYAAMIAASRAAQKAMERGIAAIHIKVRAPGGHGPKTPGPGAQAAIRALARAGFIIGRIEDVTPIPHDTTRRPGGRRGRRV", "text": "FUNCTION: Located on the platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
+{"protein": "MPAFSLMIQGTTSDAGKSTLVTALCRLFYRRGISVAPFKPQNMALNSAVTKDGNEIGRAQAVQAYAAGLEPQVDMNPILLKPNTDTGAQVIIQGKAVGNMNAVGYHEYKSIAKVAALDSYQRLANQYQAVLIEGAGSPAEINLRARDIANMGFAESIDCPVIIIADIDKGGVFAHLVGTLDLLSPSEQDRVIGFVINRFRGDISLLQSGLDWLEERTGKPVLGVLPFLKGFHLESEDAVAKSPIKADSKAKLNIVIPIMPRTSNHTDWDALRLHPEVQVTLVGANETIPPADLVILPGSKSVQSDLAYLRQEGWEDYLNKHLRYGGKVIGICGGYQMLGEQLLDPLGLENQHANTRSTGFGFIPMETVLKEEKQLKQRQGQLAFAANAQVTGYEIHSGVSRFTDETQIAHFALLDDGKNKENSEKEGYISPDGQIIGTYLHGVFDHPDALQALLNWAGVDQAAAFDYDQFRDKEIDRLADSTEQNMNIDALIEQCQNFQQ", "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": "MNRRNRSNDLNPEPSIENPNNQIAEEFPGNNSVYKSDGYVDLKNNGRLFPIWILKNFKQYKLPEIIRKENEDPCNVQVKLELRKYQEFVGQYLNPQGPYTSILLYHGLGSGKTASAINLMNILYNYDNGTNFIVLIKASLHNDPWMQDLKEWLGRDPSEQNVDNVTKLDRYKNIHFVHYDSPFADSSFMSVIKTLDLSKPTMYIIDEAHNFIRNVYSNINSKLGKRAKVIYEYIMKDKRENKNTRIVLISATPAINTPFELALMFNLLRPGIFPSSELDFNRTFVTESSYPILNPMKKNMFERRILGLVSYYIGATPDLYARQELKYINLPMSAYQYDIYRIFEKLEAEIQERARRRGKQSQLYRTYTRQACNFVFPYVNMNVNGELRPRPGKFRLSEKLADDFSKGKNLDVPDTEKEILNKYTKAIENYLNETERYFQNINKKDAENGRTIINDLDEFKKGFGTKFNSFLQYYQSEGPRSSLLTEMYNCSPKMLAIAFMTYISPGKVMIYSNYVVMEGIDVMKIYFRLIGFNDFTIAREYMGYCEYHGRIDPKDRVRIKNMFNDKNNVYGNKCKVIMLSPSATEGIQLLDIRQEHIMEPYWTEVRIQQVIGRGVRQCSHRDLPMSERIVDIYRYKVIKPENLDPDDTVRQSTDEYVEDQAKSKANLIESFLGAMKEAAVDCELFKEHNMMSQSYYCFKFPESAVTKTNVGPAYREDIKDDVKYDSGLNSKNSIVERIRVVKVNAVYQINTDNNNPVYSSPTKYWYNKKTGMVYDFETHYPVGQVEFIDNLPNKLDKDTYIMRIDVIIPSITGSVNT", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily."}
+{"protein": "MPLTKYKAAAVTSEPAWFNLEAGVQKTIDFINEAGQAGCKLIAFPEVWIPGYPYWMWKINYQQSLPMLKKYRENSMAVDSDEFRRIRRAARDNQIHVSLGFSEIDHATLYLAQALISPTGEVLNHRRKIKPTHVEKLVYGDGAGDTFTSVVPTELGRLGQLNCWENMNPFLKALNVSAGEQIHIAAWPVYPGKETLKYPDPATNVADPASDLVTPAYAIETGTWTLAPFQRLSAEGLKMNTPEGVEPETDPTTYNGHARIYRPDGSLVVKPDKDFDGLLFVDIDLNECHLTKALADFSGHYMRPDLIRLLVDTRRKELVTEAEGNDGVKAYSTRERLGLNLPLDGSKEDEKVPVAL", "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": "MRRINTIMQGKTNGGNGPESGTVVVTRTQPKTRKPSLYRVLLLNDDYTPMEFVVHVLQRFFQKNLDDATRIMLHVHNHGVGECGVFTYEVAETKVSQVMDFARQNQHPLQCVMEKK", "text": "FUNCTION: Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation. SIMILARITY: Belongs to the ClpS family."}
+{"protein": "MHSNVGLAGLAGLLATASVCLSAPADQNITSDTYFYGQSPPVYPSPEGTGTGSWAAAYAKAKKFVAQLTPEEKVNLTAGTDANNGCSGNIAAIPRLNFPGLCVSDAGNGLRGTDYVSSWPSGLHVGASWNKALARQRAVQMATEFRKKGVNVLLGPVVGPLGRVAEAGRNWEGFSNDPYLSGALVYETVDGAQSVGVATCTKHYILNEQETNRNPGMEDGVEVAAVSSNIDDKTMHELYLWPFQDAVLAGSASIMCSYNRVNNSYGCQNSKTLNGLLKTELGFQGYVMTDWGAQHAGIAGANAGLDMVMPSTETWGANLTTAISNGTMDASRLDDMATRIIASWYQMNQDSDFPSPGAGMPSDMYAPHQRVIGRDASSKQTLLRGAIEGHVLVKNNHSALPLKSPQLLSVFGYDAKGPNALKQNFNWLSYSPAIQENHTLWVGGGSGANNAAYIDAPIDAIQRQAYEDGTSVLYDISSEDPEVDPTTDACLVFINSYATEGWDRPGLADNSSDTLVKNVARKCANTIVTIHNAGIRVVGEWIDHENVTAVIFAHLPGQDSGRALVELLYGRANPSGKLPYTVAKKVEDYGSLLHPSLPETPYGLFPQSDFDEGVYIDYRAFDRANITAQFEFGFGLSYTSFDYSGLQISNPKQSPQYPPSAAIQQGGNPHLWDNIVTVSAEIKNTGRVAGAEVAQLYIGIPNGPVRQLRGFEKVDVSAGETTQVQFALNRRDLSTWDVEAQQWSLQRGTYRVYVGRSSRDLPLTGSFTL", "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": "MADIKNYTLNFGPQHPAAHGVLRLVLELDGEVIQRADPHIGLLHRATEKLAEQKTWIQSVPYMDRLDYVSMMVNEHAYVMAIERLLGLEVPVRAQYIRVMFDEITRLLNHLMWIGSHALDVGAMAVFLYAFREREDMFDMYEAVSGARMHAAYYRPGGVYRDLPDTMPQYRASKVHNERAIKAMNEARSGSLLDFIEDFTNRFPKYVDEYETLLTDNRIWKQRLVDIGVVSPERALQMGFTGPMLRGSGIEWDLRKKQPYEVYDKLDFDVPVGVGGDCYARYLVRVEEMRQSNRIIRQCVEWLRRNPGPVITDNHKVAPPSRVDMKSNMEELIHHFKLFTEGMHVPEGEAYAAVEHPKGEFGIYAISDGANKPYRLKIRAPGFPHLAALDEMAKGHMIADAVTIIGTQDIVFGEIDR", "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": "MLCLPVFIILLLLASPAAPNPLETRIQRDLIRAALEDADMKTNERFLEGVISTIKDFAGKVCCSVSVNFCCPTA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin T superfamily."}
+{"protein": "MSLALEQATLIQENLPQGNSLPRHIAIIMDGNRRWQRKHEQFCQKRAISGHRQGADSIPQIVDTALHLGVEALTLFAFSTENFSRSKSEVAELFSLFNSQLRSKLSFLHDREIRLRCIGDLSKLPQELQNNIEQASSATAHYSRMELIFAINYGSKDELVRAFKELHQDLASKKISVNDISEELISSYLDTSGLPDPDLLIRTGGEMRVSNFLLWQIAYTELYVTDVLWPDFTANDLLEAIKTYQQRSRRGGK", "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": "MTRTPTGVPMHLGHTHDAPAAVSADATRPDGTRRALRIGLGGPVGSGKTATVAALCRELRDRLSIAVVTNDIYTREDADFLLKNAVLPPERIQAVETGACPHTAIRDDISANLEAVEDLEDAVGPLDLILVESGGDNLTATFSKGLVDAQIFVIDVAGGDDIPRKGGPGVTTADLLVVNKTDLAPYVGSDLERMALDAKKQRGDLPVAFTSLTSAEGVGPVADWVRAQLAAWAA", "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": "MRHGRGSAVSAAISGLSPAKNSPFPQLCNVLLVASLSKTLSQSGTRSLDANSIPISEPVVLQILRRNSIDPSKKLDFFRWCYSLRPGYKHSATAYSQIFRTVCRTGLLGEVPDLLGSMKEDGVNLDQTMAKILLDSLIRSGKFESALGVLDYMEELGDCLNPSVYDSVLIALVKKHELRLALSILFKLLEASDNHSDDDTGRVIIVSYLPGTVAVNELLVGLRRADMRSEFKRVFEKLKGMKRFKFDTWSYNICIHGFGCWGDLDAALSLFKEMKERSSVYGSSFGPDICTYNSLIHVLCLFGKAKDALIVWDELKVSGHEPDNSTYRILIQGCCKSYRMDDAMRIYGEMQYNGFVPDTIVYNCLLDGTLKARKVTEACQLFEKMVQEGVRASCWTYNILIDGLFRNGRAEAGFTLFCDLKKKGQFVDAITFSIVGLQLCREGKLEGAVKLVEEMETRGFSVDLVTISSLLIGFHKQGRWDWKEKLMKHIREGNLVPNVLRWNAGVEASLKRPQSKDKDYTPMFPSKGSFLDIMSMVGSEDDGASAEEVSPMEDDPWSSSPYMDQLAHQRNQPKPLFGLARGQRVEAKPDSFDVDMMNTFLSIYLSKGDLSLACKLFEIFNGMGVTDLTSYTYNSMMSSFVKKGYFQTARGVLDQMFENFCAADIATYNVIIQGLGKMGRADLASAVLDRLTKQGGYLDIVMYNTLINALGKATRLDEATQLFDHMKSNGINPDVVSYNTMIEVNSKAGKLKEAYKYLKAMLDAGCLPNHVTDTILDYLGKEMEKARFKKASFVRNKPNNNNISS", "text": "SIMILARITY: Belongs to the PPR family. P subfamily."}
+{"protein": "MNNNLPTGSSAAVVDLLNKENVIAYPTEAVFGVGCDPDSETAVTRLLALKQRPVDKGLILIAASFEQLKPYIDDSILTAAQRKAVFDCWPGPVTFVFPAPATTPRWLTGRFDSLAVRVTNHPLVVALCNAYGKPLVSTSANLSGLPPCRTVEEVRAQFGDDFPVVEGATGGRLNPSEIRDALTGELFRQG", "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": "MFTINAEVRNEQGKGASRRLRTANKFPAIIYGGNEAPLAVALDHDKVMNMQVKAEFYSEVLTIVVDGKEIKVKAQDVQRHPYKPKLLHIDFVRA", "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": "MALSRGTFYFGLALFFIVVELPSGSWAGLEYSQSFPGGEFAVCETCRLGRGKCRRTCLDSEKIAGKCKLNFFCCRERI", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "KPNPERFYGLM", "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": "MNKTITALAILMASFAANASVLPETPVPFKSGTGVIDNDTVYIGLGSAGTAWYKLDTQAKDKRWTALAAFPGGPRDQATSAFIDGNLYVFGGIGKNSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFVHNGKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINAYYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVFELDFTGNNLKWNKLAPVASPDGVAGGFAGMSNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSADIHLWHNGKWDKSGELSQGRAYGVSLLWNNSLLIIGGEAAGGKAVTDSVLISVKDNKVTVQN", "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": "MKQVTEQAEDFVDTRSSGTEIREFEDLRSDSSQIRMFDTWEDYGLKEDLLKGIYSIGFETPSFIQKAAIQPIIDGRDIRAQAQSGTGKTGAFAVAALQICDMSQDVTQILVLASTREIAAQNAARFEDLGCFMGARVALLSGGSPIAADKVALEKKPHIVVGTPGRVEHMININELSMDNIKLFVIDEADEMLKAGFQEQVKSIFRRITNKDEVQIAMFSATYDEEELRVSEEILINPVIIDLRYNDQTLKGIRQYFIDLRKEPPFRKGREDYLLPKLVTLYDIFRKQRLGQSIVFINSKEDARIVYDWLIRHEWECELISAELTQAERERTLNRFRGGTGRCLISSGLLSRGIDIQNLSVVFCLDVPSFERKSTYIHRIGRSGRYGRKGIAINIVYEHELKNLKAIERFYNTTIKELPADFSFQ", "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": "MFDIGFSELLLVFVIGLIVLGPQRLPVAVKTVAGWIRALRSLATTVQNELTQELKLQEFQDSLKKVEKASLENLTPELKASMDELRQAAESMKRTYSANDPEQASDEAHTIHNPVVKGNETQHEGVTPAAAETQASAPEQKPEPVKANVPESTETASVATIDAEKKSAAPVVESSPSSSDKP", "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": "MTIPTSYLNHTDAEAARKARATYRDGLVAPTSGIAPGFTQANMIVLPRDWAFDFLLYAQRNPKPCPVLDVSDPGSPTTLLAPGADLRTDLPLYRIWRDGKLAEETADATSAWAERDDLVAFLIGCSFTFETPMVEAGIEIRHMTDKSNVPMYLTNRPCRPAGRLKGNMVVSMRPIPASRVADAATISGRFPAVHGAPVHVGAPEQIGISDLSKPDFGDAVRIEPGEVPVFWACGVTPQAAVMASGVPFAITHAPGHMFITDIPDTAYHA", "text": "SIMILARITY: Belongs to the D-glutamate cyclase family."}
+{"protein": "MNSLFATTAQGLEELLRSELETLGAASCKVALGGVHFQADSRLLYRALLWSRLASRIVLPLNVFSVGSDGDLYRGVQAVDWPSLFTVDKRFAVYFSGTNAAIRNSQYGALKVKDAIVDSFTRHGARRPDVDRQQPDIRIQAYLHRDQVMLSLDLSGSSLHQRGYRGAAGQAPLKENLAVAIVLRSGWKPGTPLLDPMCGSGTLLIEAAMIAADCAPGLTRPYWGFSAWSGHDEAQWQESLDEARARTQTGLAQTSSRFYGFDIDGRVLEKARHNARRAGVAALITFQTGEVAQLINPLPEGQRGTVVSNPPYGERLESEPALIALHNQLGRVMKSQFGGWRLSLFSASPALLGALMLRAERSFSAKNGPLDCEQKNYLLAETATAPGSVEGQIATDFANRLRKNVRSLQKWVEREKLDCYRLYDADLPEYNVAIDRYSSWVVIQEYVAPKSVDPERARQRLYDVINATLAVLAIPASRLVVKARERQKGKSQYEKLAQKGEFLLVEEYGAKLWVNLTDYLDTGLFIDHRIARRMLGEMSRGKDFLNLFAYTGSASVHAGIGGACSTTSVDMSRTYLEWAEKNLRSNGLVGRQHRLIQADCLAWLAMAQETFDVIFIDPPTFSNSKRMADTFDVQRDHLALMAQLKRLLRPGGTLMFSNNKRGFQLDEAGLAALGLRAQSITDRTRSPDFAHNRQIHLCWLISHADKDTFKSCH", "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": "MLSGLVTALRTLTLFPVPGKETDTFSRSLFWFPVVGLLLGSIQAALGYFTSLLGWNELSAAFVVLGGIALTRGMHADGLADLADGFWGGRTRESALRIMKDPNVGSFGAIALSGMMLLKWIAILKLVDIGAFACIAAGVLLARWVQVLLASALPYARREGGTAQSFVSGAGVVHIVVTSALTLLFLFPLLHADLYANLYAVVAMISAALAAALLTGLLSYRKIGGVTGDVLGAGSEVTELFVWIAAALSAALKA", "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": "MIEVGDLKKGMFIIYDGEIYRVLEASKHFMGRGSGLIRTKLKNVKTGFVREVNFPSGEKVQEAELSFRKAQYLYRDGDHYYFMTLDDYEQYALSEEEIGDAKYYLVENMEVDLVFHEGTPIGIELPTTVELTVVETEPSFKGDTVSGGGKPAVLETGLKITVPYFIEVGDKIKVDTRTGEYVGRA", "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": "MADRKCLALIAHDQKKDDLAAFAKANEAVLSKWKIVATGTTGGRVLDVCPALDIVRLKSGPLGGDQQIGALIATGDVDCLIFFVDPLTAMPHDVDVKALMRLAIVYDIPMALNRATAEQLIDFRRN", "text": "FUNCTION: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. SIMILARITY: Belongs to the methylglyoxal synthase family."}
+{"protein": "MSHPEEMPVDGTLDATGLNCPEPVMMLHQHIRDLPPGGLLKVIATDPSTRRDIPKFCVFLDHELVDQQEQAGTYLYWIRKNSV", "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": "MAPRAEKKPAEKKTAAERPVEENKAAEKAPAEKKPKAGKKLPPKEAGDKKKKRSKKNVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAQESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS", "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": "MLTMLTDRIDSQLVLSRLPRSRFQRFWETPTLIMKEESAPSSGSIILAEKSVNMRYCVRFASDSDFQTTFTLPQSTEEKYDKEQHPGEDEASSPLPSPLKVPYKWMPSSFIVKQCHTQLAFYNKHIIWLSRERKVPTSLGVSLYIPEGFFGITFYKCLDAQFVCMPELLESGLQVPQLDVVNLNDTFQSIFPGTIEGDIGVFPCFVPEPWQLMNLPPPNEHRFFSLRTRQTLVIGPGHTQTVYFDAAYVHAPGICALIVGVRQFSQSDLIIRPTIWLPGTAAGVTVVNTSHTTVCISPHTTVAKAVFTTHRFTYLPVGSHPLGQMIVPPTPDIGFTHTPEHALLQRTPSPVDDDVDETEEDEKSSDAESPVNTSDVIFDVGPKPPRHP", "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": "MGVFNYESETTSVIPAARLFKAFILEGDTLIPKVAPQAISSVENIEGNGGPGTIKKITFPEGSPFKYVKERVDEVDHANFKYSYSMIEGGALGDTLEKICNEIKIVATPDGGSILKISNKYHTKGDQEMKAEHMKAIKEKGEALLRAVESYLLAHSDAYN", "text": "FUNCTION: May be a general steroid carrier protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the BetVI family."}
+{"protein": "MKIRPITFLVALVCLGFGHAHAKDTQDTNVIDPSPENLPDPDAIIIEGDKVQVYLDRRLKSIGNASLSTGQQKVHGDTIEYDVQNEELHVIGNVRLETKGGRITGPELRMKPSESIGEMKKPAFELDSQFANMPQFGTSGNRRQDNDNLVYSSNSTTPLTQQNIEDSGYAPGLSRKQGVSRGDASGVVFEGPDRKRLKDARYTTCEVGSDDWYIRAKELELDDYTRTGTARNARVEFQGVPILWTPWINFSFLNQRKSGFLAPTWGTTSRSGFEFLVPFYWNIAPDMDATIGTRFLSKRGVQFQGEFRYLNENYQGTANLEYLPSDSSTGENRYYAKFAHLHNFHNGWTAAYNLEKVSDDRYFSEMSTRIVTTSRVNLPQQAYVNYADENWTFNALVQKFQTLDGLNYPLQRLPQLTLTGDNEWGPFDVKLFTQWANFDRNNDAISTQATLGGGTLDTLVTGKRLVAYPSISLPMARPYGYITPKLGLHYTQYQVDNGAFTLRDSNGNITSQDEYQSQSRTLPIFSIDSGLYFDRDVRIVKNRYTQTLEPRMYYVYIPYRDQSLIPVYDSSISDLNMGSLFLENQFTGQDRINNANQLTLAFTSRMISKNTGEQRLAVTVGQRYYFADEKVYLPGVNPRSGDTSDIIGEITARLLNNWNIDIFGQYNTDRSVYVRNNISARYNPEPGKTLNIGYRYTEDRLDQINLSGQWPLGKGWYGLGRWNYSLRENQPIEGIAGLEYDAGCWQARTVMQRVSTATADANYALYFQLELGGLASIGQNPLKLLNRAIPGYTSSSLIPDSYQ", "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": "MAKNSKYSDKQVDAVLHDMIAVLEKHQAPVELSLIVLGNMVTNLLASSVGTHQQAALAQAFSDALMNSVKK", "text": "SIMILARITY: Belongs to the UPF0352 family."}
+{"protein": "MVTIRADEISNIIRERIEQYNREVTIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVINALANPIDGRGKISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTSLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYREQHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFSQFSSDLDKATQNQLARGQRLRELLKQSQSAPLTVEEQIMTIYTGTNGYLDGLEIGQVRKFLVQLRTYLKTNKPQFQEIIASTKTLTAEAESFLKEGIQEQLERFLLQEKV", "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": "MNSETGALRRGWTTGTCASAAARAAFEALLGIEPEDPVPVTLPSGARPTFALARLDRGSGFVRAGIVKDAGDDPDVTHGALVLATLRFGAPATGIVFRAGPGVGIVTKPGLPLPPGEPAINAMPRRMIRTALTEVAEANGVTCDLVVEVGIEDGERIAERTMNRRLGIIGGLSILGTTGVVVPYSCAAWIASIHRGIDVARAEGLTHLAGATGATSEAAIRNLYGLPEQALIDMGDFVGGMLKYIRGHPVARVTIAGGFAKMTKLAQGRLDLHSKREAIDFRWLAELYCSIGGKAESGMSVRTANTALEVLQMAQAEHVPIAPAIARSACRVAAGALARADIALDVAIFDRDGCLIASERC", "text": "FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. SIMILARITY: Belongs to the CbiD family."}
+{"protein": "MSGHTKWHEIRRKKGVLDQRRGQRWTKIARDITIAAREGGGSPDMNFRLRLAIEKAKADNMPADNIQRAIDRGTGVSGEAALEEVTYEGYGPGGIAVIVDAATDNRNRTVSEIRTAFNKNGGTLGEGGSVGWMFDIKGLISIDRTEKTDPDEVTLLAIDADADDVIVNDDAIIVYTEFSKLAAVRDALNEQGLKISTAEKTMLAKTIMEADEATTFQILRLMERLEDLDDVQKVYSNLEVSDELAEKYAEQG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TACO1 family."}
+{"protein": "MKPGIHPEYRKVVFHDTSVDHYFVVGSTLQTDRTIEWEDGQTYPYFTIEVSSESHPFYTGKQRVVQKEGRVANFNRRFAQFGSREG", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily."}
+{"protein": "MKTASIHFWSTLVLLFSCIGSVIAYSSTDLTTMYDWNQIIKPLEWGQMNFIHTTDTHGWLNGHLRDARYKADFGEFKSFVLRMKELADFKDVDLLLVDTGDLHDGNGLSDASDPEGIYTNNIFTYLPYDILTIGNHELYQASVSNNTHEYFVPHWNGTYLASNVQIFNSSNELEQFAAESAYFTTKHGVRVLAVGFLYDFTGNANNTVVTPVETAVNSRWYQQQINRTDVDLFLLLGHIPVRDWDEWKSLHASIRKVHPDTPIQIFGGHSHIRDFAVYDESSVSLEGGRYCETVGWLSIDGLAASNATRQYVGRPVTNETRQSYPNLPIPNTPLYYTRRYIDFNRQNFRFHTQQSEDSFDTPEGIELSKIIKQYRDDLNLSYVFGCVPKNYYMTEVSPQSDDSIFKLMTDRVLPEIITNRNRSTVPRIIISNGGGIRGSMYQGKFGPDEMFQLNPFLTNYYMYLADVPYKYAKKLYSTLNGGSNLRNINENLAALNPGYVTSDDFGEDGDDTVHTSVPSYATPNILQAQAGFNATSSPETIDVVFLNFLQSIVLKALNNMANDTLYTSSNVTQYWVRDDGYDSSPYSFAYFVQQEWSDNCD", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MILEHVLVLSAYLFLIGLYGLITSRNMVRALMCLELILNAVNMNFVTFSDFFDNSQLKGDIFCIFVIAIAAAEAAIGLAIVSSIYRNRKSTRINQSTLLNK", "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": "MPLVANSDLPAFERLREEGETVIPRDVALHQDIREMHIGLLNMMPDAALAATERQFFRLIGESNQIAQFYIHPFTLKEIQRSLEANHYVERYYQTFEQIQAEGLDALIITGANVTQPQLSLEPFWKPLIKVISWAYENVTSTLCSCLATHAVLDFRYGQKRRRLSSKRWGVYSHRVVNRSHPLVRGVNTRFDVPHSRFNEISRDQFEAAGLHVLAESEKGGAHLAVSEDLFRIVFCQGHPEYDSISLLKEYKREILRFASGQRDNYPPFPENYFSPKIQAILEEYQEQIIIARDKDLPLPQLPEPLIVDYLDNTWHDTAEAIINNWMGNVYQITHSDRKRPFMEDIAPDDPLGLRRPT", "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": "MTIAVGRAPSRGWFDVLDDWLKRDRFVFVGWSGILLFPCAFLALGGWLTGTTFVTSWYTHGLASSYLEGANFLTVAVSTPADSMGHSLLLLWGPEAQGDLTRWFQLGGLWPFVALHGAFGLIGFMLRQFEIARLVGIRPYNALAFSAPIAVFVSVFLMYPLGQSSWFFAPSFGVAAIFRFLLFLQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFEDGDGANTFRAFNPTQSEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAVGIVGLALNLRAYDFVSQELRAAEDPEFETFYTKNILLNEGIRAWMAPQDQPHEQFVFPEEVLPRGNAL", "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": "MSEITSPHRSGSVAVIGRPNVGKSTLTNALVGAKVSIVSNRPQTTRHRLLGIATFPEGQLVLVDTPGLHREQKRAMNRVMNRAARGSLEGVDAAVLVIEAGRWDEEDTLAFRVLSDAGVPVVLVVNKVDRLKDKTALFPFLAQVSEGRTFAAVHPVSALKRKGLDALVGDLLKLVPEAEAMFGEDEITDRSQRFLAGELVREQLMRQLGEELPYATTVEIERFAEDGALLRIGAVIWVEREGQKAIVIGKGGTRLKEIGGKARLQMERLFGAKVFLETWVRVREGWSDDEAALKAFGYE", "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": "MKILVINSGSSSIKFKFYDLKIQKCLASGMIEQIGDEVSHSKIETCDGKTIEENMEIRTHDEGIVILNRYLKETGVLTDLKEIDGVGHRIVQGADYFEGPALVDDDVITKIEELIPLAPLHNPAHLSGIRSSLRHAPCLPNVVVFDNTFYHNIPDYAYMYALPYKFYEKYRVRKFGAHGISHEFVTKKGADFLGIDYKNFCVISLHIGSGSSISATKDGICIDTSMGLTPLEGLMMSTRCGSVDPAIIPYMKRVAGYLSEDIDTIMNKKSGLLGITGTSDFRKVLERMHKGDERAKLAFDMLTYQIVKIIGSYYAILPRVDAIIWTAGIGENSAELRESVSKRLAHFGVGVDETVNVNCIKKPTDISSQNATIKTLVIPTDEEYSIAKATERILLSLKK", "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": "MKHDWWLSAARPLDQTACALAAERQRRLTKPRGSLGRLERLAIHLAALQGRERPVVERPWIAIFAGDHGVAEEGVSPYPQAVTGQMLRNFATGGAAISVLARQLGAELELIDLGTAEPLEPPPAGVRRRHLGPGTANFLRGPAMSVRQGLDALAAGRDSVRRAQAAGAHLYIGGEMGIANTSSASALASALLEQPAAALVGPGTGLDAAGLARKVAVVERALALHGAHAGEPLEILRRLGGFEIAALAGAYLACAQEGLPALVDGFICSVAALLAVRLNPACRDWLLFAHRGAEPGHRRVLEALAAEPLLDLGLRLGEGSGAALAVPLLQSACRLHGEMATFAEAAVADAGR", "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": "MKKMMILSALALFSSSLFAANLTLQKEITPQIVNGEGVTLQEVHNGNRIELKPGHNQIAVTIGQIVFEDGKRRKFDSQPLLLEFVAKPEQALTLEYGKFRTIDDAKKFENNPTVHLTDAQGNPVAFTMVQLYKGGLQGFRDYEREVADYNAQKAQKADSAPLVNHDPKAMDLKTAFKEMTRQEQQAFMQWAMQNLK", "text": "SIMILARITY: Belongs to the UPF0319 family."}
+{"protein": "MLSLSQPCFSGTLLMLLASNFLLWKNVAPVPMYASLDEYGEMSIYDLLDHVTILSHNVSELTAEMHRIFMEDVRYKPGRWFSDRYLTACHTSTLTISVSKEGARQMPGVFLVKEMISMLTAWRYPLYHIITELSYMEQAPDEIISRARNIEEKIIVLIEALRGILSKIQPGPPENERYPVWNELASLQSPDEDLRHLTLFNLFQCLVKDSRKIDSSIRLLKCKLLYNRDC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
+{"protein": "MNFGNKIKCSICKKKIFLREKNLFFPFCSKKCKIIDLYQWISGKYKLF", "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": "MKSKIHHQPNGSNNGVVSSNDNGCRSESPSPPLSPNRRVLRRQRRQTLLRASSFSLRRNLRYLLLLPMIYASGLLMCVGPFSGLVGWVYVPGSVYRSPEIYRKLKDDIFSDNSTALELSSVWKFKRRPKMPKPCPNSTVSSHFGLNRESSALAPSSGYLIVEANGGLNQQRSAICNAVAVAGLLNAVLVIPRFEFHAIWKDSSNFGDIYDEDHFISSLEGYVKIVRDVPDEIMTRFSYNVSSIPTIRVQAWATVNYYNGEVYPVLKEHGVIRITPFANRLAMSVPPYIQLLRCIANYKALKFSSPISTLAEKLVDRMVEKSSATGGKYVSVHLRFEEDMVAFSCCLYEGGRAEKSEMDVIRQKSWKGKFKRRDRVIRPDLNRVNGKCPLTPLEVGMMLRGMGFDNNTSIYLASGRIYQPEKHLAPLQEMFPRLYTKESLATPEELAPFQGYSSRMAALDYTVSLLSEVFVTTQGGNFPHFLMGHRRFLFGGHAKTVIPDKPKLVLLLQDMEMRWEVFKKEMKLMLGESDRKGVMVPRVRKINRKTSIYTYPLPECECIFHLSSNFSNTGNILSLGALHPSSNLISSARL", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase GT106 family."}
+{"protein": "MATNNLSILFVASEVEGLIKSGGLADVAKALPEALQNLQQDVRITIPAYTSIERLADAEVVLETNLTSWPHTKYRVLLLTLGNNPVYLIDCDPYFNRPSMYAENNQAYTDNGERFAFFSAACLDMLPKLAFQPDIIHANDWHTGLVPFLLKHRYGNDPFFAHTKSVISIHNAVFKGVFSYDDVQCLPEFHCRNVPDAAVSATHITMLKAGVMNADKINAVSPTYAEELKTELGSHGMAWEFQQRAGDLVGILNGCDYSAWNPETDIYLPMNYSADKQSMVLGKNTCKRALQQRLNLAEKDVAMFGMVCRLTQQKGVHYLLPALADFLKHDVQVVVVGTGDPVLAAQLEEVAAQFSDKFVFVEAYDNELAHLVEAGSDFFLMPSEFEPCGLNQIYSMAYGTLPIVRGVGGLKDSVNDYDVDPCDATGFVFYEPTSQALLLTMLRALLLYAQNLTEVQRVQLHAMQKDFCWRKAAESYLQLYRSALN", "text": "FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. SIMILARITY: Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily."}
+{"protein": "MLETVPVRCVERKITSLVVDLSGVPIVDTMVAQQLYNLSKTLFLLGVKAVFSGIRPDVAQTSIQLGLDFSEYETYGTLKQALENMGVRCIVEELEENK", "text": "SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTSTAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV", "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": "MNLHGKSVILHDMSLRDGMHAKRHQISLEQMVAVATGLDQAGMPLIEITHGDGLGGRSINYGFPAHSDEEYLRAVIPQLKQAKVSALLLPGIGTVDHLKMALDCGVSTIRVATHCTEADVSEQHIGMARKLGVDTVGFLMMAHMISAEKVLEQAKLMESYGANCIYCTDSAGYMLPDEVSEKIGLLRAELNPATEVGFHGHHNMGMAIANSLAAIEAGAARIDGSVAGLGAGAGNTPLEVFVAVCKRMGVETGIDLYKIMDVAEDLVVPMMDQPIRVDRDALTLGYAGVYSSFLLFAQRAEKKYGVSARDILVELGRRGTVGGQEDMIEDLALDMARARQQQKVSA", "text": "SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family."}
+{"protein": "MEITFQKVEHRYQYKTPFERRALYDVDVSFPSGGYYAIIGHTGSGKSTMIQHLNGLLQPTNGTVQIGEHFISAGKKEKKLKLLRKKVGVVFQFPEHQLFEETVEKDICFGPTNFGVSEEAAKQKAREAIELVGLEPDLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGQNELMEMFYKLHKEKGLTVILVTHNMEDAAKYAEQIIVMHKGTVFLQGSAEEVFSHADELEKIGVDLPMSLKYKRAIEEKFGISIPKATLSLEDLTHEVVQVLRKGGHESCSS", "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": "MADESQKTPWLVQYSSKYPNEHPRNLIPALCREFYNLGWFTGTGGAFTIKYRYKIGITKKRNHWKRRNQRNRRNQDEYYFAPSGVQKERIQPEDLFIHDSEDKEIAHPPPEKKLKRSQCVPLFMFAYSMRGAGAVIHSHSKYAVMVSLLDQEATEFRITHQQMIKGIFNSKSHMYHNFHDLLVIPIIENAPDEADLQEPFVEALKNYPETSAVIIRRHGLYVWGKTWQETKAIAESYDYLFDLAIQMRKIGIDPAAKPKRCHLKCCQGAES", "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": "MVPPGNGNGAAAAAGNDVILELSTPGDDWSHELQGDDVEANGGGNGDAPPRRTFSFGQAYKTRHRQPQVFTVWQTLMLGYQSLGIVYGDLGTSPLYVFPSVVLPDADATDFLGILSLIIWTLTLMSLVKYALIVLKADDHGEGGTFALYSLLRQHVNFKGNIPVPLTRLESDVHLKFHSKRRSRPSRLQLFLENSPKAQLAITIIVLIGTCMLIGDGALTPAISVLSAVQGIQSRSSHIKQKHVVVLSAVILVLLFLVQRFGTSRVSFTFSPIMLLWFASIAGIGVYNIVMHYPPVLKAVSPHYIYYYFAKNKRVGWEQLGAVILCITGAEAMFADMGHFNKSSIQVAFSTAVFPSLILAYSGQAAYLIKNPGDLSTAFYSSVPAPLFWPMFVVSTLAAIVASQSLISASYSIIRQSIALGCFPRTTVKHTSDKYEGQVYCPEINYVLMVVCVLITVGFQGGPEIGRAFGVAVIWVMLLTTTLMTVVMVVIWEVNGALAGGFFVFYLAIEGTYMTSLMTKVPQGGWVPFAITVAFLSVTLSWTYGRKKKREYEARHAVGDGEFAGIVSRSARVPGMCLFCTDLMDGVPPIVRHYAANTGSLRELLLFVTFRTLPVRTVLAGERFLVAREGARAGVYRCIAQYGYMDEQDMVGDDFVRAAVAALVEVAAAAAEADSGEEEAEMIGRAPASGVSYVIGRTVLRMRRARNWPKRFVINELYRFLQKNFRSNVSTLKLDHAKTLQVGMIYEI", "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": "MKLLHLDSSALGATSISRELSAAIVAQQRRLYPEVEVTYRDLDRDPIPHLTAQTLAQTDPAEAAAAEAVMQQFLQAEVIVIGAPMYNFAIPSTLKAWIDRIAVAGRTFHYTANGPEGLAGGKRLIIASARGGVYAEPSNDFQEPYLRQLFGFLGIDDITLVRAEGVAYSPQHRADALAAALAGLCAEQDAAVMA", "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": "MTLFSSITSISKTNTSSKSSVNSLSGSSLSMGSNSVACGGCDKPAAGAAILANIDIKAKVDLSLSAAAAASAKCGACH", "text": "SIMILARITY: Belongs to the hssA/B family."}
+{"protein": "MPRPPISLKARALKYLSSREHSRLELARKLAPYAQEGDDIEALLQWLEQSRFLSQERFSESLVHRRAARYGNQRILSELHGHGIEGEAIADLKADLAAGEAERAAQVLRRKFTAPPADAETRAKQMRFLQQRGFSHRSIREAFQTAWLDEDDPS", "text": "FUNCTION: Modulates RecA activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecX family."}
+{"protein": "MSIRIGYKASAEQFGPRDLVEYAVRAEELGLDSVTVSDHFLPWRHEGGHAPFALAWMAAVGERTNRVLIGTSVLTPTFRYNPAVIAQAFATMGLLYPGRIMLGVGTGEALNEIAVSGREWPEFKERFARLREAVDLIRDLWTKEGVSSDGPFYPTVDASIYDRPETPVKVYVAAGGPLVAKYAGRAGDGFIATSGKGMELYTEKLLPAVKEGAEKAGKTFEDVDRMLEVKVSYDRDPEAALENTRFWAPLSLTPEQKHSVDSATEMERLADELPIEQVAKRWIVASDPEQAVKQFRPYLEAGFNHFVVHGPGHDQERFLTQFTEDVVPLLRKLG", "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": "MSTKEKLISHVSKEEAVGSRNKVTVVGVGMVGMASAISILLKDLCDELALVDVMEDKLKGEVMDLQHGSLFLKTHKIVADKDYSVTANSRVVVVTAGARQQEGESRLNLVQRNVNIFKFIIPNIVKYSPNCILMVVSNPVDILTYVAWKLSGFPRHRVIGSGTNLDSARFRHIMGEKLHLHPSSCHGWIVGEHGDSSVPVWSGVNVAGVSLQTLNPKMGAEGDSENWKAVHKMVVDGAYEVIKLKGYTSWAIGMSVADLVESIVKNLHKVHPVSTLVKGMHGVKDEVFLSVPCVLGNSGLTDVIHMTLKADEEKQLVKSAETLWGVQKELTL", "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": "MVKAVAVLRGDSKVSGTVTFEQADENSNTTVSWNITGNDPNAERGFHIHQFGDNTNGCTSAGPHFNPFGKTHGAPEDEVRHVGDLGNFKTDAEGNSKGSKTDKLIKLIGAESVLGRTLVVHAGTDDLGRGDSEESKKTGNAGARPACGVIGIAA", "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": "MSGFSSGNVNSRVVDILSGVVPLLKLICLTVIGLLLAHPKTQLVPRATFRLLSKLVFALFLPCLIFTELGESITLDNIVQWWFIPVNVLLSAVVGSLIGYLVVLICRPPPEFNRFTIVMTAFGNTGNLLLAIVSSVCHTKTNPFGPNCNSRGVSYVSFAQWVAVILVYTVVYHMMEPPLEYYEVVEEEGVEIEEINVENHDASRPLLVEAEWPGIEDKETEHCKTPFIARVFNSISSFSQTSFPEVDLGGEYGGESSSPRSIQCLAEPRVMRRIRVVAEQTPVKHILQPPTIASLLAIIIGSVPQLKSVVFGYDAPLSFITDSLNIMGSAMVPSVMLVLGGMLSEGPNESTLGLRTTIGISVARLLVLPLVGIGIVMSADKLGLISSADPMFKFVLLLQYSTPSAILLGAIASLRGYAVREASALLFWQHIFALLSLTFYIVIFFKLTVETTVQGMQ", "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": "MKPTLPNYDQSGVLIVGDVMLDRYWVGPTSRISPEAPVPVVKVENNEERPGGAANVAMNVAALGGQAHLVGLVGEDEPAQALTTTLESLKVHCDFVALPNFPTITKLRVMSRGQQLIRLDFEESFHDIPAEPIISRMQATLPKVKAVVLSDYAKGALEHVQLMIQEARKAGVPVFIDPKGADFERYRGATLLTPNMLEFETVVGKVKDEEDLVVKGQQIIEEFDFEALLVTRSEHGMTLLRSDMAPLHLPTQAREVFDVTGAGDTVISVLAASVSTGKPLDEACALANAAAGVVVGKLGTSTLSTIELAEAIHGSQDSGFGIINEELLISAVKQARERGEKVVMTNGCFDILHAGHVYYLNHAAELGDRLIVAVNTNESVQRLKGPGRPINPTDRRMAVLAGLGAVDWVVPFSEDTPQRLISEVLPTLLVKGGDYEIKDIAGGAEVIAAGGEVKVLNFEDGCSTTGIIEAIKGGRG", "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": "MLGRPKLVLASGSPRRLALLNQAGIEPDALRPADVDETPTKGELPRSCANRLARAKAEAALQSIQLDDDLRGAYLLAADTVVAVGRRILPKAELVDEASQCLRLLSGRNHRVYTAVCLVTPKGSFRQRLIETKVRFKRLSEEDIDGYVGSGEWRGKAGGYAVQGIAGSFVVKIVGSYTNIVGLPLYETVSLLGGEGFPIRFGWLNAS", "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": "MGAANDAVDGRELMSAAVVGRTISRIAHQIIEKTALDSPDSPRVVLLGIPTRGVILASRLAANIGEYSGIEVDHGALDITLYRDDLMSKPPRPLEETEIPAGGVDDALVILVDDVLYSGRSVRSALDALRDVGRPRSVQLAVLVDRGHRELPVRADYVGKNVPTARSESVHVQFSEHDGHDGVVISR", "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": "MAQQGSSQMRPQGTSSVTQTTTETSASPILHLRPSKRKSKKKPSVRWTEDTVDNEHMNKKKTKICCIFHPQRQFDDGSSCESCSSSDSSSDGSDTEDSKPNAYEHQPHYKNQSKVPQ", "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": "MHDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELAGAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGTTGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSRESHTGERVPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSALWLSGKESGLFDMRDVLDLNSL", "text": "FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapB family."}
+{"protein": "MAGGAWNRRTSLIVFGIVLFGCLFAFSIATEEATKLGTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVAFTDGERLIGEAAKNLAAVNPERTVFDVKRLIGRKFDDKEVQRDMKLVPYKIVNKDGKPYIQVKIKDGETKIFSPEEISAMILTKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVIAGLNVARIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLSTNGDTHLGGEDFDQRIMEYFIKLIKKKHGKDISKDNRALGKLRREAERAKRALSSQHQVRVEIESLFDGVDFSEPLTRARFEELNNDLFRKTMGPVKKAMDDAGLEKTQIDEIVLVGGSTRIPKVQQLLKDYFDGKEPNKGVNPDEAVAYGAAVQGGILSGEGGDETKDILLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSLTKDCRLLGKFDLTGIAPAPRGTPQIEVTFEVDANGILNVKAEDKASGKSEKITITNDKGRLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQINDKDKLADKLESDEKEKIETATKEALEWLDDNQSAEKEDYEEKLKEVEAVCNPIITAVYQKSGGAPGGESGASEDDDHDEL", "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": "MDLENKVKKMGLGHEQGFGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHDVLLSNEEDRKVGKLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPREVNEMEQFVKKYKSEALGVGDVKLPCEMDAQVPKQMNIPGGDRSTPAAVGAMEDKSAEHKRTQYSCYCCKLSMKEGDPAIYAERAGYDKLWHPACFVCSTCHELLVDMIYFWKNEKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDSILAGEIYVMVNDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKRMS", "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": "MTIKVAINGFGRIGRSILRALYESGRRAEIAVIAVNELADAEGIAHLLKYDSSHGRFAWDVRLNNDVLQVGDDNIRLFHQSDISMLPWQELGIDIVLDCSGIYGSRADGEAHLASGAKKVLFAHPGGNDLDATVVYGVNQHLLTAEDRIVSNASCTTNCIIPIIKLLDDQFEIESGTVTTIHASMNDQPVIDAYHKDLRRTRAASQSIIPVDTKLAAGITRIFPKFCDRFEAISVRVPTINVTAIDLSVTVKSSVTVNKINELMQKSAATSFRGIVDYTELPLVSTDFNHDPHSAIVDGTQTRVSGQHLIKTLVWCDNEWGFANRMLDTTLAMAAMGFK", "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": "MKLENKKGYLYLEDGTFIEGYSFGAKGIKVGEVVFTTSMNGYVESLTDPSYKGQILIITHPLVGNYGVPEKKYEQGILTNFESERIQVEGLIVAEHTYPSKWNSALTLDEWLKSENVPGVFDVDTRMIVKKIRTYGTMMGIIASELEIDDPRKYLEKKYDEIDFTQFTSPKSPIFHPNTGDMIVVVDCGIKHGILYGLYKRGFSIVRVPCSFSASKIIEYNPKGIVFSNGPGNPNLLENQIKTFSELVEYKIPILGICLGHQIATLALGGKIKKMKFGHRAINKPVIESNSNKCYISTHNHGYGIISKNDIPPNTKIWFYNPDDYTIEGLIHEKLPIITTQFHPEARPGPWDTTWVFDKFRTMVTGK", "text": "SIMILARITY: Belongs to the CarA family."}
+{"protein": "MKLLAVRRLLRIQRVVIRYRLDDLILELPMLPWWLRLLGATLPWRWLPRRKLELTRGARLRLALQDLGPIFIKFGQILSTRRDLLPDDIANELAWLQDKVPPFPPELAVKRIEEQLGAKIEQVFARFEREPLASASVAQVHAARLKSGEEVVVKVIRPNLEPVIRSDIAWLFILARLAERVSSEARRLHPVEVVSDYEKTIVDELDLLREAANASQLRRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGIPVTDLETLRDQRTDFKALAERGVEIFFTQVFRDSFFHADMHPGNIFVSTRAPWSPQYIAVDCGIVGSLTDEDQDYLARNLIAFFKRDYRKVAQLHIDSGWVPAETKVNDFEAAIRTVCEPIFEKPLKDISFGQVLLRLFQTARRFNMEIQPQLVLLQKTLLNIEGLGRQLYPELDLWATAQPFLERWMRERVSPKQLLRNFQQQVEQVPHLSQMARDTLERLSQPHAHNAPPPEWKGSRHDWLGRLVGAVLLVGAAEVGLGQQLEAWPAWVMLAGGVFLILRR", "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": "MPRVEVGLVIHSRMHARAPVDVWRSVRSLPDFWRLLQVRVASQFGDGLFQAGLAGALLFNPDRAADPMAIAGAFAVLFLPYSLLGPFAGALMDRWDRRWVLVGANTGRLALIAGVGTILAVGAGDVPLLVGALVANGLARFVASGLSAALPHVVPREQVVTMNSVAIASGAVSAFLGANFMLLPRWLLGSGDEGASAIVFLVAIPVSIALLWSLRFGPRVLGPDDTERAIHGSAVYAVVTGLLHGARTVVQLPTVAAGLSGLAAHRMVVGINSLLILLLVRHVTARAVGGLGTALLFFAATGLGAFLANVLTPTAIRRWGRYATANGALAAAATIQVAAAGLLVPVMVVCGFLLGVAGQVVKLCADSAMQMDVDDALRGHVFAVQDALFWVSYILSITVAAALIPEHGHAPVFVLFGSAIYLAGLVVHTIVGRRGQPVIGR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MNCLEKITNEYGQKTASRLEQFVKLIEEENKKINLTSFEGQRLWQEGIYESIKCLEPFVKSNDSLLDIGAGVGFPSVPFLIVNPEVKLTIIESNKKRVLFLEKVKKDLNLSFEIFNGRVENFNKEIHFDFITARALAPLNILMELTINLGSILPKPTNYIFVKGANYLSELNEAQNAIKILKLKVFDLKKIDVFFDKNIFMIHYIKTANVSKEYPRAWDKIIKKPIR", "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": "MDHSLTQDRWQAWCRLMRIDKPIGSLLLLWPTLWALWLAGMAIPALGTLTVFILGVFFMRAAGCVINDYADRKIDGHVKRTRARPLPSGAIGEKEAKLLFGALVGISFALVLTLNSMTIALSTVALALAWVYPFMKRYTHLPQLVLGAAFGWSIPMVFTAVSESLPLSCWLLFLANITWTVAYDTQYAMVDRDDDLRIGVKSTAILFGRFDKLIIGLLQLATLLLLGVIGWQLGLGRIYYLALAGAAGLFLWQQKLIVDREREACFRAFLNNNLVGMLIFVGILLSLLSY", "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": "MSHPALTQLRALRYFKEIPALDSQLLDWLLLEDSMTKRFEQQGKTVSVTMIREGFVEQNEIPEELPLLPKESRYWLREILLCADGEPWLAGRTVVPVSTLSGPELALQKLGKTPLGRYLFTSSTLTRDFIEIGRDAGLWGRRSRLRLSGKPLLLTELFLPASPLY", "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": "MLRKGICRLIHQVSESSKKPYFLTTPIFYVNAAPHLGHLYSLVLTDAIARFQNLKPDVSVISSTGTDEHGLKVQTVAQTEGVSPLQLCDRNSKRFADLAVAANTKFTHFIRTTNPKHQASVQEFWKTIQKAGMISFERHEGWYCVSDETFYPESAIQKVVDPATKQEKRVSMETGKEVQWSSEMNYHFLLSKFQSRLIEHYNKNPNFVQPSIFHTQVLEELKTGISDLSISRPKQRLSWGIPVPGNSQQTIYVWLDALINYISVIGYPWLNEKSSLSAGWPANMHVIGKDIIRFHCIYWPAFLMAAGLPLPEKILVHSHWTMNKVKMSKSLGNVVDPFWLIEKYGVDTIRYYLLKRGRLTSDSNFDIEELEKDEEHDLRRSLGVLLSRLQSKKLFISNEIQKQWHKKDDFTEYEDIVHELIELPVVCAQSIDGGCVYEVINLVQSVLRRVTKLFQLKEPWKLSDDSQEKIDTLMLVAHSLRISGILLQPIMPTKSTELLDQLGIPKNQRSLQNATNVFEPTEFTFHSGNNSHLFDKRTQ", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
+{"protein": "MPFSRLFGKKEKNQMDDIDNIVEEGVQRVQELPMDKIFPNQFQPRTVFDQDKIDELARTIRIHGVIQPIVVREMEPDYYEIIAGERRFRAVLSLEMEKIPAIIQNLDDEEVAAIALIENLQREELTPIEEAKAYRSLLDMQEVTQEALAQRVGKSQSAIANKMRLLKLPETVQEAVLNKQISERHARSLLALETEEQQVALLAEIAENHWNVKQTEARIQEILGVKKPVATKKTKPKRQAISRDVRIAMNTIKQSVTMVKDNGMDLDFTEEETDDFYQITIQIPKKK", "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": "MSHSVLKVPPSVIERMQSHYGPDITSLSVQGAVFQAKPQGCTITAYRSGKVLFQGKNAEKEAERWTADAETPAPKKPASKKSIPSVYQPPEGIGSMSVIGSDEVGTGDYFGPITVACVYADKAKLPLLKELGVKDSKNLKDPQIVQIARDLIKTVPYSLLVLRNEKYNEMQEKGMSQGKMKALLHNQAIGNLLKKLDGTRPEAILIDQFAEPAVYFKHLAGKTAVKERTYFSTKAEGIHLSVAAASIIARYSFLMEMDKLSKQAGITLPKGAGPLVDEAGAKLIKKHGEDALRVFTKLHFANTQKAKRIASKR", "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": "MDTTPAAPDASFDLDPAEIRVLGVLVEKAFLTPDAYPLSVNALVAGCNQLTAREPVMALSEGEVQAAIDSLLARRLVSRRDQAGGRVAKYEHQLRLRHSLPPAEQAVLALLMLRGPQTPGELRSRSERMHRFDDIAAVEAVLEHLGEKYPPMAAALPRAPGTKEIRHMHLLGGAEALEAAAEGLASAAAGGTGRGRLAELEEEVQRLRSEVAELRAAFDTFRQQFD", "text": "SIMILARITY: Belongs to the UPF0502 family."}
+{"protein": "MARKKIALIGGGQIGGVLAQLAALRELGDVVMFDIVEGLPQGKMLDIAEVGSVDGFDCNLKGTNSYEDIKGADVVIVTAGLPRKPGMSRDDLIEVNSKIMTSVAEGIKANAPNAFVIVISNPLDAMVTLCQKITGFPYNRVIGQAGVLDSARFKTFIAWELGVSVKDVNAMTLGGHGDDMVPLVRYASVNGIPVMELLEKKYKDKAKAKEVMEAMVKRTRGAGGEVVALLKTGSAFYSPASSAIQMAESILKDQKRVLPTCAHLNGEFGVKGFYVGVPCVLGENGVEQILEFELDAEEQAMMDKSVAAVKELVGSMK", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family."}
+{"protein": "LVSTPWIELFNAFPSLLRHFPGSHNTIFKNMTEQRKFILEEIKKHQESLDLNNPQDFIDYFLIKMEKEKHNKHSEFTMDNLITTVWDVFSAGTETTSLTLRYGLLLLLKHPEVTAKVQEEIDRVVGRNRSPCMQDRSRMPYTDAVLHEIQRYIDLVPSNLPHVATQDVKFREYLIPKGTAILTSLTSVLHDGKEFPNPGQFDPAHFLDESGNFKKTDHFMAFSAGKRVCVGEGLARMELFLLLVSILQHFTLKPVVDPKHIDIAPSFKGMLSIPPFCEMCFIPV", "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": "MTEPQSVGTVAPQTAHFDEPLPLRSGGTLAGYDLVYETYGQLNAARSNAVLVCHALSGSHHVAGVYADDPRNVGWWDNLVGPGKPLDTRKFFVIGVNNLGGCYGSTGPGSVNPATGRPWGADFPFVTVEDWVDAQARLADRLGIQRFAAIVGGSLGGMQALSWTLQYPERVGHAAVIASAPKLTAQNIAFNEVARQAILTDPDFHGGHYYEHGVVPARGLKLARMVGHITYLSDDSMGEKFGRSLRHGKAVYSYDVEFEIESYLRYQGDKFAGYFDANTYLLTTKTLDYFDPAFEHGGNLNAALARASADFLVVSFTTDWRFSPARSREIVYALLHNRRNVSYAEIDCPAGHDSFLLDDPQYHALLSAWFDRIEV", "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": "MTHAAASRNLSFIDKLVGEVDKALRALSPDTKPHSRPSPKAECGELSDAEKRLSASLMRVNHTGEVCAQALYQGQALTAKLPEIRQEMNNAADEEQDHLAWCEERVKALGSHTSFLNPVWYTLSFSIGAAAGLISDKVSLGFVAATEDQVCKHLQEHLARLPQQDAASRVIVEQMLIDEAKHAQTALAAGGYNFPKPVKMGMTVMSKVMTETSFHI", "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": "MYTEFYGILVLLIFSVVLSAIISGASYILGDKQPDREKVSAYECGFDPFGTPGRPFSIRFFLIGILFLIFDLEISFLFPWCVVCNQVFPFGYWTMIVFLAVLTLGLVYEWLKGGLEWE", "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": "MSAKSSEPPFEPSSEGEQLPSRFEVELEFVQSLANIPYVTFLLTQHQIWQDPRFKAYLKYLEYWCEPPYTQFIVYPNCLFVLKLLNSFLDKAVENEDGILEGAEDLPKVIQMQGGEWMNQMVERWRG", "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": "MKEIYRLVDVSYKYPNGSIALDNVNLNIYKNEVVAILGPNGAGKTTLLKILDGLVFPDKGEVYFEGKKLTDEILRDKELMKEFRRKVGFVFQNPDVMLFNPTVWDEVAFSPLHLYSKEKAIEVTDKTLKDMKIYHLKDRHPYNLSGGEKKKVSISCILSVEPEVILMDEPTSALDPKSRAEIMNLIKSFKECGKTVVLVTHDLNLACLADRCYVLNKKVIFEGKVKDLFSLNLDELNLDVPEISKLFIKLKNMGYNINEIPVTLDEAVNIISKLFQKY", "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": "IEVLLGGDDGSLAFIPNDFSVAAGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMNEEDLLNAPGEVYKVNLTEKGSYSFYCSPHQGAGMVGKVTVN", "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": "MTFEKVGVIGAGAWGTALAQVAARAGLAVTLQAREPEIVAAINDTHENAVFLPGIALEPGIKAVADLADLADCDLILAVAPAQHLRAALTAFAPHRKAGAPVVLCSKGVEQGSLKLMTDVAAEALPGAPIAVLSGPSFAGEVARNLPAAVTLACEDEALGRAIAEAIAIPTFRPYTANDLIGAEAGGAVKNVLAIACGIVEGKGLGRNAHATVITRGFAELTRLAVALGARPETVAGLCGLGDLVLTCSSPQSRNMSVGLALGQGLTLEQALAGKVSVAEGVASAPAVRALARKVGVEAPICEAVAAILAGEVAVDAAIAGLLSRPLKPEA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family."}
+{"protein": "MAKVPDLFEDLKNCYSENEEYGSEIDHLSLNQKSFYDASHEPLHEDCMDKLMSLSTSETSKTSKLTFKESVVMVASNGKILKKRRLSLNQFITDDDLEAIANDTEEEIIKPRSVPYNLQSNVKYNYMRIVNHQCILNDALNRSIIRDPSGQYLMAAVLNNLDNAVKFDMGAYTSEEDSQLPVTLRISKTQLFVSAQNEDEPVLLKEMPETPKIIKDETNLLFFWEKHGSMDYFKSVAHPKLFIATKQEKLVHMASGPPSITDFQILEK", "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": "MMAAVDAILAGKYPAKAHARRVAESLQSYRNGCPGIVYLEAQKTRLIEDNDEPAPFRQRRPFFYLSGCPLPDSCLVYDLSEDQLTLFIPPVDPEDVIWSGLPMSTEEAQNQYDVDRVLVTTELNSTLASIVSSHGGKAIAFTIADQVSESTQFHGFSEVNHSVLKGVIEQSRVVKDEYEVALLRKANDISAKAHIAAIKASQTAVNEREIEGAFIATCIANGAREQSYHPIVACGENGATLHYGKNDDTLIDPVTNQKKRNVLIDAGGEYRTYCADITRVIPVGGKFTAETRQIYDIVLQMQTECIAMLKEGVQWEDVHAHAHRVAIRGLLKLGILRGAEDEIFEKRVSVAFFPHGLGHYLGMDTHDTGGNPNYADKDTMFRYLRVRGRLPAGSVITVEPGVYFCRFIIEPYIKSPESNKYIDTNVLDRYWRVGGVRIEDNVLVTKDGYDNLTTAPKAVDELERLAAS", "text": "FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. SIMILARITY: Belongs to the peptidase M24B family."}
+{"protein": "MNVRGRVAPRRVTGRAMSTLLAYLALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLALATSWLYGAVALVAGGWFLTMAHQLYAGVRAGEPVRPLRLFLQSNNYLAVVFCALAVDSVIALPTLH", "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": "MTFDSANASKPLSVVLAGGGTAGHVSPLLAIADAIREKRPEAAILAVGTPSGMETRLVPAAGYELATIDRVPFPRRPSADLVKLPARLSGAVRQARRILEEARADVLVGVGGYVCTPMYLAARKLRIPIVIHEANMKAGLANRVGARFSNHVAVAFAGTRLRGARHVGMPMRRAISGLDRAVAAPAARAALGLDAQRPALIVTGGSSGALSINRAITAALPALAAAGVQTLHITGNGKAVKDDDGGLLTADGYRQVEYVDGMENVYAAADVLLARAGAGTVSEVAAVGVPAVFVPLPIGNGEQALNAAPLVAAGGAVMVDDKDLSPEWLRSELIPLLTDRSRLNEMARKSEALGIRNADQRMADLVLEAVSA", "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": "MLRIPSRIGSRQVLACAGRNLKCGSVMRHISRRNISKEPEKVYTNLADVNDPKRDQFFKYTWGTWLQNDKLEKDKRTTKFSLNGLNSVLDDIYRQATKNTKDNFKSETEIVPQPLTNKNRTVSMPNNIAITKLGTLNPNEKSVTIKTIASVHEGKHHRIYKVQTNLSDEKSFVLRIPYQLDDDKATISHRIRSEVATLDFLDLQLKMKVPKVICYAADDGNPLGVPFILQEYIDGSLLMKDWNPLMDDKALMVETGEGSTENPELASLNKVVKSMADFHAKLNSISFNAAGSIYFKNDSNLNSETVIDNISNDLASNLKDRWVLGPSVERRLWKKKSDLAIEERLKYLGPWKEDKETSISAQILRDTAILELKNAEARLAKSEQNGSKDKNTETLIKKQIETFQNVEKISGDLISSEMKAIPNIKDLLKPTIFHPDLDPMNVLIENKTETPFMLDLEGAVVKPFILQSSPQFVAYDGPKIYNMKSDIPEFEKLSEEERKHYEFMYKRTRNQFLWEKAVNERLPNLIMTVAPPVKVLRRPYTAVLEQKTDNDYILVDDSFFQLREAWAFFFKNGLVTKEEFPLTFTDEQVKQHADDLNSLHEKLVSTPFAATQGWVPQDMFDNLVRAGVIIKDSTGNFTVNDINPSA", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM9 family."}
+{"protein": "MDSNTVSSFQVDCFLWHVRKRFADQELGDAPFLDRLRRDQKSLRGRGSTLGLDIETATRAGKQIVERILEKESDEALKMTIASLPALRYLTDMTLEEMSRDWFMLMPKQKVAGSLCIRMDQAIMDKTIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTDEDVKNAIGVLIGGLEWNDNTVRVSETLQRFAWRSSNEGGRPSLPPKQKRKMARTTESEV", "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": "MPRANEIKKGMVLNYNGKLLIVKDIDIQSPTARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLSRRGVDFSYVDGNEYVFMDKEDYTPYTFTKDQIEEELLFMPEGGMPDMQVLTWDGQLLVLELPQTVDLEIVETAPGIKGASASARNKPATLSTGLVIQVPEYLSAGEKIRIHIEERRYMGRAD", "text": "SIMILARITY: Belongs to the elongation factor P family."}
+{"protein": "MGQKPSKPKAPPTTYESPRSSLTPDATGFGPEFCKSCWFERKGLIKCQNHYLCMTCLTLLLTVSNRCPVCKYPLPTKLRLEKSPTAPPPEATNPPPYSP", "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": "MVRIAINGFGRIGRLVLRIALSRKNIEVVAINDPFITVDYAAYMFKYDSTHGRFDGEVSHDGKALIIDGKKVLVFQERDPATLPWGAEKIDIAIDSTGIFKELDSAQKHIDAGAKKVVITAPSSTAPMFVVGVNEDKYAGQTIVSNASCTTNCLAPLAKIINNAFGIEEGLMTTVHSITATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLAKPATYEEIKAVVKKASENELKGVMGYTEDAVVSSDFLGDTHSSIFDAAAGIQLSPQFVKLVSWYDNEFGYSTRVVDLVELVAKN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
+{"protein": "MGRFISVSFGLLVVFLSLSGTEAAFCCPSGWSAYDQNCYKVFTEEMNWADAEKFCTEQHKGSHLLSLHNIAEADFVLKKTLAMLKDGVIWMGLNDVWNECNWGWTDGAKLDYKAWNEGTNCFVFKIAKNHWSHMDCSSTHNFVCKFRV", "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": "MAKPDLSVEISGIKLRNPVMTASGTFGYGKEFSDYLDLEKIGAIITKGLSLRPKAGNPTPRIVETPGGMLNAIGLQNVGIDAFIGEKLPFLRTVDTPVIVNLYGNTLEEYGELAEKLDRLPEVAGLEVNISCPNVKQGGIVFGTDPNAAAEVVGLVRRSTSKPLIIKLSPNVTDVVRMADACVNAGADALSLINTLTGMAIDLQKRRPILANITGGLSGPAIKPVALRMVWQVSQAMAVPIIGIGGIMSATDALEFMLAGATAVQVGTANFLDPSAAQTIAAGIEDYLAKNGISDVKELIGALKI", "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": "MANLGYWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQAGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENLTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG", "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": "MIASIYSFLDYLKMVKSASPHTLRNYCLDLNGLKIFLEERGNLAPSSPLQLATEKRKVSELPFSLFTKEHVRMYIAKLIENGKAKRTIKRCLSSIKSFAHYCVIQKILLENPAETIHGPRLPKELPSPMTYAQVEVLMATPDISKYHGLRDRCLMELFYSSGLRISEIVAVNKQDFDLSTHLIRIRGKGKKERIIPVTSNAIQWIQIYLNHPDRKRLEKDPQAIFLNRFGRRISTRSIDRSFQEYLRRSGLSGHITPHTIRHTIATHWLESGMDLKTIQALLGHSSLETTTVYTQVSVKLKKQTHQEAHPHA", "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": "MTNDSEIVVEEKISGPISDWLSNNGFENIPLKEDHLGIEVIKISPNNLLTIVEALKNDGFNYLQCQGGYDEGPGLNIVCFYNLIEMNELKEDISPREVRLKVFLDRNGDLTVPSLYSLFRGADWQERETFDMYGVNFQGHPHPKRLLMPEDWKGWPLRKDYVQPDFYEMQDAY", "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": "MKSILEQLSSITVVVADTGDLDAIKKFQPRDATTNPSLILAAAKNPDYIKLIDQALESSRKSLPAGFSESELIKETIDQVSVFFGKEILNLISGRVSTEVDARLSFDTEATVTKARKLINHYKSFGINKERILIKIASTWEGIKAAEILEKEGIKCNLTLLFNFCQAVACANAKITLISPFVGRILDWHKAKTGKDNFAGCEDPGVISVTKIYNYFKEKGFKTEVMGASFRNIDEIKELAGCDLLTIAPKFLDELNREEGELIKKLDEDTQSQSSIDYKFDEKDFRLSMLEDQMASEKLSEGITGFSKAIEELEELLLKRLSEINNQKLISTT", "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": "MSTTARRRLMRDFKRMQQDPPQGVSASPVADNVLTWNAVIIGPAETPFEDGTFRMVLQFDEQYPNKPPAVKFVSQMFHPNVYSSGELCLDILQNRWSPTYDVAAILTSVQSLLNDPNTSSPANVEASMLYKDHRQQYEKRVRDTVEASWTD", "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": "MLYQSETLQLHWLENGIAELVFDAPGSVNKLDTKTVANLGEALNVLEKQSELKGLLLRSAKTALIVGADITEFLSLFNAPPEKLHQWLVFANTIFNRLEDLPVPTISAINGYALGGGCECILATDFRIASPEARIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIATGKDVTANDALKIGLVDAVVDPEKLVGSALTMLKQAIDGKLDWQAARRPKLEPLKLNPTEAAMCFTIAKGRVMQVAGKHYPAPLTAVKTIEAAAKFGRTEALNLETNSFVPLAGSNEARALVGIFLNDQYVKAQAKKLSKGVAAPKLAAVLGAGIMGGGIAYQSALKSVPVIMKDINENSLDLGMNEAAKLLNKQLERGKVDGLKMASILATIRPTLDYAGIERAQVIVEAVVENPKVKAAVLAEVEALIGEDTVLASNTSTIPIDQLAKSLKRPENFCGMHFFNPVHQMPLVEIIRGAKTSDKTLAAVVAYATQMGKTPIVVNDCPGFFVNRVLFPYLAGFGMLVRDGGDFHQIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPERMNKDYRDAVDVMFDNQRFGQKNGQGFYRYTQDAKGKPRKENDEQVDKLLAEISQPLQEFSDEDIIARTMIPMINEVVRCLEEGIIASAAEGDMALVYGLGFPPFHGGVFRYLDTLGSANYVEMAQRYAHLGALYHVPAGLRAKAEHNESYYPVAAALLDVSTNQPA", "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": "MSFVIAVPEALTMAASDLANIGSTINAANAAAALPTTGVVAAAADEVSAALAALFGSYAQSYHAFGAQLSAFHAQFVQSLTNGARSYVVAEATSAAPLQDLLGVVNAPAQALLGRPLIGNGANGADGTGAPGGPGGLLLGNGGNGGSGAPGQPGGAGGDAGLIGNGGTGGKGGDGLVGSGAAGGVGGRGGWLLGNGGTGGAGGAAGATLVGGTGGVGGATGLIGSGGFGGAGGAAAGVGTTGGVGGSGGVGGVFGNGGFGGAGGLGAAGGVGGTASYFGTGGGGGVGGDGAPGGDGGAGPLLIGNGGVGGLGGAGAAGGNGGAGGMLLGDGGAGGQGGPAVAGVLGGMPGAGGNGGNANWFGSGGAGGQGGTGLAGTNGVNPGSIANPNTGANGTDNSGNGNQTGGNGGPGPAGGVGEAGGVGGQGGLGESLDGNDGTGGKGGAGGTAGTDGGAGGAGGAGGIGETDGSAGGVATGGEGGDGATGGVDGGVGGAGGKGGQGHNTGVGDAFGGDGGIGGDGNGALGAAGGNGGTGGAGGNGGRGGMLIGNGGAGGAGGTGGTGGGGAAGFAGGVGGAGGEGLTDGAGTAEGGTGGLGGLGGVGGTGGMGGSGGVGGNGGAAGSLIGLGGGGGAGGVGGTGGIGGIGGAGGNGGAGGAGTTTGGGATIGGGGGTGGVGGAGGTGGTGGAGGTTGGSGGAGGLIGWAGAAGGTGAGGTGGQGGLGGQGGNGGNGGTGATGGQGGDFALGGNGGAGGAGGSPGGSSGIQGNMGPPGTQGADG", "text": "SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily."}
+{"protein": "MTIDKTYPIFTVRWLTVHGLAVPTVSFLGSISAMQFIQR", "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": "MATPKSSSANRKKGGKKSHRKPKRTWNVYINRSLKSINNHMSMSGRTMKIVNSFVNDLFERIACEAATVVRVNKKRTLGARELQTAVRLVLPADLAKHAMAEGTKAVSHASS", "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": "MNIWLSMLTTTGLGAIIGGFTNHLAIKMLFRPHRPIYIGKFQVPFTPGLIPKRRDELAVQLGKMVVEHLLTPEGIGKKLTNEEFQKGLIHWAQVEVDKVITNEQSLRHMLEKWDVAHVEKEATEKIEQVITEKIQSFLEEYYTYTWEQALPHSVHEKIENAIPNVSAFILKRAIHFFESEEGKSRLSKMIDDFFASRGTLLNLVGMFLGNVSVVDRVQPEVIKFLGQDGTKQLLTEVLQKEWEKLKGRDVKEVETFVEKEMIVSSILSAVKVEETVSKFLNQSVQQVCEPVRETIMEKVVPSAVTKGLKWGAENVASILNNLHLAEIVQQEVSTFSTERLEDLVLSITKNELKMITYLGALLGGMIGIVQGLLLLFLK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0754 family."}
+{"protein": "MEQNPQSQLKLLVTYGKEQGYLTYSEINDHLSDNIINSDQIEDIIQMINDMGIQVVEKAPDSDDLILHEIKRNNETDEDIVEATAQVLSTVESELGRTTDPVRMYMREMGTVELLTREGEIDIAKRIEDGINQVQCSVAEYPEAITHLLEQYNRVELGELRLSELIHGFVDPNAEAVHTSITNHINTNSEEHHHNDNTEENNDDDHLVDPELAREKFIALKNQYHITNYAIKTKNRNHQDTLIEINNLSEIFKQFRLVPKQFDHLVINMRKMMQKIRIQERNIAKLCIEYGNIPKKALLNFFSLQKTNQIWSKIVQNIKKPWIDKFNTIKPDIQMILKKLQKVEEETGLTIHQVKNINKRISLGEAKAKRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQILQEIGREPTPEELSERMLIPEDKIRKVLKIAKEPISMETPIGEDDDSHLGDFLEDTNIELPLDSATSASLRSATKNVLSGLTTREAKVLRMRFGIDMNTDHTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSEILRSFLDD", "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": "MEPTLKNILENPSLKWIFVGGKGGVGKTTTSSSLATLFAKSGKKTIIISTDPAHNLSDCFDQKIGGQPILIKGIDNLSAMEIDPTVDPDKLKLPTLQGFMNDQATKSLLSELISSVPGIDEAMSFAELMNSVDEMKYDLIIFDTAPTGHTLRLLNFPNIMEKGLNKLVQLRYNFQNLASQFQGLFGSQEEFDQQMNQMFSKIETMKDTVTKVNAQMKDKNKTTFIGVCIPEFLSMYETERLVQELTKFKIDIHNIVINQVLFPDDQCKMCNARAKMQKKYLDQMIDLYDDFHVVIMPLQENEVRGIDGLKQFCELLLKPKTVPQV", "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": "MKMTFRWYGEGNDSITLKQIKQIPGCSGLMGVIDQYAAGEVWEESVIAEYVEHVHKAGLEVEVIESVNVHEDIKLGLPSRELYIENYIKTIRNLAKHGIKVIVYNFMPVLDWLRTDLARVIEEDGSNSLYYDEEELLGLTPLQIVENTSKSSNGFTLPGWEPERLKELENVLALYKNIDPDKLRENYKYFLEKVIPVCEECGVKMAVHPDDPAWPIFGLPRIAHSEELFDKILELYDSESHTICLCTGSLGSNPENNIPEIIRHFGGKNRVGCFHVRNVKYLGYRKFRESSHLSSDGSLDMFEIMKAIHETAPDTYIRPDHGRMIWDEVGRPGYGLYDRALGIAYLNGIWEALEKSSK", "text": "FUNCTION: Catalyzes the dehydration of D-mannonate. SIMILARITY: Belongs to the mannonate dehydratase family."}
+{"protein": "MSKVLAMILAGGAGTRLEPLTRERAKPAVPFGGRYRIIDFVLSNFANSGVYRMKVLTQYKSDSLNNHLSRAWRMTAFLGHYVEAVPAQMRTGLDWYKGSADAIYQNLNIITDEEPDYIFVFGADHVYRMDTRQMLDFHCTKKAACTVAAIPVPIEQGREFGIIDVGPDGRMRQFLEKPKDPPPMPGNPKMCLASMGNYLFSTDVLVQEVVRDAANEASAHDFGKSIISELYKRAPVYVYDFAQNEVPGQEAKERGYWRDVGNIDVYYQSNMDLVEVDPTFNLYNDRWPIHTQPNNYPPAKFVFADEQNHRVGHAMDTLVAEGCIISGGSVRRSVLSPKVRVNSYSEVEDSLLFENVTIGRRCRIRRAIIDKNVEIPPGMTIGFDPVEDRRRFHVTPGGVVVIPKGMKVT", "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": "MSSLAAAHATNAVNALLQSVLPGSASVNAERKKTSRDKGSKAQLIDRNLKKRVEVQEKDVYRIKKREKKMLRKKISGRKEVQEDIEQKAKLQVLRKHQVDNSLTDHEKSYLDKVVKKNVRNLKSWDYDDKEELLDLQKQILANSEDSKKVRKVKSRRQKKKQFKEKLPQSIQDHRYKALTPGLAPVGASDEEESEDEDEDY", "text": "FUNCTION: Involved in ribosome biogenesis, probably through modulation of rDNA transcription. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRT14 family."}
+{"protein": "MIEFGDFYRLIAKGPLSPWLDTLPAQLSAWQRESLHGKFKTWFNAVEHLPQLTPTTLDLHSGVRAEMSPPISAGQREGMENMLRALMPWRKGPFSLYGLDIDTEWRSDWKWQRVLPHISPLAGRTILDVGCGSGYHLWRMIGEGAHLAVGIDPMQLFLCQFEAIRKLLGGDQRAHVLPLGIEQLPELAAFDTVFSMGVLYHRRSPLDHLYQLKNQLVTDGELVLETLVVEGDSQQVLVPGDRYAQMRNVYFIPSAPALKAWLEKCGFVDVRIADMAVTTTEEQRRTDWMTSESLAEFLDPHDHSKTVEGYPAPLRAVLIARKP", "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": "MENFCFQDSVSLFITIMVLVLLPRLSLSDTSTYTRPENFYVNCGSDSNVFYGGQTFVGDTNSSTNSVSFTNKGTEVINDQSSVAPEIYRTVRIFRHPSSYKFKLDSLGLHFVRLHFSVVFSRADLLTARFTVSATSGSNHHLKSFSPQNLTNTPRVEEFLLMMNSLEFEIRFVPDHSSLALINAIEVFSAPDDLEIPSASDKNLHTIYRLNVGGEKITPDNDTLGRTWLPDDDDFLYRKDSARNINSTQTPNYVGGLSSATDSTAPDFVYKTAKAMNRSSNEQVGMLMNVTWSFKVKSNHRHFIRIHFSDILSNLSNSDSDFYLFVNGYWRVDVKPSEQPRLASPFFKDVVNVSDGSGLLNISIGTKEANKDAGFLNGLEMMEVLSKSGSDYSNRSSSRVHIITGCAVAAAAASALVFSLLFMVFLKRRRSKKTKPEVEGTVWSPLPLHRGGSSDNRPISQYHNSPLRNLHLGLTIPFTDILSATNNFDEQLLIGKGGFGYVYKAILPDGTKAAIKRGKTGSGQGILEFQTEIQVLSRIRHRHLVSLTGYCEENSEMILVYEFMEKGTLKEHLYGSNLPSLTWKQRLEICIGAARGLDYLHSSGSEGAIIHRDVKSTNILLDEHNIAKVADFGLSKIHNQDESNISINIKGTFGYLDPEYLQTHKLTEKSDVYAFGVVLLEVLFARPAIDPYLPHEEVNLSEWVMFCKSKGTIDEILDPSLIGQIETNSLKKFMEIAEKCLKEYGDERPSMRDVIWDLEYVLQLQMMTNRREAHEEDSTAINSGGSLVAPRLMVSDSFSTNSIFQNGDESKNRFGFTDSSETRVFSQLKISDAR", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MYDWLNALPKAELHLHLEGSLEPELLFALAERNRIALPWNDVEALRKAYAFNNLQEFLDLYYRGADVLRTEQDFYDLTWAYLLRCKEQNVIHTEPFFDPQTHTDRGIAFEVVLAGITGALKDGKSKLGVDSGLILSFLRHLSEDEAEKTLDQALPFRDAFVAVGLDSSEMGHPPSKFQRVFDRARNEGFLTVAHAGEEGPPEYIWEALDLLKIQRIDHGVRAIEDERLMQRIIDEQIPLTVCPLSNTKLCVFDDMAQHNILDMLERGVKVTVNSDDPAYFGGYVTENFHALHTHLGMTEDQARRLAQNSLDARLVKP", "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": "MATGDDIPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLIFHTNRGQIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTARVTYKNVPNWHRDLVRVCENIPIVLCGNKVDVKDRKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLLGDPNLEFVAMPALAPPEVQMDPTMVAQYEQEIAAAANAELPDDDEDL", "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": "MKIVVMGDSDTVVGFRLAGVHEAYEYDESLESVERARNKLRELLERDDVGIILITERLAQRIGSLPEVKFPIILQIPDKFGSIYGEDILRDVVRRAIGVELKR", "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": "MSIDKKIRQIAFYGKGGIGKSTTSQNTLAAMAEMGQRILIVGCDPKADSTRLMLHSKAQTTVLHLAAERGAVEDLELEEVMLTGFRGVKCVESGGPEPGVGCAGRGIITAINFLEENGAYQDVDFVSYDVLGDVVCGGFAMPIRENKAQEIYIVTSGEMMAMYAANNIARGILKYAHTGGVRLGGLICNSRNVDREIELIETLAKRLNTQMIHYVPRDNIVQHAELRRMTVNEYAPDSNQGNEYRILANKIINNENLKIPTPIEMEELEELLIEFGILESEENAAKMIATTSESKSK", "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": "MNVEEQLVQDIAKEIFQKSQVKDRSLSIPVGVSNRHIHLNKEDLRILFGENYELKVKSKISQVGQFAAEETVCIAGPKGCFTKVRVLGPIREYSQIELSKTDSYTLGIKAPVRVSGDIEGSANLCVIGPKGMKVFNEKVICAKRHVHMLPKDADKYGVKDGDLVDVETIGDRSVVFKDVLVRVTNKSALEMHIDTDEANASGVKSKDMVRIIRINR", "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": "MPAPRYKSGSSKKVYRKAPGNSSIVHYRRKKQSKAVCGACGALLNGVPRGRAVEITKLAKTEKRPERPFGGNLCPKCVKKMMVAKARNF", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL34 family."}
+{"protein": "GLPVCGETCFGGTCNTPGCSCTDPICTRD", "text": "FUNCTION: Probably participates in a plant defense mechanism. SIMILARITY: Belongs to the cyclotide family. Moebius subfamily."}
+{"protein": "MAVCARGLRCLGTPAVSLRLAASRSYATTTPPDPAIPNTPGAAATSSPAKRPRTSFQDKLNAGPSFSDFLSDKDDARILDPAEAYALKTALVGPKGKKKEYTRLPPWLKTSIPDSNNYKRIKNDLRGLNLHTVCEEARCPNISECWGGGSKSAATATIMLMGDTCTRGCRFCSVKTSKAPPPLDPHEPENTAEALSRWGLGYVVMTSVDRDDLPDGGARHWAETVMKIKQKAPNILVECLTGDFDGNLEMVALVAKSGLDVYAHNVETVEALTPQVRDRRAGFQKSIRVLKAAKAAQPSLITKTSMMLGLGETEEQMWDALRQLRAADIDVVTFGQYMRPTKRHMPVHEYVRPDVFEFWKEKALEMGFLYCASGPLVRSSYKAGEAFIENVLKKRRAESTGPGSASVQDVATGDLVR", "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": "MELTHLDDKNRPKMVDVSSKSETKRVAVASGEIKMSKEAYQAIISNNTKKGPVLQTAVIAAILGTKKTHELIPMCHPLLLTGIDCDIEEIPQNNTFKLYVTARLNGQTGVEMEALTGVSIGLLTIYDMVKAIDKSMIISNVQLESKSGGKSGDFKR", "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": "MSEITLGRFFFERLHQLKVDTVFGLPGDFNLALLDKIYEVEGMRWAGNANELNAGYAADGYARVNPNGLSALVSTFGVGELSLTNAIAGSYSEHVGVINLVGVPSSSAQAKQLLLHHTLGNGDFTVFHRMFKNISQTSAFIADINSAPAEIDRCIRDAYVYQRPVYIGLPSNLVDMKVPKSLLDKKIDLSLHPNDPESQTEVIETVEKLISEASNPVILVDACAIRHNCKPEVAKLIEETQFPVFTTPMGKSSVDESNPRFGGVYVGSLSKPEVKESVESADLILSIGALLSDFNTGSFSYGYKTRNIVEFHSDYTKIRQATFPGVQMKEALQKLLTTVKKSINPNYTPVPVPETKLINTPAAPSTPLTQEYLWTKVSSWFREGDIIITETGTSAFGIVQSRFPKNSIGISQVLWGSIGYTVGATCGAAMAAQELDPKRRVILFVGDGSLQLTVQEISTMCKWECNNTYLFVLNNDGYTIERLIHGEKAQYNDIQPWNNLQLLPLFNAKDYETKRISTVGELNDLFADKAFAVPDKIRMVEVMLPTMDAPANLVAQAKLSEKTNAEQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TPP enzyme family."}
+{"protein": "MSEIIYGIHAVKALLERDPQRFLEVFILKGRDDRRLQPVIAELEAQGIVIQVASRQWLDKQAEDAVHQGIVAKVKEGRKYQENDLPAMLDNLEMPFLLILDGVTDPHNLGACLRNADGAGVHAVIVPRDRSAQLNATVKKVACGAAETIPVISVTNLARTMRLLQERNIWIVGTAGEADHTLYQSKLTGPLALVMGAEGEGMRRLTREHCDELISIPMAGSVSSLNVSVATGVCLFEAVRQRGG", "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": "MNQPILELKGIEKAFPGVKALDNACLNVYPGKVMALMGENGAGKSTLMKSLTGIYAMDAGEIRYQGKAVNFDGPRHSQEAGISIIHQELNLIPELTIAENIFLGREKTNAFGGIKWAEMFREADDLLKRLNVKHHSRQLLGELSLGEQQMVEIAKALSFKSQVIIMDEPTDALTDTETESLFKVINELRAEGCGIVYISHRLKEIFEICDDITVLRDGKFIGERAVADTDEDGLIEMMVGRRLDEQYPRIDVRHGETCLEVTNLTGAGVNNVSFKLDRGEILGVSGLMGAGRSELMKVIYGALKRESGDIKLNGKTINPVTPQDGLANGIAYISEDRKGDGLVLGLSVKENMSLCSLEQLSKGVQLKHYEEVTAVEDFIRLFNIKTPTRDQIIGNLSGGNQQKVAIAKGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGMSIILVSSEMPEVLGMSDRIIVMHEGRISGEFMAADANQEKLLACAVGKTTEQNNEVAA", "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": "METPNQDSGRTPTEQSAANDLSVADRQVNILRDKLRHIDRQLAAATQNNTKLVSMLETAKAEILRLKNALDQEGQPPYSFGTILQLNPRRQPAPGNSGQAATEESADIFNAGRKMRVGLSPLVNINQLTVGQEVLLNEALLIVAGLGYERAGELATLKEMLGADRALVVGRADEERVVRLSGALLAQKLRVGDALSIDSRTGYALEKVPRSEVENLVLEEVPDITYEDIGGLGPQIEQIRDAVELPFLHPDLYREHGLKAPKGILLYGPPGCGKTLIAKAVANSLAARAAERSGNVDLKSYFLNIKGPELLDKYVGETERHIRLIFARAREKASDGSPVVVFFDEMDSLFRTRGTGISSDVETTIVPQLLSEIDGVERLDNVIVIGASNREDMIDPAILRPGRLDVKVKIHRPDAEAAADIFNKYITPDLPFHESDLAEHNGDVQATVDAMVQRTVEAMYSTDKSNEFLEVTYANGDTEMLYFKDFNSGAVVQNVVDRAKKYAIKDLLTSQQRGLRIEHLLRAVVDEFREHEDMPNTTNPDDWARISGKKGERITYIRTIVQGKAGQEPGKSIETTPTTGQYL", "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": "MKSFVKPERDSLLRTVRIVFTDPDATDDSSSSSDEWLPKPRKVKRFVHEITFLPQVSESSQDRSNAVKTPRRKSTRQFKYPVGVRPRPSGKFAAEILNPFTKTKKWLGTYETPAEAEKAYVDKKVEYDALASSGSAVSSSVVTVTSQCLRSPTSASVSCVSADDLSKEKTSLNKDVAASGDSTTKEVFTTFDFSDVKIPDLRFLAAEEDSMVSNANGAELDFDCFLTDSNILLDDYSLLENDINFSRFENSLPSELPDCDFTEMEFQLDDFKFAYTDHLTTPPLGLV", "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": "MTTEHLSQQRFADLPLHPQILAALNDQNFEYCTPIQALSLPLTLQGKDVAGQAQTGTGKTMAFLTATFHHLLTHQPDFITNQPRALILAPTRELAVQIAHDAESLAQTTKLRIALAYGGDGYDKQLKTIENGVDILIGTTGRVIDYVKQGIIRFNDIQVVVLDEADRMFDLGFIKDIRYLLRKCPAPKSRLTMLFSATLSYKVRELAFEDMNDPEYIEIEPLQKTGHRIKEELFYPSNRDKMALLMTLLEEEWPERCIIFANTKHRCEEIWGYLAADGQRVGLLTGDVAQKKRLALLKQFTDGELDILVATDVAARGLHIPDVTHVFNYDLPDDREDYVHRIGRTGRAGESGMSISFACEQYAMNLPAIEEYIGHHIPVSQYDPDSLINDLPKPYRIKRNHTIPHSSRDYKKR", "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": "MPFGWGRGRGRRRKMRMIRFPPQVRHFYPAIPSVGPPKPPIIMTYEEFEALRLVDYEGLTQEEAGRRMGISRGTVWRALTSARKKVAQMLVEGRELIILPQGNEIVRDEK", "text": "SIMILARITY: Belongs to the UPF0251 family."}
+{"protein": "MLSPKRTRFRKQHRGRMKGISYRGNAICFGKYALQALEPAWITSRQIEAGRRAMTRNARRGGKIWVRIFPDKPVTVRPAETRMGSGKGSPEYWVAVVKPGRILYEMGGVTENIARRAISIAASKMPIRAQFIISG", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL16 family."}
+{"protein": "MQPGKRFLVWLAGLSVLGFLATDMYLPAFAAIQADLQTPASAVSASLSLFLAGFAAAQLLWGPLSDRYGRKPVLLIGLTIFALGSLGMLWVENAATLLVLRFVQAVGVCAAAVIWQALVTDYYPSQKVNRIFAAIMPLVGLSPALAPLLGSWLLVHFSWQAIFATLFAITVVLILPIFWLKPTTKARNNSQDGLTFTDLLRSKTYRGNVLIYAACSASFFAWLTGSPFILSEMGYSPAVIGLSYVPQTIAFLIGGYGCRAALQKWQGKQLLPWLLVLFAVSVIATWAAGFISHVSLVEILIPFCVMAIANGAIYPIVVAQALRPFPHATGRAAALQNTLQLGLCFLASLVVSWLISISTPLLTTTSVMLSTVVLVALGYMMQRCEEVGCQNHGNAEVAHSESH", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Bcr/CmlA family."}
+{"protein": "MFMLQIADYIAENYRGKVVEVGIGRFTAVAELLARRGFEVFATDVVERRAPEGCRFYVDDVTKPNLKIYEGASLIYSLRPPPELFSAIVEVSRKVGADCLIKPLYGDYMEARIVNYKGAQFYLIRRENYD", "text": "SIMILARITY: Belongs to the UPF0146 family."}
+{"protein": "MKVTDVRIRKVAAEGKMKAIVSVTFDEEFVVHDIKIIEGQNGLFIAMPSRKMGEGDFRDIAHPINSDTRSKIQDAIFAEYAIMNEEVQVQVQVTEEAL", "text": "FUNCTION: Could be involved in septation. SIMILARITY: Belongs to the SpoVG family."}
+{"protein": "MKPYDLPDARGHFGPYGGVFVAETLMHALDELRAAYDQCRVDPSFIDEFNYELKHFVGRPSPVYHASRWSQRLGGAQIWFKREDLNHTGAHKVNNCIGQALLARRMGKPRVIAETGAGQHGVATATVAARYGMECVVFMGSEDVRRQASNVYRMKLLGATVVPVDSGSCTLKDALNEAMRDWVTNIENTFYIIGTVAGPDPYPRMVRDFQTVIGQECLTQMPEVIGRQPDYVVAAVGGGSNAMGIFHPYIPYENVRLIGVEAAGEGMETGRHAASLAAGQIGVLHGNRTYVMQNADGQVQETHSVSAGLDYPGVGPEHAWLKDSGRAEYAGITDDEALAAFHDCCRIEGIMPALESAHAIAQAVKMTPALSKDKVILVNLSGRGDKDMHTVAERAGLQL", "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": "MSRFALVGDVGGTNARLALCCLDTGSLEAVQSYPGQQFDSLESVIRTYLQAQAVSVTSACIAIACPITGDRVAMTNHSWAFSISAMQRSLGLAHLSVINDFTAVSMAVPVLPAESLLQLGGQTVQPDRPIAIYGAGTGLGVAHLIRAGERWISLPGEGGHVDFATGSDEEDALLAALRTDLGRVSAERVLSGPGLVNLYRAVARVAGRTPQPLTPQEVSERALADHCPDCRRALSLFCVMMGRFGGNLALNMGTFGGVYIAGGIVPRFLAFFRDSGFRQAFEDKGRFKAYLAPIPVFLIVHDNPGLLGAGAYLRQHLGARL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the bacterial glucokinase family."}
+{"protein": "MIIYATEVQTINSFVRLESLKEVYGFIWIFVPIFSLVLGIITGVLVIVWLEREISAGIQQRIGPEYAGPLGILQALADGTKLLFKEDLRPSRGNTPLFSIGPSIAVISILLSYSIIPFSNHLVLADLNIGIFLWIAISSIAPIGLLMSGYGSNNKYSFLGGLRAAAQSISYEIPLTLCVLSISLLSNSLSTVDIVEAQSKYGFWGWNLWRQPIGFIIFLISSLAECERLPFDLPEAEEELIAGYQTEYSGIKFGLFYVASYLNLLISSLFVTVLYLGGWNISIPHISILKLFEGDQIFGTTIGIFITLAKTYLFLFISIATRWTLPRLRMDQLLNLGWKFLLPISLGNLLLTTSFQLFSL", "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": "MLIFKICFYRLLPLSVLLLAACSALKAPESSSVLKNHIASDEWQEYQHQLKQIQQFQIQGSVAYFSDEKKAYARFFWQQYSPKNYHLLLLSPLGQTEFELKVTNGRVDMAKYKDQGEIKGDAEEILFKLTGIPIPLEHLSRWIVGASSDADEIILNRQSRLKTLIHHKKEQTWKVYYQAYNTKITPILPERLELYLISPNHQDQRMTLKINHWILK", "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": "MSQEHPEQGSSSKRRVYPQQQYDFAAAQPAGYSMPDPTQPYGASASPSAAMYGGAHAIPSPAAFQPHTANVQSGAFAPPPGTPGSAVDPPVAPGVAGGMAYGAPQAAGAAYGYQGLTNQMGNLNIGGGGAYQGGAPPGAAGGAHMAAPTQLNQIYNTDLLQNFPPPISDLTLPPPPVILPPGSSVTGNPDPNADSEFMRCTLNTVPTSSSLLKKSKLPFALVIRPYTALRDADENVPTVADTTIARCRRCRSYINPYVVFLEGGARWRCNMCNLTNDVPSGFDYDAVANKPRDRWSRAELNHSVVEFVAPAEYMVRPPQPLVYVFVLDVSVHSVKNGLLATAARTIKESLSRIPNVDNRTRVGFLAVDSSLHYFAIPRKEDVAEGEGEEGEENEWPEPRMMVVSDIDDPFLPMPTDLLVNLSQCKGGIEKLLDSLQSMFAHTVNPASALGSAVVAAHKLIANIGGKIVCLTSTLPNVGQGKLEVRDDKKALGTSREGQMLQTASTFYKSFAVECSKTQVTVDMFLFSSHYQDVASLSNLPRFSAGQTYFYPGWIASNPEDANKFALEFSEYLSQELATEAVLRVRSCDGIRMSAFYGNFFSRSSDLCSFSTFPRDQSYVIEVNIEETIVKPWVTFQAAILHSTASGERRIRVITRAFPTSALLQDIYASADQIAITTYLANKAVEKALQKGPQDARDLLMNRLNEMFTCYKKDLMTTNVGASAPLQFCTNLRMLPLLVNALIKHIGFRKTSQIPSDLRSAALCLLSTLPDKYLIQYIYPNFYNLIFMPDEAGLPDAETGQIVMPPCTNLSGEHLISHGLFLIDDGQVMFLWVGRDAQPALLQDVFGVSSITEVPTGKTELPVLDNQFNERIRNIISKAREKTDAITYQHLYVVREDGEPALRLWATTHLVEDRVEQSGVTYHQFLTSIREKLNS", "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": "MAGWSCLVTGGGGFLGQRIVHLLLEEKDLQEIRVLDKVFKPEVREEFSKLQSKIKLTMLEGDILDEQCLKGACQGASVVIHTASIIDVVNAVGRETVMKVNVKGTQLLLEACVQASVPVFIHTSSIEVAGPNSYREVIQNACEEDRLETAWSAPYPLSKKLAEKAVLEANGWALQNGGTLHTCALRPMYIYGEGSPFIFAHMNKALENNGVLTHNSKFSRVNPVYVGNVAWAHILALRALRDPRKALSVQGQFYYVADDTPPQSYDDLNYTLGKEWGFCLDSRRSLPPSLRYWLAFLLEIVSFLLSPIYNYQPPFNRHFVTLCNSVFTVSYKKAQRDLGYEPLFTWEEAKQKTKAWVGSLVKQHKEALKTKTH", "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": "MAPRKGKVQKEEVQVQLGPQVLDGEKVFAVCHIYASYNDTFVHVTDLSGRETIVRITGGQKVKADRDESSPYAAMLAAQDVAEKCKSLGINCLHIKIRATGGNKTKTPGPGGQSALRALARAGMKIGRIEDVTPVPSDSTRRKGGRRGRRL", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
+{"protein": "MQIRLNLEQKKYGYNVYINELERIEIKGKTAIVTNPKIAGLHLNTLLNSLKCDEYFIISVPDGEEYKNLATIELILEQLFTSKLDRSSTLIAFGGGVISDMTGFAASIYERGINFINIPTTLLAQVDASVGGKTGVNNKFGKNMIGSFYQPKAVYCESKFLRTLAFREFNAGLAEAVKMAVTFDKEMFEWLENVTLDEEQNLAKLVERSVLIKARVVEADEKERGLRALLNYGHTFAHVIENETGYKKYLHGEAVAIGMNMANSLSVKLGLMSEKDALRIKELLAKFSLPTHYVLRDESAFYEAFMLDKKTQEGSVKFILSNGIGSAVMKNDIKRDDVIKILREFK", "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": "MAQFSESADVPDMGRRQFMNLLTFGTVTGVALGALYPVVNYFIPPATGGAGGGTTAKDELGNDVSVTKFLENRNAGDRNLVQGLKGDPTYIVVDSKEAIKDYGINAICTHLGCVVPWNVAENKFKCPCHGSQYDETGKVVRGPAPLSLALAHTNVSDDKIVLTPWTETDFRTGDAPWWS", "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": "MLILSRKVNEGIVIDDNIHIKVISIDRGSVRLGFEAPESTLILRAELKEAIVSENQKASVCVDESLLENIKKVIKP", "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": "MDVSWDADNFEPKLPTTLAASNKWEGEDEDDNVKESWEDEEEEKKDEEKTEAAPPPQPKPKKKIHDKIAERERQEREKAERLVTEKTAEEMTPEQKLAEKLRQQKLQEESDLRLAMETFGVTEGNIGKLDNFHPTTKEEYTEFADLLTKKITFYKAKDEFPGFIDDLVKNILVQMSSADIRRIKLTVDNLYIEKQKAEKNDKTKKATKGKGKAKLKLEGDNAHLNQYESYGNFDDDYDDFI", "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": "MIKEYLKKPSLSDVQLTRDTRNIPIGKVGVKDISYPIVVMDKNKSFQNTIARINMYVDLPHHFKGTHMSRFVEILNEYREEIALDKLELILSTMKEKLGASNAHLEMEFPYFVEKTAPVSRAKSLMEYTCTFSASLSDRFDFVLGIKVPVTSLCPCSKELSSYGAHNQRSIMTVQVRYSEFIWIEDLIDIIEECGSSPVYSLLKREDEKFVTERAYENPRFVEDMVREATVRLLNMQNISWFSVEAENFESIHKHSAYAAIERSRES", "text": "FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. SIMILARITY: Belongs to the GTP cyclohydrolase IV family."}
+{"protein": "MKNWKTLLLGIAMIANTSFAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAAQARQQLPDDATLRHQIMERLIMDQIILQMGQKMGVKISDEQLDQAIANIAKQNNMTLNQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVESLAQQVGNQNDASTELNLSHILIPLPENPTSDQVNEAESQARAIVDQARNGADFGKLAIAHSADQQALNGGQMGWGRIQELPGIFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGESKNISVTEVHARHILLKPSPIMTDEQARVKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATADIFDPAFRDALTRLNKGQMSAPVHSSFGWHLIELLDTRNVDKTDAAQKDRAYRMLMNRKFSEEAASWMQEQRASAYVKILSN", "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": "MHEMSLCEGIRGIVEDQARRHGFATVKVLRLEIGRFAGVEKAALGFAFDVVMRGSAAEGARLEILDLPGRALCYDCGEEAAIEDRFDPCPLCGGGRLMPVGGDEMRIKDMEVQ", "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": "MDKYDKIIDLTKRRGFLWNSFEIYGGIAGFFDYGPLGAILKNNVINTWRKHYIVNEGFYEIDSPTVTPYEVLKASGHVENFTDPLVECKGCLESFRADHIIEENVDVDTEGKTLQELQEMIEKNNIKCPKCGGEFKDVSTFNLMFATSIGPGGKRAAFMRPETAQGIFIQFKRISQFFRNKLPFGAVQIGKAYRNEISPRQGVIRLREFTQAEGEFFIDSRKKENFEKFESVKDTVLPLLSGKNQENESLSAEEKIVRMSLSDAVKNGIIAHEAIAYYIAVTKKFLMEIGIDESKLRFRQHLPNEMAHYAADCWDAELYTDRYGWIECVGIADRTNYDLLAHMKNSGEDLSVFVELDEEHEIEAYEIELNYKLVGRTFKGDAKVLEESLKELDDKKMEELVEALETEGKYTLKTCKRDFELLKEYLTAKKVKKIVKGEKIIPHVIEPSYGIDRITYCVMEHAFKEEEDRTVMGFSNAVSPIKVGVFPLVNKEGMPEIAMDLKNKLRENGLIAEYDDSGAIGRRYMRMDEVGTPFCITIDGETLVDNSVTIRERDSRAQFRIPINEVVSYIKDKL", "text": "FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
+{"protein": "MKQSLAVKTFEDLFAELSERARTRPTDSATVASLDGGIHALGKKILEEAGEVWLAAEHEPKEVLAEEISQLLYWTQVLMISRGLSLDDVYRKL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family. SIMILARITY: Belongs to the PRA-PH family."}
+{"protein": "MITHFCELAAHRNYVLALYRHSLRNVSRINSGFVKHKMKKVITNEARKHKNDKSSWSIYRRLKELKLLSDKLEDDQVNDAYNLLDSFMKSVKKPKNELKGHLMKIRTEIETNKNIQDKTRLTRLNLLHRYIAKKQQNQLLTKHIPDEYKEKLLLPLALHEKGILRLAAIRNQFKKGGYHAKLSFTMAGKTRIWFIRSMLNKRKKQSLRLRNLITSEKRRYLEVCKIVESLNENANWALHEAIWERYLDDGYLHATSSKGYLKMVEIEDNSVKLQNQNDSKVVKCQRLQQWLSPIQSSILSLENYLNQRQMKYAKLKTKILEPKGVYDYYQKKSKRVFQNHMKTYKRMVKNELPFVNPFIERLSIGSILKRNGINVKY", "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": "MLHLHIFSWVIGIILFIVSYISFTKTGAPKKAYKPLHMTLRLFLVLILFSGVWQVVEEFATATGSTHMLLTLKMICGIGVVALMEVTLVRKQRGASHKGLFWGTIALIIVTMALGIILPGGPISNMFVITK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0344 family."}
+{"protein": "MLICHQCLSSRLTYISNLGLNIAYRLIEQFTDDSKLVIVVTSRTLPRVREVVDLIKTYAEKCGKSGAVDFDYLLVDFTDMVSVLGAAYELEKRYDAIHYFYANAAQGVYSGIDWLGATKAVLRDPLDAVTNPTYKIQRVGVKSRDGLGLVFQANVFGPYYLIRRIIPLLAKGKAKVVWLSSLMSDVKYLSLEDVELLRTDSSYEGSKRLVDLLHLATYKELKSLGIHQYVTHPGIFTSHSFYQYLNFFTYYGMLFLFYLARWLGSPWHNIQGYKGANAPIYVATLANPTFEHQALKYGSATYRDGMEYIAKHEIDPTGMHDAYKYIRDLAEEWDIKLKDQITIGRSLS", "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": "MAEVANNEAQAPQFNIQRIYTKDLSFETPNSPAVFQKEWNPEVKLDLDTRSNKLSDDTYEVILSLTVTAKNGEDTAFLCEVQQAGIFSIVGLTEQQLAHSLGAYCPNVLFPYARELVGNLVGRGTFPQLNLAPVNFDALFAQYVQQRQAAATEEATA", "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": "MTFEQLIPLIIMAFALGMDAFSVSLGMGMMALKIRQILYIGVTIGIFHIIMPFIGMVLGRVLSEQYGDIAHFAGAILLIGLGFYIVYSSILENEETRTTPIGISLFVFAFGVSIDSFSVGLSLGIYGAQTIITILLFGFVSMLLAWTGLFIGRHAKGMLGTYGEIVGGIILVGFGLYLLFPI", "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": "WASQVSENRPVCKAIIQGKQFEGLVDTGADVSIIALNQWPKNWPKQKAVTGLVGIGTASEVYQSTEILHCLGPDNQESTVQPMITSIPLNLWGRDLLQQWGAEITMPAPLYSPTSQKIMTKMGYIPGKGLGKNEDGIKVPVEAKINQEREGIGYPF", "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": "MILSDKDIFDYVNSKRVLIEPFNSKFVGPCSYDVTLGSEFIKYKDDVYDLKKNLSHNKFEIENSIMVCPLNHHLDETIIENYKEKYNVDCVVSGGLLGTTNEYVELPNDVCAQYQGRSSFGRVFLQTHQTAGWIDSGFKGKITLEIVAYDKPVILYKNQRVGQLIFSKTLSPADIGYSDRKCSKYAGQKSVMASLIKKDFEIDEEE", "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": "MAATLLDVCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIVISPGDHRFAQLPLANHPQITVVDGGNERADSVMAGLQAVAQAKWVLVHDAARPCLHQDDLARLLAISENSRVGGILASPVRDTMKRGEPGKAAIAHTVERADLWHALTPQFFPRELLHDCLTRALKEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTRTIHQEKA", "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": "MTTLTARPEAITFDPQQSALIVVDMQNAYATPGGYLDLAGFDVSTTRPVIANIQTAVTAARAAGMLIIWFQNGWDEQYVEAGGPGSPNFHKSNALKTMRKQPQLQGKLLAKGSWDYQLVDELVPQPGDIVLPKPRYSGFFNTPLDSILRSRGIRHLVFTGIATNVCVESTLRDGFFLEYFGVVLEDATHQAGPEFAQKAALFNIETFFGWVSDVETFCDALSPTSFARIA", "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": "MSNETKCPFSHAAGGGTTNRDWWPNQLRLDLLSQHSSKSNPLGGDFNYAKAFKSLDFAAVKKDLAALMTDSQDWWPADFGHYGPLFIRMAWHSAGTYRIGDGRGGAGRGQQRFAPLNSWPDNASLDKARRLLWPIKQKYGQKISWADLMILAGNVALETMGFKTFGFGGGREDTWEPDADVSWGKEKTWLGGDLRYGKGAAGKDEGVVVADEALHGTETSRTDSGRNLENPLAAVQMGLIYVNPEGPDGNPDPLAAAHDIRESFGRMAMDDEETVALIAGGHAFGKTHGAGPADNIGPEPEGADLERQGLGWASTFGTGKGADTITSGLEVTWSNTPTKWGNSYLENLFGHEWELTKSPAGANQWVAKDAAETIPHAYDPAKKLRPTMLTTDLSLRFDPAYEKISRRFLEHPDQLADAFARAWFKLIHRDMGPRARYLGPEVPAEELLWQDPIPAVDHPLVNEQDVAALKQKILASGLPVSQLVQTAWASASTFRGSDKRGGANGARIRLAPQKDWAANEPEQLAKVLKVLEGIQAEFNGAQSGGKKISLADLIVLAGGAGIEQAAQKAGHRVTVPFTPGRMDASQEQTDVQSVGALEPIADGFRNFLKGKYNIRAEDLLIDKAQLLTLTAPEMTVLIGGLRVLNVHTGQDAHGVFTDRPETLSNDFFRNLLDMRTEWKPLSEARDVFEGRDAKTGAKKWTGTRVDLVFGSNSQLRALCEVYASEDGQEKFVRDFVAAWAKVMNLDRFDVA", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
+{"protein": "MDKNKLIGLILISILLIVYTHFFDNKLPKTSQQTTTQEVAHNTSNIQLQTSEATLNLQTGIFAKATQGVTKDIILENKDIRVTLSSHGAKVKEVILKQYKDYLGKPLKLLDEQSTNMGFQFTSNQASINTNTLFFNTDDTDQYIQQASIGKVTFMIPLGEPNQYLQQVYTLPSEGYALTQNWEFVGTENYIDQGKIDFVWHDFIKRAEKDVQACRNKTTINYYLANKTFKHLKEHTEQKEEQTIQTPIQWLAIKQRFFTAGIFTDQPFESGNILLKPTTQPDKFVKEAYTTVSLASNNLQPIQKGTFRFYFGPNTYKDLNSFAQGFSKNLPLGWPIVKWINLYLIIPIFSFIEKYVSNYGLVILILVIFIKLLLLPLSYKSYISMAEMKVLKPTLDALKAKYGNDMQSVQMEQVKLYREMGINPLSGCIPVLLQMPILLAMFNFFPNAIDLRQKAFLWAPDLSTYDAIINLPFQIPFYGSHVSLFTLLMTASTILYTWSSNQVNTPQGPMKTMSYLLPITFMFILNSFPAGLSFYYFVSNLFTFAQQALIKRFVNEDKIKAKLAKNKEKSANNKEGSFKKRFQDAIKASASHKGKK", "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": "MRFETTVQRPVEASGVGLHSGVPVKIRILPAPVSTGVVFVRTDLDGFQIPASWRHVARVSYATSLMRQGVLISTTEHLLSVFYSMGIDNVYVEIDNLEVPILDGSGLPFVKLIAQAGIRQYRRKRRYLRIRRPISVEDKGKRISILPDEAFRLTCDTEYPAPVGRQSLELVVTPEHYASELAFARTFGWENDLDQMRNMGLIRGASLANAVCFTSEGPLNPDGLRAVDECCRHKALDLIGDLALLGRPLLGHVIAERAGHAMHAALVARIMGDPSIYEIITFDQLASRVTQALVS", "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": "MAFPRVRLVVTADDFGYCPRRDEGIVEAFLAGTVTSVSLLVNGTAAESAAELARRHSIPTGLHANLSEGRPVGPARHNASSLLSPEGFFLGKMGFREALAAGDVALPQVREELEAQLSRFRELLGRSPTHVDGHQHVHVLPGVCQVFAEALQAYGVRFTRLPAERGVGSCAWLEAPARAFACTVERDARAAIGPFSRHGLRWTDAFVGLSTCGRHMSAHRVLGSLARALEDIPAGHALTAELMAHPGYPSVPPAGGCGEGPDAFSCSWERLHELHVLTAPTLRAWLAQNGVQLCAIDDLDSKRPGEGVPL", "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": "MAQLFFRYGSMNSGKTIEILKVAHNYEEQNKTVAIFTSGIDDRDQVGFISSRIGLKREATPIFSDTNIFEIVANIKPKPNCVLLDESQFLEKEHVFQLAKIVDDLNIPVIAYGLKNDFRNELFEGSKYLLLYADKLEEMKTICWFCAKKATMVLRVDDKGKPVYTGEQIMIGGNDHYYPVCRKCHANPPIK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thymidine kinase family."}
+{"protein": "MLNNEYKNSSLKIFSLKGNEPLAQEVADRVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIIQPTSNPVNLHLMELLIMIDACKRASAANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPIIGQHFENDPNIDPEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGEIEGRTAIIIDDIIDTAGTITLAAQALKDKGAKDVYACCTHPVLSGPAKERIENSAIKELIVTNSILLDDTRKPSNTKELSVAGLLAQAIIRVYERESVSVLFD", "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": "MSGLFRGRVMTGLNVRIGQGYDVHAFGPGDHVMLGGVRVPHRCGVLAHSDGDVILHALCDAMLGALGLGDIGQHFPPSDVRWKGADSGVFVRHCHLLLRERDWCVGNVDATAICESPKIAPYVNAMREGIARLLEVQPECVSVKATTSEGLGFIGRGEGLAAQVVVLLYRLNGVVV", "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": "MPDAVRRCPEDGFFEGDTCPVCDGAGTHILDGARRRQLSKFVSGALRHFPEDAGIEVDKAGWTGFDALRVAVERQYDWADAAALAGVIATDPKGRFERTGVGNEAGITTAGGRVRAAYGHSVDVTLDGTDDPVPATLYHGTAPRNVDSIREAGLKPMSRQTVHLSESAAAAREVGRRHAADPVVFVVDATAMQSDDRRIVKRGTETYTTDRVSPVYLSLLEK", "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": "MQGRSSAWLVKHELVHRSLGFDYQGVETLQIKPEDWYSIAVISYVYGYNYLRSQCAYDVAPGGLLASVYHLTRIQYGVDQPEEVCIKVFVPRSNPRIPSVFWIWKSADFQERESYDMLGISYDNHPRMKRILMPESWIGWPLRKDYIAPNFYELQDAY", "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": "MTQLAIGKPAPLGAHYDGQGVNFTLFSAHAERVELCVFDANGQEHRYDLPGHSGDIWHGYLPDARPGLRYGYRVHGPWQPADGHRFNPAKLLIDPCARQIDGEFKDNPLLHAGHNEPDYRDNAAIAPKCVVVVDHYDWEDDAPPRTPWGSTIIYEAHVKGLTYLHPEIPVEIRGTYKALGHPVMINYLKQLGITALELLPVAQFASEPRLQRMGLSNYWGYNPVAMFALHPAYACSPETALDEFRDAIKALHKAGIEVILDIVLNHSAELDLDGPLFSLRGIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDYASACLRYWVETCHVDGFRFDLAAVMGRTPEFRQDAPLFTAIQNCPVLSQVKLIAEPWDIAPGGYQVGNFPPLFAEWNDHFRDAARRFWLHYDLPLGAFAGRFAASSDVFKRNGRLPSAAINLVTAHDGFTLRDCVCFNHKHNEANGEENRDGTNNNYSNNHGKEGLGGSLDLVERRRDSIHALLTTLLLSQGTPMLLAGDEHGHSQHGNNNAYCQDNQLTWLDWSQASSGLTAFTAALIHLRKRIPALVENRWWEEGDGNVRWLNRYAQPLSTDEWQNGPKQLQILLSDRFLIAINATLEVTEIVLPAGEWHAIPPFAGEDNPVITAVWQGPAHGLCVFQR", "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": "MHPRFQTAFGELPATLQSALQSYIDAPDFPAMLKAEQVDAITQRCGLDDDALAFALLPLAAACSLAPISQFYVGAIARGQSGNLYFGANMEFSGAPMQQTIHAEQCAVTHAWLRGEPALASITVNYTPCGHCRQFMNELNSGVSLKIRLPGREPATLGDYLPDSFGPKDLDITTLLMDQVDHGFQLALTDELEKAALAAANQSHAPYSNAHSGVALEAEDGTVYTGRYAENAAFNPSLPPLQAALILMNVSGDDCQKVKRAVLAEPESAILTQWDATRATLAALGCQNVSRITF", "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": "MWGKILGAFFGFLLGGPFGLLLGLFLGHKFDKARRNVYRGGGFGGFGTNRANSEERQAEFFYAGFAVMGHMAKAKGHVTEEEIRVASAIMDRMNLHGEARRQAQNAFREGKEDGFPLEETLAKVRQNCAGRADLLQFFLELQIQAAFADGSLHQNERQLLHVIARSLGFSERQLEQRLHMQEAAFRFQQGGFNQQHGGGFNQAPTRDQLADAYEVLGVTESATSQEVKRAYRKQMNEHHPDKLAAKGLPPEMMEIANQKAQELQAAYDMIRKEKGFK", "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": "MDMQHRIRQLFQASIETKQQALEVLPPYIEQASLVMVNALLNEGKILSCGNGGSAGDAQHFSSELLNRFERERPSLPAVALTTDSSTITSIANDYSYNEVFSKQIRALGQPGDVLLAISTSGNSANVIQAIQAAHDREMVVVALTGRDGGGMASLLLPEDVEIRVPSKITARIQEVHLLAIHCLCDLIDRQLFGSEE", "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": "MTRRYWNINLEEMMDAGIHFGHGTRKWNPKMAPYISAKRKGIHIINLTRTARFLSEACDLVFDAASRGKQFLIVGTKNKAADSVAQAAIKARCHYVNKKWLGGMLTNWYTTETRLHKFRDLRTEQKTGRLKRLPKRDAAVLKRQISHLQTYLGGIKYMTGLPDIVIIVDQQEEYTALQECITLRIPTICLIDTNCDPDLADISIPANDDAIASIRLILNKLVFAICEGRSSYIRNS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
+{"protein": "MKVLILVLLGVVILQAAPIRKLEDLLPTRYPPEHELVYWCTYANQCDFCWECVHGICRNRIQADWPVIHQNDWIINCTVSRWNGICSYYEGPRNHTDHQMDCANPTSHTYPHREYMKIYERDDL", "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": "MPRSRINGNFIDKTSSIVANILLRIIPTTSGEKEAFTYYRDGMSAQSEGNYAEALQNYYEATRPEIDPYDRSYILYNIGLIHTSNGEHTKALEYYFRALERNPFLPQASNNMAVICHYRGEQAIRQGDSEIAETWSDQAAEYWKQAIALTPGNYIEAQNWLKITRRFE", "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": "MNLNATLFAQMVVFLVLAWFTMKFVWPPLINALDERSKKIADGLAAAEKGKAELDAAHKRVDQELAQARNDGQQRIADAEKRAQAVAEEIKANAQAEAARIVAQAKAEAEQQIVKARETLRGEVAALAVKGAEQILKREVDQTAHAQLLNQLKAEL", "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": "MLPGEEALVKCEYMKKNFCLASLIKIIKKSPLRVNPKCSFYSDCGGCSMQEIEPHYQFAIKKKLLINALSRIGKLNDFPEPISITPSQFFHYRNKSTFPVYNESYGNTIIGYYQRNSHKIVDIDNCPVLDHKINKALSDIRLILKDNHINADHDIRRKGGLRHISIRSGINTNEVLITFVSNFSIKKLLFPITNKLNGSESNVVGILNNIQPKPNNKIFGATTEILTGRDYIYDKFCHMDILIGSTSFFQVNLVEAEKAINCIRNIISNTNKIVRIIDAYSGIGTMSIPLASDGYRVIGIEINNEAHEIAIRNAEINNIKTITFENQDVTKYLPKILLPNDFLILDPPRKGLDPSLIDVITKLMPIHICYLSCNPATLARDLSLILREHKYSIISITAFDFFPQTTHLETLVYLKRLTS", "text": "SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family."}
+{"protein": "MQGVQEQIEELQTKLAFQELTVEELNQEVIKLNQLVAHQQHQIQLLIGKLQAIEPSNMATQAEETPPPHY", "text": "SIMILARITY: Belongs to the SlyX family."}
+{"protein": "MSLKEKTQSLFAEIFGYPATHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCATRDDRKVRVIAADYDNQVDEFSLDAPIVTHDSQQWSNYVRGVVKHLQKRNNAFGGADLVISGNVPQGAGLSSSASLEVAVGTVFQQLYHLPLDGAQIALNGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRTLGTKAVSMPEGVAVVIINSNFKRTLVGSEYNTRREQCETGARFFQQPALRDVSLAAFNAVASELDPIVAKRVRHVLTENARTVEAASALEKGDLKRMGELMAESHASMRDDFEITVPQIDTLVEIVKATIGDKGGVRMTGGGFGGCVVALLPEALVPAVQQAVATQYEAKTGIKETFYVCKPSQGAGQC", "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": "MDIKLINIGFGNIVSGNRVISIVSPESAPIKRIISEARDRAQLIDATYGRRTRAVIVTDSGHVVLSAIQPETVAHRFMSNKDTKDSDK", "text": "SIMILARITY: Belongs to the RemA family."}
+{"protein": "MKTFLILVLLAIVATTATTAVRFPVPQLQPQNPSQQQPQEQVPLVQQQQFLGQQQPFPPQQPYPQPQPFPSQLPYLQLQPFPQPQLPYSQPQPFRPQQPYPQPQPQYSQPQQPISQQQQQQQQQQQQQQQQQQILQQILQQQLIPCMDVVLQQHNIAHGRSQVLQQSTYQLLQELCCQHLWQIPEQSQCQAIHNVVHAIILHQQQKQQQQPSSQVSFQQPLQQYPLGQGSFRPSQQNPQAQGSVQPQQLPQFEEIRNLALQTLPAMCNVYIPPYCTIAPFGIFGTN", "text": "FUNCTION: Gliadin is the major seed storage protein in wheat. SIMILARITY: Belongs to the gliadin/glutenin family."}
+{"protein": "MNIWVDADACPAEVKDILWRAAQRWQVPVTLVANQLLRVPASPWMRAVQVPRGFDVADAHIVASAVPGDLVITADIPLAAEVVGKGVAAMSWRGEVFDAGSIGERLTMRDMMEELRAGGVDIGGPAAFGQADRRAFANALDAAMQRRARTRGAGGKPGVV", "text": "SIMILARITY: Belongs to the UPF0178 family."}
+{"protein": "MSWITPDLIEILLSILKAVVILLVVVTCGAFMSFGERRLLGLFQNRYGPNRVGWGGSLQLVADMIKMFFKEDWIPKFSDRVIFTLAPMIAFTSLLLSFAIVPVSPNWVVADLNIGILFSLMMAGLAVYAVLFAGWSSNNKYSLLGAMRASAQTVSYEVFLGLSLMGVVAQAGSFNMTDIVNNQAHLWNVIPQFFGFVTFAIAGVAVCHRHPFDQPEAEQELADGYHIEYSGMKFGLFFVGEYIGIVTVSALMVTLFFGGWHGPFLPPFVWFALKTAFFMMMFILIRASLPRPRYDQVMSFGWKVCLPLTLINLLVTAAVILWQAQ", "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": "MSDSIVHVTDDSFEDEVLKSLEPVLVDYWADWCGPCKMIAPVLDEIAGEYAGRIKVAKLNIDENPNTPRRYGIRGIPTLMLSRQSEVEATK", "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": "MIKSERPQAYIGRFAPSPSGDLHFGSLITAIGSYLQARACQGKWLIRIDDIDPPREVPGAASRILHALEHYGLHWDGEILYQSQRHEAYCHVLNQLQQQGLSYYCTCTRQRIHQINGFYDRNCRELNLPIDHAAIRFKQRHPVYGFEDKLQGYLNADPVMAEEDFIIHRRDGLFAYNLVVVIDDDYQGVTEVVRGVDLIEPTVRQIALYRQLNLKIPDYIHLPLALNKDGNKLSKQNHAQPIPLDDPRPLLIEALSFLNQSVIENWQDLSRDQLLQKATAHWDLDRIPRQGKIHIDNMNKVTVSHNNHSQKIHSRL", "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": "MWLRFCAPALMAWYWVFFPSTSQAATMENDGQDGFWQRAKNNLSETWHNGQSQDLYVPAMTWHNRWTYSRQKIDKYNERPWGAGYGVSRLDSDGDWHGIYLMAFKDSFNKWEPIGGYGYEKRWKPVAGNDDFQLGLGFTAGVTMRDNWNYIPIPVLLPLASINYQRLSFQMTYIPGTHNNGNVYFAWLRWQL", "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": "MRKIIQEKLNEGKVLHFSLFDPDKVDLESIYSIALKLVESGTSGFLIGGTLGVSKEKLDSIIEILEDFEVPKIIFPSNVNLITEKADAILFMSLLNSDDIYYITGAQLIAAPIIKKLKLESLPTGYIIVGHGGTAAHVGKARVIPYDNIELIVAYSIMAELFGMDFVYLEAGSGAPEPIRPSVISITKKYLENSKIIVGGGIRNEEIAKELALAGADIIVTGNIIEQNLEKALKIVKEISNIRR", "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": "MQECGLVATDIACRRGDRILFRALSLDVKAGEIVHLAGANGIGKSSLIRILAGLLRPFAGTVERRGAIALSDERLALDGHLPLEDALRFWDRIDRAGRPEAEFGLDDLLDVPVRYLSTGQRKRAALARVAASGAPLWLLDEPLNGLDVHWSERAQEAIEAHCARGGAVVIASHQPLALERVRTLAIRNFQP", "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": "MKFVLLFGVLLVTLFSYSSAEMLDDFDQADEDELLSLIEKEEARAKECTPRFYDCSHDRHSCCRSELFKDVCTCFYPEGGDNEVRTCQQPKHLKYMEKAADKAKKFGGKIKKWFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 01 subfamily."}
+{"protein": "MSRGIIIIGSGFAARQLVKNIRKQDAHVPLTLIAADSMDEYNKPDLSHVISQSQRADDLTRQLAGEFAEQFNLRLFPHTWVTDIDADAHVVKSQDKQWQYDKLVLATGAAAFVPPIAGRELMLTLNNQQEYRACETPLRDAQRVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASLLASLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKIEAGIRATLASQRSIEVDAVIAATGLRPETALARRAGVVVNRGVCVDSYLQTSHPDIYAIGDCAEINGQVLPFLQPIQLSAMYLAKNLLGGNAPLKLPAMLVKVKTPELPLHLAGETQRRDLSWQITAESDGMIAKGMSGEGQLRAFVVSEDRMKEAFALLKTLSV", "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": "MIEINNKVDYIFYTNNTPNTYKIKLILLELEKKHSITFESRYINITKKENYSDEFVKINPNKKVPAIVDQTGEKPFVVFESVSILIYLAQKYNTFLPDFKTNPHENSDVITWAVWQAANLGPAFGQYFHFSYFSPTVQEYSLHRFNNEAQRVLRLLDDRLSVSQYIGGNEFSIADIASAGWLLYLNFAPIYKATKERFPHIFKWLDLINQRDAVKEINQSISEGFKTFNPSALRALFTDDPELINAKAPIGIENVVLKYD", "text": "SIMILARITY: Belongs to the GST superfamily."}
+{"protein": "MKIGFDHEKYIEEQSKYILERVNNYDKLYLEFGGKLLYDLHAKRVLPGFDENAKIKLLHKLKEKVEIIICVYAGDIERNKIRGDFGITYDVDVLRLIDDLRSYDLQVNSVVITRYSGQPSTTVFINKLERRGIKVYKHEATKGYPADVDTIVSDEGYGKNPYIETTKPIVVVTAPGPGSGKLATCLSQLYHEYKQGKVAGYSKFETFPVWNVPLKHPLNIAYEAATVDLKDVNMIDSFHFDAYNEVAVNYNRDIESFPLLKRIIEKITGEESGYKSPTDMGVNRVGYGIIDDEVVKKASEQEIIRRYFKTGCEYKKGYLDKETLHRSKIIMHELNLKEDDRKVVMPAREYSAKLKKRYNKNEVYPVVALELEDGKVLTGRNSDVMDGTAAVILNAVKYLANISDEIHLISPVILEPIINLKLKTLGSKSTALTCEEILIALSICAVTNPTAQVAMEKLSMLRGCQAHSTTILSGNEEQTFRKLGIDITCDPEYPSESLYYNN", "text": "SIMILARITY: Belongs to the UPF0371 family."}
+{"protein": "MTNVTGTERVKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVSRMADPTIVEEVMGAVSIPVMAKCRIGHLVEARVLESLGVDYIDESEVLTPADEVYHLNKRDYTVPFVCGCRDIGEAARRIAEGASMLRTKGEPGTGNIVEAVRHMRQVNAEIRQVASLREDELMTYAKNTGAPYEVLREIKRLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPAKFARAIVEATTHYEDYELIASLSKGLGNAMKGIEISTLLPEQRMQERGW", "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": "MEFSVKSGNPEKQRSACVVVGVFDRRKLSSAARVLDKASGGALSTILRRGDMDGEKGQTLWLYNLPNTLCERVLLVGCGKERDFDEPAYRSVIATVARTVNKSGAVEAVNYLTDLPVKGRDTLWKISQAVTITQDSLYSFQQLKSKKEDTQRPLKRIILSVPSRADLLPGEDAVRVATAISVGTKLTRDLANLPGNICNPTYLAEQALQLKKTYKGLKVEILEEADMEKLGMGALLSVSRGSEQPAKLITLEYRGGRKDAKPVVLVGKGITFDTGGISLKPGAEMDEMKFDMCGAASVLGVMKAVAEMMLPINLVGVVAAAENMPDGKATRPGDVVTSMSGQTIEILNTDAEGRLVLCDALSYVERFDPDVVIDIATLTGACIIALGHQATGLLSNHSPLANDLLGAGKQSYDRAWELPLWDEYQEQLKSNFADMANIGGRPAGTITAACFLSRFTKKYKWAHLDIAGVAWKSGKEKGATGRPVPLLMQYLLNKAS", "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": "MIQDEIPIPVQTLQWKCIESKKEGKRLHYGRFAVSPFRKGQASTVGVAMRRALLGEVEGTSITYAKFKNVVHEYSTLVGIKESIHDILINLKEIVLQSDSYETQKASISILGPRDVTAGDILLPTSVKIIDASQHIATITTAIPLDVELRIERDCGYRTLNLKESQSGEFFIDALFTPIRNANYSIHSFESNNKVREILFLEVWTNGSLTPGAALSEASRDLIDLFIIFLNMEKEESIKEIENNELNIKNFPSTSISVDIDRMAKEVAFKQIFIDQLELPARAYNCLKKMQVHTVSDLLKYTQYDLKKVKNFGNKSVEQVVEALQERFAIQLPKDQFNIS", "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": "MAEISLRDVRKSYAGIEVIHGVDLEIADGEFVVIVGPSGCGKSTLLRMVAGLEEITAGEIAIGGRVVNRLEPRERDIAMVFQNYALYPHMTVRENMAYGLRIAKLSKAEIEERVARSARMLELGQLLDRKPRQLSGGQRQRVAMGRALVRNPAAFLLDEPLSNLDAKLRVQMRLQIKELQRTVRTTSIYVTHDQVEAMTLADRLVVMNAGVAEQIATPAEIYDRPATTFVAGFIGSPAMNMLPARGLGDALEVAGQRLAVPAPAGRDLILGVRPEHLHAAGPEEPGFELHVQAVEWLGADAFAHGRLADGTDLVLRTPGKAPVRERDRLKVAPDAAALHLFDAETGKRL", "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": "MRREQQLPAAVAAPVADGGQLMRAVDLTLGFGPKTVLEQVSLDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVRAHKMAPRKQFKTVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTSSLDPTTTEKIEGLIRSLADRLTVIMVTHDLAQAARTGDRTAFFFEGRLVEEGPTKHLFLSPQHEETVRYFAPFRPAQGSDRGSSQTAGVAESQ", "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": "MTDAQVFTILAIALVPAVMAALLGSALARS", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaM family."}
+{"protein": "IQSTSMDQGILTEDSMNSFIRTLIQAGIWKNKVPKQTARTKDGTQTTVKKTEAEADAMVSKDTRLSFQPIVSVDAELLRQQRRFSSPRVLLSENTPLEPPPLYLTEEPTVLNRTSRRKREGKSHRGEYSVCDSESRWVTDKSSAVDIRGHQVTVLGEIRMGPS", "text": "FUNCTION: Seems to promote the survival of visceral and proprioceptive sensory neurons. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NGF-beta family."}
+{"protein": "MPEEKIRLTQLSHGGGCGCKIAPAVLQKILAGTTGSIIPPQLLVGTETSDDAAVYQINAQQAIVATTDFFMPIVDNPRDFGRIAATNAISDVYAMGGTPLFALALVGMPVNVLPLETIGQILQGGEDVCRAAGIPIAGGHTIDSVEPIYGLVAIGLVNPEHLKRNSGAKSGDKLILGKQLGVGIYSAALKKDQLQAKDYEAMVETTTQLNTPGPVLACLDGVHAVTDVTGFGLAGHLLEVCKGSGLRATVNYQDLPVLPKAREFMQAGLMTGASGRNWASYGEGVRIADGLEGIAQTLLTDPQTSGGLLVSCSPETVTEVLSLFLQHGFPHVSVIGEMAEGEPGIDVI", "text": "FUNCTION: Synthesizes selenophosphate from selenide and ATP. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I subfamily."}
+{"protein": "MNEREYIGRGRRKLEHLRFFQEDSKGSNGLEDVHLVHQALPELNWSDIDLTCRWLGKTLAAPFIINALTGGPPETLAINAALARVARRTGIALAVGSQRAGLENKEWRESFTIVRRENANGLILANIGAGNSPADAGEAVAMIAADGLQVHLNAAQELIMPEGDRAFRGWLENIRGMVNTLGVPVIAKEVGFGLSRETALQLYQAGVRIMDVGGRGGTNFAAIEERRRGRSVAALAGWGLSTAVSILEIRELGLPVEVVATGGIRSALDAARALALGAKIVGAAGYFLKILLEQGEDALTEEILQWQEDLKRICLLTGCTTPAELATKPVVITGQTRAWLEGRQRH", "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": "MDLDLNNRMTEDETLEKAYDIFLELASFNLDPADILLFSLQFEIRGGAELLPPSDGWLKHVDFNPNPDFFAEVIIGLAESEDAEINDVFARILICREKSHPIYHILWKE", "text": "SIMILARITY: Belongs to the UPF0263 family."}
+{"protein": "MIEDTMTLLSLLGRIMRYFLLRPETLFLLCISLALWSYFFHTDEVKTIVKSSRDAVKMVKGKVAEIMQNDRLGGLDVLEAEFSKTWEFKNHNVAVYSIQGRRDHMEDRFEVLTDLANKTHPSIFGIFDGHGGETAAEYVKSRLPEALKQHLQDYEKDKENSVLSYQTILEQQILSIDREMLEKLTVSYDEAGTTCLIALLSDKDLTVANVGDSRGVLCDKDGNAIPLSHDHKPYQLKERKRIKRAGGFISFNGSWRVQGILAMSRSLGDYPLKNLNVVIPDPDILTFDLDKLQPEFMILASDGLWDAFSNEEAVRFIKERLDEPHFGAKSIVLQSFYRGCPDNITVMVVKFRNSSKTEEQ", "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": "MTLARLAPLAALLLAACAQFQPPPPEPDPLPDLMRQQTSLPQGGGVFTAGGSLSLTSDNRAFRPGDVLTVVLEETTQASKQAGTSFGKKSGAKIGPSLIGNTTFNAQVGIDANRDFNGSSSSTQQNALAGSLTVVVHRVLPNGLLQVKGEKQLTLNQGEEMLRVAGYVRVEDIDTDNRVSSLRIANARIGYSGSGALADANSPGWLMRFFASPLMPF", "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": "MSEISAEERESGTVFAPKFDSDGLLTAVVQHVDTREVLMVAFMNADALDATRKTGIAHFFSRSRQTLWKKGGTSGNTLAVSQVLVDCDQDAVILLVEPAGPACHTGARTCFYRELDCGALQDVRT", "text": "FUNCTION: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-CH family."}
+{"protein": "MAVYTDIAEDDLKWFLTEYDAGTLLSYKGIAEGVENSNFLLHTSKDPLILTLYEKRVEKTDLPFFLGLMQHLSARGLSCPLPLPRRDGALLGSLSGRPAALISFLEGMWLRKPEAKHCREVGRALAEMHVAGDGFELKRPNALSIDGWQTLWEKSEARAGEVEAGLQDEIRGELDFLAAAWPKNLPAGIIHADLFPDNVFFLGDALSGLIDFYFACNDLLAYDVSICLNAWCFEKDGAYNITKGTAMLEGYQSVRPLSGEEIAALPVLSRGSALRFFLTRLYDWLTTPEGAMVTKKDPLEYLRKLRFHRQIKSPAEYGLSL", "text": "SIMILARITY: Belongs to the pseudomonas-type ThrB family."}
+{"protein": "MSMENFAQLLEESFTLQEMNPGEVITAEVVAIDQNFVTVNAGLKSESLIDVAEFKNAQGEIEVKVGDFVTVTIESVENGFGETKLSREKAKRAADWIALEEAMENGDILSGIINGKVKGGLTVMISSIRAFLPGSLVDVRPVKDTSHFEGKEIEFKVIKLDKKRNNVVVSRRAVLEATLGEERKALLENLQEGSVIKGIVKNITDYGAFVDLGGIDGLLHITDLAWRRVKHPSEVLEVGQEVEAKVLKFDQEKQRVSLGMKQLGEDPWSGLTRRYPQGTRLFGKVSNLTDYGAFVEIEQGIEGLVHVSEMDWTNKNVHPSKVVQLGDEVEVMILEIDEGRRRISLGMKQCQANPWEEFAANHNKGDKISGAVKSITDFGVFVGLPGGIDGLVHLSDLSWTESGEEAVRKYKKGEEVEAVVLAIDVEKERISLGIKQLEGDPFGNFISVNDKGSLVKGSVKSVDAKGAVIALSDEVEGYLPASEFAADRVEDLTTKLKEGDEVEAVIVTVDRKNRSIKLSVKAKDAKESREALNSVNAAANANAGTTSLGDLLKAKLSGEQE", "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": "MSASHKNLHSKLSIGGLLITLGIIYGDIGTSPLYVMKAILGNHTINADIVLGGISCVFWTLTLQTTIKYVLITLSADNHGEGGIFALYALVKKTKIQWLIVPAIIGGSALLADGIITPPISISSAVEGIRAFYPTMQTQTIVYIVITILFILFTIQQFGTKLVGKFFAPMMLIWFAMLGTLGFIQIMHFPEVIKAINPYYAYHLLSVHPDGFFVLGFVFLCTTGAEALYSDMGHCGRKNIRISWIFVKTTLVLNYFGQAAYLIHHEGSTLQQLGGENGNPFYLIMPHWFLPFGIVVATLAAVIASQALISGSFTLINEAMRLNFWPKVKIKYPTEVKGQLYIPSINWLLFFGCVGIVLHFEKSGNMEHAYGLAIILCMIMTTILLNYYLIMKRVKLYFMVPLITIYLLIEFSFLIANITKFAEGGYVTLIIAILLISIMTIWYLAKKINKNYTKVIKIDDYKKVLMELSEDLSIPKYATHLVYMTNANSVDELEEKVIYSILQKRPKRADIYWFVHVNILTEPYKTQYKVTEIAKDDIYRIDFNLGFREPTKINLMFREVIRDMVKRGEVDITSRYESLNKNNIIGDFKFVLSEKFLSNDNDLRWHENIIMNSYFFIKKLSLSEERAFGLDSSSVKIEKFPMVLHAPENIGLTRITK", "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": "MGRFVAVALLVLLSLSGLETIQHAPKIQVYSRHPAENGKPNFLNCYVSGFHPSDIEVDLLKNGKKIEKVEHSDLSFSKDWSFYLLYYTEFTPNEKDEYACRVSHVTFSTPKTVKWDRNM", "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": "MSSTIFGEQLPKYSRVEYVGDVPIVEECPRDVKTINGEPPLLFGKWSFENVVVRDPGLRRYICLKPVVLPHTEGRYQNYRFGKARIPIVERLINLMMRPGRNAGKKHKAYNIVKRAFDIVYYKTGQNPIQVFIDAIVNTAPREEITRIIMGGIAYSVSVDVSPQRRLDLALRWITEGARACSFNNPKPIEECLADELVAAAANDPKSYAVRKREELERIAAASR", "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": "MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAEDMSAHLISKLLERNGKVDPKEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTSAAQTVSRLCGSSMSALHTAAQAIMTGNGDVFVVGGVEHMGHVSMMHGVDPNPHLSLHAAKASGMMGLTAEMLGKMHGITREQQDLFGLRSHQLAHKATVEGKFKDEIIPMQGYDENGFLKVFDFDETIRPETTLEGLASLKPAFNPKGGTVTAGTSSQITDGASCMIVMSGQRAMDLGIQPLAVIRSMAVAGVDPAIMGYGPVPSTQKALKRAGLTMADIDFIELNEAFAAQALPVLKDLKVLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVATMCVGLGQGITTVFERV", "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": "MTITNEQVERINELARKKKAEGLSEAELEEQAFLRRAYLDSVKANFRSQVETIKVIDEKTGEDVTPDKLKEIQRKNGMRD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0291 family."}
+{"protein": "MDFLNDHINVFGLIAALVILVLTIYESSSLIKEMRDSKSQGELVENGHLIDGIGEFANNVPVGWIASFMCTIVWAFWYFFFGYPLNSFSQIGQYNEEVKAHNQKFEAKWKHLGQKELVDMGQGIFLVHCSQCHGITAEGLHGSAQNLVRWGKEEGIMDTIKHGSKGMDYLAGEMPAMELDEKDAKAIASYVMAELSSVKKTKNPQLIDKGKELFESMGCTGCHGNDGKGLQENQVFAADLTAYGTENFLRNILTHGKKGNIGHMPSFKYKNFSDLQVKALLNLSNR", "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": "MDLSVKSEENVEYMVEAIKEKLRMVNAGAMRAASFNEEMYEDLRDIYDHVMKRETFSISEMQAITEELGTLIKK", "text": "SIMILARITY: Belongs to the UPF0435 family."}
+{"protein": "MIIVTGGAGMIGSNIIKALNDTGYRDILVVDNLKDGTKFANLVDLDIADYIDKEDFIANIIAGDDLGEIDAIFHEGACSSTTEWDGKYMMDNNYQYSKDLLHYCLDREIPFLYASSAATYGGREEFIEERQFEAPLNVYGYSKFLFDQYVREILPEAESQICGFRYFNVYGPREGHKGSMASVAFHLNGQINRGENPKLFDGSQDFKRDFIYVGDVAAVNLWFLKSGVSGIFNCGTGRAETFQAVADAVVDFHQKGAVENIPFPEKLKGRYQAFTQADLTKLRAAGYDAPFKTVAEGVKEYMAWLNRTA", "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": "MALLQISEPGLSAAPHQRRLAAGIDLGTTNSLVATVRSGQAETLADHEGRHLLPSVVHYQQQGHSVGYDARTNAALDTANTISSVKRLMGRSLADIQQRYPHLPYQFQASENGLPMIETAAGLLNPVRVSADILKALAARATEALAGELDGVVITVPAYFDDAQRQGTKDAARLAGLHVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSRGVFEVLATGGDSALGGDDFDHLLADYIREQAGIPDRSDNRVQRELLDAAIAAKIALSDADSVTVNVAGWQGEISREQFNELIAPLVKRTLLACRRALKDAGVEADEVLEVVMVGGSTRVPLVRERVGEFFGRPPLTSIDPDKVVAIGAAIQADILVGNKPDSEMLLLDVIPLSLGLETMGGLVEKVIPRNTTIPVARAQDFTTFKDGQTAMSIHVMQGERELVQDCRSLARFALRGIPALPAGGAHIRVTFQVDADGLLSVTAMEKSTGVEASIQVKPSYGLTDSEIASMIKDSMSYAEQDVKARMLAEQKVEAARVLESLHGALAADAALLSAAERQDIDDAAAHLSEVAQGDDVDAIEQAIKNVDKQTQDFAARRMDQSVRRALKGHSVDEV", "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": "MTTTQKHDLFTPEPHYVPGYAGFFPQLRYQVGNTYGRTTGQLLTDPSVQKSPCSVLSPMSKPKFIEDFSQSKPPRVPCQDLTEPYIPHYTSLKPSKNFEILGQLPPLEVDAQEPPGVENIPRQILLPAGFTPDTPHPPCPPGRKGDSRDLGHPVYGEEAWKSATPVCEAPRQHQLYHCQRDEYPPPARRQQETLDVGSFQRLPQLDHPNLIQRKAISGYAGFIPRFTWVMGLNYRDGVMQAMDEFDKSQFLFRNPHCDLGEKLPGTHWPSNHIYSSQGLIPFYMGFIPAMQDNYALTFGNSTRRAYWKEWAKRNHTL", "text": "SIMILARITY: Belongs to the UPF0605 family."}
+{"protein": "MVDMKASMFLTFAGLVLLFVVCYASESEEKEFPKEMLSSIFAVDNDFKQEERDCAGYMRECKEKLCCSGYVCSSRWKWCVLPAPWRR", "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": "MGTSPFVLPFAALEVGQHLYWQIGKLRIHGQVFMTSWILIGALLTLVVVGTKKMERDPKGVQNLLEFLWDYIRDLARTQIGEKVYRDWMPFIGTLFLFIFVSNWGGALIPWKLIELPSGELGAPTADINTTVALALLVSLSYFYAGLSNKGLRYFEYYVHPTPIMLPFKIVEDFTKPLSLSFRLFGNILADELVVAVLVFLVPLVLPVPVMFLGLFTSAIQALIFATLAAYYIGEAVEEHH", "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": "MADEDIQPIVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQAKRGILTLKYPIEHGIVNNWDDMENWHHTFYNELRVSPEDHPVLLTEAPLNPKANREKMTQIMFETFECPAMYVAIEAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYTLPHAILRLDLAGRDLTDHLMKILTERGYSLTTSAEREIVRDIKEKLAYVALDYEQELETAKSSSSVEKSYEMPDGQVITIGSERFRCPEVLFQPSLVGMESPSVHEATYNSIMKCDVDIRKDLYGNVVLSGGFTMFPGIADRMSKEITSLVPSSMKVKVVAPPRRKYSVWIGGSILASLSTFQQMWISKGEYDETGPGIVHMKCF", "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": "MNPQELKSILSSGLLSFPVTDFNAQGDFHRAGYIKRLEWLAPYGASALFAAGGTGEFFSLAASEYSEIIKTAVDTCATSVPILAGVGGATRQAIEYAQEAERLGAKGLLLLPHYLTEASQDGVAAHVEAVCKSVKIGVVVYNRNVCRLTPTLLEQLAERCPNLIGYKDGLGDIELMVSIRRRLGDRFSYLGGLPTAEVYAAAYKALGVPVYSSAVFNFVPKLAMDFYHAIARDDHQAVGKYIDDFFLPYLEIRNRKAGYAVSIVKAGAKIAGYDAGPVRAPLTDLTSDECDMLAALMDKQGKQ", "text": "SIMILARITY: Belongs to the DapA family."}
+{"protein": "MAGKKGSSPNVYAYFKVDGDKVSRIKKVCSRCGKGTYMSEHKDRNTCGKCGLTEFKQ", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS31 family."}
+{"protein": "MSSYFVNPLFSKYKGGESLEPAYYDCRFPQSVGRSHALVYGPGGSAPGFQHASHHVQDFFHHGTSGISNSGYQQNPCSLSCHGDASKFYGYEALPRQSLYGAQQEASVVQYPDCKSSANTNSSEGQGHLNQNSSPSLMFPWMRPHAPGRRSGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKLPGARDEEKVEEEGNEEEEKEEEEKEENKD", "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": "KQFTKCELSQVLKDMDGYGGIALP", "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": "MTIAIGQEKTRGGFDLVDDWLKRDRFVFVGWSGLLLFPCAYLAVGGWLTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSMGHSLLFLWGPEAQGDFTRWCQIGGLWAFIALHGSFGLIGFCLRQFEIARLVGLRPYNAIAFSGPIAVFVSVFLMYPLGQASWFFAPSLGVAAIFRFLLFLQGFHNWTLNPFHMMGVAGILGGALLCAIHGATVQNTLFEDGDAADTFRAFTPTQSEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWTSAFGIVGLALNLRAYDFVSQELRAAEDPEFETFYTKNILLNEGIRSWMAAQDQPHENFIFPEEVLPRGNAL", "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": "MAALSTGLSTSSGDLTQSADEDGFLDAPLLPSQKLQSVIRPHFHPVPTICISILLALVNLAYVTLAVVAIYFCLFSEKEKKCKQSIDPFQLSTVLVISKLVLWLLHVVNERFAQHHHCKARSRGFLHLYRSTRHLKALPLIIHSTGNAALLLILSVQDSFTSNSQLYPCLILSVLLLELILSVICLIIYTVRIYRFNKSKPRPDIIEEEKINAFHGHVNPEIGFRHSASLEEVVEKQGDTIEYLKHHNALLSKQLLALASNQD", "text": "SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Late endosome. SIMILARITY: Belongs to the TMEM192 family."}
+{"protein": "MSINVKSVIEAALFIAGNEGVHKDKLKSISRLSVQDFEAVMEEMIFEYEKDPQRGLVVRKVGENYKLFTKPDISKIVASGFGIKQKNPLNQGMIETLAIIAYNHPCTRSQIHELRKTDPTPMLEKLIEIGLVEEAGRSEAVGKPYLYQVTPKFYDIFGLDSIKDLPEIVLPEQKIEELTYEEEINFFDTNREDNGDE", "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": "MSNSSARPESLGEYLAHLPLSDEQRAELASCTSFSELHQRLAANPAASSAEAVQASVGPRLTVGSAAELEEAEMLGVDGSGRLCLKIAPPIKRTKVVPEPWRTNVLIRMWRRMTGRPNAPQPPKRELPPARWRTVGSIRRYILLALMIGQTIVAGWYMKGILPYQGWSFVDFDEIVNQPLWDTVVQVWPYALQTSILILFGILFCWVSAGFWTALMGFLELLTGRDKYKISGSSAGNEPIAPEARTALVMPICNEDVPRVFAGLRATFESVAASGNLDRFDFFVLSDTNDTDIAVAEQQAWLDVCRETKGFGRIFYRRRRRRVKRKSGNLDDFCRRWGGEYKYMVVLDADSVMSGECLSSLVRLMEANPDAGIIQTGPKASGMDTLYARMQQFATRVYGPLFTAGLHFWQLGESHYWGHNAIIRMKPFIEHCALAPLPGKGAFAGAILSHDFVEAALMRRAGWGVWIAYDLPGSYEELPPNLLDELKRDRRWCHGNLMNFRLFLVKGMHPVHRAVFLTGVMSYLSAPLWFLFLVLSTALLATNTLMEPQYFIEPYQLYPLWPQWHPEKAVALFSTTIVLLFLPKLLSVILIWAKGAVEYGGRVKVTLSMLMEMLFSMLLAPVRMIFHTRFVLAAFLGWAATWNSPQRDDDSTPWGEAVRRHGPQTLLGIAWAALVAWLNPSFLWWLAPIVGSLVLSIPVSVISSRTRLGLAAKDEKLFLIPEEYATPQELLATDQYTHENRWHALHDGFVRAVVDPRQNALACAMATARHGQAAPIEALRAERVAKAIEVGPKGLDLNTRLALLSDPVALSRLHEQVWAEHNAAWIDVWRASINNDPHSPLLPLHPENAGQPSLVGA", "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": "MTNWQQQLPLTDTQKNELDKSVLRYLNWNYKQTVRHEHAQDYESVRHAIVTLSGFLLQESVDRQEFISNNDTSNESMVDIDELLLPKKWNSIVRLQKKIIELEQNTETLVSQIKDLNTQVSELAQFKPTTSNGTSAHNVLKWIPRNLPSCLINVESSVTSVKLHPNLPIVFVATDHGKLYAFDLFNYTIPLASLQSHTKAITSMDVLFTNFTNSSKKNYLVVVTASKDLQIHVFKWVSEECKFQQIRSLLGHEHIVSAVKIWQKNNDVHIASCSRDQTVKIWDFHNGWSLKTFQPHSQWVRSIDVLGDYIISGSHDTTLRLTHWPSGNGLSVGTGHEFPIEKVKFIHFIEDSPEIRFRTPSTDRYKNWGMQYCVSASRDRTIKIWEIPLPTLMAHRAPIPNPTDSNFRCVLTFKGHLSWVRDISIRGQYLFSCADDKSVRCWDLNTGQCLHVWEKLHTGFVNCLDLDVDFDSNVTPRQMMVTGGLDCKSNVFMR", "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": "MAVGIVGWGAYIPRYRIKTREIAEAWGDDALRIRDMYLVEEKAVGYIDEDPVTMAVEASRDALIRAGVKPSEVGAVFAGTESKPYAVKPISSILIDALGLNRQVYSVDMEFACKAGSDAIINLMGLVKANSIKYGIAVGTDSSQGEPGEHLEYTVGTGAVAYVIGSSNLAAEIKYTYPYASDTPDFWRRDSSPYPVHGEGFTGEPAYFKHIIGAAKGLMDELGMKPNDFDYAVFHQPNARFPVRVAQMLGFPLEKVKPGIVVDLIGNTYNASALLGLAKVLEEAKPGAKIIVVTFGSGAGSNAFYIETTDQLPGKVKLARTIGEMLEDKVYIDYSLYLKYRKIIKMIHG", "text": "SIMILARITY: Belongs to the thiolase-like superfamily. UPF0219 family."}
+{"protein": "MQYQVDTHTHTVASSHAYSTIHDYIAVAKQKGIRLFANTDHGPAMADAPHFWHFVNLRVLPRMVDGVGILRGIEANIKNIDGEIDFFGDYLKQLDIVLAGFHEPVYPPSDKATHTEAMINTIKSGKVDIITHPGNPAYPIDIEAVARAAAEYGVALEINNSSFEVSRKGSEANCTAIAKAAKEFGTILVMGSDSHVAFSLGGFARAQAIIDEVAYPPSRLLNRSPSALLTFLAARGHETVADLIPLFSDDEPCC", "text": "SIMILARITY: Belongs to the PHP family."}
+{"protein": "MLKKTLAALAIGTALLSAGQVMAADYKIDKEGQHAFIDWKISHLGYSYIHGTFKDWDGTFSWDAAKPETSKIAVDVKTASLWSNHAERDKHIASKDFLDVAKFADAKFVSTAVKSTGEKTADVTGDLTFHGVTKPVTFKATFNGEGKDPWGGERAGFNAKTTVNLNDFGIKGPGPSSQTVDLDISLEGVKQK", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the UPF0312 family. Type 1 subfamily."}
+{"protein": "MSQEDEYLSVEQFLELQKAETREIIESLKADGSEPDALYAIEHHLMAEDFKALENAVVEAFKMGFEVLEAEELEDEDGAKILCCDAVMDSALDAEVIDAQVEKLVNLAEKYDIIYDGWGTYYEGEDAEYDVIEDGDED", "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": "MKHIIHFDCFAGISGDMTVAALLDLGVPLEHLRDELARLDLPRDSYSLSIHRTERRHLAALRFDVQVLDQRTERGYAAIDGLIAASSLSGPVRERARAIFRRLAEAEALVHGVAVGEVHFHEVGAVDSIVDIVGTAICLDYLGVDGLSAAPLPLGSGFVHTAHGVLPVPAPATAELLKGMAVHGECGPGERVTPTGAAILAALATSVTAQPAMTVTAVGSGAGSRDFPDVPNILRAFLGRPEGEMSDGVLVAETNIDDSTPELLGYVMELLLEAGALDVFFTPIQMKKNRPGVQLSFLCRSGLLERLAALVLVETSAIGIRHYPVSRTTLERCMEERETPFGPLPFKLLFHDGRPLRAAPEYEACRRVARERGIPLQEVIRIVSQPTVVEGG", "text": "SIMILARITY: Belongs to the LarC family."}
+{"protein": "MDTMDTMGRHVIAELWDCDFDKLNDMPFIEQLFVDAALRAGAEVREVAFHKFAPQGVSGVVIISESHLTIHSFPEHGYASIDVYTCGDRIDPNVAAEYIAEGLNAKTRESIELPRGTGSFEIKQRETKAL", "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": "MSVPFDPASYDRQLEEKTVRLRELLAPFDAPEPQVFDSPREHYRLRAEFRLWREDQKRYYAMFAPGDNRTPILLEGLPIASERINALMPVLRERWEASPTLNHKLFQVDFLTTLAGDAMITMCYHRPLDAEWQAAAEQLAAELNVSLIGRSKGQKLIIGQDYVTEKLDVAGRTFSYRQPEGAFTQPNGTVNGKMLNWAFDALGERQDDLLELYCGNGNFTLPLATRVRKVLATEISKTSVNAALSNLDDNGVDNVTLVRLSAEELTEALNEVRPFRRLHGVDLKSYDFGSVFVDPPRAGMDPDTCELTRRFERILYISCNPETLAANIAQLHDTHRVERCALFDQFPYTHHMESGVLLVRR", "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": "MDLITSLQEITKLSHLYYERQWMYATAGNLSTRDGSSRDQFWITASGKHKGELKDTDFVCVSVADGTLLKASDGLKPSAETSIHQVLYSQMPDIGCCLHVHTIDSNLLEFGVGKEEGSREIPIPPIEIIKAFGIWDEKPNLTMPVFYNHTHVPTIADEIKRYFISVGIPKVPFLLIEGHGPTVWGKSIAEANKHLEAVHFLLQVMARKV", "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": "MKRIAVLTSGGDAPGMNAAIRAVVRQAISEGMEVYGINEGYAGMVAGDIHELSARSVGDIISRGGTFLCSARYPEFAKLEGQLKGIEQLKKHGIEGVVVIGGDGSYHGAMRLTEHGFPAIGVPGTIDNDIVGTDFTIGFDTAVTTAMDAIDKIRDTSSSHRRTFVVEVMGRHAGDIALWAGIASGADVIVVPEEDFNINDVVDRIKAGYDKGKKHSIIVLAEGVMPAAQFAEELKAAGDTSDLRVTELGHIQRGGSPTARDRVLASRMGAHAVKLLKEGRGGLAVGIRNEQMVENPILGTAEEGALFSLTTDGKIVVNNPHKADLELADLNRNLSI", "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": "MKAIVVKPPKPGVEVRDLSQVIRHGSGTVKVRILENGICGSDREIVKGELTTARPPEGRDWLVLGHEALGIVEDSSDPRFKPGDLVMPINRRSYHGKCLNCLVGRPDFCEANEFVEAGMVGMDGFMVEYWYDDPKYLVKVPKDIADIAIVAQPLSDLEKSVEEILNVQRRFIWTCDDGTYNCRRSIVFGTGSTGILISLLLRTVGFEVYVANRRDPLESEAKITEEAGIIYYNYSKDGLDKLKSMGFDLVVDTTGASASLIGHEVEMLKPNGILGLFGFPSEGELTLRYDVIQRFIYKSNAIVGLINGQKPHFQQALAHLAQWKVVWPTVAKSLITRVVDVNNDKELLQVLNHKERGEIKVKIKWS", "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": "MNKLMLMLITFATSLLAQTNKASTGLKTDQSFNNSLSESVKLKEIADIYPTNTNFLTGIGIVAGLAGKGDSIKQKDLIIKILEENNIINEIGSNNIESKNIALVNVSLQVKGNTIKGSKHKACVASILDSKDLTNGILLKTNLKNKEGEIIAIASGITQPNNKLKGSGYTIDSVIINENQNINHSYNIILKKGNYTLINRIHKILTSKKINNKIKSDSTIEIEAKNISLLEEIENIKIETNPKILIDKKNGIILASENAKIGTFTFSIEKDNQNIFLSKNNKTTIQVNSMKLNEFILKNSNNLSNKELIQIIQAAQKINKLNGELILEEIDGNQN", "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": "MAVTFPPKISPTLMTPDPHFIPGYSGFCPQYRYSLGKTYGQLTSHLLTNPDIRRSGHLVLQSNPFPPAPRGHSYNEASQELGGRRRRQRLGDPKLTISMIPGYTGFIPRSQKFFAKTYAETSWDALSDFHNEQQMQESQRQEMLLTSKLQEGRQPQTEHEKQLLTARHRTPLPALSKEPAPFMSLRGFQPQGSPYYMEEENPNKYFISGYTGYVPRSRFLIGNGYPITTNRAMVEFAHMNQKKGVRFSDQQGHNEGDNLHTEQGQIYLEELGLLPRYTGYVPGYKFQFGNTFGRLTQNALGQSTLQKQTVN", "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": "MTTAAVFGSTGAVGGQILATLLASDAFSSVKTVSRRLPNAQSPKLQTLEEGDITKWGGLIASLSPKPSIVFNAVGTTRAAAGGIANQWKIDHDLCIENAKAAKEAGVKTYVFISSGGTRGFFSRYVPYSKMKIGVEDAIKELDFEQAIILRPGLILQREKPKAALLENIVQNLNKLGQGVQDMIGQDQTVIGRAAVAAARMAEEGKAPSKYWVLEQADIVRLGRDEWKQ", "text": "SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein. SIMILARITY: Belongs to the FMP52 family."}
+{"protein": "MITLTHYLVLGALLFGISAMGIFMNRKNVLVLLMSIELMLLAVNFNFIAFSQHLGDTAGQIFVFFVLTVAAAESAIGLAIMVLVYRNRQTINVADLDELKG", "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": "MEHPVFERDPSQKSEAERREVPPLLKLALELGPLLVFFFANARGEMLIERFPVLASIGAPIFLATALFMGATVIALAISWTMTRTLPIMPLVSGIVVLVFGALTLWLHNDTFIKMKPTIVNTLFGAILLGGLFFGKSLLGYVFDSAFRLDAEGWRKLTLRWGLFFIFLAVVNEVVWRNFSTDAWVSFKVWGIMPITIVFTLLQMPLIQKHSLTEDNKTAS", "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": "MPFLKPSKVSLKRILQGNPPKPIGLTEYGHLLRLVGLREADSKEENERTILKLNEGIIQMHAIERLDTSFIKEPFRTLNHAINAESLPSLPDQEPWNVFQNAKKRDGQYFAVYSKLKDDSSNESPNKQ", "text": "SUBCELLULAR LOCATION: Mitochondrion."}
+{"protein": "MAMRFFQLHRNRLVKGNSGKALSFSRLLDLSFWVRAFCNYREILRNGLHSLQFNEALDLFTHMVESRPLPSIIDFTKLLNVIAKMKKFDVVINLCDHLQIMGVSHDLYTCNLLMNCFCQSSQPYLASSFLGKMMKLGFEPDIVTFTSLINGFCLGNRMEEAMSMVNQMVEMGIKPDVVMYTTIIDSLCKNGHVNYALSLFDQMENYGIRPDVVMYTSLVNGLCNSGRWRDADSLLRGMTKRKIKPDVITFNALIDAFVKEGKFLDAEELYNEMIRMSIAPNIFTYTSLINGFCMEGCVDEARQMFYLMETKGCFPDVVAYTSLINGFCKCKKVDDAMKIFYEMSQKGLTGNTITYTTLIQGFGQVGKPNVAQEVFSHMVSRGVPPNIRTYNVLLHCLCYNGKVKKALMIFEDMQKREMDGVAPNIWTYNVLLHGLCYNGKLEKALMVFEDMRKREMDIGIITYTIIIQGMCKAGKVKNAVNLFCSLPSKGVKPNVVTYTTMISGLFREGLKHEAHVLFRKMKEDGVS", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PPR family. P subfamily."}
+{"protein": "MIYRNWSLLSSTVVIWGGVATAGLAGIFLFGGKEKFQNYLCREGERLRQQDRAAMGKN", "text": "SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein."}
+{"protein": "MAHKKGSGSTRNGRDSNSKRLGVKKYGGEQVTAGNILIRQRGTKVKPGQNVGKGKDDTLFALIDGFVLFEKSNQKQKTISVYSSKN", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
+{"protein": "MAKGIMTYDVGEQVDLHLLIKSSTKGIASNGKPFLTLILQDQSGDIEAKLWDAKQNDEQTYAAQTIVKVVGDIHHYRGRNQLKLRNIRPVAENEQIRIDDFLETAPIPKHDMMDTIMQYIFDMKNPNIQRVTRHLLKKYGQEFADYPAATKNHHEFVSGLAYHVVSMLHLAKSIVDLYPSLDRDLLYSGIILHDLGKVKELSGPVSTTYTVEGNLIGHISIMVTEIAKAAEELGIDSEEILILQHLVLSHHGKGEWGSPKPPMVKEAEILHYIDNLDAKMNMMDRALEHVKPGEYTERIFALENRSFYKPTFHE", "text": "FUNCTION: Shows a 3'-5' exoribonuclease activity. SIMILARITY: Belongs to the YhaM family."}
+{"protein": "MDSKNCVVIAIAGASASGKSLIANTIYQELCEELGTNQIGMISEDSYYRDQSHLELELRKLTNYDHPKAFEHELLCSHLKMLKENCSVNIPVYSYTEHTRTLESETMTSKKVIILEGILLLNDSALREQIDVSIFIDTPLDICLMRRLVRDMAERERTMDSVLLQYTKTVRPMFLQFIEPSKQHADIIVPRGGKNRIAKDLLKTRIKYLLGK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the uridine kinase family."}
+{"protein": "MREVLYMTDKKNLRTPIVCVMGHVDHGKTTLLDKIRGTAIVSGEAGAITQHIGATEVPIDVIVNKLGDPKLRDRFMVPGLLFIDTPGHHAFTTLRSRGGALADLAIVVVDINEGFKPQTYESLQILKRFKTPFVVVANKIDRIGGWASQKDMPFAATFKKQSPDVQGRLETKLYEVIGELYNQGFAAERYDRVTNFQKTLGVVPASAVTGEGIPDVLMVLLGLAQKFLEANLQYSAKNPGVGTVLEVKEEKGLGATLDVILYDGTLKKGDTVVIGSLGEPIQTKVRALLKPRELSEIRYESKFKQVSEVTAAAGVKISAPGLDGALAGSPIRVATEETLGEIVAQVKSEIDEVRIDTGSVGVMIKADTLGSLEALVHEFQKDEVPIRKAEVGDISHRDAVEASTVEDPLYSVLIGFNVKVHPDARDFLQESTVKVFTSDVIYRLVEDYQKYVKEQQELAEKKIFETIIRPGKFKILPGCVFRQSKPAVVGVRVLGGVVRTNADVMLENGNVVGKIKGLQSEGENIPSAKVGKEVAMAIEGATVGRQIKEEDVLYINVPERHAKVLEHEIYDSLSTDEKETLDIFLTLKRKNNPFWAK", "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": "MKFFQEQIAIKETNILLKVDNPKFFKMAKNAVINERLNLENYILRNPIFLTSYSPLEVPDNAPKIVKLMAEAGFNADVGPMAAVAGTFSQLIVENLIENDCKNAISENGGDICLKCEMDTTVGLYAGNSSLSGNLGFKLKKEKMKNGYGICTSSGTVGHSVSFGNADSVTVFSKSAIIADAAATSIGNFAVGNAVDAMNNCLEKAETISKIDGVFVCMGEHAGKIGKIPQLIKTDKKEVLGNVFEMV", "text": "SIMILARITY: Belongs to the UPF0280 family."}
+{"protein": "MVKSDNITWHQSQVSKAERQALNHHKSVVLWFTGLSGSGKSTIANAVEKALFDQQVGSYVLDGDNMRFGLNKNLGFSAEDREENIRRIGEVAKLFVDAGVITLTAFISPYRADRDKVRANLEVDEFIEVFVDTPLEVCEQRDVKQLYAKARRGEITGFTGIDAPYEAPIDPEITIDTSKQPLTASVQQVLNYLAEHHYVSLVTANEN", "text": "FUNCTION: Catalyzes the synthesis of activated sulfate. SIMILARITY: Belongs to the APS kinase family."}
+{"protein": "VLSPADKTNVKAAWAKVGNHAADFGAEALERMFMSFPSTKTYFSHFDLGHNSTQVKGHGKKVADALTKAVGHLDTLPDALSDLSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPGDFTPSVHASLDKFLASVSTVLTSKYR", "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": "VEWTDAERKAIASL", "text": "FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. SIMILARITY: Belongs to the globin family."}
+{"protein": "MDVRQSIHSDHAKTLDTAGLRREFLIETIFVADEYTMTYSHIDRIIVGGVMPVNRTVSVGSEVGKQLGVSYFLERRELGVINIGGPGLITVDGTRYEMNSRDGLYVGKGAKEVVFESADAANPARFYYNCAPAHTTFPTKRVTPADVSPVHLGEDVTSNRRTINKYFIPDVLETCQLSMGLTELAPGNLWNTMPCHTHERRMEVYFYFGLEENSCVFHMMGQPQETRHIVVQNEQAVISPSWSIHSGVGTRAYTFIWGMVGENQVFDDMDHVAVKDLR", "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": "MNTNADPAEVQKFSDLAHRWWDPASEFKPLHEINPLRLDWIDGHCGLAGKKVLDVGCGGGLLSEGMAQRGAEVSGIDLSEKALGVARLHLYESGLQVDYQLTSAEAHAATHPAQFDVVTCMEMLEHVPNPESTVHACAQMAKPGGAVFFSTLNRNFKAYLFAVVGAEYLLNLLPRGTHDYAKFIKPSELSRYCRNAGLELVSLSGMTYNPITKVYALSRDTDVNYMVHARKLG", "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": "MKLYQKFPETQVLTTQGVIDFYKDIFGKGKWLFLFAHPADFTPVCTTEFVEFSKAYNDFANLGVQLVGLSVDSVYSHIEWLKDIQEKYGIKVPFPVIADPDKKFARLLDIVDEASGQTIRGVFLVSPDGVIRFIAYYPLEAGRKISELLRITKAMIVNYKAKVVLPANWEPGQDVIVPPPNVFDEATMRMKMPKAKSWYLLFKDYNELPQDQKV", "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": "MDPYKVIVRPVVTEKAISMVERENKLTFIVDKRATKPDIKKAVETVYEVKVDKVNIVITMKGEKKAYVKLKPEYSASEVAARIGLF", "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": "MKLFQLTLFLLVNAFLALASSESVDVESSSNETAVEEPSTIDFDVGYNILEHLDTDLSRGVEFSMQEVATFNYSFTNNEKVNVSVVGVAGSVISTPDGYQVANITEQPIGPVPIGVNETANFQAGVQLILPEGNFYMLPVLNVMKDGEPLRVGIRPLLITVNPPPLSFFNPSFLSVQILLGLLIAGATYAFITFDKSETKRKPAKNAKPVAVDQSWLPDTYKKPEKP", "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": "MEEEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKILAERGYSFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSRLEQSYELPDGQVITIGNERFRAPEALFQPSVLGLESGGIHVTTFNSIMKCDVDVRKDLYGNIVMSGGTTMYPGIADRMQKEITALAPSSMKVRIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "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": "MDTHTTKLVAISLLLLLVISDYTRLMIQVHSYVPFCAYTYDYFSYCLDFLTGYYYKPGKKCCVHIVKLNIIAKHKKENPRLLCNCVEMMTRGYTPPMLADKIQQLPLLCNTHLSFPISSSMDCSTV", "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": "MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGIYALDTGCCWGGTLTCLRWEDKQYFVQPSNRHKDMGEGEAAAS", "text": "FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. SIMILARITY: Belongs to the Ap4A hydrolase family."}
+{"protein": "MLINRWLFSTNHKDIGTLYLLFGAWAGVTGMALSLLIRAELGQPGNLLGNDHIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRLNNMSFWLLPPSFLLLMASTAVEAGAGTGWTVYPPLSGNFSHPGASVDLVIFSLHLAGISSILGAINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPVGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTHYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTMGGLTGIILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFSGYTLDQTCAKAHFIITFMGVNLTFFPQHFLGLSGMPRRYSDYPDAYTTWNILSSMGSFISLTATILMIYMIWEAFASKRKVLLTEHPSTSLEWLNGCPPPHHTFEEPAYIKL", "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": "MNESGSIGIIETKYAEFKELPLKNGSVLSPVVIAYETYGTLSPSKNNAILICHALSGDAHAAGYHSESDKKPGWWDDYIGPGKSFDTNQYFIICSNVIGGCKGSSGPLSIHPKTGTPYGSRFPFVSIQDMVKAQKLLVEFLGIDKLFCVAGGSMGGMQALEWSIAYPDSLLNCIVMASTAEHSAMQIAFNEVGRQAILSDPNWNNGLYNENSPRKGLALARMVGHITYLSDDKMREKFGRNPPRGNILTTDFAVGSYLIYQGESFVDRFDANSYIYVTKALDHYSLGKGKELTAALSTATCRFLIVSYSSDWLYPPAQSREIVKSLEAADKRVFYLELQSGEGHDSFLLKNPKQIEILKGFLENQSSP", "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": "MRRVVILWNPDDPASKNIAESLTEDAEKLDTEDLQHYTVETWERDGVRFHLTAALGDLIEEDEARELARKFDVIVFASRHESRTKKPSLTVHVPGNPTPEAKFGGKPLEVCTADPAGMKAALLELKRFRDKRGLDYDVCYEVTHHGPRDPGAPCFFIEIGSDEERWTDEEAGEACARAILAAVDPPDVKAVVGYGGGHYAPAHTDAALSNRKLAYGHIVPDYAVDHDYLRDQFREVVDKTPRAREIIVDDRNLDSGIVERLEDLVRDRGLRLRDVEEVK", "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": "MAQKIRKSTFKKDKNSSINGVVHIQSTFNNTIVTITNITGDTISWASAGSSGFKGARKGTPFAAQTAAEKAALDALSKGMKSVEVLVKGQGSGRETAIRSIEGAGFEVTSIQDITPVPHNGCRPPKRRRV", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
+{"protein": "MSIRFPEIPGTTRAPGTSLSSRGIFPTSPGVPQIPTTPNSYSALLHPHKSEAKGKHPLSFSSSMTKRLTPQEKKARRPTSRACVFCHSKHLQCSHSRPCQNCIKRNLAHECRDVVRKRAKYMSTTEVPAVSGESSSESGRATGENGSEMGNPPDPQIAYLDGVFERSSIHESLQDSPMSTPASNFNSNFLNQEYMMLGDLISKPSSPSLDVPMMYAENPSRPFISLGQSDERPKSPEFNNFDFSSLDKAQYVSPLVSHHIYQNVQDIYANKVIDFDYPSSYHSLTSFLRQRFSFTGKSLSDSEKAKKRENLLMILRLIASYRPTFISTHKALFRPFDFQFLEMSFQRCLLDYENLSRLNASPTIIWRRTGEIVSMSNDLVALLGLNISTILSKRTFILELMYDDESIVEYFRLFESVAVGNLHSTIVTRCKLIKRPSEGIETNTSMDSDYIEFCSVWTVKRDLFDLPMMVVGQFLPVLPTPDGFRTY", "text": "FUNCTION: Transcription factor which regulates nonfermentable carbon utilization. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ERT1/acuK family."}
+{"protein": "MPTLLLGASIPFGTIAYTLFIFLLLLVMLRKFAWGPLMGIMKEREEHVTNEIDAAERSNAEAKKLVEEQREMLKQSRVEAQELIERAKKQAVDQKDVIVAAAKEEAESIKTSAVQEIQREKEQAIAALQEQVASLSVHIASKVIEKELKEEDQVKLIRDYIKEVGEAR", "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": "MLTLKVFVYTVVTFFVFLFIFGFLSNDPARNPGKGNLD", "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": "MTKNSTECSPANQTGLERVLRSPAIAGLVLLVSMLVAFFWVNSPFADSYEAIHHAPAAISIGSFELAKPLILWINEGLMIVFFFLIGLEIKREVFEGQLSSPKQIALPAFAALGGMLVPAAIFLAFNNGSEEYVRGWAVPAATDIVLALALLAMLGSRVPIALKVFLTALAIFDDFGTLVIIALAYSEGLSLPSLLMAALGTLALIVLNRLRVASLTAYVLVGVFVWVSVLESGVHSTLAGVIIAWCIPMRVSGREFLHKIEHDLSPWVALLIVPLFAFFNAGIDLGGVDFETFFGPLGLGIILGLFVGKQVGVMLGVGLAVVLRIGARPIEVSWGHLYGAALLSGVGFTMSLFVAGLAFEQPGAVLTVNLAVVVGSVLSATGGLVVLARSYQTSPSLANAPD", "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": "MPKIEMEPLRRRELIDAAIRTIGQRGSLDVTVAQIAHEAGVSPALAHHYFGGKDKLILATMRHLLRELGRDLNAAIKQANTPHERIAAIIAVNFSAAQFAQETIAAWLTFYVHAQQSDDIKRLLRIYARRLHSNLVFALEQLTSRARANRIAEGAGAMIDGLYIRHALGADAPDAASAIALVEDYIAIQLSGQPSAEN", "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": "MKQRSFLSILCFILLAFGVASVSAQTCIENRKYFTPNGTYDSNRRLILSSLPNNTASQDGFYYGSIGEEQDRVYALGMCIPRSTPSDCFNCIKGAAGWLIQDCVNQTDAYYWALDPTLCLVRYSNISFSGSAAFWEIEPQYLVLNTATIASDLTDFKNIWEDLTSRTITAASAARSTPSSSDNHYRVDFANLTKFQNIYALMQCTPDISSDECNNCLQRGVLEYQSCCGNNTGGYVMRPICFFRWQLFTFSKAFHNITLATPPKPPMNVPRPPSVGHGANTTDNDSRGVSAGIVVVITVPAVVIVLILVVLGFFICWRRKSLQRTEFESDSDVSTTNSLQYEFKTIEAATNKFSKSNKLGEGRFGEVYKGKFSNGTEVAVKRLSKVSGQDTKKFRNEAVLVSKIQHRNLARLLGFCLQGDGKFLIYEFVLNKSLDYFLFDPEKQGELDWTRRYKIIGGIAQGILHLHQDPQLTIIYRDFKASNILLDADMNPKISDFGMATVFGMEESRGNTNWIAETFVYMSPEYAVHGKFSMKSDVYSFGILILEIISGKKNSSLYQNDETTTAGNLVTYAWRLWRNGSQLKLLDSSIGRNYQSNEVTRCIHIALLCVQENPEDRPKLSTIVSMLTSNTISVPAPGIPGFFPQSRRELDPLSEGLESG", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CRK subfamily."}
+{"protein": "MTTQFSVSGIELELFRYPSRQESNLQAWDAADEHLIKHLIDTEQTSISTAVVNDGFGALTAGLLSINPSWPLTLETDAKTSQLGTSQNLTRNQLSQESITWVNSRDELPQVIELVLMKLPKNLNYFSHQLNRLSHVLPAGTQVLIGAKAKSINKSLLETIEKNLGPASASLTWKKTRVITCIADGKARALPKATTWSVPEFKLQISNLSNVFAANKLDIGARIMLDNMPKGDYKSIVDLGCGNGILGLHAKQVFPEAYIHFIDDSEMAVASARENWALNKLDNPALVGEQATFGWDDCLTNMSEGFRPDLVLCNPPFHQGEAITDHIAWQMFLDAFRRLKNGGILHVVGNRHLAYHVKLQRIFKNCTTVASNGKFVILQAQKISKKAQEAEVEQAFDTETPHPQSALYGKPKA", "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": "MKLYSVAYIPQSYEVLGLVKGSMVQSKHIGRDIMAGLKGIVGGEIKGYTEMLNDARNIATDRMIEEAHALGANGIIGISYVTSSLMSNTSEVLVYGTAVKILS", "text": "SIMILARITY: Belongs to the UPF0145 family."}
+{"protein": "MTDAAAVIERVRQRVDPTPAERRALAAAASRLTERAEAAIAELPVAADVVQVGSTARGTWVAGDRDIDLFVRFPSDLPREQLETYGTTVGAAVLPDGHEEYAEHPYVTGTFEGYAVDLVPCYDVAAATEIKSAVDRTPFHTTYLQEHLDDGLAADVRLCKQFLKGIGVYGSDLRTQGFSGYLCELLVVEYGGFEAMLAAIEDWQPPVVIDPAAHQQASFDDPLVVVDPTDPERNVAAVVSAANVATVQHHARRFRATPSEDAFTPASPAPLDAAALRSHIDRRDTTPLAVVLDAPDVVADQLYPQLYRSRDGVVRGLREHGFDVVRAAAWADERAVVFVELASAELPAVERHVGPPVSVGTHAERFYETYADDDGVYGPFVDDDGRYVVERDRDVRTAGGFARTELGTVALGARIESRVASGDYDVYVGDAVVEALLPEFESELAAYVDPKA", "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": "MERILYQVFPSDTNYSYDPPAVTAPSQGSSQTDFGKVVIALVVILVSVGVFYLAYTLFLKDCILLFKAKKQRTTTEIGFGQTPARNQDHPGP", "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": "MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGSALTHKWITTDFAEALLEFITPVDGDIEHMLTFMRDLHRYTARNMGDERMWPLSMPCYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVHYNFSLPMAFWQAKCGDISGADAKEKISAGYFRVIRNYYRFGWVIPYLFGASPAICSSFLQGKPTSLPFEKTECGMYYLPYATSLRLSDLGYTNKSQSNLGITFNDLYEYVAGLKQAIKTPSEEYAKIGIEKDGKRLQINSNVLQIENELYAPIRPKRVTRSGESPSDALLRGGIEYIEVRSLDINPFSPIGVDEQQVRFLDLFMVWCALADAPEMSSKELACTRVNWNRVILEGRKPDLTLGIGCETAQFPLPQVGKDLFRDLKRVAQTLDSINGGEAYQKVCDELVACFDNPDLTFSARILRSMIDTGIGGTGKAFAEAYRNLLREEPLEILREEDFVAEREASERRQQEMEAADTEPFAVWLEKHA", "text": "SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily."}
+{"protein": "MNLAIIAGDGIGPEVIGEAVKVLDAVLPEVEKTTYDLGARRYHATGEILPDSVLEELKVHDAILLGAIGDPSVPSGVLERGLLLRIRFALDHHINLRPAKLYSGVTGPLAGNPEIDFVVVREGTEGPYTGTGGAIRVGTPHEVATEVSLNTAFGVRRVVEDAFRRAQQRRKHLTLVHKNNVLTFAGALWWRTVQEVGAEYPDVEIAYQHVDSAMIHIVTDPGRFDVIVTDNLFGDIVTDLAAAVCGGIGLAASGNIDATRTNPSMFEPVHGSAPDIAGQGIADPTAAIMSVALLLAHVGETDAAARVDKAVEAHLSSRGDQELGTAAVGDRIVGLL", "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": "MSLFNTVRNTIVPVHKEGYPFVAAFFVASLVLGWIFKPLFWIGMIFTLWCAYFFRDPERVTPQDDDLVISPADGKVSAIQMVTPPAELDLGSEPMLRISVFMNVFNCHVNRAPMRGRIVSINYRSGSFVNAELDKASEDNERNGLVIETRHGQIGVVQIAGLVARRILCWANTNEPLDAGERFGLIRFGSRLDVFLPAGAAPRVSLGQTAIAGETVIAEFASAKGPVISRHS", "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": "MIEPILLGIVLGMVLVTLAGLFVAAYRQYQRGNKMGL", "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": "MKLSLMAAISKNGVIGNGPDIPWSAKGEQLLFKAITYNQWLLVGRKTFESMGALPNRKYAVVTRSSFTSSDENVLVFPSIDEALNHLKTITDHVIVSGGGEIYKSLIDKVDTLHISTIDIEPEGDVYFPEIPSSFRPVFSQDFVSNINYSYQIWQKG", "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": "MAFKIASSPHVTRNLHTSTVMQRVILCLLPGLVVQCAFFGWGTLIQVLLAIIVALSCEAAVMKLRNRSIKASLSDNSAMLTAILIGVAIPPLAPWWMIVMGTVFAIVIVKHLYGGLGHNLFNPAMAAYVLLLVSFPVQMTSWIAPSTVALNTPSVIDSLQLIFNVGAHGGMEQFRLGIDGISMATPLDTLKTDLSLGLTTTESMAKSIFDGGTGVGWFWVNLAYLAGGLVLLKLKAIRWHISTGVLAGLFVASSIGFLLSPDTQASPLFHLFSGATMLAAFFIATDPVTAATSPRGRLIFGALIGVLVYIIRTQGGYPDAFAFAVLLANLCAPFIDYYVRPRTYGHSAP", "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": "MVDDSTRKTLSNIPLLQIRAGPREKDVWVQRLKEEYHALIMYVKNNKQSGSDWFRLESNKEGTKWFGKCWYMHNLLKYEFDVEFDIPVTYPTTAPEIALPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGIAHAMALGLAPWLAVEVPDLIEKGIITYKEK", "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": "MFRFQSLDDDCTLEEEEGLVEEEDEIDQFNDDTFGAGAIDDDWQEEHTRLAELDERVRDVLPGAGDSDTSHGGSNAHSSVLPPPSSSSRLYPDIDERGGGDLAESLTRLILGSDPAIAGVGSTSSDRSHLPPMLSAHPPHPSALAGPSSLLRSYQQHQQFLHRGPAPLSQINSHSIWENSMGFSPVSVNSGLIGQKEDKTLLSIIKEVGLPNRPPSLSRDEGRDLSERVPPPRSSSPVIGSPPVRAVPIGTPPKQPMSQILNQQNNHPSAIHVRASVPMRFPPPFPERLSPNNLLSIAKSPLSHSPFPAGVNPVLSQIQRAQLLNSQVGQFQRGPAPPLLQGGVGGFRPFFGQSGPRIGPHGPPLGHAPIRHNTTHLHPQHRRMLSQRMQNRGDHVGGRGVGERKNRDPYSNLMTQREKEWVAKIQMMQLQSTDPYLDDYYYQNYYEKMEKRQERDRDNRKEHTTKLITPQVAKLEHTYRPVQFAGSLGKLTVSSVNNPRKMIDAVVTSRSDDEEKREKQVWNKRRQILYTVEKMYSLLLEVQDFEKKFLQTPEHQRDVLLEQHKTHTLQLYNSLREKEWDDRVSDEQCLMIMSVRKGKRLISRLLPFLPQPQAAAVVMGIARNLPALAKKDKQDQVLCWLVEPVSVVIQSMSSTSLTDLLQELQGSEGQLPLVLQNKFGVTLLYLILSEGERMQSSDPNCQLMDDNRWTELVFSVTRELLKVPSSALSSPLFTPPNLVSLFSRYVDRQRLELLQEKLQITALSR", "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": "MEINGNGHVSSPSLCLNKDPLNWGAAAEALTGSHLDEVKRMVEEYRCSTVRLEGADLKISQVAAVAAVASTVSVELSEAAKDGVKASSEWVRESMAKGTDSYGVTTGFGATSHRRTKQGGALQNELIRFLNAGIFGSGKESGNTLPASTTRAAMLVRINTLLQGYSGIRFEILEAITALLNANVTPCLPLRGTITASGDLVPLSYIAGMLTGRPNSKAVGPDGTTIDASEAFKLAGIPNGFFELQPKEGLALVNGTAVGSGLASTVLFDANILAVLSEIISAVFCEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILEGSSYMQMAKKLHELDPLQKPKQDRYALRTSPQWLGPQIEVIRSSTKSIEREINSVNDNPLIDVSRNKAIHGGNFQGTPIGVSMDNTRLAIAAIGKLMFAQISELVNDFYNNGLPSNLSGGRDPSLDYGFKGAEIAMAAYCSELQYLANPVTNHVQSAEQHNQDVNSLGLISSRKTAEAVEILKLMTSTFLVALCQAIDLRHLEENFKQAVKNTVSQVSKRVLTTGISGDLHPSRFCEKELVKVIDREYVFTYIDDPCSYAYPLMQKLRQVLVEHALSNGEKEKDANTSIFQKIAAFEEELKAALPKEVEAARVSVENGSAAIANRIKECRSYPLYRFVREELGARFLTGEKVVSPGEEFDKVFVGI", "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": "MFRTMMRAKLHRATVTEANLNYVGSITIDEDLMDAVNIVENEKVQIVNNNNGARLETYVIKGERGSGVVCLNGAAARLVQPGDKVIIICYGLVTEEEVHKQEPKIAVLDDNNQIIEMLGAEKAGTIL", "text": "FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanD family."}
+{"protein": "MWGGSKLSSSGSRFLGALRSGFQSTQVDSSRLTTSAVYPKNQLSWILQIKPWVFNENRIMWFKSYSITFACLNWMKSYRLPWTRPYSTSRTTVDKNEMKTFLALAHRWWDEQGVYAPLHSMNDLRVPFIRDNLLRTVATHQPGKPLSGMKILDVGCGGGLLTEPLGRLGASVIGIDPVDENIKTAQHHKSFDPVLDKRIEYRTCSLEEIVKDTVETFDAVVASEVVEHVIDLETFIQCCFQVLKPDGSLFITTINKTQLSYALGIVFSEQIAGIVPKGTHTWEKFVSPEKLESILESNGLSVQTVVGMLYNPFSGYWHWSENTSLNYAAHALKSSLQEQPAPAEFALKGEAEELQAEASTNSGVQEDLKK", "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": "MGITIENVSKSFGSFQAVKQVDLDIASGSLVALLGPSGSGKSTLLRLIAGLEMPDTGRILLTGKDATYQSVQERNIGFVFQHYALFKHMTVRQNIAFGLELRKVPRAKINARVAELLELVQLTGLGDRYPSQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRAWLRRLHDDVHVTTVFVTHDQEEAMEVADQIVVMNKGQVEQVGTPAEIYDHPASPFVMSFIGPVNVLRSRVFQQSEGTAAHCDIFLRPRDIIIETRPNGNTVSARIHRIIHLGWEIQVELRLDDGQELMAHLSRERFDELHLEPQQQVFIKPREAKSFPLYYSI", "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": "MSTKKIEQWEIERYWEIFASLSNGQPHLNSSQAASVLRNSRLRDEQLEKVWDLADVDGDGELDFEEFCVAMRLVFDLVNGELQEVPRVLPDWLVPESKAHLVQAGRALSGRPEQFERIEDEDDTPGLKDGFDWYMNPADKSKYEEIYSANRNHRGEVTFESLQGLYDSLDVPDTDVRSAWNLVNPSASPAINKDATLAFLHILNYRHEGFRIPRTIPASLRASFENNKIDYQVDNARPAQKWGADGSTETLTGRKTKFGDTYLSRLGVGGKGSYTPKGTDFSDTIQDEEWEKVRLRRELAEMEAKLDAANKASEGRRDRPRNDGRPNWVLIKKEALQLLEYKERELRELREGTGRAKEGQDLERLRDDIKTVGDQVEGLKAHLAERKDVLADVRRQIEEERLHR", "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": "MGDDELSEIRKRRMAQLQQQAGDQQAMQEEVERQQRLKSQIQMVLMQVLEPDARERLNTIRLTKPDFASAVEQQLVMLAQSGRLRQKITDAQLKDLLRQLAPAKRDYSITRK", "text": "SIMILARITY: Belongs to the PDCD5 family."}
+{"protein": "MGLEERLPGGILLSTVETVAGYVRKGSLWPATFGLACCAIEMMSTAGPRFDIARFGMERFSATPRQADLMIVAGRVSQKMAPVLRQIYDQMVEPKWVLAMGVCASSGGMFNNYAVVQGVDHVVPVDIYLPGCPPRPEMLLHAILKLHDKIQQMPLGVNREEAIREAEQAALAVPPTIELKGLLR", "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": "KIPCGESCVYIPCISSVLGCSCSNKVCYKD", "text": "FUNCTION: Probably participates in a plant defense mechanism. SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily."}
+{"protein": "MNAVTDLKQDYIVADIGLAGWGRKEIAIAETEMPGLMAIRDEFAAAQPLKGARIAGSLHMTIQTAVLIETLKALGADVRWASCNIFSTQDHAAAAIAASGTPVFAFKGESLKEYWDFTHRIFDWADGGTPNMILDDGGDATLLLHLGARAEKDASLIAKPTSEEETFLFAAIKEKLAKDSTWYSRNLAAIRGVTEETTTGVHRLYQMAQKGELKFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKIAVVAGYGDVGKGSAQALRALSAQVWVTEIDPICALQAAMEGYRVVTMDYAAEHGDIFVTCTGNYHVITHDHMAKMKDQAIVCNIGHFDNEIDIASVEKYEWDEIKPQVDHVKFPDGKKIIILAKGRLVNLGCATGHPSYVMSSSFANQTIAQIELWAERDSGKYPVGVYVLPKHLDEKVARLQLRKLNAQLTELTEQQAAYIGVKKEGPYKADHYRY", "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": "MSGLFETLGRRALFTFDAEQAHGLSITGLKTGIVTCRTPEDPALSVKVAGLKFPNPLGMAAGYDKNAEVPDALLKLGFGFAEVGTLTPRPQSGNPRPRIFRLVDDKAVINRLGFNNEGHEAAFKRLSRRAGKSGIVGVNIGANKDAEDRIADYVAGIRRFYQLARYFTVNISSPNTPGLRNLQAREALHELLSRVLEARDEEGNMCTLKRPVFLKIAPDLTDEELDDIAAEADAQKLDGIIVSNTTLSRSGLKNPENSNETGGLSGAPLFERSTVVLARMRERVGPDMPLIGVGGIDSAETALAKIKAGADLVQLYTGLIYRGPGLPGEILRGLSTAIKHEGVSSIAELRDRDTKEWAARKLIS", "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": "MELEYESKRPLYIPYAGPILLEFPLLNKGSAFTEEERNHFNLQGLLPDAVETIEEQAERAYRQYQDFKNDSDKHIYLRNIQDTNETLFYRLLDSHLSEMMPIIYTPTVGEACEHFSDIYRRARGLFISYPNRDRIDDMLQNATKQNVKVIVVTDGERILGLGDQGIGGMGIPIGKLSLYTACGGISPAYTLPVVLDVGTNNPQRLNDPLYMGWRHPRISGDEYHAFVEEFIQAVKRRWPNVLLQFEDFAQNNATPLLNRYRDEICCFNDDIQGTAAVTLGSLIAASRAAGSQLRDQTVTFLGAGSAGCGIAEQIIAQMKSEGLSEDEARARVFMVDRFGLLTDKLPNLLDFQSKLVQKSENLTAWQTQSDAISLLDVVRNAKPTILIGVSGQPGLFTEELIREMHKHCPRPIVMPLSNPTSRVEARPEDIINWTEGAALVATGSPFAPVHYKEQQIPIAQCNNSYIFPGIGLGVLASGATRVTDAMLMAASRALAECSPLATDGHGALLPDIDDIQGVSKCIAMEVGKAAQLQGMAVVTSEEALSKAIEHNFWRPQYRSYKRTSF", "text": "SIMILARITY: Belongs to the malic enzymes family."}
+{"protein": "MSFKVNWNSLETEPLTNWTKELLTSALNSGKSPNILASNITIKDLNFGKIAPDFEILEIGELDRDRFRGIFKIDYQGDFHLTLHTKVQANPLNIYYHNSLEKEVCNYSQDEFITPNFLLSNEQFAIPLDLKLSDIKINGIGIIVFSKSKGLTLVFRNDPLDSIKVSSTFDTVQVLANFLQKQIENQIRDLFRETLPTLIHQLSLKYLSLDNNINEIKSKLSQQDSVSMTNNELASSLKLFDDEENEFPLIYSSKNLQKNMQLFKSRETFRLSVPKFKNIVQRTRLDKFTKSYPNLLNSLYANNADLQHRFVNNINHGHNNNSNTSSNGIPIELLVSHDDKQHYDKTDDLLKDISSIQANNFYKYSNKDAPNKPKRRRIKVHKKSKAKQDDNTVKASELQNVDSTFMDSRSISPQETIDTTSTLIESAPMTRNVSTNIKSPTLETMSTGSSSSASSQVIAHPTPKRAYQPADTTVSTTTINKENHIDYIKARNLYQDFIQMSQSPGYYDKVISNGGGIGLGNSGGNYFGFNGNGNGLERTMSASPIKHLNKDKKSINYIDTSKINEKLNQFRLDGGKNSANTNNSSGGKNFRPGFTRNESNGQQGILFEAFNFPSVAPPPPYC", "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": "MVNAALPLLAQLPEAYRAFGPLVDILPLIPVFFLLLAFVWQASVGFR", "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": "MNHFPKLLSSQIGFDVAQTMLENFDRHYRIFREAAVEAKTLYEHGDWHGLQRLARERITSYDDRVKECVEVLEDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLATTLERIVTNFQLEPAFDDLPRDIGCVMQAIHDEFGHFDEAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGVLSLDTVLLRRDQLMIIFGFSHSYFLVDMGVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTRAQIMEKYQLVKRHDRLGRMADTLEYSSVALPIARLDHALVRELEKEVPSLLEYEDGNLVIEHLYIERRMTPLNLYLQNGSDSDVEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRDVFMKHHADFFDPALWQASKDKLIQGELPDFYPYDTALRFCTRYPARFGATDQNDGAGDAQRAA", "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": "MQCALYDAGRCRSCQWITQPIPEQLSAKTADLKNLLADFPVEEWCAPVSGPEQGFRNKAKMVVSGSVEKPLLGMLHRDGTPEDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGGMMLRFVLRSDTKLAQLRKALPWLQEQLPQLKVITVNIQPVHMAIMEGETEIYLTEQQALAERFNDVPLWIRPQSFFQTNPAVASQLYATARDWVRQLPVNHMWDLFCGVGGFGLHCATPDIQLTGIEIAPEAIACAKQSAAELGLTRLQFQALDSTQFATAQGEVPELVLVNPPRRGIGIPLCDYLSTMAPRFIIYSSCNAQTMAKDIRELPGYRIERVQLFDMFPHTAHYEVLTLLVKQ", "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": "MPGIETIKSSWADEVELDYGGLPPTTETVENGHKYVTEYKYNKDDKKTKVVRTYKISKQVVPKTVAKRRTWTKFGESKNDKPGPNSQTTMVSEEIIMQFLNSKEDEKANDPLLDPTKNIAKCRICNGEHWSVNCPYKGTAMDTNMMEKKATAAAAAAVDAPKSGKYVPPFLKDSVGKVGMGMRGRDDTAAIRISNLSESMTEADLEELVKKIGPQSKMYLARDKNTGLCKGFAYVHFKQRKDAAAAIEILNGHGYDHLILSVEWSKPQNN", "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": "MIDVIVLGAAAGGGFPQWNSAAPGCVAARTRQGAKARTQASLAVSADGKRWFILNASPDLRQQIIDTPALHHQGSLRGTPIQGVVLTCGEIDAITGLLTLREREPFTLMGSDSTLQQLADNPIFGALDPEIVPRVPLILDEATSLMNKDGIPSGLLLTAFAVPGKAPLYAEAAGSRPDETLGLSITDGCKTMLFIPGCAQITSEIVERVAAADLVFFDGTLWRDDEMIRAGLSPKSGQRMGHVSVNDAGGPVECFTTCEKPRKVLIHINNSNPILFEDSPERKDVERAGWTVAEDGMTFRLDTP", "text": "FUNCTION: May be involved in the transport of PQQ or its precursor to the periplasm. SIMILARITY: Belongs to the PqqB family."}
+{"protein": "MPLSLSSRVREELAKETCEKLSTQHQAKKKAKAIDRDFFLSVLGSSATKREARSYIQNFKPPNTAPTKSKIQESTQQNSTENGANLGSIYTATRAVAESPKFVQQPVLPKPAPEGPLLHVALVKIRAPQLLDDETLSGIGKTLSRLSRLGLVSTVVVDGDDGSDTFLRISNCEWRNMVKEQAARVVAAIDASGTEARLVDNVIGIAEDGSNFEQRPYLKGRVHVTLRELLMTPLRRGVLPIIPSIGHTDITQTVVSATANDVVLALTREFAGIWSSESPDEHPNVVKERLQALRSEVSLDRLILVDPLGGIPASDRKNGYHVFLNMEQEYELAKQDLINRGGMHSVAPQKPTLPEASANFTVGDPILLSSFTENKPGELDDSPPPQNGSPAKHDPRMKFHLENLELVRSTLSLLPPSSSALITTPHEAANSEKQPEFKAAGVGTRRQRNPLIHNLLTDKPAFSSSLPVGRLGPMDKNEPISSSTKFAPTTFAKHGMPVTIFPDPKTTPWQPPIAGVPQISLTDPQIDLPRLVHLIEDSFNKKLDVQHYLRRVNNRIAGVIIAGEYEGGALLTWELPPGVPDGSEESRKRMVPYLDKFAVLKKSQGSGGVADVVFKSMVRDCFPGGDNPVNKWYFERSRATLKLSDTNWTMFFTTPEENMDHQTFKDYEAVCKFFGRENVGGYYQQGKRGIYVLDSE", "text": "FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acetyltransferase family."}
+{"protein": "MINNVVLVGRMTRDAELRYTPSNQAVATFSLAVNRNFKNQSGEREADFINCVIWRQQAENLANWAKKGALVGITGRIQTRNYENQQGQRVYVTEVVAESFQLLESRATREGGSPNSYNNGGYNNAPSNNSYSASSQQTPNFSRDESPFGNSNPMDISDDDLPF", "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": "MFARRVCGSAAASAACLARHESQKVQGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKDIKNVPYKIVRAGNGDAWVQDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMRISRSKFEGITQRLIERSIAPCKQCMKDAGVELKEINDVVLVGGMTRIRSGGGGEEVLPEGPVRGVNPDEAVALGAATLGGVLRGKASDLILVDVTPLSLGTSVVGDVFVPIIPKNTTIPCMRSHIFTTVDDGQTAIKFKVFQGEREIASENQIRGEFDLSGIPPAPRGVPQVEVTFDIDANGICHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSDAEKENVKTLVAELRKAMENPNVAKDDLAAATDKLQKAVMECGRTEYQQAAAANSGQC", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MIDTSIPLVDLHRHLDGNVRVNTIWELGHQHGIALPADSLETLAPFVQIQGKETSLVAFLKKLDWMVGVLADLDAVKRVAYENVADAALSGLDYAELRFSPYYMAMNHKLPIEGVVEAVVDGVKAGLKDYNVKINLIGILSRSFGQAACTQELEGLLAHKQHLVAMDLAGDEMGFPGELFNEHFKRVRDADLAITAHAGEAAGSQSMWQAIQELGATRIGHGVNAIHDPKLMEYLAKHRIGIESCPTSNLHTSTVASYADHPFRTFMDAGVLINLNTDDPGVSAIDINHEYRIAKSELKLTDAELAQVQRNGVEMAFLSDSERKALYAAKV", "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": "MKVKGTRRNYQHLWRWGTLLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDARAYDTEVHNVWATHACVPTDPNPQEVVLGNVTENFNMWKNNMVEQMQEDIISLWDQSLKPCVKLTPLCVTLNCTDLGKATNTNSSNWKEEIKGEIKNCSFNITTSIRDKIQKENALFRNLDVVPIDNASTTTNYTNYRLIHCNRSVITQACPKVSFEPIPIHYCTPAGFAILKCNNKTFNGKGPCTNVSTVQCTHGIRPIVSTQLLLNGSLAEEEVVIRSDNFTNNAKTIIVQLNESVAINCTRPNNNTRKSIYIGPGRAFHTTGRIIGDIRKAHCNISRAQWNNTLEQIVKKLREQFGNNKTIVFNQSSGGDPEIVMHSFNCRGEFFYCNTTQLFNNTWRLNHTEGTKGNDTIILPCRIKQIINMWQEVGKAMYAPPIGGQISCSSNITGLLLTRDGGTNVTNDTEVFRPGGGDMRDNWRSELYKYKVIKIEPLGIAPTKAKRRVVQREKRAVGIVGAMFLGFLGAAGSTMGAVSLTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEDIWDNMTWMQWEREIDNYTNTIYTLLEESQNQQEKNEQELLELDKWASLWNWFSITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTRLPVPRGPDRPDGIEEEGGERDRDRSVRLVDGFLALIWEDLRSLCLFSYRRLRDLLLIAARTVEILGHRGWEALKYWWSLLQYWIQELKNSAVSWLNATAIAVTEGTDRVIEVAQRAYRAILHIHRRIRQGLERLLL", "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": "MAPPQAPVQPPKRRRIGVLTSGGDAPGMNGVVRAVVRMAIHSDCEAFAVYEGYEGLVNGGDMIRQLHWEDVRGWLSRGGTLIGSARCMTFRERPGRLRAAKNMVLRGIDALVVCGGDGSLTGADVFRSEWPGLLKELVETGELTEEQVKPYQILNIVGLVGSIDNDMSGTDATIGCYSSLTRICDAVDDVFDTAFSHQRGFVIEVMGRHCGWLALMSAISTGADWLFVPEMPPKDGWEDDMCAIITKNRKERGKRRTIVIVAEGAQDRHLNKISSSKIKDILTERLNLDTRVTVLGHTQRGGAACAYDRWLSTLQGVEAVRAVLDMKPEAPSPVITIRENKILRMPLMDAVQHTKTVTKHIQNKEFAEAMALRDSEFKEYHFSYINTSTPDHPKLLLPENKRMRIGIIHVGAPAGGMNQATRAAVAYCLTRGHTPLAIHNGFPGLCRHYDDTPICSVREVAWQESDAWVNEGGSDIGTNRGLPGDDLATTAKSFKKFGFDALFVVGGFEAFTAVSQLRQAREKYPEFKIPMTVLPATISNNVPGTEYSLGSDTCLNTLIDFCDAIRQSASSSRRRVFVIETQGGKSGYIATTAGLSVGAVAVYIPEEGIDIKMLARDIDFLRDNFARDKGANRAGKIILRNECASSTYTTQVVADMIKEEAKGRFESRAAVPGHFQQGGKPSPMDRIRALRMATKCMLHLESYAGKSADEIAADELSASVIGIKGSQVLFSPMGGETGLEATETDWARRRPKTEFWLELQDTVNILSGRASVNNATWSCYENA", "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": "MVLVTYPAPDFTASAISCNGDIINNFNFKEFTNNQTSILFFWPMDFTFVCPSEIIAFNQELSKFKKRNVKLIGVSIDSVYVHHAWRNTLSHNGQIDKINFTMVSDLKREIQRSYGIEHPQLGVALRATFLIDKNRIIRHQTINDLPFGRNISETLRMIDALHFYEKYGEVCPANWKKGDTGIKTTQEGIHKYLEKISKK", "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": "MSITAKSVYRDTGNFFRNQFITFLLIALLCALITVVLGHAFSPSDEQIASLSQGDNLAGSVGLFDLVQNMTPEQQQILLRASAASTFSGLIGNAIMAGGVLLMVQLVSAGQRVSALRAIGASAPVLPKLFILIFLTTLLVQMGIMLVVVPGVLLAIILSFAPVMLVQDKMGIFTAMRSSIKLAWSNMRLVAPAVIGWLLAKTLLLLFAPNFAVLTPNIGAVVANTISNLISAVLLVYLFRLYTLIRQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0259 family."}
+{"protein": "MSIEVTVEIPKGSRNKYEIDHETGKVYLDRYLFTPMAYPLDYGYIDHTLGEDGDPLDALVILPESVFPAVVVKSRIIGVFKMTDEAGGDDKLLSVLDDPRYDHIQDISDVSDFLKDEIEHFFVHYKDLEKGKHVDGSGWGDKAEAEKIHAEAIDRYKA", "text": "FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase family."}
+{"protein": "MNPNQKLFALSGVAIALSIFNLLIGISNVVLNVSLHLKNNNDQDKNWTCTSITQNNTTLIENTYVNNTTVINKETEAAKQNYLMLNKSLCKVEGWVVVAKDNAIRFGESEQVIVTREPYVSCDPLGCRMYALHQGTTIRNKHSNGTIHDRTALRGLISTPLGSPPVVSNSDFLCVGWSSTSCHDGIGRMTICVQGNNDNATATVYYDRRLTTTIKTWARNILRTQESECVCHNGTCVVVMTDGSASSQAHTKVLYFHKGLIIKEEALKGSARHIEECSCYGHDSKVTCVCRDNWQGANRPVIEIDMNAMEHTSQYLCTGVLTDTSRPSDKSIGDCNNPITGSPGAPGVKGFGFLDSSNTWLGRTISPRSRSGFEMLKIPNAGTDPNSRITERQEIVDSNNWSGYSGSFIDYWDESSECYNPCFYVELIRGRPEEAKYVWWTSNSLVALCGSPVPVGSGSFPDGAQIQYFS", "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": "MKRLLALLATGVSIVGLTALAGPPAQAATGCKAEYTITSQWEGGFQAGVKITNLGDPVSGWTLGFTMPDAGQRLVQGWNATWSQSGSAVTAGGVDWNRTLATGASADLGFVGSFTGANPAPTSFTLNGATCSGSVTDPPTDPPTDPPATGTPAAVNGQLHVCGVHLCNQYDRPIQLRGMSTHGIQWFGPCYGDASLDRLAQDWKSDLLRVAMYVQEDGYETDPAGFTSRVNGLVDMAEDRGMYAVIDFHTLTPGDPNYNLDRARTFFSSVAARNDKKNVIYEIANEPNGVSWTAVKSYAEQVIPVIRAADPDAVVIVGTRGWSSLGVSDGANESEVVNNPVNATNIMYAFHFYAASHKDDYRAAVRPAATRLPLFVSEFGTVSATAWSVDRSSSVAWLDLLDQLKISYANWTYSDADEGSAAFRPGTCEGTDYSSSGVLTESGALVKSRISTTDDFPTS", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
+{"protein": "MALLVEKTTSGREYKVKDMSQADFGRLEIELAEVEMPGLMASRAEFGPSQPVKGAKITCSLHMTIQTAFLIETLTALGAEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGPGGGPDLIVDDGGDATLLIHEGVKAEEEFAKNGTVPDPTSTDNVEFQLVLTIIKESLKTDPLRYTKMKERLVGVSEETTTGVKKLYQMPANGSLLFLPINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVALVAGYGDVGKGCAAAMKQAGARVIVTEIDPICALQATMEGLQVLFLEDVVSEVDIFVTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDMHGLETFPGVKRITIKPQTDRWVFPDTNSGIIVLAEGRLMNLGCATGHPSFVMSCSFTNQVIAQLELWNERSSGKYEKKVYVLPKHLDEKVAALHLGKFGAKLTKLTKDQADYIYVPVEGPYKPAHYRY", "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": "MAKAKRMYGCTECGATFPKWAGQCADCGAWNTLVETVVEAAPSGSGRGGWAGQQANLKTLAEVSVEEMPRFTTGSTELDRVLGGGLVDGSVVLIGGDPGIGKSTILLQTLCNLASRVPALYVTGEESQQQVAMRARRLSLPEDKLKVMTETSIETIIATARQEQPRVMVIDSIQTIFTEQLQSAPGGVAQVRESAAMLVRYAKQSGTAIFLVGHVTKEGALAGPRVLEHMVDTVLYFEGESDGRLRLLRAVKNRFGAVNELGVFGMTDKGLKEVSNPSAIFLTRAQEAVPGSVVMATWEGSRPMLVEVQALVDTSHLANPRRVTLGLDQNRLAMLLAVLHRHGGIPTYDQDVFLNVVGGVKVLETASDLALMAAVMSSLRNRPLPHDLLVFGEVGLSGEVRPVPSGQERLKEAGKHGFKRAIVPLGNAPKEAPAGLQVIAVTRLEQALDALFE", "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": "MVDFQLNNFSFDPVVSLGFAAFLFLLMALPISFWAVAGSSDSSKARFLVAISNLFLTSQLILRWWQSGHFPISNLYESLCFLTWGCTLAQLFLERAWRSPIVSAVATPVSLLSIGFASFVLPENLQSSAPLVPALRSSWLVMHVSVIMCSYAALLIGSILSFGVFLVDGKKQFNIRNSSFGSGSFRQSSELYLDERNENLNSIQPIEFTNAEQLDSLSYRSITAGFLLLTVGLISGAVWANEAWGSWWSWDPKETWALICWLVYAAYLHTRITRGWQGKKPAILAIAGFFVIIVCYIGVNLLGVGLHSYGWFFDA", "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": "MSTVAAYAAMSATEPLTKTTITRRDPGPHDVAIDIKFAGICHSDIHTVKAEWGQPNYPVVPGHEIAGVVTAVGSEVTKYRQGDRVGVGCFVDSCRECNSCTRGIEQYCKPGANFTYNSIGKDGQPTQGGYSEAIVVDENYVLRIPDVLPLDVAAPLLCAGITLYSPLRHWNAGANTRVAIIGLGGLGHMGVKLGAAMGADVTVLSQSLKKMEDGLRLGAKSYYATADPDTFRKLRGGFDLILNTVSANLDLGQYLNLLDVDGTLVELGIPEHPMAVPAFALALMRRSLAGSNIGGIAETQEMLNFCAEHGVTPEIELIEPDYINDAYERVLASDVRYRFVIDISAL", "text": "SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MSVSTNLKGLAELGLKPSEVFHNLSYEEIYQHELNNKEGVTSDNGTMMVDTGIFTGRSPKDKYFVDEPSSQNNIWWGPVNTKVSEAIFNELYAEVTKFLDNKKLYVFDGHAGTNDDTRISLRVVTERAWQHHFCTNMFLRPTKEELAKLDPEFTIINASGYKNPKYKEHGLNSEVFVIFHLAKKICIIGGTEYGGEMKKGIFSVMNYYLPLKNVLTMHCSANVGKDGDSALFFGLSGTGKTTLSTDPNRKLIGDDEHGWDDNGIFNIEGGCYAKTINLDPKTEPEIYAAIRRDALLENVVYDATTKKVDYSSAAKTENTRVSYPIFHIDNIQPGSKAGHPNTVIFLTYDAYGVLPAVSKLSIEQAMYHFLSGYTAKVAGTERGVKEPQATFSACFGQAFMTLHPTYYAKLLGEKMKKHQVNAYLINTGLVGGKYGVGKRMNLPATRQIINEILNGNIEKSEFEKHPVFQVSFPKSVNGVDAHILNPRNAWENKEDYDKTAADLAKQFVENYKKYLTGSKEFDYSQYGPIA", "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": "MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESKESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGRDAFIDKIWQWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETILGDTGVAVNPEDPRYQSLIGKFVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAEVFDTKGEESDVYSSEIPAEFQKLERFAARKAVVAAVDALGLLEEIKPHDLTVPYGDRGGVVIEPMLTDQWYVRADVLAKPAVEAVENGDIQFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDNDGNVYVGRTEDEVRQENNLGADVALRQDEDVLDTWFSSALWTFSTLGWPENTDALRQFHPTSVMVSGFDIIFFWIARMIMMTMHFIKDENGKPQVPFHTVYMTGLIRDDEGQKMSKSKGNVIDPLDMVDGISLPELLEKRTGNMMQPQMAEKIRKRTEKQFPNGIEPHGTDALRFTLAALASTGRDINWDMKRLEGYRNFCNKLWNASRFVLMNTEEQDCGFNGGEMTLSLADRWILAEFNQTVKAYRDALDSFRFDIAAGILYEFTWNQFCDWYLELTKPVMTGGSESELRGTRHTLVTVLEGLLRLAHPIIPFITETIWQRVKVICGITADTIMLQPFPEYNAAQVDEAALADTEWLKQAIVAVRNIRAEMNIAPGKPLELLLRGCSEEAVRRVNDNRSFLQTLARLESITVLPADDKGPVSVTKIIDGAELLIPMAGLINKDDELARLAKEVAKIEGEIARIEGKLSNEGFVARAPEAVIAKEREKLDGYAEAKAKLIEQQAVISAL", "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": "MIETSQTIPELVSWAKDREFSLNLPTERLVFLLAIAIYNNERLDGEMLEADLVDIFRHTMNAFEQSTDAIATRANNAINELVKQRLLNRFSSEFTEGLAIYRLTPLGVGVSDYYIRQREFSALRLSVQLSIVADEIQRASDSAEEGVENNESEHYWRRNVFAPLKYSVAEIFDSIDLSQRIMDENQQSIKDEIAELLTKDWQAAISSCERLLDETSGNLRELQDTLNAAGDKLQAQLLRIQDCVIGRDDLYFIDQLITDLQSKLDRIISWGQQAIDLWIGYDRHVHKFIRTAIDMDKNRVFSQRLRNSIHNYFEHPWFLWTAQAERLVDLRDEEMVLREDDALGELPEELQYESLSDLHDQIVEHMQDLLIAYRENNRPIDLSLVLKEQLENYPLSRHFDVARIIVDQAVRLGMANDDLSGIYPDWQVINKRGAEVQAHVIDKY", "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": "MQKLRVFLLALAALCISCEAKYFATNCELVHELRRQGFPEDKMRDWVCLIQNESGRNTSKMGTINKNGSRDYGLFQINDKYWCSKTSTPGKDCNVTCAEMLLDDITKASKCAKKIYKRHKFQAWYGWRNHCQGTLPDISKC", "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": "MTQALKDLGEYIAQALPQDVLGTEVNRCGELSLTVKAASIVKVMTYLKDDAGCLFKQLVDVCGVDWPGREQRFDVVYHLLSMKHNQRVRVKVATDEETAVPSVTGVFSSAGWFEREVWDMYGVLFSDHPDLRRILTDYGFEGHPLRKDFPLTGYVEMRYDDETKRVVYEPVKLTQDFRSFDFLSPWEGPGMLPGDEKAN", "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": "MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKTSMPDGERSCPVCRISYQHKNIRPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCREDRKVICWLCERSQEHRGHHTFLMEEVAQEYQVKLQAALQMLRQKQQEAEQLEADIREEKASWKTQIQYDKTNILADFEQLRHILDWVESNELQNLEKEEKDVLRRLMKSEIEMVQQTQSVRELISDLEHRLQGSVMELLQGVDGVIKRMKNMTLKKPETFPKNKRRVFRAADLQVTLEVLRELRDVRRYWVDVTVAPNNISYAVISEDMRQVSSPEPQIIYEAQGTISQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDAMYNIEQNENYQPKYGYWVIGLEEGVKCNAFQDGSSHTPSAPFIVPLSVKICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCTVPMTLCSPSS", "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": "MGSAKSAMLILLVAMVIASCATAIDMSVVSYDDNNRLHSVFDAEASLIFESWMVKHGKVYGSVAEKERRLTIFEDNLRFINNRNAENLSYRLGLTGFADLSLHEYKEVCHGADPRPPRNHVFMTSSDRYKTSADDVLPKSVDWRNEGAVTEVKDQGHCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKENNGCGGGKLETAYEFIMKNGGLGTDNDYPYKAVNGVCDGRLKENNKNVMIDGYENLPANDESALMKAVAHQPVTAVIDSSSREFQLYESGVFDGSCGTNLNHGVVVVGYGTENGRDYWLVKNSRGITWGEAGYMKMARNIANPRGLCGIAMRASYPLKNSFSTDKSSIA", "text": "FUNCTION: Probable thiol protease. SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MYVLKNGQVLNASGELENKDVLIQNGKVNLIADSIEVTSGEEFDATGKLIAPGFIDVHVHLREPGGEHKETILTGTQAAARGGYTTICSMPNTKPVPDSKEVMESLQAKIKETAKVRVLPYASITTSLGTDELVDFEALKEAGAFAFTDDGVGVQLAGTMYEAMKRAAALDMAIVAHCEDNSLIYGGVVHDGIFAEKEGLKGIPNIAESVQIARDVLLAEAAGCHYHVCHISTKESVRVVRDAKRAGIRVTAEVSPHHLILDEEAIPGNDGNWKMNPPLRSKEDRAALLEGLLDGTIDFIATDHAPHAAEEKNVPMEQAAFGIVGLETAFPLLYTHFVKTNEWTLKQLIDWMTVKPAECFKLPYGKLEEGSVADIVVLDLEKEANIDPATFYSKGKNTPFVGETCIGWPVATFSEGTLVYNEGEIK", "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": "MLDLIQTRRALHQIPEIGLEEFKTQAYLLDVIEKLTTGKDFVQIRTWRTGILVYLQGSQPERTIGWRTDIDGLPIVEQTGLPFASQHQGRMHACGHDFHMTIALGCLERALEEQPKNNLLFLFQPAEENEAGGMLMYEDGAFGDWLPNQFYGLHVRPDLKVGQIATNTHTLFAGTCEVKIRFKGKGGHAAFPHEANDALVAASYFVTQVQSVVSRNVNPIEGAVVTFGVFQAGTTNNVITDTAFLHGTIRALTQDMSLLVQKRVKTVAEGVAAAFDMEVEVELKQGGYLPVENNPALARELMDFFDEKDGIELIDIEPAMTGEDFGYLLSKVDGVMFWLGIDSPYALHHPQMSPKEEVLAIGVAAVSSFLKKKAAE", "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": "MSWQTYVDDHLMADIEGQQGNHLAAAAILGNDGSVWAQSTTFPKFKPEEITNIMKDFDEPGHLAPTGLFLGGAKYMVIQGEPGAVIRGKKGSGGITIKKTNQALIFGIYEEPVTPGQCNMVVEKIGDYLVDQGY", "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": "MSQTPPSFIRLLNNTSLVSQILIGMIVGILLATLIPSAAQSAGLLGTLFVGALKAVAPVLVLLLVTDSIAGHKQGQKTSIRPLLILYLFGTFCAAVVAVVASFAFPSVLHLSAQNADIVPPGGIAEVLNTLLFNVVANPVKALLEGNYIGILAWAIALGLSLRKASDTTKAVIHDLSHAVSGIVKGVIRCAPLGIMGLVASTFAETGFSALLSYAQLLIVLIGCMLFVAFVVNPLIVFWKIKRNPYPLVLMCLKESGVTAFFTRSSAANIPVNMALCEKLRLPEETYAVSIPLGATINMAGAAITITVLSMAAVNTLGISVDLATAVLLSVVATISACGASGVAGGSLLLIPLACSLFGISNDVAMQVVAVGFIIGVLQDSAETALNSSTDVLFTAAACMAEDGSLSEGNLQEDADIV", "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": "MLRLVQSNTGFRSLSCRLLSSTKLVTPRFWYSQDNSKAEEIFKRKLIAREKEFRSRLPQWEKRDISLKKRYGVWNPTKKVSRVQMQDIRSLKLQMPNLKTVDMANMFGVSPESIRRILNSKWQPSENDMKKLEKRAERRKAESRERKEQSEQDLKDGVRRIHRAKTIKLQNVRYKETDAINEKDTSKKTASKRQSHAVTGKQGKMKTTIDKPFVPSVADLIK", "text": "FUNCTION: Required for respiratory activity and maintenance and expression of the mitochondrial genome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RRG9 family."}
+{"protein": "MVWSTNIKHEGLKSWIDEVAKLTTPKDIRLCDGSDTEYDELCTLMESTGTMIRLNPEFHPNCFLVRSSADDVARVEQFTFICTSTEAEAGPTNNWRDPQEMRRELHQLFRGCMQGRTLYIVPFCMGPLDSPFSIVGVELTDSPYVVCSMKIMTRMGDDVLRSLGTSGKFLKCLHSVGKPLSPGEADVSWPCNPKSMRIVHFQDDSSVMSFGSGYGGNALLGKKCVALRLASYMAKSQGWLAEHMLIIGITNPEGKKKYFSASFPSACGKTNLAMLMPKLPGWKIECIGDDIAWIRPGRDGRLYAVNPEYGFFGVAPGTSERTNPNALATCRSNSIFTNVALTADGDVWWEGLTEQPPEPLTDWLGKPWKPGGSPAAHPNSRFTAPLRQCPSLDPEWNSPQGVPLDAIIFGGRRSETIPLVYEALSWEHGVTIGAGMSSTTTAAIVGQLGKLRHDPFAMLPFCGYNMAYYFQHWLSFAENRSLKLPKIFGVNWFRKNNQGEFLWPGFSENLRVLEWIFQRTDGLEDIAERTPIGYLPNIQKFNLNGLNLDLQTVQELFSVDAEGWLAEVENIGEYLKIFGSDCPQQITDELLRIKSELKEK", "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": "MFESKINPLWQSFILAVQEEVKPALGCTEPISLALAAAAAAAELDGTVERIDAWVSPNLMKNGMGVTVPGTGMVGLPIAAALGALGGDAKAGLEVLKDASAKAVADAKAMLAAGHVAVMLQEPCNDILFSRAKVYSGDSWACVTIVGDHTNIVRIETNKGVVFTQADNAQEEEKNSPLGVLSHTSLEEILAFVNAVPFDAIRFILDAARLNGALSQEGLRGSWGLHIGSTLAKQCDRGLLAKDLSTAILIRTSAASDARMGGATLPAMSNSGSGNQGITATVPVMVVAEHVGADDERLARALMLSHLSAIYIHHQLPRLSALCAATTAAMGAAAGMAWLIDGRYDTIAMAISSMIGDVSGMICDGASNSCAMKVSTSASAAWKAVLMALDDTAVTGNEGIVAHNVEQSIANLCSLACRSMQQTDKQIIEIMASKAH", "text": "SIMILARITY: Belongs to the UPF0597 family."}
+{"protein": "MLGFLKRFFGSSQERILKKFQKLVDKVNIYDEMLTPLSDDELRNKTAELKQRYQNGESLDSMLPEAYGVVKNVCRRLAGTPVEVSGYHQRWDMVPYDVQILGAIAMHKGFITEMQTGEGKTLTAVMPLYLNALTGKPVHLVTVNDYLAQRDCEWVGSVLRWLGLTTGVLVSGTLLEKRKKIYQCDVVYGTASEFGFDYLRDNSIATRLEEQVGRGYYFAIIDEVDSILIDEARTPLIISGPGEKHNPVYFELKEKVASLVYLQKELCSRIALEARRGLDSFLDVDILPKDKKVLEGISEFCRSLWLVSKGMPLNRVLRRVREHPDLRAMIDKWDVYYHAEQNKEESLERLSELYIIVDEHNNDFELTDKGMQQWVEYAGGSTEEFVMMDMGHEYALIENDETLSPADKINKKIAISEEDTLRKARAHGLRQLLRAQLLMERDVDYIVRDDQIVIIDEHTGRPQPGRRFSEGLHQAIEAKEHVTIRKESQTLATVTLQNFFRLYEKLAGMTGTAITESREFKEIYNLYVLQVPTFKPCLRIDHNDEFYMTEREKYHAIVNEIATIHGKGNPILVGTESVEVSEKLSRILRQNRIEHTVLNAKNHAQEAEIIAGAGKLGAVTVATNMAGRGTDIKLDNEAVIVGGLHVIGTTRHQSRRIDRQLRGRCARLGDPGAAKFFLSFEDRLMRLFASPKLNTLIRHFRPPEGEAMSDPMFNRLIETAQKRVEGRNYTIRKHTLEYDDVMNKQRQAIYAFRHDVLHAESVFDLAKEILCHVSLMVASLVMSDRQFKGWTLPNLEEWITSSFPIALNIEELRQLKDTDSIAEKIAAELIQEFQVRFDHMVEGLSKAGGEELDASAICRDVVRSVMVMHIDEQWRIHLVDMDLLRSEVGLRTVGQKDPLLEFKHESFLLFESLIRDIRITIARHLFRLELTVEPNPRVNNVIPTVATSFHNNVNYGPLELTVVTDSEDQD", "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": "MTKQTLTQLEQHDLFLRRHIGPDSSQQQAMLNYVGAESLDDLTAQIVPESIRLSQELSIGDSCGEAEGIAYIRGLAKQNQVFKSYIGMGYYGTQVPNVILRNVLENPGWYTAYTPYQPEIAQGRLEAILNFQQVSMDLTGLDLASASLLDEATAAAEAMALAKRVSKAKKANIFFVADDVFPQTLDVVKTRAECFGFEVVVGPASEAVNHELFGALFQYTNRFGQITDFTELFAELRAKNVIVTVAADIMSLVLLKSPGAMGADVVFGSAQRFGVPMGFGGPHAAFFVARDEHKRSMPGRIIGVSKDARGNRALRMAMQTREQHIRREKANSNICTAQILLANMASFYAVFHGPDGLKTIASRIHRFADILAAGLQAKGVSLVNSTWFDTLSIKGLDVAAVNARALAAEMNLRFDADGTVGVSLDETTLRTDIDALFDVILGAGHGLDVAALDAQIVAQGSQSIPAALVRQDAILSHPTFNRYQSETEMMRYIKRLESKDLALNYSMISLGSCTMKLNAAVEMIPVSWPEFANMHPFCPLDQAKGYTQLIEELSSWLVNVTGYDAVCIQPNSGAQGEYAGLLAIKKYHESRGDAHRNICLIPQSAHGTNPASAQLAGMQVVVTACDKQGNVDLEDLKTKAAEVAENLSCIMITYPSTHGVYEESIREICDIVHQHGGQVYLDGANMNAQVGLTSPGFIGADVSHLNLHKTFAIPHGGGGPGMGPIGVKSHLAPFVAGHVVVKPGRVSDNNGAVSAAPYGSAGILPISWMYIKLLGSNGLKKSTQTALLNANYVMKKLSEHYPVLFRGRNDRVAHECIIDLRPLKEASGVTEMDIAKRLNDYGFHAPTMSFPVAGTLMIEPTESESKVELDRFIDAMVSIRAEIAKVESGEWPADNNPLHNAPHTMADIMDPEFDTRPYSREVAVFPSAAVRTNKFWPTVNRIDDVYGDRNLMCSCAPLSDYE", "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": "MEYDLTKQICSFLDAHMMLPLINYLKDTQQYQENEINKAMADILSQTGCCDYAINAYESIGRDTAPLQAKKQELVGELNKLKEQCSFVTQYIESKKQQKEQQKELKEQQKEQQKEKDTDKTTPTTTDETTTTTTTAPTTTTTTTTTTITPITVIPFSQLLEKITPEILDSIYRFSKLLFEIGQYGSAREHLEIFLQLSPTHQNKDKRLSALWGILESDILSLNWGQAVGDISPLQDQIDSNGTPVEQLGQRAWLIHRALFVYFYNPESRSSLVDLLLEDKYLNAIQTTCPHILRYLAVAIIVNKKKQQSNVFQRILNALVRVVEQEAYVYRDPITQFISSLFVKFNFEDAQAQLILCEKVLKNDFFLNTCVDEFMENARVCVFETYCNILESIDIDMLCKNLRIDPESSEKWIVEAIRNTRFSAKIDSANNQIKMFTQHNSYRQVMDKTKALFNRGIEMVVGINESRSQQNRKGGDNRKNQRGQNRNQQNQQNQQSNESNETTTTTTTAAAATTTTTTTATPTSA", "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": "MASRRSAAAKKEDFSFEAAATQSAHEAQEGFPSSVIIKLVLVTVAMICAPLGTYFGTLNTICGGDSSYAGALAAISVNVVLIIYLIIAAREDTGESEEERKGKEGKEE", "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": "MMEGHILFFFLVVMVQFVTGVLANGLIVVVHAIDLIMWKKMAPLDLLLFCLATSRIILQLCILFAQLCLFSLVRHTLFEDNITFVFIINELSLWFATWLGVFYCAKIATIPHPLFLWLKMRISRLVPWLILGSVLYVIITTFIHSRETSAILKPIFISLFPKNATQVGTGHATLLSVLVLGLTLPLFIFTVAVLLLIYSLWNYSRQMRTMVGTREYSGHAHISAMLSILSFLILYLSHYMVAVLISTQVLYLGSRTFVFCLLVIGMYPSIHSIVLILGNPKLKRNAKMFIVHCKCCHCTRAWVTSRSPRLSDLPVPPTHPSANKTSCSEACIMPS", "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": "MPYRSTEILSPGPADKAPLHRVTLTHDQRHLRRKLLHLENDDVVMLDLKEAVMLADGDLLALEGGGYIEVKAAEEALYEIRPRDRLHLIELAWHLGNRHLAAAIDEGRILIVRDPVIRAMLEGLGATVNEAVEPFHPLRGAYHGTGHHHHGHGHDPHHG", "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": "MVLNIKAPENIVLKPTITVFGVGGAGSNAVNNMISANLQGANFVVANTDAQSLEHSLCTNKIQLGVSTTRGLGAGASPEVGALAAQESESEIRSYLENSNMVFITAGMGGGTGTGSAPVIARIAKELGILTVGVVTKPFHFEGGHRMKTADKGLIELQQFVDTLIVIPNQNLFRIANEQTTFADAFKMADDILHAGVRGVTDLMIMPGLINLDFADIKAVMSEMGKAMMGTGEASGEDRAIKAAESAISNPLLDHSSMCGARGVLINITGGSDMTLFEVDNAANRIREEVDNLDANIIFGSTFNPELKGIIRVSVVATGIDADKVPTYKPAIAETTNIVPEETYNEPIVQPTQIEEIPDFNSYSTENIEITDSPINQNFIGNEKELGLHANSFNKSEDDSPKPSFLGKIWGSLRASNNQTLERKNIVVNTLDQDNKESDIHDIPAFLRKKRD", "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": "MNYSTLIAVASLLTAGTESKKDGYPVEGSCAFPCGYDNAYCDKLCKERKADSGYCYWVNILCYCYGLPDNAAIKGYGRCKPGKK", "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": "MTKDVVIEHGESSKAPLVPAPVAAGVGRAVSIADVFLRFLSIVATIASAISMGTTNETLPFFTQFIQFEAKYSDLPSFTFFVAANAVVCTYLVLSIPLSIVHIIRPRARYSRLILVFFDAVMLALLTAGASAAAAIVYLAHKGNVRANWFAICQQFDSFCERISGSLIGSFAAMVLLIVLIFLSAFALARRH", "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": "MMKSIRYYLAFAAFIALYYVIPVNSRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWINSLGQWLFGATNFGVRAGAILTTLLAAALVAWLTFRLWRDKRTALLASVIFLSLFAVYSIGTYAVLDPMIALWLTAGMCCFWQGMQATTRTGKIGMFLLLGATCGLGVLTKGFLALAVPVVSVLPWVIVQKRWKDFLLYGWLAVLSCFVVVLPWAIAIARREADFWHYFFWVEHIQRFAMSDAQHKAPFWYYLPVLLAGSLPWLGLLPGALKLGWRERNGAFYLLGWTIMPLLFFSIAKGKLPTYVLSCFAPIAILMARFVLHNVKEGVAALRVNGGINLVFGIIGIVAAFVVSSWGPLKSPVWTHIETYKVFCVWGVFTVWAFVGWYSLYHSQKYLLPAFCPLGLALLFGFSIPDRVMESKQPQFFVEMTQAPLASSRYILADNVGVAAGLAWSLKRDDIMLYGHAGELRYGLSYPDVQDKFVKADDFNAWLNQHRQEGIITLVLSIAKDENISALSLPPADNIDYQGRLVLIQYRPK", "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": "MAAAAAAGPGAGAGIPGASGGGGAREGARVAALCLLWYALSAGGNVVNKVILSAFPFPVTVSLCHILALCAGLPPLLRAWRVPPAPPVSGPGPSPHPASGPLLPPRFYPRYVLPLAFGKYFASVSAHVSIWKVPVSYAHTVKATMPIWVVLLSRIIMKEKQSTKVYLSLVPIISGVLLATVTELSFDVWGLVSALAATLCFSLQNIFSKKVLRDSRIHHLRLLNILGCHAVFFMIPTWVLVDLSTFLVSSDLAYVSQWPWTLLLLVVSGFCNFAQNVIAFSILNLISPLSYSVANATKRIMVIAVSLIMLRNPVTSTNVLGMMTAILGVFLYNKTKYDANQQARRHLLPVSTSDLSNREHLRSPMEKPHNGALFPQQGDFQYRNILLTDHFQYSRQGHPNSYALSRHDV", "text": "FUNCTION: Putative transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. SLC35E subfamily."}
+{"protein": "MEDFVRQCFNPMIVELAEKAMKEYGEDPKIETNKFAAICTHLEVCFMYSDFHFIDERGDSIIVEVGDPNALLKHRFEIIEGRDRNMAWTVVNSICNTTGVEKPKFLPDLYDYKENRFVEIGVTRREIHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRRLADQSLPPNFSSLENFRAYVDGFEPNGCIEGKLSQMSKEVNARIEPFLKTTPRPLRLPEGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMKTFFGWKEPNIVKPHEKGINPNYLLAWKQVLAELQDIENEEKIPKTKNMKKTSQLKWALGENMAPEKVDFEDCRDFSDLKQYNSDEPEQRSLASWIQSEFNKACELTDSSWIELDEIGEDVAPIEHIASMRRNYFTAEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCVLEIGDMILRTAIGHVSRPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESIIEAESSVKEKDMTKEFFENKSETWTIGESPKGVEEGSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLIVQALRDNLEPGTFDLGGLYEAIEECLINDPWVLLNASWFNSFLTHALK", "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": "MSCCGGSCGCGSGCKCGNGCGGCGMYPDMEKSATFSIVEGVAPVHNYGRVEEKAAGEGCKCGSNCTCDPCNC", "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": "MNLIDQIKNTLIISCQAVDDEPLNDSYVLSKMCYALVLGGAKVLRLSQVEHIKKIKEVVNVPIIGLIKKHYDNSEVFITPTIKEVDQLVDLKVDIIALDATLRKRPDQDLTNLIKTIKTKYPNQLLMADCSNINDAINAQNLGFDLISTTLRGYTKDTLNHNNIENDYQFLKDLKKVITKPIIAEGGIWTPQQAKEILNLGIHSIVVGSAITRLHLIVKYWNDNLK", "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": "MDPQYARWVKAAALSATALASILLIIKIFAWWHTGSVSLLAALVDSLVDLAASLTNLFVVRYSLQPADEEHTFGHGKAESLAALAQSMFISGSALFLFLTGFRHLASPEPLQDPSIGIGVTLVALFSTLILVTFQRWVVRKTHSQAIRADMLHYQSDVLMNGAILIALALSWYGFRRADALFALGIGVYILYSALRMGYEAVQSLLDRALPDDERQQIIDIVTSWPGVIGAHDLRTRRSGQTRFIQLHLEMEDMMPLMEAHVLAEQVEHALLYRFPGADVLIHQDPCSVVPKERHAHWEL", "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": "ADREPNHFVA", "text": "SUBCELLULAR LOCATION: Secreted, cell wall."}
+{"protein": "MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVASGAVKPLMRDLIIADNVHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWTPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKWGFVGAPLHDPCTIAWLLKPELFTTVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLAERLKFYA", "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": "MPELPEVETVRRTLAELVIGKTIEQVDVGWAKMIKRPDDVDQFKWLLKGQTIRSMGRRGKFLLFHLDDYTLVSHLRMEGRYGLYQQNESVAKHTHVRFVFGDGTELRYQDVRKFGTMHLFQSGREQMEPPLAKLGVEPFSDQFSAKLLTERLSKTSRKIKSALLDQGIIVGLGNIYVDEALFRARIHPERLAKDVTVAEVKILHQAILNTLTEAVNLGGSSIKSYVNGQGEMGMFQQRLDVYGRKGETCRQCGTPITKTVVGGRGTHFCSVCQK", "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": "MLKEIRPAIVLLLALTLLTGLAYPLAMTALAGVIFPKQAQGSLIEQDGQVIGSALIGQPFTEDKYFHGRPSATTAADPQDSSKTVPAPYNAANSAGSNLGPTNKALIDRVKDDVDKLKAENPSAAVPVDLVTTSASGLDPDISPEAALFQVPRVAKARGLSEERLRQLVSDHSKARLAGLLGEPRVNVLALNLALDAAK", "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": "MNGTEGPYFYIPMVNTTGIVRSPYEYPQYYLVNPAAYAALGAYMFFLILLGFPINFLTLYVTLEHKKLRTPLNYILLNLAVADLFMVFGGFTTTMYTSMHGYFVLGRLGCNLEGFFATLGGEIGLWSLVVLAIERWVVVCKPISNFRFGENHAIMGLAFTWIMACACAVPPLVGWSRYIPEGMQCSCGVDYYTRAEGFNNESFVVYMFTCHFCIPLTIIGFCYGRLLCAVKEAAAAQQESETTQRAEREVTRMVILMVVGFLVCWLPYASVAWYIFSNQGSQFGPLFMTIPAFFAKSSSVYNPMIYICMNKQFRHCMITTLCCGKNPFEEEEGASTTASKTEASSVSSSSVSPA", "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": "MSEFKRLMRLKLKMKQKRPEFKRQDWFKCSRIGTSWRRPFGKHSGMRIGLTHRAAVATVGYRGPALVRGLHPSGLQDILVNNVKELVALNPEIQGARIAATVGKRKRIEIVKKANELGIRVFNVSKQKQDEFLSL", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 family."}
+{"protein": "MGQVFLLMPVLLVSCFLSQGAAMENQRLFNIAVNRVQHLHLLAQKMFNDFEGTLLSDERRQLNKIFLLDFCNSDSIVSPIDKQETQKSSVLKLLRISFRLIESWEYPSQTLTISNSLMVRNSNQISEKLSDLKVGINLLIEGSQEGILSLDDNDSQHLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCRKSLEANCTL", "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": "MDTSRLTLDHFLSRFQLLRPQMTHETLNQRQAAVLIPVVRRPQPGLLLTQRAIHLRKHAGQVAFPGGAVDSTDASLIAAALREAQEEVAIPPQAVEVIGVLPPVDSVTGFQVTPVVGIIPPNLPWRASEDEVSAVFEMPLAQALQLGRYHPLDVYRRGNSHRVWLSWYEHYFVWGMTANILRELALQIGVKP", "text": "FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily."}
+{"protein": "MSQSTSTLRRNGFTFKQFFVAHDRCAMKVGTDGILLGAWAPVAGVTRILDIGTGSGLLALMLAQRTDESVTIDAVELDSEAATQAQENIAHSPWPQRITVHTEDVRQWVPRQTARFDLIISNPPYYEQGVECATPQREQARYTTTLDHEALLTTAAECITEEGFFCVVLPEQTGNTFTQQALSMGWHLRLRTDVAETESRLPHRVLLAFSPRTGECFSDRLVIRGPDQLYSEGYTALTQAFYLFM", "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": "MQTIYTKITDIKGNLITVEAEGASLGELVQIERADGRSSYASVLRFDARKVTLQVFGGTSGLSTGDKVIFLGRPMEVIYGDSLLGRRFNGTGKPIDHEDECFGEPIPITTPSFNPVCRIVPREMVRTNIPMIDMFNCLVKSQKIPIFSSSGENHNALLMRIAAQTDADIVIIGGMGLTFVDYNFFVEESQRLGFADKCVKFIHKAVDAPVECVLIPDMALACAERFALEQQKNVLVLLTDMTAFADALKEIAITMDQIPANRGYPGSLYSDLAVRYEKAVDIAQGGSITLISVTTMPGDDITHPVPDNTGFITEGQFYLKDNRIDPFGSLSRLKQLVIGKKTREDHGDLANALIRLYADSRKSAERMSMGFKLSNWDKKLLAFSELFEARLMSLEVNIPLEEALDIGWKILSQSFHSEEVGIKEQLIQKYWPKACLHK", "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": "MLDRSRLRIAIQKSGRLSKESQQLLEQCGIKINLQQQRLLAFAENMAIDIMRVRDDDIPGLVMDGIVDLGIIGENVLEEALLTRRSQGDNPCYIMLLRLDFGDCRLSMALPIDEPWNGPKSLQGKRIATSYPHLLKQYLDKLGIHFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLHEVEVIYRSKACLIQRSGELSNIKQSLINKLIIRIQGVIQARGSKYIMLHAPAEQLEEIINLLPGAESPTVLPLAGNQHRVAIYMVSNETLFWETMENLKNLGASSILVLPIEKMME", "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": "MSTCVEQPTHSASLDPTAAQRLPYPDLPVDILRRSSVRGSGFVAAALVSSARKADDDARHDDDDPSGDRHETYGSHYLANLGVEQSVRDEGTVDAWVESSQSLIRLTGKHSLNGELPRLMRHGFITPVPRHYVRNHGPVPRGDWATWTVEVTGLVRRPRALTMDELARDFPALELPVTLVCAGNRRKEQNMVRQTLGFNWGPGAVSTSVWRGARLSDVLRRCGSMSRKGGALFVCFEGAEDLPGGGGTKYGTSITREVALDPTMDVMLAYQQNGGPLLPDHGFPVRLIVPGCTAGRMVKWLKRIVVAPAESDNYYHYRDNRFLPSHVDAKLADAEGWWYKPEYVINEMNTNSVITTPAHNEFLPINAITTQRIYTMKGFAYSGGGKKVTRVEVTLDGGENWLLCELDHPEKPTKYGRYWCWCFWSIDVELIDLLACKEIAVRAWDQSLNTQPEFLTWNLMGMMTNCWFRVKVNVCRPRHGEKAGLAFEHPVRTNQPGGWMAQQKHLETAERTSAATSTTNQQFTMSEVRKHASQDSAWIVVHGHVYDCTAFLKDHPGGADSILINAGTDCTEEFDAIHSDKAKELLDTYRIGDLVTTGGAEQRSPLELAPSPPIRHEGPAAPVIALSNPREKVPCQLVARTVLSRDVRLFRFALPSSGQVLGLPVGKHIFVCASIDGKLCMRAYTPTSSVDEVGHFDLLVKVYFRNENTKFPDGGRMTQYLDSLPVGAHVDVKGPLGHVEYVGRGGFVIDGKPRKAGRLAMVAGGSGITPIYQVIQAVLRDQPEDKTEMHLVYANRTEDDILLRAELDRWAAEYPERLKVWYVVSQVKRLDEWKYSVGIVTEAVLRDDVPEARDGTLALLCGPPSMIQSPILPNLEKMKHQLDDSVVSF", "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": "MFARLARANYLKNSGRYFSTEPTLKERLVQIIPGKIEQVKQLKTEHGDKIIGTCTVAQAYGGMRSVKSLVTETSSLDPEEGIRFRGLTIPECQEKLPKAPGGAEPLPEGILWLLLTGEVPTESQVKTLSKDLAKRAGLPKHVTSMIKAFPEQMHPMSQLAAAILALQGESKFVKAYNDGVKKDKYWESTLEDSLDVIAKLPEVAALIYQNTYKKSDITHKIDENLDWSANFNRMLGYTSKDFDELMRLYLTIHTDHEGGNVSAHTTHLVGSALSDSYLSLSAGMCGLAGPLHGLANQEVLSWTMKLQEKLGNKEVSNEVLSEAIWEGLNAGRVVPGFGHAVLRKTDPRYTCQREFALKHLPQDPLFKLVSQIYEVVPDILTKHGKTKNPYPNVDAHSGCLLQYYGLKEHNFYTVLFGVSRAIGVLSSLVWDRILGHPIERPKSVTTEWISSYVNSDQSKK", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the citrate synthase family."}
+{"protein": "WMMIVEQKCRVIVMLAKCFEAGKKKCQKYWPDSKEAKTFGRVKVFNAEEVKYCGFLRRRFYIDSFDEMMSVEVFQYQYINWPDHSVPNTTSNLVRMHKYVIQCLEETGSDAPMVV", "text": "SIMILARITY: Belongs to the protein-tyrosine phosphatase family."}
+{"protein": "MRLAFWLYEGTALHGISRVTNSMKGVHTVYHAPQGDDYITATYTMLERTPQFPGLSISVVRGRDLAQGVSRLPSTLQQVEHHYHPELIVIAPSCSTALLQEDLHQLAAHSGLPQEKILVYALNPFRVSENEAADGLLTELVKRFASPQEKTAQPSVNLLGFTSLGFHLRANLTSIRRMLQTLGIAVNVVAPWGASIDDLRKLPAAWLNIAPYREIGSTAAEYLADAFAMPALYEAPIGVEPTLAWLRSLIEKLNAAGAERGVAPIVMPQLNAFSLDGLSAPSGVPWFARTADMESFSNKRAFVFGDATHTVALVKFLRDELGMQIIGAGTYLERHADWVRKELEGYLPGALIVTDKFQDVAQIIDDQMPDLVCGTQMERHSCRKLDVPCMVVCPPTHIENHLLGYYPFFGFDGADVIADRVYLSCKLGLEKHLIDFFGDAGLEYEEPEVSAPSEEPVALSVAPNDHPSPEAAAEAVVIAEEGEMKWSDEAETMLKKVPFFVRKKVRKNTETFARASGASMISVDVFRQAKESLGG", "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": "MLLKELSSLASPLSQPQVEKLKQLTAELNAVQLAWVSGYLAATANAPGNLAQLAPVSDAQAAQTVTILYGSQTGNGRGIAKALAEKAKAQGYSVNLASMGEYNVRQLKQETLLLLVVSTHGEGEAPDDAIELHKFLASKRAPQLSNLHYSVLALGDSSYEFFCQTGKDFDARLSALGAKALLPLVECDVDYEAAAGQWHADVLTAVKPLIQTTANVVALNDTSSALAASESEFTKQNPYSAEVLVSQKITGRGSDRDVRHVEIDLGESGLCYEVGDALGVWFSNNETLVDEILAGLGLAADTKVTVGNESISLKQALLEKKELTQLYPGLVKAWAELSASPELLALSGDKEQVRQFILHHQFADLVANYQLKADANLDANKLVELLRPLTPRLYSIASSQSEVDTEVHLTVALVEDEHQGQARFGGASHFLASAEEGAEVKVYVEPNKHFRLPEDPQTPVIMIGPGTGVAPFRAFMQERVAQGAEGDSWLFFGNPHFEQDFLYQTEWQQYLKNGDLTRIDVAFSRDQAHKIYVQHRIKEQGQTLWQWLQNGAHLYICGDAERMAKDVHQALLAIAVEFGGLSSEAAEEYFETLRSHKRYQKDVY", "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": "MIHPDPTLFGHDPWWLILAKAVGVFVFLVLTVLAAILIERKVLGRMQMRFGPNRVGPKGLLQSLADGIKLALKEGITPAGVDKPVYLLAPVISVIPAFLAFAVIPMGGEVSVFGHRTALQLTDLAVAVLYILAVTSVGVYGIVLAGWASGSTYPLLGGLRSSAQVVSYEIAMALSFATVFLYAGTMSTSGIVAAQTSTWYVFLLLPSFLVYVTSMVGETNRAPFDLPEAEGELVGGFHTEYSSLKFAMFMLAEYVNMTTVSALATTMFLGGWHAPWPISLWEGANSGWWPLLWFTAKVWVFLFVYIWLRGTLPRLRYDQFMAIGWKMLIPVSLAWIMIVATAHSLRTTGHGGWASGLLIAGTVLTFGLAVVLWRTMRFRADRTVPARTAADVFPIPPIPGRAGAARTPESRETTDA", "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": "MRTLLLTLVVVTIVCLDLGNSLICYVSEYGAKMTCPEGKTLCEKYAVPLMQGHFYFAWRCTSTCKAGAYNICCSTDLCNKIP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily."}
+{"protein": "MISSYGDVDMELRDEDLILEEVRDYLTAYLRNIHQEDIILDNERVVVDLNQLYNYGLMEFVEFLINNPQKGIDFIKECYNDAYYTLRNEYPTNVIIAVKNLPKIFKTTRKGKIFTIEDIRSKTLGKLVEFEGIIVMASKIRPMLKKAYYICPKCGREVVREIDILNTDSEKAVCECGAELNLIEHKSIYTDFQEIKVQQPLDLMENPEEPPKYITVFLENSPGIYAGRVKITGIPIKVKKSKKLPIYDIHVKALHCEVLDGEVKIKLTNSDIENIKKIAKRKDVVNILADRLIPEIKGHSAIKKAVLLQQIKGVKKPGKRADIHILLITDPGIGKTVILRKIAEIPGNLYGSVTTATGVGLTAAVVREKTEIGEDTWVIKPGLLVKAHKGTACIDELTVNKELQSYVLEAMESQTIHISKGGINAKLPAECAILAACNPRWGRFNPEVSVAEQINIPAPLLSRFDLIFPIRDVSDKDKDKDIAEYIVDLHRAYLDEKINREMGLDYLEVDGVKIDKEFIIKYIYYARQKKPIISEKAKELFVNYYVEMRKKHQITARQLEAAIRIAEAHAKAKLKDVVDEEDAKEAINIITECLKEIAYDPETGIFDVDKILGVSKKERDKLTTVYEIIKELSEKSELVEHEDIAEEAKKKGIKEDELENIIKKLIKYGDIDEPKPGRYRLL", "text": "SIMILARITY: Belongs to the MCM family."}
+{"protein": "MSTGVRPGRRFTVGRSEDATHPDTIRAAISEFIATAIFVFAAEGSVLSLGKMYHDMSTAGGLVAVALAHALALAVAVAVAVNISGGHVNPAVTFGALVGGRVSLVRAVLYWVAQLLGAVAATLLLRLATGGMRPPGFALASGVGDWHAVLLEAVMTFGLMYAYYATVIDPKRGHVGTIAPLAVGFLLGANVLAGGPFDGAGMNPARVFGPALVGWRWRHHWVYWLGPFLGAGLAGLVYEYLVIPSADAAVPHAHQPLAPEDY", "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": "MDPEGLALLLPPATLATLADSWLREDCPGLNPVALVTGAAPSQAVLWAKSPGVLAGRPFFDAIFAQVNCQVSWFLPEGSKLVPVAKVAEVQGPAHCLLLGERVALNMLARCSGVASAAATAVETARGTGWAGHVAGTRKTTPGFRLVEKYGLLVGGATSHRYDLGGLVMVKDNHVVAAGGVEQAVQGARRAANFALKVEVECSSLQEALEAAEAGADLVLLDNFRPEELHPTAAALKAQFPTVGVEASGGVTLDNLPQFCGPHIDVISLGMLTQAAPALDFSLKLFAEGTTPVPYARKS", "text": "FUNCTION: Involved in the catabolism of quinolinic acid (QA). SIMILARITY: Belongs to the NadC/ModD family."}
+{"protein": "MKPIIPPQNLSELLERANMMAGISLAQIAAHRGITVPKDLKRDKGWVGQLIEMELGATAGSKPEQDFLHLGVELKTIPIDSKGKPLETTYVCVAPLTNIEGLTWQDSLVCHKLQRVLWVPVEGERHIPVGERRVGTPILWEPDQQELALLQQDWEEIMELIALGKVEKLTARHGEVLQLRPKAANSKALTQSIAEDGGLKMTNPRGFYLKTAFTAMLLNKVFG", "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": "GPMGIMGPRAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGIPGFKGHNGIDGIKGQPGAPGVKGEPGAPGENGTPGQAGARGRVGGTGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGPVGNPGPSGPAGPRGEMGIPGVTGPIGPPGNPGANGISGAKGAAGIPGVAGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEPGSAGPVGPPGIRAGVMGPPGSRGSSGPAGVRGPSGDSGRPGEPGIMGPRGIPGSPGNVGPAGKEGPVGIPGIDGRPGPVGPAGARGEPGNIGFPGPKGPTGDPGKIGEKGHVGIAGPRGAPGPDGNNGAQGPPGPQGIQGGKGEQGPAGPPGFQGIPGPSGTAGEVGKPGERGIHGDFGIPGPAGPRGERGIPGQSGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAPGTAGPSGPSGIPGERGAAGIPGGKGEKGETGIRGDTGNTGRDGARGAPGAIGAPGPAGATGDRGEAGPAGIAGPAGPRGEVGPAGPNGFAGPAGAAGQPGAKGERGPKGENGPVGPTGPIGSAGPAGPNGPPGPAGSRGDGGPPGVTGFPGAAGRTGPPGPSGITGPPGPPGAAGKEGIRGPRGDQGPVGRTGETGASGPPGFTGEKGPSGEPGTAGPPGSPGPQGIIGAPGIIGIPGSRGIPGVAGAVGEPGPIGIAGPSGARGPPGGVGSPGVNGAPGEAGRDGNPGSDGPPGRDGIPGHKGERGYPGNAGPVGTAGAPGPQGSVGPAGKHGNRGEPGPAGSVGPVGPVGPRGPNGPIGPRGDKGEPGDKGPRGIPGIKGHNGIQGIPGIAGQHGDQGSPGTVGPAGPRGPAGPSGPAGKDGRSGHPGAVGPAGVRVS", "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": "MAADIRIVPCLTDNFGYLIHDPSSGATASIDAPEAAPLIAALEKEGWKLTDILVTHHHGDHVGGVAELKKKYQCRVVAPHDANAKIADIDLRVEEGDVVRVGGLSARVLETPGHTLDHISYVFDDDRALFAADTLFSIGCGRVFEGTYPMMWESLLKLRELPDDFKLYCGHEYTASNVKFALTIEPDNAALQARAKQVEQQRAAGQPTIPVTLGEEKQANLFLRADVPSVAAAVGLPGESAADVFGELRERKNNS", "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": "MSREMGELTQTRLQKIWIPHSSSSSLLQRRRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAVSYRNYEFFRPDNMEAQLIRKQCALAALKDVHKYLSREEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPDIIAENIKQVKLGSPDYIDCDQEKVLEDFLKRIECYEINYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHVQSRTAYYLMNIHVTPRSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSDELPYLKCPLHTVLKLTPVAYGCRVESIYLNVEAVNTHRDKPENVDITREPEEALDTVPAHY", "text": "FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate mutase family."}
+{"protein": "MLDKRLLEVLVCPLTGGELYYDADSCELVSENAGLAFPVHDGIPVMLADEARKLEPDTK", "text": "SIMILARITY: Belongs to the UPF0434 family."}
+{"protein": "MQKTYLLALLVSSLASVRSLADQTRLDLGGSFDSTDSADGGSDNVMIQKSEMNEVIASSELLSLHRSLVEIKSISDNEQAVGEFLIDYLDSKNFTVEMQYVDFDDDTGKTIRSPRRFNIFAYPGNNASPGIILTSHIDTVPPFIPYSLSHPASTSLKRDDILISGRGTVDDKASVACQVIAAMDHLEKHPDIPIGLLFVVSEEVGGKGMSTFSNSRLNSGTYHTIIFGEPTEGALVAGHKGMVSFTLRVHGKPAHSGYPWLGRSAVSEIIPILAEVDRLGDIPVSQGGLPSSEKYGRTTLNIGFMSGGVASNVVAEEAVAKVAVRLAAGDPEDAKDIIFRAIRNVATKNRNDATVVLSNGHERPKGDIEIIFGLEAYGVIDLDSDVDGFNVTTVNYGTDVPHWKIYGDNVKRYLYGPGTIFVAHGKNEALTVGEMEAGLEGYKKLVAKAVERERP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M20A family."}
+{"protein": "MAVSATGFEGFEKRLEISFFETTDFLDPQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIIIKTCGTTKLLLSIPHILRLADSLCLTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKLNAGSKAFVMGGSDNNPQRWHVYSASSTEESAVCDKPVYTLEMCMTGLDNIKASVFFKTNSVSASEMTISSGIRNILPGSEICDFNFEPCGYSMNSIEGDAVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGTEVLASDCVADVNGYFSQERELEELGLGGSVLYQRFVKTVECCSPKSTLGFC", "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": "MKKLLENLSLWMGIIILVTLLFGQVALNFGFGIRNEKIQFSEFLDLVEKGEVQKIVIEGYDISGVLKSGTRFYTKATQYTELIPLLRKNNVDFQVASGDSFLGLLFNILISWFPMLLLIGVWIFFMKQMQAGGNKTMTFGKSKARLLSDRSNKVTFHDVAGIDEAKEELAEIVEFLREPKKFQKLGGKIPKGCLLIGPPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGASRVRDMFEQGKKNAPCLIFIDEIDAVGRHRGVGFGGGNDEREQTLNQLLVEMDGFEANEGVIIIAATNRPDVLDPALLRPGRFDRQITISIPDIAGRQKILEVHLKKIPTAPNVEVSIIARGTPGFSGADLANLVNESALIAARRNKKVVTNEDFEYARDKILMGMERKSLVMREEEKLLTAYHEAGHAVTSLKLEASDPIHKATIIPRGRALGLVMRLPEHDRVSFTRAKMHADLIVAMGGRAAEQVIFGDDKTTSGAASDIKQATHLARSMVTKWGMSEKVGPLLYGEQNDPNNHILSIEMSNLIDSEVKQLITDALKEATKILNENIESLHRIAKALLEYETLTGQELSDLLEGKPFLKKTADDKKVVSKSSLDVEDDTVDKETLEKLESDLDTGDKE", "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": "MSHGEETELLLDPKEERFVLLPIKYHDIWKMYKKAESSFWTVEEVSLDKDIDDWGKLNAKERHFISYVLAFFAASDGIVNLNLVERFSTEVKVLEARFFYGFQMAIENIHSEMYSLLIDTYIRDNDEKNFLFDAIRTIPSVKEKADWAIRWIEDKNSDFATRLVAFACVEGIFFSGAFASIFWLKKRGLMPGLTFSNELISRDEGLHCEFACLLHYHLKKKCNRIKEVVMDAVEIEKKFLSESLPVNLIGMNCNLMCRYIEFVADRLLENLGEERVYNATNPFDFMENISLVGKTNFFDKRESQYQKAFVGIENGNDSFRIDVDF", "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": "MNTMTLTPGQLSLSQLYDVWRHPVQLRLDASAIDGINASVACVNDIVAEGRTAYGINTGFGLLAQTRIADEDLQNLQRSLVLSHAAGVGDPLDDAMVRLIMVLKINSLARGFSGIRLSVIEALIALVNAGVYPLIPAKGSVGASGDLAPLAHLSLTLLGEGKARWQGEWLPAQAALKKAGLEPVALAAKEGLALLNGTQASTAFALRGLFEAQELFASAVVCGALTTEAVLGSRRPFDARIHAARGQQGQIDAARLFRHLLTDTSAIAESHHHCHKVQDPYSLRCQPQVMGACLTQLRQTKEVLLAEANAVSDNPLVFADAGEVISGGNFHAEPVAMAADNLALAIAEIGALSERRIALMMDKHMSQLPPFLVKNGGVNSGFMIAQVTAAALASENKALAHPHSVDSLPTSANQEDHVSMAPAAGRRLWEMAANTRGIIAVEWLAACQGIDLREGLTSSPLLEQARQTLRERVAHYTQDRFFAPDIECATTLLAQGALQRLLPDFM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PAL/histidase family."}
+{"protein": "MENRWQVMVVWQVDXMKIRTWNSLVKHHMYVSKKAKGWYYRHHYETKHPKTSSEVHIPVGXAXLVIVTYWGLTTGEQPWHLGHXVSIEWRQGKYKTQVDPEMADKLIHCYYFNCFTASAIRQAVLGRPVLPRCXYPAGHXQVGTLQYLAXTAXVGVKKRRPPLPSVTKLTEDRWNERQKTQGHRGNPIMNGP", "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": "MVLSGRGMLDGGADDVGLWLGMQDFLVFCESAMYATCPLCGLFSDSPKEGRSGGGGGSEGQRTDSRLQLPTTSIVDSPGKRSLCVRASDGAGERDAGRAAAAPVRERLWLLRLCQHPRPLLQVLPRQPPPDRDVPGAVVIVVHGASRRGTVPEGIPVDEGAMPPPPPPRAKTKSRCAACGRRVGLMGFECRCGAVFCGAHPLLGQARLWLRLQGRAGRDAIARANPVVSADKVDKL", "text": "FUNCTION: May be involved in environmental stress response."}
+{"protein": "MPLYLPDDETFASFWPGDNPSLLAALQNVLRQEHSGYIYIWSREGAGRSHLLHAACAELSQRGDAVGYVPLDKRTWFVPEVLEGMEQLALVCIDNIECVAGDEPWEMAIFNLYNRILESGKTRLLITGDRPPRQLNLGLPDLASRLDWGQIYKLQPLSDEDKLQALQLRARLRGFEMPEDVCRFLLKRLDREMRSLFMTLDQLDHASITAQRKLTIPFVKEILKL", "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": "MSDTAESVDVVLVGGGIMSATLGTLIKQLEPDWTIQIFERLGEVAMESSNPWNNAGTGHAALCELNYTPEKDGKIEIGSATRINEQFQLSRQFWAHLVTAGAVPEPKEFINPTPHMTFVRGKENAEYLRRRFDALRAHPLFDAMEYTEDPAVIHSWAPLLVLQRDKDEVIAATRFEGGTDVDFGALTNKLVDYLMEHGAALHLNHEVRGLSKNADGTWHLRVRNDVGRSTVEVDAKFVFIGAGGGALPLLQKSGIPEIKGFGGFPISGEWFRTDDPEIVAKHRAKVYGKAAIGSPPMSVPHLDTRVVGGETSLLFGPYAGFSPRFLKKGSLLDLFASIRPHNIIPMLAVAKDNMSLIKYLVSQLLASKETKFDALREFMPTADPKDWYQVTAGQRVQVMKKDAEKGGVLQFGTEVVAAADGSIAGLLGASPGASTAVPIMLDVLERCFPDCIAGWKKPLTRMIPNYGTLVASDPKKTPKIIRETAEVLELQH", "text": "SIMILARITY: Belongs to the MQO family."}
+{"protein": "MKIGIDAGGTLIKIVQEHDNRRYYRTELTTNIQKVIDWLNNEEIETLKLTGGNAGVIADQIHHSPEIFVEFDASSKGLEILLDEQGHQIEHYIFANVGTGTSFHYFDGKDQQRVGGVGTGGGMIQGLGYLLSNITDYKELTNLAQNGDRDAIDLKVKHIYKDTEPPIPGDLTAANFGNVLHHLDNQFTSANKLASAIGVVGEVITTMAITLAREYKTNHVVYIGSSFNNNQLLREVVENYTVLRGFKPYYIENGAFSGALGALYL", "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": "MTESEFLKQAEATLDQIEASLEDLADTSDLDVECTRSGNVLEIEFIDNGSKIIVNSQAPMQELWVAAKSGGFHFKATGTQWINTRDGAELFAALSEMVSKQGGIPVVLQDAN", "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": "MKNIDEQIKIIKKGAEEIIDAKELKEKLIKAEKENTQLVVKLGLDPSAPDIHLGHAVVLRKLKQLQDLGHKIVIIIGDFTGMIGDPTGKSKTRKQLSSQQVMKNAETYEKQIFKILDRNKTDLRFNSQWLEKLNFKEVIELASKYTVARMLEREDFKKRFKNQQSIGIHEFFYPLMQAYDSMAIKADIEFGGTDQRFNLLMGRTLQAEYGEEKQIAIFMPLLEGIDGKEKMSKSLGNYIGIEESAKDMYVKVMQIPDSLIIKYFELCTDMHPDAIDIIRKQLNEDKVNPRDIKMKLAKEIVCLYHNEAEALNAEIYFKNLFQDKEIPEDIPIFKVRSENNLIEAIVKINSNTSKSEARRLIAQGGVKLNGRKVIDFNDIILKSNDVIQIGKKKIVKLLVE", "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": "MTVKYVESSKLPTPMGMFAMHGFSDDSSDKEHVVLTMGDVSSEEPVLVRIHSECLTGDALFSLRCDCGAQLQAAMHKIAIEGRGAIFYLRQEGRGIGLLNKIRAYKLQDCGADTVEANERLGFGADMRDYSILKPMFEHLGIAQVKLMTNNPRKIDALTQYGINIVNRIPHETGRNPHNADYLETKKGKLGHMFGEKDGE", "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": "MDIRQVTETIAMIEEQNFDIRTITMGISLLDCIDPNINRAAEKIYQKITTKAANLVAVGDEIAAELGIPIVNKRVSVTPISLIGAATDATDYVVLAKALDKAAKEIGVDFIGGFSALVQKGYQKGDEILINSIPRALAETDKVCSSVNIGSTKSGINMTAVADMGRIIKETANLSDMGVAKLVVFANAVEDNPFMAGAFHGVGEADVIINVGVSGPGVVKRALEKVRGQSFDVVAETVKKTAFKITRIGQLVGQMASERLGVEFGIVDLSLAPTPAVGDSVARVLEEMGLETVGTHGTTAALALLNDQVKKGGVMACNQVGGLSGAFIPVSEDEGMIAAVQNGSLNLEKLEAMTAICSVGLDMIAIPEDTPAETIAAMIADEAAIGVINMKTTAVRIIPKGREGDMIEFGGLLGTAPVMKVNGASSVDFISRGGQIPAPIHSFKN", "text": "SIMILARITY: Belongs to the UPF0210 family."}
+{"protein": "MRIFVKAAISTAAWRFYAHPTVAMGICVGTALAYSPENTFELLKNTTYTGIEAAKFAYENTAGIVNGIAGLAHLVYDNLPSYSETPQVDLVGSIEIS", "text": "SIMILARITY: Belongs to the UPF0416 family."}
+{"protein": "MQAPWAGNRGWAGTREEVRDMSEHVTRSQSSERGNDQESSQPVGPVIVQQPTEEKRQEEEPPTDNQGIAPSGEIKNEGAPAVQGTDVEAFQQELALLKIEDAPGDGPDVREGTLPTFDPTKVLEAGEGQL", "text": "SIMILARITY: Belongs to the GAGE family."}
+{"protein": "MKEIISRHKAGEQIGICSVCSAHPLVIESALRFDLNSGNKVLIEATSNQVNQFGGYTGMKPADFRDFVYGIAQEVGFPRERLILGGDHLGPNCWQNEPAAAAMEKSVELIKAYVAAGFSKIHLDASMSCADDPTPLDPMVVARRAAVLCKAAEETANEEQKCHLTYVIGTEVPVPGGEASTIGSVHVTREVDAARTLETHQIAFRESGLEEALSRVIAIVVQPGVEFDHTQIIHYQPQAAQALSAWIKETPMVYEAHSTDYQTRQAYRALVRDHYAILKVGPALTFALREAIFALAQMENELISPEQRSRVLEVIDEVMLNEPGYWKKYYRPTWSQAMVDIHFSLSDRIRYYWPHPRIRQSVEKLIANLNNVTLPLGLISQFMPVQFERLSEGVLTPTPHNLIIDKIQDVLRAYRFGCTPDVA", "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": "MIEARDVSVDIAGKRIVGGVDFDARPGEVAAIVGPNGSGKTTFLKALSGEFAYTGRIALNGHNLSSMRPAEMAVHRAVLPQATTLSFPFTVREVVKLGLVGGRSGALPGEDARLPERALARVDLDGFAGRFYQELSGGEQQRVQLARVLCQVWAPVLDGKPRYLFLDEPVSSLDIKHQLIIMNIARDFAKRGGGVVAILHDLNLTSMYADRIFVMHRGRLAATGSPQDVLSDDLIEKVFDCRLRVGVLPAGNMPFVLPQSSVY", "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": "MSIEPRATADLVDEIYPDVRSCDLQLQNYGGKIMFAGPVTTVRCFQDNALLKSILSTPGEGAVLVVDGAGSLHTALVGDVIAGLAADNGWSGVIVNGAVRDAAALRTIDVGIKALGTNPRKGTKTGEGERDVEVSFGGVTFTPGDIAYCDEDGIVVVTP", "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": "MDIGDFVKLELENTTYSGTVMPSLNEDTVVIKMKSGYNVGIDKKKIKNIEILESGDKPKYGLPPLNLEKNPKLKNISILSTGGTVASRVDYKTGAVHPAFTADDLIRAVPELMDVANIKGKVILNILSENMLPKYWVMTADAIKEEIENGAEGIVIAHGTDTMHYTASALSFMVNSEVPIILVGAQRSSDRPSSDAALNIIAAVKAATEPIKGVYVLMHGETGDTVCHLHEGTKVRKLHSSRRDAFKSVNETPIAEVNPFTKKVTYLREVKSQDRSKIKEVVLNTNLEEKVALIKVYPGIDSEILKFYVDNGYKGIILEGTGLGHTPETFFEGIDYANENNVLVAMTTQTINGRVNMNVYSNGRELQAKGVIPCEDMLSEVAFVKLMHLLGNYEFKEAKELMSKNIAGEINESINLEC", "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": "MSRRNTAKKRFASPDPLYKSRLVSMLTVRILKSGKKTLSQRIIYQALDIVKERTESDPLNILEKAIRNITPLVEVKARRVGGSTYQVPIEVRAYRGTNLALRWITKFSRDRSGKSMSMKLANEIMDAANETGNSIRKREDTHRMAEANKAFAHYRY", "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": "MSDFNLVGVIRVMPTDPDVNLDELEEKLKKVIPEKYGLAKVEREPIAFGLVALKFYVLGRDEEGYSFDEVAEKFEEVENVESAEVETVSRI", "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": "MIFSTLERILTHISFSVVSIGITIYLITFLVDEIRGLYASSERGMTATAFCLTGLLITRWVYSRHFPLSDLYESLIFLSWSLSIIHKIFDFKNNQNHLSAITAPSAFFTQGFATSGFLTKMHQSRILVPALQVQWLMMHVSMMVLGYAALLCGSLLSTALLVITFRKVIRLFLKRKNFVHVNGSFCFSEIQYMNEKKNVFLNSLSARNYYRYQVIQQLDRWSYRIISLGFIFLTTGILSGAVWANEAWGSYWNWDPKETWAFITWTIFGIYLHTRTNTKWEGVNSAIVASMGFLIIWICYFGVNLLGIGLHSYGSFN", "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": "MRRPLCAALLAAAVLALAAGAPAAARGGAGGRSREHRDARYEIEEWEMVVGAGPAVHTFTIRCLGPRGIERVAHIANLSRLLDGYIAVHVDVARTSGLRDTMFFLPRAAVDNASAADIPDTPAVQSHPGLFGAAFSWSYLQTRHLVDYDLVPSRPLQDWYFSQARAESNAARPPPAPRVTPTPAGRVAAFDINDVLASGPEHFFVPVRADRKRRERHVADFAAVWPVSYIPAGRAVLSCERAAARLAVGLGFLSVSVTSRDLLPLEFMVAPADANVRMITAFNGGGAFPPPGPAAGPQRRAYVIGYGNSRLDSHMYLTMREVASYANEPADFRAHLTAAHREAFLMLREAAAARRGPSAGPAPNAAYHAYRVAARLGLALSALTEGALADGYVLAEELVDLDYHLKLLSRVLLGAGLGCAANGRVRARTIAQLAVPRELRPDAFIPEPAGAALESVVARGRKLRAVYAFSGPDAPLAARLLAHGVVSDLYDAFLRGELTWGPPMRHALFFAVAASAFPADAQALELARDVTRKCTAMCTAGHATAAALDLEEVYAHVGGGAGGDAGFELLDAFSPCMASFRLDLLEEAHVLDVLSAVPARAALDAWLEAQPAAAAPNLSAAALGMLGRGGLFGPAHAAALAPELFAAPCGGWGAGAAVAIVPVAPNASYVITRAHPRRGLTYTLQGIDVANPLLVTFVRGTSCVSASGAVEARRLAVPGPLDACAYCGSVFVRYLPSGAVMDIVLIADKRTEVEFSRGANSSMPVFNPRLHSGRSRAMLLFPNGTVVSVLAFAGHEAPTFSPAYVWASVGGALVAGTTIYAIAKMLCSSVPLARGYSSVPVF", "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": "MARTKQTARKSTGGKAPRKAVATKARKTAPPVGGVKKPHRFRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIAALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA", "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": "MEGDLAHIGAGLAAIGSGAAAIGVGNVAGNFLAGALRNPSAAASQTATLFIGIAFAEALGIFAFLVALLLMFAV", "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": "MYYYLITLAVIALDQLTKWIVVQNMEIGQKIEVIPGFLYWTSYRNDGAAWSILEGHMWFFYLITVVVIGIIIYIMQKYAKGKRLFSISLAFILGGAIGNFIDRVLHQEVVDFVQTVWGNYYFPIFNVADASLSVGVVLMLVYVFVDDRKTKGIK", "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": "MESENKNNNKKVKEESKVKVKFITNDANIRVTDTPIAVPVRLGRLGLSEVIHHLREEENETSKPFDFLINGKFIRTTLDKHIKNANLSEEQIITIEYLEAITEPKREKECQHDDWVSCVDGSNFGLVVSGSYDLGVRVWGYDGELISTGTGHLAGVKSVCWISDKNADNLSFVSASMDKTLRVWNFNKSQSEIKALACLKEHTGTIESVYVSPDSSRIVSASMDSTIKLWSIKDIPNQHATTSSSIEKSNSKKRRLANNTNNETAAVDQQSEIIHNITESLASVTVPNSQGVTVVNWTTQFQMLSGSMDSKIRLWDVSTLVANDTIPTPAPLTDLDYSMESGLIVTAHKDRIVRIWDPRSSDETKSQTQSLISHKTWVTSVNWNPSSKYHCCSTSHDGTVKYWDIRTKIPLYTIDTLEKSKDKVLSSSFISNKNKNINDYSIVSGGTDSKLRIHYNDKQEQQQ", "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": "MSTPSSLQVLVKRVLDFQHVSEDDYCILKCCGLWWHGGPIMLSTNEDNQMMIKSASFKDGLEINLALMMAVQENNCSLIELFTEWGADINSGLVTVNTEYTRNLCRNLGAKETLNKREILDVFLKLKNFKSSNNIILSHELLSNNPLFLSEDNDYFRRIINCNLRRISINFILDEISFNEKLTRFWYSQAVLYNLTEAIQYFYQKYEHLNEWRLICALSFNNVFDLHEIYNKEKVGMDINQMIEITCAYMCSYSTIYYCFVMGADINRAMIISVTKSYTYNLFFCIDLGATAFEECLEIAKQQNNNELVKILSLKNYYSPDSSLISLKITDPEKINILLDEENYESKNELIYEESNINNSDDIF", "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": "MSINVTEIVLHQIHQTEGETSELNTVLRDNLLAISPEVEQMMLQLHQAYQSKAKAYGIFKNESIFAQQLNRLLEQETDFLPFSHSCAKMLSSELAKYPFASGGTFILCRYNFLATDYLFIALIDSRTSMLVDDQLEIKRTEYLDITQYDIACRINLTELKINAQSNRYLTFIKGRVGRKIADFFMDFLSAEEGLNPQLQNQTLLQAVSDYCDQGELSAPQTREVKKQVFEYCKGQINSGEEIALSELSEALPTLNEVDFAQFTQEQEYGLEENIPPVRNALKTLTKYSGSGKGVTISFNADLLGERLIWDELNDTLTIKGLPANLRDQLARNK", "text": "SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the YejK family."}
+{"protein": "MKYQDLRDFIALLEERGELKRIQQEIDPYLEITEISDRTLKAQGPALLFENVKGHDMPVLANLFGTPDRVALGMGQESVTALRDVGKLLAFLKEPEPPKGFRDALNLLPKYKKVLSMSPKSIKKAPCQQVVMSGDDVDLTKLPIQHCWPGDVAPLVTWGLTVTRGPHKERQNLGIYRQQLLGPNKLIMRWLSHRGGALDFQEWCQQHPGERFPVSVALGADPATILGAVTPVPDSLSEYAFAGLLRDSKTEVTQCLSNDLQVPAHAEIILEGYIEPGEMAAEGPYGDHTGYYNEVDEFPVFTVTHVTHRKDPIYHSTYTGRPPDEPAVLGVALNEVFIPLLQKQFPEIVDFYLPPEGCSYRLAVVTMKKQYPGHAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWKDVIWAMTTRMDPARDTTLVENTPIDYLDFASPVSGLGSKMGMDATNKWPGETDREWGEPIVMSDEVKQRVDELWDELNIMES", "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": "LAGSKHKEEKADLDPSNPVANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARVLNLTERQVKIWFQNRRMKMKKMNKEKTDKEQS", "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": "MSRGSGGGYDRHITIFSPEGRLFQVEYAFKAVKAAGITSIGVRGKDSVCVVTQKKVPDKLLDQTSVSHLFPITKYLGLLATGMTADARTLVQQARNEAAEFRFKYGYEMPVDVLSKWIADKSQVYTQHAYMRPLGVVAMILGIDEEKGPQLFKCDPAGHFFGHKATSAGSKEQEAINFLEKKMKNDPAFSYEETVQTAISALQSVLQEDFKASEIEVGVVKKEDPIFRVLTTEEIDEHLTAISERD", "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": "MVQHLSAQEIIQYISDAKKSTPLKVYVNGHFENVTFPESFKVFGSEHSKVIFCEANEWKQFYQQNHSLITELEIEMDRRNSAIPLKDLTNTNARIEPGAFIREQAIIEDGAVVMMGATINIGAIVGEGTMIDMNATLGGRATTGKNVHVGAGAVLAGVIEPPSASPVVIEDNVLIGANAVILEGVRVGAGAIVAAGAIVTQDVPAGAVVAGTPAKVIKQTSEVQDSKREIVSALRKLNNE", "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": "MVAYSTPSSSLHKPSPYNESRRMARFRPSNILGDPFALATISISILAWVIAFISSIVSAINARGYPTYSWWGVAYSLCIILGMTAVFGTDTGSVYGVAIVGYLSAGMVITTLGVNSLVYRSDSASQAAGAGFILMSMVIVIWIFYFGSTPQASHRGFIDSFALQKEHPGAYGNGRPMSTAFGNRPETTSSQAPQMYTSAQLNGFETSSPVSGYPGGAPGSENRSSSQPRFGNPSNANLTANGNENEVPQPTEYPYRAKAIYSYDANPEDANEISFTKHEILEVSDVSGRWWQARKSNGDTGIAPSNYLILL", "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": "MSYLLPTIITTLLILLALIIWFYVKTQTLRTQLQFLSEQNLEISNNNQLLNQEQIGYLQKIEQLQCKIEYQAQTIKDSEKIREESFSSAKAALFDLGQDLSKQLIEIHKMENTAARELAEKNIATASGKFNSEFERLITMVGALNKDIEQSKGTVDLIKQSLLSPIGAGLLAEITLENILKSSGLRPNLDFIMQYGLTTLDSGKLRPDALIFLPSGNLMVIDSKASKFLVDKQDNNMSLNKTMNYHLKSLANKEYAANILTNLNKKDQSFNNVMTLMFLPTEQAVEKVIAADPEFLQKAWGCNIFPVGPSGLMNMLSFAKFQITDHRRSENYKVIIEEVRKLLSSIGTMADYSQKIGNNLHNMVTNYDKFAASFNRNFMSRVKNIQKLGIDSGNKAMPATLERYQIVSSKSEIIEVEAENPPQIAEKL", "text": "FUNCTION: Involved in DNA recombination. SIMILARITY: Belongs to the RmuC family."}
+{"protein": "MVEGESKALWIILATVFAVAAVAPAVHGQQTPCYFVFGDSVFDNGNNNALNTKAKVNYLPYGIDYFQGPTGRFSNGRNIPDVIAELAGFNNPIPPFAGASQAQANIGLNYASGAGGIREETSENMGERISLRQQVNNHFSAIITAAVPLSRLRQCLYTINIGSNDYLNNYFLSPPTLARRLFNPDQYARSLISLYRIYLTQLYVLGARNVALFGIGKIGCTPRIVATLGGGTGCAEEVNQAVIIFNTKLKALVTDFNNKPGAMFTYVDLFSGNAEDFAALGITVGDRSCCTVNPGEELCAANGPVCPDRNKFIFWDNVHTTEVINTVVANAAFNGPIASPFNISQLVN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family."}
+{"protein": "MVHYKLVYFPLRARAEIARQIFAYAGQDYSEENLSFEQWPARKNNTPFGQLPILEVDGKPLGQSYAIARYLAREFGIAGQNDTEAAEVDAIADQFKDYLNDVSPYLTVLAGFKPGDKDQLRTDVFVPAFKKNFEFFENILASNHSGFFVGNSLTWVDLLISQHVQDILDKDLAVVEEFKKVLAHRKKVQSIDRIQKYIANRPDYPF", "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": "MNNLLLNCDIGESFGAWRMGLDAEVMPLIDCANIACGFHAGDPGTMRRTVALAVEHGVRIGAHPGYPDLVGFGRRSLACSAQEVEDLLLYQIGALDGLCRAQGTRVRYVKPHGALYQDMMRDPAILAAVLRALAAYDRTLPLMLMSTRDNTAARALGEAHGIELWFEAFADRAYDGAGYLVSRSQPGAVHHDAETVLAQALLLARGAALRASDGSALALEAQTLCVHGDNPASLAAVRRIRDALEAA", "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": "MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPSLRMKWMMAMKYPITADKRITEMVPERNEQGQTLWSKMSDAGSDRVMVSPLAVTWWNRNGPMTSTVHYPKVYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRAAVSADPLASLLEMCHSTQIGGTRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSIKREEELLTGNLQTLKIRVHEGYEEFTMVGKRATAILRKATRRLVQLIVSGRDEQSVAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEHIDNVMGMIGVLPDMTPSTEMSMRGIRVSKMGVDEYSSTERVVVSIDRFLRVRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQNPTMLYNKMEFEPFQSLIPKAIRGQYSGFVRTLFQQMRDVLGTFDTTQIIKLLPFAAAPPKQSRMQFSSLTVNVRGSGMRILVRGNSPVFNYNKTTKRLTILGKDAGTLIEDPDEGTSGVESAVLRGFLILGKEDRRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN", "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": "MAMQFYASPEQIMRDRSELARKGIARGRSAVVLSYAGGVLFVAENLSSALHKVGEIYDRIGFAAVGRYNEFENLRRAGVRMADLNGLSYDRRDVTGRALANSFAQTLGAIFTEQSKPFEVEICVAQVGVTAEDDELYRLTYDGSVNDEPGRMAMGGQAEAIAGALKSNHRSDMSLGDAVKVAVRALGSVGGEGGAARTIAADQLEVAILDRHRDGRTFRRVTGAALTALLDDGAAAASTDAPAAAADSADVEERPDSEAP", "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": "MADQKILWGIAPIGWRNDDIPEIGAGNTLSHLLSDIVVARFQGTEVGGFFPDAKTLNKELELRNLKIAGQWFSSYLIRDPFESVSKEFHAHCAYLEEVGASVAVVSEQTYSIQQSEQNIFTEKPMFTDSEWLTLCEGLNELGKIAQQYGLTLVYHHHMGTGVQTLAEVDRLMENTDPTLVSLLYDTGHIYVSDNDYMLLLTKHLDRIKHVHFKDVRSDILAKCQEQGQSFLQSFLAGMFTVPGDGCIDFTKVYDVLLTHDYRGWIVVEAEQDPAKAHPLEYALKARQYIDEKLLTTDEMKERI", "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": "MSEGPKGLAIAAPASGSGKTTLTLGLLRALTRRGLRVQPFKNGPDYIDPAFHAAAAGRASFNLDGWAMDRPQLHALAGQAAGADLVIFEGAMGLYDGPADPGRSGRGTSAEIARMFGWPVVLVLDVKGQGQSAAATALGFARHPEAPPLAGVILNHVASPRHEAMIRAEMDRLGLRVLGALPRRSDLSLPERHLGLVQAEEQAGLEATLEALADFVAAHVDLEALLSVAGAGPAPGAGAWAVPPAGRIALARDAAFSFVYPHMLEAWRRAGVTVLPFSPLADQAPDPSADLVWLPGGYPELHAGRIAAATRFKAGLRAFAETRSVHGECGGYMVLGARLVDAEGRAHAMAGLLGLVTSYEKRRLHLGYRSADLLAPLPGYGAGSRLYGHEFHYSTILEQPDAPLAKVCDAAGAPVAETGSVRGHVTGSFFHLIAG", "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": "MRMNEPVDAQPAPSFLPMSRRFRGYLPVVVDVETGGFDWNKHALLEIACVPIEMDTDGRFFPGETASAHLVPAPGLEIDPKSLEITGIVLDHPFRFAKQEKDALDHVFAPVRAAVKKYGCQRAILVGHNAHFDLNFLNAAVARVGHKRNPFHPFSVFDTVTLAGVAYGQTVLARAAQAAGLDWNAADAHSAVYDTEQTARLFCKIANAWPGPV", "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": "MRQKTSSNKKKQKNTNNISLRRKLGLMYKKAILGLKIVLMIFVCLFVFTKYFTSIKTYLITNIYQITTKLGFRLENVIIEGQQNVDELTILKVLNANKRSSIFALKLDEISNNLKKSKWIKEVYVSRRLPNTVYIKLFEREPIAIWQINNQLFLVDEEGYKISKDIQPFSHLLHVVGEGANIYASQLVLELKKYPALLNKTLVAIRVGDRRWDLNLKGNISIKLPEKEFEAALKYIDALNKNNRLFNQNYKALDLRDRNKYYIQKY", "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": "MNENLFASFTTPTMMGLPIVILIIMSPSIMFPSPNRLINNRLISIQQWLLQLTSKQMMSTHNNKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVLTGFRHKTKASLAHFLPQGTPTFLIPMLVIIETISLFIQPVALAVRLTANITAGHLLMHLIGGATLALMNISPTTSFITFITLVLLTILEFAVALIQAYVFTLLVSLYLHDNT", "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": "MQIKILGCESFGARSLACIVKTGERKILIDPGVALARLRYGLLPHPVEVAAALRVREKILAELEGTTDIVISHYHGDHMPMKAEDPYQLPVEALPDLKGVRFWCKGPGNISGLSARRRKEFFRYLGHSLPASEGISSEGVSFSPAVPHGTRDKGFGTVMMTRVSEEDEVFVHGSDIQLLDREAVMQILAWKPSVVFVSGPPLYLSHHVPEASNEALENALLLAENAGTLILDHHLLRFLEGYRWLKDLAGMVKNTVVCAAEFMGKKPELLDAQRKSLYEEMPVPRGWHEAYEKGEAGVEDYLL", "text": "SIMILARITY: Belongs to the UPF0282 family."}
+{"protein": "MAVGKNKRLSKGKKGIKKRVVDPFSRKDWYDIKAPSFFEVKNVGKTLVNRTAGLKNANDALKGRIVEVSLADLQKDEEHSFRKVKLRVDDVQGKACLTTFNGMSMTSDKLRSLVRKWQTTIEADQTIKTTDGYVCRIFVIGFTRRRYNQIKKTTYAQSSQIRAIRQKMFQVIQNQATGCSMRELVQKLIPEIIGREIEKATGGIFPLQNVFVRKVKILKSPKLDAQKLLEQHGEAQDVGTKVIKDVAPLASV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family."}
+{"protein": "MKELFKRGGIMLFDKNILQKIDEELKTYVDKDDKLYNASKHLLFAGGKRIRPYLTVVTYMLKKDDIEEVLPAAAAVELIHNYTLIHDDIMDNDDERRGKPTVHVVYGEPMAILAGDLLYAKAFEAVSRIKDNKKAHEVLKILSKACVEVCEGQAMDMEFENYYPTMEEYLDMIRKKTGALLEASVGIGAVMADCNEEEREALKEYAKRIGLTFQIQDDVLDLIGDQKKLGKPVGSDIREGKKTIIVIHALKTLDEDKKKRLLEILGNKNVKDEEIKEAIEILKPSIEYAKELMKQKTEEAKEYLKIFNKDRRKVLEDLADFIMSRIY", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MAGRSAVSASSKWLDGFRKWYYNAAGFNKLGLMRDDTLHETEDVKEAIRRLPEDLYNDRMLRIKRALDLTMRHQILPKDQWTKYEEDKFYLEPYLKEVIRERKEREEWAKK", "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": "MASIIFTPKDIFDQDFKTAVRGYSKQEVDEFLDDVIKDYETYSALVKELREENSRLKQELSKRMQEAPNSTASQVHQSFGDTTQTTITNFDILKRLSRLEKEVFGKQIQASELNQL", "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": "MSFEEEEKNKVTCTQDFLRQYFVSESVSIQFGLNNKTVKRINEDEFDKAINCIMAWTRYPEAVVKRTASTYLLSDSCKKSTTLSLPFVLDDALCIPKGVESNNNDTSLLYSDTLYGDDSLIRRNEQVRDELEEELSFTLLRSEINEIKPISSSSTPQILQSDYSAVMQETQASNGSIFQFSSP", "text": "FUNCTION: Potential transcriptional regulator that is required to activate expression of a number of early meiotic genes including HOP1."}
+{"protein": "MKKNFYTISKTMSRSLKLILFSVFIGFSIFLIPQPTWAYPFWAQQKFENPREATGKIVCANCHVASMPTRAEVPQAVAADSVFKTVVEIPYKKDLQEIGADGSKVPLQVGAVVMLPDGFKLAPQERWTDEIKEETQGVYFTQYSEEQENIILVGPLPGDQNREIVFPVLSPDPRKDSNYNFGKYSIHVGGNRGRGQVYPTGEKSNNNLFTATNSGTITSIETNEDGTQIINLNNEEGESFTENLPAGTSLLIKEGDTIEKGAKLTEDPNVGGFGQLDKEIVLQSKARVIGMIIFFIGVGLSQIMLVLKKKQVEKVQAAEGI", "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": "MQERHTEQDYRALLIADTPIIDVRAPIEFEQGAMPAAINLPLMNNDERAAVGICYKQQGSDAALALGHKLVAGEIRQQRMDAWRAACLQNPHGILCCARGGQRSHIVQRWLHDAGIDYPLVEGGYKALRQTAIQATIELAQKPIVLIGGCTGSGKTLLVQQQPNGVDLEGLARHRGSAFGRTLQPQLSQASFENMLAAEMLKTDAHQDLRLWVLEDESRMIGSNHLPECLRERMTQATIAVVEDPFEIRLERLNEEYFLRMHHDFTHAYGDEQGWQEYCEYLHHGLSAIKRRLGLQRYNELAARLDAALTTQLTTGSTDGHLAWLVPLLEEYYDPMYRYQLEKKAEKVVFRGEWAGSGGMG", "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": "MSRLLVGLKLAQSHYLSQLHKYPVATKAVTSGFLYLISDSLVQGIELSRDKDKKYDFKRSMRMAVFGFAVTGPLFHYWFKYLDKHFPKKSYRHAFIKLTIDQVVCSPVFNFLFFSGMGILEGKSKDDIVEKLKKDWLTTYVSDCVVWPFINFVNFAYISSIHRVTFMNVCNIGWGAFLAKMNSSH", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family."}
+{"protein": "MLLPDLHPYTILLSIFLVLVAKQLVATIGKSTIQEFVWLVYLKVSSNQSIKTYNSKQHELHETNRQKRAISAQDEYAKWTKLNRQADKLSAELQKLNQEIQQQKSSIDKASNALILVLTTLPIWIARVFYRKTHLFYIRQGIFPKYVEWVLALPFLPNGAVGLTIWMFAVNSVVSNFSFLVSFPFAKRVSKPVRDTKVE", "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": "MGFEWGFKPSSKITQSTVSSQGTGNVMIPTAGVKQKRRYANEEQEEEELPRNKNVMKYGGVSKRRPQPGSLIRGQPLPLQRGMELMNKNQLQQLLVDLMTKHPEIQQSVHTRVIGLDFSIQKCLDMLKQKSEAVYQSIPYNRSYESNKLDDYAFVRMKPQILEFLNCLVDFILDNIPPRLENLHASLKFLDICTELVIKLPRFELASNNYYYDKCIEQLSHVWCTLIEHVARDRIILLADNSSVWKSHMTRLQVYNEHSNGLLERPLQLFKSLDMGSPSAASSSTLSLQESIIYHHDTMTANENNNNSGSAATDSPFN", "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": "MPSILDLPIGTGATGKRKESDSLGEVEVPADHYWGAQTQRSLIHFSIGDDYMPKEVYHAYGYVKKAAALVNEAAGIIPPWKAELIARVADEVIAGKLDSEFPLYVWQTGSGTQSNMNVNEVISNRAIQLVGGSLGSKHPVHPNDDVNMSQSSNDTFPTAMHIATVLEFSNRLIPAVTVLEESIWAKAREWVDIVKIGRTHLQDATPLTVGQEWSGYATQLDDALAFVKHSLRGLYRLAIGGTAVGTGINTPPDFGEKVADEIARLTGHPFVTAPNKFAAQGSLDAMVTSSAALRTLAVALMKIANDLQWLGSGPRSGLHELILPSDEPGSSIMPGKVNPTQEEAMLMVCIQVIGEDNAVAFAGSQGNFELNAMCPIIINNVLHSARTLGDACVKFREYGINGIMLDRSRIDKFVGTSLMLVTALSPVIGYDKASAIVQRALDENTTLREAAVKGGFISAEDFDRIVDPKKMVGDPRHDLKLASE", "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": "MGVNLKDLIPEEAKMTIEDLRMLRGKIVVIDGYNALYQFLTAIRQPDGTPLMDSQGRITSHLSGLFYRTINILENGIKPAYVFDGKPPEIKAKEIEKRRKIREDASKKYEEALRKGDIEAARRYAMMSAKLTDEMVQDAKKLLDAMGIPWIQAPAEGEAQAAYIVSKGDAWASASQDYDSLLFGSPRLIRNLTISGKRKLPRKNVYIEIKPEIIELKKLLEKLGLTREQLIYVAILIGTDYNPDGVKGIGPKKALQLVKAYKTLDKILKIIPKTEFPIEPEKIVEYFLNPPVSTDYKLEWRAPDESKIREILVEEHDFNPERVKNAVERLVKAYREHIKSKQLGLEAWFS", "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": "MKLRLRHHETRETLKLELADADTLHDLRRRINPTVPSSVHLSLNRKDELITPSPEDTLRSLGLISGDLIYFSLEAGESSNWKLRDSETVASQSESNQTSVHDSIGFAEVDVVPDQAKSNPNTSVEDPEGDISGMEGPEPMDVEQLDMELAAAGSKRLSEPFFLKNILLEKSGDTSELTTLALSVHAVMLESGFVLLNHGSDKFNFSKELLTVSLRYTLPELIKSKDTNTIESVSVKFQNLGPVVVVYGTVGGSSGRVHMNLDKRRFVPVIDLVMDTSTSDEEGSSSIYREVFMFWRMVKDRLVIPLLIGICDKAGLEPPPCLMRLPTELKLKILELLPGVSIGNMACVCTEMRYLASDNDLWKQKCLEEVNNFVVTEAGDSVNWKARFATFWRQKQLAAASDTFWRQNQLGRRNISTGRSGIRFPRIIGDPPFTWFNGDRMHGSIGIHPGQSARGLGRRTWGQLFTPRCNLGGLN", "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": "MSNLFKYLPSVDSVLTRLEEEGVIDGLPRTLSRDLVNGFLDVCREEIKGGIITEEKQLSPDVLFPRLTCHVRAGAKPHFRRVLNGTGVVVHTNLGRSLLAESAVKAVTEACACYSNLEFDLKTGERGSRYSHVEKLICEITGAEAALVVNNNASAVLITLETLAKGREAIVSRGQLVEIGGSFRIPDVMTKSGAFLREVGATNRTHLHDYENAINEETALLMKVHTSNFRVIGFTKEVSGGELAELGRKHDLPVYEDLGSGNLTNFSGLGLMREPTVQEVVAEDVDVVSFSGDKVLGGPQAGIIVGKKKYIDAIKKNPLNRAVRIDKMTLAALEATLRLYLDPETAKREVPTVRMITEKPENLKKQAQALARTLRRELGETANIGVREGVSRVGGGAFPEQDLKTFLVTVVPSAKVTVEELKEGLLSTEPPLVGRIEEDAFCLDPRTLTREEYKLCAEAINQILE", "text": "FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SelA family."}
+{"protein": "MPDYQYKRIFLVVMDSVGIGEAPDAAEFNDVGADTLGHIAEKMNGLHMPNMAKLGLSHIKEIKGIPADEKPLAYYGKMQEASNGKDTMTGHWEIMGLYIDTPFRVFPDGFPDELLNELKEKTGRGIIGNKPASGTEILDELGEEHMKTGDLIVYTSADSVLQIAAHEEVVPLDELYRICEIARELTLDEKYMVGRIIARPFVGEPGAFVRTPNRHDYALKPFDRTVMNELKDDGLDVIAIGKISDIYDGEGITSSLRTKSNMDGMDKLVDTLKTDFTGISFLNLVDFDALYGHRRDPEGYGKALEEFDARLPEVFDLLKEDDLLVITADHGNDPVHHGTDHTREYVPLIAYSKKHQGANELPTSKTFADLGATVADNFKTTMPKYGTSFLSKLK", "text": "FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of pentose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphopentomutase family."}
+{"protein": "MKKTAVLNSHISSAISTLGHYDLLTINDAGMPIPNDDKRIDLAVTKSLPCFIDVLETVLTEMEIQKIYLAEEIKTANAQQLKAIKKLINDDVEIKFIAHSEMKEMLKSPLNKGNIRTGEITPFSNIILESNVTF", "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": "MELLLLSNSTLPGKAWLEHALPLIANQLNGRRSAVFIPFAGVTQTWDEYTDKTAEVLAPLGVNVTGIHRVADPLAAIEKAEIIIVGGGNTFQLLKESRERGLLAPVADRVKRGALYIGWSAGANLACPTIRTTNDMPIVDPNGFDALDLFPLQINPHFTNALPEGHKGETREQRIRELLVVAPELAVIGLPEGNWIQVSNGQAVLGGPNTTWVFKAGEEAVALEAGHRF", "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": "MRRQRRSITDIICENCKYLPTKRSRNKRKPIPKESDVKTFNYTAHLWDIRWLRHRARKTR", "text": "SIMILARITY: Belongs to the ninE family."}
+{"protein": "MYPAHLLVLLAVCVSLLGAASIPARPLNLYQFGNMIQCANHGRRPTRHYMDYGCYCGKGGSGTPVDELDRCCQIHDDCYGEAEKLPACNYMMSGPYYNTYSYECNDGELTCKDNNDECKAFICNCDRTAAICFARTPYNDANWNINTKTRC", "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": "MDWTWRILFLVAAATSAHSQVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMNPNSGNTGYAQKFQGRVTMTRNTSISTAYMELSSLRSEDTAVYYCAR", "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": "MPANLSSALETFKQQRDAAEAHYLKTNRVSVFFREYTAAVETLLAALWVEHFQNSALCLMAVGGFGRGELYPCSDVDLAVVSPAPLSDGIQEQIARFVQTLWDCKLMPSVKSGGIDELCESVRNDITGDTAFLEARFLFGNRQTADELAEKMNAQRNVAAFIEAKLVEMEHRHAKSQGSGAVLEPNIKSCPGGLRDIHTLLWIAKAQGLATNLPALVKQGILTRTEAGMLSHGYRRLAHIRIHLHLNAKRAEDRLLFDLQPQVAESMGYQGLNLRRQSEELMRVFYRAIKTVKQLSGILTPMLQSRVSSTPLRVTLRIDDDYIQVNNQIAARHTDIFFRRPEHIFKIVEIMQQRNDITALEPQTLRAWWGATRKINRSFYQNSENRHRFAGFFRNGNGLTQTLRFLNLYGVLGRYLPAWEKIVGLLQHDLFHIYPVDDHILTVVRNVRRLALDMHSHELPYASALMQSFERQDILYLAAFFHDIAKGRGGDHAIQGIADARQFAADHFLTEEESDLLAWLVENHLLMSTVAQKEDIQDPSVLDAFCKRVQTHERLSALYLLTISDIRGTNPKLWNAWRASLLESLFHAAGRYLAGNGGNPHALFGRRQQEAADLLTRAAVPEKQQKKLWNALGSAYFARHQSREILWHAANLVHDFETPIVRSRILPQSDSFQVMVFMPNGPRLFARLCRIFSRHGFDILAARAFITEHDYILDTFIVQIPSQHAPEDYPDIQSALEAELNSFIHGHTVAEISSHSRRISRRSRYMPIAPSITITPEEDYPDWYSVEITAVNRPFLLADMAEIFFAHNVSLRYAKISTLDERAEDSFTVFSPDLKNPKIQSSLKQALLEQLA", "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": "MGNFVCIEISGDQMLDRIIRCLCGKGYIRNLEKNLRALQREMEDLRATQHEVQNKVAREESRHQQRLEAVQVWLDRVNSIDIECKDLLSVSPVELQKLCLCGLCSKYVCSSYKYGKRVFLLLEEVTKLKSEGNFDEVSQPPPRSEVEERPTQPTIGQEEMLKKAWNRLMEDGVGIMGLHGMGGVGKTTLFKKIHNKFAETGGTFDIVIWIVVSQGAKLSKLQEDIAEKLHLCDDLWKNKNESDKATDIHRVLKGKRFVLMLDDIWEKVDLEAIGIPYPSEVNKCKVAFTTRDQKVCGQMGDHKPMQVKCLEPEDAWELFKNKVGDNTLRSDPVIVGLAREVAQKCRGLPLALSCIGETMASKTMVQEWEHAIDVLTRSAAEFSDMQNKILPILKYSYDSLEDEHIKSCFLYCALFPEDDKIDTKTLINKWICEGFIGEDQVIKRARNKGYEMLGTLIRANLLTNDRGFVKWHVVMHDVVREMALWIASDFGKQKENYVVRARVGLHEIPKVKDWGAVRRMSLMMNEIEEITCESKCSELTTLFLQSNQLKNLSGEFIRYMQKLVVLDLSHNPDFNELPEQISGLVSLQYLDLSWTRIEQLPVGLKELKKLIFLNLCFTERLCSISGISRLLSLRWLSLRESNVHGDASVLKELQQLENLQDLRITESAELISLDQRLAKLISVLRIEGFLQKPFDLSFLASMENLYGLLVENSYFSEINIKCRESETESSYLHINPKIPCFTNLTGLIIMKCHSMKDLTWILFAPNLVNLDIRDSREVGEIINKEKAINLTSIITPFQKLERLFLYGLPKLESIYWSPLPFPLLSNIVVKYCPKLRKLPLNATSVPLVEEFEIRMDPPEQENELEWEDEDTKNRFLPSIKPLVRRLKIHYSGMGFLNVKNQNPRFFFYCFIYLLVVHLDCIIDLHSDTSGMCCVVHLDYVFHFPFVFPKTFCILFRLHFYTIKSLCV", "text": "FUNCTION: Probable disease resistance protein. SIMILARITY: Belongs to the disease resistance NB-LRR family."}
+{"protein": "MPYNCCLPAMSCRTSCSSRPCVPPSCHGCTLPGACNIPANVGNCNWFCEGSFNGNEKETMQFLNDRLASYMEKVRQLERENAELECRIQERNQQQDPLVCPAYQAYFRTIEELQQKILCGKSENARLVVQIDNAKLASDDFRTKYETELSLRQLVEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHEQEVNTLRCQLGDRLNVEVDAAPTVDLNRVLNETRCQYEALVETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDIRSRLECEINTYRGLLESEDCKLPCNPCATTNACDKPIGPCVPNPCVTRPRCGPCNTFVR", "text": "SIMILARITY: Belongs to the intermediate filament family."}
+{"protein": "MQITKTAVAGTLESSDVQIRIAPSTTMDIEINSSVAKQFGEDILNSVTAVLAQFEVSSAQIIIEDKGALDCVLRARLKAALLRATDEALAWEKIL", "text": "FUNCTION: Covalent carrier of the coenzyme of citrate lyase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CitD family."}
+{"protein": "MAARMCCKLDPARDVLCLRPIGAESRGRPLPGPLGAVPPSSPSAVPADDGSHLSLRGLPVCSFSSAGPCALRFTSARRMETTVNAPWSLPTVLHKRTLGLSGWSMTWIEEYIKDCVFKDWEELGEEIRLKVFVLGGCRHKLVCSPAPCNFFTSA", "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": "MIVTQIAGKIQVIFGPMFSGKTTELIRRIKRFNFANKKCLLIKYSKDTRYNDNIDKSFLVTHDKQNYQAFPCSILEDVKEQAQNYDVIGIDEGQFFPDVVQFSEDLANQGKTVIIAALDGTFQRKPFQSVIDLVSKAEYITKLTAVCMVCYNEAAFSKRIVESDDIELIGGIDKYISVCRGCYNSDQNEGNSTKPSKTARHSHSQSAPSVAPLAVNINPDDHLNNDY", "text": "SIMILARITY: Belongs to the thymidine kinase family."}
+{"protein": "MDSYEPSQLIWARLLLYEISKRNGETEYQHTNGPVWWGPNDNKTVYLSITDCSGFVNALLRKSFELSQKDMVEWFDSQRPLAVDYYNTIYHQNGFTRIKNIYKLEPGDFIAIKFPNHHPSLDDTGHIMMINSYPEIMASKNLPDEYQNYNNILQFRVNVIDQTATPHGRYDTRYSPDDNQNGLGSGYIKLYTNIDGTIIGYSWSLSKKSRYIDKTVHPIVVGRLDIY", "text": "SUBCELLULAR LOCATION: Virion."}
+{"protein": "MGIRIYRSYTPGTRNRSSSDFSEITKSKPEKSLLAKKTQKAGRNHRGVITVRHRGGGHKQRYRIVDFKRNKRDIEAKVASIQYDPNRNARIALLHYKDGEKRYILAPKNLSVGAQVSAGETAPLDVGNALPLSNIPLGTSVHNIELLPGKGGQIIRAAGTSAQIVAKEGNFVTLKLPSSEVRMVYKQCYATIGEVGNAEFKNLTLGKAGRKRWLGIRPTVRGVVMNPCDHPHGGGEGRSPIGRARPVTPWGAPALGMKTRRKNKYSDFCIIRRRK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
+{"protein": "MANLKEIRDRIVSVKNTRKITEAMRLVAAAKVRRAQEQVLRSRPFADRLARVLENIQSRMKFEAADSPLLKARAVQKVTLLAVTGDRGLCGGYNTNVIKRTEQRYGELSSQGFEIDLVLIGRKAITYFQNRSSQYKIRASFQDLEQVPTSKDAEEATSEVLSEFLSESTDRVEIIYTKFISLVSCDPVVQTLLPLDPQGIAKEDDEIFRITTKGSRFVIEKDPAPANEEPVLPSDVVFEQSPDQLLNSLLPLYLQNQLLRALQEAAASELASRMTAMNNASDNAKELAKTLNLTYNKARQAAITQEILEVVGGASV", "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": "MDVDVEEAALEQVAALLQRPDQLEKLPELKKRADRKKLAVEAMLRTGVQGQLEGIRTAIAHLQTASDDITAISQGVHDIRERLGPFPQLKEKLRELRDANARHGQYAAAMENLKHIFNLQTTLQEIRDALDDEKSGGNLLLAHKHIMDLERARDELLAEVHKMSGTNTEKEQMLLVNFFKGVDSVVAELSKNMWFILGRTLEMVKGNEQGGGPQQVVTCLRIVEREERIDKFYMEARSKNSSAFVPPGRPRNWKEKALRSLEKTVSNRVDGNQLEDRSLNKAWLARYLEVCKNVIMDDLQLAKVAIPCFPPDWQIYDRYVHMYHTSVCRRLREVASEHLEKSELVQLMSWIKFYASEDMLGHPKLRINAQAILQDSPVLSRSTLNQLCDQFVEMSRDDLKLWLKNTVSHETHDWYKNLRPSEDNHGYFYTDLPNTVFGMLKDTVTLAKEVSVEVIPSIINLTIQEFNELAGKYRDAFTAYKTDYFAERSKYQEFTSNIIAIANNLHTCIESTEKYKQQIRLSMEGEQNAAAAMTTPLASGRRTAVRQQQLIENMDALNTKWSNAASVAVNYLREEVITDIAPSLVEIFSKKWLTGSAALETVCMTISDYYHDHKHLRPVTRSTLLMDLQFRIVSEYLKAIETKRVSLNSYEERALAGKRMKADVVRLDNLYAEFATSSDMADQLPLLTSIVAAAGDVISLKDKSLLSLEATSFARKFPNCPAELLSAVIATRDDISGSEARSLASEVLQHVQFHPKDQIFDQLFALRQQENSERLPNLGMANMFKADFMSMLKRDA", "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": "MRSFRSLHLLLLAASAITADAVPAGSSITPPPPVEPVSLLSSHSNPQRPWTRLRNWVIESIWGIPKSQTSRPTAHDYSAPLQGSTRYGSDVVLRFRVQGLDEAEALTEATNILFLDVWASTTEFVDIRLAKEVIPSLLGLLPDSLQTAYVPLIDNLPEAISATYPARRSLGLNDQFMPSPSTRAPDLFFEDYQPLSVITPWMQLMASMFSSHARMINVGVSYEGRQIPALRLGRSSQPGESRPMILIVGGNHAREWISTSTVAYIAYNLMTRYGSSAAVTSLLQDYDWVLVPTVNPDGYVYTWDSDRLWRKNRQPTSFRFCPGIDLDRSWSFEWDGNQTQTNPCSENYAGEEPFEGVEAQQLAEWALNETEHNNARFVGFLDFHSYAQQILYPYTYSCSSVPPTLESLEELGLGLAKVIRLTTHEIYDVTSACEGVVIPASGDKSAKSLFPVGGSSGGSGLDWFYHQLRTRYAYQIKLRDRGSYGFLLPSEYIVPTGTEAFNAVLKLGQFLTEQDYPGIRNIDWESEYQVGDETPTQESTAFTDESHEEEGKDVTVDTDDEDDDYYDRWEPLKWEDQRPLGFRRRR", "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": "MASSSLFLLGALLVLASWQAIVAYDPSPLQDFCVADMNSPVRVNGFACKNPMDVSSEDFFNAAKFDMPRNTFNKLGSNVTNLNVMEFPGLNTLGISLARIDYAPMGVNPPHIHPRATELLTVLEGTLYVGFVTSNPNKLFSKVVCKGDVFVFPKAMIHFQMNLDHDKPAVAQSALSSQNPGVITIASAVFGSQPPISDDVLTKAFQVEKKLIDWLQSQFWENNY", "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": "MNDIWWQTIGEGDCHLVLLHGWGLNAQVWDCITPQLASHFTLHLVDLPGYGRSGGFGAMSLEAMAQRVLEQAPPQAVWLGWSLGGLVASQVAIMRPERVQALVTVASSPCFAARDDWPGIKPEVLAGFQQQLSDDFQRTVERFLALQTMGTESARQDARALKQAVLSLPMPSAEALNGGLEILRTVDLRQALVRLPMPFLRLYGRLDGLVPRKIVPLLDDLWPESESILFDKAAHAPFVSHPAAFCEPLLALKTRLG", "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": "MPIGVPKVPFRSPGEEDAAWVDIYNRLHRERLLFLGQELDSEISNQLVGLMVYLSIEDKTRDFFLFINSPGGWVIPGIGLYDTMQFVPPDVHTICMGLAASMGSFILVGGEITKRLAFPHARVMIHQPASSFYEAQAGEFVLEAEELLKLRETLTRVYVQRTGKPLWVVSEDMERDVFLSATEAQAHGIVDLVGDENMGDLV", "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": "MFMRLKVLEMNSIRRQTLLRQFTNVYNVVSRSARLCSQAIPKRLFYSTGSRANSIPDALSRLRNIGISAHIDSGKTTFTERVLFYTGRIKDIHEVRGKDNVGAKMDSMELEREKGITIQSAATYCNWKRKQKDGDEQDYIINIIDTPGHIDFTIEVERALRVLDGAVLILCAVSGVQSQTITVDRQMRRYNVPRITFINKMDRMGANPWRAIEQLNAKLRIAAAAVQIPIGSEDNLEGVVDLIHMQSIYNRGKKGEKVEITGSIPEHLKELANEKRALLIETLANIDEEIGELYVMEETPSPEQLMSAIRSATLSRQFTPVFMGSALANIGVQPLLDAVCDYLPNPSDVTNTALDVNQGEKSVTLHTDYNEPLVALAFKLEDGRFGQLTYMRVYQGVLKRGNQITNVNSGKRIKVPRLVLLHSDEMEDVEEAPAGSICAMFGVDCASGDTFTDGSIKYVMSSMYVPEPVVSLSIKPKNKDSPNFSKALARFQREDPTFRVHIDKESNETIISGMGELHLEIYLERLAREYRTECITGKPRVAFRETITTKAPFSYLHKKQSGGAGQYAKVEGYIEYMEPKEDGNGRLVDHEFVNHVVGGAIPSQYIPACEKAFKECLERGFLTGHPIKNCRLVLEDGAAHSVDSSELAFRVALTHAFRQAFMAAKPIVLEPIMNVTVTAPVDDQGVVIGNLDKRKATIVNTDIGEEEFTLQAEVPLNSMFSYSSDIRSSTQGKGEFTMEFLKYLPAPGYVQKELIAEYEKQHK", "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": "MRLLPLFLMVTLAASGCGIVESKKIDYKSSNKLPTLEIPPDLVAPTADNRYAIPDTEGSGTATLSTYSAERKAAPSGTPSLLPAQDKARIERAGTQRWLVVQATPQQVWPVIKDFWQENGFIVNLESPETGVIETDWAENRAKIPQDVIRRTLGKVLDGLYSTAERDKFRTRIEAGSGGTEIYLSHRGMMEVYATEGKDKTVWQPRPADPELEAEMLRRLMLRFGVEENRAQTLLTAKQTPDQARVIRDAGGSLLEMDEGFDRAWRRVGLALDRVGFAVEDRDRSKGTYFVRYIDPDADNASKRDEGMFAKLAFWRSKKDQASPQLQIVVDEAGEGKSRVRVAGGEGRAADAATQNRIINLLHKELK", "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": "MSLEGIGFGYRERAPYASNPAFSRGRLVPEPESPTRTPFQRDRDRIIHSTAFRRLKHKTQVFIAHEGDHYRTRLTHTIEVAQIARALARALRLDEDLAEAVALVHDFGHTPFGHTGEDALNERMKNFGGFDHNAQSLRIVTKLEHRYADFDGLNLSWETLEGLVKHNGPLLGPYAAHPDIPVPQPILDFNARYDLELSRFASLEAQCAAIADDIAYNAHDIDDGLRAGLLTLESLDEVPLAKRLLDIVRTRYPNLDPVRTGHELVRRQITIMVEDVIEEAQRRLASARPGTMEDVHNQPRALVGFSDAMRAEEKVLKRFLFKNLYFHESVVVRRHAADRIVQDLFDACFTDPSLMPDEWRLGCEALDKAALARRVADYLAGMTDNYAVREHRRLFDRTPDLA", "text": "SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily."}
+{"protein": "MSLDNLKSGLPEYAKDLKLNLGSLARSTELTEQQLWGTFLAVAAATRNEAVFSEISEEASEHLSEEAINAALGAASIMAMNNVAYRAKGWLGDDYAQVKMGLRMNIIAKPGVDKVDFELWSLAVSTVNGCEHCTIAHEKTVRSEGLTKEQIFEAVKIAATLQGVAQAIEIEASR", "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": "MGRLFVIDLEGLVYSCKYCQTHFAVTNDIISKSFHCKHGRAYLFDNVVNVTVGEKEHRVMITGWHTVADIFCVSCGSLVGWKYEIAYDKSQKYKEGKFILERFKVLGPYGGGYDMNQNEPMTGSDDEE", "text": "SIMILARITY: Belongs to the yippee family."}
+{"protein": "MNHFELFGLVEGFELDTRKLADTYRQLQTQFHPDRFATAPEREQLVAVQRAAQINDAYTTLKTPLRRAEYLLSLRGTDIRGEQQTLQDTSFLMQQLEWRERLADLKGEADPEGAIKDFRQEIGHDHQLLMQQLTLTLAAGDDLIAADCVRKLKFVDKLLEELERFEDSLFES", "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": "MGDNYSTYLLDIEGTVCPISFVKETLFPYFTKKVPQLVQQDTRDSPVSNILSQFHIDDKEQLQAHILELVAKDVKDPILKQLQGYIWAQGYESGQIKAPVYADAIDFIKRKKRVFIYSSGSVKAQKLLFGYVQDPNAPAHDSLDLNSYIDGYFDINTSGKKTETQSYANILRDIGAKASEVLFLSDNPLELDAAAGVGIATGLASRPGNAPVPDGQKYQVYKDFETL", "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": "MRHGDISSSNDTVGVAVVNYKMPRLHDRAGVLENARKIADMMIGMKTGLPGMDLVVFPEYSTQGIMYNEEEMYATAATIPGDETAIFSAACREADTWGIFSITGEQHEDHPNKPPYNTLILIDNKGEIVQKYRKILPWCPIEGWYPGDTTYVSEGPKGLKISLIICDDGNYPEIWRDCAMKGAELIVRCQGYMYPAKDQQVMMSKAMAWANNCYVAVANAAGFDGVYSYFGHSAIIGFDGRTLGETGEEEYGIQYAQLSVSAIRDARENDQSQNHIFKLLHRGYSGVHAAGDGDKGVADCPFEFYKLWVTDAQKAQERVEAITRDTVGVADCRVGNLPVEKTIEV", "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": "MSDALPMSPAEFEQALRAKGAYYHIHHPYHVAMYQGRATREQIQGWVANRFYYQVNIPMKDAAILANCPDREVRREWIQRLLDHDGAPGEDGGIEAWLRLGQAVGLDPDQLRSQELVLPGVRFAVDAYVNFARRASWQEAASSSLTELFAPQIHQSRLDSWPQHYPWIDPAGYEYFRTRLGQARRDVEHGLAITLQHYTTRAGQERMLEILQFKLDILWSMLDAMSMAYELNRPPYHSVTQERVWHKGITL", "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": "MLEQQPTQNPLTVSMLNAQAQQVDRPLRENVKQAVRNYLRNLDGQDPTELYELVLSEIEHPMLDMVMQHTRGNQTRAATMLGINRGTLRKKLKKYGMG", "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": "MEAAKVYTQDGTVDLQGRPVLASKTGRWRACSFLLGYEAFERMAFYGIASNLVNYLTKRLHEDTISSVRNVNNWSGAVWITPIAGAYIADSYIGRFWTFTASSLIYVLGMILLTMAVTVKSLRPTCENGVCNKASSLQVTFFYISLYTIAIGAGGTKPNISTFGADQFDSYSIEEKKQKVSFFNWWMFSSFLGALFATLGLVYIQENLGWGLGYGIPTVGLLVSLVVFYIGTPFYRHKVIKTDNLAKDLVQVPIAAFKNRKLQCPDDHLELYELDSHYYKSNGKHQVHHTPVFRFLDKAAIKTSSRVPCTVTKVEVAKRVLGLIFIWLVTLIPSTLWAQVNTLFVKQGTTLDRKIGSNFQIPAASLGSFVTLSMLLSVPMYDQSFVPFMRKKTGNPRGITLLQRLGVGFAIQIVAIAIASAVEVKRMRVIKEFHITSPTQVVPMSIFWLLPQYSLLGIGDVFNAIGLLEFFYDQSPEEMQSLGTTFFTSGIGLGNFLNSFLVTMIDKITSKGGGKSWIGNNLNDSRLDYYYGFLVVISIVNMGLFVWAASKYVYKSDDDTKEFSGGGCVQMEAKALDTSPLSI", "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": "MDSAARPVSFPKSRWYAKSSKPKAPYKLPESVKPPQSEQPSSTPKPEYSAEQTEFDTKADPAGNAAPEASEATESKPQQPLPDLTQGIPSTLAAELEGRTKKSGQTSLNLTEDPSRFEDYTDDGRGDIPKDGYVSSLDRRRARMANLMYAFFLLAGAGGVAYLGRNWETEEEAKAHPDIPSGWSFSSWYNRMKARLSDITSYYKDPAFPKLLPDEDPNLRQPYTLVLSLEDLLVHSEWSREHGWRIAKRPGVDYFLRYLNQYYELVLFTSVPSMMADQVLRKLDPYRIIRWPLFREATRYKDGEYIKDLSYLNRDLSKVILIDTKEEHARLQPENAIILDKWLGDPKDKNLVALIPFLEYIAGMGVEDVRPVLKSFEGTSIPVEFAKRERIMREKFEKELEEERKRRPKRGVGSLASALGLKSTRTLDGEQSPSEGLAQGKMLWDQIRERGQKNYEMIEKEIRENGEKWLAEMAAEEEKARQEQMKMMKGSFTSMFGAGKQ", "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": "MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELAREYRFKHSGWQWSGVPLIAANMDTVGTFSMARVLAGFDVLTAVHKHYSVEQWQSFVSSVGEETLRHVMVSTGTSEADFIKLRQILALSPSLKFICIDVANGYSEHFVDFLRRARDVCPDKVICAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTMPGDVAKAFGGGADFVMLGGMLAAHAECEGRIVEEQGRKMMLFYGMSSASAMNRHVGGVADYRAAEGKTVSLPLRGPVENTVRDILGGLRSACTYVGASRLKELTKRTTFIRVAEQENRVFGRAD", "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": "RRLSLHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGTFEGGLKGGVKIVFSPEEAKAVSSRMIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGIKKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDWTQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKLSEIVTLAKQAHLDVKFQLPI", "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": "METTYRREALTVRVIFCTSGDSAETIADVLTGAPTSASFFSVLHDLFYSQILAPRVTLKLCLPARRPGNGTRCSPVLVLRTDASVASGFLGGRPLEASDIKYMLLSDQTAGLFKPLLEIIGGARAPPNQDACTFQSQVAWLRTKFVTALRKLYKMTPSPYWMLSAFGAQEAQFVLTSSFYFFEHTVVCTTETVSHLSRLFSPQQGQTLVSVTSHEELGQLYGTSPFRRRVPAFVAYVKEKLARDSLETEAIDRTIDQIRGKLMLSNQDLVHFIYISFYQCLNKRAFLRYSRQTSSSSALRELGEDPQLCGALHGEFRDHVQSYYHKKTYLSTYIDIRYVGGVLPDGYFGGSLVGERCVYWCGQSKDTASLLATISQQVPHLRLQNEFAGMLDVAALRGSDDGQFKEGLFSHSQALPLYRCEFLGKQFFTMLQEDGLERYWEQSVIFPGDQDWDMLSDKDLTYRIFYHDLSLSLPTLKEQLLVSRHEYFNPRLPVYRWVLDFDLPVCRDIDRTFEEVHSLCCSLREAILDIIQLLGPVDPRTHPVYFFKSACPPDEWRGEDVASTSFCRCHDKLGMRIIVPFPEGVCVVGSEPMVALTGILNRTIKLDPELVHRFPSIQKKGGPFDCGIYGRGRSVRLPHCYKVGLVGELCRLLKILVCHPAPNGKAQYVRRAFTLRELLHHSPGHSAGHVGRIIYSIMDRNENFLENKTISYLPAKIPHIFQRIETLSGRSIEDWLHSAVWDKAYDTICKFFPDEKAQQFSHVAFTQQGENIIQLRPRQGRHFLCINHNHKNKSKTVRVFLTLHSIRVSEVTVTLMSQCFASKCNNNVPTAHFSFVVPVGLAS", "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": "MTDLTTHDLAQPGWQTRDHLNDPVVGELCNRFGPDAFTVQATRTGIPVVWVKREQLLDVVTFLKKQPKPYVMLFDLHGMDERLRTHREGLPAADYSVFYHLISIERNRDIMLKVALAENDMHLPTVTKLFPNANWYERETWEMFGMAFDGHPNLTRIMMPKTWEGHPLRKDYPARATEFDPFELTKQKEDLEMESLTFKPEEWGMKRGTENEDFMFLNLGPNHPSSHGAFRIILQLDGEEIVDCVPDVGYHHRGAEKMGERQSWHSYIPYTDRIEYLGGCVNEMPYVLAVEKLAGIEVPDRVKTIRVMLSELFRINSHLLYISTYIQDVGAMTPVFFAFTDRQKIYDLVEAITGFRMHPAWFRIGGVAHDLPRGWERLLREFLDWMPARLDTYVKSALQNTILKGRTQGVAAYNAKEALEWGVTGAGLRATGIGFDVRKWRPYSGYENFDFEVPVGDGISDCYSRVMLKVEELRQSLRILDQCLKNMPEGPFKADHPLTTPPPKERTLQHIDTLINHFLQVSWGPVMPANESFQMVEATKGINSYYLTSDGGTMSYRTRIRTPSYAHLQQIPSVIRGCLVSDLIVYLGSIDFVMSDVDR", "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": "MAKIQFSRGLDEVVIPEVRLTRSRTGDSGTATFIFTNPKILDQGSTEDITGMYLSDEEGEIITREVKAKFVNGKPEALEALYVMKSAQEWDRFMRFMERYAEENDLGLSKAEK", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the Psb28 family."}
+{"protein": "MVKNAFISVISQEEKEENKGSAEFQVFNFTNKIRRLTSHLELHRKDYLSQRGLRKILGKRQRLLAYLSKKNKVRYKELISQLDIREPKIR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
+{"protein": "MTEAKGDIGLIGLAVMGENLVLNMESRGFTCSVYNRTTSKVDEFVQGRGKGKKFIGCHSLETLVQSLKTPRRVMLMVKAGEVVDHFIQLLLPLLEKGDIIIDGGNSLYTDSDRRTKDLDAKGILFIGTGVSGGEEGALLGPSIMPGGNPKAWEHVKPIFQAISAKVQPGDQPCCDWVGDGGAGHYVKMVHNGIEYGDMQLISEAYFILKHYLGLSNDELQKTFAKWNTGDLDSYLIEITADIFAKKCEKDPNTYVVDTILDSAGQKGTGKWTAINALDVGIPLTLVAESVFARCVSSFKEERVKASTILAGPNPNEANKKFTGDKEQVIEAVRQALFASKLVSYAQGFTMMKAAAKEYKWNLNYGNIALLWRGGCIIRSTFLGEIKGAFDKNPQLDNLLTDCWFRDKLAAAQDGWRQVASISVLHGIPTPAFTSALSYYDSYRCAKLSANLVQAQRDYFGAHTFQLLDDPKGAPVHVNWTGRGGSTHSTTYSI", "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": "MIIRPSEPEVKIAVDRDPVKTSFEEWARPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTGDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALIFASLMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQIHVSLPINQFLDAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYAEFLSFRGGLDPITGGLWLSDIAHHHLAIAILFLIAGHMYRTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSTTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPIFAQWIQNIHAGAPGVTAPGATTSTSLTWGGGELVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGTISDQGIVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIIQGRAVGVTHYLLGGIATTWAFFLARIIAVG", "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": "MSLISRLRAVVAGDDYLDGDLDDLVYDDDQPEQDQRASQADGGALATIGDGNPFDLGDNFSGSNVIGMPGISTAAAEVNLMEPRSFDEMPRAIQALRERKTVILNLTMMEPDQAQRAVDFVAGGTFAIDGHQERVGESIFLFAPSCVTVTNTSHDEASTPTVVSRDAEAEQQQEAAAAPSPAWGATAL", "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": "MWLTLITGALILLLTWDFGRKRQRVLAFEKSAIPGPISIPILGCGLQALHLGAENIIGWVGEKFDKYGKTFRFWILGESLIYTKDLQYFETILSSTTLLEKGQLYEYLRPFLNDGLLVSTGRKWHARRKIFTHAFHFKVLEHYVEIMDRHSSVMVDNLRKVADGKTAVDMLKYVSLAALDVITEAAMGVQVNAQNDPDFPYIKALKSVVYIQPDRMFRFSRRYNWLFPLAAPLLHRQLLSDIRVMHDFTDKVISERRETVRRAKADGTYRPLSLGDAEIGSKSQMALLDILLQSSINNQPLSDADIREEVDTFMFEGDDTTSSGVSHALYAIARHPEVQQRIFEELQRVLGPDASAPVTQAQLQDLKYLDCVIKETMRLYPPVPAIGRHAQKELEIGDKTIPANTSIYLVLYYAHRDANYFPDPLSFRPERFLEDQEQGHNTFAYVPFSAGPKNCIGQKFAVLEMKVLISKVLRFYELLPLGEELKPMLNFILRSASGINVGLRPRKALR", "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": "MKFDTVIMGGGLAGLLCGLELQKHGLRCAIVTRGQSALHFSSGSLDLLSTLPDGQPVTNITEGLNALREQAPTHPYTTIGASAVLELAQQAQALLEASGAHLQGDVQQSHQRVTPLGTLRATWLSSPEVPVWPLAAQRICVVGISGLLDFQAHLAAASLRQHHLTVETAEIDLPELDVLRDNPTEFRAVNIARLLDNEEKWPLLHDALLPIAKTCDMIIMPACFGLADDSLWRWLNERLPCSLNLLPTLPPSVPGIRLHNRLQRQFVRQGGIWMPGDEVKKVTCRNGVVSEVWTRNHADIPLRPRFAVLASGSFFSSGLVAERDGIREPIMGLDVQQTATRAEWYQRDFFDAQPWQQFGVTTDDALRPSLAGQTVENLFAIGSVLGGFDPIAQGCGGGVCAVSALHAARHIAERAGGQQ", "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": "MKGFNCNGQVILISGGSQGLGESFAKRFVQDDDGPGSNTNKVIIVSRSQSKLVKACERIGVDGVSLDRYVNDTNRNETKLIYHSCDTSSYDKVALMFKLLVKSELVPSQVYMCAGGSIPKLFLDLTPEELQNGITTNYSTAVNLAHVSLKHDVPHLLFFSSEVAFFPFIGYAQYAPLKQSIRSLVAILRQEHSSTRITCVYPGNFQSEGFDLENITKPAITKEIEGPSNPVTAAQCRDKIISSLKWGLDDITTDSIGWLLMACDQGLNKHSTSQFMFVFSWILGALLNITIVPIYMLICKFQIYQWKRNKDTK", "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": "MFNQAAQELTTIRDVLRFAVSRFNEAGLFFGHGTDNAHDEAVYLILHTLNLPLDMLAPYLDAKLLEAEKEEVLAVIERRAVEHIPAAYLTHQAWQGEFDFYVDERVIVPRSFIYELLGDGLRPWIEYDELVHNALDLCTGSGCLAIQMAHHYPDAQIDAVDVSLDALEVAGINIEDYGLEERIQLIHTDLFEGLEGTYDLIVSNPPYVDAESVGALPEEYLHEPELALGSGADGLDATRQILLNAAKFLNPKGVLLVEIGHNRDVLEAAYPELPFTWLETSGGDGFVFLLTREQLLGEE", "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": "MGHNQPMQSSNPQEHFVQIALDIEHRLTTPISLTSDSNQRRNQWVTIIICTILAVTGQCIARLLENYYFLHKNLSRRRGILTQTLLQVVGFPILLLPFLLHFLIKKQKQLLIFSGETSLKHLAITYSILCIYMFCQAFFSDVRNQIPYRVFTLTYTTQLLFTLIFSKYYNDIKFNRWTFISLILAVLAGAFTLYTFSAGSPIYGKKSYGYGIINVAFGAAIFFSLLLCIIRKVFEELISFCNTSTNRKQPSFVVVLEMIIFLSLVVTIILVAAVLISGEHHDMKKEMETFTKGDIAYVRTMVGQAVAWQIYWVGIVGLVFAVSAVFSNVISVCTWPIVSLLVAFLYNTHDHFDVFRGIALGAAALSVSCYIYIIHKEKSDDDDQSTS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the purine permeases (TC 2.A.7.14) family."}
+{"protein": "MKKTFFIADLHLSENRPHLTELFVHFMQTQAPQAEKLYILGDLFDFWIGDDEQSALIETVQQQILQLTQKGISCYFIHGNRDFLVGRQFANSCGMELLPTYQIVNLYGKKVLICHGDTLCTDDLAYQQYRKKVQQKWLQWLFLHLPLKVRLKIAEKIRQKSKTDKTHKSIEIMDVNKDFVEQIMQQFQVNILIHGHTHKQNIHQNPPHFTRIVLGDWGATASVLEVSANGFQFI", "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": "MSTENMIRDVELAEEELQRKARGPQGPGRCLCLILTFFLLLAGATLLFCLLHFGVIGPQNEEASTDAFLGMKPVTQRVRSCQTESNKPVAHVIADPLAEGKLQWLKRRANVLLSNGMDLVDNQLVVPSTGLYLVYSQLLFKGEDCANEPLLLTHTVSRVALSYQSKVNLLSAIKSPCQKTVKGAREASPWYEPIYLGGVFQLEKGDKLSADTNYPNYLDFAESGQVYFGVIAL", "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": "MKVLCFGMGQAGGNVLDALLRYEQRTNADYVVDAVAYNTASADLRGLDLVPEENRILFGADEVSGHGVGADNELAAELAERDSRQLLRGTDGAPTSTADAFLIFAGLGGGTGSGAAPVLAKHLNRIYEQPIYGVGILPAADEGALYSRNAARSLKALVDVTDHVFAFDNGAWAESGEDVAQAHDTMNEVLVRRLGILFASGEVAESGTVAESVVDSSEVINTLRGGGISTIGYAASELPESDGGGGFSIKGLLGGDSSSTDELDSINRITTQTRKAVLGQLTLPCDVDSASRGLVVVSGPPEWLNRKAVERSRTWVEEQTGSMEVRGGDYPLSESNHVGVLVLLGDVSRSDRVAEIRSTAVEAEQNRRERIASDAADREDGTEAVVDDRLDSLF", "text": "FUNCTION: Involved in cell shape control. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CetZ family."}
+{"protein": "MVRAARRKRASEDDLSRGCRAGQDCPIDIKNKYEQNTLADRILKWVSSFLYFGTLGISSGKGTGGATGYTPIGGGGVRGGKGANVVRPTVLVDALGPTGVPIDPVTPDEALVPLLESSGGSTTLDVPPGGEIEVIAEVHPPPAAGDPEITIGHPEEPPILEVIPETHPTTRVRTTVSKHDNPAFTAYVASAQLPGETSASDNVFILHGFNGEYVGPAQTGEDTVFEEIELENFGVPESPPSSSTPNTSFRNILNKFQRRLYNRRLVQQVKITDRTFLTKPSKLVSWEFDNPTYTDDSLSLIFQQDVDEVSAAPMAEFQDIVTLSRPVVYEREGLVRVSRLGQRGTIRTRSGLRIGGHVHYYTDISPIRPVEDIEMRTLGEVSGDSVIMQPLAESTFVDSGDVLNEGNIEFPDSTLEDDYNEDFSRARLEITTSARSRTSIVTVQEGIPPGSVKLFINDAETIVTPHGPESNDTDRYQPFIPVTPAATPDIIITFEEGTATFFLHPSLLKRHKHKHWFF", "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": "MLFNKDKNNIGGRSIESTGFAWWSGNARLINLSGKLLGAHVAHAGLIVFWTGAMTLFETSHFIPEKPLYEQGMILLPHLATLGWGVAPGGEIVNTYPYFATGVIHLVSSAVLGFGGIYHSIVGPDVLEDSFSFFGYDWRDKNKMTTILGIHLILLGIGAFLLVIKALFIGGIYDTWAPGGGDIRFITNPTLNPAIIFSYLLKSPFGGEGWIVGVNNMEDVIGGHIWIGVTCVIGGIWHILTRPFSWARRAFVWSGEAYLSYSLGALALMGQTAAEYAWYNNTVYPSEFYGPTAAEASQAQAFTFLVRDQRLGANIASTQGPTGLGKYLMRSPTGEVILGGETMRFWDLRAPWLEPLRSSNGLDLNKIKNDIQPWQERRAAEYMTHAPLGSLNSVGGVATEINSVNYVSPRSWLTTSHFFLGFFIFIGHLWHAGRARAAAAGFEKGINRENEPVLSMRPLD", "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": "MRYIELAQLYQKLEKTTMKLIKTRLVADFLKKVPEDHLEFIPYLILGDVFPEWDERELGVGEKLLIKAVSMATGIDSKEIENSVKDTGDLGESIALAVKRRKQKSFFSQPLTIKRVYQTLVKVAETTGEGSQDKKMKYLANLFMDAEPIEAKYIARTVLGTMRTGVAEGLLRDAISLAFNVKVELVERAYMLTSDFGFVAKIAKTEGNDGLAKVTIQIGKPIKPMLAQQAANIKEALLEMGGEAEFEIKYDGARVQVHKDGEKVTIYSRRLENVTRAIPEIVEAIKEALKPAKAIVEGELVAIGEDGRPLPFQYVLRRFRRKYNIEEMMEKIPLELNLFDVLYVDGVSLIDTKFMERRKKLEEIVEANGKVKIAENLITKNVEEAEQFYKRALEMGHEGLMAKRLDAIYEPGNRGKKWLKIKPTMENLDLVIIGAEWGEGRRAHLLGSFILGAYDPETGEFLEVGKVGSGFTDDDLVEFTKMLRPLIIKEEGKRVWIQPKVVIEVTYQEIQKSPKYRSGFALRFPRYVALREDKGPEDADTIERIAQLYELQERMKGKV", "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": "MDIERVEQVRAVERLAHRRGLALMPRAGLAAADFVAARLPAGAQVLALAGPGNNGGDALVAATLLQARGYRVAVVMPAGPARLPDDARRAWQDWCAAGGQASADLPAHAPALVIDGLFGIGLARPLGGAWQGLIDQVNAWRVPVLALDVPSGLSAASGQPLGDPPGRPVRATWTLSFIGVPAALRAPGAAAWCGQQHLSLLGLTPAFLAEAVGPCGQATATAARRSGP", "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": "MTISALELISYYTKFLSMLSQDEINKKLEEWPKHYDPKGIELKWQNIWMTKEFWEKVFRFRDEDEKSPVFVIDTPPPFTSGELHMGHAYWVTISDTIGRFKRLEGYNVLLPQGWDTQGLPTELKVQYKLKVPKENRELFLKKCIEWTEDMIKSMRTAMIRLGYRAEWERFEYRTYESKYRRIIQKSLIDMHKMGLVEMREGPVYWCPKCETALAQSEVGYKEEDGVLAYILFPFVDGEGGVTIATTRPELLGATQAVAVNPDDERYKSLVGRKVKIPLFDKEISIIADKAVEMTFGTGAVMISTYGDPQDIRWQLTYRLPVYEVVDDKGKIKNTNGLLDGLTVKEARKKIIEILKEKGYLIKVEKITHNVLAHTERSDCLSPIEFLIKKQIYIKVLEWRNKLLEDYKKMKFTPQRMSYYLEEWIKNLEWDWNISRQRVYGTPLPFWYCDNGHLIPAPEEVLPIDPSKVNPPVEKCPHCGLDLKPVKDVADVWVDSSVTVLYLTGFYDDKSRFTKTFPSSLRLQGTDIIRTWLFYTYYRTLALAGNIPFKEVLINGQVLGPDGTRMSKSKGNVVSPLDKVDEYGADAIRLTLLDAKIGDDFPFKWDTVKSKKLLLQKLWNAGRLSYPFIGKKKINKPSKLHEIDKWILQEHKKFVQQSIEAYRNYDFYIVVESIYSYFWETIADEYLELIKHRLFMEDESAIYTLSRIIKDLLILLYPIAPHITEEMYERLYGDKMSIALENLPDTSDLEDDGEAQKLGEYIKKATSAIRTLKIQNRLAIPTPISVKIYGPDDFIAKIKIIEEDLKKTLKLIDIIYQENNEIKVELLSDHGS", "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": "MTNNQQQPITIKISEFEGPLDLLLHLIRQNKMDIYDIPIAAITQQYLDYLHSMRALKLDIAGDYLVMAATLMTIKSRFLLPQPEPDEMDEDNEDDDPRDSLVAELLAYKVYQEAAGELREKEQARHQHFTREAMLVPADLSAPKLTAGITLDDLQAAFRQLVAKRRRVRPLTKTVVAETINIDERMTQITTQLQHQPQGLDFADLFTVSASDEMLVTTFMAVLELTKQDQVALQQAEPLSPIHLYLRQDEQHDEH", "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": "MKLTCVLIIAVLFLTAYQLATAASYAKGKQKHRALRPADKHLRLTKRCNDRGGGCSQHPHCCGGTCNKLIGVCL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
+{"protein": "MALLQIAEPGQAAAPHQHRLAVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSRYSSLPYEFVASENGLPLIITAQGPKSPIEVSSDILLRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTKLKPQTANQQRELITLANQAKITLTNEKSAVISWQDFSVEISREQFNELIYPLVKRSLLTCRRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTDSDMLLLDVVPLSLGIETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLSVTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALQADGAELLSTDEFHHIETVLKQLMDVKQGSDRDAIAQGIKALDTATQEFAARRMNASINKALTGKNLSDIENP", "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": "MRTPLIDLRGIRKSYGGGDSPLVNVLRGIDLSIHTGEFVAIVGASGSGKSTLMNILGCLDRPTSGEYLFAGENVAALGSDELAWLRREAFGFVFQGYHLIPSGSAQENVEMPAIYAGTPAAERHARAAALLDRLGLASRTGNRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMTLLDELASQGHVVILITHDREVAARAKRVIEISDGLVISDTAQDASDVQRSVNPAALQAVDLRKRLSEGSGSQSAWQGELFDAIRAAWRVMWINRFRTALTLLGIVIGVASVVVMLAVGEGSKRQVMAQMSSFGSNIIYLNGKAPNPRAPKGVITLEEVAALGELPEVKMIMPVNGGQAGVRYGNLDHSSYVGGNDTHFPAIFNWPVVEGSYFSEADEQNAAAVAVIGYKVRQKLFGEQSDPVGQYILIENVPFQVVGVLQEKGATSGDLDSDNRIAIPYSSASIRLFGTQDPEYITIATRDANNVKQAEQSIRNLLQQLHHGKQDYELTNNAAMIQAEARTQNTLSLMLGSIAAISLLVGGIGVMNIMLMTVRERTREIGIRMATGARQSDILRQFLTEAVMLSVVGGLAGIVLALGMGAALLLSKVAVAFTLPAVAGAFACALITGVIFGFMPARKAARLDPVAALTSE", "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": "MTKAVLTSISQLALKALLYEVSLSPKPGLVDRFDNGAHDDMSFMTFIDSMIALSPFFQAYIETGFAYAKEEPLLLFNRLRQLGQKAEEIMFCATQGINTHKGLNFSMALLLGATGAYLARTPHLMTDLGCFSKEDTLAICRLVKPMTAHLIQADLGHLNTKKEFTYGEQLFVTYGIKGPRGEASEGFTTLTDHALPYFRQMISQNDPETSQLRLLVYLMSIVEDGNLIHRGGIEAWKGVKADMRLLLQQDLSTTDLRLALSSYNQCLINQHLSPGGAADLLALTFYFAFLEKLL", "text": "SIMILARITY: Belongs to the CitG/MdcB family."}
+{"protein": "MISLESQVLERHLSFFDGKSVLFAGGISDNFPQTLASKCSSIQIWSCYFDYARTQSAVNFSVEFQGQADLIVYYWTKNKQEVNFQLIQLLAQASIGQEILIIGENRCGVRSVEKTLAPYGEIAKIDSARRCGLYHFSLQNKPHFELKNFWKTYQHPTIQDLTIYSLPGVFSAAELDTGTELLLSTIDNKIKGKVLDLGCGAGVIGSVIKKSSTNAQITMTDIHAMALESAHKTLSENQLQGEVYASDVFSDIEGKFDLIISNPPFHDGIDTAYRAVTELITQAKWHLNQGGELRIVANAFLPYPELLRQHFGDYEILAQTGKFKVYSVKN", "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": "MIPPEIRRSVLLQKAIKLALAGTLLTFASFSATAADPSSDTETPQPPDILLGPLFNDVQNAKLFPDQKTFADAIPNSDPLMILADYRMQRNQSGFDLRHFVDVNFTLPKAGEKYVPPAGQSLREHIDGLWPVLTRSTKNVEKWDSLLPLPESYVVPGGRFREIYYWDSYFTMLGLAESGHWDKVADMVANFGYEIDAWGHIPNGNRTYYLSRSQPPFFAFMVELLAQHEGDDALKEYLPQLQKEYAYWMEGVETLQPGQQNQRVVKLEDGSVLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLSTIRTTTIVPVDLNALLYQLEKTLARASAAAGDRAKASQYDALANARQKAIEMHLWNNKEGWYADYDLQNNKIRNQLTAAALFPLYVNAAAKDRAAKVAAAAQAHLLQPGGLATTSVKSGQQWDAPNGWAPLQWVAAEGLQNYGQDDVAMEVTWRFLTNVQHTYDREKKLVEKYDVSSTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPQEKPCDSVPSTRPASLSATPTKTPSAATQ", "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": "MKIRASVRKICEKCRLIRRRGRIIVICSNPKHKQRQG", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
+{"protein": "MSHRDTLFSAPIASLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPNTQVYDLGCSLGAATLSVRRNISHPGCRIIAIDNSPAMVERCRRHIDAYKAPTPVEVIEGDIRDVAIENASLVILNFTIQFLEPGDRQAILNKVYQGLNPGGALVLSEKFSFEDAHVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLRQAGFEHAELWFQCFNFGSLVAVKSGEQA", "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": "MATLEAIKYDGEKLLVLDQIKLPLETHYDEVLSIQDGWDAIREMRVRGAPAIAIVAALTIAVVMKRSTFATAAELAAFVRTSLEHLRTSRPTAVNLFEMAGRLEALLQEQPADCTEAALRQAVLSYIEGMMQADIADNQAIGKFGAEAILKDLSADVKVKVLTHCNTGSLATARYGTALGVIRSLHEQQRLEHAFCTETRPYNQGARLTAYELVTEGIPGTLVADSMVSLLMKQKGISAVVVGADRVVANGDTANKIGTYQIAIAAKHHGVPFFVAAPLTSVDLKLSHGSEITIEERPGKELTHIFGQQLAAPGIGTWNPAFDVTPADLITGIITERGVAYKAEGQQEFDMASFAASVGRA", "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": "MKSVNTIHEVKNIVKDWKKQGLSVGLVPTMGYLHEGHGSLILKARENSKVVVSIFVNPMQFGPTEDLEKYPRDLEKDLKYCEELGADLIFSPEPGEMYPEGFCTSVDMSVLTEELCGLSRPSHFKGVCTIVNKLLNIVNPDRAYFGEKDAQQLVIVKRMVRDLNMDIEIVGCPIIREKDGLAKSSRNTYLNSEERRAALVLSKSIFTGKDMVKKGCRETDVLLKKMKAIIDQEPLARIDYLKAVDTMTMQQVDTIDRPVLIAMAVYIGNVRLIDNFSFIPD", "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": "MGKPKGLCTARKLKTHRQEQRWNDKRYKKAHIGTRWKSNPFGGASHAKGIVLEKIGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPNDGCLNFVEENDEVLVSGFGRSGHAVGDIPGVRFKIVKVANTSLIALFKGKKERPRS", "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": "MSSAAPAPSTHAAKSIRKNGKNWHDNKKPFRPNGGLTSYTKRAAARKEQEAIKEYEKELREEREAERQAHIQRIKERRAAKEEKERYEKMAEKMHRKRVERLKKREKRNKLLNS", "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": "MEEFVRQCFNPMIVELAEKAMKEYGEDRKIETNKFAAICTHLEVCFMYSDFHFINEQGESIIVELDDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGAEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFVSPKEAKKQLKKDLKSQGQCAGSPTKVSRRTSPALRILEPMWMDSNPTATLRASFLKCPKK", "text": "FUNCTION: May play a role in the modulation of host immune response. SIMILARITY: Belongs to the influenza viruses PA-X family."}
+{"protein": "MSIDINWEAATSGPDGEKLAERIRSFIHDKFQQIALPRFIRSVEVNSFDFGTVSPELQVRDICDPFNDFYEEDEDGEDLSESSVSDEPAPSSQGLSQSTPNGDAGSSNSSSNGDGGGNTNSRVGYFQRRYPSGEYAGDFPQPLMSPINLGESFNPYLFPRAGTPGIPGGTSNLGYYNMPRGGLSGTQTPLASVASVARGGPLSLAEGWPPPARQRERARSSDADVDSPQSRSRPSTSSTRQRTSTDGGTPHDSAEIPESESVITGHLDSALPTRRMREQKPDDFQVLCRLQYSGNMRLSITAQILLDYPMPSFVGLPLKLNITGFTFDGVAVVAYIRKRIHVCFLSPEDADTLLGADDKMASTEGYHDHHNHHHSGNTNTTGSRRSNDSLLREIRVESEIGRKESGKQVLKNVGKVEKFVLEQVRRIFEEEFVYPSFWTFLV", "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": "MFLPQEFIRRKRDGQPLDRDDMAAFVRGVTDGSVTEGQVAAFAMAVYFNDLSTDERVALTLAQRDSGDVLDWRALDLGGPVIDKHSTGGVGDVVSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLSAIPGYDVMPDTDAFRRTVREVGVAIIGQTARLAPADKRIYAIRDVTATVESVAMITASILSKKLAAGLDGLVMDVKVGSGAFMPTAEKSAELARSIVDVGNGAGMKTTAILTDMNQSLAPCAGNALEVACAIDYLTGKSRPARLHDVTMALSAELLVTGGLARDAAHAREKLQQALDSGAAAERFARMVAALGGPADLLDAPARHLARAAVIVPVPAPVSGVVQRVDCRALGLAVVALGGGRTRAEDAIDVSVGLSALAEIGQRIEAGEPLGFVHARDEAAAAHAVDAIRRGYVLGETGEAPPTLYQRVD", "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": "MEFFLDTANLEEIRKAKAQGLMDGVTTNPTLLSREGGDWRKQAEAICAEVEGPVSLEVVGESAEEMIREAEDLASFGDNVVIKVPMTNEGLVATESLYRKGVKTNVTLVFSPLQALLAAKAGATYVSPFVGRLDGIAHDGMELIRQIRTIFDNYDFPTKILVASIRHPMHVLDSALIGADVATIPYSVISQLAAHPLTDKGLAAFNADWEKLTK", "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": "MSILTYLEFHLYYTLPVLAALCWLLKPFHSQQDNLKYKFLMLMAASTASIWDNYIVYHRAWWYCPTCVVAVIGYVPLEEYMFFIIMTLMTVAFSNFVMRWHLHTFFIRPNTSWKQTLLVRLVPVSALLAITYHAWHLTLPNKPSFYGSCILWYACPVLAILWLGAGEYILRRPVAVLLSIVIPSVYLCWADIVAISAGTWHISLRTSTGKMVVPDLPVEECLFFTLINTVLVFATCAIDRAQAILHLYKSSVQNQNPKQAISLFQHVKELAWAFCLPDQMLNNELFDDLTISWDILRKASKSFYTASAVFPSYVRQDLGVLYAFCRATDDLCDDESKSVQERRDQLDLTRQFVRDLFSQKTSAPIVIDWELYQNQLPASCISAFRAFTRLRHVLEVDPVEELLDGYKWDLERRPILDEQDLEAYSACVASSVGEMCTRVILAQDQKENDAWIIDRAREMGLVLQYVNIARDIVTDSETLGRCYLPQQWLRKEETEQIQQGNARSLGDQRLLGLSLKLVGKADAIMVRAKKGIDKLPANCQGGVRAACQVYAAIGSVLKQQKTTYPTRAHLKGSERAKIALLSVYNLYQSEDKPVALRQARKIKSFFVD", "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": "MRLFAFLWSSVAFLSTVQAQVSQTASQTQDDSSTPTPTPTDKYVNIADALRTKTPMATPNRTIMPTRQDPRATEPPTPEPTYLPTPSPTPAPTPDPGPWVAKWMDHDQVQPFKQPDPVTVSEKAAVKFKPQIHITNGCHPYPAVTWWGETSGGLKTKGAPSAGCKGSGWGSQVYGRSTWVKGVWAIMYSWYFPKDSPSTGLGHRHDWEHVIVWIDNPDIENPKILAVTPSAHSGYSKQVPPSADCVDGTSVKVKYESKWPINHALESTTEGGETQDLIMWNQLSENALRAMNSVTWGDANCPFCDGNFQAKLDKAWPF", "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": "MDILKSEILRKRQLVEDRNLLVENKKYFKRSELARKEEEAYYERCGYKIQPKEDDQKPLTSSNPVLELELAEEKLPMTLSRQEVIRRLRERGEPIRLFGETDYDAFQRLRKIEILTPEVNKGLRNDLKAALDKIDQQYLNEIVGGQEPGEEDTQNDLKVHEENTTIEELEALGESLGKGDDHKDMDIITKFLKFLLGVWAKELNAREDYVKRSVQGKLNSATQKQTESYLRPLFRKLRKRNLPADIKESITDIIKFMLQREYVKANDAYLQMAIGNAPWPIGVTMVGIHARTGREKIFSKHVAHVLNDETQRKYIQGLKRLMTICQKHFPTDPSKCVEYNAL", "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": "MSDLVSRPGLSERTARAVADRLAGRAGWRNPLIFAGPAVVASIAYMDPGNFATNIQAGARYGYDLLWVVLLASLIAMLFQGLSARLGIVTGRNLAELCRDTLPPALTIPMWIISEIAAMATDLAEFLGGAIGIALLAHLPLMAGMAITGIVTYGILLLDRRGFRPMELVIGALVGVIALCYLAELLIVPVHWRQAALHTVLPSLPDAEALTIAVGIVGATVMPHALFLHSGLSGARVAPQDAAQRRRLVRYSNIEVLAALGVAGMVNMAMVAMAAGAFHPAHQGIAEIGEAYRTLSPLLGAGAAVIFLISLLASGVSSSVVGTLAGQMVMQGFVGFSIPIWLRRALTMIPGFVVIGLGVNPTRALVLSQVVLSLALPVPMLALLWFSTRRALMGALAVRGITAIAAIGGAIVILGLNVILLLQIFGVNVPLPG", "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": "MQNKNNYNWLKEWVIRSFLLLTLLTWPSVSNAYPIFAQQGYENPREATGRIVCANCHLAKKPVDIEVPQSVLPDTVFEAIVKIPYDMQVKQVLANGKKGGLNVGAVPILPQGFELAPSDRIPTEIKEKIGNLSFQNYSPDKKNIIIVGPVPGKKYSEIVFPILSPDPASNKESNFLKYPIYVGGNRGRGQIYPDGSRSNNTVYNASATGKVIKIFRKEKKGGYEITIEKTSDGRQVVDIVPPGPELIISEGEFLKVDQPLTNNPNVGGFGQGDAEIVLQDPLRIQGLLLFFASVVLAQIFLVLKKKQFEKVQLAEMNF", "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": "MLIIELLKAIFFGIIEGITEWLPVSSTGHLILVQEFIRLNQDKAFIEMFNIIIQLGAIIAVMLIYFERLNPFQPGKTAREVQLTWQLWLKVVIACIPSILIAVPLDNWFEAHFYFMVPIAIALIVYGIAFIWIEKQNAQQEPAVTDLARMSYKTAFFIGCFQVLSIVPGTSRSGATILGAIILGTSRTVAADFTFFLAIPTMFGYSGLKAVKFFLDGHHLDFAQVLILLVASLTAFVVSLLAIRFLTDYVKKHDFTIFGKYRIVLGSLLLIYSFFKFVF", "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": "MRNIAFLIGLFFIGYSSCVLHATPTRASLVEKSDAESTHVEQWDSNGKRTLQADDRERILAEERGMEQTLLPAAEAIGKTKVSEKAVSRASLGSKLNPMTWPKRILYKIKLWYARFRQNLLKRATMDEESIDRSMMSGLTPFALKKIKNDIFHYSSSVPRDAIKIEKDYNSYVDQFFGQFNGLFKDPPVFEMAKWKKLEADMTSTEQIVERTALNKVSQYIDKGFSNEKLISLDVSPFVYMRLLEKRGVFKDVENNIDKIEHLKVYVKAYEEHLMV", "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": "MEYQGQHGGHASSRADEHGNPAVTTGNAPTGMGAGHIQEPAREDKKTDGVLRRSGSSSSSSSSEDDGMGGRRKKGIKEKIKEKLPGGNKGNNQQQQQEHTTTTTGGAYGPQGHDTKIATGAHGGTAATTADAGGEKKGIVDKIKEKLPGQH", "text": "SIMILARITY: Belongs to the plant dehydrin family."}
+{"protein": "MTPHINAKIGDFYPQCLLCGDPLRVSYIAKKFLQDAKEITNVRNMLGFSGKYKGKGISLMGHGMGIASCTIYVTELIKTYQVKELLRIGTCGAISPKVGLKDIIMAIGASTDSKTNRVRFLNHDLSATPDFELSLRAYQTAKRLGIDLKIGNVFSSDFFYSFETHAFDLMAQYNHLAIEMEAAGLYATAMELSAKALCLCSVSDHLITKEALSPKERVESFDNMITLALEMMS", "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": "MADAVTPRDEDYSQWYQDVVRNGQLAENSPARGCMIIKPNGMALWENMRDQLDQMFKDTGHQNYYFPLFIPERYMEREAEHVEGFAKECAVVTHSRLTQDEEGDLVPDPESELGENYIVRPTSETIIWDTYSKWIQSYRDLPLLYNQWANVVRWEMRPRLFLRTAEFLWQEGHTAHATETEAVEEAERMLDVYTTFAEEYMAMPVLQGRKTESERFPGAVDTYCIEAMMQDGKALQAGTSHFLGQNFAKAFDCTFTNEDNEEEYVWATSWGVSTRLIGGLIMTHSDDQGLVLPPKLAPHQVVIVPLFFDDDQEGPVMETCERLQERLEDHGIRVKMDQNHTQSPGWRFSEHELRGVPLRLAIGPRDLENDNVEMARRDTQEKEVVPQDGIAERVSDTLDDIQHALHERAQDRQADNTRVVEDYDAFREVIGRGGFAWAHWDGTPETEARIQEETSATIRLIPFDREDHEEGEDMLTGEPSEGRVLFAQAY", "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": "MGPVMLDVKGYELDAEEREILAHPLVGGLILFTRNYHDPAQLRELVRQIRAASRNHLVVAVDQEGGRVQRFREGFTRLPAAQSFAALSGMEEGGKLAQEAGWLMASEMIAMDIDISFAPVLDVGHISAAIGERSYHADPQKALAIASRFIDGMHEAGMKTTGKHFPGHGAVTADSHKETPCDPRPQAEIRAKDMSVFSSLIRENKLDAIMPAHVIYSDVDSRPASGSPYWLKTVLRQELGFDGVIFSDDLSMEGAAIMGSYAERGQASLDAGCDMILVCNNRKGAVSVLDNLSPIKAERVTRLYHKGSFSRQELMDSARWKAISTRLNQLHERWQEEKAGH", "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": "MSTAELACSYAALILADDGVEITADKIQTLLGAAKVADVEPIWTSLFAKALEGKDIKDLLTNVGSGGAAAPAAVGGAAAGAAAPAEAAAAEEKKEEEKEESDEDMGFGLFD", "text": "FUNCTION: Plays an important role in the elongation step of protein synthesis. SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family."}
+{"protein": "MDFEQLKQDVIAYSKTIGIDKIGFASASPFEELKQRLIQQQQLNYQSGFEEPDIEKRTNPQLLLPGAKSIIAIALAYPSKLKNAPLSKRGERRGIFCRASWGQDYHLVLRDRLQKLEAYLIEKLPDIEVKSMVDTGELSDRAVSERAGIGWSGKNCSIITPEFGSYVYLGEMITNVPFPPDKPIEDQCGGCTKCIDICPTGALIQGGQLDSKKCIAFLTQTKGFLPEEYRDKIGNRIYGCDTCQTVCPKNKGMDFHNHPEMEPDPELVKPLLTPLLTISNRDFKEKYGIMSGSWRGKKPLQRNAILALAHFKEASAIPDLIGVMKDDPRPVLRGTAAWALGKIGGDGVGEAIEKAMEREKDEEVLHEMNRGLELLAQKKE", "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": "MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANAGQISPGYAAPWAAPGVPLKAVKWMFEKHAPLAIRLDGTRFQLQWMVQMLRNCTAERYAVNKGRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQLDGAAKDIAVLQEANVPFELLSPAELKHAEPALAAVSHKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCGSETVRADAYVVALGSYSTNFISNLMKIPVYPLKGYSITAPIVDAAAAPVSTVLDETYKIAITRFDQRIRVGGMAEIVGFDKTLRAARRETLEMCVNDLFPGGGDTSKATFWTGLRPMTPDGTPIVGRTPVSNLFLNTGHGTLGWTMSCGSGQLLADLISGKKPAIQADDLSVHRYLKDAPGQTRPAYA", "text": "FUNCTION: Oxidative deamination of D-amino acids. SIMILARITY: Belongs to the DadA oxidoreductase family."}
+{"protein": "MINAPVFRRVLALLGDLRLAILLLLVIAIASMAGTVIEQGQSLSFYQANYPENPALFGFLSWRVLLALGLDHVYRTPWYLTLLVLFGASLTACTLTRQVPALTTAQRWHYYQEPRQFTKLALSTTIPQGSLTALATALRAKGYRVWQTDTQLYARKGLVGRLGPIVVHASMLLILLGGILGALTGFMAQELIPSGETVHLQHIVEAGPLARIPQDWSVKVNRFWIDYTDAGEIDQFYSDLSIQDAKGQEVKRGTIHVNRPLRYGGVSLYQADWGIAAIRFRLNRSPVLQLPMAPLDTGGKGRLWGTWLPTRPDLSAGVSLIARDLQGTVLLYGPKGEFLTSLRTGMSTEVNGVTLTLVELVGSTGLQIKADPGIPLFYAGFALLMAGVIMSYVSHSQVWGLQENQRLYLGGRTNRAQLAFEQELVAIARELAPPSQTTAVDL", "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": "MENIDIRGARTHNLKNINLTIPRNKLVVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDSIEGLSPAISIEQKSTSHNPRSTVGTITEIYDYLRLLFARVGEPRCPDHNVPLTAQTISQMVDKVLSLPEDSKMMLLAPVVKNRKGEHVKILENIAAQGYIRARIDGEICDLSDPPKLALQKKHTIEVVVDRFKVRSDLATRLAESFETALELSGGTAIVAEMDNPKAEELVFSANFACPHCGYSVPELEPRLFSFNNPAGACPTCDGLGVQQYFDEDRVVQNPTISLAGGAVKGWDRRNFYYYQMLTSLAKHYHFDVEAPYESLPKKIQHIIMHGSGKEEIEFQYMNDRGDVVIRKHPFEGILNNMARRYKETESMSVREELAKNISNRPCIDCGGSRLRPEARNVYIGRTNLPIIAEKSIGETLEFFTALSLTGQKAQIAEKILKEIRERLQFLVNVGLNYLSLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLNTLIHLRNLGNTVIVVEHDEDAIRAADHIIDIGPGAGVHGGQVIAQGNADEIMLNPNSITGKFLSGADKIEIPKKRTALDKKKWLKLKGASGNNLKNVNLDIPVGLFTCVTGVSGSGKSTLINDTLFPLAQNALNRAEKTDYAPYQSIEGLEHFDKVIDINQSPIGRTPRSNPATYTGLFTPIRELFAGVPEARARGYNPGRFSFNVRGGRCEACQGDGVLKVEMHFLPDVYVPCDQCKGKRYNRETLEIRYKGKTIHQVLDMTVEEAREFFDAIPMIARKLQTLMDVGLSYIRLGQSSTTLSGGEAQRVKLATELSKRDTGKTLYILDEPTTGLHFADIKQLLEVLHRLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGQIIATGTPEQVAKVTSSHTARFLKPILEKP", "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": "MKIPLILVTIAIILLMVPTESDAFDLGGLIKGVVDLFGRRSLKNRDYFDYMQDPSLSNADLRELEELLEDY", "text": "FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family."}
+{"protein": "MFTTVRPQSTLTPPTANLIPNDLFTAINELKKDLNAVILAHYYQDPDIQDIADFIGDSLALSQQAASTNAEVIVFAGVHFMAETAKILNPDKLVLLPDLNAGCSLADSCPPEAFAQFKAQYPGCLVVSYINCTAEIKAMSDIICTSSNAVKIVNQLPKDRPIIFAPDRNLGRYVMEQTRRELILWQGSCMVHETFSEKKIVQLKIEYPEAEIIAHPECEPSVLRHANYIGSTTALLNYSQQSASQIFIVATEPGIIHQMEKETPHKRFIPAPAINNCACNECPHMRLNTLEKLYLAMKFKQPEITMDETIRLAALRPIQRMLEMS", "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": "MLAQFYVNLVVLLVLLICGLLSQNAAVTIAAGVLIVIKITPLNQFFPYIQAHGLNLGILILTIGVLTPIASGKLSGESILKSFISFKSLVAIAIGLLVAWLGGRGVKLMSSQPDVVAGLLIGTVAGVALLRGVPVGPLIAAGLLSLFIGK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0756 family."}
+{"protein": "MSHEEDLIDYSDEELQTTDAAATTAAPAANGAQDKKGDLTVSGGRPDKKGSYVGIHSTGFRDFLLKGELLRAITDCGFEHPSEVQQVCIPTAILNVDVLCQAKSGLGKTAVFVLTTLHQLEPVPGECSVLVMCHTRELAYQIKNEYARFSKYLPDVKTAVFYGGTPIQKDIEVLSNKESYPNIVVGTPGRLNALVREKKLSLRNVKAFVLDECDKMLDQIGKQAQIAHMRRDVQEIFRATPADKQVMMFSATLSQEIRPICKKFMRNPLEVYVDDDTKLTLHGLQQYYIKLSESEKNRKLNELLDSLEFNQVIIFVKSTLRANELDKLLRECNFPSIAVHSGVSQEERIKRYKEFKEFNKRICVATDVFGRGIDIERINLAINYDLPADADSYLHRVGRAGRFGTKGLSISFVSSEEDEKVLKEIEKRFEVALPEYPEGGVDSSTYMA", "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": "MNIQEEIKKRRTFAIISHPDAGKTTITEQLLYFGGEIREAGTVKGKKTGTFAKSDWMDIEKQRGISVTSSVMQFDYDGKRVNILDTPGHEDFSEDTYRTLMAVDAAVMVVDSAKGIEAQTKKLFEVVKHRGIPVFTFMNKLDRDGREPLDLLQELEEILGIASYPMNWPIGMGKAFEGLYDLYNQRLELYKGDERFASLEDGDKLFGSNPFYEQVKDDIELLNEAGNEFSEEAILAGELTPVFFGSALTNFGVQTFLETFLKFAPEPHGHKKTDGEIVDPYDKDFSGFVFKIQANMDPRHRDRIAFVRIVSGEFERGMSVNLPRTGKGAKLSNVTQFMAESRENVTNAVAGDIIGVYDTGTYQVGDTLTVGKNKFEFEPLPTFTPEIFMKVSAKNVMKQKSFHKGIEQLVQEGAVQLYKNYQTGEYMLGAVGQLQFEVFKHRMEGEYNAEVVMNPMGKKTVRWIKPEDLDERMSSSRNILAKDRFDQPVFLFENDFALRWFADKYPDVELEEKM", "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": "MRLRNGTVATVLVFITTFLSLSWYTAWQNGKEKLIAYQREFHALKERLRIAEHRTLQRSSELNAILEQFRRAVAETNGSKNALNNFSDETLKLLKELTSKKSLQVPNIYYHLPHLLKNEGSLQPSVQVGLGRTGVSIVMGIPTVKRKVKSYLTETLHSLIDKLSPEEKLDCVMVVFIGETDLDYVNNVVASLEKEFSTEINSGLVEVIAPPATYYPDLTNLKETFGDSKERVRWRTKQNLDYCFLMMYAQKKGVYYIQLEDDIVVKQNYFSTIKNFALQLASEDWMILEFSQLGFIGKMFQSPDITLIVEFIFMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKSNLRIRFRPSLFQHVGLHSSLAGKIQKLTDKDFLKPLLHKIHVNPPAEVSTSLKVYQGHTLEKTYVGEDFFWAVTPVAGDYILFKFDKPVNVERYLFHSGNPEHPGDILLNTTVEVLPFQNEELVLSKETKDKRLEDGYFRIGKFENGVAEGTVDPSLNPISSFRLSVIQNSAVWAILNEIHIKKMTN", "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": "MFRLVSSNAQGSFRSSLLTKVRIPISVPASSPLNTSTSNNTTTNNNNFGVNNSTNNTQFTRHQSSAAVDLSARKVYQDEFLRSHSSFTAPDHETKVKLNHFKELLVTGNQKLRALNRQEARAFYSVLQSLSHMLEDAKLRRSLNVDLLHQYSLLLHSAIFSSRTNRLAEKRNRDKDEYNATSYTDEVVLRGSVLNFAQLVEAGEFKYCFTDKVLQYLLYSMFQFKFNTEALNLWENGVNDAETGSVYLRPLVLATVLPRAFELKRFTYEEILHIYELNTKKEQFPHHTLVTAMGKIAIHAGDYSRALDFLERLLEKYDQKPTGLKLASLSDLHLSFIGDCKEIAIAKHFFDKVIEDELPYKVLLKVPYVTSLLDNAYQAGDSLEEAIYFWKNSVAYYMKTRQQLNSRYSLLNNKFFELFFQAYPELNEESFAMLRDLITFYAQTKPLDETFLNTIITHYSWKSKEVLDQLMQNYEIYEVERTPVSHRICLKKTGQYADYTNEEILARWNENLKCLDNSKYFYIPNADWSALRDATIYSIVPDKRTDLYYSVLNTYKNYMQDARACIKFVGNWTKRPAYLESIARITLEKNFEPAVKVDVPLFRNLKENVNYADATRDLIITARNSKPRV", "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": "MSTELIKTRAIYSGTGRRKCSVAQVRLVPGSGNLIINGIPGESYLQFSPNYLRVSYAPLQVLGLLNQYDIHVNARGGGLTGQADAIRLGVARALCSINPENRTTLKSEGYLTRDPRVKERKKYGLKKARKAPQFSKR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
+{"protein": "MKTLLLTLVVVTIVCLDLGYTMTCYNQQSSEAKTTTTCSGGVSSCYKETWYDGRGTRIERGCGCPRAKKGIERICCGTDKCNN", "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": "MSSKQVPDTLTFECETGNYHTFCPISCVAWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIFAEPRYAMAELEEGDISAQLNDYEELKRLCVQIKKDRNPSVIVWIGTCTTEIIKMDLEGMAPRLEAEIDIPIVVARANGLDYAFTQGEDTVLAAMANRCPEWIQNAQNNNDQDQAIQGLMSFFPLKNTKLSSEPTLLSNHPPLVLFGSLPSNVASQITLELKRQNIHVSGWLPAQRYSELPSVGEGVYVCGVNPFLSRTATTLMRRRKCKLIGAPFPIGPDGTRAWIEKICSVFGIEPQGLEEREAQVWKGLQDYLDLVRGKSVFFMGDNLLEVSLARFLIRCGMIVYEIGIPYMDKRYQAAELALLQQTCEQMGTPMPRIVEKPDNYNQVQRMRELQPDLAITGMAHANPLEARGISTKWSVEFTFAQIHGFTNARDILELVTRPLRRNLSLEDLGWSALVKRDKINLV", "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": "MESDNLQDPQEETLTCSICQSIFMNPVYLRCGHKFCEACLLLSQEDIKFPAYCPMCMQPFNQEYINDISLKKQVSIVRKKRLMKYLNSKEHKCVTHKAKKMIFCDKSKILLCHLCSDSQEHSGHTHCSIDVAVQEKMEELLKHMDSLWRRLKIQQNYVEIERRTTLWWLSVKLREEVIKRVYGKQCPPLCEERDQHIECLRHQSNTTLEELRKSEATIVHERNQLIEVYRELMTMSQRPYQELLVQDLDDLFRRSKLAAKLDMPQGMIPRLHAHSIPGLTARLNSFRVKISFKHSIMFGYTSVRPFDIRLLHESTSLDSAETHRVSWGKKSFSRGKYYWEVDLKDHEQWTVGVRKDPWLRGRSYAATPTDLFLLECLRKEDHYILITRIGGEHYIEKPVGQVGVFLDCEGGYVSFVDVAKSSLILSYSPGTFHCAVRPFFSAVYT", "text": "SIMILARITY: Belongs to the TRIM/RBCC family."}
+{"protein": "MADFDMVLKCWGPMEADHATHGSLVLTRLFTEHPETLKLFPKFAGIAHGDLAGDAGVSAHGATVLNKLGDLLKARGAHAALLKPLSSSHATKHKIPIINFKLIAEVIGKVMEEKAGLDAAGQTALRNVMAIIITDMEADYKELGFTE", "text": "FUNCTION: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. SIMILARITY: Belongs to the globin family."}
+{"protein": "MRLKIGIIGAMAQEVEILRNLMVEAKVIEIAGCKIYDGKINNTQVALLQSGIGKVAAAVGTALLLELTKPDVIINTGSAGGLDANLNVGDIVISTEVRHHDADVTAFGYEKGQLPANPAAFLPNEQLVSVALKETQTAGFNAVSGLICSGDVFVNGAEKIAQIRQDFPNVAAVEMEAAAIAQVCHAFNVPFVVVRAISDVADKESHLSFDEFLPLAAKNSSEIVVAMLNNFA", "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": "METATLIAIFISCSLVSFTGYALYTAFGQPSKELRDPFEEHED", "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": "MAINIILLGPPGAGKGTQARRLIDERGLVQLSTGDMLREARSSGTEMGKRVAEVMDRGELVTDEIVIGLIREKLGQGGKGFIFDGFPRTLAQADALQALMAEMDQRIDAVIEMRVDDAALVSRISGRFTCGNCGEVYHDVTKPTKEPGKCDVCGSTDLRRRADDNEESLKTRLMEYYKKTSPLIGYYYVKGNLNPVDGLAEIDEVAAQVAKVMDKIPA", "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": "MTRLVKALVIAYQRFFSARRPYRVCRFEPTCSEYMLQAIDRYHSRGILMGLARILRCQPFARGGYDPLPDHFTLKRNQPK", "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": "MTKGNYSYPLDPSWSTEEITTVLHFLSQVEKAYESKVDRDQLLEAYKAFKTVVPGKASEKQLDKAFQEASGFSTYQAVRAAKAKEKGFVTLGK", "text": "SIMILARITY: Belongs to the UPF0223 family."}
+{"protein": "MHGRLKVKTSEEQAEAKRLEREQKLKLYQSATQAVFQKREAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQKSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVAPAEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPENVLLRELELVQNAFFTDPNDQSAWFYHRWLLGRAEPHDVLCCLHVSREEACLSVCFSRPLIVGSKMGTLLLTVDEAPLSVEWRTPDGRNRPSHVWLCDLPAASLNDHLPQHTFRVIWTGSDTQKECVLLKGHQECWCRDSATDEQLFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLEYFSTLKAVDPMRAAYLDDLRSKFLVENSVLKMEYADVRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRALPPALAALRCLEVLQASDNVLENLDGVANLPRLRELLLCNNRLQQSAALQTLASCPRLVFLNLQGNSLCQEEGIRERLAEMLPSVSSILT", "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": "MFAGLPSLTHEQQQKAVERIQELMAQGMSSGQAIALMAEELRANHSGERIVARFEDEDE", "text": "SIMILARITY: Belongs to the UPF0181 family."}
+{"protein": "MRVGVIGAMEQEVKLLREQIENCEIVSRGGCEIYTGKINGVDVALLKSGIGKVAAAIGTTLLLEHFRPDVVINTGSAGGLDAKLNVGDIVVSTEVRYHDADVTAFGYEPGQMAQCPPAFIADPKLVNIAQECIGSLKLNAVRGLICSGDAFINGAEPLARIRRTFPEVVAVEMESTAIGHVCHQFDTPFVVVRAISDVADKESHLSFDEFLSVAAQQSSLMVTTMLDKLKTETQF", "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": "MSISLGNAFIKNFLGKAPDWYKIAILSFLVINPLVFFFVDPFTAGWLLVVEFIFTLAMALKCYPLQPGGLLAIEAIAIGMTSPEQVKHELVANIEVLLLLVFMVAGIYFMKQLLLFIFTKILIGIKSKTALSVAFCFTAAFLSAFLDALTVIAVVISVAVGFYAIYHRVASGQGGSQTHDHTCDSDVDELTREDLEDYRAFLRSLLMHAGVGTALGGVMTMVGEPQNLIIADQAGWMFGEFIIRMLPITAPVFICGILTCIAVEKLGICGYGAKLPENVRKILEDYEAEERKNRTNIDNAKLIIQGLIAVWLIVGLALHLAAVGLIGLSVIILATAFTGVIEEHSMGKAFEEALPFTALLAVFFAVVAVIIDQELFKPIIDAVLAVEDKGAQLALFYVANGLLSMVSDNVFVGTVYINEVKAALMDGVITRDQFDLLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIQLSYGRMVWMALPYTIVLALVGMFGIIFFLEPMTAMFYDLGWIAPGTIESATSAISSGH", "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": "MNGNEPHGGVLINRCDPACHFEGCACQAELDQLALSDLELIAIGGYSPLTGFLGEKDYHSVVKEMRLANGLPWSLPITLPVGEKTARQLSAGDHVKLVKDGVTYGMITVTDIYQPDKTQEALSVFKTNDPAHPGVKKLLARPDYYIGGPITVSSLPDKSFEQFYATPAETRAAFQKLGWKTIVGFQTRNPVHRAHEYIQKTALETVDGLLLHPLVGETKSDDIPSDIRMESYQALLNHYYPKDRVMLSVFPAAMRYAGPREAIFHALVRKNYGCTHFIVGRDHAGVGSYYGTYDAQNIFQSFTEEELGIKPLFFEHSFYCRKCGNMGTSKTCPHSPRDHIHLSGTKVRELLRQGKKPPKEFSRPEVAAVLIKGLHQQPVAIKQNSGELQ", "text": "SIMILARITY: Belongs to the sulfate adenylyltransferase family."}
+{"protein": "MRDLKTYLSVAPVASTLWFVALAGLLIEINRLFPDALTFPFFSF", "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": "MIWLTLVFASLLSVAGQLCQKQATCFAAVNKRRKHIVLWLGLALACLGLAMVLWLLVLQNVPVGIAYPMLSLNFVWVTLAAVKLWHEPVSLRHWCGLAFIIGGIVILGSTV", "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": "MVKKEKTPSPYTKPLDGGWGWMVVLHFFLVNVFVMGMTKTFAIFFVVFQEEFEGTSEQIGWIGSIMSSLRFSAGPLAAIICDVLGEKATSILGTFLVSGGYVISSWATGIPFLCVTMGLLPGLGSAFLYQVAAVVITKYFKKRLGLSTAIARSGMGLTFLLAPFTKFLIDLYDWTGALILFGAIILNLVPSSMLLRPIHSQSNNNSDIENKGSILSATEPEASYKTETSKCKETQEPFIKDSTMKKSEQPTTTLTVLGNQSEEFSNRPHRNRPLLMSNGKSHKKKFVSWNCKQKLLDISLFRNPFFYIFTWSFLLSQLAYFIPTFHLVARAKTLGIDVMDASYLVSVAGITETVSQLISGWIADQNWIKKYQYHKSYLILCGVTNLLAPLATTFPLLMAYTILFAIFAGGYLALILPVLVDLSKNSRVHKFLGYASFFAGIAVLSGPPIAGWIYDYTQTYTGSFYFSGTCYILSSVSLFFVPLAERWKRKQSDLLRTTIK", "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": "MTDLKKAAQRAIELMDLTTLNDDDTDQKVIDLCHKAVTPAGNTAAICIYPRFIPIARKTLDELGAEDIQIATVTNFPHGNDDIAIAVLETRAAVAYGADEVDVVFPYRALMEGNESVGYELVKACKEACGDVLLKVIIESGVLADPALIRRASELSIDAGADFIKTSTGKVPVNATIEAAEIMLTVISEKNTKVGFKPAGGVRDAAQAAEFLGVAERILGADWVSPRTFRFGASSLLNSLLHTLELADAPKPTQGY", "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": "MGSKAKKRVVLPTRPAPPTVEQILEDVRGAPAEDPVFTALAREDPLGPSGRTEDAEAQREQLYFQSRIYVAMNQRLQQAGAQLEQKRADLQQAGEELERDISQVGHVALPSTAAASLG", "text": "SIMILARITY: Belongs to the UPF0449 family."}
+{"protein": "MISIKGTGRFLLDNYRIWQRRAFNRPIQLRKGYKVLAIETSCDDTCVSVLDRFSKSAAPNVLANLKDTLDSIDEGGIIPTKAHIHHQARIGPLTERALIESNAREGIDLICVTRGPGMPGSLSGGLDFAKGLAVAWNKPLIGVHHMLGHLLIPRMGTNGKVPQFPFVSLLVSGGHTTFVLSRAIDDHEILCDTIDIAVGDSLDKCGRELGFKGTMIAREMEKFINQDINDQDFALKLEMPSPLKNSASKRNMLSFSFSAFITALRTNLTKLGKTEIQELPEREIRSIAYQVQESVFDHIINKLKHVLKSQPEKFKNVREFVCSGGVSSNQRLRTKLETELGTLNSTSFFNFYYPPMDLCSDNSIMIGWAGIEIWESLRLVSDLDICPIRQWPLNDLLSVDGWRTDQL", "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": "MLITKTAFLAFLLSSVPLAHGAGGNSSSPDARGRRCVVRSSNGTADDSPEVSRVFAQCATNSVIVFQEGVDYNIFQPIKATNLSNVEIQMHGNLHLPQNISAVRDIVNAGTSTWFTLEGPRVDWTGPEDVNNGWIKSYGQAWWDANPPNGTGISGRPHLMSYKTSQATIKYFRSGKPIAWNMKLHGEDIAVSHAIVDASSTGSFPFNTDAFDVQGTNIRISDSIMYNGDDAIAVGSDSHNIVFERNTIGYQSHGMSIGSLGKDASAFANITNLRFEDVTVIDALYAARFKSWTGGQGLVKNVTWKNIRVYNVTFPIFVTQSYYDQSVSRDGVDTESSVMMEDFTWEDFSGSINSYQPGDGSCATDPCWYNAGLPNLKHTEALVIECNTDKSCKNFVTKNIQLYPQVLEPASVICMKATAELNPNLGFNCSNGTFTSA", "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": "MEEQREALRKIITTLAMKNEEIQSFIYSLKQMLLNVEANSTKVQEDLEAEFQSLFSVLEELKEGMLMKIKQDRASRTYELQNQLAACTRALESSEELLETANQTLQAMDREDFPQAAKQIKDGVTMAPAFRLSLKAKVSDNMSHLMVDFAQERQMLQALKFLPVPSAPVIDLAESLVADNCVTLVWRMPDEDSKIDHYVLEYRRTNFEGPPRLKEDQPWMVIEGIRQTEYTLTGLKFDMKYMNFRVKACNKAVAGEFSEPVTLETPAFMFRLDASTSHQNLRVDDLSVEWDAMGGKVQDIKAREKDGKGRTASPINSPARGTPSPKRMPSGRGGRDRFTAESYTVLGDTLIDGGEHYWEVRYEPDSKAFGVGVAYRSLGRFEQLGKTAASWCLHVNNWLQVSFTAKHANKVKVLDAPVPDCLGVHCDFHQGLLSFYNARTKQVLHTFKTRFTQPLLPAFTVWCGSFQVTTGLQVPSSVRCLQKRGSATSSSNTSLT", "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": "MAQRTRLGDILKPLNSEYGKVAPGWGTTPVMAVFMALFFVFLLIILQLYNRSLLVQDVLVDWRSLGR", "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": "MVQLKTAALALLFAGQALSGPVDSRQASVSIDAKFKAHGKKYLGTIGDQYTLTKNTKNPAIIKADFGQLTPENSMKWDATEPNRGQFTFSGSDYLVNFAQSNGKLIRGHTLVWHSQLPGWVSSITDKNTLISVLKNHITTVMTRYKGKIYAWDVLNEIFNEDGSLRNSVFYNVIGEDYVRIAFETARSVDPNAKLYINDYNLDSAGYSKVNGMVSHVKKWLAAGIPIDGIGSQTHLGAGAGSAVAGALNALASAGTKEIAITELDIAGASSTDYVNVVNACLNQAKCVGITVWGVADPDSWRSSSSPLLFDGNYNPKAAYNAIANAL", "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": "MKLKLYNVRGEEAVLAKKWADDNGIEISLTESPLTPETVKEAEGFDGIANAQIGPLDDAIYPLLKEMGIKQIAQHSASVDMYNLDLATENDIIITNVPSYSPESIAEFTVTIVLNLIRHVELIRENVKKQNFTWGLPIRGRVLGDMTVAIIGTGRIGLATAKIFKGFGCKVVGYDIYQSDAAKAVLDYKESVEEAIKDADLVSLHMPPTAENTHLFNSDLFKSFKKGAILMNMARGAVIETQDLLDALDAGLLSGAGIDTYEFEGPYIPKNFEGQEITDSLFKALINHPKVIYTPHAAYYTDEAVKNLVEGALNATVEIIKTGTTTTRVN", "text": "SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family."}
+{"protein": "MSVIGIVAEYNPFHSGHEFLLNQARLVSENDPIIVMMSGNYVQRGQMAIMDKWQRAKAALNSGADLVFELPFSFAVQPADIFANGSIRMLSNLGVSELFFGVEDANLNFSYLGQKINQIPKNRMDFRDYTQTYATQYNEMVAREVGHEVNQPNMMLAVAYAVASEQLDTPLHLHPVTRLGSGHDDQLLQDKIISSATAIRNYCLHHPNDLIELKKYLPKGELAALEKQKVYPNWNLLFNFLKYRIESASLEELRSIYQMSEGLEYKMKEEIHNAEDFTSFLRQIKSKRYTYARLRRLCLYTLLNVTEKEMQASYQDVSTLLLGYNSRGRNYLKKIRKDVELPIISKVDKKNAASGTLGLQVRVDRLFEQIMGEDQNFGRRPIEVK", "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": "MLTLDTLNVMLAVSEEGMVEEMILALLASPQLVIFFEKFPRLKNAVTADLPRWREALRSRLKDARVPQKLTEEVMCYQQSQLLSTPQFIVQLPQILALLHRLHSPYAAQAKQLVESNSTFTPSLHTLFLQRWRLSLVVQATTLNQQLLEEEREQLLSDVQERMTLSGQLEPTLAENDNAAGRLWDMSAGQLKRGDYQLIVKYGEFLAAQPELKQLAEQLGRSREAKSVPKKDAPMETFRTLVREPATVPEQVDGIQQSDDILRLLPPELATLGITELEYEFYRRLVEKQLLTYRLHGEAWREKVTERPVVHQDVDKQPRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSTEVVRYELSGPEGIEQAIRFLSQRFRGGTDIASCFRAIIERMQRRKWFDADAVVISDFIAQRLPDDVVSKVGELQRLHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTGMRSRLLRRWRR", "text": "SIMILARITY: Belongs to the ViaA family."}
+{"protein": "MDIKAYFELIRLKNCLTASFGAFIGGLIASYFNISMIDNLILASIVVFLVCGFGNALNDIYDLKIDKINKPKRPIPSKRISLGEARIFSYLLVVMGLIISMFNITCFLMAVLNSIVLQQYASTYKKNKIVGNLIVAYLTGSVFIFGGIAVGNIDVTIMLFLCALFAMWSREIIKDYEDIEGDIKEKVISIPIKCGEKSIYIAAFLLVFAVLLSPLPYLFGFFGIYYLISVIFCDLLFLIGIYNLVMNPSKKEAKKASRNIKIVTNLVLIAFLIGSLFK", "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": "MSQQRILPQSKETLLQSYNKRLKDDIKSIMDNFTEIIKTAKIEEEHQVSRSTQGEQDNYEMHVRSANIVRAGESLMKLVSDLKQFLILNDFPSVNESINQRNQQLRTLREECDKKLIALRDDIAIDLYELEEEYYSSSYSVCDPSDLPLCEVYWNRESTASSPEDLSVPLAPIMAEASTVTSQIHTPPHLNGHGAGMTEHT", "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": "MKKEQFYPLGIFLAAMLGGLVRYLVSTWLPASPDFPWGTLFVNYLGIFCLIYLVKGYLVYKGTSKGLILALGTGFCGGLTTFSSLMLDTVKLLDTGRYLSLILYLLLSIGGGLLLAYYLGRKKW", "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": "MSTEAALLKLQSWFSPSFPVGGYTYSHGLEYGVECGLIHHRESLQTWLEGLLQWGAGHGEGVLFHGAYGAAVRQDWAALHEVTVWAQALRPTAELALESRGQGRAFLVAVQQGWPHPWVQRWGDGLAEHAPYGVVTGLACAAHGVPEAMGLSALLHGMVAGWISAAVRLIPLGQQAGVLVQSALEGEIQTLVRALLSQPASAFQAELGGCAWMAEWCSLKHETQYTRLFRS", "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": "MGKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFSSVQYIMTEVNFGWLVRSVHRWSASMMVLMMILHVFRVYLTGGFKNPRELTWITGVILAVLTVSFGVTGYSLPWDQIGYWAVKIVTGVPEAIPVIGSPLVELLRGSVSVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL", "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": "MAKILLVYATMSGNTEAMADLIEKGLQEALAEVDRFEAMDIDDAQLFTDYDHVIMGTYTWGDGDLPDEFLDLVEDMEEIDFSGKTCAVFGSGDTAYEFFCGAVDTLEAKIKERGGDIVLPSVKIENNPEGEEEEELINFGRQFAKKSGCAV", "text": "FUNCTION: Low-potential electron donor to a number of redox enzymes. SIMILARITY: Belongs to the flavodoxin family."}
+{"protein": "MKQYKILFFIADGLGDRPVRKLQGKTPLEYVDKPNIRELLKNSIIGLMDPISPGVVAGSDTSHLSMFGLDPHKYYRGRGAFEAIGAGARLKASDVAFRGNFATVNNEFIVVDRRAGRKIEEADDLVKELNEKIGEIDGVKVRFYHGTEHRVAVVLSGKGLTDKVSDTDPHEVNKKVLESKPLDNSPESQFTANIINKLTRKIYEILNSSEINKIRVSKGELPANIILLRGAAEFVELPQFESYTKLKAAAVSATALIKGICEQIGMRVVTPPGATGGLDTNYLGKADAAVELLKEYDFVFLHLKATDAASHDGNVDGKVYAINKMDEMIGRILDKLGSELVIAISGDHTTPVEVKEHTGDPVPFLLYVPYDIINDVVNDFNEREARRGSLRIRGLDVINLLLNYSNRAEKYGA", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily."}
+{"protein": "MRYAVLVTGPAGAGKSTFCASLITHAQTIGRSVHLVNLDPAADKFEYEPTIDIRDLINLEDVMEELEFGPNGGLIYCFEYLLNNLDWLEDELGAYEDDYLIIDCPGQIELYTHVPLLPRLATFLSTSLNFRTSAVYLIDSQFMQDKSKFFAGVMSAMSCMLSLGISMLCLMSKMDLVKDKKGRTKREVGRYLDPDPNLLLEDINQGTNSKFNQLNRAVVSLIEDQNIVSFLPLDVTSEDSVNTVLSHIDNMMQYGEDEEPKVPKDMDDGEFVAPPRSYNIKLIVRDR", "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": "MHAIAENHGVKASYTKEELQACGQGRLFGEGAAKLPVDQMLMVDRVSQISAEGGAYGHGIVRAQLDINPDLWFFKCHFVGDPVMPGCLGLDAMWQLVGFFLAWKGHKGLGRALGVGEVKFTGQVLPSAKSVEYVLDIKRVIARKLIMALADGTVYVDGKAIYTAKDLRVGLFDPAAMSGAEIK", "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": "MTAARAGALGSVLCVLTGASRGFGRTLAHELCPRVLPGSTLLLVSRTEEALKGLAEELGHEFPGVRVRWAAADLSTTEGVSATVRAARELQAGTAHRLLIINNAGSIGDVSKMFVDFSAPEEVTEYMKFNVSSPLCLTASLLKTFPRRPDLQRLVVNVSSLAALQPYKSWVLYCSGKAARDMMFRVLAEEEDDVRVLSYAPGPLDTDMHEVACTQTADPELRRAIMDRKEKGNMVDIRVSANKMLDLLEADAYKSGDHIDFYD", "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": "MPEKSLYEMAVEQFNRAASLMDLESDLAEVLRRPKRVLIVEFPVRMDDGHVEVFTGYRVQHNVARGPAKGGIRYHPDVTLDEVKALAFWMTWKTAVMNLPFGGGKGGVRVDPKKLSRNELERLSRRFFSEIQVIIGPYNDIPAPDVNTNADVMAWYMDTYSMNVGHTVLGIVTGKPVELGGSKGREEATGRGVKVCAGLAMDVLGIDPKKATVAVQGFGNVGQFAALLISQELGSKVVAVSDSRGGIYNPEGFDVEELIRYKKEHGTVVTYPKGERITNEELLELDVDILVPAALEGAIHAGNAERIKAKAVVEGANGPTTPEADEILSRRGILVVPDILANAGGVTVSYFEWVQDLQSFFWDLDQVRNALEKMMKGAFNDVMKVKEKYNVDMRTAAYILAIDRVAYATKKRGIYP", "text": "SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
+{"protein": "AREGYLVSKSTGCKYECFWLGKNEGCDKECKAPNQGGGYGYCHAFACWCENLPESTPTYPIPGKSCGKK", "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": "MGIDLVKAGRVKKPGRKALVSKNPYLRLLVKLFKFLARRTDFPFNKIVLKRLLMPRRYKAPLSLSKLSKHMESRPNNTAVVIGTVTSDERMDVVPKLSVCALRVTETARKRILASGGEVLTFDQLVARSPIGGKCTLLRGETKAREAVKHFRNEVKGNPKPYVRSKGRKFEKARGRRHSRAFKA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family."}
+{"protein": "MLKILLPTVMLLPLISFSKKEWMWINSSAYSILISSLSLLTLNQHMDLGLNFNLNFFTDPLSSPLLVLSCWLLPLMILASQFHLMNESTTHKRMYLILLVSLQVALLMAFSAVEFMMYYILFETTLIPTLIIIARWGNQTERLNAGLYFLFYTLLGSLPLLVALIFTQAQMGSLHILLLTLTPNPLLNSWSNDILWLACMMAFLVKMPLYGFHLWLPKAHVEAPIAGSMVLAAILLKLGGYGILRIIIILEPISKLMAYPFIILATWGMIMTSSICLRQTDLKSLIAYSSVSHMGLVVAASLIQTPWGFMGATAMMIAHGLTSTMLFRLANTNYERAHSRTMVLIRGLQMVLPLMSSWWLLASLANLGLPPTINLISELMIIVSAFSWSNLTLILLGLNTVITAIYSLYMLTSVQRGKMTTHSLSINPTFTREHMIMALHLLPLILLTLNPKLILGVAY", "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": "MVNIPKTRRTYCKGKACRKHTPHKVTQYKKGKDSLSAQGKRRYDRKQSGYGGQTKPVFHKKAKTTKKVVLRLECTVCKTKHQLALKRCKHFELGGDKKQRGAAISF", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family."}
+{"protein": "MPSDMLQFPSENDRQTFERLVSELPDLIHKRCHDYDELYGHKLLEEGPAEVAKFYSKDHAHALLFKFLKANAFSYEGAVKQLVSTLNWRREFQPLKAAFAEEHDERLMAAGYISYDASAAPNTRTVTWNLYGKLGACKDLFADQDTFIRYRVGLMERGLQALNLLDPDNCSMTQVHDYKDVSVWNMNADVKKCSRRVIAIFQDHYPELLYAKYFVNVPTILRWVYDVVRAFVSEETSRKFVVLNDGTKLAAYFAGVPAAYGGTAPATLAELPKPASRPSPYALFLLQKHISEELD", "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": "MSSPDQDPREAIAQGDDEVIDVRRGMFGAAGTGDTSGYGRLVRTVTLPGSSPRPYGSYFDDVVDTLTESLQSNGIEFHQAIEKVVVYRDELTLHVDRAALPHVAQHLRDDPRLRFEMCLGVSGVHYPHETGRELHAVYPLQSITHNRRVRLEVAVPDEDPHIPSLYRIYPTTDWHERETYDFFGIVFDGHPSLTRIEMPDDWHGHPQRKDYPLGGIPVEYKGAQIPPPDERRAYN", "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": "MLLSLHQLSVKFGKHLILDRINISIGRGEIVTIVGPNGSGKSTLLKTLIGAIKPVSGCIERAEKLKVGYVPQRLHIDEALPMTVFRFLTLPVQRSKKTISQALVRAGIPGVEKQQLNSLSGGQLQRVLLARALLEEPMLLLLDEATQGLDQRGTVDFYQHIDSFRKETGCAIIMVSHDLHVVMKNTDRVICLNGQICCEGTPEKVSNSPEYKVLFGLDDNDVLGVYRHKAASNQFNGSVLNVG", "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": "MVKLRLKRCGKKQRAVYRIVAIDVRSRREGRDLRKVGFYDPIKNQTYLNIPVILNFLEQGAQPTGTVQDISKKAGFFMDL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
+{"protein": "MKVWWAVLAAAILAGCRAQTEQEVEVPEQARWKAGQPWELALGRFWDYLRWVQSLSDQVQEELLSSQVTQELTMLMEETMKEVKAYKSELEEQLSPMAQEHRARLSKELQVAGALEADMEDVCNRLAQYRGEAQAMLGQSTEELARAFSSHLRKLRKRLLRDAEDLQKRMAVYGAGAREGAERGVSAVRERLGSRLERGRLRVATVGTLAGRPLRERAQAWGERLRGHLEEVGSRARDRLNEVREQVEEVRVKVEEQAPQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKLQAAMPSKAPAAAPIENQ", "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": "MAEEEVDYVFKVVLNGDSAVGKSQLRARFTRDEFSMDSKATIRCRFQYSNAPYYKGAVGAMLVYDMTIRESFEHIPQWLEELRVHADKNIVIILIGNKTDLENQRSVPVEDAKEFAEKEGLFFLETSALNSTNVENSFNTLLTEIFNKVNKKNLAKTTVSCSSQVSLLRPPCVAAQ", "text": "SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MKLPIYLDYAATTPVDPRVAEKMFQYMTMDGIFGNPASRSHRYGWQAEEAVDIARNQVADLINADHREIVFTSGATESNNLAIKGVAHFYNKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLEPASNGIIPMERLEAAMRDDTILVSIMHVNNEIGVIHDIDAIGELCRSKGIIFHMDAAQSAGKLPIDVQATKVDLISISGHKMYGPKGIGALYVRRKPRIRLEAQMHGGGHERGMRSGTLPTHQIVGLGEAAAIAKAEMATDNERIGRLRDKLWNGIKHIEETYINGDLTQRFCGSLNVSFNYVEGESLMMALKDLAVSSGSACTSASLEPSYVLRALGLNDEMAHSSIRFSIGRFTTEEEIDHAIETITQSIDKLREMSPLWEMFKDGIDLNQVQWAHH", "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": "MKMERKNVWQHRNREEIESFSKEYMDFMGRAKTERLAVREIRKFLEKEGFVPIEDFAGDPMDMAVYAVNRGKAIAAFRVVDDLKKGLNLVVAHIDSPRLDFKPNPLVEDEQIALFKTHYYGGIKKYHWFNIPLEIHGVLFRGDGEEIEIHVGDKPEDPVFTIPDLLPHLDKEDAKISEKFKGENLMLIAGTIPLSGEEKEAVKMNVLKILNEMYGISEEDFVSGEIEVVPAFPPREVGIDRSLIGAYGQDDRICAYTALRAFLEANPKKSIGVVFLDKEEIGSDGNTGAKARFYLRVLRQILKIQGGPEIQNSHSMRYWKKSAVISGDVCAAVNPPYKDVHDLHNAPRSGYGVALVKYTGARGKYSTNDAHAEFVARVRQVLNERNVIWQVATLGKVDQGGGGTYAKFFAERGADVYDMGPALLGMHSPFEISSKADLFETYRAYRALLEDL", "text": "SIMILARITY: Belongs to the peptidase M18 family."}
+{"protein": "MDLSNRTVVQVVVLALVAQVTLSQHWSYGWLPGGKRSVGELEATIKMMDTGGVVALPEETSAHFSERLRPYDVILKKWMPHK", "text": "FUNCTION: Stimulates the secretion of gonadotropins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the GnRH family."}
+{"protein": "MKALSKLKAEPGIWMTDAPKPEVGHNDLLIKIRKTAICGTDVHIYKWDEWAQKTIPTPMVVGHEYVGEVVDMGQEVRGFKVGDRVSGEGHITCGHCRNCRAGRVHLCRNTTGVGVNREGAFAEYLVIPAFNAFKIPDNISDELASIFDPFGNAVHTALSFDLVGEDVLITGAGPIGIMAAAVAKHVGARHVVISDVNEYRLELARKMGATRAVNVANEKLEDVIKELGMTEGFDIGLEMSGVPSAFNSMLNNMNHGGKVAMLGIPPSDMAVDWNQVIFKGLVIKGIYGREMFETWYKMASLIQSGLDLNPIITHQYSIDDFQAGFDMMISGQSGKVILNWD", "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": "MKKHLHEIKMLLKITIPIFLAQISQTSMSLINSIMIGHLKENNIAAISVGISIWSPIILFGHGLLLSLVPTVSRIHGSGKINKIPEQINNAYWLATLISLVIMIVLWNSDVIIHTISQVNPIIEQESIKYIRILLWSTPGYLYFQVIQNQCEGLLKPKPAMVIGLIGLLFNIVVSYTLISEKFHCFNYGSTGCGISAIIVYWFMFIAMKKITKNDILINYNIKNKNISNLEMYLPNYKIIWNLFKMGFPIALSLFCEITLFTLITLLIASMETFQIIAHQIALNISSTIFILPLSIATAASIRLGFYLGKKSFSKISTIILSSQIIGLIISTTISTFIILFHYQIITLYTKNANIIKLTKQMLFITASYQIFDFFQIIGNGILRSYKDTNIIFIITCTSYWIVGFPFGYFLALTNYIVPHMGAIGFWYGILIALITSSIMILFRIYILQKK", "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": "MFLLPRFVLVSCIIGSLGFDNPPTNVVSHLNGDWFLFGDSRSDCNHVVTTNPRNYSYMDLNPALCGSGKISSKAGNSIFRSFHFTDFYNYTGEGQQIIFYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIAREANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGNYLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSILSGLLYDSPCFSQQGVFRYDNVSSVWPLYPYGRCPTAADINTPDVPICVYDPLPIILLGILLGVAVIIIVVLLLYFMVDNGTRLHDA", "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": "MPKVAVGGTFQYLHDGHARLIEKAFEIAGDGKVYIGLTSDEMLQKNHSIDNYENRRVRLLEYIDEMEIPKEKYEITRLNDPCGPTVEEDFDYIVVSPETYPVALKINRIREKKGKNPLEIVYVEYVMAEDGTPISSTRIAKGEIDRHGKMKRESQA", "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": "MADWTEKYRPSTLSEVRGNDKARDAFADWARSWDDHHEAVVLHGSPGVGKTSAAHALANDMGWETVELNASDQRTADVIERFAGRAARNATLGGSAAGGGAAGGDTASRQLVILDEADNIHGNYDRGGASAITELVKESGQPIVLIANDYYDMARGLRNATQEIEFRDVSARSIVPVLRDICRKEGIEFESDALERIAERNRGDLRGAINDLQAATEGRDSIAVEDVVTGDRDKALGLFPYLDAVLKEESAEEALQSAYAVDETPDDLTKWIENNVLDVYDPSEVVRAYDFLANADVWLGRVRATQNYSYWRYATDNAAAGVAAARDGTKGGWTRYGRPQFWSPSDATADEVVGQIAAKSGCSVATARREVLPFLEAVTHHCKPRELTVAMAAAYDLDEAGIAFVTGSGESTNKVASIAEDAQALREERMEDHAEGAFAGGRHAADDLGASDGETTNASGTASSSGDDGDADGTTDGDGSDANDGNDDDDDGQAGLSDFV", "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": "MSTMLIAVILLTLLALFFGVLLGFAALKFKVEGNPIVDELEAILPQTQCGQCGYPGCRPYAEAIANGDKVNKCPPGGTATMEKLASLMGVEPEPLNAEAQSQVKKVAYIREDECIGCTKCIQACPVDAIIGAGKLMHTVLTADCTGCDLCVEPCPVDCIDMLPVGQNLKNWNWRLNAIPVTLIQETPHEEKRG", "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": "MGRRPARCYRQIKNKPYPKSRYCRGVPDPKIRIFDVGAKKRLVDEFPFCVHLVSWEKENVSSEALEAGRIACNKYMVKFAGKDGFHLRVRVHPFHVLRSNKMLSCAGADRLQTGMRGAFGKPQGTCARVAIGQVLLSVRSRDNHSNHAQEALRRAKFKFPGREKIIVNRKWGFTKYTRADYLKWKTENRIVPDGVNPKLLGCRGPLSNRKPGQAFLKPAVVLSSDLVA", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL16 family."}
+{"protein": "MGFWKLSPFLAIGLLVMYQAGILQAAPFRSALENPLESATLTEDEICVLLTAVVKDYVQMKARELQQEQETEGSSLTAQKSSCKDGPCVTNRLEGWLARAERMVKNTFMPTDVDPEAFGHQHKELAA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calcitonin family."}
+{"protein": "DHKNSPEKFYDNIEHHYEFIGDKLIIGKFCAIAEGVKFIMNGANHRMDGITTYPFNIFGCGWEKVTPTIEQLPFKGDTVIGNDVWIGQNVTIMPGVIIGDGAIIAANSTVVKSVEPYSIYSGNPAKFIKKRFSDEKIEFLLKLEWWNWSGEEIFDNLEILTSEAGLEELMNKYSKRDAIN", "text": "SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
+{"protein": "MMGMNPRQMKKLMKQLGIKMEELEGVEEVVLRMKGKEIILKEPAVTVMVVQGEKTYQIIPGSEEVREVLEISEDDIKLVMEQAGVDYDTAKKALEEAKGDLAEAILKLTEG", "text": "FUNCTION: Contacts the emerging nascent chain on the ribosome. SIMILARITY: Belongs to the NAC-alpha family."}
+{"protein": "MDIIGGQHLRQMWDDLADVYGHKTALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLTDVALPADDGVSSFTQLKNQQPATLCYAPPLLTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATITECIPMMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK", "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": "MQSMPWLFRQSLRTGLNLSRTSLPGRSPISPAPISKVHSKTARRNFSVCLRCHFRYQPSLRSDEIKRSTDEKQDKKIEEPVIALGAPESTQAEPNAGAQDTSQTADTVHTQGQEGKKEDEPGSTQNGGLPSYIEDRRSQFSKQFTTWMDNLQSNVFVAGQRLNDLTGYSSIEALKRNIQEQEKRLRAARHRVRTAKEAYAAAINRRSTSQREVNELLQRKHAWSPADLERFTHLYRNDHTNEVAENETQEALSAAERESEEAAASLTKSILSRYHEEQVWSDKIRRMSTWGTWGLMGVNVLLFLIFQIAVEPWRRKRLVKGFEEKVLEAIEKEKILVHSQPVPPVEFTATQDAHSPTSGLVTPSPGDNIASEESSEATVAANTPTTTAEDEASGSMAPENITSSSLESYKPPSLQSLLSSMSIECCRQYIHYLLSESPVTVTQRDISVVAATSAAAGATLMGLVVALIRSQ", "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": "MTDKNNKRLFKVAPLATAIAASLFTVNASAVEWHGYARSGIGMSDNGDQQCINKQAVGRLGNECETYAELDLQQELFNRDGKTFKVETMLSYKSNQDGDYEALNSEDDEIALRQMNVQAKGVLGFAPEATLWAGKRYYQRHDIHHLDLFYWDVSGPGAGIEGIDAGAGKFSAAWTRGYGNINILDFRYSGIQVGASSLEVGLDLAKPRLTDAQKDAGAADDLSTLFTAELSTPIMDGFNKIVFQYGTEGYASPMRNFGGGQWNGTLDKGGKGFRLIDWGVVKPSANIELSYAAMYGVFEDDDMNDDSSFYSISARPAYKWSDYMRTYLEVGYFAADDDGVDSQLDKITIAQAWSAGPSFWARPEIRVFASYINDGEGTPFEGGEDSVLNFGVQMEAWW", "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": "MGLPWYRVHTVVLNDPGRLIAVHLMHTALVSGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGVTQSWGGWSITGETVTNAGLWSYEGVAAVHIVLSGLLFLAAIWHWVYWDLELFRDERTGKPSLDLPKIFGIHLFLSGVLCFGFGAFHVTGLFGPGVWVSDPYGLTGRVQPVAPAWGAEGFDPFNPGGIASHHIAAGILGILAGLFHLSVRPPQRLYKGLRMGNVETVLSSSIAAVFFAAFVVAGTMWYGCAATPVELFGPTRYQWDQGYFQQEIDRRIRNSVAENVSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGAMDNGDGIAVGWLGHAVFKDKEGNELFVRRMPTFFETFPVVLVDEEGIVRADVPFRRAESKYSIEQVGVSVEFYGGELNGVSFSDPATVKKYARRAQLGEIFEFDRATLKSDGVFRSSPRGWFTFGHACFALLFFFGHLWHGSRTLFRDVFAGIDPDLDSQVEFGLFQKLGDPTTRKQTV", "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": "MARCSNNLVGILNFLVFLLSIPILAGGIWLSQKGSTECERFLDKPVIALGVFLMVVAIAGLIGSCCRVTWLLWVYLFVMFLLILLVFCITVFAFVVTNKGAGEAIEGKGYKEYKLGDYSTWLQKRVENGKNWNKIRSCLVESKVCSKLEAKFVNVPVNSFYKEHLTALQSGCCKPSDECGFEYVNPTTWTKNTTGTHTNPDCQTWDNAKEKLCFDCQSCKAGLLDNVKSAWKKVAIVNIVFLVFLIIVYSVGCCAFRNNKRDDSYSRTYGYKP", "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": "MDRTLIQEILEIVEQAAIASATLSGKGLKDEADALAVDAMRKRMNQIQMKGRIVIGEGERDEAPMLYIGEEVGTGTGPGVDFAVDPCEGTNLCAYSQRGSMAVLAASDRGGLFNAPDFYMKKLAAPPAAKGKVDIRKSATENIKILSECLGLAPDELTIVVMDRARHKDLITEIRATGARIQPISDGDVQAAIACGFAGTGTHCLMGIGAAPEGVISAAAMRALGGHFQGQLVYDPAIAQTSEWADMTKEGNLARLAEMGITDPDKVYEASELACGEHVVFAGSGITDGLLFNGVKFETDCTRTSSLIISNLNNTCSFTNTIHMKDGAQSIALN", "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": "MKFVLLFGVLLVTLFSYSSAEMLDDFDQADEDELLSLIEKEEARKDCIPKHHECTNNKHGCCRGHLFKYKCQCTTVVTQSGEETERCFCGTPPRHKAAELVVGFGKKIFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 03 subfamily."}
+{"protein": "MSAAARTFISIHIGVCFDEMDSPGSSAPSPPDLTIIPKISSKKCQICENPAHGKHFGAVTCRACAAFFRRFGISNNFKPCKTENKCSFRKNGYFSCKKCRMQRCLQFGMTIDNFQFDREPFNPLKMNVGIPQTVDTFSGRPSLILFSAPSGSSGPKRYIDVQFLVDRAVEVLLNGSETPYQVSNVLQKLAIGLQNIRGPQQKVSQIVTKIGKEGIFKLWEEEMLRMAKWLTYFDDFQRLPHSVQIEILNGVWFLFGRLENIASTALARKRKLCKDDMVMTCVNKNVLICDLRTLEIDLSWCSKYTFQQLKFFDQYDDLRQLDILINAMLDLEPTHEELSYMICQLCFHQVGKKLQGNILKTVEKLQEVLSNNLHDYYVNQMNQPKYSKRIARMMKINNTVEQCLYRDRVKADLMKVFEVFHVECSHPGIFLNA", "text": "FUNCTION: Orphan nuclear receptor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family."}
+{"protein": "MTEPTNTLPNLGAAELAAYIDHTLLRPDAGAAEIAAWCDEAVTHGFKSVCVNPIQIPLVAAKLAGTGVGVCSVIGFPFGASPTAVKVAEAAWVVAHGATEVDMVIDIGALKDGRAEAVRDDIAAVKAACGKALLKVIIEACLLDDEQKALACRLSAEAGADFVKTSTGFAGGGATAKDVALMRRTVGSALGVKASGGVRTRDDALRMIAAGASRIGASASIAIVAEADAASTGAKGGY", "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": "MPSPPEPPLHWRDCRLEPILGFPRPRELAKSLEVQGEEWIALLESGGGLQHRSRYSFLAWGRRKSSETDAIRAYEELERLADDKCRALPCRSPTFFLVSYEAVVGEEPWLSRLVGRHEWPGMTAFSPEYVVVYDHAGGRVSVCPGDTPLPAPASRKESFSAEGPTYETSRKGFEAMVADALERIRAGEAFQVVLSRVERYRVWGSLFSAYERLADANPSPYLYYARLGGRVIIGSSPELLVKLEAGRVETHPIAGTRPRGSTPIEDIELEVELLNDEKERAEHVMLVDLARNDITRVSIPGTVQVTSFMDIERYETVMHIVSRVEGVTRPSTTFVEALKALHPAGTVSGAPKPRAMEIIAELEEEARGPYAGAIGVAGSSAGEAAIVLRSAWLLDDGETLEARAGAGIVYDSKPEREYMETVQKLGSLKRALGVDMCG", "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": "MVTINNAHSELIHDAVLDYYGKRLATCSSDHTVKIFEVEGETHKLVDTLQGHEGPVWQVDWAHPKFGVILASCSYDGKVLIWKEVNGRWSQIAAHEVHSASVNSIQWAPHEYGPLLLAASSDGKVSVVEFKENGTTSPIIIDAHSIGANTACWAPATLQQQSNQGTSGSASPQQVRRFVTGGADNLVKIWKYNSDAATYLLEHTLEGHSDWVRDVAWSPTVLSRSYLASVSQDRTCIIWTQDSKEDTWKKTLLKEDKFPDVLWRASWSLSGNILALSCGDNTVTLWKENLEGKWEPAGQVTE", "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": "MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEANDQGKPPLDIHVLPRDKHWQKLLHSLIAELKPEMNGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE", "text": "FUNCTION: Necessary for formate dehydrogenase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FdhE family."}
+{"protein": "MQSILTQETIIIALIYLSLSVLYLLVIPAVIYYYLNTRWYVASSWERGFMYFLMSFFFPGMLLLSPFLNFRPQRRTLKA", "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": "MIKEYYGAETFILNKDFAYILVIGTTDVSLIPGLTIAGATPELTHFTPAADAEYVLLGKCKSINTIPVSPTGIPTPALLTRASLSFINPLKIVVNAGSRILPKIPYIDLQGEPGKDIRKQALSMEKVNNIIENSIKLGEELSNEYELIMIGESIPAGTTTAMATLLALGYDAMDKVSSASPDNPKELKRKVVEEALRNLPTDSLQRLAKVSDPVLLGVAGTSLGFKGKILLAGGTQMTAAAAIINEFDKNKLKDITIGTTKWIVEDKFADMLSLAKQVGVKVLASMLDLSISAYEGIRAYEKGYVKEGVGAGGSAIMALVRGVSNNTLVRKIDELYGELVGSNNLHI", "text": "SIMILARITY: Belongs to the UPF0284 family."}
+{"protein": "MAVTAAQVKELREKTGAGIMDAKRALVETDGNMEAAAELLREKGIAKAAKKADRVAAEGLTGIAVNGNVAAIVELNSETDFVAKNDQFVALVKETAELIASKKPATNEEALALETASGITLEAELVQATATIGEKITFRRFAVIEKTDAQHFGAYQHNGGKIGVVSVVEGADETLAKQVSMHIAAMNPTVLSADELDSEFVKAELAQMNHKIDEDNASRVLVNKPELPHHEFGSKSQLTEEVLAAAKASFEEELKAEGKPEKIWDKILPGKMAKFIVDNTKVDQQFALLAQLYIMDDSKTVEAFLESKGAKAIAFTRFEVGEGIEKAETDFAAEVEAAKAGL", "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": "MHPDLSPHLHTDECNQLITLLKQCHKEHNVLKFFGTCNDMDRAMRECLRKEYQTKRERSKAHAEEMRRRLKEQPKEHP", "text": "FUNCTION: May be involved in cytochrome c oxidase biogenesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the CMC family."}
+{"protein": "MEANFSIPQNGSEVVFYDSTTSRVICIFLVVVLSITFLLGVIGNGLVIYVAGFRMTHTVTTICYLNLALSDFSYMASLPFQITSIVMNGEWLFGWFLCKFVHMIINVNLFLSIFLITFIAMDRCICVLHPVWAQNHRTVNVATKVIFGAWILVLMLIFPHCIFVTTVKDESGKVHCICNFESWAATPEEQVKVSMTVSLISVTISFIIGFSIPMIFIVICYGLMAAKIGRRGFVNSSRPLRVLTAVAISFFVCWFPFQLIFLLGNIGNKETQNNIDTWVNTASTLASFNSCLNPILYVFLGQQFRERLIYSLSASLERALREDSALNSDKTRNLSSQRL", "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": "MEEFRRAYAKLCAAPQEAVLRRLRERGEAPGRARLDLAEQSLSLETCGALGRLLPGAAHFAEVALGDCGLSEDGVKLLLHGLCSNSTVKSLDLKGNNLRTTGAEALGKLLRQNKSIRSLILEWNSLGVWEEGFSFFCQGLGANNFLQRLDLRNNQINHHGAGELAMALKRNASLQELDLRWNNIGLLGGRALLNCLQSNKTLKKLELAGNNVPSDILKAVEQAMDHNRDRQTILSETQNRTSVLSKEILNLKDEKTKQFLDLMDTIDKQREEIARSGRISAGRVSQLQEALNEQHSIMNSLKAKLQMTEAALALSEQKVHNLGELLSATKQEQASMAERHFAELQQQKQEGADREGKLFRDLSASNEKNLFLRNQVDELEKKCKVQQDQIFQLKQDLTNTTAELKLRAVQAEERLEMEKRRFKQSLEDMESLRLKEVDHLTQHMEASERSMQDRVQRLEAIRIALEEELSQVKAAALTERGHAEEELIKVRNQARLEEQQRVEHLEEKLRLMTEARDEAQNCCLKQKQMVGEAQVKANQLNLHADGLRRRIEELQQDLNSKEQEKVTEVNKVKVELQEQIGHLQAERTAQEGLREKIAALERQLKVLSSNHREALLDKEGEISMLMEKLRMKEADISRMKEEEAQRASILQNAIMAYVQGSSLGTHSLRK", "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": "MTNAATDKSVASVARDVSTGKPGKSPDAAVHLLSGGLAGLTSAVTLQPFDLLKTRLQQQHSETSKLTIAGEIRKLSQLKELWRGAVPSALRTSVGAGLYFTTLSKMRAAVAQYNHRDSSVTSVLPKLLPMENLATGFVARAIVGYITMPITMVKTRFESNIYSYRTMGESIVGIYKDIGPDGVVHRSSLLNFFKGSVATLARDCPYAGLYVLFYEGFKNDVLVKVIPESVTGSDSRSSVINSSSAILAASVSTTITAPFDAIKTRLQLTKETSILKTTGILLREDGGVFNLFRGLSLRFGRKALSAGISWCIYEELIKSDFSQCRLFNKERLA", "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": "MSVTKKPDLTDPVLKEKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTFACVIGLSVLDPAAIGEPANPFATPLEILPEWYFYPVFQLLRTVPNKLLGVLLMAAVPAGLITVPFIENINKFQNPYRRPIATTLFLVGTLVAVWLGIGATLPIEISLTFGLF", "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": "FLIFLGGILVMFIYVSSLSANEKFAVDLTSFMWVVPTIVLSFLVLNKNFMFMSPSS", "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": "MGKKRIMFFASLLLITIFLSFSYAGITRESPLSIGKTLSSSNGVYELGFFSFNNSQNQYVGIWFKGIIPRVVVWVANREKPVTDSAANLTISSNGSLLLFNENHSVVWSIGETFASNGSRAELTDNGNLVVIDNNSGRTLWESFEHFGDTMLPFSNLMYNLATGEKRVLTSWKSHTDPSPGDFTVQITPQVPSQACTMRGSKTYWRSGPWAKTRFTGIPVMDDTYTSPFSLQQDTNGSGSFTYFERNFKLSYIMITSEGSLKIFQHNGMDWELNFEAPENSCDIYGFCGPFGICVMSVPPKCKCFKGFVPKSIEEWKRGNWTDGCVRHTELHCQGNTNGKTVNGFYHVANIKPPDFYEFASFVDAEGCYQICLHNCSCLAFAYINGIGCLMWNQDLMDAVQFSAGGEILSIRLASSELGGNKRNKIIVASIVSLSLFVILAFAAFCFLRYKVKHTVSAKISKIASKEAWNNDLEPQDVSGLKFFEMNTIQTATDNFSLSNKLGQGGFGSVYKGKLQDGKEIAVKRLSSSSGQGKEEFMNEIVLISKLQHKNLVRILGCCIEGEERLLVYEFLLNKSLDTFLFDSRKRLEIDWPKRFNIIEGIARGLHYLHRDSCLRVIHRDLKVSNILLDEKMNPKISDFGLARMYQGTEYQDNTRRVAGTLGYMAPEYAWTGMFSEKSDIYSFGVILLEIITGEKISRFSYGRQGKTLLAYAWESWCESGGIDLLDKDVADSCHPLEVERCVQIGLLCVQHQPADRPNTMELLSMLTTTSDLTSPKQPTFVVHTRDEESLSQGLITVNEMTQSVILGR", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MDFIKKYLYVCDHPGFFELTQETFQNRWFPAQINLSVDVKCLSLMSEADVNFYKYLFTFLGMAETLVNFNIDELLVDFECHDIKHYYCEQMAMECVHGKVYFNILNMLFKNNLAATWEFAEAVLKDEALQKKLEWLESKIKMAKTKAEKVLIFYLIEGVFFISSFYCIGLLRVKGVMPGVCMANDYISRDELLHTRAAALLYNTMIPKEERPSSEWVVSLFKEAVEIECAFIEAKTKQVTFVSMDDIRAFLEATADRLLNSIELPRYYKSDPPQSCPLTYTGCIKNVSFFERESTEYSSFIINDL", "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": "MDDSEEDQRLPHHRDPKEFIPLDKLSELGIISWRLNPDNWENDENLKKIREARGYSYMDICDVCPEKLPNYEIKIKNFFEEHLHTDEEIRYCLEGSGYFDVRDENDQWIRVAVKKGGMIVLPAGMYHRFTLDNENYIKAMRLFVGEPVWTPYNRPHDHLPARKEYLDKLLKPEGQAVEAR", "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": "MVSTNPPVLPISTTATDTTNQPPIVTAVVESQPPVVRAFVNGVTETVCGGLSRSRPWSELLDRSAFTKPDSLSEAGTRFRKNSSYFRVNYVCIVALILGFSLLAHPFSLILLLCLAASWLFLYLFRPSDRPLILFGRSFSEYETLGGLILSTIAVIFFTSVGSVLISALMIGIATICVHGAFRAPDDLFLDEQDHAASGFLSFIGVPAIPSVAPSASSAASPV", "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": "MSETEAAPVVAPAAEAAPAAEAPKAKAPKAKAPKQPKAPKAPKEPKAPKEKKPKAAPTHPPYIEMVKDAITTLKERNGSSLPALKKFIENKYGKDIHDKNFAKTLSQVVKTFVKGGKLVKVKGSFKLSEALKAKAKKSTPKKAKADGEAKPKKSEAKPKKAEAVKKTKAPKEKVERPKKEKKEKVEKKKATPKAEKPKKAATPKSAGKKKATPKPKAAPKSPAKKDAKPKKATPSKKAAPKKAPAKKSTPKAKEAKSKGKK", "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": "MGDRRPQDRPRSQGMDSKPWYCDKPPSKYFAKRKHRRLRFPPVDTQNWVFVTEGMDDFRYACQSPEDTLVCRRDEFLLPKISLRGPQADRKSRKKKLLKKAALFSELSPVQPARKAFVEEVEAQLMTKHPLAMYPNLGKDMPPDLLLQVLKQLDPERKLEDAWARCEAREKTTEVPTESGKYPCGESCPRPPETPVSRLRPQLPKTPVSSRRPEPPKTRVSSLRPEPPKTRVSSLHPEPPETRASHLRVDPPETGVSHLCPEPPKTLVSSVHPEPPDTGASHLCPEPPETRVSHLHPEPPETGVSHLRPEPSKTQVSSLCPEPPEAGVSHLCLEPPNTHRVSSFLLQVLKLDSEKKLEDARARCEGQEMTTEELTKPGKYHFWESCPRPFESRMPHLRLVLPITRRMASLCLKPPKTRRVSSLCPEPTKTGASHLKELFQEDTPSTMECVSDSLQRRHTSRKLRDFKWAGDLGVNEESISSLFDFTPECRTTDQDQKIKKANECASRLMYGMELDDMDEVEFLRIKYWDRRRRAAPHSYSAQRGRIRYGPWYFEPKLGKKLRSDEPLIDPKPVLEKPDEPDILDGLYGPIAFKDFILSKGYRMPGVIEKLFAKKGWTYDSVKTPIQRAVQVYKYKEDVTDASKED", "text": "SIMILARITY: Belongs to the FAM47 family."}
+{"protein": "MGNDSVKDKMKGGFNKAKGEVKDKVGDMADRTDMQAEGKKDKAKGEIQKDIGKAKDKFSDKD", "text": "SIMILARITY: Belongs to the UPF0337 (CsbD) family."}
+{"protein": "MLKGIHPALSPELLKTLAEMGHGDEIVLADTHFPAHSLHKNVIRADGISIDILLEAITPLFEFDAYVDAPLLMMKAVEGDSLDPNVETRYLNAIESAVGFTPNLTCLERFDFYTRAKQAYAVVVSGEIAKYGNIIIKKGVTPIL", "text": "FUNCTION: Involved in the anomeric conversion of L-fucose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RbsD / FucU family. FucU mutarotase subfamily."}
+{"protein": "MSKLDLNALNELPKVDRILALAETNAQLEKLDAEGRVAWALDNLPGEYVLSSSFGIQAAVSLHLVNQICPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWEPSMAEEETRFFGLKRECGLHEG", "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": "MKNLHALMPACLLLTASAMAAPSNIGSAGDIHFTITIKAATCELENDSIDVNMETVVLQRPVKVGKELNQKNFSIGLKDCAYATKASVTMDGSPDPTDPSLFALDSGGATGVALKIKTSGGEQQYPSSTDSTPVEHTVWFDGTNKLNYIASYVPVKPDATVGTANATVNFSVTYE", "text": "SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the fimbrial protein family."}
+{"protein": "MSTSHAAHPDRLLPADPATRDIARRLLTYVEDLPIISPHGHLEASMFVKDEPFADPTTLLISPDHYLTRVLHSAGVDLADLRVGGTEGKTPREAWRIFASNWDLYTGTATGYWVEQEFEHVFGINPDRLSAENADDIYDELSEILARPDFRPRALAEQFNLEILATTDDPLDDLADHKALAQDPTFSPRVLPTFRPDAYTKMYNPGWAEKTTRLIDVAGDGKAGWEGYLQAMRNRRQYFIDHGATSADHGTHDTDTTPLSHEDAQRILDKGLAGTATLAEMRAFEANTTYRFAEMCQDDGLVMTLHPGVYRNHSASAQKKFGNDIGADIPFQLEYTRGLRPLLSDFGENKDFHFVMFTIDETVFSREVAPLAGYYPAAYVGAPWWFIDEIDAMNRFRSLTTGTTGFSRYSGFIDDTRAYCSIPARHNTSRRVEANYLARLVAEHRISETRASEIIVDLIDASPRRVFKL", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family."}
+{"protein": "MRSGEELDGFEGEASSTSMISGASSPYQPTTEPVSQRRGLAGLRCDPDYLRGALGRLKVAQVILALIAFICIETIMACSPCEGLYFFEFVSCSAFVVTGVLLIMFSLNLHMRIPQINWNLTDLVNTGLSAFLFFIASIVLAALNHRAGAEIAAVIFGFLATAAYAVNTFLAVQKWRVSVRQQSTNDYIRARTESRDVDSRPEIQRLDTFSYSTNVTVRKKSPTNLLSLNHWQLA", "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": "MFTRADFEIFDDPTLKGRLNKIYTELDPKFEVFGAQLQNELAVATNREFTLHIAKHLRRFKNPPMNTWMALSESSRGYKMMPHFEVGFGDDRIFVWFALMAEMPDKTDYAPLLASQSEKLLSDFTDYDLSYDHMTKQKFPMSPDNLQLIQDKFAKTKKGEWLLGKVYLKDNPLFDHPEELMADIQTTLLKMVPLYELINAK", "text": "SIMILARITY: Belongs to the UPF0637 family."}
+{"protein": "MRLFLSLPVLVVVLAMVLEGPAPAQAAPEISSTLERIPDKLKEFGNTLENKARAAIESIKQSDLPAKTRNWFSETFNKVEQLKTTFS", "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": "MERAKSRKPHIMMIPYPLQGHVIPFVHLAIKLASHGFTITFVNTDSIHHHISTAHQDDAGDIFSAARSSGQHDIRYTTVSDGFPLDFDRSLNHDQFFEGILHVFSAHVDDLIAKLSRRDDPPVTCLIADTFYVWSSMICDKHNLVNVSFWTEPALVLNLYYHMDLLISNGHFKSLDNRKDVIDYVPGVKAIEPKDLMSYLQVSDKDVDTNTVVYRILFKAFKDVKRADFVVCNTVQELEPDSLSALQAKQPVYAIGPVFSTDSVVPTSLWAESDCTEWLKGRPTGSVLYVSFGSYAHVGKKEIVEIAHGLLLSGISFIWVLRPDIVGSNVPDFLPAGFVDQAQDRGLVVQWCCQMEVISNPAVGGFFTHCGWNSILESVWCGLPLLCYPLLTDQFTNRKLVVDDWCIGINLCEKKTITRDQVSANVKRLMNGETSSELRNNVEKVKRHLKDAVTTVGSSETNFNLFVSEVRNRIETKLCNVNGLEISPSN", "text": "SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MRLFNWRRQAVLNAMPLVKPDQVRTPWHEFWRRFRRQHMAMTAALFVILLIVVAIFARWIAPYDAENYFDYDNLNNGPSLQHWFGVDSLGRDIFSRVLVGAQISLAAGVFAVFIGAAIGTLLGLLAGYYEGWWDRLIMRICDVLFAFPGILLAIAVVAVLGSGIANVIIAVAIFSIPAFARLVRGNTLVLKQQTFIESARSIGASDMTILLRHILPGTVSSIVVFFTMRIGTSIISAASLSFLGLGAQPPTPEWGAMLNEARADMVIAPHVAVFPALAIFLTVLAFNLLGDGLRDALDPKIKG", "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": "MTSADYASRQRAIIAELNVAPHFDAEAEIARRIDFLAQYLRSTGLRTYVLGISGGVDSSTAGRLAQLSVERLRADGYDARFIAMRLPNGVQNDEEDAQRALAFVRADEVLTVDVKPAADAMLRSLVASGHAFETPAQQDFVHGNIKARERMIAQYAVAGARRGIVIGTDHAAESLMGFFTKFGDGGADILPLAGLSKRRVRGVARALGGEELIVMKVPTADLEELRPLRPDEHAYGVTYDEIDDFLEGKPVADRVYETVLRFYDGSRHKRALPYTMFDWPAA", "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": "MIIYLHGFDSTSPGNHEKVLQLQFIDDDVRFINYSTLHPKHDMQHLLKEVSKVIDQSDDPNPLICGVGLGGYWSERIGFLCGIKQVMFNPNLHPENTMAGRIDRPEEYEDIATKCVDQFRAKNQGRCLVILSKEDEIHDNTKTASELEKHYDIIWDESQSHKFKKISQHLQAMKEFKNT", "text": "SIMILARITY: Belongs to the UPF0227 family."}
+{"protein": "MSEEGGVEVKLLKPRKPLPDVGEIVVGTVQEVHDYGAYLILDEYGGVRAFLPWSEIASRAVRNIHAVLKPRQKVVVKVIRVYKKRGQVDVSLKRVMDSEKKRKMMFYKRYLKAATLVELIAEKLGKSVDEAYREVLWKLEDAYGDPMKGLEAAVLQGREALEKAGVPEEWIEPLLETAKTHVRVKTVKITFYLTLRSMAGDGVERVRKVLEAAKSQIESFKDSKVVARIYTVGAPKYRVELQGYNYKTLEKALEKMVEAARKTASKLGVEFSFERED", "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": "MMIQLECLSVTYPGGVQALQAVSLNFNPGEFTVILGASGSGKSTLLRCLNGLIQPTAGTITIEGYRQINDPKVLHQHRQRTGMIFQQHQLIARQTALQNVLTGRLAYHSTVRSFFPLPKADKYIALECLDRVGLLSKALARVDNLSGGQQQRVGIARALAQQPRLMLADEPVASLDPASSHKVISFLRQICQEDGIAAIMSLHQVDLAKAYADRIVGISQGRIVFDGSAADIEECELNRIYGNAENIHFDDIPSNQYPIASN", "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": "MSDLFATITTPNGVKYEQPLGLFIDGEFVKGAEGKTFETINPSNEKPIVAVHEATEKDVDTAVAAARKAFEGSWRQVTPSTRGRMLTKLADLFERDAEILASIEALDNGKSITMAHGDIAGAAGCLRYYGGWADKIHGQTIDTNSETLNYTRHEPIGVCGQIIPWNFPLLMWAWKIGPAIATGNTVVIKTAEQTPLSGLYAANVIKEAGIPAGVVNVISGFGRVAGSAISHHMDIDKVAFTGSTLVGRTILQAAAKSNLKKVTLELGGKSPNIVFNDADIDNAISWANFGIFYNHGQCCCAGSRILVQEGIYDKFIARLKERALQNKVGDPFAKDTFQGPQVSQLQFDRIMEYIQHGKDAGATVAVGGERHGTEGYFIQPTVFTDVTSDMKINQEEIFGPVVTVQKFKDVEDAIKIGNSTSYGLAAGIHTKDVTTAIRVSNALRAGTVWVNSYNLIQYQVPFGGFKESGIGRELGSYALENYTQIKAVHYRLGDALF", "text": "SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
+{"protein": "MDEDLRERIEREAETAALFNALKHESDAQVGAILGPMMGENPDFRPHGDEIPGIISPVIERVNGLSDEEKRERLEELAPEKVEALAAEDEGDDRPLPELPNADAYDDVRMRLAPNPNGPWHVGHARMPAVIGTYKDRYDGWFCVRFDDTDPETKRPDLDAYGEILDAIDYLGFEPDEVVKASDRVETYYEYGRKLIKAGGAYTCSCDAESFSELKNNAEACPHRDKDIETTLSEFEAMIDGEYSAGEMVLRVRTDIEHKNPALRDWVAFRMVDTPHPREEAADYRCWPMLDFQSGIDDHEFGISHIIRGIDLQDSAKRQQFVYEYFDWEYPEVIHWGHVQIDAYDIEMSTSTIKQLIDDGELDDWDDPRAPTVASLKRRGIRGQAIVNAMVELGTSTSNVDLAMSSVYAENREFVDDEADRRFFVRDGVEKPLAGGPESASPPLHPNDEDRGRREIPVGDAVYVEPDDVPADGERVWLKGLGPVRHEDGAFVATDDDIEVVRDGAVDVVHWVPAQESVPLRLRTVDGDEAGHAEPGIETYDADDIVQFERIGFARIDRHDDEESVAYFAHP", "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": "MNGAEAMIKALEAEKVEILFGYPGGALLPFYDALHHSDLIHLLTRHEQAAAHAADGYARASGKVGVCIGTSGPGATNLVTGVATAHSDSSPMVALTGQVPTKLIGNDAFQEIDALGLFMPIVKHNFQIQKTCQIPEIFRSAFEIAQTGRPGPVHIDLPKDVQELELDIDKHPIPSKVKLIGYNPTTIGHPRQIKKAIKLIASAKRPIILAGGGVLLSGANEELLKLVELLNIPVCTTLMGKGCISENHPLALGMVGMHGTKPANYCLSESDVLISIGCRFSDRITGDIKSFATNAKIIHIDIDPAEIGKNVNVDVPIVGDAKLILKEVIKQLDYIINKDSKENNDKENISQWIENVNSLKKSSIPVMDYDDIPIKPQKIVKELMAVIDDLNINKNTIITTDVGQNQMWMAHYFKTQTPRSFLSSGGLGTMGFGFPSAIGAKVAKPDSKVICITGDGGFMMNCQELGTIAEYNIPVVICIFDNRTLGMVYQWQNLFYGKRQCSVNFGGAPDFIKLAESYGIKARRIESPNEINEALKEAINCDEPYLLDFAIDPSSALSMVPPGAKLTNIIDAVQEHPNEKIVCFDEIKRRYMENKRNRK", "text": "SIMILARITY: Belongs to the TPP enzyme family."}
+{"protein": "MLKDAYTADVTPERDGEEVRLAGWVHEVRDLGGIKFVLLRDRTGIVQLTLPKQKVPKETFEKVPKLTKESVIRVEGTVQANEKAPGGVEVIPQRIEVLSESDTHLPLDPTGKVDADLDTRLDARVLDLRREEPQAIFKIRNVVTTAIREFLEERGFIEVHTPKIIASATEGGTELFPVVYFERDAYLAQSPQLYKQMLMAAGFERVYEIGPIFRAEEHNTRRHLNEAISVDIEMSFIESEEDVMRVLEELLAHVFRKVREECEKELEALDRELPELETPFERITYEETLDLLSEHGIEVEWGEDLPTEAERKLGEIFEEPFFITEWPRETRPFYTMAKDDEVTTAFDLMYQGLELASGAQREHRYDVLVRQIEEQGLSPEDFRHYLEAFKYGMPPHGGWGLGLERTLMTITGAENIREVTLFPRDRKRLHP", "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": "MDLEHQTMETFLRWAAEIGISDSIDSSRFRDSCLGHSLSVSDFPDAGGRGLGAARELKKGELVLKVPRKALMTTESIIAKDLKLSDAVNLHNSLSSTQILSVCLLYEMSKEKKSFWYPYLFHIPRDYDLLATFGNFEKQALQVEDAVWATEKATAKCQSEWKEAGSLMKELELKPKFRSFQAWLWASATISSRTLHVPWDSAGCLCPVGDLFNYDAPGDYSNTPQGPESANNVEEAGLVVETHSERLTDGGFEEDVNAYCLYARRNYQLGEQVLLCYGTYTNLELLEHYGFMLEENSNDKVFIPLETSLFSLASSWPKDSLYIHQDGKLSFALISTLRLWLIPQSQRDKSVMRLVYAGSQISVKNEILVMKWMSEKCGSVLRDLPTSVTEDTVLLHNIDKLQDPELRLEQKETEAFGSEVRAFLDANCLWDVTVLSGKPIEFSRKTSRMLSKWRWSVQWRLSYKRTLADCISYCNEKMNNLLGTQDRLRDL", "text": "SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
+{"protein": "MFFRNLTLFRFPTSLDFSQIDSILPNARLRPVGPLEMTSRGFISPFGREEQEVLNQRQGDFLWLTVGSEDKILPASVVNDLLTRKCSEIEEKKGHPPGGRERKRIKDDLIHELLPRAFVKKSRIDAMLDLRYGYVAVDTASRKAAETVISEIRDLLGSFPALPLNAEISIRSMLTSWIAGEPLPEHLNLGDECEMKDATEGGAIIKCQHQALRCEEIDKHLEVGKQVSKLALILDDHVSFVLGDDLVIRKLKFLDGMLDQLEHSDTDGIRAELDARFALMSAEIRRLFLLLEVPLKLSKANN", "text": "FUNCTION: May be involved in recombination. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the RdgC family."}
+{"protein": "MAKENAEFKEYEKLLDQAYEQLPDKIFEAKRFKVPKGYSVIQGNRTIIKNFGDVSRTLNRDPQHVLKYLLRELGTSGNVEGNRAILQGKFTHYVINDRVKEYVDNFVMCHECNRPDTVIIREDRIDMLKCSACGARAPLKSL", "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": "MRRELLLEKIETYKAIMPWYVLDYYQSKLAIPYSFTTLYEYLKEYKRFFDWLMDADLTQAPKIADIDLSTLEHLTKKDLEAFVLYLRERPSLNTYSTKEGLSQTTINRTLSALSSLYKYLTEEVENDQGEPYFYRNVMKKVSTKKKKETLASRAENIKQKLFLGDETLAFLDYVDKEYEQKLSNRAKSSFRKNKERDLAIIALLLASGVRLSEAVNLDLKDVNLNMMIIEVIRKGGKRDSVNVAGFAKGYLESYLAVRQRRYKAEKQDLAFFLTEYRGVPNRMDASSIEKMVGKYSEDFKIRVTPHKLRHTLATRLYDATKSQVLVSHQLGHSSTQVTDLYTHIVNDEQKNALDNL", "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": "MSEFIAENRGANAITRPNWSAVFSVAFCVACLIIVEFLPVSLLTPMAQDLGISEGVAGQSVTVTAFVAMFASLFITQTIQATDRRYVVILFAVLLTLSCLLVSFANSFSLLLIGRACLGLALGGFWAMSASLTMRLVPPRTVPKALSVIFGAVSIALVIAAPLGSFLGELIGWRNVFNAAAAMGVLCIFWIIKSLPSLPGEPSHQKQNTFRLLQRPGVMAGMIAIFMSFAGQFAFFTYIRPVYMNLAGFGVDGLTLVLLSFGIASFVGTSLSSFILKRSVKLALAGAPFVLALSALVLTLWGSYKIVATGVAIIWGLTFALIPVGWSTWITRSLADQAEKAGSIQVAVIQLANTCGAAIGGYALDNIGLTSPLMLSGTLMLLTALLVTAKVKMKKS", "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": "MSFQEVWEKEPMKKPRIQKVTVNFGVGEAGDRLTIGAKVIETLTGQAPVRTLAKQTNPAFGIRKKLPIGLKVTLRGKNAEEFLENAFVAFKVSGKVLYASSFDKVGNFSFGVPEHIDFPGQKYDPTVGIYGMDICVTFEKPGYRVKSRKLKRSHIPAKHLVKKEEAIEYIEKKFGAEVVME", "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": "MIISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSQVALRQRVLKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARRGEVQAAGAADAHGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMRRYWQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLANNFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAYLYALATAGKAGVANLLNLIEKEMKVAMTLTGAKSISEISQDSLVQELDKALPAALAPLAKGNAA", "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": "MIKADLKIINGQIYNTFTRQFTAKEVAIVDGKFFQIADKLSDDFKFEDILDLKGSYVIPGLIDSHMHIESSMATPTNFSETAIRFGTTTVIADAHEIANTSGIKGLKRFMDQPSLIDTFFAIPSSVPSTNPELETTGGIIDLEEVKELLADPRIICLGEAMNFKGITSEPNSLIRKIIALCQKKRPRMPLEGHVPNISKEDLAKFIFAGILSDHTQQTPALIKEKIENGMFIQLQKKSLNKENIETIVKNHFYDYSALVTDDTMADDLINGHLNSIIKLAVKCGLPLEWAIYMTTYTPAQHMHFQDRGVIAPGKIADFVVLNNLDGFSIKNVYKRGVPIDKLSIDDEKPFASEEYHSIYVPNRSAKDFTLRVSKDLKKITANVIEIAAKGTFTKAVKKELLVKDGIVDWQKAGLALLAVQERYGKTGQLTLALVSKSINKSGAIATTWAHDHHNLMVLGTNPDSMAIAYDKVASQQGGYLVVKDKEIVANVQLPIAGIISDEPIDIIGHKLKKVRLAMKDLGYVNTNEIMSLSTLSLLVSPSIKVSDKGIFDVKTQTKIPLLLAGEE", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family."}
+{"protein": "MGKASHSSTAQDAVALFDSLRSAYSATPTTLKIIDLYIGFAVSTALIQVVYMAIVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKENKEFKDLAPERAFADFVLCNLVLHMVIMNFLG", "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": "MCGIMGAVSERDISKVLLEGLRRLEYRGYDSAGIAVIDSQDRLKRVRIQGKVQNLADAMQETAIAGNTGIAHTRWATHGKPSEQNAHPHLSHGEIALVHNGIIENHEHLRQQLITYGYQFTSETDTEVAAHLIHYHYQQHENLLLAVQKSAAEMQGAFALGVIHQKRPEELVAIRKGSPLVLGFGIGENFIASDALALRSFAQSVIYMEEGDSACVTTQDIKVYDSNRILVQRATHPLNSDSEIVNKGPYRHFMLKEIFEQSKVITDTLESRINSIDVLRASFGEKASHIFPMVKNIHIVACGTSYHAGMIAKYWLESLAGLPTQVEIASEYRYRDVVVPDNTLFITVSQSGETADTLAALFKAKQSNYLASLAICNVATSTLVREADCVFLTRAGIEIGVASTKAFTTQLAAFLMLAAALCKDNRAQEVLRQLQELPACCERVLQMNEEVESLASLFVNKVHALFLGRGVQYPVALEGALKLKEISYIHAEAYPAGELKHGPLALVDKDMPVIAVAPNDELLDKLKSNLHEVSARGGQLFVFVDDSQNWKANGARLIKVPSCGAWLAPIIYTIPLQLLAYHVAVAKGTDVDQPRNLAKSVTVE", "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": "MTTQASTFAVAVPSVATPFRRHRNPFVVRAQAEPSDKSVEIMRKFSEQYARKSGTYFCVDKGVTSVVIKGLADHKDTLGAPLCPCRHYDDKAAEVAQGFWNCPCVPMRERKECHCMLFLTPDNDFAGNEQTITLDEIKESTANM", "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": "MITTEIKRVKNHINGEWVESTGTEVEAVPNPATGKIIAYVPLSPKEDVEKAVEAAKAAYETWSKVPVPNRSRQLYKYLQLLQENKEELAKIITLENGKTLTDATGEVQRGIEAVELATSAPNLMMGQALPNIASGIDGSIWRYPIGVVAGITPFNFPMMIPLWMFPLAIACGNTFVLKTSERTPLLAERLVELFYEAGFPKGVLNLVQGGKDVVNSILENKDIQAVSFVGSEPVARYVYETGTKHGKRVQALAGAKNHAIVMPDCNLEKTVQGVIGSAFASSGERCMACSVVAVVDEIADEFIDVLVAETKKLKVGDGFHEDNYVGPLIRESHKERVLGYINSGVADGATLLVDGRKIKEEVGEGYFVGATIFDGVNQEMKIWQDEIFAPVLSIVRVKDLEEGIKLTNQSKFANGAVIYTSNGKHAQTFRDNIDAGMIGVNVNVPAPMAFFAFAGNKASFFGDLGTNGTDGVQFYTRKKVVTERWF", "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": "MVQMKKCTTKEDVLEAVKERDVKFIRTQFTDTLGIIKSWAIPAEQLEEAFENGVMFDGSSIQGFTRIEESDMKLALDPSTFRILPWRPATGAVARILGDVYLPDGNPFKGDPRYVLKTAIKEAEKMGFSMNVGPELEFFLFKLDANGNPTTELTDQGGYFDFAPLDRAQDVRRDIDYALEHMGFQIEASHHEVAPSQHEIDFRFGDVLCTADNVVTFKYVVKSIAYHKGYYASFMPKPLFGVNGSGMHSNQSLFKDGKNVFYDPDTPTKLSQDAMYYIGGLLKHIREFTAVTNPVVNSYKRLVPGYEAPVYISWSAQNRSSLIRIPATRGNGTRIELRCPDPACNPYLAFALMLRAGLEGIKNKIDPGEPTNVNIFHLSDKEREERGIRSLPADLKEAIDEMKGSKFVKEALGEHVFSHYLCAKEMEWDEYKAVVHPWELSRYLSML", "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": "MYKHPDEEWLDEIPGQQENEDDDEIIWVSKSEIKRDAEALKALGAELVDLGKNALDRIPLDEDLRAAIELAQRIKKEGRRRQLQLIGKLLRQRDPEPIQTALDKLKNRHNQQVALFHKLEQLRDRLISDGDEAISEVLNLYPHADRQQLRALIRNAKKERDGNKPPKSARQIFQYLRTLAEAND", "text": "SIMILARITY: Belongs to the UPF0307 family."}
+{"protein": "MEALRQKVKEDGVVIGEKILKVDGFLNHQIDAQLMYDIGETFYEQFKDQKVTKILTVEASGIAPAIMVAYKFGVPCLFAKKAKPNTLNKGFYQTDIHSFTKDKTNSVIISEEFLDEHDRVLIIDDFLANGDASLGLNRLVHQAGAETVGVGIVVEKSFQQGRTRLEEAGLKVSSLCEVASLSGNKVTLVGEE", "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": "MAGETSFKYIVRIAGVDIDGDLKLPYGLASIKGIGYTTAMAVIRMLGLDPEKKVGFLTEEEIRRLDEVLRDITQLGLPKWLYNRRKDYETGKDLHLIGSELIFYARRDIEREMKIGSWRGIRHKYGLKVRGQRTRTTGRLGMTIGVRKKR", "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": "MTTIAVIGGGQIGEALVSGLIAANMNPQNIRVTNRSEERGQELRDRYGILNMTDNSQAADEADVVFLCVKPKFIVEVLSEITGTLDNNSAQSVVVSMAAGISIAAMEESASAGLPVVRVMPNTPMLVGKGMSTVTKGRYVDAEQLEQVKDLLSTVGDVLEVAESDIDAVTAMSGSSPAYLFLVTEALIEAGVNLGLPRATAKKLAVASFEGAATMMKETGKEPSELRAGVSSPAGTTVAAIRELEESGIRGAFYRAAQACADRSEELGKR", "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": "MKPLLILASASPFRRALLSNAGLAFEARAAAIDERALEQPLEASGASPADVALALAEAKAKDVARYFSDALVIGSDQTMSLGTRVYHKPRDMTEAAEHLRSLSGRMHSLNSAIVLVRNDEVVWRHVSTANMTVRPLSDGFIDRHLAKVGEKALTSVGAYQLEGEGIQLFERIEGDYFTILGLPMLPLLSKLRELGAIDA", "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": "MSITIPYDGSISREPSPSPPPPKANTKNLPTKILSNFLIGLIMIPVAITAFIFILTSLGFTFFFAFYWFLQRNYRHRLRRHRRHEYSDGLSPRCVKRLPQFKYCEPSSEYGGDDCVVCIDGFRQGQWCRKLPRCGHVFHRKCVDLWLIKVSTCPICRDRVYRFEEGRRWRPQGEIF", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily."}
+{"protein": "MAKFRRRTCIILALFILFIFSLMMGLKMLRPNTATFGAPFGLDLLPELHQRTIHLGKNFDFQKSDRINSETNTKNLKSVEITMKPSKASELNLDELPPLNNYLHVFYYSWYGNPQFDGKYIHWNHPVLEHWDPRIAKNYPQGRHNPPDDIGSSFYPELGSYSSRDPSVIETHMRQMRSASIGVLALSWYPPDVNDENGEPTDNLVPTILDKAHKYNLKVTFHIEPYSNRDDQNMYKNVKYIIDKYGNHPAFYRYKTKTGNALPMFYVYDSYITKPEKWANLLTTSGSRSIRNSPYDGLFIALLVEEKHKYDILQSGFDGIYTYFATNGFTYGSSHQNWASLKLFCDKYNLIFIPSVGPGYIDTSIRPWNTQNTRNRINGKYYEIGLSAALQTRPSLISITSFNEWHEGTQIEKAVPKRTSNTVYLDYRPHKPGLYLELTRKWSEKYSKERATYALDRQLPVS", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 99 family."}
+{"protein": "MYKNQLQELAQRSCFSLPSYVCTREGPDHAPRFKATVTFNGETFDGPSNCTTLRQAEHAAAEVALARLSLRGPSSSLTARVLDETGVYKNLLQETAHRAGLKLPVYTTVRSGPGHSPVFSSTVELAGMSFAGDPAKTKKHAEKNAAMAAWSSLKQSNIRTTVSPLVFDLVWIVCHGGDVFVVVWCSAGGAQGARRRRRRGAGACGRRQGARRAEAAGRLRRRRWRREGGGGVSTEEASRRRVLFVRHVAVQTSMGASVAAAAGGRTQDTASPAPAAAAASGGVRLPSRRRRAGARAEEGRRAGAHAARRHAARQGGRRNAAADAVLLRAVLPPRRRRRPDEALRRRRRVPRAAGGERPFSDPGLRRATVAAAAAAQGGRSSDLIQEGVVVVKTSIQSIAQPAPI", "text": "FUNCTION: Binds double-stranded RNA."}
+{"protein": "MGTEEKMTRSDIDLNEPAFYNNRELSWLAFNERVLEEAIDERNPLLERLKFLAIFSSNLDEFFMVRVAGLKDQVKAGFNKPENKAGLTPKQQLRQISERNHQLVQLQDRVYTETIIPMLSQHGIQFLTFDELSDKQRSFLEKRFDHYIFPVLTPMAVDAYRPFPMLLNKSLNLAVVIKNKESDSREQLAIVQVPSVLNRFILLPCEDGKNQFILLENVISYFIEKLFKGYTVKSVSPFRITRNADLPIHEEGARDLLREIEKELKKRKWGAAVRLEMQEGLMDPNVLKLLLDVLEIHKNDVYSLQGPLDLTFLFKLYNRLIVDYEHLTNETLIPQPPEDLIGETNIFDAILKRDIFLHHPYESFQPVIDFIATAAEDPQVLAIKQTLYRVSGDSPIINALARAAENGKQVTVLVELKARFDEENNIQWAKKLEKSGVHVIYGITGLKTHSKITLVVRHHNDEIQRFVHLGTGNYNDSTAKLYTDMGLLTADEEFGIDATNFFNHLSGYSEKPQWHHLSTAPFEIRDTFLDLIDQEIECHKQNGNGHIIAKMNSLTDKPIILKLYEASRAGVRIELIVRGICCLRPGIPNVSEHIRVFSIVDRFLEHSRIFYFHHGGDDKVFLSSADWMTRNMEKRIEILFPIYQQSTKRRIIEILTITLLDNMKAREQNQFGQYRYVKRNPSEQPVQSQLTFFDMASRFSDSEAE", "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": "MPSIKQCSFCGKEIPPATGLMYIRNDGSILWFCSNKCKKSMLKLHRDPKKLKWTKSYIGGK", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family."}
+{"protein": "MALLRRPTVSSDLKNIDTEVIPKAKSHVTIRRAVLEEIGNKVRNRTTQVAKKPQNTKVPALPTKVTNVNKQPKPTASVKPVQMEALAPKDRPPAPEDVSMKEESLCQAFSDALLCKIEDIDNEDRENPQLCSDYVKDIYQYLRQLEVLQSINPHFLDGRDINGRMRAILVDWLVQVHSKFRLLQETLYMCIAIMDRFLQAQLVCRKKLQLVGITALLLASKYEEMFSPNIEDFVYITDNAYTSSQIREMETLILKELKFELGRPLPLHFLRRASKAGEVDVEQHTLAKYLMELTLVDYDMVHYHPSQVAAAASCLSQKVLGQGKWNLKQQYYTGYMESEVLEVMQHMAKNVVKVNDNRTKFIAVKNKYASSRLLKISTIPQLNSKIIKDLASPLLGSP", "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": "MAAQVPTEELKKLKVAAKSDDPAAANGANGNTANDSDGSDDDDEPEDAGAAAGGEGAKKKKKRKPRKKKKKNANGQTDPPRIPISQLFPDNSYPKGQEVEYLGENTYRTTNEEKRHLDSLNSDLLTDYRHGAEAHRQARRWAHKHVKPGMSLTDIANGIEDSVRALVGHSGLEEGDAIIAGMGFPTGLSINHCAAHYTPNAGNKMVLEHDDVLKVDIGVHVNGRIVDSAFTVAFNPRYDNLLAAVKDATNTGIREAGIDARLGEIGEAIQETMESYEVEIDGETYPVKPIRNLNGHTIDRYTIHGGKSVPIVKSADQTKMEEGEIYAIETFGSTGLGYVRDEGEVSHYAKRADAPNVALRLTSAQKILNVINKNFGTLPFCRRYLDRLGQDKYLLGLNNLVSNGIVEAYPPLVDKKGSYTAQYEHTILLRPTVKEVISRGDDY", "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": "MAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYITSEILWGYRFTPVLTLEDGFYEVDYNSFHETYETSTPSLSAKELAELASRAELPLSWSVSSKLNQHAELETEEEEKNLEEQTERNGDVANLENESKV", "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": "MADKKAPASGWPIVSGEYVVGNPESCVAVVTLGSHGLDEAAIEAGAAISGPCHTENLGIEKVVANYISNPNIRFMLVTGSEVQGHITGQCFKALYENGIGDDGGIIGAKGAIPFLENAGQDAISRFQNQLVEIVDLIDVEDTGKISSAIKDCISKDPGAFEEDPMILDLEGGGGEAGADESTSIKPAAPETVLLEARMRMISEKINDAALIAKFNSGYYNGKIQGIAIGLFLSLLIFSLL", "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": "MHPTTLMYTSSLLLMFAVLLYPLLVTFTSLPLNNDWASSHAKTAVKSAFLISLAPLSLFLSTGMEAVTSSWTWMVTTTLDITLSFKFDHYSIIFIPIALYVTWSILEFATWYMHSDPFMNRFFKYLLTFLVAMLILVSANNLFQLFIGWEGVGIMSFLLIGWWHGRADANTAALQAVLYNRVGDIGLILGMAWLATNVNSWDIQQMFILSKNLDMTLPLLGLILAATGKSAQFGLHPWLPAAMEGPTPVSALLHSSTMVVAGIFLLIRMSPLMENNQTALTLCLCLGALTTMFTATCALTQNDIKKIVAFSTSSQLGLMMVTIGLNQPQLAFLHICTHAFFKAMLFLCSGSVIHSLNDEQDIRKMGGLHHLAPFTSSCLTVGSLALTGTPFLAGFFSKDAIIEALNTSHVNAWALTLTLIATSFTAIYSLRVIFFVTMGTPRFLPLSPINENNPAVINPLKRLAWGGIFGGLLVMLNINLFKTPVLTMPAELKLAALAVSILGLLTALELATLTSKQFKVTPLRTPHHFSTSLGFVPAIIHRQIPQLSLLLGQKIASQMVDQTWLEKTGPKAIANATTPLASATSNMQQGLIKTYLTLFLMTLVLVTLISAT", "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": "MNTIRNSICLTIITMVLCGFLFPLAITLIGQIFFYQQANGSLITYDNRIVGSKLIGQHWTETRYFHGRPSAVDYNMNPEKLYKNGVSSGGSNESNGNTELIARVKHHVKFDNSNVTIDAATSSGSGLDPHITVENALKQAPRIADARHISTSRVADLIQHRKQRGVLTNDYVNVLELNIALDKMKD", "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": "MPAPCNCIETNVCICDTGCSGEGCRCGDACKCSGADCKCSGCKVVCKCSGSCACEGGCTGPSTCKCAPGCSCK", "text": "FUNCTION: The metallothioneins are involved in the cellular sequestration of toxic metal ions. SIMILARITY: Belongs to the metallothionein superfamily. Type 2 family."}
+{"protein": "MKVYKDVFTNDEVCSDSYNQEDPFGIADFREIAFEVKSNKRIKGNDDYGIADNSEEAVDGMGADVEQVIDIVDSFQLTSTSLSKKEYSVYIKNYMQKILKYLEEKKPDRVDVFKTKAQPLIKHILTNFDDFEFYMGESLDMDAGLTYSYYKGEEVTPRFVYISDGLYEEKF", "text": "FUNCTION: Involved in calcium binding and microtubule stabilization. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCTP family."}
+{"protein": "MEKVLVFGHKNPDTDAICSAIAYAELKKELGMNAEPVRLGEISGETQFALDYFKVEGPRFVETVANEVDNVILVDHNERQQSANDIESVRVLEVIDHHRIANFETSDPIYYRCEPVGCTATILNKMYKENGVTIRKEVAGLMLSAIISDSLLFKSPTCTEQDVAAARELAEIAGVDADKYGLEMLKAGADLSGKTMEQLISLDAKEFQMGNAKVEIAQVNAVDTNDVLVHQAELEKVISAVVEEKGLDLFLFVVTDILTNDSVGLAIGKAANIVEKAYNVSLENNTATLKGVVSRKKQIVPVLTEAFQA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase class C family."}
+{"protein": "MAEIAAELVAVEKALWSGTATAVIAETTEGEIGVLPGHEPLLGQLVENGVVIIRTTEGEKLVAAVQGGFLSVSSKKITVLADSAVWADEVDQADAEARVREASSEEEKSRAESELRAVKRSKEK", "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": "MIINETKGKAWHGKVKLADTFLKRFRGLMLVKNVNHALVFVLPAETRANASIHMFFMLSDIDVIWLDSSRRVVDFKTAKKWRLYTPKKAAQYIIEGPVGLIRTLEVEEGDLISWTPTEEREKAVPVKSLIPGKINLNGSKNSIAMVESVKEVKANEV", "text": "SIMILARITY: Belongs to the UPF0127 family."}
+{"protein": "MPINYTNLLLMLRECKNFRCLLQVHGSLIVSGLKPHNQLINAYSLFQRQDLSRVIFDSVRDPGVVLWNSMIRGYTRAGLHREALGFFGYMSEEKGIDPDKYSFTFALKACAGSMDFKKGLRIHDLIAEMGLESDVYIGTALVEMYCKARDLVSARQVFDKMHVKDVVTWNTMVSGLAQNGCSSAALLLFHDMRSCCVDIDHVSLYNLIPAVSKLEKSDVCRCLHGLVIKKGFIFAFSSGLIDMYCNCADLYAAESVFEEVWRKDESSWGTMMAAYAHNGFFEEVLELFDLMRNYDVRMNKVAAASALQAAAYVGDLVKGIAIHDYAVQQGLIGDVSVATSLMSMYSKCGELEIAEQLFINIEDRDVVSWSAMIASYEQAGQHDEAISLFRDMMRIHIKPNAVTLTSVLQGCAGVAASRLGKSIHCYAIKADIESELETATAVISMYAKCGRFSPALKAFERLPIKDAVAFNALAQGYTQIGDANKAFDVYKNMKLHGVCPDSRTMVGMLQTCAFCSDYARGSCVYGQIIKHGFDSECHVAHALINMFTKCDALAAAIVLFDKCGFEKSTVSWNIMMNGYLLHGQAEEAVATFRQMKVEKFQPNAVTFVNIVRAAAELSALRVGMSVHSSLIQCGFCSQTPVGNSLVDMYAKCGMIESSEKCFIEISNKYIVSWNTMLSAYAAHGLASCAVSLFLSMQENELKPDSVSFLSVLSACRHAGLVEEGKRIFEEMGERHKIEAEVEHYACMVDLLGKAGLFGEAVEMMRRMRVKTSVGVWGALLNSSRMHCNLWLSNAALCQLVKLEPLNPSHYSQDRRLGEVNNVSRIKKVPACSWIEV", "text": "SIMILARITY: Belongs to the PPR family. PCMP-E subfamily."}
+{"protein": "MTQKEKNETCIHATVSGKVQGVFFRESVRKKAEELQLTGWVKNLSHGDVELVACGERDSIMILTEWLWEGPPQAAVSNVNWEEIVVEDYSDFRVR", "text": "SIMILARITY: Belongs to the acylphosphatase family."}
+{"protein": "MEIEKLLEQVNWEKNNGIVPVIVQDEKGEVLTLAYMNKEALRKTLETGIAHYYSRSKGRIRMKGEVSGNIQTVKEIKIDCDNDALLLIVSPKGPACHTGNYSCFYRKLGEPERVLPIDYSLSILKELEEIIKRRKETPVEGSYTSKLFKEGREKIYKKFGEEAIEVLVAEKRERIIYEVADLLYHLLVLLTYNDISLGEVMNELRRRRK", "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": "MIKTESIDFHSYLPPYRSLLTPNARYDYKTHTLVPIKEHDLRALTSMNLGGKHTTTSKIKMKYKSLLSDVSKRTSILSLRIGSTANAKQTPIGVKSLPSEVLEYIFELVDSEEAYINCMLVCKQFYQVSKPFLYEDLSFTSTYRFAQFITYLRVNPEVGQYIKSVDLSQIKHGEPDDYEDENRELEQTHTSTSHGDSDTLNSVSRILAGWRDWKYKNNPLYSIQPYLNLTKVNSNSQTSSKSSKTTNSMKMLRLSKTLSYFKPKKRQKLNSSRNKNRAHPPLQTLNLGNRRNNSHPQINKFLMNYSASKDLPIGYILHLISLCPNIISLNLGNLSLSTDYEISRSMMYKFRTFDLMDNYPKETAATINGIMNHNNKSNEESLFGFNQEKNSFTSLSILNINDAKSQQLQQSRQNPTSSASSVYSVAFSKPIVKYNSLLPPLPPAIHDLSYMNKGDGKVYLSDLNLKSMNNNYLTKLSENEILHAIAKAHSSSDGPYGNRLKYINLSSMIWLTKTSAQRFLDQIVNKCLWEESYFSDAETVNSDSDSEIIGQDLVIDLRDSGMYKNLEWAKLIDLNQSEGRRLIKRIINDDVLNTFDEFMRRERLRRGRIGENYLN", "text": "FUNCTION: F-box protein probably involved in ubiquitin conjugation pathway."}
+{"protein": "MVTVREAKLEDIKDIAKVHVDSWRTTYHEIIPIDYLNSLNYKEFEDKWKSRSLKGVFVAQDEKGSVFGFASFGPIRSEQEGYDGELYAIYLLEERQRQGAGRALLAKGAEFLLQHGFSSMFVWVIEQNPSIIFYQAYSPERVAEDNFEIAGVRLKEVGLGWPDLSALKTLLNR", "text": "SIMILARITY: Belongs to the acetyltransferase family."}
+{"protein": "MTVLIHVLGSDIPHHNRTVLRFFNDALAATSEHAREFMVVGKDDGLSDSCPALSVQFFPGKKSLAEAVIAKAKANRQQRFFFHGQFNPTLWLALLSGGIKPSQFFWHIWGADLYELSSGLRYKLFYPLRRLAQKRVGCVFATRGDLSFFAKTHPKVRGELLYFPTRMDPSLNTMANDRQREGKMTILVGNSGDRSNDHIAALCAVHQQFGDTVKVVVPMGYPPNNEAYIEEVRQAGLELFSEENLQILSEKLEFDAYLALLRQCDLGYFIFARQQGIGTLCLLIQAGIPCVLNRENPFWQDMTEQHLPVLFTTDDLNEDIVREAQRQLASVDKNTIAFFSPNYLQGWQRALAIAAGEVA", "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": "MKERSTELVDGFRHSVPYINAHRGKTFVIMLGGEAIAHENFPSIINDIGLLHSLGIRLVVVYGARPQIDVALEEQKISPLYHKHTRITDSKTLEVVKQSAGTLQLDITARLSMSLSNTPLQGAHINVVSGNFVIAQPLGVDDGVDYCHSGKIRRIDEEAIHRQLDNHAIVLIGPVAVSVTGESFNLTSEEVATQLAIKLKAQKLIGFCSSQGVVDASGQIVSELLPNQAEERIQALQTTGDYHSGTVRFLRGAVTACRRGVERSHLLSYQADGAIVQELFSRDGIGTQIVMESAEKVRRANINDIGGILELIRPLEQQGILVRRSREQLEMEIDQFTIIERDNLTIACAALYPYQSEKIGEMACVAVHPDYRSSCRGEVLLQRISTQAKQMGLDKLFVLTTRSIHWFQEKGFTPAEIDKLPIEKQALYNYQRRSKILILDLHKE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily."}
+{"protein": "MAIDSKPHDDLQLFKTNLHPCGYWPDRWASDLVMDPNDPRLGAIYPQTLAWGFRRSGNLLYRPHCEHCNACVPVRVNVNAFVPNRSQRRCLARNATLVTRIVPAERNAEQLSLYRRYLHQRHPDGGMDGHGAIEFDQFLIGPWGYGRFMEIREPATNGTPGQLLAVAVTDLIHQALSAVYTFYEPNAAARGLGTLAILHQIHWAQREQRPYLYLGYWIKDHFKMDYKRRFQKLEIYDGYCWRPFSTTYPTTHTL", "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": "MAKFAPVQYKYIIKAEFEIDGIVDREDIIGAIFGQTEGLLGMELDLRELQKQGKLGRIEVEYKRVGNKTIGTITIPTSLKAVETSLIAAAIETVDRVGPAKARFRVKEIVDVRSSKREYIRNRAKELFVQLLSKTAPDIEELRRELEEAYYSKQLIEYGEEKLPAGPLVEKSDEIILVEGRADVVNLVKHGILNVLGMNGINIPKSVVELSKRKKVTLFIDGDRGGELVLRNLLAAGADIDYVAVAPPGREVEELTNKEILKALKSKIPLEQYIKNLRISINNDENKEKYKELLSKVFDTKKAIVFDEQFNIIDEKPLEEIDKLPSAYGIAIDKILDNETYAKIKGKYQLILALDSNVNAQERVITLKDIQ", "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": "MTRSLKKNPFVDNHLLGKIEKLNMREEKEIIVTWSRASTIIPTMIGHTIAIHNGKAHLPIYIIDRMVGHKLGEFAPTLTFRGHARNNNVSRR", "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": "MAVYNYDVVVLGSGPAGEGAAMNAAKAGRKVAMVDSRRQVGGNCTHLGTIPSKALRHSVRQIMQFNTNPMFRAIGEPRWFSFPDVLKSAEKVISKQVASRTGYYARNRVDLFFGTGSFADEQTVEVVCPNGVVEKLNAKHIIIATGSRPYRPADIDFHHPRVYDSDTILSLSHTPRKLIVYGAGVIGCEYASIFSGLGVLVELVDNRGQLLSFLDSEISQALSYHFSNNNITVRHNEDYERVEGLDNGVILHLKSGKKIKADALLWCNGRTGNTDKLGLENIGIKVNSRGQIEVDEAYRTSVPNIYGAGDVIGWPSLASAAHDQGRSAAGSIVDNGSWRFVNDVPTGIYTIPEISSIGKNEQELTQAKVPYEVGKAFFKSMARAQIAGEPQGMLKILFHRETLEILGVHCFGYQASEIVHIGQAVMNQPGELNNLKYFVNTTFNYPTMAEAYRVAAYDGLNRLF", "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": "MEIAIIALFIVSIALIAFSYSQRDPMKDVEQELETLQLSAMQEIYKLKKKMTVLEEELLETNLVIRKSKQNDINQKIAKQILSKYNNGMSAEAIAKAEHVSVEDVNTIIKDNEKVLV", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
+{"protein": "MSKKALLMILDGWGLGDQKKDDVIFNTPTPYWDYLMNNYPHSQLQASGENVGLPDGQMGNSEVGHLNIGAGRVVYQDLVKINRACADNSILQNPEIVSAFSYAKENGKSVHFMGLTSNGGVHSSMVHLFKLCDISKEYGIDNTFIHCFMDGRDTDPKSGKGFIEELSAHCEKSAGKIASIIGRYYAMDRDKRWERVKEAYDLLVNGQGKKATDMVQAMQESYDEGVTDEFIKPIVNANCDGTIKEGDVVIFFNYRNDRAKELTVVLTQQDMPEAGMHTIPGLQYYCMTPYDASFKGVHILFDKENVANTLGEYIASKGLNQLHIAETEKYAHVTFFFNGGRETPFDNEDRILVPSPKVATYDLKPEMSAYEVKDKLVDAINENKYDFIVVNFANGDMVGHTGIYEAIEKAVVAVDACVKDVIEAAKAQDYEAIIIADHGNADRALNEDGTPNTAHSLNPVPCVYVTGNKAAKVEDGRLADVAPTILKIMGLEAPADMNGQILIK", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family."}
+{"protein": "MASRNITVSEASRPALPRHAKLRFDETRQRWVILAPERVLAPDDIAVEILQLCDGARSVSAIIDQLATKYTADRAEIGTDVVAMLQDLADKGFLTEARESAP", "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": "MKSLVIVFVVLLGVAMISANEEELLAILQDQRNDARGGCVNKYKRNICGTLVTPMNCIAPRTRMGKFARRFCKFMCGFC", "text": "SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone 8 toxin family."}
+{"protein": "MKPPVRVAITGAAGHVSYSLIFRIAAGHMLGKDQPVILQLLEIPQAMDVLKGVVLELEDCAFPLLHGLVCSDDVHVAFKDADYAILVGARPRGPGMERSDLIQANGPIFTTQGEALSAEANPEVKVLVVGNPANTNALILLKNAPYINPRNITAMMRLDHNRALFQVAKKMGCHCSDVEKMVVWGNHSASQFPDISYAEIAGEKVAKGVENNWHGDNLIPIIQQRGAAVIKARGASSAASAASAAIDHMRNWVLGSGGKWVSMGVYSRGNSYGLDEDIMFSLPVICEDGDWREVAGLELSSFQRAMLEATEAELQAEREAVADII", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
+{"protein": "MPSPALLCCCLVLLAGVGASRHQSTLSEDDCTHFPASLPHMLRELRAAFGRVKTFFQMKDKLDNILLTGSLLEDFKGYLGCQALSEMIQFYLEEVMPRAENHDPDIKDHVNSLGEKLKTLRLRLRRCHRFLPCENKSKAVEQVKSAFSKLQEKGVYKAMSEFDIFINYIETYMTMRMKI", "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": "MVYRGFGLEHISPPVNKPFAEMTPEEQGERGAQMMMEFMTSCPGKSAISGVTGFALGGVFGLFMASMAYDTPLHTPAPVGAGPGAGIPGAPTLQQMADLPLKQQIKIQFADMGRRAYSSAKNFGYIGMIYSGVECTIESLRAKNDLYNGVAAGCLTGGGLAYKSGPSAALIGCAGFAAFSTAIDLYMRSENGRPPKNDFDE", "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": "MGVPSEGAVGNVNGNEVGTTASFAGYMETRGVREARVLASELCRHMYTLGWFSGTGGSITIKVHDDSIPKPRQLVVISPSGVQKERMVPEDMYVLSSDGFILSTPPLKPYPHKPPKCTDCTPLFMKVYEMRDAGAVIHSHGMESCIVTMILPFSKEFRITHMEMIKGIKGHGYHDELVVPIIENTAHEAELVESLTEAITAYPKTTAVLVRNHGVYVWGDSWISAKTQAECYHYLFDAAIKLHQLGLDWSTPTHGPIRSINGIWGCNGTMSRGLKVGGLSLDDMIEPSQRCILLDIEGTTTPISFVTDVLFPYAHANVGKHLAATFDSEETQDDINLLRSQIQHDLEHGVVGAVPIPPDYVGKELVIASFVANVEAMIRADRNITALKQLQGHIWKTGFQSNELVGVVFDDVPEALERWHASGIKVYIYSSGSREAQQLIFSNSNYGDLRKYFCGFFDTTMGNKKETHSYFEILRTVGIDRPSDMLFVTDVFQEAVAARAAGLEVVISIRPGNGPLPENHGFRTIETFLEI", "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": "MTRVRRGYIARRRRTKIRLFASTFRGAHSRLTRTTTQQKMRALVSTHRDRGRRKRDFRHLWITRINAVTRENRVSYSYSRLIHDLYKRQLLLNRKIPAQIAISNRNCLYTISNEIIK", "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": "ASYKVKLVTPEGTQEFECPDDVYILDHAEEEGIVLPYSCRAGSCSSCAGKVAAGEVNQSDGSFLDDDQIEEGWVLTCVAYAKSDVTIETHKEEELTA", "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": "MEHFDVAIIGLGPAGSALARKLAGKMQVIALDKKHQCGTEGFSKPCGGLLAPDAQRSFIRDGLTLPVDVIANPQIFSVKTVDVAASLTRNYQRSYININRHAFDLWMKSLIPASVEVYHDSLCRKIWREDDKWHVIFRADGWEQHISARYLVGADGANSMVRRHLYPDHQIRKYVAIQQWFAEKHPVPFYSCIFDNEITDCYSWSISKDGYFIFGGAYPMKDGQTRFTTLKEKMSAFQFQFGKAVKSEKCTVLFPSRWQDFVCGKDNAFLIGEAAGFISASSLEGISYALDSAEILRAVLLKQPEKSNAAYWRATRKLRLKLFGKIVKSRCLTAPALRKWIMRSGVAHIPQLKDYPTRFTSPTSRM", "text": "SIMILARITY: Belongs to the CbrA family."}
+{"protein": "MNAKIKAKTRSQMIDELSKMLNIEKKQTKAFMDTYEAFLILELSRAKEVRLGNIGKFKVSVRAERKGINPKTGETVIIPEKTIPKFTFTKGIKEIINAGISIDNERVSIDDNDFDDDDEFVEEYIVSENN", "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": "MADYLVRAIGAGGNVRAFAAVTTALTEEARRRHDTWPVATAALGRALTGTALLAATLKDPNESLTLRVAGDGPLRGILCDADEQGHVRGYVTEPHVDLEPAARGKLNVGAAVGTGMLYVTRQLALQGIYTGSSELVSGEIAEDLAYYLTRSEQTPSAVGLGVRVGPDGAVVAAGGYMVQLLPATPDADRDRLEENLGRLGSVSLAVEQGMTPEEILSVVLTGIDYQILERRDLSFPCRCSRERALGAIALLDETELSGLVEEGRGAELTCHFCNAVYRFSPEEVLQVQRGMKDKQ", "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": "MRLSRYFLPILKENPKEAEIVSHRLMLRSGMIRQQSAGIYSWLPIGLKVLNKVCTIIREEQNRAGANEILMPTIQSADLWRESGRYGAYGKEMLRIQDRQEREMLFGPTNEEMVTDIFRSYVRSYKDLPLNLYHIQWKFRDEVRPRFGVMRSREFLMKDAYSFDLDYEGAKMAYYRMFVSYLRTFARVGLQAIPMRADTGPIGGDLSHEFIILAETGESQVYCDRAYLDLAVPGADTDFRNDAQLTDIVTRWTTPYAATDEMHDEADWAKVKPESQVSARGIEVGHIFHFGTKYSEPMGAKVQGPDGKEHLVSMGSYGIGPSRLVAAAIEASHDDAGIIWPKAIAPFGAGIVNMKPGDEGCDGVSEKLYEALTNAGVDPLLDDKDERPGAKFATMDLIGLPTQVIVGPRGVAAGEVEVKDRKMGERQSLGIEAAINMLTAQA", "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": "MAALIYRQLLTNSYTVELSDEIQEIGSTKTQNVTVNPGPFAQTNYAPVNWGPGETNDSTTVEPVLDGPYQPTTFNPPVSYWMLLAPTNAGVVVEGTNNTNRWLATILIEPNVQQVERTYTLFGQQVQVTVSNDSQTKWKFVDLSKQTQDGNYSQHGSLLSTPKLYGVMKHGGKIYTYNGETPNANTGYYSTTNFDTVNMTAYCDFYIIPLAQEAKCTEYINNGLPPIQNTRNIVPVSIVSRNIVYTRAQPNQDIVVSKTSLWKEMQYNRDIVIRFKFANSIIKSGGLGYKWSEVSFKPANYQYTYTRDGEEVTAHTTCSVNGVNDFNYNGGSLPTDFVISKYEVIKENSFVYIDYWDDSQAFRNMVYVRSLAADLNSVMCTGGDYSFALPVGNYPVMTGGAVSLHSAGVTLSTQFTDFVSLNSLRFRFRLSVEEPPFSILRTRVSGLYGLPAAKPNNSQEYYEIAGRFSLISLVPLNDDYQTPIMNSVTVRQDLERQLGELRDEFNNLSQQIAMSQLIDLALLPLDMFSMFSGIKSTIDAAKSMATNVMKRFKKSSLANSVSTLTDSLSDAASSISRSASVRSVSSTASAWTEVSNIASDINVTTSSISTQTSTISRRLRLKEMATQTDGMNFDDISAAVLKTKIDKSTQLNTNTLPEIVTEASEKFIPNRAYRVIKDDEVLEASIDGKYFAYKVETFEEIPFDVQKFADLVTDSPVISAIIDFKTLKNLNDNYGISRQQALNLLRSDPRVLREFINQDNPIIRNRIESLIMQCRL", "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": "MEKYAFRMRLHPGKAAEYQARHDAIWPELVTLLKDAGVSDYSIHLDEENCLLFGVLWRSDDHRMGDLPSHPVMRKWWAHMADIMETRADNEPVAVPLKTVFHLK", "text": "FUNCTION: Involved in the anomeric conversion of L-rhamnose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose mutarotase family."}
+{"protein": "MKDVYLYIVEKSVAWEFDSPEYGRLARKVAEMLYERKEDLTDDRIAILLNISTAETRRILQYLMRLNLVGVKKRTTEDYRIEYTWYVDDEIIKQAIGGRARTAREKISMLIRALTEGSYYICPNCHMRYSLDEAVNKGGVCPVCGAELEYVESLEEINKLTKVLQKLEKL", "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": "MLERLKKSLLEAPVFKRGEYDYFIHPITDGVPEIRPDLIREVTANIVRIANLDVDKIVTVEAMGIPIGIVLSILCDIPLVIIRKRKYGLPNEVEISQVTGYSRSQLYLNGINRGDRVIVVDDVISTGGTLQATLDSMELAGAEVMDTVIVVERGNGAELLRSKGYNLKTMVRVKVEGGRVSEVEPGISK", "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": "MARLNVNPTRMELTRLKKRLTTATRGHKLLKDKQDELMRRFIDLVKYNNELRKDVEEMIKNSLKDFVMARALMSSEILEEAIMYPKEKISLDVNIKNIMSVNVPEMKFKRLLEDDNGSIYPYGYSNTSAELDDAIEKLYSILPKLLELAEVEKSTQLMADEIEKTRRRVNALEYMTIPQLEETIKYIQMKLEENERGALTRLMKVKTMLEKEQESV", "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": "MSHILDKIDTVYPFPPKPIPLTQDEKAAYIASIKQLLKEKDAVLIAHYYTDPEIQALAEETGGFVGDSLEMAKFGNRHPAGTLIIAGVRFMGESAKILTPEKRILMPTLEAECSLDLGCPADKFTEFCDAHPDHTVVVYANTSAAVKARADWVVTSSIALEIVEHLDAEDKPIIWGPDRHLGSYIANKTGADMLLWQGECVVHDEFSADALRKMKAVYPDAAILVHPESPASVVELADAVGSTSQLIKAAKELPQQKMIVATDKGIFFKMQQLVPEKELIEAPTAGAGATCRSCAHCPWMAMNGLKAIETALREGGEQHEIFVDEALRVKSLIPLNRMLDFAEKLNMQVKGNV", "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": "MTDHLIAKVQEHVPNIPLKIISQGAEALVFETSVHPYYNYNSSEKHHESPSLHNHTTFIIKYRPTKPYRHPKIDLQINKSRTIGEVKFMYKLSKLNIACPNIISTDFNNGIIWMECLGSKLPNGTISSFKNWLWYLESQEKEDPSINLHDDDQVELVCQKVGQLIGRLHLNDMIHGDLTSSNIILTEVDTKKNEDTDANNSSVYFEPALIDFGLSSFSGLAEDKAVDLYVLERAILSTHSNYADKLNGWLLEGYQQIHDSIEFNKTKQQLGKSKLKDTIKRLEDVRLRGRKRSMLG", "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": "MLILTRRVGETLIIGDEITVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKKK", "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": "MDYEFLRDVTGVVKVRMSMGHEVIGHWFNEEVKENLALLDEVEDAARTLKGSERSWQRAGHEYTLWMDGEEVMVRANQLEFAGDEMEEGMNYYDEESLSLCGVEDFLQVVAAYRNFVQQK", "text": "SIMILARITY: Belongs to the UPF0231 family."}
+{"protein": "MERINTTFYKTKVIPQLQQKYSYSNVHQIPKLRSIHLNRCLGAVSQKIFQKSSEEIAMISGQRPKITYAKKAIAGFQIRKGMPIGMTVTLRRERMYDFLTKFIHLILPRLKDFRGLNPTSFDGNGNYHMGLPDQLAFPEIDYDQIDQYRGMDISIITTAKTDEEAKFLLEALGMRFQ", "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": "MAIQKKHGKGRLDKWYKLAKEKGYRARAAFKLIQLNKKYGFLEKSKVLLDLCAAPGSWCQVAAEVMPVSSLIVGVDLAPIKPIPKVITFQSDITTEKCRATIRQHLKTWKADTVLHDGAPNVGTAWVQDSFNQAELTLQAMKLATEFLVEGGTFVTKVFRSKDYNSMLWVFNQLFKKVEATKPPSSRNVSAEIFVVCRGFKAPKRIDPKFLDPRAVFAELADPTPNNEAKVYKPEIKKRKRDGYEEGDYTQYKELPAYEFIQSTDPIAILGSTNRLSLEQSKNGDVALAVLEKLPETTDEIRTCCADLKVLGRKEFKLLLKWRLAVREKLGFPTKKSVKKEEEAAAAVAAAEEVAKIESMDEEMRIQHELEKLKERNSTKKKRERRKENERKQKDIVRMQMHMVAPMDIGVEQAGPEGEDAMFALRAVEKGDVMRRLAKGKMVVASEADAKKDRDSGIGSSGETDDESDEELDRLETELDDMYDQFRERKAASDAKYRAKKARQARNGDGDEEWEGVSDNEKADEISDDSELEEESSGDSDDEDDTAPRKSLLTDLDTTPSDNSGLSKRARAFFNQDIFKELDGDMDEPMDEELRAALAGEDEDADMEDTVSKADSKKTKEKTADKKAAKKAKKAAQKAQQVKDDDSDDESDGGFEVVKSGKEDDWEDEDKRTKDGRLDIDIITAEAMTLAHQLATGQKSSHDVIDDGFNKHAFKDREGLPEWFLDDETKHDKPQKPITKAAAAAIKEKMRAFNARPIKKVREAKGRKKMKAAQRLEKLKKKSDLLVNEEGMTEKEKAESIAKLLRKATKKKPKQAVKVVVAKGANRGIKGRPQGIKGRYKIVDPRMKKEMRALKRVAQKAKKRR", "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": "MMHRGYGGDRRGFRPSFRSDRNSRYAPRTRREPQRYDPMPELAPVEFQKNFYQEAESISRMTPSEVSSFRKTNEMIVKGTNVPHPIQKFEEAGFSSEVVSSLVEKGFSEPTAIQGQGWPMALSGRDMVGIAQTGSGKTLSFILPALVHAKDQQPLRRGDGPIVLVLAPTRELVMQIKKVVDEFCGMFNLRSTAVYGGASSQPQIRALHEGAEVVIATPGRLIDLHDQGHAPLSRVTFLVLDEADRMLDMGFEPQLRKIIPKTNANRQTLMWSATWPREVRGLAESYMNEYIQVVVGNEELKTNSKIKQIVEVCSGREKEDKLIGVLDNFKGDKVIVFCNMKRTCDDLEYVLNRSGYGAAALHGDKSQNIRDKVLDDFRSGRRPILIATEVAGRGLDVNDVKLVINFDFPGSCEDYVHRIGRTARGNTKEGISHTFFTVGDKANARELIRMLREANQTVPSDLEDMVRVSNDRYGSRSTRHGYDYRGRAGRFPYRG", "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": "QLGLQDPPHMVADLSKKQGPWVEEEEAAYGWMDF", "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": "MITVLSGGTGTPKLLRGLHALVPDEEITVVVNTAEDLWISGNHLSPDVDTVIYLYAGLLNTDTWWGIRGDTFLTHEALVPLSANEFIAIGDQDRAVHIARGEMLRNGSTLTEATRHLCRSFGVKARVLPMSDAPVGTMVATENGLIHFQEYWIRHHGQVPITSVVRQPERFEASQAVLEALMECDAVIVGPSNPVTSIGPILECIWVPDLLREKPVIAVSPFIGDAPISGPAAALMKASGVEPSSLGTFGLYRDFVDIFVQDIRDPVAVPGAVRCDTLMKDQEKSTALAAEVLSLMKSLA", "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": "MKISCLICLVIVLTIIHLSQANDYCKIKCSSGVHTVCQYGESTKPSKNCAGKLIKSVGPTEEEKKLIVEEHNRFRQKVAKGLETRGNPGPQPAASNMNNLVWNDELAKIAQVWASQCQILVHDKCRNTEKYQVGQNIAYAGSSNHFPSVTKLIQLWENEVKDFNYNTGITNKNFGKVGHYTQMVWGNTKEVGCGSLKYVEKNMQIHYLICNYGPAGNYLGQPIYTKK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family. Venom allergen 5-like subfamily."}
+{"protein": "MGTTKVTPYLIFATSVAAIGSFQFGYNTGVINAPEMIIRDFLNYTLDEKLDEPPSRLLLTNLWSLSVAIFSVGGMIGSFSVGLFNRFGRRNSMLIVNLLAVIGGCLMGFCKISESVEMLILGRLVIGVFCGLCTGFVPMYIGEISPTALRGAFGTLNQLGIVIGILVAQIFGLEIILGSEVLWPVLLGFTIIPAILQSAALPFCPESPRFLLINKKEEDEAKQILQRLWGTQDVAQDIQEMKEESARMAQEKQVTVLELFRAPSYRQPIIISIVLQLSQQLSGINAVFYYSTGIFKDAGVKEPIYATIGAGVVNTIFTIVSVFLVERAGRRTLHLIGLGGMALCSVLMTVSLLLKDKYDTMSLVCIAAILIYVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGCSNWTSNFLVGLLFPSAAYYLGAYVFVIFAVFLVAFFIFTFFKVPETRGRTFEDITRAFEGQAAEANKLGKGPTMEMNSIQPIETTTHV", "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": "MPREIKEIKEFLIKARRKDAKSVKIKKNPTNVKFKVRCSRFLYTLVITDKEKAEKLKQSLPPGLQVKEIKCRKSKTTP", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL38 family."}
+{"protein": "MAVVSVEELVVDPPTAARRLLGATLRSGQVAVRLVEVEAYGGDAEGPWPDPASHSGRGRTKRNAVMFGPAGYLYVYLSYGMHTCVNVTTGPDGTAGAVLLRAGEVVDGLDVVRGRRPTARTDADLARGPGNFGTALGIALDDYGTALFDPAAPIRLELADPLPAALIADGPRVGVSSEADRPWRFWLPSSPAVSAYRRSPRAPGAATVRAPR", "text": "SIMILARITY: Belongs to the DNA glycosylase MPG family."}
+{"protein": "MNWESEWFRIELIRGSRRISNFFWAFILLSGALGFLSVGLSSYFGKDLISFLSYEQIVFIPQGIVMCFYGIAGSAFSLYLWGTIFWNIGSGYNKFDKGKGIVCIYRWGFPGKNRRIRIEFSMKDIEAIGMEVQEGFYPRRTLRLKIKGQQDVPLTYIGENLTLREIEEEAAELARFLQISIEGF", "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": "MRLHHLLLALLFLVLSAGSGFTQGVRNFVTCRINRGFCVPIRCPGHRRQIGTCLGPRIKCCR", "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": "MQTYGNPDPTYGWWVGNSVVTNKSSRFIGSHVAHTGLIAFTAGANTLWELARFNPDIPMGHQGMVSIPHLASLGIGFDQAGAWTGQDVAFVGIFHLICSFVYALAGLLHSVIFSEDTQNSSGLFADGRPEHRQAARFKLEWDNPDNQTFILGHHLVFFGVANIWFVEWARVHGIYDPAIEAIRQVNYNLDLTQIWNHQFDFIQIDSLEDVMGGHAFLAFFQIGGGAFHIATKQIGTYTNFKGAGLLSAEAVLSWSLAGIGWMAIIAAFWCATNTTVYPEAWYGETLQLKFGISPYWIDTGNMDGVVTGHTSRAWLSNVHYYLGFFFIQGHLWHAIRAMGFDFRKVTSAVANLDNSRITLSD", "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": "MVRQLALACGLLAAVAVQAAPAEPAHPMVTEAPDASLLHKRATTCTFSGSEGASKVSKSKTACSTIYLSALAVPSGTTLDLKDLNDGTHVIFEGETTFGYEEWEGPLVSVSGTDITVEGASGAVLNGDGSRWWDGEGGNGGKTKPKFFAAHDLTSSTIKSIYIENSPVQVFSIDGATDLTLTDITIDNTDGDTDDLAANTDGFDIGESTDITITGAKVYNQDDCVAINSGENIYFSASVCSGGHGLSIGSVGGRDDNTVKNVTFYDVNVLKSQQAIRIKAIYGDTGSISDITYHEIAFSDATDYGIVIEQNYDDTSKTPTTGVPITDFTLENVIGTCADDDCTEVYIACGSGACSDWSWSSVSVTGGKVSSKCLNVPSGISCDL", "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": "MIHETAQIHPTSVVEEGAIIGANVKIGPFCFVDSKVEIGEGTELLSHVVVKGPTKIGRFNRIFQFASIGEACQDLKYAGEDTQLIIGDRNTIRESVTMHRGTVQDKGITIVGSDNLFMINAHVAHDCVIGDRCIFANNATLAGHVKVGNQAIVGGMSAIHQFCHIGDHCMLGGGSIVVQDVPPYVMAQGNHCAPFGINVEGLKRRGFDKAEIHAIRRAYKSLYRNGLTLEAAKAEIAQEAEQYPSVKLFLDFLEKSERGIIR", "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": "MSHTVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKASQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGSETTRSMGLAY", "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": "MNQAFLPFSRPSIGEEEIAAVEQVLRSGWITTGPKNQELEQQFAERVGARHAVALSSATGAMHITLLALGIGPGDEVITPSQTWVSTANMICLLGATPVFVDVDPDTLMSDAATIEAAITPRTKAIIPVHYAGAAFDLDPLYALADKHGIAVIEDAAHAAGTTYRGRAIGARGTAIFSFHAIKNMTCAEGAMFVSDDEALANRVRMLKFHGLGVDAYDRLTHGRKPQAQVIEPGFKYNLADMNAAIALVQLQRLDEINAKREVLAKAYLQRLEGLPVQPLLLPQYPQQHAWHLFILRIDAERCGLDREAFMKGLQEQNIGTGIHFIATHLHTYYRQRFPEVQLPHTEWNSARLCSIPLFPDMTLDDVERVTGAIANLLD", "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": "MENKYTHGVLFYHEHSGLKNINQGIGEVTTALSSICKHLSIQLSENEGDIIKYCQEIKTKNYAKDVDILFILGGDGTVNELINGVMTHDLQLPIGILPGGTFNDFTKTLNIAPNHKQASEQMISAQVGTYDVIKINNQYALNFVGLGLIVQNAENVQDGSKDIFGKLSYIGSTVKTLLNPTQFNYQLSIDDKTYSGETTMILTANGPFIGGSRIPLTDLSPQDGELNTFIFNEQSFSILNDIFKKRDSMNWNEITQGIEHIPGKKISLTTDPAMKVDIDGEISLETPIDIEVIPNAIQLLTVNDL", "text": "FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids other than diacylglycerol (DAG). SIMILARITY: Belongs to the diacylglycerol/lipid kinase family."}
+{"protein": "MSSIIHGAGAATTTLSTFNSVDSKKLFVAPSRTNLSVRSQRYIVAGSDASKKSFGSGLRVRHSQKLIPNAVATKEADTSASTGHELLLFEALQEGLEEEMDRDPHVCVMGEDVGHYGGSYKVTKGLADKFGDLRVLDTPICENAFTGMGIGAAMTGLRPVIEGMNMGFLLLAFNQISNNCGMLHYTSGGQFTIPVVIRGPGGVGRQLGAEHSQRLESYFQSIPGIQMVACSTPYNAKGLMKAAIRSENPVILFEHVLLYNLKEKIPDEDYVCNLEEAEMVRPGEHITILTYSRMRYHVMQAAKTLVNKGYDPEVIDIRSLKPFDLHTIGNSVKKTHRVLIVEECMRTGGIGASLTAAINENFHDYLDAPVMCLSSQDVPTPYAGTLEEWTVVQPAQIVTAVEQLCQ", "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": "MLEKVKNIIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDEGWVPVYTDESQTLAVMSIGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEVGCHGAIIVTTPQEVALDDVRKEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGASLANYAQVPHLGTLPIDPRVGVLAGSTTSVLDELPDSTTAEVLTHIVEKLKTIFVS", "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": "MPSGVRRRKMNRSSITKVTRKDKDNHKRIVVTGSDIIRQRWDKNLSMAQNYKKLGLATKTGSRKIRGLEEDLREKSLRLTIQQGKNPHDQELRDLMEQQEQEELEKSNLVVNERKIPKLGAGEAFIVRDDKGEVVEVIYGKDHQTGSDEEDEEEWTGFEDKPEEEETETIKILQERAKRAASNPHVQSDREQSWIEQLINKHGDDIDGMFWDKELNIYQQSRGDLKRRIKKWKQGNKRNQ", "text": "FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NOP16 family."}
+{"protein": "MDIEAEPSLRSIVNHESLKWIFVGGKGGVGKTTTSSSISIQLALHNPNKKYLLISTDPAHNLSDAFNQKFGKDARQVEGLPNLSCMEIDPDSTLENLQKNNESTFGSAGGNDPLKSMMGDITGSIPGIDEAFSFMEVLKHIGETKENQIKYDTVIFDTAPTGHTLRFLQLPSTLEKLLGKVNELSGRFGPMLNNLLGSQGGQSIDFASKIKEIQVQVTEVNKQFQDPELTTFVCVCISEFLSLYETERLIQELMSYNMDVNSIVINQLLFSDDSECRRCNARWRMQKKYLDQMDELYEDYHLVKMPLLAMEVRGLENLKKFSKYLIEPYNSETDGHVVFDLEEQ", "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": "SDPKIGNGCFGFPIDRIGSVSGLGCNRLVQNPPKPISGES", "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": "MEQAPEDQGPQREPYNEWALELLEELKQEAVRHFPRPWLHNLGQYIYETYGDTWSGVEALIRTLQQLMFIHFRIGCQHSRIGILRQRRARNGASRS", "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": "MDSLARQSAKICPFVSRVTSSMQQVQVLHKTNMSAMAQQCPVMRRAMAARGYVTASPPAGAAAADVGEARPITPVLERGTQERTFDYDGLFETELQKKRLDSSYRFFNNINRLAKEYPMAHRLEEEDKVTVWCSNDYLTYSRNEKVMETMKRTIDKYGAGAGGTRNIAGHNRHAMRLEAELAALHKKEGALVFSSCFVANDAVLSLLGQKMPNMVIFSDEMNHASMIMGIKHANVQKHIFRHNDLQHLEELLAMYPKSQPKLIAFESVYSMSGSVADIRKICDLAEKYGALTFLDEVHSVGLYGPHGAGVAEHLDFEAHRKAGLASPAQTTVLDRVDMITATLGKSFGSVGGYLAASEKLVDFVRSYAPGFIFTSSLPPAVMAGSAAAVFDQRSSLHLRQLQQKHTSYVKTGLGDLGIPVQPNPSHIVPVLVGNPDLAKRASDILMEKHRIYVQAINFPTVPRGTERLRITPTPGHTNDLSDVLLDAMDDVWKTLQLPRVSDWAAHGGLLGVGEPDYVPEANLWTEEQMSLTNDDLHPSVFSPVEKFLEVSSGIKA", "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": "MLSNAQRALIKATVPLLETGGEALITHFYRTMLGEYPEVRPLFNQAHQASGDQPRALANGVLMYARHIDQLQELGPLVAKVVNKHVSLQVLPEHYPIVGTCLLRAIREVLGEQIATDEVLEAWGAAYQQLADLLIEAEESVYAASAQADGGWRGVRRFRVARKQAESEEITSFYLEPVDGQPLLAFQPGQYIGLRLDIDGEEVRRNYSLSAASNGREYRISVKREAGGRVSNYLHDRVAEGDELDLFPPAGDFVLRDSDKPLVLITAGVGITPALAMLQEALPQARPIRFIHCARHGGVHAFRDWIEDVSAQHEQVEHFFCYSEPRAGDSADAEGLLSREKLADWLPQERDLDAYFLGPRPFMAQVKRHLADLGVPSQQCHYEFFGPAAALDA", "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": "MFAELAPYLSNPRQTLAQLLNFALVLSTAFMGWKALSVYTNSSSPIVVVLSGSMEPAFQRGDLLFLWNNSPRAEVGEIVVYNVQGKDIPIVHRVIKAFGTGDGGKKSQRRLEREADKRSGPGLSSPVSHQMLTKGDNNIADDTELYAQGQDYLDRKLDIVGSVRGYIPAVGYVTIMLAENPWMKTVLLGIMGVMVMLQRE", "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": "MIKNRCLDIDLETKEKVLIVDDEASIRKILETRLSMIGYFVVTASDGEEALNLFHQEMPDVVILDIMMPKLDGYGVCQEIRKDSDVPIIMLTALGDVADRITGLELGADDYVVKPFSPKELEARIRAVLRRTNKAAFSSHLTTSGIINFNFLTIDLNKRQIYKDNERIRLTGMEFSLLELLISRSGQPFSRADILQEVWGYTPERHVDTRVVDVHISRLRAKLETDPSNPDLILTARGTGYLFQRITDQHVLKT", "text": "FUNCTION: Probable promoter-specific protein mediating the interaction between DNA and RNA polymerase. SUBCELLULAR LOCATION: Plastid, chloroplast."}
+{"protein": "MNVFEPRLSSWLENAGDDDDVVLSSRIRLARNLKDEQFPVYEQKEEIVDNIAEVFDDNFTLIKMNQISLLQKALLVEKHLISPYMMNKSEYGAVLLNEEENVSIMLNEEDHLRIQCMTPGLRLFDALEAALQIDGYVEEKLSYAFDKEFGYLTSCVTNIGTGMRASVMVHLPGLVTTKRIKSVIEAIRSLGFVVRGIYGEGSMPASNIFQVSNQVTLGKTETEIVEDLTQVMEQIIMQERVARTTLKQKFHIALEDRVFRSYGLLMNCRIISMKEASDAISDIRLGVELGFFEHISRQKMNELVLFSQPAFLRREAGRDMDELEEKVIRAKVIREILGDK", "text": "FUNCTION: Catalyzes the specific phosphorylation of arginine residues in proteins. SIMILARITY: Belongs to the ATP:guanido phosphotransferase family."}
+{"protein": "MTVHKSRIRRSRSLSVTHRIQKRPDHREKTKLYLQLKLHDLHTVFNLFPEYEQKFLAIIKLPITGKEPIDVPFSLSNHHQHTCLEFSPYANEQISKSACLHCESVSVPTSSDAMVAHLNQVNNVMQNRLYFYGFRKDMELIRMSAKQPTIFQIFYIVHNTINNIFPIMFERKQKLGMHIVFQSRTLHIPCECIKQIVAVSSGYNVYLDILQESVILTVLCETLDTNTNIHIDIGMLQKKLEEMDIPNEISDRLEKYKGHLIGFH", "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": "MLRNLLALRQIAKRTISTSSRRQFENKVPEKQKLFQEDNGIPVHLKGGIADALLYRATLILTVGGTAYAMYELAVASFPKKQD", "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": "MRAKWRKKRVRRLKRKRRKTRARSK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL41 family."}
+{"protein": "MNPTQSDELRDEPRGAIELPVSRTRGGAVDTAHDFVGQEWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVILHADAPLPHAEVHLDVVQQAFAALKDRRRALAGRTGCGVCGIESIDLLDLAPERVPDTGFLARLAPDALARAAHALPAHQALTKLTGGLHAAAWCDATGAIRAAFEDVGRHNALDKLIGSLVLSRADTTDGFVFLSSRASYELVRKAARVGIPLVATISAPSSLAIEIAKAAGLRLVSFCRETGHVDYGTV", "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": "MYKVVVIIALLGAVRGLDKICLGHHAVANGTIVKTLTNVQEEVTNATETVESTSLNRLCMKGRSYKDLGNCHPIGMLIGTPACDLHLTGTWDTLIERKNAIAYCYPGTTINEGALRQKIMESGGISKTSTGFAYGSSINSAGTTKACMRNGGDSFYAEVKWLVSKDKGQNFPQTTNTYRNTDTAEHLIIWGIHHPSSTQEKNDLYGTQSLSISVGSSTYQNNFVPVVRARPQVNGQSGRIDFHWTLVQPGDNITFSHNGGRIAPSRVSKLVGRGLGIQSEASIDNGCESKCFWRGGSINTKLPFQNLSPRTVGQCPKYVNKKSLMLATGMRNVPEIMQGRGLFGAIAGFIENGWEGMVDGWYGFRHQNAQGTGQAADYKSTQAAIDQITGKLNRLIEKTNTEFESIESEFSEIEHQIGNVINWTKDSITDIWTYQAELLVAMENQHTIDMADSEMLNLYERVRKQLRQNAEEDGKGCFEIYHTCDDSCMESIRNNTYDHSQYREEALLNRLNINSVKLSSGYKDIILWFSFGASCFVLLAAVMGLVFFCLKNGNMQCTICI", "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": "MTGHAPLVGVIGGSGLYKLEGIEPVESLNIDTPWGRPSSPITLFKLPSGPVVAFLARHGVSHQFTPSEVPSRANIAALKKIGCQVIIAFSAVGSLREEIKPRDIVVPSQIIDRTKSAHAMFGEPFDTELTGLVTKSIKEAVTGFEMNDRIGVHAEKVAICMEGPAFSTRAESNMYRMFGGDIINMSVLPEAKLAREAELSYALIAQITDYDAWRESEEPVTVAEVMATIAANVSVSNRLTLTILDEVHNAVAKGQLKTCKGTMEYSVMTKKEMISEESKKTLSFILPYFS", "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": "MSYVIDRRLNGKNKSTVNRQRFLRRYRDHIKKAVEEAVSRRSITDMEHGEQISIPGRDIDEPVLHHGRGGKQTVVHPGNKEFTAGEHIARPPGGGGGRGPGKAGNSGEGMDEFVFQITQEEFLEFMFEDLELPNLVKRNLTGTDTFKTVRAGISNEGNPSRINIIRTLRSAHARRIALSGSSRAKLREVKEELARLKREEPDNFGDIQDLEAEIERLSARIHRVPFLDTFDLKYNLLVKQPNPSSKAVMFCLMDVSGSMTQATKDIAKRFFILLYLFLKRNYDKIDVVFIRHHTSAREVDEEEFFYSRETGGTIVSSALKLMQEIMAERYPSNEWNIYAAQASDGDNWNDDSPICRDILINQIMPFVQYYTYVEITPREHQALWYEYERIAEAFSDTFAQQQLVSAGDIYPVFRELFQRRLVT", "text": "SIMILARITY: Belongs to the UPF0229 family."}
+{"protein": "MIIMDVSVQRRMAAEILKCGIERVWIDPTQLDRVKMAMSKDDIRALIKEGVIKKKQKKGISSARVKKLKEQRKKGRRRGPGSRRGAAGARTPPKERWMATIRALRKTLKQLRDSGKIDRKVYRKLYRMAKGGAFRSRSHLFLYMREHELLK", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family."}
+{"protein": "MASNGHFSSVGDVDGGNYQHGVQVVDGDKEFNPNLSKYLAHENVTPAGFNYHLISVFGSQSTGKSTLLNTLFKTDFSVMSETERRQTTKGIWLSKNKRTASNEKEKMADNVLVMDVEGTDGRERGEDQDFERKSALFALATSEVLIVNIWEHQVGLYQGANMGLLKTVFEVNLQLFLKDTKSTPRSLLFFVIRDFVGTTPLENLRNTLMQDLQRIWMSLSKPEGTENSTIEDYFDFEFAGLPHKSFQPEKFASEVDKLSTRFRDGHRDPSSTSAKGTAVEGGVFLPEYHRRIPADGFAVYAEGIWDQIVNNKDLDLPTQQELLAQFRCDEIAREVLILFDETIGPFEVQQAEGVRSGIPLILGSLGVAMRAARGKTMTSFETEASRYHKRVFMTKKSELEEKIDTRLKALFSGQLSAAHKSGVTQFSEAVSAAVKAGQKKGASYDFAEIVTRERKLAIEKFENEASTTMVEGAPWSDYKQELSLFQKDLEKISSQLRKDEMRRLATRVERWVRSRLGDSIDLEFNALGSGRGGSRAPENGDKPSEKTIWDRIWSLFVNTVLDAERRFTERARSFDASLEEVDVGLWRLRRKSWGVLRSKIEEEMMEGNILHKLRENFEDKFRYDDVGVPRIWRPTDDIEGIYTTARESTLSLIPLLARFRLNETSAPPPLDKWVGHMPSSASAADEEDLAPIGGVDEDDGKSLEEEMTMLSEAKRQDLTVRFKKAADGVYVEAKRSAIGGITQVPLYFYGLLLALGWNEIIAVLRNPIYFIFLLLIGVGAYVTFRLNLWGPMINMAEAASRQAVEEGKRRLREFLESSDSGRQAMAMSGRNARGTEEYEMSSNLKSKGRRTDTSDDDNDDDL", "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": "MKKENKSVIIWLLSGCVLLFLMVVVGGITRLTNSGLSMTDWHLVTDTFPPLTDAKWQAAFDEYKKFPEYQKINIHNDFQLSDYKFIYFWEWFHRFIGRIIGLVFFVPFVYFLAKKKLDTSTIKKCIVLLAMGAFQGFLGWFMVRSGLIDNPDVSHFRLSLHLTFAFITFAYTLWVALDLIYPERNINKILPLRNIARYALAALLIQIIYGGFVAGLNAGLIHNHWPLMSDGEFIHESVFIEQSSLIKNLIEGKSGVQFVHRTFAYAVVAVILFLFFKSKKYTLTRTQSNGINTLVVFVFIQFLLGVFTLLYSVPLALGLIHQIMAFFLLSAMTYTLHRLSK", "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": "MAFALLRPVGAHVLYSDVRLLSEDEENRSESDASDQSFGCCEGLETTRRGPGPGGGRRASSGAGPVVVVRQRQAANARERDRTQSVNTAFTALRTLIPTEPVDRKLSKIETLRLASSYIAHLANVLMLGDAADDGQPCFRAAGGGKSAVPAADGRQPRSICTFCLSNQRKGGSRRDLGGSCLKVRGVAPLRGPRR", "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": "MDSPSTTASGWIDEHHQGVRYGLQGRVLVDEKSPYQRITVIDSSRYGKGLLLDGCWMTAEHQERHYHESLVHPALCSAAQLERVLVIGGGDGGTARECLRYQDVKHLDMVEIDGRVVELSQKHLPSIGGHAWSDARLQLNLEDGIAWTANATDSSYDVILVDGSDPTGPAEGLFNEAFFKQCRRILRPGGVFATQSESPEAFRQIHIDTVRLIRQVFGYADPLYGWVPMYPSGWWSWTFAAVDGPRYRNPLPARAAAISSGCEIWSPRWQQGAFEAIPAFIERELT", "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": "MSAFKPLVFSGVQPTGNLHLGNYLGAIKKFVALQETSDCIYCVVDLHSLTAQLVHEDLADQTRSITAAFLASGIDPKKHIVFNQSRVMQHAELAWIFNCVARIGWMNKMTQFKDKAGKDRENASLGLLAYPSLMAADILLYRATHVPVGEDQKQHLELTRDIAQKFNNDFSDRIARLGVGVEMQVGEETVNGFFPITEPVIGGPAARIMSLRDGSKKMSKSDPSDLSRINLTDDADTISKKIRKAKTDPEALPSEVSGLESRPEAENLVGIYAGLAEMSKADVLKEFGGQQFSVFKPALADLAVEKLAPIAGEMRRIEGDRAYVDAVLRDGGERAGVLAETTMKTVRDIIGLLQG", "text": "FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
+{"protein": "MNTHFTYVLQCADQTLYCGYTTDLEKRLATHNSGKGAKYTKTRLPVKLLASVNFDNKNDAMSCEWWFKHKLVRQQKLKLIKNNLIKEKFLEYLLAKQK", "text": "SIMILARITY: Belongs to the UPF0213 family."}
+{"protein": "MIRLRRVLFLLTSVLVLTACQPPGLVVDAPQPKAEAETLRVGTLYGAQIYMSSGQGLSGFDYELAQKFADYLGKPLEMQPYSNRSELYDALAKGEIDLIAAGITESPNRRNRFRMGPPLYRVDQVVVYRQGNRAPESIEQLSGNLTVVADSAFVETLTRLQQTHTNLSWEQTSEKDNDELIAMIASGELNYTLAQSTSLDINRRYMPELRSGLVLEEKVPVVWLLPAQNSDALMSKLLAFWHQEKRAGTLAHLNEKYFGHVKRFDYVDTRAFIRAIDAKLPRYRPLFEEYAGDLDWRKLAAASYQESHWNPNARSPTGVRGMMMLTNATASQLGVTNRLDPRQSIRGGADYLRDLINRLPESIPENQRMWFALAAYNIGLGHLEDARRLAEAQGLNPSAWRDVKQVLPLLQKRKFYSQTRYGYARGGEAVHYVDSIRRYYDTLVWVDNQKPKDEPQLPDEIQVEETAASSGAEPPTAAPRE", "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": "MVPCTLLLLLAAALAPTQTRAGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPSTVSNMATVAVLVVLGAAIVTGAVVAFVMKMRRRNTGGKGGDYALAPGSQTSDLSLPDCKVMVHDPHSLA", "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": "MRRNPHFSLLKPQYLFSEISKKLAQFRKENPEISVIDLSIGDTTQPLCRSITQAIKEFCVSQEKQETYRGYGPETGLEKLRTKIASEVYENRISPEEIFISDGAKPDIFRLFSFFGSEKTLGLQDPVYPAYRDIAHITGIRDIIPLACRKETGFIPELPNQQSLDILCLCYPNNPTGTVLTFQQLQALVNYANQHGTVLIFDAAYSAFVSDPSLPKSIFEIPEAKYCAIEINSFSKSLGFTGMRLAWNVIPKELTYDNNEPMINDWKRLFATTFNGASLLMQEAGYYGLDLFPTPPAISLYLTNAQKLKKSLETAGFSVHGGDHAPYLWVELPEGISDEEAFDFFLHQYHIAVTPGHGFGSCGQGFVRFSALTQPQNIALACDRLCTASLKETMVLA", "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": "MAMTAEVKDELSRLVVTHVSCRKAEVSSLLRFAGGLHIVGGRVVVEAEVDLGSTARRLRREIFDLFTYSADVHVLSAGGLRKSSRYIVRVAKEGEALARQTGLLDLRGRPVRGLPAQVVGGSVADAEAAWRGAFLAHGSLTEPGRSSALEVSCPGPEAALALVGAARRLGISAKAREVRGTDRVVIRDGEAIGALLTRMGAQDTRLVWEERRMRREVRATANRLANFDDANLRRSARAAVAAAARVERALDILGDEVPDHLAAAGHLRVEHRQASLEELGQLADPPMTKDAVAGRIRRLLSMADRKAKETGIPDTESAVTADLLDDA", "text": "FUNCTION: Involved in cell division and chromosome segregation. SIMILARITY: Belongs to the WhiA family."}
+{"protein": "MMEKFEKIEMKIPAKAEYVAIIRLTMAGVANRMGFAYDDMEDMKIAISEACTNIVQHAYKEDVGEITIVFGLYEDRLEIMVADNGVSFNFSTLKSKVGPYDINKPVEHLPENGLGLYLINTLMDDIQIMHDEGMTVLMTKYIQREQVENDGNPISTYRSY", "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": "MASACASSTIAAVAFSSPSSQKNGSIVGATKASFLGGKRLRVSKFIAPVGSRSVAVSAVAADPDRPLWFPGSTPPEWLDGSLPGDFGFDPLGLGSDPESLKWNAQAELVHSRWAMLGAAGIFIPEFLTKIGVLNTPSWYTAGEQEYFTDTTTLFVIELVLIGWAEGRRWADIIKPGCVNTDPIFPNNKLTGTDVGYPGGLWFDPLGWGSGSPAKIKELRTKEIKNGRLAMLAVMGAWFQHIYTGTGPIDNLFAHLADPGHATIFAAFSPK", "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": "MRTVLLTGFEPFENEPINPSWEAVRALDGERVGDAVIVARQLPCVFGAAIDTIGELVDVLRPALVIAVGQAGGRAEMSVERVAINVDDARIADNAGAQPIDTAIVAGGPAAYFATLPIKAMVRDMRAAGVPASVSQTAGTFVCNHVFYGLMHRLSQQPDGDVRGGFIHIPYLPEQAARHPGQPSLAQETLVKGLRAAVATALSTRADVREQGGQLH", "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": "MFLLYEYDIFWAFLIISSLIPILAFFVSGVLAPINKGPEKLSSYESGIEPMGNAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGISVFVEALIFVLILIVGLVYAWRKGALEWS", "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": "MTKVGLRIDVDTLRGTREGVPRLLATLHRHGVQASFFFSVGPDNMGRHLWRLIRPRFLWKMLRSNAASLYGWDILLAGTAWPGKNIGNANAGIIRETATYHETGLHAWDHHAWQTHSGHWSIRQLEEDIARGITALEAIIGKPVTCSAAAGWRADGRVVRAKEPFNLRYNSDCRGTTLFRPLLMPGQTGTPQIPVTLPTWDEVIGPAVQAQSFNTWIISRMLQNKGTPVYTIHAEVEGIVHQPLFEDLLVRARDAGITFCPLGELLPTSPESLPLGQIVRGHIPGREGWLGCQQAASAS", "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": "MKFLVLAALLTAGTAASGVSPTALWQFRGMIQCTIPGSSPYLEFNGYGCYCGLGGSGTPVDELDRCCQTHDQCYTQAKKLSSCSFLVDNPYTNSYSYSCSGTTVTCSSKNKECEAFICDCDRKAAICFSKRPYNKEYKPISKYC", "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": "MAKNVLDLLMWHPKWDIERCRISYLHRGACRNLKTIRGSDIERLERGFMILRDGSSIPYHRVVKIVCDNSFIWKKQKKGIG", "text": "SIMILARITY: Belongs to the UPF0248 family."}
+{"protein": "MSDLRITLDPDFIAQTKKEVTPHWGELGWVTYKRTYARWLDDKNRSENWDETVKRVIEGNINLDPRLKNNPSKKTIHELTAEAKQLFRLVYGLAATPSGRNLWISGTDYQKRNGDSLNNCWFISIRPQKYGNSHIVPAYLTQDQVAPSMPFSFLFDQLMKGGGVGFSVVDENINQIPKLDQKVDLTIVIDKQSKSYDASLKLGATDLDEWKKTNQEKEDYIYYKLPDTREGWVLANARLIDMHFNSTNPENKKKLVLDISDIRPYGAKIHGFGGTASGPMPLIEMLFDINQILNERAGQKLTAVDATDICNLIGKTVVAGNVRRSAELALGSSNNQDFITMKQDKKKLYHHRWASNNSVAINSEFDNYQPIADSILHNGEPGVVNLELSRNYGRIKDGYQAGIDGEVEGTNPCGEISLANGEPCNLFEVFPFIAQKQGWDLKEAFKLAARYTKRVTFSPYDWEVSRKIINKNRRIGVSMSGIQDWILSTFGHRVVTGFKTATDSETGKEIKDPVYDPEIIKTVDGLYQAVVDADKDYSQELNCNTSIKHTTVKPSGTVAKLAGVSEGMHFHYSGYLIQRIRFQETDPLLPALKDCGYRTEPDIYTPHTICVEFPIKAANADSDNFASAGTVSIAEQFATQAFLQTYWSDNAVSCTITFQNDESDQIAPLLHQYRYAIKSTSLLPYYGGSLKQAPKEPISKEKYEKADNHITGNVEIVFEQTNEDQKGLELVDQSDCDNGACPIK", "text": "SIMILARITY: Belongs to the class II ribonucleoside-triphosphate reductase family."}
+{"protein": "MWLRPSIWLCFPLCLALPGQSQPKAADDLGGLYCGPSSFHFSINLLSQDTATPPALVVWDRRGRLHKLQNDSGCGTWVHKGPGSSMGVEASYRGCYVTEWDSHYLMPIGLEEADAGGHRTVTETKLFKCPVDFLALDVPTIGLCDAVPVWDRLPCAPPPITQGECKQLGCCYNSEEVPSCYYGNTVTSRCTQDGHFSIAVSRNVTSPPLLWDSVHLAFRNDSECKPVMETHTFVLFRFPFSSCGTAKRVTGNQAVYENELVAARDVRTWSHGSITRDSIFRLRVSCIYSVSSSALPVNIQVFTLPPPLPETHPGPLTLELQIAKDERYGSYYNASDYPVVKLLREPIYVEVSIRHRTDPSLGLHLHQCWATPGMSPLLQPQWPMLVNGCPYTGDNYQTKLIPVQKASNLLFPSHYQRFSVSTFSFVDSVAKQALKGPVYLHCTASVCKPAGAPICVTTCPAARRRRSSDIHFQNGTASISSKGPMILLQATRDSSERLHKYSRPPVDSHALWVAGLLGSLIIGALLVSYLVFRKWR", "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": "MLSTGVKSLDELLGGGIAPEVLTQVYGSFATGKTTLAVQIGLLSGGKVAYVDTEGGFSPERLAQMAESRGLDPEEALQRFILFTPADFKEQRRTIGSLKKIVDKSFSLIVVDSITAHYRVEEQRKNLTAELGKQLQVLLWLARKLGIPVIVINQVHFDSRAERMKPVAEHTLGYRCKDILRLDKLNTPGLRVALLERHRFRPEGGMVYFRITEKGIEDVLGREE", "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": "MAISELKLPAGVGLQVWGSAAEQARGLAAEVAGRLRSALAEQGQALLVVSGGRSPVAFLEALSEEPLDWSRITVSLADERWVPESHADSNAGLVRRHLLRGEAAKARFIGLYQPAASLEEAAELADHHLHELPLPIDVLVLGMGDDGHTASLFPNSPGLDLAMDPQGTRRCLPMWAPSVPHQRLTLPRAVLAAAKVQLLAIQGQSKLATLNAALAVEDERRMPVRAFLRAPLTIHWYP", "text": "FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily."}
+{"protein": "MIKFALALTLCLAGASLSLAQHNPQWWGNRNTIVHLFEWKWSDIAEECETFLAPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGNEEEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTAGTEAEPSKKSFPGVPYSAQDFHPSCEITDWNDRFQVQQCELVGLKDLNQHSDYVRSKLIEFLDHLIELGVAGFRVDAAKHMAAEDLEYIYGSLSNLNIEHGFPHNARPFIFQEVIDHGHETVSREEYNGLGAVTEFRFSEEIGRAFRGNNALKWLQSWGTDWGFLSSEQALTFVDNHDNQRDMGSVLNYKSPRQYKMATAFHLAYPYGISRVMSSFAFDDHDTPPPQDAQENIISPEFDEDGACVNGWICEHRWRQIYAMVGFKNAVRDTELSAWWDNGDNQISFCRGNKGFLAVNNNQYDLSQELNTCLPAGEYCDVISGSLIDGACTGKSVHVNEHGYGYIHIGSDDFDGVLALHVNAKV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MKILINKSELNKILKKMNNVIISNNKIKPHHSYFLIEAKEKEINFYANNEYFSVKCNLNKNIDILEQGSLIVKGKIFNDLINGIKEEIITIQEKDQTLLVKTKKTSINLNTINVNEFPRIRFNEKNDLSEFNQFKINYSLLVKGIKKIFHSVSNNREISSKFNGVNFNGSNGKEIFLEASDTYKLSVFEIKQETEPFDFILESNLLSFINSFNPEEDKSIVFYYRKDNKDSFSTEMLISMDNFMISYTSVNEKFPEVNYFFEFEPETKIVVQKNELKDALQRIQTLAQNERTFLCDMQINSSELKIRAIVNNIGNSLEEISCLKFEGYKLNISFNPSSLLDHIESFESNEINFDFQGNSKYFLITSKSEPELKQILVPSR", "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": "IRALPWDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAQRRLGLAVVWLWFLGMMIMAVGLHWAG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the heme-copper respiratory oxidase family."}
+{"protein": "MKRNDPCWCGSQKKWKHCHYPTKPERPSDNLRQLYASRYDIIIKTPDQIEKIRKACQVTARILDALCKAAKEGVTTNELDQLSCNLHKQYNAIPAPLNYGQPPFPKTICTSLNEVICHGIPNDTPLQNGDIMNIDVSCIVDGFYGDCSRMVMIGEVPEIKKKVCEASLEALNAAIAILEPNLPLYEIGEVIENCAARYGFSVVDQFVGHGVGVRFHENPYVAHHRNSCKIPLAPGMTFTIEPMINVGKKEGFIDPTNHWEARTCDHQPSAQWEHTVLITDSGYEILTLLDN", "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": "MPHSTNKELILGIMAGTAGISLLAFWYHKVLKPRTTMNFPKLLSLGKKFGSLTLPEESHSAQGASVVFQRRQLQILEKLNELLTNMEELKEEIRFLKETIPKLEECIQDEFGGKVTVHKISPQHRARKKKGTTVQRSATSNSSEEAESEGGYITANTDTEEQNFPFPKALNTHIEELKLDVLLQKADHLRTNESHKMESFELLCDHKEKFSEETEFLWRLARAYGDMYDLSTSTQEKKHYANIGKTLGERAITRAPMNGHCHLWYAVLCGYVSEFEGLQNKINCGHLFKKHLEIAIQLLPEEPLLYYLKGRYCYTVSRLSWIEKKMAATLFGEIPYSTVHEALHNFLKTEELQPGYSMSNYMYTAKCYVELGEPQEACKFCNLALLLPVVTKEDKDAHKEVKKMISSLKR", "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": "MSGDARKTAEGLAYLSGFGNEHASEAVAGALPEGRNSPQRAPLGLYAEQLSGTAFTEPRAHNRRSWLYRIRPSAAHPAFTRSGNGTIRTAPFNQAVPDPNRLRWNPLPVPGPATDFVEGLWTLGGNGDATQRTGMAVHLYHATASMDRVFSDADGELLIVPERGGLLLRTEFGLLHAEPGHVALIPRGVRFRVQLLDEDARGYVCENYGAPFQLPDLGPIGANGLANARDFRAPVAAYEDDESTPGPVEVVNKFCGNLWTAEYDHSPLDVVAWHGNHVPYVYDLRRFNVIGSISYDHPDPSIFTVLTSPSDTPGLAGVDFVVFAPRWLVGEDTFRPPYFHRNVMSEYMGLIEGAYDAKAEGFVPGGGSLHNMMSAHGPDRETFDRASAAELKPQRIDDGLAFMFETRWPVTLTPQAARAEHLQPGYDDVWQGLERHFRPLH", "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": "MANEKTLFYALLGVGAIIVVLSTTGYLNNASNLSIAILFAVFAIAIASVYEFREPEIVVKPAKPTFEEKVIG", "text": "SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein."}
+{"protein": "MPEFVTFSRNVFIPVTNICRNLCGYCTFRRDAGHPEAHLMSMSEIRPILERGEKAGCTEALFVFGEYAEEVPEYLLELEKLGYSTTVEYVADLCKLAIEIGLLPHTNAGILNRKELEILKPLNISMGLMLETTAELKAHSESPGKKPSTRIEMIRTAGKLKIPFTTGILVGIGETKDDRKRSLNTIADIHKEFGHIQEVIIQNFMPKPDTPMADHAPPSKEEMIDTVAIAREILPSDVAVQVAPNLIDPYSLIKAGASDLGGISPTTIDWINPEAEWPDVIELQKMIKEIELRERLPIYPQHIKKGWYSNNLSYLIETLTDKNGFKRKQR", "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": "MLFDQIASNKRKTWILLLVFFLLLALVGYAVGYLFIRSGLGGLVIALIIGFIYALSMIFQSTEIVMSMNGAREVDEQTAPDLYHVVEDMALVAQIPMPRVFIIDDPALNAFATGSNPQNAAVAATSGLLAIMNREELEAVMGHEVSHIRNYDIRISTIAVALASAITMLSGMAGRMMWWGGAGRRRSDDDRDGNGLEIIMLVVSLLAIVLAPLAATLVQLAISRQREFLADASSVELTRNPQGMINALDKLDNSKPMSRHVDDASSALYINDPKKGGGFQKLFYTHPPISERIERLKQM", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family."}
+{"protein": "SSTCIPSGQPCPYNENCCSQSCTFKENENGNTVKRCD", "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": "MRKSFYTWLMTERNPKSNNPKAILADLAFEEAAFPKHTDDFDEVSRFLEEHASFSFNLGDFDSIWQEYLEH", "text": "SIMILARITY: Belongs to the UPF0346 family."}
+{"protein": "MERVLIVNADDFGLSKGQNYGIIEACRNGVVTSTTALVNGAAIDHAAQLGRSTPELAVGMHFVLTLGEPLSAMPGLTRDGRLGKWIWQQAEEDSLPLEEIAHELACQYHRFVELFGHEPTHIDSHHHVHMFAQIYPIVAAFAREKGIALRIDRQVAAQSGLDQQAARSSAGFSSEFYGEAVSEELFLQTLDASIARGERSLEVMCHPAYVDRIIMGSAYCYPRLDELDVLTAASLKAAVADRGYRLGTYRDV", "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": "MNKKKNTILIGLYFLVGIMLFPDRIYAMHIAEGFLPVKWAGIWWIAMLPFLALGIKKVKSITQKEGPGIKMLLALAGAFVFVLSSLKLPSLTGSCSHPTGVGLGAILFGPWPMVVLGCIVLIFQAVLLAHGGLTTLGANVFSMAIVGPFVAYGAYRLLKKLNAPNWLSVFTGSALGNLLTYITTATQLAWAFPGKTGFIASLIKFMGVFATTQVPLAVTEGLVTVLIFNLLLEYSEGELKELSVISKGETV", "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": "MIGWLEAMLRVGRKLFVKAETQLYPEEKPKLFPRSRGRIVLTRDPDGQERCVACNLCAAVCPVGCIDLSKAVADDGRWYPEHFRINFARCIFCGFCEEACPTAAIQLTPDFELGEWRRDALVYEKHDLLIAGEGKVRGYRYWSVAGKAIDGKDKGCAENESPPVDLKGLLP", "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": "MNSITLLQPDDWHAHLRDGLALKRTVPDLAKQFARAICMPNLVPPVKTVEEALAYRERILAHVPEGNNFDPRMVLYFTDHTSPDEVRKIKESEHVNAIKLYPAGATTNSNNGVSDIRKVYAVIEQLEEHQVPLLLHGEVTHNHVDIFDREKRFLDEVLSPLLKQFPKLKVVLEHITTSDAAHFVLEQDRNVAATITPQHLLFNRNDMLVGGIKPYFYCLPILKRQTHQTTLLEVATSGNPKFFLGTDSAPHAQNAKENACGCAGCYSAPNAIELYAQAFDQVGKLERLEGFASHFGADFYGLPRNTSTITLVKEDNLVPESFDYLDNQKIIPLHAGKTLQWRKV", "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": "MLKVAFQMDEDVVVGRDVSVKLVEEAQRRGHEVFFYRPTSLAFVCGELVAEAFSVRVGADSLHFHDKTRLPLGKLDMLFVRQNPPFDMRYVTTTYLLERLDILMINNPKAIRDHPEKLLPLSFPKFIPPTLITESVSEISAFYAEYGDIVLKPLYDYGGNGVCRICGRADVGAISSAMVERYEAPLVAQQFIDDISSDKRVVLLGGRPIGAVRRKVTAMGEIRTNLRVGATPEATELSDREREICHDVGMLLSSVDILFAGIDILGGHLIEVNVTSPCGILEINQVYGKTLERDCWDYFEYALLHRSP", "text": "SIMILARITY: Belongs to the prokaryotic GSH synthase family."}
+{"protein": "MATEVQFACALVVLLGCGYAGTPTPSKSTLIYNSQNCTTYPSIENGQSSLYYNGSWFIRYEFNCSSGYELQGWPYTTCIFWPKNGTIWTNGPPSCVKLNITTTLMPTSTSTTPVTTGTFPDPQNTTHPTHHTVKPTRRPINLLRFGYTPWAIITLVVIILLVVWIVNCCMGPMF", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein."}
+{"protein": "MDSVTIAWAALMAISTFSLSLVVRGRSGL", "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": "MTTKYTIGVDYGTESGRAVLIDLSNGQELADHVTPYRHGVIDQYLPNTNIKLGHEWALQHPLDYVEVLTTSVPAVMKESGVDADDVIGIGVDFTACTMLPVDEEGQPLCLLAQYKDNPHSWVKLWKHHAAQDKANAINEMAEKRGEAFLPRYGGKISSEWMIAKVWQILDEAEDVYNRTDQFLEATDWIVSQMTGKIVKNSCTAGYKAIWHKREGYPSNEFFKALDPRLEHLTTTKLRGDIVPLGERAGGLLPEMAEKMGLNPGIAVAVGNVDAHAAVPAVGVTTPGKLVMAMGTSICHMLLGEKEQEVEGMCGVVEDGIIPGYLGYEAGQSAVGDIFAWFVKHGVSAATFDEAQEKGVNVHALLEEKASQLRPGESGLLALDWWNGNRSILVDTELSGMLLGYTLQTKPEEIYRALLEATAFGTRAIVDAFHGRGVEVHELYACGGLPQKNHLLMQIFADVTNREIKVAASKQTPALGAAMFASVAAGSEVGGYDSIEEAAKKMGRVKDETFKPIPEHVAIYEKLYQEYVTLHDYFGRGANDVMKRLKALKSIQHRPSSLLT", "text": "SIMILARITY: Belongs to the ribulokinase family."}
+{"protein": "MYVVSTKQMLNNAQRGGYAVPAFNIHNLETMQVVVETAANLHAPVIIAGTPGTFTHAGTENLLALVSAMAKQYHHPLAIHLDHHTKFDDIAQKVRSGVRSVMIDASHLPFAQNISRVKEVVDFCHRFDVSVEAELGQLGGQEDDVQVNEVDALYTNPAQAREFAEATGIDSLAVTIGTAHGMYASAPVLDFSRLENIRQWVNLPLVLHGASGLSTKDIQQTIKLGICKINVATELKNAFSQSLKNYLTEHPEATDPRDYLQSAKSAMRDVVSKVIADCGCEGRA", "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": "MSALKDIVELTAKELVDNKDKVRVTEIEGEKTVVIELRVDPAELGKVIGKQGRIARALRTILTAIGRKIGKRVVLEILE", "text": "FUNCTION: A probable RNA-binding protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KhpA RNA-binding protein family."}
+{"protein": "MPKASHHDLRFAFRELLASGSCYHTASVFDPMSARIAADLGFEVGILGGSVASLQVLAAPDFALITLSEFVEQATRIGRVAQLPVLADADHGYGNALNVMRTVIELERAGVAGLTIEDTLLPAQFGRKSTDLISVEEGVGKIRAALEARVDSALAIIARTNAGVLTTEEIIVRTQSYQKAGADGICMVGVKDFDQLEQIAEHLSVPLMLVTYANPNLRDDERLARLGVRVVVDGHAAYFAAIKATYDCLRLQRGLQHKSDSLNATELSHTYTQPEDYIRWAKEYMSVEE", "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": "MEPQAEEFHHPYSPYDIQLQFMRALYSCIEKGKVAVFESPTGKLAGLSTGTLELLKRFQHKSSAHPRQDEDYGDEDIKILYCSRTHSQLTQFASELRRVNMPSSIPKDFSEGVADTDGLQEGVRHLSLGSRKNLCINPRVSSLDNVTAISERCLDMQQPGVAAEQRCPFLPSNENEAQVLQFRDHVLATVKDIEDIGKLGKDIGICPYYASRSVTKHSEIVTLPYPLLLQRSARDALDLSIKGHVVVIDEAHNLMDAISNIHSVTITLSELQTSLFQLTTYARKFKTRLKGKNRNYIAQVIRLVTSITDHLKTILETSQAPEGPVQPSDLMSGKGVDQINPYKLCRYLRESKLARKVDGYSEFSRERADRQADRKPSTPVLFHIQSFLLPLMNLSAEGKLFYIKAQGDIQLKYMLLDPMNQFREIVDDARAVILAGGTMSPMTDYIHHLFPYVPSSRLGTFSYGHVIPPENLIAQVLGKGVTGTEFDFTFETRDSERMVIPDGVVAFFPSYDYLSQVLSIWKRTLAGEKNRTVYDLIEGKKTILHESRDVTISTEELLQEYASIVGSGRGALLLSVVGGKLSEGINFSDRLGRGVLIVGLPFPNIRSAVWQAKIHYVEQKAYKESSGSDANRQLVAKAAGKDFYENSCMRAVNQCIGRAIRHRNDYAAIVLMDRRYDKPAIQGKLPAWIKQSMASSSALRPAGATIGSLSKFFVAQRTSKT", "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": "MTTVTQMKCACPHCLCIVSLNDAIMVDGKPYCSEVCANGTCKENSGCGHAGCGCGSA", "text": "FUNCTION: This protein complexes cadmium, zinc and copper. SIMILARITY: Belongs to the metallothionein superfamily. Type 14 family."}
+{"protein": "MITAEECRTYKEFVDLYQSYLYPLLGARLSRMYSPKNKVIIDMGTGPGYLSIQLAKRTNAHVHAVDINPAMHEIAQEEAKKSGVSSLISFDLEDVHHLSYADQYADFIVSYSCLHHWEDVVKGLKECYRVLAPGGKIVILDTFNPQGSHLEIMRKQIKEPEYFRFVREAFEESYSFEDIHQFVQDAGIPNYSLETFHFLPEDFIESLDELEDAPLWEQNDQSTDHEIESVTWMLTIEKEKEGAL", "text": "SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "MPQNEYIELHRKRYGYRLDYHEKKRKKEGREAHERSKKAKKMIGLKAKLYHKQRHAEKIQMKKTIKMHEKRNTKQKDDEKTPQGAVPAYLLDREGQSRAKVLSNMIKQKRKEKAGKWESPLPKVRAQGETELLKVIRTGKRKKKAWRRMVTKVCFVGDGFTRKPPKYEKFIRPMGLRFKKAHVTHPELKATFCLPILGVKKNPSSPLYTTLGVITKGTVIEVNVSELGLVTQGGKVIWGKYAQVTNNPENDGCINAVLLV", "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": "MERSHIRDVDPDAADALSSERQRQEDTLAMIASENHVSEAVLEAQGSALTNKYAEGYPGERYYAGCEYADEIESLAIERAEELWGAEHVNVQPHSGTQANMAVYLTALDPGDKILSLDLTHGGHLSHGHPANFTGQTYTVEQYEVDPETGYIDYEGLKTKADEFNPDIIVSGYSAYPREVEFERIQEAADLADAYHLADIAHITGLVAAGVHTSPVGVADFVTGSTHKTIRAGRGGIIMCNEEHADDIDNSVFPGAQGGPLMHNVAGKAVGFKEALSDEFEAYAEQTVKNAEELANTLTDAGLSVVSGGTDNHLVLVDLRPSHPETTGKEVEAALESAGIIMNANTVPGETRSAFNPSGIRVGTPALTTRGFTESTVREVGELMIELIDDPTDDEAIAAVSDRVDTLTDEYPLYR", "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": "MKLTQGAFSFLPDLTDAQVTKQIQYALNKSWAISIEYTDDPHPRNSYWEMWGLPLFDVKDPAAILFEINMARKAKPNYYLKIACFDNTRGIESCVLSFIVQRPSYEPGFKMTRQEVKGRQLVYTLESYSVDAKPEGERY", "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": "MQQKTKLFLQALKYSIPHLGKCMQKQHLNHYNFADHYYNRIKLKKYHLTKCLQNKPKISELARNIPSRSFSCKDLQPVKQENEKPLPENMDAFEKVRTKLETQPQEEYEIINVEVKHGGFVYYQEGCCLVRSKDEEADNDNYEVLFNLEELKLDQPFIDCIRVAPDEKYVAAKIRTEDSEASTCVIIKLSDQPVMEASFPNVSSFEWVKDEEDEDVLFYTFQRNLRCHDVYRATFGDNKRNERFYTEKDPSYFVFLYLTKDSRFLTINIMNKTTSEVWLIDGLSPWDPPVLIQKRIHGVLYYVEHRDDELYILTNVGEPTEFKLMRTAADTPAIMNWDLFFTMKRNTKVIDLDMFKDHCVLFLKHSNLLYVNVIGLADDSVRSLKLPPWACGFIMDTNSDPKNCPFQLCSPIRPPKYYTYKFAEGKLFEETGHEDPITKTSRVLRLEAKSKDGKLVPMTVFHKTDSEDLQKKPLLVQVYGAYGIDLKMNFRPERRVLVDDGWILAYCHVRGGGELGLQWHADGRLTKKLNGLADLEACIKTLHGQGFSQPSLTTLTAFSAGGVLAGALCNSNPELLRAVTLEAPFLDVLNTMMDTTLPLTLEELEEWGNPSSDEKHKNYIKHYCPYQNIKPQHYPSIHITAYENDERVPLKGIVSYTEKLKEAIAEHAKDTGEGYQSPNIILDIQPGGNHVIEDSHKKITAQIKFLYEELGLDSTSVFEDLKKYLKF", "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": "MSKKLLYAAQMTAFDKDGNINLDGIRALVRYNIDVNKVDGLYVCGSTGEAFMLNTDEKKQVMETVYDEANGAIDLVAQVGSLNLKEAKELAKFATDLGYPKLSAVTPFYYNFTFEQIKDYYNEILKDVDNKLLIYSIPALTGVALTTDQFAELFENPKIIGIKYTNADFYLLERVRNAFPDKLILSGFDEMLLPALALNVDGCIGSTYNLNAPRVREEMDAFEAGDIDKARQLQNISNDMITDLIANDIYPTLKLVMKHMGVDAGYVKKPMSHPTPEMEAGATAIYEKYFKN", "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": "MSKSNSIFPVLFCAAGIYASFLTWALVQEPLTTQVWENSHKRFQCPNVIAVVQAVAAVCVGYFYMRAKGAQRNYGAIAMVRDYAKPLALISFTQSASSPLSQYALQYVDYLTYMLAKSCKMIPVLLVHLIIYRTTISRKKSVVAVLVSIGVTIFTIGGSKGKISGSISGSNDEHFFQKASGFLLLFLSLFMDGLTNATQDKMLKNNRVQMAIQNAETQDKKQQHKVFHTLTGAHMMFALNFFVAIWNIAYLLVIDRGQICNAHAMLKKDPIIVSYLLAYALCGSLGQCFIFYTLELYGSLVLIMITVTRKMMSMLLSIIVFGKTVNATQWLGIVIVFSGITWEALDKRREKKALEAKVQKSE", "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": "MQSMQPSTVDKLKMGAIMGSAAGLGIGFLFGGVAVLRYGPGPRGFLRTLGQYMLTSAATFGFFMSIGSVIRNEDIPLIQQSGSHWNQRLLNENANSSRIFALAMQQAKSSPRKSNEVAEC", "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": "MHHRDLLAIIIISALLFINVILWGFILRKYLEQKEQDRKEREILERLRRIREIRDDSDYESNGEEEQEVMDLVLSHGFDNPMFEP", "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": "MDKLKIQVEVAYALPEQQKIIPLAVVEGTTAYEAVQMSGITHFFPQIELDSAKMGIFGKSIPEPKSHALREGDRVEIYRPLKIDPKQARLNRAKKG", "text": "SIMILARITY: Belongs to the UPF0125 (RnfH) family."}
+{"protein": "MFDISFLFIGINSILTLLGCFINLFLCYLAIFQSPKAIRTYSLVLINITLTNVGACVTGFLLDQRIIQSGKSMLYVSYGYCSLLGEGFCFNIFAAYLHFHTHALWLLFLSFVYRYYVIIRQEPTKKVLQISVVIVYIPSLIQLISMCLQEMNFDELRSLSKEVVPQYNLTGLTITGSLDFFTFAPFYCLVHMAIISFLIAIGIHILRKMIINRMVLNGVDVTIRSRNLHAQLLRTLSFKATVPIIYYFGCIFFILGRIWINPIFEFSIFVPTVIVPVLTPLSAFIHVAPYRDFVSKMFHGRPKNKTVNSICIIPIISH", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nematode receptor-like protein srd family."}
+{"protein": "MSAHAAPSPEALSRRAEFKAAKTEMLERFRRAANVASLMHALSKLTDEALKRVWDDCGLPATLALVAVGGYGRGELAPYSDVDILVLLPDAHDPALDARIERFIGMAWDLGLEIGSSVRTVAQCIEEASQDVTVQTSLLEARRIVGSTALFERFTVHYHEALDARAFFTAKVLEMRQRHAKFQDTPYSLEPNVKESPGGLRDLQTILWIARAAGFGSSWRELDTRGLITDREARELRRNEGFLKTLRARLHVIAGRRQDMLVFDLQTQAAESFGYEPTQAKRASEQLMRRYYWAAKAVTQLATILIQNIEAQLFPATSGITRVLSPDRFVEKQGMLEIVDDGVFERHPDAILEAFLLYETTRGVKGLSARTLRALYNSREIMNNTWRRDPQNRDTFMRILQQPEGITHAFRLMNQTSVLGRYLLNFRRIVGQMQHDLYHVYTVDQHILMVLRNIRRFAVAEHAHEYPFCSQLIGNFERPWVLYVAALFHDIAKGRGGDHSTLGMADARRFCREHGIASDDAALIVWLVQHHLTMSQVAQKQDTSDPEVIKRFAEVVGNERYLTALYLLTVADIRGTSPKVWNTWKGKLLEDLYRITLAVLGGANPDAHSELKSRQEQALALLRLETVPDDAHRTLWDQLDVGFFLRHDAADIAWQTRVLYRHVNAETAIVRARPSPIGDALQVLVYVKDRPDLFAGICAYFDRNGLSVLDARVSTTRHGYALDNFIVTQTERDVRYRDIANLVEQQLASRLTETAPLPEPSKGRLSRLSRTFPITPRVDLRADERGQYYILSVSANDRPGLLYSIARVLAEHRIGVHAARINTLGERVEDIFLLAGAGLSDNRLQIQLETELLRAIAV", "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": "MASKQYEEALQKANLSDMAERYDDMAKEMRLAVTLAHEDKHILNVMARNLFSVAYKNLVSSRRSSWRMLCSERQKLEGKDPSVVHVINEKIKVVEEELLRFCDEVLDIITTYILSLEEAQKNIEYNIFFLKMKGDYYRYKAEVVTGPEHSEVSKHAAESYKEATEKAKTLPPTNPIKLGLALNYSVFHYEILNDSEKACSIAKGAFDEAIKELDTLSEEHYRDSTLIMQLLRDNLTLWTSREEGNVMGDEGKGDPDEN", "text": "SIMILARITY: Belongs to the 14-3-3 family."}
+{"protein": "MSAVAEITETTTTEMPTPIVFTDSAAAKVADLIAEEGNPDLKLRVFVQGGGCSGFQYGFTFDEITNDDDTTMTKNGVSLLIDAMSYQYLVGAEIDYKEDLQGAQFVIKNPNASTTCGCGSSFSV", "text": "FUNCTION: Required for insertion of 4Fe-4S clusters. SIMILARITY: Belongs to the HesB/IscA family."}
+{"protein": "MGESSNVHEKSQAFYGPNLGYIIELYEQYLEDPSSVDEETRRYFDEFGAPETSTPTEVPVSGPSFDLEKVVSATRLINDIRAFGHKAADIYPLKDHPREQELFELSRYDLTEEDLKQIPARLLSDDAPKPNASALELFRHLLDVYTGTVAIELRHLDDMEEKKWIRRQVEQGALQQTFSKEEKIELFKRLAETELFESFLHKTYVGQKRFSIEGLDAMVPLLDAMVGGLISSGSEHINIGMAHRGRLNVLAHVLGKPYEMIFAEFQHAPNKELIPSEGSIGINFGWSGDVKYHLGLDRKVVEQQKEVRLNLANNPSHLEFVGSVVEGYTRAAQDDRSEKGSAVQHDDLAASILIHGDAAFPGQGIVAETLNMTNLTGYRTGGTVHVIANNTIGFTTDPNDSRSTRYASDIAKGYEIPVFHVNADDPEACVAVAKLISEYRAKFHKDILVDLIGYRRYGHNEMDEPMNTNPVLYKAIKGHQSVRHVYAARLEEEGVMTKDEKAQIEQKIEEALKAARDLVPSEEEDADIVLPDAVHKGFPKVDTSVEREFLTQLNEELLNWPEGFGVFHKLQKVLDRRRDAFSEGGKIDWGHAETLAFASILSDGTPVRLSGQDSERGTFAQRNIMLNDVESGKKFSPLHELSTAKASFSVYNSPLSEGSVLGFEYGYNVFAQDTLVLWEAQYGDFANSAQVMFDQFISAGRAKWGQKSGLVMLLPHGYEGQGPEHSSARMERYLTLAGEKNWTVANLSSAAQYFHILRRQAEMLGKEEIRPMIIMTPKSLLRHPLATSPVEAFTEESFKPIVEQPGLGENTEKVERLVFCTGKMAIDLAEAVGKSEESLDFLHIVRVEEIYPFPVREIRDVISRYPNAREIVWVQEEPKNMGAWTYIEPRLEAVTTNRLDVRYIGRRRRSSPAEGNPTAHKQEQARIIREALSRDVVSSGAGTSTYQKDRK", "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": "MSAPILFPLSAPESSFTIAGRLFHHAWPVLVAQLLSMSMLIADTVITGRYGTLDLAAVAVGSGVYISIVMLLVGVLQAVAPTVAHHFGARRVDAIGPALQQGFWLALMLALPGIALLAFPGFLLELSSVPADVAGKTRDYLLATAFGLPAVLLYRTFYAFNNALGRPRALMMISFIVTSTHIPLAWALVHGAFGLPPLGAIGCGISTAIVNWIAFACGAGYLAHNRDYRPYRLFANWQPPRRRDLLALLKLGIPMGLSTFIEVSSFTLIALFAARLGAEAVAGHRVVANLAALIYMLPLAISIAILVLVGQAAGAREPARARATVRVGMGLTVGLVALIGVLLWVGREPVVALFSADPAVRAVALGLVFYICIYQIFDAVQTVAAHALRGYKVTFMPMLLHALCFWGIALAGGYWLAFHAPGREQSPTVAGFWEASVVATILASVLFGWLLRVVMRRPQNVQT", "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": "MALLSFERKYRVRGGTLVGGDLFDFWVGPFYVGFFGVTTAFFALLGTILIFWGASQQGTFNPWLINIAPPDLSYGLGLAPLLEGGLWQIITICATGAFISWALREVEICRKLGMGYHVPFGFAAAIIAYMTLVIFRPLLMGAWGHGFPYGIFSHLDWVSNVGYAYLHFHYNPAHMLAVTLFFTTTLALALHGGLILSACNPEKGEEAKTPDHEDTFFRDFIGYSVGTLGIHRLGYLLAINAGLWSAICIIISGPVWTAGWPEWWNWWLDMPIWGEPIAVIGGM", "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": "MTEKFDYKELGLKVGLEIHRQLDTKKLFSPVPSELTEKVDFTFERRLRPTMSELGEIDPAALEEFKKGRKYIYEGNYELSDLVYMDEEPPRGPDREALEVTLQIAYLLNAKPVDEVHFMRKIVIDGSNVSGFQRTAIIALDGKVDTPWGSVGIPTICLEEDACRIVERKEKEVIYRLDRLGIPLVEISTTPDIHHPEQAKVVAKYIGDALRATRKVKRGLGTIRQDLNVSIKGGARVEIKGVQELDMIPLIIEREVERQLNLLKIRDELRERGVRPEDIKEEFYDVTDVFENTESKIIARTIKKGGNVLAVKLPKFRGLIGREIQPGRRLGTEMADRAKKYVKGIFHIDELPNYGITEKEVNAVIEKLGLGELDAFVLVAADEETAKKALREVIKRAREAIEGVPEETRRALPDGNTQYMRPLPGKARMYPETDIPSIFIPPEEKERIKANLPELPQERVERYVKEYRIDKSLAETLVNDERDELFEELVKKGVKPSLAASILVVVLKGLKKEVPIENITDDHIREAFQLYTEGKIAKEAFEEIFKELALHPEKSAAQVAEEKGLTLLSEEEVERIIDEVVQQNIEVIKAKGMGAMGMIMGRAMAKLRGRADGKLVSTLVRRKIQELS", "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": "MFTKVLIANRGEIAMRIIRTCSRLGIKTVAVYSEADKDAPHTKAATEAYLIGESRVSESYLNIERIIKTAKKAKADAIHPGYGLLSENSRFAERCKQENIVFIGPSPDIIAKMGSKIEARKAMEAAGVPVVPGVSESLGDIEAACRTASQIGYPVMLKASAGGGGIGMQRVENEEALKKAYEGNKKRAADFFGDGSMYIEKVIEHARHIEVQLLADQHGHTVHLFERDCSVQRRHQKVIEEAPSPFVDDELRMKIGQTAVKAAKAIGYTNAGTIEFIVDQKQNFYFLEMNTRLQVEHPVTEEITGLDLVEQQLRIAAGHTLTFSQKDIQRNGHAIEVRIYAEDPKTFFPSPGTITAFSLPDQKGVRHECAVAKDSTVTPFYDPMIAKMIVKGQTRTEAIEKLETALRDYRVEGIKTNLPLLIQAAATKAFKEGDVTTDFLKQHL", "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": "MAAKIFCLIMLLGLSASAATASIFPQCSQAPIASLLPPYLSPAMSSVCENPILLPYRIQQAIAAGILPLSPLFLQQSSALLQQLPLVHLLAQNIRAQQLQQLVLANLAAYSQQQQLPLVHLLAQNIRAQQLQQLVLANLAAYSQQQQFLPFNQQLAAAYPRQFLPFNQLAALNSHAYVQQQQLLPF", "text": "FUNCTION: Zeins are major seed storage proteins. SIMILARITY: Belongs to the zein family."}
+{"protein": "MAQLAKFDVPEELTNKALEALELARDTGKIKKGTNEATKAIERGNAKLVLIAEDIEPAEIIAHIAPLSEEKKAPYIFIKNQKELGAASGLGVSCATVAIVDAGKAGEMVQDIAQKLEALK", "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": "MKSERAKQIIDSKKYIPVYYKNTPVHIEKVDNKENIAHIKSLNTDKEIVVNVKTLSECNKLNN", "text": "SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspH family."}
+{"protein": "MEGYKSFLVFLVSSLLLGFLGVIFTLVWVLHWREGLGWDGGAAEFNWHPVLVTSGFIFIQGIAIIVYRLPWTWNCSKLLMKFIHAGLHLTAFVFTIVALVAVFDFHNAKNIPNMYSLHSWIGLTVVILYALQLVLGVSIYLLPFARDTLRAALMPVHVYSGLLIFGTVIATALMGITEKLIFSLKEPPYSKMPPEAIFVNTFGLIILVFGGLVVWMVTTPAWKRPREQEIKALNPTVSSPDGTEEGSTITDCSNTEKSDVELNSEAARKRILKLDDAGQRSTM", "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": "MRHYVLSISFAVALFLECYTPSTAISIGKMDDVALEQDTLDSLLSVEVSENSPDSVRGRSSKIVLLADSGLWMNLNRGLPFYKLRAAAAGPDRALTLDRREAGQDLSPSISIVRRDTMRCMVGRVYRPCWEV", "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": "MSQTSPLSEQADSSLKYDYSNVPAQALDAIRMRLAQLTHSLSKIRDDMSKADLPQWYSLQAQLSVTLTQLSSLTSTLQHFEDTLECTVPYPLPSFPTTAHEGLLTTLMRKKQIPEVENWIKDAIDHSGLDLEGRNWDEIESAIQRDKSTTARALDFINQEYSNYSFQGLYTAEELSKNVGDPQSMIYRSATSNAKPKAPFSVDSILTFMYQGTMKTEETSIAK", "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": "MVTSWYKIWYHTTQVIFILLFVGFSVVVPLDCIVQASDSSNDAVNTFIVVGAAVVLVVFGISISFARVLIFRRSLQDIPKKYIPVTAQDMRHKPSREYVIENMKRAGELAEKFKVPKEPVLHAGMEPKDSDMFPEHLKYAEIVKFISDRFRFDGALLLNFVTESDLSTTFKTALHKLFENEKHPYKQYLDEFISLYEKFRFSGQDIERNDFVKFLRLYKYLADLSNNLDLTRIESVPSQFLHVPTEDYDTDARSRTDSEFSTPYLRPYPSDAFMHNTTPASHVGSRSSNFSYDIDESAEPPESVEDQQRYHDMLTRVDTYNTVIHR", "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": "MDAFKLLTRSTKLKSATTQSSTLPSTGKAANPQLFRGAAAEKLEKGSGKKRKRAHAADDEAVVNEDALNLDFFSQGRSSIPKSSDAATTKGSGAPAGQEGASESDSDADDEPMDEVQRRTILNAHKIKVTDMRDLEELAPAQVQSEEPKKKKKRKQQEEAEKQQPQTLSKKEQKKARRLFPQPLVSFKELRSKYKISRRLAENIAEQGFTVPTEVQLGSLPLLLGNSAVPGGSSDSTSATEPDLLVVAPTGSGKTLSFMIPVINKIVRHHHTHPEERGIFAVVVAPTKELASQIVNEGRKLALGTGVKVTLMKKGMRVVERENEDEDVLDESNSESSESESDERTPNNKNKGPVPITKSDILVSTPLQLVNALSDNKTKPLATLPLVRNLVLDEADVLLDPLFRDQTLDIWRSCTHPELRASLWSATMGSSIEDMAKTTIKERKLSLPQTKSYPLLRLVVGLKDSAIPNIKHKLVYAATEQGKLLGLRQLIHPTAATTSDVRLRPPFLIFTQTIPRAIALHSELLYDIPPEAGGSARIAVLHSDLSDTQRSDIMKGFRKGEIWILVTTDLLARGVDFRGINGVVNYDIPNSPAVYVHRVGRTGRAGREGGVAVTYYTKEDIPYVKSIANIIDVSEKLRGENGERSVQKWLLDALPDLSKKNKKELKKHGVKARQTGLKGATDEKEQRRTRISTKSGFDRRKEYNKKMMIAASQKKTQARKNGADSDSAGDDDDEDGWNGLDD", "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": "MFVRKSCYSLINATRRCLRYRQLSSTTAGTVGTTAPTANISLNDEPQPAAAEMDEFTKEFLRNRIEVSDIQRLILSAGSSVAALVDPRRHDMIACLGETTGREALEKILHYMRSTEEGQRILVEKPRINTRTVDMEALKKMPEHTFGYTYVKFMEDNNITPDSRMEVRFLDEPGLAYVMTRYRETHDMVHAILDMPTNMLGEVTVKWVEALNTGLPMCYGGAVFGAFRLRTKQRQNYLRKYLPWALRTGNRIKPLMGVYWEKRWEQDVTELRKELNIELLAP", "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": "MPLSYPHFRKLLLLDDEAGPLEEELPRLADEGLNRRVAEDLNLQLPNVSIPWTHKVGNFTGLYSSTVPTFNPDWLTPSFPDIHLHQDLIHKCEQFVGPLTKNELRRLKLVMPSRFFPKVTKYFPMEKGIKPYYPDNVVNHYFKTRHYLHTLWKAGILYKRESTRSASFCGSPYSWEQELQHGSTSINDSKGHGTESLCTQSSGILSRPSAGSSIQGKFQQSRLGLQQKQGQLANGKQGRSGRIRSWVHTPTRWPVGVESTGTGCAYNIASRSASCFHQSAVREKTNPSLSTSKRHSSTGHAVELHSVPPGSVRSEGKGSVFSCWWLQFRDTEPCSDYCLSHIINLLEDWGPCYEHGQHHIRTPRTPARVTGGVFLVDKNPHNTTESRLVVDFSQFSRGNTRVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHLPLHPAAMPHLLVGSCGLSRYVARLSSTSRIHDHQHGTMQNLHNSCSRNLYVSLLLLFQTLGRKLHLYSHPIILGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDLVLGAKSVQHLESLYTAVTNFLLSVGIHLNTSKTKRWGYTLNFMGYVIGSWGSLPQDHIVQKLKDCFRKLPVNRPIDWKVCQRIVGLLGFAAPFTQCGYPALMPLYACITAKQAFVFSPTYKAFLCQQYMNLYPVARQRPGLCQVFADATPTGWGLAIGHQRMRGTFVAPLPIHTAELLAACFARSRSGAKLIGTDNSVVLSRKYTSFPWLLGCAANWILRGTSFVYVPSALNPADDPSRGRLGLYRPLLRLPFQPTTGRTSLYAASPSVPSHLPDRVHFASPLHVAWRPP", "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": "MNTKITNFTFAFDKKNLNLAETIIKKYPPEGKRSAILPLLDLAQRQNGGWLHVSAIEYVANMLEMPYMRAYEVATFYTMFNLNPIGKYHIQVCTTTPCWLRGSDNIMKICEKKLAIKHKETTKDQKFTLSEIECLGACVNAPVVQINDDYYEDLNEAKMEKLIEQYLNEFKSKMQNG", "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": "MAMKSLSFLAVLSLLALTLPLAIASDPSQLQDFCVSANTSANGVFVNGKFCKDPKLVTADDFFFSGLQTARPITSPVGSTVTAVNVNNLLGLNTLGISLVRIDYAVNGQNPPHTHPRATEILVVEQGTLLVGFVTSNPDNRLFSKVLNEGDVFVFPEGLIHFQANIGKAPAVAFAALSSQNPGVITIANTVFGANPAINPTILAKAFQLNPRVVMDLQTKFKK", "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": "MPQLDTSTWFITITSMTITLFIMFQLKLSKHSYPSNPELKPINTSMHTTPWESKWTKIYSPLSLPQQ", "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": "MLKTTFANAEFANPFMNASGVHCMTTEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLDYVLKNQKEKAQEAPIFFSIAGMSAAENIAMLKKIQESNFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDSEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIKIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMDKKGYQSIADFHGKLKSL", "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": "MAPLISLQDVSKTYFNGDIAVEVLHHISLDIEAGEFVAIIGQSGSGKSTLMNILGCLDQPTSGSYFIEGENVSGFDSDELAALRRRTFGFIFQSYNLIPTASARENVEVPAVYAGVSARDRHDRAEALLQSLKLGERIDHRPNQLSGGQQQRVSIARALMNGGRVILADEPTGALDSQSGDEVMRLLRDMNENGHTVIVITHSREVAAQADRLIEISDGHIVADRSKKRRSNRDAAVGLAQRTREGFAAIADVSEAVKMALRALRANLFRTILTLLGIVIGVGSVVAMLAIGTGAQNSVLDRISSMGSDLLVVRPSMANFRGSAGGTNVTLVPADADAITELANVAFAVPEMTSTVTLRRGNIDYQTTANGTVPQFTEAKSWKIGRGEFINRNDMETYAPVAVLGETVVKTLFPEGSDPIGQYVLVNKIPFQVIGVMSGMGASAGGNDQDDVVLVPLTTGSMRLFGQRNIRTITVKVQDASAIDLTQERIQALLNERHRKDDTQITNMSSVREAFTETSNTMKFFLGSVAAISLLVGGIGVMNIMLVSVSERTREIGVRMATGARERDILVQFIVEALVVSAIGGAIGVVAGLSTGYAAKAFGMPVSFTPGPVALAFACAFLTGLLFGYLPARNASRLQPAVALSAD", "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": "MNKKILQILEYDKVKEQFMNALTTAQGQQELKDLKPLTDKEKIQLLFDEVADFRLLTQENGLLNLGKTNDLTEILRRLELEASLSGKEFVEIKKVIQLGINIQRFFDEAENVETPSLAITLEKLVDLSALVKKLEIFDNAGSLYDNASLELMHIRASIKSHQSEIRKIMQEMLTKNLSSLSENVITIRNDRQVLPVKAENKNKIAGVVHDMSASGQTLYIEPNAVVSLNNKLNQKRIEERQEITRIYRELASQLKPYSFDIRQNAWLIGHIDFVRAKYLYLAANKATLPELTTDKDITLFAARHPLIEAKIVVTNDIKFDAGLNTIVITGPNTGGKTITLKTVGLLTILAQSGLPILAADGSRIHLFDDIFADIGDEQSIEQSLSTFSSHMTNIVHILAQADENSLVLFDELGAGTDPKEGAALAIAILENLRERNVKTMASTHYPELKAYGVETQRVINASMEFNIDKMQPTYHLQLGVPGRSNALEISRRLGLPETIISVASQQISDSEHDVNQMIEKLEEKTREVIESSRNIKKIERENQSLHKDLTKVYNQINREREFELEKAQKEAQEVVKKASLEAQEILKNLNDKAALKPHEIIAARKELEGLAPTIDFSKNKVLKKAKAQRGLKQGAEVNVTSYGQRGKLIRLEKDGRWTVQMGSITTRLNEDEFEVIESPEQIQAKTKNVSKKVTSKVKAQLDLRGMRYEEAELELDNYIDQALLANLIQITIVHGIGTGVIREMVQKKLQKHRHIKSYEYAPINAGGSGATIAILK", "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": "MKQNVFEVLMYLFENYLYNDEEPGDRDSLESELHEAGFSAMEIRKAFEWLDALADSRVLPAAPSGKSSIRLFGEPELARLDTETRGFILYLEQVGILTAESRELVLDRILALDDHEVDLDTVKWVILMVLFNRPGEEEAYNWMENLMFDVPTHLVH", "text": "SIMILARITY: Belongs to the Smg family."}
+{"protein": "MGQTKSKIKSKYASYLSFIKILLKRGGVKVSTKNLIKLFQIIEQFCPWFPEQGTLDLKDWKRIGKELKQAGRKGNIIPLTVWNDWAIIKAALEPFQTEEDSISVSDAPGSGIIDCNEKTRKKSQKETESLHCEYVAEPVMAQSTQNVDYNQLQEVIYPETLKLEGKGPELVGPSESKPRGTSPLPAGQVPVTLQPQKQVKENKTQPPVAYQYWPPAELQYRPPPESQYGYPGMPPAPQGRAPYPQPPTRRLNPTAPPSRQGSELHEIIDKSRKEGDTEAWQFPVTLEPMPPGEGAQEGEPPTVEARYKSFSIKILKDMKEGVKQYGPNSPYMRTLLDSIAHGHRLIPYDWEILAKSSLSPSQFLQFKTWWIDGVQEQVRRNRAANPPVNIDADQLLGIGQNWSTISQQALMQNEAIEQVRAICLRAWEKIQDPGSTCPSFNTVRQGSKEPYPDFVARLQDVAQKSIADEKARKVIVELMAYENANPECQSAIKPLKGKVPAGSDVISEYVKACDGIGGAMHKAMLMAQAITGVVLGGQVRTFGGKCYNCGQIGHLKKNCPVLNKQNITIQATTTGREPPDLCPRCKKGKHWASQCRSKFDKNGQPLSGNEQRGQPQAPQQTGAFPIQPFVPQGFQGQQPPLSQVFQGISQLPQYNNCPPPQVAVQQ", "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": "MSDIALTVSVLALVAVVGLWIGNIKVRGVGFGIGGVLFGGIIVGHFVDQAGVTLSGDMLHFIQEFGLILFVYTIGIQVGPGFFASLRVSGLRLNLFAVLIVIMGGLVTAILHKIFAIPLPVVLGIFSGAVTNTPALGAGQQILRDLGTPVDLVDQMGMSYAMAYPFGICGILLTMWLMRLIFRVNVEAEAQKHESSLANGHSLIQTMNIRVENPNLNNMAIQDVPILNSDKIICSRLKRDDTLMVPSPGTIIQAGDLLHLVGQPTDLHNAQLVIGKEVDTSLSTRGTDLRVERVVVTNEKVLGKRIRDLHFKERYDVVISRLNRAGVELVASSDASLQFGDILNLVGRPASIDAVANVVGNAQQKLQQVQMLPVFIGIGLGVLLGSIPLFVPGFPVALKLGLAGGPLIMALILGRIGSIGKLYWFMPPSANLALRELGIVLFLAVVGLKSGGDFVDTLTQGEGLSWIGYGIFITAIPLITVGLLARIFAKMNYLTLCGMLAGSMTDPPALAFANNLHATSGAAALSYATVYPLVMFLRIITPQLLAVIFWGMG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family. YidE subfamily."}
+{"protein": "MASMVSFCFLLLFLAFFASSFNEIYAEESESKEFVLTLDKSNFFDTVSKHNFIVVEFYAPWCGHCKKLAPEYEKAASILSSHDPPVILAKVDANEEANKELASEFEVRGFPTIKILRNGGKIVQEYKGPRDADGIVDYLKKQSGPPSAEIKSIEDATNLVSEKKIVVVGIFPKFSGEEFENFSALAEKLRSDYEFGHTLDAKLLPRGESSVSGPVVRLFKPFDELFVDFQDFDVNALEKLVEESSVPTVTIFDKDPSNHPFVVKFFNNANAKAMLFLNFTSEVVESFRSIYREVAEKNKGEGISFLIGDTESSQGAFQYFGLRDDQVPLIVIQNNDGTKYLKPNLEPDHIASWVKEYKDCKLSPYRKSEPIPEHNNEPVKVVVADSLDEIVFKSGKNVLLEFYAPWCGHCKQLAPILDEVAVSFENDPDVLIAKLDATANDYPTNTFDVKGYPTLYFKSASGELLQYDGGRTKEDFIEFIEKNREKSSKKESIVKDDQTDSETKAEL", "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": "MIRFEIHGDNLTITDAIRNYIEEKIGKLERYFNDVPNAVAHVKVKTYSNSATKIEVTIPLKNVTLRAEERNDDLYAGIDLINNKLERQVRKYKTRINRKSRDRGDQEVFVAELQEMQETQVDNDAYDDNEIEIIRSKEFSLKPMDSEEAVLQMNLLGHDFFVFIDRETDGTSIVYRRKDGKYGLIQTSEQ", "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": "MAEVEVRVRQEQVAEFRETFAFFDKDGDGCITLEELDTVVRSLGQTPTREELAEMIRDVDVDGNGTIEFAEFLALMARKASRGGENGGGGDDSGDAADEELREAFKVFDKDQDGLISAAELRHVMISLGEKLTDEEVEQMIREADLDGDGQVNFDEFVRMMMLSDQ", "text": "FUNCTION: Potential calcium sensor. SIMILARITY: Belongs to the calmodulin family."}
+{"protein": "MPKGCLVITVSGLAGSGTTTLCRNLAKHYGFKHIYAGLIFRQMAKEMGMTLEEFQKYVELHPEIDREIDRRQIEAAKECNVVIEGRLAGWMVKNADLKIWLDAPIMERAKRVAKREGISVEEAFVKIAEREKQNRKRYLNLYGIDIEDKSIYDLIINTAHWGPDGVFAIVKAAIDHLSPSGDAGEDEKEKEVG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily."}
+{"protein": "MAMNFVTFNQDYSYLAVGNIAILEMLFSTSLVALILSPRRLQITNTKRQSTICELTFPTTVLAVRLNRKRLVIVLEDQIYLYDIQTMKLLYTIETSPNPNAICALSPSSENCYLAYPLPQKAPPSSFTPPSHAPPSSAHISPTSGEVLIFDTLKLEAINVVEAHKSPLSCLAINTEGTLLATASDKGTIIRVFSVPDAQKLYQFRRGSMPSRIFSMSFNITSTLLCVSSATETIHIFKLGHQDPSEDLPTSPIGTDSRKTNSTPRERAFSQGSSTLSGGDNSPTDGDPSDISSRKHNGTLMGMIRRTSQNVGNSFAATVGGYLPKGVTEIWEPARDFAWIRLPKTAGYGGPGSNAGPVRSVVAMSSNTPQVMVVTSDGNFYVYNVDLSKGGEGTLTKQYS", "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": "MADEHRQPEVNIGLVGHVDHGKTTLVRALSGEWTDQHSEEMKRGISIRLGYADATLRRCPDCDEPECYTVAETCPEHDTATEIERTVSFVDAPGHETLMATMLSGAALMDGAVLVVGANEPVPQPQTEEHLMALDIIGIENIVIAQNKVDLVDAEEARQNYEEIQAFVEGTVAEDAPVVPVSAEQEINVDLVIDALQTEIATPDRDPSADPLLYAARSFDINRPGTEWGGLLGGVIGGSLVDGELEAGDELELRPGREVEEGGKTEWRPVTTDVRSLQAGGEDVDSASPGGLLGVGTGLDPSLTKGDALAGQVAGPPGSLPPTWESFEMDVDLLERLVGAADGEQIDDISTGEPLMLTVGTATTVGSVTSARDGECEVALKRPVCAPAGAKIAINRRVGARWRLIGVGTLTESE", "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": "MGGKWSKSKMGGWPAVRERMQKAEPAADGVGAASRDLEKHGTITSSNTAANNAACTWLEAQEDEDEEVGFPVRPQVPLRPMTFKAAVDLSHFLKEKGGLDGLVFSQKRQDILDLWVYHTQGYFPDWQNYTPGPGTRYPLTFGWCFKLVPVEPDKVEEATEGENNSLLHPICLHGMDDPEKEVLVWKFDSRLAFHHVAREKHPEYYKDC", "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": "MIKLAILLLFTVAIVRCQGPFGPGCEEAGCPEGSACNIITDRCTCSGVRCRMHCPHGFQRSRYGCEFCKCRLEPMKATCDISECPEGMMCSRLTNKCDCKIDINCRKTCPNGLKRDKLGCEYCECRPKRKLIPRLS", "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": "MFNFINSLKNYSQESFRAARYIGQGFIVTLNHINRSAITVQYPYEKLITSERFRGRIHFEFDKCIVCEVCVRVCPINLPVVDWNFQQDIRKKKLKNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELSVYDRHELNYDQIALGRLPFNSFQDALVTKAS", "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": "MARITTEDCTGKISNHFDLTLVAARRARQLENGNTPLVDDVRNNKPTVTALREIAAGHIGTELLTRNK", "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": "MGSGPRGALSLLLLLLAPPSRPAAGCPAPCSCAGTLVDCGRRGLTWASLPTAFPVDTTELVLTGNNLTALPPGLLDALPALRTAHLGANPWRCDCRLVPLRAWLAGRPERAPYRDLRCVAPPALRGRLLPYLAEDELRAACAPGPLCWGALAAQLALLGLGLLHALLLVLLLCRLRRLRARARARAAARLSLTDPLVAERAGTDES", "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": "MQPISPDGSLSPWEPGMFSLAVYAVLVAAFVAVQLFVAWWLGERKPGVEKARPYECGIIPTGSARLRYPVPFYLVAIFFLIFDMEGAYILTWAVAFEELGWAGWLQMSFFIGLLLVGLVYVWKKGGLDWRPSYGKK", "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": "MGDSSGSRPTWPRRSAACSRNKVGKDCMPDDYSYINTRVRVMRTKLLDGRALDAALASGSYQEFLRVLSETDFAPNMRETTAEGAGLPELDRALSQNLFDTTQRVLGFADGDAKREIETLLMKWDLTNLKTLARGIVSGRGAETIQQNLIPGGTIKPSVLQTASQSTDLASAATALGVGGHPLAKVFRNAVTAYNTTGRLLDLEVLLDQGYYRYATQVSRDTSLRRYLSREIDITNALIARNSRGGTLDTNLFVPGGSLDAAGYGRLGAGDAGGNADITAILEAPSIEDAEVAARTALDRAARSSAVSDVEGVGIILDFLRRKEIEVAKLRLIGRGKYYDLPTDEIRREVQA", "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": "MGVANDSSPEYQWMSPHRLSDTVILGDCLYFNNIMSQLDLHQNWAPSVRLLNYFKNFNRETLLKIEENDYINSSFFQQKDKRFYPINDDFYHISTGGYGIVFKIDNYVVKFVFEATKLYSPMETTAEFTVPKFLYNNLKGDEKKLIVCAWAMGLNYKLTFLHTLYKRVLHMLLLLIQTMDGQELSLRYSSKVFLKAFNERKDSIKFVKLLSHFYPAVINSNINVINYFNRMFHFFEHEKRTNYEYERGNIIIFPLALYSADKVDTELAIKLGFKSLVQYIKFIFLQMALLYIKIYELPCCDNFLHADLKPDNILLFDSNEPIIIHLKDKKFVFNERIKSALNDFDFSQVAGIINKKIKNNFKVKHNWYYDFHFFVHTLLKTYPEIEKDIEFSTALEEFIMCTKTDCDKYRLKVSILHPISFLEKFIMRDIFSDWINGGN", "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": "MSCLPALDKFLDNYHRSYLSTLGELPRYYPQGEPSLCIQGEFDEASDEAVSWLPVKREHLGSFANVEHALELTLWPDINHFYGEYFAAPVLFDSPWGTGELLQVWNEADFDALQQNIIGHLMMKQKLKQPATWFIGLLDEGDKMLTVDNADGSVWGEIPGELPSAQLAPSLAEFIEALSPRIAPPVKHEELPMPALEHPGIVASFKRMWHNLIGKR", "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": "MDTELLKTFLEVSRTRHFGRAAESLYLTQSAVSFRIRQLENQLGVNLFTRHRNNIRLTAAGEKLLPYAETLMSTWQAARKEVAHTSRHNEFSIGASASLWECMLNQWLGRLYKNQDAHTGLQFEARIAQRQSLVKQLHERQLDLLITTEAPKMDEFSSQLLGYFTLALYTSAPSKLKGDLNYLRLEWGPDFQQHEAGLIGADEVPILTTSSAELAQQQIAMLNGCTWLPVSWARKKGGLHTVVDSTTLSRPLYAIWLQNSDKNALIRDLLKINVLDEVY", "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": "MIYLNNVILNDKTLPMCFNLNVKAGERVAIIGESGAGKSTLLNLIAGFEFPAQGEIWLNDKNHTRSAPYERPVSMLFQENNLFPHLTVQQNLALGIKPSLKLTALEQEKIEQAACSVGLGDYLERLPNSLSGGQKQRVALARCLLRDKPILLLDEPFSALDQKLRVEMLALIAKLCDEKDLTLLLVTHQPSELIGSIDQVLVVENGQISQLQKGV", "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": "MLLGFFRLLFKGLYRVRLTGDTQALYQQKVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQRWFMRALTPIIDFVPLDPTKPMSIKHLVRLIEQGRPVVIFPEGRISVSGSLMKIYDGAAFVAAKSQATIVPLRIEGAELTPFSRLKGLVKRRLFPRIQLHLLPPTHLPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQDRFGARKPCVEDINFQPDTYRKLLTKTLFVARILEKYSQPGEKIGLMLPNAGISAAVIFGAIARGRIPAMMNYTAGVKGLSSAIAAAELNTIFTSRTFLDKGKLWHLPEQLTQVRWVFLEDLKGDITLADKLWIFAHLLAPRLAQVKQQPEDAAMILFTSGSEGNPKGVVHSHKSLLSNVEQIKTIADFTANDRFMSALPLFHSFGLTVGLLTPLLTGAEVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLANYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKVGTVGRILPGMDARLLAMPGIDQGGRLQLKGPNIMKGYLRVENPGVLEAPAAENQHGEMEAGWYDTGDIVTFDEQGYVRIQGRAKRFAKIAGEMISLEMVEQVALGASPDKMHATAIKQDASKGEALVLFTTDNELTREALLRYARQHGVPELAVPRDIRWLKQLPVLGSGKPDYVTLKNMVDEAETTHE", "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": "MASLEDGTYRLRAVTTSNPDPGVGGEYATVEGARQPVKAEPSTPPFFERQIWQVTRNSDGQSTIKYQGLNAPFEYGFSYDQLEQNAPVIAGDPKEYILQLVPSTTDVYIIRAPIQRVGVDVEVGVQGNNLVYKFFPVDGSGGDRPAWRFTRE", "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": "MLSTHLLFLATTLLTSLFHPIAAHVAKRSGSLQQITDFGDNPTGVGMYIYVPNNLASNPGIVVAIHYCTGTGPGYYSNSFYATLSEQYGFIVIYPSSPYSGGCWDVSSQATLTHNGGGNSNSIANMVTWTISEYGADSKKVFVTGSSSGAMMTNVMAATYPELFAAGTVYSGVSAGCFYSDTNQVDGWNSTCAQGDVITTPEHWASIAEAMYPGYSGSRPKMQIYHGSVDTTLYPQNYYETCKQWAGVFGYDYSAPESTEANTPQTNYETTIWGDNLQGIFATGVGHTVPIHGDKDMEWFGFA", "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": "MELQRIFPLYTATGAARKLTPEAVQRLCDALTLDMGLWKSILTDPRVKIMRSTAFITLRIAPFIPLQTDTTNIAVVVATIYITRPRQMNLPPKTFHVIVNFNYEVSYAMTATLRIYPVENIDHVFGATFKNPIAYPLPTSIPDPRADPTPADLTPTPNLSNYLQPPRLPKNPYACKVISPGVWWSDERRRLYVLAMEPNLIGLCPAGWHARILGSVLNRLLSHADGCDECNHRVHVGALYALPHVTNHAEGCVCWAPCMWRKAGQRELKVEVDIGATQVLFVDVTTCIRITSTKNPRITANLGDVIAGTNASGLSVPVNSSGWQLYMFGETLSRAIINGCGLLQRICFPETQRLSGEPEPTTT", "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": "MVANKDKATKRKIPAVDDAVKVSTANGKQQTKLKEPVDDESASDYYESDEENLFASIDNGNDEDSTDSEGEGEESDDEEVQEFESADSDFEDESGKDDEEEAEDEEDDADEEDADSADDVNSDSSPEPEEEESDDELEFEEDLEEPEQPKAIQKVIVGRQKKSVEATAEDEDEEDDEETRDLLEAAQKEDEKLGEIDAALGIAPAKTRGVGIFPPEAKSRFKGGKNQDEYAAGDTSDEEDIRNTVGNIPMHWYDEYKHIGYDWEGNRLIKPAKTDAIDDFLKKMEDPNFWRTVKDPQTGQNVVLTDEDIGLIKRIMAGKNPDEQYSDYEPWIEWFTSEVEKMPIRNIPDHKRSFLPSKSEKQKVGRLVHALKMGWIKTRAETERLAALSKGPKFYMIWESDHGKEEMRRIHDHVVAPKRPLPGHAESYNPPPEYLFNEQELAEWNSHEEEPWKRKLHYVPQKFNSLREVPYYDKYIRERFLRCLDLYLCPRGKRTRVTVGPEYLIPKLPSPKDLQPFPTLQNLIYKGHTDMIRSVSIEPKGEYLVTGSDDQTVKIWEVSTARCIRTIPTGDVVRSVAWCPNSKISLIAVASGKRVLLINPQVGDSLLVKKTDDLLAEAPKSETVDNERITTAVQWVDFTEEERKSGVRIVINHFKEIKQVTWHGRGDYFATVMPEAANRSVLIHQLSKRRSQFPFSKSKGLIQCVLFHPVKPCLFVATQRHVRVYDLVKQELLKKLFPSCKWISSMAIHPKGDNLLVATYEKKMMWFDLDLSTRPYQQLKLHHSAIRNVAFHLRYPLFASASDDRSVIVSHGMVYNDLLQNPLIVPLRRLEHHERVNDFGAFDVVFHPTQPWLFSSGADNTVRLYT", "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": "MRLLFLAVLRPHTGNAVTAQRVRAHLEAAGHVCVLKDAFDFESRSEIANLILAENCEAALALHLYRGGRLLQGHRIPFGVIFGGTDVNEDANQAEKNTVMGRVLEEARFAVAFTESMKEMAQAQWPHAKGKVYVQSQGIATTPNAAFNWNTFLQRSEINQSADNLHIFLLICGLRQVKDPLYLVDAFSAWHQEEPNVHLVIVGPEVDPVFTREVKAKVKRAAGVRLIGEMPQEDLHAVVKNCFAVVNSSVSEGMSAAILEAMDLEVPVLARNIPGNAAVVKHEVTGLLFSNPQEFVHLAKRLVSDPALEKEIVVNGREYVRMYHSWQVERDTYQQLIRKLEGSTED", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
+{"protein": "MMETPAESVRARVSSVTFYNVTQTAGRWWAIWVVGIVPIKREDVETLIVVQACQPPLGGSLEPPVVNAPSTTELNFLRWERELRRSGGLIAMLADAAEKDLFDLSFRTRDRRLLSAARVEDEQGLIFQPLFPAQVVCQSCSGDDGRDQQPPPVDGFGSEMEGEQTCPHAQRHSESPGQLDVYIRTPRGDVFTYSTETPDDPSPVPFRDILRPVTYEVDLVSSDGATGRGGDARRHRVSLKILEPAGGFESWLVNSWSMAGGGLYAFLRSIYASCYANHRGTKPIFYLLDPELCPGGSDFQPYVPGFPFLPIHYVGRARPAFWHRAPHSEGLLLLDLNLGVSGTPLADALLGLDARSGQRRGSLLLQQIWPPTRKEINPRHVCTREGGEGGGEDETTVVGRAEATAILEADATWWLYELARCHLSARGAPVGTPDGGGQARDAQTWLRALHRYGTSDTRRALGGLYTAVTRVLLHAAADLGLTWAYADEFILGFVAPTSAHPSEEPLAQAFLQGVKDSEDASRLDRDVMGGEATVARRHIRVKARRGPGCLLMAIFQGDLYVGGCREHSGPFLVWHEAFSWTLDQLAARPEADKAPPSHDHLLTLVRDLTRRLAPGRRRNRFWALPRAWLQRLRRAGLRLSGSHVCLLDKDGARPAPCQTATEHGLSPTAYFREIMAFLLDVISALHPGYTIPMEITRETDLLMTVLSLF", "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": "MTTTLQQRESASLWEQFCQWVTSTNNRIYVGWFGTLMIPTLLTATTCFIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVVFHFLIGIFCYMGRQWELSYRLGMRPWICVAYSAPVSAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTEVESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVIGIWFTAMGVSTMAFNLNGFNFNQSILDSQGRVIGTWADVLNRANIGFEVMHERNAHNFPLDLASGEQAPVALTAPAVNG", "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": "MKIAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRISRVKGKTLFEMAESEPSLDYVCEFYLNIADQLLARPEGVVPKEVPDRELFSLLSDFYLNPANNASSIEQPTDSIVQSEQEPFLII", "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": "MSEIKDVIVQGLWKNNSALVQLLGLCPLLAVTSTATNALGLGLATTLVLTLTNLTISTLRHWTPAEIRIPIYVMIIASVVSAVQMLINAYAFGLYQSLGIFIPLIVTNCIVVGRAEAFAAKKGPALSALDGFSIGMGATCAMFVLGSLREIIGNGTLFDGADALLGSWAKVLRVEIFHTDSPFLLAMLPPGAFIGLGLMLAGKYLIDERMKKRRTEAAAERALPNGETGNV", "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": "MMKQVDMYKRVALIALMGMSLAGCSTVKGWFAGKDAAAKKAQEPAELVKFEPSVKVDKLWSTGVGKGEGHIGVRQRPAVADGKVYAAAITGGVQALDLQTGKRVWEYKPKKEERNDRKFKQRLSGGPGVGEGLVVIGTLSGDVIALNQADGTEKWRAKVPNEVIAAPAIAQSLVLVRSNDGRVSAFDAATGERRWFHAEEGPTLSVRGNAPIVTGPGVVFVGNDVGTLSALALQDGRPLWEQAIGVPEGRTELERMSDVDGAPVLDGTTLYATSFKNETLALEGPSGRPLWTRDHGGAGGPGVSSSVVVVADNAGSVWGLDKSSGAAMWSQAALARRSLTGVAIQGDYAVVGDYKGYLHWLKLSDGALAARARAGRDTLLAQPLVVDGILLVQNTDGDITAFRLAQ", "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": "MPEEPVDSDASKLLESLSINKQGDSAPIKDEKPVVESENKVSDEQNSEPTKEPETKTETENNDSNLISSSYEVQVKLADLQADPNSPLYSVKSFEELGLSPELLKGLYAMKFNKPSKIQEKALPLLISNPPKNMIGQSQSGTGKTAAFSLTMLSRVDVNDPNTQCICLSPTRELARQTLEVITTMGKFTKVTTQLVVPQAMEKNQGTQAHIVVGTPGTLLDMIKRKLLRTGKVKVFVLDEADNMLDGQGLAAQCIRVKKVLPTSCQLVLFSATFPTEVRKYAEKFVPNANSLELKQEELNVDAIKQLYMDCDSEKHKAEVLSELYGLLTIGSSIIFVKTKATANYLYAKMKSEGHACSILHSDLDNSERDKLIDDFREGRSKVLITTNVLARGIDIASVSMVVNYDIPVDKDDKPDPSTYLHRIGRTGRFGRVGVAVSFVHDKKSYEDLEQIRSYFNDIEMTRVPTDDWDEVEKIVKKVLKK", "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": "MKTIIALSYIFCLAFAQDLPGNDNSTATLCLGHHAVPNGTLVKTITNDQIEVTNATELVQSSSTGKICDNPHRILDGINCTLIDALLGDPHCDGFQNEKWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFINEGFNWTGVTQNGGSSACKRGPDNGFFSRLNWLYKSGSTYPVQNVTMPNNDNSDKLYIWGVHHPNTDKEQTDLYVQASGKVTVSTKRSQQTIIPNVGSRPWVRGLSSRVSIYWTIVKPGDILVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIGTCSSECITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQTRGIFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQTAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEDMGNGCFKIYHKCDNACIGSIRNGTYDHDVYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLLCVVLLGFIMWACQKGNIRCNICI", "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": "MERRIFGIETEYGVTCTFRGQRRLSPDEVARYLFRRVVSWGRSSNVFLRNGSRLYLDVGSHPEYATAECDDLSELVVHDKAGERILEGLLVDAEQRLAEEGVTGDIYLFKNNTDSAGNSYGCHENYLVGRHGEFSRLADVLIPFLVSRQIVVGAGKVLQTPRGAIYCISQRAEHIWEGVSSATTRSRPIINTRDEPHADAERYRRLHVIVGDSNMNETTTLLKVAVTDLVLRMIEAGVPIRDMTLENPIRAIREISHDMTGRRKVRLANGKEMSALEIQSEYHSRAAEFVDREGFGPVHRQMLELWGRVLKAVDTGDLSLIDREIDWATKYQLIERYRAKRDLPMSSPRIAQMDLAYHDISRTRGLYYLLERNNQVDRVAHEPRVFEAKNVPPQTTRARLRGEFIRRAQEKRRDFTVDWVHLKLNDQAQRTVLCKDPFKAVDERVDKLIASM", "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": "MATHEEFIRTQVFGTVFEITNRYTDLNPVGMGAFGLVCSATDTLAGQPVAIKKIMKPFSTAVLAKRTYRELKLLKHLRHENLICLQDIFLSPLEDIYFVTELQGTDLHRLLQTRPLEKQFVQYFLYQILRGLKYVHSAGVIHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFSEMIEGKPLFPGKDHVHQFSIITDLLGSPPRDVINTICSENTLKFVTSLPHRDPVPFQERFKTVEPDAVDLLERMLVFDPKKRITAADALVHPYLAPYHDPTDEPTAEAQFDWDFNDADLPVDTWRVMMYSEILDFHKIGGGDGQIDTNAAFDDQVAAATAAAAHAAAMAQHHHQTQQQSSGKHTNPTTSSSAATHNSNGPHSNHDAIANYGNQAVHYANEFQQ", "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": "MSAQIENSIPLDFDLGNMAAFDISPLDETKLSGSEKESFLFSLSRDNVQQLVNKMISLPKERTSDGVLLQLPETVTPLPRAKPLPKPKPETKWQRFARIKGIAPKKREGRLVFDEASGEWVPKWGYKGKNKELETQWLVEEGEKEKKLTSKQVRNTSKKIKRSRRH", "text": "FUNCTION: Involved in ribosomal large subunit assembly. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRS1 family."}
+{"protein": "MSQQALADKPLLSRGMIAVLCAQFFSAFGDNALLFATLALIKQQLYPDWSQPILQMAFVATYIVLAPFVGQFADSFAKGRVMMVANGLKLAGALVICFGFNPFLGYSLVGVGAAAYSPAKYGILGEITSGEQLVKANGMMEASTIAAILLGSVAGGVLADWHLGVALGVCALVYAIAVVANMFIPKLAAARSGSSWRPRAMTGSFFTACLVLWRDGEARFSLAGTSLFWGAGVTLRFLLVLWVPIALGITDNATPTLLNAMVAIGIVVGAGAAARFVTLKTVKRCLPAGVLIGVAVAIFALQHSMPMAYLLLIIIGILGGFFVVPLNALLQERGKNSVGAGNAIAVQNLGENTAMLLMLGLFSVVVKLGVPVIAVGVGFGVIFALAIALLWGWQWRQQRQKTAE", "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": "MKYDTSDLCDIYHEEVNVVEPLFSNFGGRTSFGGKITTVKCFEDNGLLFDLLEENGLGRVLVVDGGGSVRRALINAELADLALKNEWEGIVVYGAVRQVDELAELDIGIQAMAAIPVGAADEGIGESDIRVNFGGVTFFSGDHLYADNTGIILSEEPLDIE", "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": "MDNFLALTLTGKKPVITEREINGVRWRWLGDGVLELTPLTPPQGALVISAGIHGNETAPVEMLDALLGAISHGEIPLRWRLLVILGNPPALKQGKRYCHSDMNRMFGGRWQLFAESGETCRARELEQCLEDFYDLGKESVRWHLDLHTAIRGSLHPQFGVLPQRDIPWDEKFLTWLGAAGLEALVFHQEPGGTFTHFSARHFGALACTLELGKALPFGQNDLRQFAVTASAIAALLSGESVGIVRTPPLRYRVVSQITRHSPSFEMHMASDTLNFMPFEKGTLLAQDGEERFTVTHDVEYVLFPNPLVALGLRAGLMLEKIS", "text": "FUNCTION: Transforms N(2)-succinylglutamate into succinate and glutamate. SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily."}
+{"protein": "MFPAMLNVGLGLRRGLLPELLAMEAGAVDFLECAPENWIAVGGAYGKGLAQLAERFAVTCHGLSLSLGGSAPLDRHFLEQTRQFLDRYQVRLYSEHLSYCSDDGHLYDLMPIPFTDEAVRHVAARIRQAQEQLERRIAVENISYYAAPYQAMSELDFIQAVLEEADCDLLLDVNNVYVNACNHGYDAQQFLAGLPQARVAGMHVAGHYDEAPDLKVDTHGAAVKEDVWALYASACARFGVQPTVLERDFNYPPLAELLAETARMRAVQCAAGGQADE", "text": "SIMILARITY: Belongs to the UPF0276 family."}
+{"protein": "MRVLLVGAGGRENAIAEVLARDAELYVVAGHKNPGIARLAKDYALAKETDVPRVLDFALKWGVDMAFIGPEAPLEKGIVNVLEENGVPTVGPTREAAMLETNKAFARWLMEEYKIPGRKLFKVFDDVSEMKSWIDDFGRPVVVKPLGLTGGKGVKVVGYQLKDNEEAKAYAEELIKRDGKVLIEERTDGVEFTFQVFTDGKRVVPMPLAQDYPHAYEGDVGPITGGMGSYSCEDHRLPFITKEDYEKALETLKATVEAMRKNGTPYKGILYGQFMLAKDEPKIIEFNARFGDPEAMNVLPILKRSLVEIGEEIVDGNLKGAEFERKATVVKYIAPKGYPTNPVRGIKLHVDEAKIREEGARVYYASLDENFRMLGSRALAVVGIADSLEEAERIASAGIRHVRGEIFYRKDVGTRESIARRIELVRAMRGE", "text": "SIMILARITY: Belongs to the GARS family."}
+{"protein": "MTKTLPEDFIFGGATAAYQAEGATNTDGKGRVAWDTYLEENYWYTAEPASDFYNRYPVDLELSEKFGVNGIRISIAWSRIFPNGYGEVNPKGVEYYHKLFAECHKRHVEPFVTLHHFDTPEVLHKDGDFLNRKTIDYFVDYAEYCFKEFPEVKYWTTFNEIGPIGDGQYLVGKFPPGIKYDFEKVFQSHHNMMVAHARAVKLFKDGGYQGEIGVVHALPTKYPFDPSNPEDVRAAELEDIIHNKFILDATYLGKYSRETMEGVQHILSVNGGKLNITDEDYAILDAAKDLNDFLGINYYMSDWMRGYDGESEITHNATGDKGGSKYQLKGVGQREFDVDVPRTDWDWMIYPQGLYDQIMRVVKDYPNYHKIYITENGLGYKDEFIESEKTVHDDARIDYVRQHLNVIADAIKDGANVKGYFIWSLMDVFSWSNGYEKRYGLFYVDFETQERYPKKSAYWYKELAETKEIK", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
+{"protein": "MGLTSQLLPPLFFLLACAGNFAHGHNCHIALREIIETLNSLTEQKTLCTKLTITDILAASKNTTEKETFCRAATVLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEASQSTLEDFLERLKTIMKEKYSKCRR", "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": "MTLDVFTKVVSQADSRGEFLSNEQLDALANVVKEGNKRLDVVNRITSNASAIVTNAARALFEEQPQLIAPGGNAYTNRRMAACLRDMEIILRYVTYAILAGDASVLDDRCLNGLRETYQALGTPGSSVAVGVQKMKDAAVGIANDPNGITKGDCSQLISEVASYFDRAAAAVG", "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": "MVTSSSVIGLTLWAALVSASPVADPLVTPAPKLEDLEKRATSCTFSGSEGASSASKSKTSCSTIVLSDVAVPSGTTLDLTDLNDGTHVIFEGETHFGYEEWSGPLVSVSGTDITVTGADGAYLNGDGSRWWDGEGSNGGKTKPKFFYAHDLTSSTISGIYIQNSPVQVFSIDGSTYLTMEDITIDNTDGDDGEAANTDGFDIGDSTYITITGANVYNQDDCVAVNSGENIYFSGGVCSGGHGLSIGSVGGRSDNTVKNVTFYDSDIKSSQNGVRIKTIYGDTGSVSEVTYKEITLSDITDYGIVVEQNYDDTSESPTDGITIEDFVLDNVQGSVESSGTNIYIVCGSDSCTDWTWTDVDVTGGKTSSDCENVPDDISC", "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": "MNIIPRTSLIIYLKHMKHERQIRKYGHIVHSNRQRKYVVMYINEADADNIVHKLMQLKYVHDIQGSPYKYLKKTYEKEKHEIQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0298 family."}
+{"protein": "MPEPQEGETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLESGKELFIKIIPNKEAGTLTLIDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVVVTSKNNDDEQYVWESSAGGSFTVRPDSGEPLGRGTKIVLHIKEDQLEYLEESKIKQIVNKHSQFIGYPIKLLVEKEREKEVSDDEAEEEKKEEKEEKKDDEPKLEDAEDDEDKKDKKKKTVKVKYTEDEELNKTKPIWTRNADDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLDFRALLFVPRRMPFDLFENKKKKNNIKLYVRRVFIMDNCEELIPDYLNFIKGVVDSEDLPLNISREMLQQNKILKVIRKNLVKKCLELFEELAEDKETYKKFYDQFSKNLKLGVHEDSQNRQKLADLLRFNTSASGDEYCSLNDYVGRMKENQTQIYFITGESIDQVKNSAFVERVKKRGFEVIYMTEPIDEYVIQQLKEYKGKQLVSVTKEGLELPEDEAEKKKREEDKAKFENLCKVMKSVLESKVEKVMVSNRLVDSPCCIVTSQYGWSANMERIMKAQALRDSSAMGYMAGKKHLEINPDHAIIETLRQRAEADKNDKAVKDLVILLFETALLSSGFSLDEPGTHASRIYRMIKLGLGIDEDEPMTTEESSSGAAAAAPASGDAPPLVDDSEDLSHMEEVD", "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": "MTVVVVTGTDTGVGKTVACAALACHARQAGIEVAVCKPVQTGTQIGDDDLAEVARLSGVTELTGLVRYPQPLAPAAAAEHAGMALPTREQLLELIAGLDRPGRLILVEGAGGLLVELADASATLRDLAVELGALALVTVSVELGTLNHTALTLEALTTRGVACAGLVIGSWTGRPGAVQISNRSALARLAPMRATLPAGAGSMDATDFAAMSAAAFDRDWVTTLVH", "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": "MDFLPLFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEQGGGELLERDYQDGDQPGCVLIIAATDDEPLNAEVSRAANARGIPVNVVDAPALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWIPSTYGQLAGLASRFRHRVKELLPDLQQRRVFWENLFQGEIAERVLAGRPAEAERLLEEHLAGGLAHIATGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGTTDLPWQDLVAPGQTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVVQLRDKLAWFEGAREDA", "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": "MSAQVSLELHHRISQFLFHEASLLDDWKFRDWLAQLDEEIRYTMRTTVNAQTRDRRKGVQPPTTWIFNDTKDQLERRIARLETGMAWAEEPPSRTRHLISNCQVSETDIPNVFAVRVNYLLYRAQKERDETFYVGTRFDKVRRLEDDNWRLLERDIVLDQAVITSHNLSVLF", "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": "MDPLKAQQLAAELEVEMMADMYNRMTGACHKKCVPPHYKEAELSKGESVCLDRCVSKYLDIHERMGKKLTELSLQDEELMKKMQQGVTST", "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": "MAWTPLLLLLLSHCTGSLSQPVLTQPTSLSASPGASARFTCTLRSGINVGTYRIYWYQQKPGSLPRYLLRYKSDSDKQQGSGVPSRFSGSKDASTNAGLLLISGLQSEDEADYYCAIWYSSTS", "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": "MSQGLIETTTIVETRELGHQIHASLLEQLKLQQEELLQQQRDLFFQEQQLQQQANHPVSNNGNTWSFTQGLVIGQISVIFIIIVFVKFFVFADSSSHIPTKPGLDGATGVIVKRNKKKQHLNGQFANDDGNEDDISLNSNESKISSILEKTYYDVNNHASESLDWFNVLVAQTISQLRSEALLKDNIYHSLNNFLTNAKLPDFIDTINLTEIDIGDDFPIFSNCRIKYGEDLKRLEAKIDVDLSDTLTLGIATKLLLNQPRPLTAVLPVSLTVSIVRFSGCLTVSLINTKDIDLKNFNKASNMNGYSKENGSADSASDNDEDEDDGGTALMFSFSPDYRLEFIVKSLIGSRAKLQDVPKISSLIENQLRTWFIERCVEPRFQVVRLPSLWPRTKNTREPVIKKTPTTSTTINGTSAATVTTPGEFVNSNI", "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": "MDTTTSNPRIEASAKYIRMSPHKARRVVDQIRGRAYEQAPMILEFMPYRVCDSISQLLSSAAANANHNFGLSKTDLFIDAIQVDGGSFLKRIRSGARGRTYPIHKPTCHITIVMRMDSGWRNKISLRRFGK", "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": "MHGLLLAGLLALPLNVLAHPTESHSSGISRRAIDITSYRLPQISKYTKSDAVPKQDDESFTTSSTGDDNVSSGDYVTTATDWLKKTLPKATYRLVNDHYIGDSGIGHVHFRQTAHGIDIDNTDFNVNIGRDGKVFSFGNSFYDGEIPKANPMVKRDFSDPVNALQGAIQTLNLPVTAKPENVKAKPVEGKENFKFEGTSGAFSDPKAQLVYLQKDGGLVLSWKVETDIGDNWLLTYVDANKNDKVHSVVDYVSAAEYKVYPWGINDPTEGNRTSIHLPWFKTLSTDWHIDGKGWYSTTRGNNAIAQENPTGGPEYENNYRPKSPLFIFKYPYSEAMTPPSSYRDASITQLFYTTNVYHDVLYILGFNEKAGNFQVNNWNKGGVGGDFAILNSQDGSGVNNANFATPPDGQPGRMRMYTWNASTPERDGCFEAGIVIHEYTHGVSNRLTGGPANSRCLAALESGGMGEGWSDFFATAIRLKAGDTRATDYTMGEWASNRPNGIRKYRYSTNLTTNPHMYVDADGLTSVHAIGTIWASMLYELLWNLIDKHGKGNVTKVRPVLKNGVPTDGRHLAMKLVLDGMALQPCLPNFVQARDAILDADKVLTQGSNKCEIWKAFAKRGLGVGAVFNPSKRTGSNELPAGC", "text": "FUNCTION: Secreted metalloproteinase probably acting as a virulence factor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M36 family."}
+{"protein": "MTDLSITPLPAQAAPVQPASSAELVVLLDEAGNQIGTAPKSSVHGADTALHLAFSCHVFDDDGRLLVTRRALGKVAWPGVWTNSFCGHPAPAEPLPHAVRRRAEFELGLELRDVEPVLPFFRYRATDASGIVEHEICPVYTARTSSVPAPHPDEVLDLAWVEPGELATAVRAAPWAFSPWLVLQAQLLPFLGGHADARVRTEALVS", "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": "MQVLWFIPTHGDSRYLGTSEGAREVSFDYLKQVAVAADTLGYDGVLIPTGRSCEDPWVVASALAAVTRKLRFLVALRPGLMTPTLAARMAATFDRVSNGRLLVNLVTGGDVAELEGDGLFLNHAERYEASAEFIRVWRDLLAASHENGEISFEGKHVTVKGARVLYPPIQRPHPPVYFGGSSEAAHDLAAEQVETYLTWGEPPADVAKKIADVRARAAKHGRTVRFGIRLHVIVRETDAAAWAAADELISKLDDQTVARAQAVFAKMDSEGQRRMAALHAGGTRRTREALEISPNLWAGVGLVRGGAGTALVGDPKTVAARIEEYAALGIDTFVLSGYPHLEEAYRFAELVFPLLPRKVRDKLPGQVLSGPFGEVMATGIVPIASQS", "text": "FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates. SIMILARITY: Belongs to the SsuD family."}
+{"protein": "MFQDNPLLAQLKQQLHSQTPRVEGVVKGTDKGFGFLEADGQKSYFIPPPHMKKVMHGDRITATLHTEKDREIVEPETLIEPFLTRFVGRIHKKDDRLSITPDHPLLKDAIPCRAARDVTHTFQEGDWAVAEMRRHPLKGDRGFHAELTQYITTGDDPLVPWWVTLSRHNLERAAPDVEATERHDGELVREDLTALSFVTIDSASTEDMDDALYVQDNGDGSLQLTIAIADPTAYVDAGSELDKIARQRAFTNYLPGFNIPMLPRSLSDDICSLRPDERRPVLACRVTIAADGALGDDIHFFAAWIESKAKLAYDNVSDWLEEQGEWQPQNDAIAEQIRLLHRVCLARSEWRTTHALVFKDRPDYRFLLGEKGDVLDIVVEHRRIANRIVEEAMIAANVCAAIVLRDKLGFGIYNVHNGFDPVSIDQAVTVLDTHGVQADAQTLLTLEGFCKLRRELDAQPTQFLDSRIRRFQSFAEVSITPGPHFGLGLEAYATWTSPIRKYGDMVNHRLLKAVITGQAAEKPQDDVTVQLAERRRLNRMAERDVGDWLYARYLSDKAGTDVRFNAEIIDVTRGGLRVRLLDNGAVAFIPSSFIHAVRDELVCSQEMGTLAVKGDVVYRQGDTLDVVIAEVRLETRSVVAKPAA", "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": "MSEKNEIYDESQIQVLEGLEAVRKRPGMYIGSTGTRGLHHLVYEIVDNSIDEALAGYCSHIKVFIHKDNSVTVSDDGRGMPIGIHHKMKKPTVEVIMTILHAGGKFGGGAYRVSGGLHGVGASVVNALSETCEVEVKTEGHIWKQTYHRGKVASPFEKIGDSDEHGTKIYFKPDPEIFEDTEYDYDTLSQRLRELAFLNKGIKIELTDERHDKNEIFHYEGGLKSFVSYLNRNKEVVFKEPIYVEGSIDSNYSVEIALQYNDGYNENIFSFANNIHTIEGGTHLAGFKTALTRVINDYAKKFGYLKENDKNLSGEDIREGLTAVVSVKLTEPQFEGQTKTKLGNTEVRGIVDSIISERVSTYLEENPQIGKLVIDKALVASRAREAAKKAREITRRKSVLESTSLPGKLADCSSKDAEECEIYIVEGDSAGGSAKQGRNRRFQAILPLRGKIMNVEKQRIDKILNSEEIKAMATAFGGGIGKDFDVSKLRYHKIIIMTDADVDGAHIRTLILTFFYRYMTELISEGHVFIAQPPLYKVTKTRKEYYAYSDKELEDVLQDVGGKDKNTDIQRYKGLGEMNPEQLWETTMNPEQRTLIKVNIEDAMAADEIFTILMGDKVDPRRKFIEENATKVVNLDV", "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": "MADSESKIYHERQRLQFCLLHCLNNLFQDKDAFTKESLNSIAEKLETNDPNKETWTPLSFVLKPHHNTITGNYDVNVMITALEGKGKSVVWHDKRIGASSIDLDDADTLMGIVLNVPVKRYGGLWRSRHWVVVRKINGVWYNLDSDLVVPQLFRDDDEVRGFLDQNLSLDVIGLIWNLPYNANQLPLASNYRVVITHWSDLNGMFSHVTNYPLDFDVYPQVSSKVSAIYKATGTKRFNANTRPVTPGKQSSVKGPYYKNPGCTTSCGLRLPRKTECTAARLIKDLSCKFVMGLRLVVMRKKKKKRSPPLKKASSSGISQPSVISVVNDNNHRSAAIEDCIQFINSSSSFTRSNSTCGSKS", "text": "FUNCTION: May act as a deubiquitinating enzyme."}
+{"protein": "MDSIINALTSNNFQRTNTPISKPLVVHAVAGAGKTTLIQNLLPEHPNLAAQTAGSPQTPNLTGAFIRKLTCPESNKINLLDEYAALQPLKGSWDVVLADPLQHPGLALRPHFIKSVSHRLCPATTRLISKLVCPCTSSRTEESTIQFSGLFEGPLLGTVIALDQTTQALLTAHGAHFLCPTAALGLEFDTVTVVSALPLEEVADKVGLYISLSRHRSQLHVRSPPPHPSH", "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": "MGETEGKKEEADYKRLQTFPLVRHSDMPEEMRVETMELCVTACEKFSNNNESAAKMIKETMDKKFGSSWHVVIGEGFGFEITHEVKNLLYLYFGGTLAVCVWKCS", "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": "MTVLHSVDFFPSGNASVAIEPRLPQADFPEHHHDFHEIVIVEHGTGIHVFNGQPYTITGGTVCFVRDHDRHLYEHTDNLCLTNVLYRSPDRFQFLAGLNQLLPQEQDGQYPSHWRVNYSVLQQVRQLVAQMEQQEGENDLPSTASREILFMQLLLLLRKSSLQENLENSASRLNLLLAWLEDHFADEVNWDAVADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLMKARHLLRHSEASVTDIAYRCGFSDSNHFSTLFRREFNWSPRDIRQGRDGFLQ", "text": "FUNCTION: Activates expression of the rhaBAD and rhaT operons. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MRVKGGTVTRARRKKWLKLAKGYFGHKSIGYKVAKQAVVKSWTYAFRDRKQIKREFRKLWIARINAATRAEGLSYSKFINGLKRANVTINRKMLSELAISEPKTFAMLIKIARDAK", "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": "MGLYFRVRKSDASARLSELKTKSGTLILPEFFPVYNPNKPVITPREMSEMGIKAIITNSYLIYRSPELREAAIERGIHSLLGFDGVVMTDSGAYQIYRYGRVDVTNSEILRFQHSIGSDIGSILDVPMSSEIGREEAESGVERTIRNAEEWASMREELSNTLWVGTPQGSIYRDLVIKCSERIRELDFDYNGVGSIKVALEKYDFVTQVDHFMSIRSILRAGKPFHFWGIGHPSTFAFFAAIGADSFDSASYSLYAEQGRYMTPHGTLLLDEIEEFPCSCPVCSSHDPKEVKAMSKEERTKLLAKHNLYISISEIKKVREAIRGEWLWELVQERSRFHPNLYFALMHLLRRYSSLLEAREPLFKSSGLQCSGPESFLRPEVVRARNRLKYIHYNGKFRRVLYGDVPLGLKYLYPFGQTICPYDEEVQDEPEDDEIITCVLSYQYEFPFPKLPAIMRRSKSTGTLREVSLEGKVIGHFRPNDGAFIPTLDGASLILSHLPYPKGRVVVKGLFSDTVARGTTVFVKFVKEADPSIRPKSEVIVVNESDELLATGKAVLSGVEYHQYHPDHPFIIIRRHVKPRSEEKPPEVDS", "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": "MSIVLFLIVFILLSLIVSRYLYSVALNVPSKIDVVFNPIEKLIYRLIGTNLEHMSGKTYIKHFLLFNGLMGGLSFVLLLIQQWLFLNPNHNLNQSVSLAFNTMASFLTNTNLQHYAGETGLSYLTQMCVITFLMFTSAASGYAVCIAMLRRLTGMTDVIGNFYQDITRFIVRVLIPFALIISLFLISQGTPQTLKGNLVIETLSGVKQTIAYGPMASLESIKHLGTNGGGFLGANSSTPFENPTYWSNYAEALSMMLIPGSLVFLFGRMLKTKQQIHPHAIMIFVAMFVMFIGFLVTCLYFEFAGNPELHHLGIAGGNMEGKETRFGIGLSALFTTITTAFTTGTVNNMHDSLTPLGGMVPMVLMMLNAVFGGEGVGLMNMLIYVMLTVFICSLMIGKTPSYLGMKIEGKEMKLIALSFLVHPLLILVFSALAFIVPGASDALTNPQFHGVSQVLYEFTSSSANNGSGFEGLGDNTVFWNISTGIVMLLARYIPIVLQILIVSSLVNKKTYQQHTQDVPINNLFFSSVLIIFIILLSGLTFLPDLMLGPIGEQLLLHV", "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": "MSGARLHTLLPELTTRQSVMVVGAAVIDVIADAYALPWRGCDIELKQQSVNVGGCALNIAVALKRLGIEAGNALPLGQGVWAEMIRNRMAKEGLISLIDNAEGDNGWCLALVEPDGERTFMSFSGVENQWNRQWLARLTVAPGSLLYFSGYQLASPCGELLVEWLEELQDVTPFIDFGPRIGDIPDALLARIMACRPLVSLNRQEAEIAAERFALSAEITTLGKQWQEKFAAPLIVRLDKEGAWYFSNDASGCIPAFPTQVVDTIGAGDSHAGGVLAGLASGLPLADAVLLGNAVASWVVGHRGGDCAPTREELLLAHKNV", "text": "SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
+{"protein": "MAESDWDTVTVLRKKGPTAAQAKSKQAITAAQRRGEEVETSKKWSAGQNKQHTITRNTAKLDRETEELHHDRVPLEVGKVIQQGRQGKGMTQKDLATKINEKPQVIADYECGKAIPNNQVMGKIERVIGLKLRGKDIGKPMDPGPKK", "text": "FUNCTION: Probable transcriptional coactivator. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAGDESGTTLGQPHLYKQDLSTLDVSKLTPLSQEIISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKVYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVNKIPVPVRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQELEVRPGIVSKDHEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLAKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTITPTVDDD", "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": "MTTREKDLQKGLRLLHLLHQTNPYPQTPGTASQRRNRRRRWKRRGLQILALADRIRSLSDSPTEEPLDLAVQRLQELTVEDLPNPPTSTPTAQAFTCIPPVWDQLVPRSNPSSNEGCERDSCEHRKSPMESSQKDSGSNHRDPQEDQTRT", "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": "MSTDKITFLTNWHATPYHAPLYLAQSKGYFKEEGLKVALLEPNDPSDVTEIIGSGKVDMGFKAMIHTLAAKARNFPVTSIGSLLDEPFTGVVYLKDSGITEDFRSLKGKKIGYVGEFGKIQIDELTKYYGMTADDYTAVRCGMNVTKAIIRGDIDAGIGLENVQMVELAEWLASQNRPRDDVQIVRIDQLAELGCCCFCSILYIANDAFLAANPEKVQKFMRAVKRATDYVLAEPAAAFEEYVDMKPIMGTPVNRKIFERSFAYFSRDLKNVSRDWAKVTNYGKRLGILDADFQPNYTNQYLSWTLDADSTDPLGDQKRMAELQKEVACEGGFKRLQVASSA", "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": "MPKDFKPPRTPRKTPYPDRPHKSKSKSQPDREEKQHPSVNELKRRIRDVKRLLAKPDLSADKRVIQERALAGYEKELADEERRRERSRMIKKYHFVRFLDRKTATKEVKRLTRKRDELAKNSDIDEATKQKKLEQLNVRLHTANVNLNYTIYYPLTEKYISIYAEKKKKNEGQNEDEDVQMEGGPTQEEEIVTAATTAQKKAMLQTVEKCMQDGTLDLLREGKLNLNADSVTEGGTKTETKSKPKSKPSSKDTGVKTVGGKENAKPRTKTSDSKRGKSAKHTAPAPAESDSESDGGFFEI", "text": "FUNCTION: Involved in rRNA processing. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the EFG1 family."}
+{"protein": "MMMTKQKSTLTERLNIGGDEVRELKLGATFNPKNTSTAFHTIKYDFKPASVDTSRMATVDVGSNNQVTVTVPNLESSGVPQTVYKGNHKKYTKECLIIFDKETGAITLERLNHNIQVKKTRSEVTNKPSLMSATNAPMSNGAPVPSSAAAGTGSAGKLENSTMRISSKTKVSTGSRRNNIIDFKPRNSPMQQSSPSRPVASHRSPQSAPAWHANNAQQTLPSIPMIMDDDDFGLSAALHNGSQANISGSSTGSSAGQPDYASVHSGKQRQATPQGHAKRQQLTQRSSPPMQQQQHQNYGRGSNNYAQQQQQQQQQQLQQRASFSHSNHSNSMPMDMDSPTHNEQTAQSMAQAAAALEQQIGGELSASSSSSESDSSDSDSGSDSDDSTEDDRPNHHTNQQLPPAQQPQHHHMQHQQQQHMHQLPNLELGSVSPAYNSHHHHQQQQQSHHHHHHQQQQQQQHQQSGIYASNGGFPNDLLQNDLQLSSNSSDDDDD", "text": "FUNCTION: Promotes transcriptional elongation by Su(Tpl)/ELL. Essential for development (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EAF family."}
+{"protein": "MSSYKVVIVGGGPVGALAGLYAAQRGFQVEIYEMRDEYSQVQTATAFSAKSISLTLSERGIKALRHSQCRGLAERILSTTVPVYGRMVHSRSKKRLTSRRIAYDVHGQALYAISRSEINQSLLEELSAFPNVHIFYKHRLNGLDMKQKCATFHNISRPQEPSHETKFDLLIGADGAHSTTRFFLSRYAKININQKWEDIFWCELTIPAGHALPMDCLHMWPQRDFMLFACPDKEGTLTCNLFAPENVFLELKSSGRIVEFFEKNFPGITPDLIPTDNLQKQFKSNLHHPMIDIRCSPYHYQDSCVLIGDAAHAMVPFYGQGMNTGFEDVRILFEDFLDQRRSFPSWKDNLSLSYAMQQKELPDTPQAIVEDYLEQYTKYRQPDVHIINELALQNYRELRQGVFKMSYHIRKHIEEFLSLHAPQLGWATQYRLVAFETMRYTDVLRQVRKQGLILSAVAWSCLLLFFLLCLLSLRL", "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": "MPDLHRLALSALQYRPVGAQSGNASSAAASCTGDYMAGDSSLERDCGRLADGCSFPQVRGSATGVSDQSLGGSIHFSNAGRDEYVVELGRLLDLTDGVAQPKKLFDLLSAFAFKFGCKWLAYGPLTSDHKALNRVKCDSEEILNYPDGWRERCLEMGYETIAPVIKESRMGAGPIRWSDMYSDASTTEYERRMFDEAAMFGLRSGITVPLRGPRGSCAIMSFARHCEREFHDRTIAYLQLAATHFHLRVAKIANLNAVQKIPALSLREKECVLWVARGKSSWDIGVIMRISENTVNFHIKNVMRKLGTSSRTVAAIKAISLGIIEL", "text": "SIMILARITY: Belongs to the autoinducer-regulated transcriptional regulatory protein family."}
+{"protein": "MLKLIQNNREITALIAILCLFGLLSVIDHQYFSLQTVTLVFSSAQILILLAIGATLVMLTRNIDVSVGSIAGLCAVIMGMSLNAGFNLPVSCLLTLLLGMCAGFINGALVTWLKIPAIVTTLGTLGLYRGLMLLLTDGKWIEXLPDELKRLSAPLWLNISPIGWLLMILILAMAWILAKTTFGRNFYATGDNLQGARQLGVRTDSIQIIAFSVNGIMAALAGIVFASQIGFIPNQTGSGLEMRAIAACVLGGISLLGGTGTVIGAILGAFFLTQINSGLVLLKLPAWWNDFIAGFVLLAVLIFDGRLRCAIEKISANKNMPVSSKMTKVIR", "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": "MAQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKDH", "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": "MLGDDKDSDDLNLFLNAIGEAGDEEGPTSFNDIDFLTFDDEDLHNPFQDCETSPINEPPKVYVAPRVMISHQDSFSEDSRTDVIEDARILPASPRLRVPASPRAFVYPRSVESPRFGSPRSVESPCFGSPIGVIDTASPFESVREAVSKFGGITDWKAHKIQTIERRKMVDEELEKIQEAMPEYKREAELAEEAKYDALEELENTKGLIEELKLELEKAEKEEQQAKQDSELAQMRVEEMEKGVANEASVAVKTQLEVAKARQVSATSELRSVREEIEMVSNEYKDMLREKELAAERADIAVLEAKEIERTMDGLSIELIATKELLESVHTAHLEAEEKRFSVAMARDQDVYNWEKELKMVENDIERLNQEVRAADDVKAKLETASALQHDLKTELAAFTDISSGNLLLEKNDIHAAVESARRELEEVKANIEKAASEVKKLKIIAGSLQSELGRERQDLEETKQKESTGLARTNDKDAGEELVETAKKLEQATKEAEDAKALATASRDELRMAKELSEQAKRGMSTIESRLVEAKKEMEAARASEKLALAAIKALQETESSQRFEEINNSPRSIIISVEEYYELSKQALESEEEANTRLSEIVSQIEVAKEEESRILEKLEEVNREMSVRKAELKEANGKAEKARDGKLGMEQELRKWRSENGKRRTDEGREPEKSPTRSSTEGRNKENGFGQSKSFAFGEQGSSSNNTGGSTTTNNNNLTPETKKKKKKLSLFPKVFMFLSRKKSHSHK", "text": "SIMILARITY: Belongs to the WEB family."}
+{"protein": "MTENKSFKESHPLDDFISDKELSNTTIQKEKLTIEQQKQVDTISKQINPLDNEGLLAFGSDLQKQMSQFSHQMLDEVQSKDVGPIGDTLSDLISKLKSVNPNELNTDKPSMLKRIFSRAKSSINEIFSRMQSVSAQVDRITIQLQKHQTHLTRDIELLDTLYDKNKQYFDDLSLHIIAAQQKKLQLENEKLPQLQQQAQQSTNQMDIQHVADMQQFIDRLDKRIYDLQLSRQIALQTAPQIRMIQNVNQALAEKIQSSILTSIPLWKNQMAIALTLMRQRNAVAAQRAVTDTTNDLLTANAEMLKQNAIETATENERGIVDLDTLKRTQRNIIETIEETLIIQQHGREERQLAEKELQQLEQDLKSHLVNIKGTNKQS", "text": "SIMILARITY: Belongs to the TelA family."}
+{"protein": "MNSTSLYAAIDLGSNSFHMLVVREAAGSIQTLTRIKRKVRLAAGLNNDNHLSAEAMERGWQCLRLFAERLQDIPQPQIRVVATATLRLAVNAGEFIAKAQTILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFSDRNLAQENFDDAEKAARDVLRPVADELRFHGWKVCVGASGTVQALQEIMMAQGMDERITLAKLQQLKQRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFTELNIQSMTLAGGALREGLVYGMLHLAVDQDIRSRTLQNIQRRFIVDTDQANRVAKLADNFLKQVENAWHIEPISRELLLSACQLHEIGLSVDFKQAPYHAAYLVRHLDLPGYTPAQKKLLATLLLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAILFAGRRRDDLVPEITLRALNENLTLTLPGDWLAHHPLGKELIDQESQWQSYVHWPLDVR", "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": "MSIQTQEAHDMSLKSLSLIATHSHIVGLGLDENLQPKPSSQGMVGQLQARRAAGVILKMVQNGTIAGRAVLVAGPPSTGKTALAMGLSQSLGADVPFTAMAGSEIFSLELSKTEALTQAFRKSIGVKIKEDTELIEGEVVEIQIDRSITGGHKQGKLTIKTTDMETIYELGNKMIDGLTKEKVLAGDVISIDKACGKITKLGRSFARSRDYDAMGPDTKFVQCPEGELQKRKSVVHTVSLHEIDVINSRTQGFLALFTGDTGEIRSEVRDQINTKVAEWKEEGKAEIVPGVLFIDEVHMLDIECFSFINRALEDEFAPIVIMATNRGISKTRGTNYKSPHGLPLDLLDRSIIITTQNYSEQEIKTILSIRSQEEEVELTEDALDLLTKIGGETSLRYSSNLIAVSQQIAQKRKSSSVDVQDVKRAYLLFLDSTRSAKYLQEYESRYIDDHGRVDISTTGRNADAMDTNE", "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": "MLSMQVVSLISLLVSVCLAQPLPLSKRYFEYENYKVRGVNLGGWLVLEPFITPSLFETFRTNEYNDDGIPYDEYHYCQYLGEDLARDRLKQHWSTWITEADFEDISNTGLNTVRIPIGYWAFELLDDDPYVSGLQEAYLDQAIEWARSYGLKVWVDLHGAPGSQNGFDNSGLRDQVEFQQDGNWDVFKNVLAYVIEKYSRDEFTDTVVGVEVLNEPLGPVIDMDKLKELYNWAYDYLRNDLQRDQILVIHDAFQKANYFDDQLTVEQGAFGVLVDHHHYQVFSPEEVGRTIDEHISVVCEQGKETLTEAHWNVVGEWSAALTDCTKWLNGVGIGARYDGSFVKNQDTSYWIGSCEGSQDISTWTSDKKDNYRKYIEAQLDAYEIRNGWIYWCYKTEDTLEWDYRKLVQSGLFPQPLTNRQFPNQCSSTY", "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": "MNRSVVLILLLNIIVSVVIVLSSHSWFSVCDGLELNTLSVLPILCGQFSPRGVESTIKYFLVQAFSAAMILNVALVQLWLCSSWSVSCPLNSFSSIVLTLALCLKLGLFPCHFWFPDVLQGLSFLQGLLLSTWQKVAPFIILVSVCNIISINVLTTLGCLSVLVGGWGGLNQSQVRKIMAFSSISHLGWICSVLSYSIYVGCIMFVVYIVLSSTVFLINNEGNLYNLSSLARLVYCNNVMGNVLVLVILSLGGLPPLTGFLNKFIALECLLSNNLLVPCAILIVGSLLSLFFYLRISFNSVLCLFPQHSMMLFSWRNVSGYYGNTSFYTVLLSILSSMSILGLLLVPALWSYH", "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": "MRPAKLVKSKASALLYTRNDVSDSEKKATVELLNQQVIQFIDLSLITKQAHWNMRGANFIAVHEMLDGFRTALTDHLDTMAERAVQLGGVALGTTQVINSKTPLKSYPLDIHNVQDHLKELAERYAVVANSVRKAISEAKDEDTADIFTAASRDLDKFLWFIESTFE", "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": "MTDHLKHIGVADPQRIEKYTLRTEAENDILKIYYKKEKGDLFHRSLKVKFPRLQKQLLVDSGGAKRYENTSEIAPNLLHVLDELDKITSKETEQVDVKEKILKDLRHLERVVNNKIKEIERDLDKLSSR", "text": "SIMILARITY: Belongs to the UPF0325 family."}
+{"protein": "MTVGARLRSKAASSLVGRRPLGRSRRAGDEETDAIVEHLEGEDEDPASPDCEREEGGRRAGTPSARRVHLAALPERYDSLEEPAPGDKPKKRYRRKLKKYGKNFGKAISKGCRYIVIGLQGFAAAYSAPFGVATSVVSFVR", "text": "FUNCTION: Regulates drug efflux through modulation of ABCB1 localization and activity. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
+{"protein": "MGFKLISLLLLFLPLLTVTILSGVEQAFASDKALLVTGRNITADGGRSSLRGKKQRRASGCNLFQGRWVFDASYPFYDSSKCPFIDGEFDCLKFGRPDKQFLKYSWQPESCTIPRFDGGAFLRKYRGKRVMFVGDSLSLNMWESLACMIHASVPNAKTTFLKRTPLSTLTFQEYGVTLYLYRTPYIVDISKERVGRVLNLGAIEGGADAWKNMDVLVFNSWHWWTHKGQSQGWDYIRDGSSLVRDMNRLDAFYKGLSTWARWVDQNVDTAKTRVFFQGISPTHYEGREWNEPRKTCSGQMQPLGGSSYPSGQPPSSGVVSKVLSSMKKPVTLLDITTLSQLRKDAHPSSYGGDGGTDCSHWCLPGLPDTWNQLLYAALTM", "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": "MIKGIQITQAANDNLLNSFWLLDSEKGEARCLAAKAEFVEDQIVAVSELGQIEYRELPVDVAPTIKVEGGQHLNVNVLRRETLEDAVNNPEKYPQLTIRVSGYAVRFNSLTPEQQRDVITRTFTQSL", "text": "FUNCTION: Acts as a radical domain for damaged PFL and possibly other radical proteins."}
+{"protein": "MASSNLLSLALFLVLLTHANSASQTSFSFQRFNETNLILQRDATVSSKGQLRLTNVNDNGEPTLSSLGRAFYSAPIQIWDNTTGAVAASPTSFTFNIDVPNNSGPADGLAFVLLPVGSQPKDKGGLLGLFNNYKYDSNAHTVAVEFDTLYNVHWDPKPRHIGIDVNSIKSIKTTTWDFVKGENAEVLITYDSSTKLLVASLVYPSLKTSFIVSDTVDLKSVLPEWVIVGFTATTGITKGNVETNDILSWSFASKLSDGTTSEALNLANFALNQIL", "text": "FUNCTION: This insecticidal carbohydrate-binding lectin is toxic for the cowpea weevil. SIMILARITY: Belongs to the leguminous lectin family."}
+{"protein": "MKILEYDEKTGALRLHVENEDDLWLIHLVLSKGDIVVARTTRDVSMGNDSRRVPMVVELEVEFSEFQPFTSRLRIHGIVRDAPERYGIKGSHHTINLDIGDEIVIIKKWTKGLIDRIRKQAEKNKRVLIVLTDQDELLVALPMEQGIRILTERSLPGVSDEDKSLESVALEVSKEVEQYVKQYSPDAVIIAGPGPFKEIVRDKLKIKPRIYVDNVSSASRAGLNEILRRDIIDEVMRDYQISVASRELERGLSLLAQGSSLVVYGRDEVERASQIGAVETLLVTDDLLTLEDEETRRKTEAIMEAVESKGGKVMIVPKDSPVYLQLKNLTGLLAILRFRIN", "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": "MKIAILSRDGALYSCKRLREAAEARKHSVEIIDPLSCYMNINSAAPSVHYRGRRLDKYDAVIPRIGSQITFYGTAVLRQFEMLGSYPLNNSVAVIRARDKLHSLQLLAREGIDLPITGFAHSPDDTGDLIAMVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYVREAQGKDIRCLVIGNRVVAAIERQAKAGEFRSNLHRGGSANNVKITAQERAIAIKATKTLGLNVAGVDILRADRGPLVMEVNASPGLEGIETTTGFDIAGMMIEFIEQNTQRRFATSASISKS", "text": "SIMILARITY: Belongs to the RimK family."}
+{"protein": "MGSLNIQHNGYDADVEKIREEEYPMLKDSIYLDHAGTTPYPKSLMDRFAQEMTTNLFGNPHSASASSQLSTQRIQDIRLRALQFFNADPADFDLVFVANATAGIKLVVEAMRCLPTGFDYVYHQSSHTSLVGVREEARSSVCLDTRQVEDWLSGSCPFDDNEDEERPILFAYPAQSNMDGRRFPLSWSSQICRQSLSPTNKRKTYTLLDAAALVSSSPLDLSNAETAPDFVVLSFYKIFGFPDLGALIVRKEVQDVFLSRRYFGGGTVDMVVCLKEQWHAPKDGFLHERLEDGTLPIHSIIALDVAMDVHAKLFGSMERVAGHTGFLARRLYQGLKGLRHANDELVCAIYSPDPETEESGPLVAFNIRNAQGIWISLAEVEKLATLKGIHIRTGGVCNPGGIASALGLEPWEMKQNFSSGFRCGTDNDTMGGKPTGIIRVSLGAMSTIADVDRFVQFVKEFYCEDTPPILPPPETKLDPSLRNTPELFIKSIVVYPIKSCAGFHVPPGIDWEVRPEGLVWDREWCLVHRGSGQALSQKRYPRMALLRPNLDFTKGELQVTFAGDISSSPGLPSSISVPLSKNPKMYAPKKSGMSSRVCGEEITPQTYASAQINDFFSTVLGVPCVLARFPPGGQGKGMTRHAKAHLQRHQHQQPHPAVSVSTRLTKPAMMPGAFPSPKAVETPPSPPDSDTERSATPTQEAQGPKPRRILLSNESPILAITSTSVDALNQSIALLNPSVSQPISEAVFRANLVLSPSPSTPSASPSNPLTPSPSPSTTSKPTPKPKQKPKQKLNPYEEDTWSSLTIFNSSSFSSSSSSCSTPSSSGFQTTTKFQMLGSCRRCHMVCIDQTTGSKTAGGEPFVTLSKTRRFEGKVFFGVHMGLQAEDEEDGHAEDIEKEGTGMGMGTGTGTGTGTRSMGGNGSVVKVRVGDVVRPSYL", "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": "MAIYKTKNTLKKMNLDYSFRTNSTLVSNSEMFSLLYADTTLQKYYKNIVCQDLCLKQDYKNIMECVSLNKIVCNTSSKHYAGEKESILPAFTALEMITGQKPKYTCAKKSISTFKLRQNQILGCKNSLRGNTMYRFLEKYISIVSTRIKDWSENYSSSNKSNSLTTAYNKDYVVLNSNLFPELQQHDELFQNVTGIEISFSTLSNNVKTSTKTSRYKKDGILLYSAFQMPK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL5 family."}
+{"protein": "MVETQMDKLGFLLNHIGKQVTTKVLSNAHITQTMKEIILENHGVDGGAAKNVSKGKSSPKEKKHWTEFESWEQLSKSKRSFKEYWAERNEIVNTLLLNWDNVRGAIKKFLDDDREWCGRINMINGVPEIVEIIPSPYRAGENIYFGSEAMMPADIYSRVANKPAMFVFHTHPNLGSCCGGMPSICDISTTLRYLLMGWTAGHLIISSNQVGMLTVDKRIIVDLWANENPRWLMAQKILDIFMMLTSRRSLVNPWTLRDLKKILQDYGIEYIIFPSNDFFIYEDERLLMFSKKWTNFFTLHELLDDLETIETKASSTT", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the asfivirus F317L family."}
+{"protein": "MGNYHVTLQASYIAKNVEDVEDAIGVAISQIGKLLNKGSLDYVDIDVGLTICPKCGEPIDCVLVVAKTAIVGILLSMKVFNAESPEHAVRIAKSSIGRALKDIPLEDVDVVEI", "text": "SIMILARITY: Belongs to the UPF0212 family."}
+{"protein": "MEMNKVLHQDLVQATRRILKLGPSELRVTDAGLICKNPNYSVCDAMLKTDTVYCVEYLLSYWESRTDHVPCFIFKNTGCAVSLCCFVRAPVKLVSPARHVGEFNVLKVNESLIVTLKDIEEIKPSAYGVLTKCVVRKSNSASVFNIELIAFGPENEGEYENLLRELYAKKAASTSLAVRNHVTVSSHSGSGPSLWRARMSAALTRTAGKRSPRTASPPPPPPRHPSCSPTMVAAGGAAAGPRPPPPPMAAGSWRLCRCEACMGRCGCASEGDADEEEEELLALAGEGKAAAAAAGQDIGGSARRPLEEHVSRRRGVSTHHRHPPSPPCTPSLERTGYRWAPSSWWRARSGPSRPQSGPWLPARFATLGPLVLALLLVLALLWRGHGQSSSPTRSAHRD", "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": "MASQYSVRKVGAPYTLEHRVYIEKDGVPVSPFHDIPLYANAEQTILNMVVEIPRWTNAKQEISKEELLNPIKQDTKKGKLRFVRNCFPHKGYLWNYGAFPQTWEDPNSIHPETKAKGDNDPLDVCEIGELVGYTGQVKQVKVLGVMALLDEEETDWKVIVIDVNDPLAPKLNDVEDVERHLPGLIRATNEWFRIYKIPDGKPENQFAFTGECKNKTYAMDVVRECNEAWERLITGKTAPGGVSTTNVTVQHSSSRVAPDQLPPLPPNENLPPAPIDSSIDKWFFISGASA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase family."}
+{"protein": "MTTLGQRDRRPDALGSLSVLPDETICVLLEYLAPRDIAHLACVSSVMYILCNEEPLWMSLCLRRAKGPLEYKGSWKKTTLHLEGVTQENDAYRKCFHFDGFMSLYLYKRFYRCNTSLDGFSFDNGNVERRRNISLDEFSKEYDAKKPVLLSGLADSWPASNTWTIDQLSEKYGEVPFRISQRSPNKISMKFKDYIAYMKTQRDEDPLYVFDDKFGEAAPELLKDYSVPHLFQEDWFEILDKESRPPYRWLIVGPERSGASWHVDPALTSAWNTLLCGRKRWALYPPGKVPLGVTVHVNEDDGDVSIDTPSSLQWWLDYYPLLADEDKPIECTLLPGETIYVPSGWWHCILNLEPTVAVTQNFVNKENFGFVCLDMAPGYHHKGVCRAGLLALDDENSEDLEEETHDEEDNTLSYSDLTRKEKRTRMNGGGETENREEDVNGVSKRYNMWKNGFSYDIDFLASFLDKERDHYNFPWSMGNSVGQREMRAWLSKLWVLKPEMRELIWKGACIALNAEKWLRCLEEVCTFHNLPLVTEDEKLPVGTGSNPVYLLSDYAIKLFVEGGLEQSMYGLGTELEFYDILGRADSPLKTHIPEVLASGILFFEKGSYKVVPWDGKRIPDIISSSSFDFDASMLNSEFPFGIWNKTLREHKNQGKPAPDSFGSLSSHVWPYIITKRCKGKIFAQLRDDLTWNDAQNLAFFLGQQLRNLHLLPYPPVTRPELLNVNAVHEELNIPAEWKVFVDALCQKKKDVTSRLENWGNPIPRALMTKIDEYIPDDFFVDLLHVFKETNGGDEIKPCTWIHSDVMDDNIHMEPYADDSVDGQHNSWRPSHILDFSDLTIGDPICDLIPIYLDVFRGDADLLKKLLENYGLPLIRSRSSENGTTKTADSTRKKVLSPSYRTMCYCILHEENVLGSIFSIWDELRTAESWEQVEQTVWSLLNTY", "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": "MRVDDDRFPWDQDSILSRDLLSASSLQLCYENLNRSCVRSPYSPGPRLILYAVFGFGAVLAVCGNLMVMTSILHFRQLHSPANFLVASLACADFLVGLTVMPFSMVRSVEGCWYFGDTYCKLHTCFDVSFCYCSLFHLCFISVDRYIAVSDPLIYPTRFTASVSGKCITFSWLLSIIYGFPLIYTGASEAGLEDLVSALTCVGGCQIPMNQKFVLINFLLFLVPTLVMMTVYSKIFLIARQQAQNIEKMRKQTARASESYKDRVCKRERKAAKTLGIAVAAFLLSWLPYFIDSIIDAFLGFITPTYVYEILIWIVYYNSSMNPLIYAFFYPWFRKATKLIVTGKILRENSSTINLFPE", "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": "MNDTPENPHVPVGEKLQKVLARLGVGSRRDVEVWIAEGRVNVNGSVASLGQRVDSHDAITVDGHLIRREEAAESVRRVLIYNKPEGEVCTRDDPEGRPTIFDRLPRLRTGRWINVGRLDINTTGLLLFTTDGELANRLMHPSYEMDREYAVRVRGEVTEEMIERLLNGVMLEDGPAKFSDIQQAPGGEGFNHWYHCVVMEGRNREVRRLWESQGLVVSRLKRVRFGPVFLTSELTMGRYREMDQREIDILSEEVGLKPVALPGMTTKAREKAERQQRKQARPLARSERPEAGRKRAPRREDGENAARRAPASRPARGPQPSAERKGREQGTPVAERPRESNRKPRPSKPRDERPASAPGDKPAARKPQVKRRPKPAGDGMRPGFRR", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-2605 in 23S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RsuA family."}
+{"protein": "MKQNFFAVDLGATSGRTILGSFIEGGLNLEEINRFPNHLIEVGGHFYWDIYALYRHIIDGLKLVAHRGESIASIGIDTWGVDFVLLGKDGNLLRQPYAYRDPHTVGAPEAFFSRISRSEVYGKTGIQVMNFNSLFQLDTLRRNHDSALEAADKVLFMPDALSYMLTGKMVTEYTIASTAQLVNAHTQRLEPELLKAVGLQEENFGRFVFPGEKIGTLTEEVQKITGLGAIPVIAVAGHDTGSAVAAVPALDRNFAYLSSGTWSLMGVETDAPVITAETEALNFTNEGGVEGTIRLLKNICGMWLLERCRLNWGDTSYPELITEADSCEPFRSLINPDDDCFANPADMEQAIREYCRTTGQPVPEQRGQIVRCIFESLALRYRQVLENLRALSPRPIETLHVIGGGSRNDLLNQFTANAIGIPVVAGPSEATAIGNVMIQAMTVGEATDVAGMRQLISRSIPLKTYHPQDMAAWDAAYIHFKNCVR", "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": "MSALSSENVNGVYIPSALLVFGTFLVKKEFVPYAVALTAVLAGFKLFTGDSKARKVLNPTEFQEFVLKEKTDISHNVSIYRFALPRPTDILGLPIGQHISLAATIEGQPKEVVRSYTPISSDNEAGYFDLLVKAYPQGNISKHLTTLKVGDVMKVRGPKGAMVYTPNMCRHIGMIAGGTGITPMLQVIKAIIRNRPRNGGTDITKVDLIFANVNPEDILLKEELDKLAAEDEDFNIYYVLNNPPQGWTGGVGFVTPEMIKERLPAPASDVKVLLCGPPPMISAMKKATESLGFTKARPVSKLEDQVFCF", "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": "MAPITEEVVHGLKDMIEKLENRVQELEGRLGGESKPKSIAEQMRIVLMGPPGAGKGTQAPRLKEKYCVCHLATGDMLRSQVAKKTELGKEAKKIMDQGGLVSDEIMVNMIKNELDTNTECKNGFILDGFPRTVAQAERLDDMLEARKQKLQHAIELQIDDALLVARITGRLVHPASGRSYHKIFNPPKNDMKDDVTGEPLIQRSDDNAETLKKRLSTYHAQTAPVVEYYKKTGIWRGIDASQEPGQVWKSLLGVFQK", "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": "MSESHLYTYGIIDDNESLALNVDGVAGATRAYTVSYRSLSAVVSDIETTDPERTDAAVEAHNTVLQAVLEHDATRAVVPMSFGMAFKNARTLKGVLRGARRALRSTLTEIAGTVELGVKVLAPGDDTAVDTAAVRSDVTARLSALSVGETENDCFTDRLIINKSYLVEHDTRDAFDAAIDEIDAAHDDLTVRYTGPWPPYNFVDIHIGAEQAQQGGR", "text": "FUNCTION: May play a structural or regulatory role in gas vesicle synthesis. SUBCELLULAR LOCATION: Gas vesicle."}
+{"protein": "MKKINILVPDLPESISDATVVKWHKKIGDTVHCDDNIVDIETDKVMLEVSSPCDGILQSILEKEGKVVISQQTLGEINKSTVVDNHLSNNHIIEKEDNLLKKEEKYITTEEKKEIEYLLKDNHKHLTPSMRRSVKIHNINNGFLNQVIETSKKTNFENIIKEEKKESNQILFNHNIFNANENNKNNNNKVTNRVKMTRLRQRIAERLLDSKNNTAMLTTFHEVNMKPIILLRKKYGEDFEKKHNVRIGFMSFFVKAVIQALKNFPEINAYIDQTDIVFYKNFDISIAISTPRGLITPVIRNADTMTMAEIEKKIKDFSIKGLQNKINIKELMGGNFTITNGGVFGSLMSTPIINPPQTAILGMHVIQERPVVVNGQIKILPMMYLALSYDHRLIDGKESVGFLINIKNILEDFNRIAIDV", "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": "MARVVPAWLLLPLAVWVVLPTWLSSAKFSSLIERISDPKDLKKLLRTRNNVLVLYSKSEAAAESHLKLLSTVAQAVKGQGTICWVDCGDAESRKLCKKMKVDLSAKDKKVELFHYQDGAFHTEYNRAVTFKSIVAFLKDPKGPPLWEEDPGAKDVVHIDNEKDFRRLLKKEEKPILMMFYAPWCSVCKRIMPHFQKAATQLRGQFVLAGMNVYPSEFENIKEEYSVRGYPTICYFEKGRFLFQYDSYGSTAEDIVEWLKNPQPPQPQVPETPWADEGGSVYHLSDEDFDQFVKEHSSVLVMFHAPWCGHCKKMKPEFESAAEVLHGEGDSSGVLAAVDATVNKALAERFHIAEFPTLKYFKNGEKYAVPALRTKKSFIEWMRNPESPPPPDPAWEEQQTSVLHLSGDNFRETLKRKKHALVMFYAPWCPHCKKAIPHFTAAADAFKDDRKIACAAIDCVKENNKDLCQQEAVKAYPTFHYYHYGKFVEKYDTNPTELGFTSFIRTLREGDHERLGKKKEEL", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the protein disulfide isomerase family."}
+{"protein": "MAGKDRKTIEKNYPGAEVDEGGRFKPLPPADDDAKLLVCEYPSLGVIRLDYDYPPALGDIDHPGSFYYDVFYRVVPGLTFGMCQKGEMPDEIKQRFIDAIKWLDAQGVAGITSDCGFFMNFQDLARTVTDKPVFMSSLCQLPAVVCAYAAHEHIALFTANGESLKPMRDLIKKECGVDPEESRFIIVGCQDVPGFEAVANGDRVDVDSVMPHIVRLAKETVAKYADTAKPIRAILFECTELPPYSDAVRAATRLPVFDAITSCNSFLAALMDNPRFGVNNWHLSWDGSQTDYRYGDNLSADLKAKLVNAEHAENVAAAERKLAKDRQKPKPATGTGTAFDA", "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": "MTTLAIDIGGTKLAAALIDKNLRISQRRELPTPASKTPDALREALKALVEPLRAEARQVAIASTGIIQEGMLLALNPHNLGGLLHFPLVQTLETIAGLPTLAVNDAQAAAWAEYHALPDDIRDMVFITVSTGVGGGVVCDGKLLTGKGGLAGHLGHTLADPHGPVCGCGRVGCVEAIASGRGMAAAARDDLAGCDAKTLFIRAGEGHQQARHLVSQSAQVIARMIADVKATTDCQCVVIGGSVGLAEGYLEQVRAFLMQEPVPYHVALSAARYRHDAGLLGAALLAQGDTL", "text": "FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily."}
+{"protein": "MPSLLLIIFVTELVVQLVNTLGATTINDLLWRIYLTLPTPLSLEFAQQRRKQKEYLAVRHELKATSSQDEFAKWAKLRRQHDKLLEDLEKKKASLEAARTKFDRTLTTTRTVSTRSVQWFLPFWYSKEPMFWLPYGWFPYYVEWFASFPRAPMGSVSIVVWQWACTAVIALMIEAATAALVYVAAKQSQKIRQPVPAQSEKKDS", "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": "MSALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDNLGADAVATGHYARTSLEDEEVFEQKHTKKPDGLFRNRFEVRNPVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLHHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIEDNTVLGTHKGWFLYTLGQRAKISGLREPWYVVEKDGTKGDVLVAPRVDHPALYRDLLRTNRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKILRLGPSAYTLQKGKNRTRVAPEASSDSPGLHPTS", "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": "MANVRKRRKKKNEHKALRLTFITLLMVFLFSCVAAAGVGLAMIKAAPPLDVDKVLNPSEPSVIYDDKNKLVDTVISDTYRTIVSYEDVPDNLKNAFISIEDERFFNHRGIDYKRVFGAFFRNISNKLKGKSALQGASTITQQLVRNTLLSQEVRIKRKVQEMYLSIQLEKKVSKEQILEAYMNTIPLGGSAYGIEAASKQYFGKSVKDLNLIESAFIAGLPQSPSTFYNAAMSQKNTERYINRTKLVLGKMREHNYISKEDFDKSMAYIDKNKIPLKTSNINISRLNYEWFSREIIKQVKKDLMNEYKISPTEADKTIMYGGLKIYGTMDKSLQDFSQNTLDNLDGILGINSKDYSGIIQPEASVSIVDYKTGNVKVLIGGRGKQPPLSFNRATEFYRAPGSTIKPLTVYGPAIDTKTSTAASSYNDAPVPEEIGKLYDKEPYNPKNSPNIYEGKMTLREALMKSKNVISVRIEHELGLKTGAEYGKKFGLTIDDSMDGTSMAALSLGQLSAKTGVSGTNTLGMAAAYGVFGNKGALSKPVVYKKVVDRTGKVLLENKYASSKVMSPEAAYILYDLLKGPVSYTPGATGMKANFGPMARGKTGTSNQSSDLWFAGLSPYYSAAVWIGKDDYSPFTNEFGRYIGSSDAALIWKLIMGEAHKNLEYKTIEKPAGVTEAYVCSKSGKIPSSSCPRDSIKLEYFIEGTIPGEICDYHTGIFNNNKDKDDDDDDKDKDKEDEEENKDEKNEDKKEAKDNTKNKDKDKKKDNDRKIDMDKKPDSSKRKRKMIKPQI", "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": "MTKSQQKLASIEQLSNQDGIISALAFDQRGALKRMMAEHQTEPPTVEQIEQLKVLVSEELTQYASSILLDPEYGLPASDARNKECGLLLAYEKTGYDVNAKGRLPDCLVEWSAKRLKEQGANAVKFLLYYDVDDSEEINIQKKAYIERIGSECVAEDIPFFLEVLTYDDNIPDNKSAEFAKVKPRKVNEAMKLFSEDRFNVDVLKVEVPVNMNFVEGFTEGEVVYTKEEAAQHFRDQEAATHLPYIYLSAGVSAELFQETLTFAHDAGAHFNGVLCGRATWSGAVKVYIEQGEQAAREWLRTTGYKNIDDLNKVLKTTATSWKAK", "text": "SIMILARITY: Belongs to the aldolase LacD family."}
+{"protein": "MMEESGIETTPPSTPPPSTIGTSVPAATTAISTPVPPIFSSPLAAPVFSPLPSFAQPIFSTPLPSSVPPLRTSVPLTYAPPLPVTGVHSPPAHTSVPAAFSSPLPAFSSPPSFPPPPLNTTPGPVLTAPPTGPPVGGFSMSSHYDITKGHAGRAPQTPLMPTYSAAPVTVLPNPVIQAPLAGSGSSITFPEEPEDSRVHTMHVDGSAGGIWGFFKGVAGNPMVKSVLDKTKHSMETVITTLDPGMASYIRTGGEMDIVVTSVKEVKVAAVREAFQEVFGMAVVTGEDGQSNIAPQPVGYAAGLKGAQERIDSLRRSGMIHEKQPAVSVENFIAELLPDKWFDIGCVIIDDPTHGIRLETFTQATPVPLEYVQQAQNLTPQDYNLRWSGLSVTVGEVLERSLAHVCRTDWHVAFTGMSRRQMIYSAAKALAGMYKQRLPPRIL", "text": "SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the PRRC1 family."}
+{"protein": "MEESINPIISIGPVIFNLTMLAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKDYSLFFLCLFLFMVIANNLGLMTKIQTIDGTNWWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSPVFVIPMNILEEFTNFLSLALRIFGNIFAGEVMTSLLLLLSHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKINIEEE", "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": "MKGGFSLNSELQLEADAVIIGSGAGGASVADVLTAAGLYVIMLEEGGHVPSSSASPFASEAFAAAWRGGGLTAAIGRPPIAYAEGRCVGGGTEINSAIAQRADSDLLDQWRKLYKIENFTPDELSQYYGRAETTVNASLTPGPLGRPTDILRLGGEALGWKVSELKRGQRDCKGANRCSFICPNGAKQSMAVTLLPKSMDRGMRLLARTRVDKIRIEKGRAAVVVAQLQDAGGQGVHVRVKAGLVFVCAGAIHTPALLRRSGLRKRIGDTLRIHPTIRATALFDEPVDAHQSRLPLTAVTEFMPEQRIGGSVFTPAVFGLSLAEDWTNRGDLMQAWRLCGSYYGMIRPRGVGSVRPLPGINEPLVSFKLAPEDWISLGQVLTLLGQAMFAAGARKVIPSISGHEGWTNPDEVDEFRNKPLPEKATNLMTIHLFSTCPPGEHRDACAVDSYGRVRGVENLFVADGSVIPEAPGVNPQMTIMALAFRIAEAALSHSSRERAQSAARE", "text": "SIMILARITY: Belongs to the GMC oxidoreductase family."}
+{"protein": "MKAVVLAVAVLFLTGSQARHFWQQDEPPQSSWDRVKDFATVYVDAVKDTGRDYVSQFETSALGKQLNLNLLENWDTLGSSVGRLQEQLGPVTQEFWDNLEKDTDWLRQEMNKDLEDVKTKVQPYLDQFQSKWQEEVARYRQKVEPLGAELREGARQKLQELQEKLAPVGEDLRDRMRQHVDTLRTKLAPYSDKMRDRLAERLAQLKDSATLAEYHTKATEHLKTFSEKAKPALEDLRQGVMPMLESFRVRLMSMIDEASKKLSAQ", "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": "MASRQPEVPALEPSGPLGKMSLPIGMYRRAFSYDDALEDPTPMTPPPSDMGSIPWKPVIPERKYQDLAKVEEGEPSVSPPAPAPPPATDSAEKAPVVKAKATHVIMSSLITKQTQESIQRFEQQAGLRDAGYTPHKGLTTEETKYLRVAEALHKLKLQSGETAREERQPASTQSTPSSSPQASPKQKSRGWFTSGSATALPGPSLSTMDSGSGDKDRSSADKWSLFGPRSLQKSESGGFAIQAYKGAQKPSPMEVMRAQATRRAEEPATFKPPKMDIPVMEGTKQLPRAHSLKPRDLNVLTPTGF", "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": "GHGGASNYVRL", "text": "FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRF amide related peptide) family."}
+{"protein": "MDASQRNRVIALAALFQAASLVKDVAWHGRCDPDEFRTMVGSLFSFEASDVEGIYGNVHRLRRGLQALASQLENRGSGNDMELTRYVIGLLFLERKLMKQPHMIQGVREGIQGAERQRDYFDDPTHESVNAALAQTYQDTISQLGPRIIVQGEQAHLSNSDNAARIRTLLLSGIRAAVLWRQAGGSRWRLLFSRAGLLRETRALLAH", "text": "SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the HflD family."}
+{"protein": "MAAGRGERAGQSAEGPKQYRLIGAEAVLARTLRAFTDCPLIGTIAVVIHPDDHALYRRAVPEKHENVILVTGGPTRQESTRLGLLALKDEAPQYVLIHDGVRPFIGQDLLERIIANLTPDNGVLPALAVPDTLKRAAADGMVETTISRTGLFAAQTPQAFPYAPILDAHEKAFAINRTDFTDDAAIAEWQEIAVRIIEGSADNTKLTWAKDIEMADKRLRQDHAVFPDIRTGNGYDVHSFEPGDHVTLCGVKIPHEAKLNGHSDADVALHALTDALLATRGAGDIGTHFPPSDSQWKGAASRIFIEHAAKIVREAGGRIANVDVTLISEAPKIGPHRAAMTQALCDMLGIAADRVSIKATTNEKLGFVGRREGIAAIATATVIYPGEVPE", "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": "MNSGIDLQASFIESLNQLGIPSGAAKALWIPFPSFLMIIGATVGVLVVVWLERKISAAAQQRIGPEYAGPLGVLQPVADGIKLVFKEDVIPAKADPWLFTLGPVLVVLPVFVSYLIVPFGQNLVITDLNVGIFFWIALSSIAPIGLLMAGYASNNKYSLLGGLRAAAQSISYEIPLALSVLAIVMMSNSLSTIDIVEQQSGYGILGWNIWRQPVGFFIFWIAALAECERLPFDLPEAEEEIVAGYQTEYAGMKFALFYLGSYVNLVLSALVFAILYLGGWEFPVPLDKLAEWLGVSEDSSWLQVITASLGITMTVLKAYFLVFIAVLMRWTVPRVRIDQLLDLGWKFLLPVSLVNLLLTAALKLAFPVAFGG", "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": "MGRGRIEIKRIENTTSRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSSRGRLYEYSNNNNVKATIDRYKKAHACGSTSGAPLIEVNAQQYYQQESAKLRHQIQMLQNTNKHLVGDNVSNLSLKELKQLESRLEKGISKIRARKNELLASEINYMAKREIELQNDNMDLRTKIAEEEQQLQQVTVARSAAMELQAAAAAQQQQQNPFAVAAAQLDMKCFFPLNLFEAAAQVQAVAAQRQQIIPTELNLGYHHHLAIPGAAAADAPPPHF", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSPIQYDYHHLPHVKTQNQSKKTLWITLVLTLFFTIVEIVGGLLSNSLALLSDSAHMASDVLALGLSMIALYLAMRPPNHRFTFGYLRFEIITSFLNGLTLAIISIGI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To cation A.eutrophus efflux system protein CzcD."}
+{"protein": "MLKQPEMILIDVDGTLVDSVPDLTFCTDTMMERLGLPLRGETKVRQWVGNGVERLIKRALVDNMEGEPEEDLYQKAETIFLALYADNTSKRSHLYPGVNEGLAWLKSQGYRVGCVTNKAAQFTYPLLTELGIIDYFEIVISGDTLPEKKPHPAPLLHAASHFGIAPEKALMIGDSISDVKAARAANFQIVCLSYGYNHGVDIRDSQPDSVIDSLIEIKNLLSQAA", "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": "MAFPAPSSSSPRRRGRGLAYLLVSVLLLASRVPGAAGADSEFEDGVSPKFPGCDNPFQKVKVTYWVDGDERSSLTGITARFGEVLPATGSDGDKRKAVVPAPKTGCAKSSAPLASSIAVAERGECTFLEKAKTAESGGAAALLLINDEDDLQKMVCTQNDTVPNIGIPVVMVSQSAGRKILSGMDGGAKVDILMYAPEKPSFDGAIPFLWLMAVGSVACASVWSFVVVGDEDKNAPTLGGEEAADSEIVELQTKTALVFIVTASLVLLFLFFFKSTWSAWLLVVLFCLSGLQGLHYVASTLIVRTCDRCREAKVALPVLGNVTVVTLVILPLALIFVVVWAVHQNSPFAWVGQDLMGICMMILVLQVVHLPNIKVATALLVSAFMYDIFWVFISPFIFKKSVMITVARGSDEGPSLPMVLKMPKEFDTWNGYDMIGFGDILFPGLLVAFSFRYDRANGKDLTDGYFLCLMIGYAFGLSCTYVGLYLMKSGQPALLYLVPSTLGTIVTLGAKRGELSQLWNAKV", "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": "MNSERSDVTLYQPFLDYAIAYMRSRLDLEPYPIPTGFESNSAVVGKGKNQEEVVTTSYAFQTAKLRQIRAAHVQGGNSLQVLNFVIFPHLNYDLPFFGADLVTLPGGHLIALDMQPLFRDDSAYQAKYTEPILPIFHAHQQHLSWGGDFPEEAQPFFSPAFLWTRPQETAVVETQVFAAFKDYLKAYLDFVEQAEAVTDSQNLVAIKQAQLRYLRYRAEKDPARGMFKRFYGAEWTEEYIHGFLFDLERKLTVVK", "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": "MKAILRSSTRNLITSSRVFKNLRTSEEIRSFLAESTWSISELLQPPTGSSQTEVSPEIVKKMLKLSGLNDLKHDKSVTKALNLQMMLINHLYDNEQDTVTPSRERNDNNGIFRLLASDHLPQQPWDLDDLLKQINELKPDPSKGEVDFTISDLQRDSFVIKKEKNVK", "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": "MESCARRCAVSGLTALSMRLTKQLSAAAASKAGAAGNLVFSPLSIYSVLSVVTAGARGRTLTELLGALGAESREKLAANAGEMARALPAPGGGAAQPGGGPRVAHACGVWHERTRTVRPAFRDAAAASFNAAALAVDFLNNPEEARKEINSWVAAATENLIDTILPPGSVSTDTGLVVTSAIYFNGQWWTPFCKEITEKRAFHRLDGGDVEADFMRSGEDQYIAVHDGFKVLKMPYAACVSARTTTTPRYSMYVFLPDERDGLWSLEDRMAAGGEGFLREHTPERRVEVGEFRIPRFKLSFDDSVVGALQRLGVRDVFKPFVADLADVLEAENSGDDPPLFVSDVKHKAVIEVNEEGTEAAAATAVCLTFASAAPSSRRPARVDFVADHPFAFLVLEESSGAVLFAGHVVDPTDE", "text": "FUNCTION: Probable serine protease inhibitor. SIMILARITY: Belongs to the serpin family."}
+{"protein": "MTNIGSLLVDAAALMVTGMGVVFIFLTILIFLVRLMSKLVPQEVPPPITAPKAVKNQANHTSTVSPQVVAAISAAIHQHRASVAK", "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": "MDKSKRPFIKSKRSFRRRLPPIKSGDRIDYRNISLISRFLSEQGKILSKRVHRFTLKQQRLITLAIKQARILSLLPFTKRKGFERSESTPRTNALKPRNKNKQNNQTQF", "text": "SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family."}
+{"protein": "MASWEKEKELAHLHQPEDDPLPDLSLLLDMDQFEPTEGPDSNPGAEKIYLQLQVAPGDPSEKTYKFGYEDKEAQNPDLKMRNWVPDPEKMSKWACARLILCGLYNAKKAKELLKMDYDIHWEQSKEDSQYFEIEYHCKMCMTVIHEPMPVSYDKKTGLWIKMGPLRGDIGSVVHTCRRHYERCMSALPSSGEPLKPRVRANPVRRYREKSLIVADRPKRSRWGVAPREQPNTSSGDAMALMPGPCGPFNMDPPGCLLERVPGSEPGTSEMALAMSGGPFWEQVYRDSISGPPTGPSEN", "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": "MGFIAQFLEMLLAERALSKNSILSYKRDLFDFQNYLAKHKLSELNITTENIRDWIEYLASNDLQARSINRKISTIKSYYEFLISENHTAFNPVLNVDLPKYQNKLPEILSIAQIKSLLEHCSQDNSPEGIRLNAMIHLLYASGLRVSELVSLKLADILTNKTSKGEVRKIFSVLGKGNKERVIVINEQAVISIAKYLTIRGVFVNKAKPRNLIYLFPSSALAGYMTRQNFAILLKSAALYAGLNPEYISPHILRHSFASHLLEGGADLRVIQELLGHADISTTQIYTHLQTNHLKKALLRHPLNKN", "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": "MTAAETGRGKPRLGGGSGLGGSPAAVVWLHVGATGRDAVSPREPVVAAQAAGRPLKLPRRLLRQPTPGLRGAESGPTVDMPVPSSFNDIGQGWRLRHFVSWLWYEREVTLLERWIQDLCTRVVLRIGSAHFYAIVWVNGVDTVEHEGGYLPFEADISSLFQVEPLPSHLCITIAINNTLTPQPCHQGPSVHDRHLQVGTILPPLHAPTFPPHPVVFLPGTGYPKGYFVQNTDFDFFSYAGLLWSLLLYTTPPTYIDDVTVTTGVKRDSGEGFW", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 2 family."}
+{"protein": "MPKYTPEEVLDLIQKEGVQYVDLRFSDPFGQWQHLTIPAYEISKETFEVGRGFDGSSIRGWQSINESDMLAKPDPNTAFIDPFIEPKTLVMICDIYDPVTGERYGRDTRYIAQKAEQYLKQTGIGDTAYFGPEAEFFIFDSVEFGTAANYAFWRVDSEEGWWNREVPSSGYKIPHKRGYFPAPPVDKMMQLRNEMVSIMSDLGIIVELHHHEVATAGQGEIDIRYDSLLNQADKLFLYKYIVRMVAAKHGKYATFMAKVLPNDNGSGMHTHFSIWKNGENLFAGSEYAGLSKTALYAIGGILKHGPAIAAFTNPTVNSYHRLVPGYEAPVRLAYSARNRSAAIRIPMYSQNPKAKRIEVRFPDATSNPYLAFAAILMAAIDGIENEIDPGEPFDKDIYSLPPEELEGIPQLPGSLEEALKALEEDYEFLLKGNVFTEEFIQLWIESKRAEIDELRFIPHPKEFELYWDI", "text": "FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family."}
+{"protein": "MIIPWQGLAPDTLDNLIESFVLREGTDYGEHERSFEQKVADVKRQLQSGEAVLVWSELHETVNIMPKKQFRE", "text": "SIMILARITY: Belongs to the UPF0270 family."}
+{"protein": "MSLLRHSLQALPLLCLCVLVLACIGACQSEAYEGTPSPPPEQKKSHWNLVQSRMKEFLEPAVTRTRDRWQWLWSLSALRGFMQTYYDDHLRDLGPRTKTWLLESKDSLLNKTYSLCPRLLCADKK", "text": "FUNCTION: May participate in lipoprotein metabolism. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C4 family."}
+{"protein": "MGAPYDFAPERPDHIQQILDGLDRYNPETTGVFQDYVMQQCESQTYDCYANLALLKLYQFNPHLSRDETVTNILVKALTMFPSPDFALGLSLLPSHLLAPLNSSAHNPAAGDAPLSEAVQKLNELRNLLEGADYATFWSTLDSDDLYADLIADVSGFEELMRVRIAATVSQAVREVDRSILESWLNLEGSDFEHFVGSVCGWTIEGAKIKVPMNKDNEAKGTVVRENVKFDQFARVIKRAYEQPA", "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": "MATIQFIQGINEEVVPDVRLTRSRDGSTGTATFRFTNPKILDASMADKGEITGMYLMDTEGQIITRDVNAKFINGKPQAIEAVHVIKSPDDWDRFMRFMERYAQDNGLTFTKASS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the Psb28 family."}
+{"protein": "MDAIKKKMQAMKIEKDNAMDRADAAEEKARQQQERVEKLEEELRDTQKKMMQVENELDKAQEELTGANAQLEEKEKKVQEAEAEVAALNRRIQLLEEDFERAEERLKIATEKLEEASQTADESERVRKVMENRSLQDEERVYQLEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRLLTQRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKEKYKAISEELDQTFQELSGY", "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": "MKKISTFIITKNESARIARAINSVKNITDEVIVVDNESTDDTVHIAKTLGAQVIVKPWLGYVGQKSFAESMCVNDWVLNIDADEELSQELQDEIEYIFTSHNQDRYLAYQIKLLIMYRGDQKPRMFAPLNKCTRLYNKKFASFANTINSTTHDSVVFNKDVDFTGKIYLLNGIAYHYSGTSIEQLVNKANFYSSEQAKDLVKQGKKLSNFRLATEMIWCFLKAFFIRRYFVFGFDGFVDSIIFAFARFLRLAKLRDLSLKSQNVITSDNYINYCMDFKSLLQQKKRNRYPKK", "text": "SIMILARITY: Belongs to the glycosyltransferase 2 family. WaaE/KdtX subfamily."}
+{"protein": "MSFNVDIDEADVAVLNQNLIKSKELFTSISRSLNKISTKSSTASIKIKPILKDVNKLNDNRNQLDSGLNLLSEVSNYASETSKYEAVLNNSIELIGLKKFIDTLTRSKVLLTEMKSNIKRFKGILINFENLIDKSELNLENYFQKSLKSNVMGTNKMNEIILIFQYFYSSSMSGQKTIDKIFMRSQSIKMAEIMRPHEEPTKPIKRSSNIPYEKGSNGINRYNNEMIKAIKGEIGLLNEVGAKINLNASAKDMFVLDIVRKVVNESYAEVIGNFNKVFGQSKILHNDLLILETIENLNHFEKFLNVSNIDVRSFPAFNENYHQLINISSEIFRELIEYSENRVKSVERLTDLNATEAVVELISRIRKLSEYNISLLKLISGMKLGSWLNLKPAVRFISVYTSVIPNLSDDIDETAPEHLLSCFISDYIDSIIINIEIGLKADVSLKKSMQGYYLIKNTILIETIVNRSQQLFNSLGNLGIERLNRLKKRFLKLFLDDWNYASYIIIRDMTTITTTNAVSGHSGSGMSSKEKEQIKDLFKNFNESFEDALRNYEKYNITDVNLRAYLSGEIKKLIMNAYFKLYDKYGSGEFTKNKAKYIKYNKHQFEQILNEKL", "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": "MTVSISSYLMVALILFCVGLYGALTKRNAVVVLLSIELMLNAVNINLVAFSKFGLYPSVTGQIFTLFTMTVAAAEVAVGLAILIALYRNKETVNVDEMNQMKR", "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": "MDHALFTHFVGRPRHCRLEMLILDEQVSKRSWDTTVYHRRRKHLPRRRAPCGPQRPAEIPKRRKKAAVLLFWHDLCWLFRRLFFPREDSEPLMSDPARSPEEEE", "text": "SIMILARITY: Belongs to the HHV-5 UL17 protein family."}
+{"protein": "MAAVEEAQFWQAIGILIKNYHALNKKIFEVVITQVTKQQNGRVCESSAEELAMSLKEDPSQRTCTGFTIGFKLLSKKLAENILGTGIVDFENCLYECQFASDSIEGFSVGLLGGEFKLKSKSNTNWLEFVLRPKLLSWSQSKQDEAKVKSLGLVNVEKYNDLYKELKQRHSQRLLEHWKTAQESTDPLKFIYEDLAIAAYLIVLWSQTQSEPTAFADLGCGNGLLVHVLNAEGYKGYGYDIRKRKLWSLYPPDTQRSLIEKAVEPNSFRLDFPGVDWLIGNHSDELSPWLPVLAGRLNINYFLLPCCPFELSGAKFRRRNTKISAYQDFFQYVTQVSHECGYEILQDRLKIPSTKRLALLGIKRKASKAIEDLEYFVQEELRKYKTGDAKIKLREKEESVRNCTQVDKTIIDGLVFKIFKLILDSNEDKWSGRLPMREIAQALTKEELSGIKSECGGIKTLLRNKHEVFEFCGGDLIGIRTPKPTATLPKSHLTIKKRSCFFKLHHPLGCPLDDAECSFIH", "text": "FUNCTION: Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRM44 family."}
+{"protein": "MKNILSIQSHVVFGHAGNSXAEFPXRRMGVNVWPLNTVQFSNHTQYPEKWTGCVMXAEHITEIVDGIAAIGKLAQCDAVLSGYLGSAEQGRRIVDIVKKVKQANPNAWYFCDPVMGHPEKGCIVPPEVSGVLCEDALPISDIIAPNLLELETLAGGATLHNVDQCVKAARQLCQQGPKIVLVKHLSRAGFRHDRFEMLLVTADHSWHVSRPLVDFGERQPVGVGDLTSGLMLVDLLKGVELKTALEHVAAAVYEVMLKTKEMNEYELQLVAAQDQMVHPTHNFCATQLD", "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": "MDWGREFFKWRGYEETVKLQEELSKKIILEDKFKELRYIGGVDTSSLGEKIVGIITILVFKTLELVEISVALSEVNFPYIPGFLSFREGPVILRAWEKLKIKPDLLIFDGQGIAHPRRLGIASHIGYVLDVPSIGCAKNILVGFYKEPDKRKGSFEYIYHKGEIVGAAVRTKDNVKPVFVSLGHKISLNTSIDIILKTSTKYRIPEPVRLAHLYSKRMLNSEIEGEPF", "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": "MSVGMGVDLEAFRKSQRADGFASILAIGTANPPNVVDQSTYPDYYFRNTNNEDNTDLKDKFKRICERSAIKKRHMYLTEEILKKNPELCAFLEVPSLDTRQAMLAVEVPRLGKEAAEKAIEEWGQPKSRITHLIFCTTTTPDLPGADFEVAKLLGLHPSVKRVGVFQHGCFAGGTVLRLAKDLAENNRGARVLVVCSENTAVTFRGPSETHLDGLVGLALFGDGAAALIVGADPIPQVEKPCFEIVWTAQTVVPNSDGAISGKLREVGLTFQLKGAVPDLISTNIEKCLVEAFSQFNISDWNQLFWIAHPGGRAILDQVEASLNLDPTKLRATRHVMSEYGNMSSACVHFILDETRKASRQNGCSTSGGGFQMGVLFGFGPGLTVETVVLKSIPFP", "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": "MATYKVTLVRPDGSETTIDVPEDEYILDVAEEQGLDLPFSCRAGACSTCAGKLLEGEVDQSDQSFLDDDQIEKGFVLTCVAYPRSDCKILTNQEEELY", "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": "MRSEVVNMLEYLYPLRTYLIVSGVEKPNVMTADWVVPLSFSPQLLGVAIGHSRYTHSLIKECGEFVVAVPTIELLKDVWKAGTLSGAKENKMEKLSLTLVESKKVKVPSIKECQANLECRVVKEVETGDHTLFVGEILHVTHGDAFKDGKPDINYKFVMHASFGKNFTTNSSERFEP", "text": "SIMILARITY: Belongs to the flavoredoxin family."}
+{"protein": "MALQFFSCKPKYTFLSSLLLLLLLSSSVAELSFNFYAGSCPGAELIVRNTVRSASSSDPSVLGKLLRLIFHDCFVQGCDGSVLIRGNGTERSDPGNASLGGFAVIESVKNILEIFCPGTVSCADILVLAARDAVEALGGPVVPIPTGRRDGRVSMAANVRPNIIDTDFTVDKMINIFSSKGLSVHDLVVLSGAHTIGAAHCNTFNSRFKLDPKGNLELIDASLDNSYAQTLVNKCSSSLDPTTTVVDNDPETSSTFDNQYYKNLLAHKGLFQTDSALMEDDRTRKIVEILANDQESFFDRWTESFLKMSLMGVRVGEEGEIRRSCSAVN", "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": "MTARVLPSTTAKPLRLWDISPPVAPGSPVFPGDTPYQQQWAASIAPGCPVNVSTLTLSPHIGAHADAPLHYDPQGATIGAVDLTPYIGPCRVIHAIAKGPLIEWEHLAHAVHDLPPRVLVRTYARMPVERWDPTLAAYAPETVERLAALGVKLIGIDTASIDPAGSKTLDSHQVIRQRGLRVLENLVLDEVPEGDYELIALPLKLMTADASPVRAVLRELP", "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": "MLSVAARSGPFAPVLSATSRGVAGALRPLVQATVPATPEQPVLDLKRPFLSRESLSGQAVRRPLVASVGLNVPASVCYSHTDVKVPDFSEYRRPEVLDSTKSSRESSEARKGFSYLVTAVTTVGVAYAAKNAVTQFVSSMSASADVLALAKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTQKEIEQEAAVELSQLRDPQHDLDRVKRPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRLGPAPLNLEVPTYEFTSDDMVIVG", "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": "MIKERVKMEVIGLEIPLISGNEEYTLAELISKYPLEENDIIVIAETVVSKSEKNVILKDTIKPSNEAIELSKKLGKEPEVVQVILDESNETVRLGPNFIVTETKHGFVCANSGVDESNTSKGIKPLPKNPDKSANEIRKGIEEITGKKVGVIINDSMGRPFRKGSCGVAIGVSGVCGLWDRKGEKDLFGRELKTTEVGIADELAATASVVMGQSDEGIPLVIIRNAPVPFKEGTGKELIRKKEEDVFR", "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": "MGIRNIGIMAHIDAGKTTTTERIIYYTGKSHKMGDVDSGNTITDWMPQEQERGITISSAAITCHWKEHQINIIDTPGHVDFTAEVERSLRVLDGGIVIFSAVDGIQAQTETVWKQAEKYEIPRLAYVNKMDRVGANFFKVVEDIENKFKTIPLVLQIPIGNESNFEGVVDIILNKELHFAMENGIPKLTYSQIREEFIEKTALFKKKLIDILSQFSEEITQLFLEDKEISLDVIKSEIRRGTISRFIIPVLMGTSLKNIGIEPLIDSIVDYLPSPFEKSFTAFSLDTNKKILVDPNENKKLSALVFKVQYSSVIAAHLYFVRVYSGEINSNKKIFNASNGKREKFTKIFRVFSNKNEQIDFVKTGDIGAVLGLKFSVTGDTLIEENNNILLESVMFPEPVVLMSVEPERSSDEVRLKEIFEIISKEDPTFSYSESKETGQLIISGMGELHLEIILTRIKDEFNLNVYTGKPQVSYRESAGKIVKEVFEFNNIFAGKNINFKIGMIIKPLSRGEGNKIDFECSIDSTIKSAILRGITTTFVSGAFGYPIIDINVIIFSIVCEISKISESVFESISGFAFHSIFQKSDPIRLEPIMLLEIRTPIEHTGEIISTLNVIGGVIHSVSNIGEYDLIKSEAAFEKLFGYASILRSSTKGRGSFTMEFSYFKEKVS", "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": "MKYQQLENLESGWKWKYLVKKHREGELITRYIEASAAQEAVDVLLSLENEPVLVNGWIDKHMNPELVNRMKQTIRARRKRHFNAEHQHTRKKSIDLEFIVWQRLAGLAQRRGKTLSETIVQLIEDAENKEKYANKMSSLKHDLQALLGKE", "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": "MPTNCISYPETNYFTPLILDYLSEKKELSNFYHRFPEIENFGAQITEKKKSYDHTIRKDLIQVLNDQYSKLTVSENTRANIDALESKNTFTVVTGHQLNLFTGPLYFLYKIISTINLTKKLKEKYPENNFVPIYWMATEDHDFEEINFFNLNGKKFKWNNADDRAGKTAVGGLSTEGLDEVFKLFSAEIGGGENAEFLKSTFEKGYLEHDTLSDATRFIANEIFGKYGLVIVAAGDKRLKKHFIPNVGSELVEHSSHKQTTETLQKINSLGYNIQVNPRDINLFYLTDEIRERIIERDGNYFVHETEISWTKEEILQELKDHPERFSPNVMTRPLYQEVILPNLCYIGGGGELAYWLELKSYFEAENVTFPMLLLRNSAMLQTGKQNDKREKLKISIQELFLKQHELINRKVRKISDIDIDFSGQKEHLVEQFQHMYDLAEKTDESFIGAVKAQEVKQLKGLDHLEKRLLKAQKRKLKDEVERIAELQNDLFPNRSLQERQTNFSEFYVEYGEELINKLMEELDPLESNFKILTFGRE", "text": "SIMILARITY: Belongs to the BshC family."}
+{"protein": "MKKLLKQSLLGFALVSMTGAAFADAQSVAELQRRLEQVSQYSADFDQTVRSSKGKQIQSGKGKFQVKRPNLFRMDTKSPQENLIVSDGANLWFYDPFVSQVTVNTVQDAVNNTPFVLLTSSDKSHWDQYDVTQNADTFVLKPKSKKSNLKQFDVRIDQSGMLKGFSTIERDGQSNLYVLRNITGGGVSSDLFKFSVPKGAELDDQRGGKKSKK", "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": "MEFKHVLMILGVIILILAPLIMYSGLGEDEGYFGGADGAAGDLIMEISPNYEPWFEPFWEPPSGEIESLLFALQAAIGAIIIGYFFGYNKAKYEDKN", "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": "MNSKYLFVFLILNVIFIDLCQGFLWSLIPSAISAVTSLIKKGRRRRELGSQYDYLQDFRKRELDLDDLLSKFPDY", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family."}
+{"protein": "MSRIPTRELGRYLLQGQICQRGCVASSVSKSRAKQLGRHPLLPHDRHQPTQARHAHTVTTTATPTQLAPSVPLRKKLKDEAKQLKKNAKKDNRKGSNQTVDGWELTVGIEIHAQLNTARKLFSPAATSFNDAPNSHVALFDLSMPGSQPLLQKETLIPALRAALALNCDIQPISRFDRKHYFWWDQPSGYQITQYYEPFARNGQITLFARDGIAPEDGESVTIGIQQVQMEQDTAKTLAQPGDTHWLDFNRVGVPLIEIITKPELHHPRTAAVFVRKMQTLLNAVDACVSGMETGGLRADVNVSVRRTSDASAPLGTRTEIKNLSTIKAVEDAIIAERDRQIQELEAGGTIAGETRGWTLGTKQTRRLRGKEGEVDYRYMPDPDLGPLIIADDLVDHIRKSVAYLPDHELSELADVYGLTAKDALSLLSLDNGGRIEYFYNVVESFGTRLQQGTEGGLDVRAYAPLAANWILHEFGRLVDDDSDNESTPFEVSPDGQCERVPVESLAELLFHLQQKKITGKVAKELLTALHQGNLADAENITAAIDAHDLWFHELSTEEYQELAALAVEGEDKVLREFRDKKVFPQGKLMYLVGKMLRLGATERIDPSNAEKFMRAKVEELL", "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": "MSGLTIFSDQEPQQPLWQSRDAQAIGQQLAQIGVRFERWQADRELGENPDPAVVIAAYQHQIDRLVAEKGYQSWDVISMRPDNAQREVLRSKFLSEHTHGEDEVRFFVEGAGLFCLHLDGKIFQILCEKNDLISVPANTRHWFDMGSAPNFTAIRVFDNPEGWVAHFTGDNIADAYPRLD", "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": "SCMKAAPMKEVSIRGQGSLAYPGLRTQGNLETLGGPNDATRGLTSLADTFEHVIEELLDEQQAIQPSKENKDADLYSTRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSTSEWVTAAEKKTAVDMSGATVTVLEKVPVPKGQLKQYFYETKCSSKGYAKEGCRGIDKRYWNSQCRTTQSFVRALTMDNKKRVGWRFIRIDTSC", "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": "MEKIFERLMYASRWIMAPIYLGLSLVLLGLGIKFFQEIFHILPIIFEMTEVDLVLVTLSLIDITLVGGLIVMVMFSGYENFVSQLDVGEDSEKLSWLGKLDSGSLKNKVAASIVAISSIHLLKIFMDVKNIDNDKIMWYLLIHITFVLSAFAMGYLDKMTRK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0114 family."}
+{"protein": "MAAKEKISRREHILQCLAQMLETNPGQRITTAKLAAEVGVSEAALYRHFPSKARMFEGLIEFIEDSLLSRINLIMDDEKDTMRRCQLVLQLLLLFAERNPGISRVLNGDALLGENERLRSRVSALFGKIETQLKQILREKTLREGKGFELDEAMLANLLLAVAEGRIAQYIRSEFKQKPTEHFDEQWGFIQKQLLQS", "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": "MNINIILYSSRIQQGGLNMSNETFNRVSEILRHIMEDNSVPRNIRRAAEESNEILNNPDEDSTVRASTVISILDEISNDPNIPIHARTLVWEILSELESIRE", "text": "SIMILARITY: Belongs to the UPF0147 family."}
+{"protein": "MLHTLHRSPWLTDFAALLRLLSEGDELLLLQDGVTAAVDGNRYLESLRNAPIKVYALNEDLIARGLTGQISNDIIPIDYTDFVRLTVKHSSQMAW", "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": "MFITSKEMRRIELNSRWLGFEEDFMMENAGAGVARVVIGEYSPNDVLVVCGTGGNGGDGFVTARHLDSEGVDVDVLLVGRREAIKNEAAELNLRRLDRAGIPVQEVRDSEDLESVDFERDVVVDALLGFGIRGRLREPVRSAVLRINEASRAGTRVVSIDIPTGLDPDSGETPDVAVEADLVVSIHRHKRGVRKLRDVFLRRVNAGIPEIAERICGPGDLITSDIWRRDPWSHKGQHGRVLIIGGSRKYVGAPQLAARGALRAGVDLVFLLTVDAVPKNDPNVIYRAVPAERLEPEHLDEVDLEGVDTVVVGPGLGADADSVGILRELAESFDGMIIVDADGLRGISGVNVDDRFVLTPHAGEFRREFGEELGRSLEDRSEAVRRVSEELGCTILLKGRVDVIGSPDGEIRWNVTGTPAMTVGGTGDVLAGVVAGVAARCREGFEAACIGAFVVGSAGCLAERRLSQGLTAEDVAEYVPKVLRNPWAAEPEAVTEVRRD", "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": "MRNQQFAIRPTTLDQARVELQQIHFLDDTNLSFTTPSDLLRDFYDRSWPEYTTSSVVAQQLSNLMATPETDGLTYLTTHEQVPVDVFYNLALQRLGFAVDLDFQLTDPLAAMTKIQLPVADHEGTTFTLNELMNAWYVLLTTHNKTGQTFLDQLTTHGYFAPLIHDNSVPKPLIFNGKAQAVFDTTQLIHEVVYVESPQDTDHDGHRDLLKAEIIRPAETANGLKVPVLYTASPYNQGTNDEAGEALTHNVNVPLTAKQPAATTLADVTAESVTTPLPDARPVTATTHTAAETFAREQSYTLNDYFLARGFAVVYAAGIGTKDSDGLRTTGDPEETTSTIAIIEWLAGNRTAFTTRNATQAIPAWWSNHQVAMTGRSYLGTLATAAATTGVAGLKTVISEAAISNWYDYYRDGGLVVAPGGFPGEDADVLAEETFSRQLLAGDYHRIQEKWQHQLAAITQNQDRVTGNYNRFWDARNYLKNAKNIKADLLLVHGLNDWNVKPRNVNNLWRAVRDLPVTKKLILHQGQHIYINAFRSIDYTDIVNLWLTHELLGVDNHAETLLPNVIIQDNVTPETWQAYPDWDAPSNPVQHFNLQADELVAPSDHIPAAATSFNDQLPVDQFNHYTHHIDEWQADLLGDKHNAMFKHRLLFKSAVLTDDLVLDGRPTIDLQVAVNQPLGLLSFQLVDYGDAKRLGVSPTPLRIRLDEGYRWREDNLREFTVAATTPWKMITKGHRNLQNRTNAYQVDELKPNTFYDLSVTLQPTHYRLLAGHQLGLVIYATDFGMTVRGNQDLQYSIQLGQSALHVPFITD", "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": "MTRKKTNPFVARHLLAKIEKVNMKEEKEIIVTWSRASSILPAMVGHTIAIHNGKEHIPIYITNPMVGRKLGEFVPTRHFTSYESTRKDTKSRR", "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": "MNPRRKKRLTLAVALIAGVAAVASLLLYALNSNLNLFYTPYEITHGKNDTGVMPEVGQRIRVGGMVTIGSMKRDPDSLHVEFAVHDSAGGTVFVTYDDLLPDLFREGQGIVAQGVLVESGKLEATEVLAKHDENYMPPEVAEAMGQTHEKPTYNQKALEDK", "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": "MQHKLLINGELVSGEGEKQPVYNPATGEVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTAPSIKLTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLDRVSKAVEEAKATGHIKVITGGEKRKGNGYYYAPTLLAGALQDDAIVQKEVFGPVVSVTLFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVKH", "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": "MKLFYFSLLFTLFFGLISANRGPKVTDTVYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGEKGFGYEGSIFHRVIPNFMIQGGDITKGDGTGGKSIYGSRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKIIKSGQLSQENVEDDGTDEL", "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": "MIRFAVIGTNWITRQFVEAAHESGKYKLTAVYSRSLEQAQHFANDFSVEHLFTSLEAMAESDAIDAVYIASPNSLHFSQTQLFLSHKINVICEKPLASNLAEVDAAIACARENQVVLFEAFKTACLPNFHLLRQALPKVGKLRKVFFNYCQYSSRYQRYLDGENPNTFNPAFSNGSIMDIGFYCLASAVALFGEPKSVQATASLLASGVDAQGVVVMDYGDFSVTLQHSKVSDSVLASEIQGEAGSLVIEKLSECQKVCFVPRGSQMQDLTQPQHINTMLYEAELFATLVDEHLVDHPGLAVSRITAKLLTEIRRQTGVIFPADSVKL", "text": "SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
+{"protein": "MVAKEKIGTVVSDKMLNTRIVAVSDRVSHKNYGKVITRTKRYVAHDIESNSKIGDKVKIQETRPISKSKNWILVSILEKSST", "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": "MPFERFVQTGRIAKASAGPLKGRLVAIVDVIDQNRVLVDGPLTGVPRQEYRLNNLHLTKYRIKFPYTAPTRIVRKAWTESDLKAQWKVSPWSVKAQNICKRSSLNDFDRFKLRYAKRQRNKLLTIAFNTLKKRTKADGTPRVLKKDRRERLRAEKAKGGKKAAAKK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL14 family."}
+{"protein": "MSRQSRSRFPSPTLITKSEDLAALCTTLRREPYVTIDTEFMRERTYWPELCVVQLGGADCVAVIDTLAPELDLAPVGELLADPAVIKVFHACRQDIEIFLLRFGSIPQPMFDTQVAAMVAGFGDQVGYDTLVSSLTGGHIDKAHRFSDWSRRPLSQAQIDYAAADVTHLRGVYETLRDRLEKEGRLAWVSEEMAVLNDPATYRTDPVTMWERLRPRTNNRRYLGLLRAICAWREVEAQRLNIPRQRLIKDESLLEIAATSPADAESLAQARGVGRGFAEGRSGATLLAAIAEARGLPDADLPAIPRSRESGARPSPALVSLLKVLLAAKSEQHNVAPKLLASSEDLDRLATEAEPDVPALTGWRRDVFGQDALALKNGEICLGVDGKQIKLITTG", "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": "MKTDTSTFLAQQIVRLRRRDQIRRLMQRDKTPLAILFMAAVVGTLTGLVGVAFEKAVSWVQNMRIGALVQVADHAFLLWPLAFILSALLAMVGYFLVRKFAPEAGGSGIPEIEGALEELRPVRWWRVLPVKFIGGMGTLGAGMVLGREGPTVQIGGNLGRMVLDVFRMRSAEARHTLLATGAAAGLSAAFNAPLAGILFIIEEMRPQFRYNLISIKAVFTGVIMSSIVFRIFNGEAPIIEVGKLSDAPVNTLWLYLILGIIFGCVGPVFNSLVLRTQDMFQRFHGGEIKKWVLMGGAIGGLCGILGLIEPEAAGGGFNLIPIAAAGNFSVGLLLFIFIARVVTTLLCFSSGAPGGIFAPMLALGTLLGTAFGMAAAVLFPQYHLEAGTFAIAGMGALMAASVRAPLTGIVLVLEMTDNYQLILPMIITCLGATLLAQFLGGKPLYSTILARTLAKQDAEQAAKSQNAPAGENT", "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": "MAKKSLIQREKKRQNLEKKYKILRNSLKKKITETSSLDEKWEFQKKLQSLPRNSAPTRLHRRCFLTGRPKANYRDFGLSRHLLREMAHACLLPGVTKSSW", "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": "MSINLLHKDDKRIDLVFEGYPLEFVNAIRRATMLYVPVMSIDDVYFIENNSPLYDEILAHRLALIPFTSEEALDTYRWPEECIECTENCEKCYTKIYIEAEALNEPKMLYSKDIKSEDPSIVPISGDIPIVLLGANQKISLEARLRLGYGKEHAKFIPVSLAIVRYYPKVEILGNCEKAATVCPEGVFELKDGKLSVKNELACTLCEECLRYCNGLIRISSIEDKYILELESVGSLKPERILLEAGKSIIRKIEELEKKLVEVIK", "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": "MAAVTKKIKRDPAKNPMRDLHIRKLCLNICVGESGDRLTRAAKVLEQLTGQQPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILERGLKVREYELRRENFSSTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGYNVNHRKRKSGTVGFQHRLTKEDAMKWFQQKYDGIILNTKK", "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": "MSSGQSFSRSLMKLPLSLLVKSTSIPSNPVEDLNIDLSKPIVYALPFRSSVDILTLQKHALELGLPDPLSKLEINGKSLQRYVFISSRKTLLQDDDYVPSSSIEVFSELLSLHAEDSELDVQVIPATVLWGRKPGKENNQKPYLQAMNGLEKSKAVLLAGRDCLVRFSPVVSLRYMANSHGTDSTIAHKLARVARIHFSRQKLAASGPNLPSRQALFDRLLKSEAIKKAIEDEAESKNISIEKASKEAQDIMDEIAANFSYSLIKRGEKILGWLWNKLYQGLHISNASTVRKLAQDGHEIVYVPCHRSHMDYLLLSYVLYHEGMVPPHIAAGINLNFFPAGPIFRHGGAFFIRRSFKGNKLYSTIFREYLAELFAKGYSVEYFSEGGRSRTGRLLQAKTGMLAMTIQAMLRGMNRPVTLVPVYIGYEHVMEVATYAKELRGKRKEKENASLVIRTIRKLRNFGKGYVNFGEPIQLNQYLNEHAPEWTKDIDPMGTSKPQWMNPVVNDLATKMMTHINDAAATNALTLCATALLASRQRALSRDSLVSQINCYLSLLKNVPYSDTFTVPKDSAEDLVKHAESLNKFLIESDTMGDIISLDRHQSILMTYYRNNIIHLFALPSLIAQMTIRQHGLSIDAIQENVAAIYPFLKKELFLSYDEDQLESVVANIIDELVGQGMLVVSNNQVTINQSNSQALMLLGRTISETLQRYSIALNLLAENPDLDKSDLEQKSQDIAQRLGRLHGINAPEFFDKGVFASMFATLKQQQYLDNDGNCDLEKTQQFAKLLYSMLYPEVRLTIQESIHQAE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family."}
+{"protein": "MDRTETRFRKRGQITGKITTSRQPHPQNEQSPQRSTSGYPLQEVVDDEMLGPSAPGVDPSPPCRSLGWKRKREWSDESEEEPEKELAPEPEETWVVEMLCGLKMKLKQQRVSSILPEHHKDFNSQLAPGVDPSPPHRSFCWKRKMEWWDESEESLEEEPRKVLAPEPEEIWVAEMLCGLKMKLKRRRVSLVLPEHHEAFNRLLEDPVIKRFLAWDKDLRVSDKYLLAMVIAYFSRAGFPSWQYQRIHFFLALYLANDMEEDDEDSKQNIFHFLYRKNRSRIPLLRKRWFQLGHSMNPRARKNRSRIPLLRKRRFQLYRSTNPRARKNRSRIPLLRKHRFQLYRSMNSRARKNRSQIVLFQKRRFHFFCSMSCRAWVSPEELEEIQAYDPEHWVWARDRAHLS", "text": "SIMILARITY: Belongs to the Speedy/Ringo family."}
+{"protein": "MSMEEAEECSAACGFSLTCQEDGADLGDGVVDDDDDGDVFLFYNAVAAADDEEEEEEYVEQMVSKEASFCCSSSSSLFDAAAGDGYGDGDGDGDWFRQARLAAVKWILETRGYFGFGHRTAYLAIAYFDRFCLRRRVDREAMPWAARLLSIACVSVAAKMEEYQSPALSEFDAGGGRVFCSDSIRRMELLVLSTLGWRMGAVTPFDFLPCFSSRLHRHHHGGAGAAGHGAAAAARVALNAVGFIFATAEAGSVLDYRPSTVAAAAILAASYGAPLTKEALESKMSNLSPSCLIDKENVHACYSMMVGDMNNNRRSSKRPLQCSDSNEITTTSTYDSVLVDDVTDTAAFAATAMNKRLRPEPPRIR", "text": "SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily."}
+{"protein": "MDGTVLVADDDRTIRTVLTQALTRAGCKVHATASLMTLMRWVEEGKGDLVISDVVMPDGNGLEALPRIARERPGLPVIVISAQNTIMTAIQAAEADAYDYLPKPFDLPDLMKRAARALELKRRAQVVPKVIETSRPEGTDLPLVGRTAAMQALYRLVARVMNADLPVMIMGESGTGKSLIAKAIHDFSDRRTLPFVVAQAADLLGADGPSSLLARVKGGSLVFDEVGDYDDETQGRIVRMLDALPDPAPRIMATTQVDLGALMEAGRFRQDLYYRLGGVTLAVPALRERVEDIPLLAEHFLGRAERDGLGMRRFSAEAMGLVRAYAWPGNVRQLENTVRRLVVTASEEEITRTEVEFVLGNQPAVDALRGAGGEGEKLSASIARHLRRYFDLHGGNLPPPGLYDRILAEMEAPLIEIALDATGGNQAKCADLLGINRNTLRKKITDLDIQVTRRRKLM", "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": "MPKIGPMEILIIVLLVVVVFGIGKLPQVGDAIGKGIRNFRKASSGEEEKEEVETKEETKTIEKSE", "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": "MAELGQKHALEMVRTDGADEGCVTFVLNEEDHTLGNSLRYMIMKSQDVEFCGYSITHPSESKINFRIQTRDGVPASEPLRNGLNNLTDVCKHVLQTFEARMKEFKEQEESMT", "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": "MGREFLDLFEQWAESYDRSVEGYDEQYRDVFAGYDRILSTVADKAGQVVLEFGVGTGNLTKKLLERGKQVYGIEPSAPMRKKAAEKLSGRAVILDGDFLQFPTPPEPIDTIASTYAFHHLTDAEKDEALAKYSQLLHPGGKIVFADTAFRDKEAFRQAIEEARARGFHDLADDLEREYYTTLDVLASLFSKHGFSASFAQQNAFVWVMEAVKQTT", "text": "FUNCTION: Could be a S-adenosyl-L-methionine-dependent methyltransferase. SIMILARITY: Belongs to the methyltransferase superfamily. YrrT family."}
+{"protein": "MATTKSVLVLFFMILATTSSTCATLGEMVTVLSIDGGGIKGIIPATILEFLEGQLQEVDNNKDARLADYFDVIGGTSTGGLLTAMITTPNENNRPFAAAKDIVPFYFEHGPHIFNSSGSIFGPMYDGKYFLQVLQEKLGETRVHQALTEVAISSFDIKTNKPVIFTKSNLAKSPELDAKMYDICYSTAAAPTYFPPHYFVTHTSNGDKYEFNLVDGAVATVGDPALLSLSVATKLAQVDPKFASIKSLNYKQMLLLSLGTGTNSEFDKTYTAEEAAKWGPLRWILAIQQMTNAASSYMTDYYLSTVFQARHSQNNYLRVQENALTGTTTEMDDASEANMELLVQVGEKLLKKPVSKDSPETYEEALKRFAKLLSDRKKLRANKASY", "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": "MTDLSKKVRAWGRRLLVGTAAAVTLPGLIGLAGGAPTAGAFSRPGLPVEYLQVPSAGMGRNIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIIMPVGGQSSFYSDWYSPACGKAGCTTYKWETFLTSELPQYLQSNKSVKPTGSAAVGISMAGSSALILAAYHPQQFIYAGSLSALMDPSQGMGPSLIGLAMGDAGGYKASDMWGPSSDPAWQRNDPTIQIPKLVGNNTRLWVYCGNGTPSELGGANMPAEFLENFVRSSNLKFQDAYNAAGGHNAVFHFDQNGTHSWEYWGAQLNAMKPDLQGTLGATPGGGG", "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": "MITTPRYIVIEENGINLLNDILLKLNLKNPLVITGKRTKKYISNFDYFYYFDYIDIKRNEPNKEFIENICNFDCIIGVGGGKAIDVGKYIAYKYNKQFISIPTTASNDGIASPIISQQGKSITAESPIAIIADLNIIKKSPKRLLSAGMGDIVSNITAVLDWKLSYKETKEPYSESSAIFSKTIAMELVEFVLSNDKNNLEEYPKKLVKALIGSGITISIAGSTRPASGSEHLFSHSLDIITKKLNLNINGIHGEQCGIGTIISAYLHLIEGNITIGEYENIKLSLEKVGAPTIGEQLGYDKNILIDALANAHKIRNRWTILRNGISKEKAEKILKKTDII", "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": "MEVNILAFIATALFILIPTAFLLIIYVKTVSQSD", "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": "MVSGSGICAKEVVVDARHHMLGRLASILAKELLHGQRVVVVRCEEICMSGGLVRQKMKYLRFLRKRMNTKPSHGPIHFRAPSRILWRTIRGMIPHKTKRGAAALATLRAFEGVPPPYDRKKRMVIPDALKVLRLQPGHKYCLLGRLSKEVGWHHFDTITELEEKRKAKAQVSYERRKQLAKLRSKAVELAEKQLAPEMELLASLKY", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL13 family."}
+{"protein": "MEEVKKRDCMEKARPFISMVVLQVGLAGMDILSKAVLNKGMSNYVLVVYRHAVATIVMAPFAFYFDKKVRPKMTLMIFFKISLLGLLEPVIDQNLYYLGMKYTTATFATAMYNVLPAITFVLAYIFGLERVKLRCIRSTGKVVGTLATVGGAMIMTLVKGPVLDLFWTKGVSAHNTAGTDIHSAIKGAVLVTIGCFSYACFMILQAITLRTYPAELSLTAWICLMGTIEGTAVALVMEKGNPSAWAIGWDTKLLTATYSGIVCSALAYYVGGVVMKTRGPVFVTAFSPLCMIIVAIMSTIIFAEQMYLGRVLGAVVICAGLYLVIWGKGKDYKYNSTLQLDDESAQPKLELSGNGKDNVDHEVITISKQGEQRRTAVETV", "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": "MDYIFLITGYKYRHLNLEAYNAKSRAIENEKRYLGNDRNLPFHREREKVESNPNSSDEEDLTSTNNTRSSDNTTSDTEDDSGEDSYQVEWESGKDPLAPKNWPMWKKIYTLLVASFIAIVITANSSIFSDGGGIAAQQYHVGATVGDLCSATFLLGFAAGSVLFAPLSEVYGRLPLYSVTLVIFVVFQIGGGCSKNIWSLVIFRFFHGFFGCTPMSACGGTISDLFNPIQRTGALLVFCAAAFVGPLVGPVMGGYITESKLGWRWDFWINMIWAGLTWVIVCFTMPETHSETLLDFKARYLRKKTNCDKWYNEHEHQRDPAYAIRTALTRGVRLLCTEPIVQAFCMYLVFINILLYICMVGYPLIFYQYGFNAGEVGLAILGILVGILLGLALTPIIYVHYRRRYEMRDGNICPEDRLFPLFFGSFFIPIALFWLGWTCYPSVHWAAPMVSGIFLGWGFLYVLAVCYSYLVDCYHEMAASALSVATFTRYAAGGGMTIVARPMYNNLNYHWATSLLAFVGCGLVPIPFIFFFWGRRIRQRSPHAYKG", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family."}
+{"protein": "MSKGFSNGTNIKRVRKSGFRARMSNSSGRKILNSRRRKQRKKIAL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family."}
+{"protein": "MRLKTILLGFCAFHVARSKMVVNLINMIDEQTGEQRKVVPLELERFFPLDFDEILLRDTMQRNAAMEEEDYRELGKRDIEVAFQNTGVTLDDRLQSLPAISLFGRYVRDIDGMSEALADGDRHIMVFAPTNDAITAMPKKPWEYPRNIDKLEQAGASASEIHDAIQANVRRFVLTHVVSDIDLSKVGREDGSAVLTSDLHPKSMQGDILLRKDGDRYTVSSKTGRDLAVEEVHTASNGIVLVIDSSLDAE", "text": "SUBCELLULAR LOCATION: Vacuole."}
+{"protein": "MQYLAIAVIVALAGLSAAAHKPAYYDDNMANQMVDQIVKSLTTKKELDPFKIEQTKVPIDKKIGLIHIKGSATIKNAVITGLSHISRRGDAKIDTDGGAFAATLKLGDKNIRIKTDLHLDLGKIIHPNLKFEGHIGDIDMKLKLKLDAEGKPSLDQFEIDEFEQVELFIHGLGPLDPLVDVIADSFVKYFNPQARKLVTDMLKPILVEEIKKLKLN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the mite group 7 allergen family."}
+{"protein": "MKRTNKIKGTLERPRLSVFRSNCHIYAQVIDDSSGMTIVSTSTLDKDVKSLLNNTSTCEASKIVGQVIAKKTLARNIKQVIFDRGKRVYHGRISALAEAARESGLEF", "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": "MASLQTQMISFYLIFLSILLTTIFFFKVNSTETTSFSITKFSPDQKNLIFQGDGYTTKGKLTLTKAVKSTVGRALYSTPIHIWDRDTGNVANFVTSFTFVIDAPSSYNVADEFTFFIAPVDTKPQTGGGYLGVFNSKEYDKTSQTVAVEFDTFYNAAWDPSNKERHIGIDVNSIKSVNTKSWNLQNGERANVVIAFNAATNVLTVTLTYPNSLEEENVTSYTLNEVVPLKDVVPEWVRIGFSATTGAEFAAHEVHSWSFHSELGGTSSSKQAADA", "text": "FUNCTION: D-mannose specific lectin. SIMILARITY: Belongs to the leguminous lectin family."}
+{"protein": "AAPANAVTADDPTAIALKYNQDATKSERVAAARPGLPPEEQHCANCQFMQANVGEGDWKGCQLFPGKLINVNGWCASWTLKAG", "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": "MRLTVGQVHRHVLALASSRSCFVLGDHLPFRMLSLPRVVRFHQTAWHDIQTVEDKSGPLTLASLEVQNKVEYVKKERATRTGGIKPSSRASALNMKPKVSSFNAKPVKSALPKSAVLKKTLKIDESLFSAKSFEELGLPPLLIDRLNKEGLTAPTEVQSAAIPIISQKHDAVIQSYTGSGKTLAYLLPILSEIGPLKRPTEQDSSDKRSGVEAVIVAPSRELGMQIVREVEKILGPNDKRLVQQLVGGANRSRQEEALKKNKPIIVVGTPGRISEISAAGKLHTHSCRFLVLDEVDQLLSFNYREDMHRILEHVGRKSGTSSRDILGPLARRSERQTILVSATIPFSVIRAARSWGHDPVLVRAMSVVPLESITVPRPVLSQPDANSNSPSNSVNQAAVDSLPPSLEHYYCTSKAQHKVDTLRRCIHALEAQTVIAFMNNTKPLKDVVFKLEARGMKATELHGDLGKLARSTVLKKFKDGEFRVLVTNELSARGLDVPECDLVINLDLPTDSTHYAHRAGRTGRLGRKGTVVTICEETETFVVRKMRKQLAVPIKPCEFTEGKLLVHKEEDVE", "text": "SIMILARITY: Belongs to the DEAD box helicase family."}
+{"protein": "MRLVIARCCVDYVGRLEAHLPPADRLILLKADGSVSIHADDRAYKPLNWMMPPCSLEAVEASSFDGDDAPTEYSELGNEGVEQLWIVTNPKGEQLRIQIFEIYSDTEHDLGEDPGLVKDGVEAHLQELLAEQIEILGEGYSLIRREYPTAIGPVDILSKDSTGATVAVEIKRRGGIDGVEQLTRYVELLNRDELLAPVTGVFAAQEIKPQARTLAEDRGFRCVTLDYEAMRGTDSSELRLF", "text": "FUNCTION: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NucS endonuclease family."}
+{"protein": "MGSNSGRTTKLPLVPLPKGSVLLPGITLRIPVSNRPDLANLLSTIVDRSAVAKRDGTAITFGCVPLSSPYLSKDGQRLIDDGSLDEDRREEFDMIDAGQSRKEDLFRHGTIGKVIGIQRRAYSEPALVVQGVQRFTIRRVLKERPFFEAEAVVHDEKVSGDAETVELFQQLRQLSRELLTLLRLSSLLPSPGSRLSPLIARKFELFITKSDVSHASRLADFMADVADSGFEEKLRILASLDVKIRLERVVEILTRQLQSIKSNVKVTTITTNSFPSSGFDINQIDPRDREILARKAMAGLSGLTPPGLSAGRNNDNDDKESNEVDELQQRLQEAQLSPEARKVADKELRRLRKMNPANAEYGVCRTYLENIADIPWTKMTEDQLGPETLKRARKQLDDDHYGLEKIKKRLLEYLAVLRLKQSTNRDVERQIESLSKELEASDGGDLEKEVPVLSETDRVAVETKLHMLKTRRMGDKSPILLLVGPPGVGKTSLARSVASSLGRKFHRISLGGVRDEAEIRGHRRTYVAAMPGLIVSGLKKVGVANPVFLLDEIDKVGGANFQGDPSAAMLEVLDPEQNHTFSDHYINIPIDLSKVLFIATANSLDTIPAPLLDRMETISLSGYTTVEKRHIAKRHLIPKQIRANGLSDGQVVLSDEVIDKIITSYTRESGVRNLERELGSVCRFKAVQFADAGDAGRLDAYNPVVSMDELEEILGIERFEEEIAEKHGRPGVVTGLVAYSTGGQGSILFIEVADMPGNGRVQLTGKLGDVLKESVEVALTWVKAHAFELGLTADPTEDIMKNRSLHVHCPSGAIPKDGPSAGLAHTMGLISLFTGKAVPPSVAMTGEVSLRGKVMPVGGIKEKLIGALRAGVKTVLLPHHNRKDVKDVPQEVSEGLEIVYVTHIWEAIRQVWPDAHWPGQHTHFIESRL", "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": "MSQIESPNPEPVFQLKGSMLAITVMELARSNLEALDRQLAAKVAQAPNFFSNTPLILALDKLAPNEGPVDLPGLVRICRQHGLRTLAIRANRIEDIAAAIAVDLPVLPPSGARERVIDPIEAEAPKKLPEKPPEPLIKPTRVITSPVRGGQQIYAQGGDLVVVAPVSPGAELLADGNIHVYGPMRGRALAGIKGDTKARIFCQQLSAELISIAGQYKVSEDLRRDPLWGSPVQVSLSGDVLNIIRL", "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": "MFNSTALVIFAILFLLISADAFPIPSPNGEIDAMLIRNSIIGEDEDLMPTEISRRVLMAQKRYIGYETLRRDMVPCQKPGASYYDCRSGQANSYSRGCDTITRCARDTNDINT", "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": "MKPSDVRSKAFAMPLTSPAFPMGPYRFVDREFLIITYRTDPDRLREIVPEPLQVTEPLVHYEFIRMADSTGFGDYTESGQVIPVEYNGQAGGYTLAMYLDDHPPIAGGRELWGFPKKLASPTLHVNTDHILGTLDYGKVRVATGTMGYKHKELDIDEQTKRLAGPNFLLKIIPHVDGTARVCELVRYYMQDIKMKGAWTGPASLELAPHALAPVADLPVLEIVEARHLVADLTLGLGEVVYDYLAQ", "text": "FUNCTION: Catalyzes the conversion of acetoacetate to acetone and carbon dioxide. SIMILARITY: Belongs to the ADC family."}
+{"protein": "MDELSILNELRKYRDMDLDYEDGTILGSMCTKPHPLTRKISEMFFETNLGDPGLFKGTRELEKQAISMIGNVLGNKDAFGYIISGGTEANLTAMRAFKNVSKKSGKSLNIIIPETAHFSFDKAKDIMDLNVIRPPLTKYFTMDVKFIRDYVFDNPNKISGIVGISGCTELGSIDNIAELSKIAVDNDILLHVDAAFGGFVIPFLYDKYKLKNYRYEFDFSLEGVSSITIDPHKMGLAPISAGGILFRNNSFKKYLDVDSPYLTEKQQATLIGTRSGVGAAATWGVMKLLGTSGYKKIVNDSMEKTYYLTRKLREYGFKTAIDPVINIVSIVDEHKNETCAKLRENGFHVSVSRCVDALRIVIMPHIEFEHIDIFLDCLSNTKRY", "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": "MWELNMSYLWLAQRLLQSDRASGMFRLGVTADVAAALAALSMKQMNDLASAGQLICALRPSRYGVLSALTRATPPVDLVRVHTAMALAGLALPDEETS", "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": "MFKWPWKADDESGNAEMPWEQALAIPVLAHLSSTEQHKLTQMAARFLQQKRLVALQGLELTPLHQARIAMLFCLPVLELGIEWLDGFHEVLIYPAPFIVDDEWEDDIGLVHNQRVVQSGQSWQQGPVVLNWLDIQDSFDASGFNLVVHEVAHKLDTRNGDRASGVPLIPLREVAGWEHDLHAAMNNIQDEIDLVGESAASIDAYAATDPAECFAVLSEYFFSAPELFAPRFPALWQRFCHFYRQDPLARRRENGLQDEGDRRIVH", "text": "FUNCTION: Involved in the regulation of ptsG expression by binding and inactivating Mlc. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MtfA family."}
+{"protein": "MPLFSHRFTTASSSSPASPSYYNKPSSKTHKPNSSSSSYTSSRIHVAIIFFSLVSVFIGVAGTIFALSSTGPASVYRCGGSKDTSRVVSASRKLGGDGGNNGVVVERRKLLGFVGIQTGFDSGDRRTALRSTWFPSDPDSLLRLEQATGLAFRFVIGKSKDAKKMAELEKEIKEYRDFVLLDTEEEYIRLPYKTLAFFKAAFKLFEADYYVKADDDIYLRPDRLATLLANERLHSQTYIGCMKKGPVITDPKLKWYEKQGNLIGNEYFLHAYGPIYVLSAEIVASLAAARNGSLRMFNNEDVTIGSWMLAMDVHHEDNRALCDPHCSPKSIAVWDIPKCSGLCDPESRLKELHKTDMCSKSPTLPPDDIDQ", "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": "MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDKMGFNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSSLIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE", "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": "MFGQQLASDVQQYLERLEKQRQQKVGVDEASAGLTLGGDALRVPFLDFATATPKRHQTVVPGVGTLHDCCEHSPLFSAVARRLLFNSLVPAQLRGRDFGGDHTAKLEFLAPELVRAVARLRFRECAPEDAVPQRNAYYSVLNTFQALHRSEAFRQLVHFVRDFAQLLKTSFRASSLAETTGPPKKRAKVDVATHGQTYGTLELFQKMILMHATYFLAAVLLGDHAEQVNTFLRLVFEIPLFSDTAVRHFRQRATVFLVPRRHGKTWFLVPLIALSLASFRGIKIGYTAHIRKATEPVFDEIDACLRGWFGSSRVDHVKGETISFSFPDGSRSTIVFASSHNTNGIRGQDFNLLFVDEANFIRPDAVQTIMGFLNQANCKIIFVSSTNTGKASTSFLYNLRGAADELLNVVTYICDDHMPRVVTHTNATACSCYILNKPVFITMDGAVRRTADLFLPDSFMQEIIGGQARETGDDRPVLTKSAGERFLLYRPSTTTNSGLMAPELYVYVDPAFTANTRASGTGIAVVGRYRDDFIIFALEHFFLRALTGSAPADIARCVVHSLAQVLALHPGAFRSVRVAVEGNSSQDSAVAIATHVHTEMHRILASAGANGPGPELLFYHCEPPGGAVLYPFFLLNKQKTPAFEYFIKKFNSGGVMASQELVSVTVRLQTDPVEYLSEQLNNLIETVSPNTDVRMYSGKRNGAADDLMVAVIMAIYLAAPTGIPPAFFPITRTS", "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": "MAKELKGIAASDGIAIAKAYLLVEPDLSYEKTEVTDVESEVKRFESALEVSRTELSTIREKAAKDLGEDKAQIFDAHLLVLNDPELTGPIEESIKNAKTNAETALQETTDMFIGMFESMDNEYMRERAADIKDVRKRVLSHLLGVTIPNPALIDEEVVVVAADLTPSDTAQLNRKFVKGFVTDIGGRTSHSAIMARSLEIPAVVGTKEVTASVAKNDIVIIDGLEGNVIIHPTEEQIAHYEKIKSDFALQQAEWEKLKNEKTVSKDGVHVELAANIGTPNDLEGVISNGGEAVGLYRTEFLYMGRDNFPTEEEQFEAYKAVVSGMDGKSVVVRTLDIGGDKTLPYLELPEEMNPFLGFRAIRLCFANEELFRTQLRALLRASVYGNLKIMFPMIATVNEFRQARDILLDEKAKLKAAGTEVSDSIELGIMIEIPAAAVLADQFAKEVDFFSIGTNDLIQYTMAADRMNERVSYLYQPYNPSILRLVKMVIDASHKEGKWTGMCGEMAGDQTAVPLLLGLGLDEFSMSASSILKSRSLIKRLDQSEMVKLAEEALNKSTAEEVVELVEKYTAE", "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": "MTAEKITQGTEGLNVPNEPIIPFIIGDGIGPDIWKAASRVIDAAVEKAYNGEKRIEWKEVLAGQKAFDTTGEWLPQETLDTIKEYLIAVKGPLTTPIGGGIRSLNVALRQELDLFTCLRPVRWFKGVPSPVKRPQDVDMVIFRENTEDIYAGIEFKEGTTEVKKVIDFLQNEMGATNIRFPETSGIGIKPVSKEGTERLVRAAIQYAIDNNRKSVTLVHKGNIMKFTEGSFKQWGYDLALSEFGDQVFTWQQYDEIVENEGRDAANAAQEKAEKEGKIIIKDSIADIFLQQILTRPAEHDVVATMNLNGDYISDALAAQVGGIGIAPGANINYETGHAIFEATHGTAPKYAGLNKVNPSSVILSSVLMLEHLGWQEAADKITDSIEDTIASKVVTYDFARLMDGAEEVSTSAFADELIKNLK", "text": "SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family."}
+{"protein": "MPVKFSKVLIPQPRSKFIKVRCPDCGNEQVVFSHAAMVVRCLVCGRVLAEPTGGKARLAGHVVKILE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family."}
+{"protein": "MTPVIIKNIECFITRPDRHNLVTVRVTTDQGVTGHGCATFQQRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMMNVNAYWRNGPVMNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHASGDTLDALFASVDALIEKGYRHIRCQLGFYGGTASGLHAPENPTPGAWFDQQEYMSNTVDMFRALREKYGWKLHILHDVHERLFPQQAIQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHSCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGDMTPVGVAVNTHLNIHLHNAAIQEFIPRSAMTDKIFPGAPEVKDGFIYPPVNAGIGVGFNEELARAHPVMYRPHEWTQSRLPDGTLHTP", "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": "MYGIEYTTILIFLISIILLNYILKSVTRIMDYIIYRSLLIYVALFALTRAQNYGLNLPITGSMDTVYANSTQEGIFLTSTLCLYYPTEASTQINDGEWKDSLSQMFLTKGWPTGSVYFKEYSNIVDFSVDPQLYCDYNLVLMKYDQNLELDMSELADLILNEWLCNPMDITLYYYQQSGESNKWISMGSSCTVKVCPLNTQTLGIGCQTTNVDSFEMVAENEKLAIVDVVDGINHKINFTTTTCTIRNCKKLGPRENVAVIQVGGSNVLDITADPTTNPQTERMMRVNWKKWWQVFYTIVDYINQIIQVMSKRSRSLNSAAFYYRV", "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": "MDMKNMREYMSWLYYQYLLITGIYVLEPWEQSIFNTVLFTMVAMVIYTSYVFVPIHVRLALEFFCELVGGQPESTVALMT", "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": "MLTITSYFGFLLVVLTITSALFIGLSKIRLI", "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": "MIKHLAEALRFLTILPIPGKPALSEQALVRSMVAFPLAGTLIGGLVAATWFGATWLWGTTTGSLCAILTWGAITSGLHLDGIADSADALFSWRSRERKLEIMKDSRIGTMGAIALISILLLKWLFVLGCGDLAWRALIVAPTLGRWVDIIGIFWFPPAAEGGLGRTFHDHTRRSDFWWATSCAGLVAAGLLWWWAGLIFAVVIVATIIIARWMVRSLGGLTGDTYGALCEIAEMLVLAVVAALVNHQVL", "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": "MGKLIKLITTLTVLVSLLQYCCEFNSGSISCERTQTLCHYTNPRVWNTYFSRNCELYKNKVSPGFDIVARKYDTAVKPVIDDATVKVNKAAIQPAFKVIHSQCKKWNCGKYYQLVRSPMVKTRRFFFAKYNAFVKPNLDKFFTAEFRSHLKERILKYKNIGHYYFTITSRCIKSKYDFTVGNTEEKLMGKFKNKDTHGIHGSVTREPSSEDMVLTVSTMESDEEELTTTSTQTVVETITLDQEEASAVANHAHDDEASTDVEGSTDVNVNEQALLQEDFDMWSETILQKTQDVIQLFEKDVSKYINGKLVEEANHFKAKFQSLDDKSKKFFSKISLAINDIECVEGIDSETGKKIFFDKSGSTEISQYITRELVREYFNETRSTLDELTNAMEKDLSEITDEIEKKVNAIREENVEVFEEWGDIIVNEWSKRMAYVDVINAHMGADDDTTLDEEKAKSSVNWKKFLKGKKQIIESRDKLAHHSADLSRVNAFRQKVQKKILSFTQESGEFLYILRSKANLQFQERERKERERKEREKAAAEEFQRQQELLRQQEEEDEEDVSYTSTSTITTTTTMTL", "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": "MAELSTRYNLPANVTEKSINLDLNSTARWIKEPSVGGWTVKWGNFVFHIPNTGMALLHHLKSNFVVPEWQQTRNLFSHLFKNPKSTIIEPFLALRILLGVALKDQELQQSLIPGFRSIVHMLSEWLLLEVTSAIHISPNLLGIYLTSDMFKILMAGVKNFFNKMFTLHVVNDHGKPSSIEIKLTGQQIIITRVNMGFLVEVRRIDIEPCCGETVLSESVVFGLVAEAVLREHSQMEKGQPLDLTQYMNSKIAI", "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": "MPKRTLEDTELNSGDNDIKISSKKSRKEKKDKKEKKSKDVEEPTTESTPIEVEVESKEARRERKRLKKEKKAQEAEKETEEEEKSGVEAIEPASDANAAADAKAAKKAEKARLKALKKEGKEEKADSTKSIETAAPASVTPQQNGTTYTEDPNLSGLPQSEIDSFLTTHFITITDPLSTSATLRPLTKFDYLPITDPAQRAPFKDFKAPTPIQAAAWPFLLAGRDVIGVAETGSGKTMAFAVPCINKGPRAVVVSPTRELAMQSYEQIVKLAKASGLECVCVYGGVPKDEQIRALKTADIVVATPGRLNDLINQGCADLSKARYVVLDEADRMLDKGFEEEIRKIINTTPSLGKRQTLMFTATWPESVRELAATFMTSPVKIAIGDNPTGDLRANSRIVQKVEVVEPRDKEYRLMQLLKQYQSGSQKDDRILVFCLYKKEATRVESFIRQKGFRVAGIHGDLSQEQRTRSLEAFKSGNTPVLVATDVAARGLDIPAVKLVINCTFPLTVEDYVHRIGRTGRAGKDGLAITLFTEHDKAQSGALINVLKAANQPVPDELLKFGTTVKKKAHDAYGAFFKNVDTTKKATKITFD", "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": "MMARRDPKSWAKRLVRAQTLQKQRRAPVGPRSPPPDEEDPRLKCKNCGAFGHTARSTRCPMKCWKAALVPATLGKKEGKENLKPWKPRAEANPGPLNKDKGEKEERPRQQDPQRNALLHMFSGKPPEKPLPNGKGSTESSEHLRVASGPMPVHTTSKRPRVDPVLADRSATEMSGRGSVLASLSPLRKASLSSSSSLGPKERQTGAAADIPQPAFRHQGPEPLLVVKPTHSSPEGGCREVPQAASKTHGLLQAVRPQAQDKRPAVTSQPCPPAATHSLGLGSNLSFGPGAKRPAQAPIQACLNFPKKPRLGPFQIPESAIQGGELRAPENLQPPPAATELGPSTSPQMGRRTPAQVPSVDRQPPHSTPCLPTAQACTMSHHPAAGHDGAQPLRVLFRRLENGRWSSSLLAAPSFHSPEKPGAFLAQSPHVSEKSEAPCVRVPPSVLYEDLQVSSSSEDSDSDLE", "text": "SIMILARITY: Belongs to the FAM90 family."}
+{"protein": "MKVLALRHSVAQVYADTQTYLHDDSKDEYENAFLISNLTTHNILYLNYSLKTLKILNKSGIAAVEVQSPDELFALIRCNFTYDYEDNIVYLHDYSYYTNNEIRTDQHWITKTDIIDYLLPGWKLTYVGYNGKNTRGHYNFSFICQNAATDDDIIIEYIYSNELDFQNFLLRKIKERMTTSLPIARLSNRVFRDKLFPSIVNIHKKVINVGPRNESMFTFLNFPTIKQFSNGAYIVKHTIKLKQEKWLGKRVSQFDIGQYKNMLNVVTTIYYYYNLYYSKPIIYMLGSAPSYWIYDIKQYSDFTFETWDPLDTPYSTTHHKELFFDKDVNKLKDNSVLYIDIRTDRGNMDWKEWRKIVEQQTVSNLNIAYKYLSTGKAKVCCVKLTAMDLELPITAKLLHHPTTEVRSEFYAILDVWDIITIKRFIPKGVFYAFINNVTTENVFIQPPFKLKTSPTDYIVALYALSNDLNSRQDVINLINKQKQSLITVRINNTFKDEPKVNFKNIYDWTFLPTDFELKDSIITSYDGCLGIFGLSISLSSKPTGNNHLFIINGTDKYDKLDQYANHMGVSRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNVENSVSGHVYNALIYYRYNYAFDLKRWIYLHSIGKVAVEGGRYYEHAPIELIYACRSAKEFAILQDDLTVLRYANEIEGYINKVYSITYADDPNYFIGIKFNSIPYEYDVKIPHLTLGVLFISDNMIHDVITVLKKMKTELFKMEISTSYTYMLSDNTYVANASGVLSTYFKLYNMFYRNHITFGQSRMFIPHITLSFSNKQTVRIESTKLRINSIYLRKIKGETVFDMSE", "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": "MFSEVKVLQIVLVQWLTLFSFTYNSHGTYILDGSAVFNENSYLVLTNTTKHSYGQAFDNTTFEMKDQSFSINFFFAIVPEHKQQGSHGMTFAFSPTRGLPGASSDQYLGLFNKTNNGKTSNHVIAIELDIHKDEEFEDIDDNHVGININGLRSVASASAGYYDDNDGSFKNLSLISGKLMRLSIVYSHPDTKLDVTLCPAEFLVPPRKPLLSLNRDLSQYVLKHMHIGFTASTGSIRALHYMVLVYTYPEAVYQPLEFGRVPTLPPYPKKPSDRLRTVLAVCLTLALFAVFLASGIGFVFYLRHKKVKEVLEEWEIQCGPHRFSYKELFNATKGFKEKQLLGKGGFGQVYKGTLPGSDAEIAVKRTSHDSRQGMSEFLAEISTIGRLRHPNLVRLLGYCKHKENLYLVYDFMPNGSLDKYLNRSNTNENQERLTWEQRFKIIKDVASALLHLHQEWVQVIIHRDIKPANVLIDHDMNARLGDFGLAKLYDQGFDPQTSRVAGTFGYIAPEFLRTGRAVRVKFF", "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": "MSMLCYTLIIAFLIGIWAAPKSEDNVPLGSPATSDLSDTSCAQTHEGLKTSRNTDQRHPAPKKAEDQELGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVEFLDNEDTLNRNIRAKRETHPVHNLGEYSVCDSISVWVANKTKAMDIKGKPVTVMVDVNLNNHVFKQYFFETKCRNPNPVPSGCRGIDSGHWNSYCTTTQTFVRALTMEGNQASWRFIRIDTACVCVISRKTENF", "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": "MDNIPQSINPIPAFYCCYLLRSTVRHASLYIGSTPEPSRRLAQHNGDRTGGARKTSSEKLRPWEMVAIVSGFTNRAGALQFEWAWQHTKESRHAEVERCESEQLGTRGSSRTGKEVKRAGKPRTSLPNILENLHILLRSPYFSEWPLEVWFFSADVWQVWSQPKGNLLDNSIKVVTAFSSKEAGDTNRREILGKRIETLDTGYDALIEYVEKSQFLLESEEAIDCGVCKQRLNPRNDMIAICSHSLCRCASHLLCLSAHFLEAAGFIGKLIPKEGTCPACLGKLEWPTLMKEITLRLRGQEEVKRLLGRRRRTEQVGKRKISNHVSSEKGESEASMPSTDAKTMALPIRSHPSVGGSNFGKLGRSVGSAIRTNTDNGSVKAVTPEIEFYRRRKCNAKKNFSGLYSTPRINISDWDNAEIIE", "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": "MPLQLAKSLKLHNDKVWSIDFEPVRGLLATGSTDRAIKVLQLKNGKENLLDVLDDTVHKKAVRSVAWRPHSDLLAAGSFDSTISIWTQSDLDLEEGAKLEMELLAIIEGHENEVKGISWSQDGCLLATCSRDKSVWIWETDEAGEEYECISVLQEHSQDVKHVVWHTKHNLLASSSYDDTVRIWKDYDDDWECAAVLTGHEGTIWCSDFSKEEDPIRLCSGSDDSTVRVWKYIGDDEDDQQEWVCESTLPNAHRSQIYGVAWSPSGRIASVGADGVLAVYKEKQNDSEVSEWEISATYKAAHTVYEINTVKWVNIDGKEMLITAGDDGRVNLWNYQD", "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": "MLLNDLIQRQQTRWKASFLVVSILMVATCILSLSIGEMWILPWSPDGALEQQLLTQLRMPRLIAALAIGASLAASGAVLQVLLGNPLAEPGVLGISGGASLALVILLFALPFVPTPLLTMLAAMLGALIFTLILVGLSRRRKVSTARLLLIGVALGILSGSVVTWAFYFSDDLNLRQLMYWLMGSVGGVSWQQLSVLLFVVPVLVWLCLQGKKLDLLMLGEIQAKQLGLDVAALRWRFILIVSLLVGASVALGGVIGFVGLVIPHLLRMSLGAENRYLLPLSALCGGLLLALADTLSRVILPSAELPVGVVTTTIGAPIFVWMLLRSHID", "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": "MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGLHHHRINFDKYHPGYFGKVGMKHYHLKRNQSFCPTVNLDKLWTLVSEQTRVNAAKNKTGAAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKSVGGACVLVG", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
+{"protein": "TMELLEDLIEQVRQLPMVNFIEKNSLVHANEFTVAKGAPWGLARISHRDPLSLGSFDQYLYDSNGGTGVTSYVIDTGVNVHHEQFEGRAKWGKTIPQGDEDEDGNGHGTHCAGTIGSNAYGVAKNAEIVAVKVLRSNGSGSMSDVIKGVEFAVKSHQDSVKKGKNSFSTANMSLGGGKSPALDLAVNAAVKAGLHFAVAAGNENQDACNTSPASAENAITVGASTISDARAYFSNYGKCVDIFAPGLNILSTYIGSDAATAYLSGTSMASPHIAGLLTYYLSLQPSSDSEFFIGAEGITPAQLKKNLIAFGTPDVLADIPADTPNILAFNGAGQNLTKFWGH", "text": "FUNCTION: Serine protease. SIMILARITY: Belongs to the peptidase S8 family."}
+{"protein": "MAAHLLIVDALNLIRRIHAVQGSPCVETCQHALDQLIIHSQPTHAVAVFDDDARSSGWRHQRLPDYKAGRPPMPDDLHNEMPALRAAFEQRGVRCWASDGNEADDLAATLALKVTEAGHQATIVSTDKGYCQLLSPGLRIRDYFQKRWLDAPFIEKEFGVLPRQLPDYWGLAGISSSKVPGVAGIGPKSATQLLIQFQNLEGIYAHLDEVPEKWRKKLETHKEMAFLCRDIARLQTDLHIDGNLQQLRLAR", "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": "MSAEIKGSTQVKAGLAQMLKGGVIMDVVNAEQARIAEAAGACAVMALERVPADIRAQGGVARMSDPSMIKEIQAAVSIPVMAKVRIGHFVEAQILESIGVDYIDESEVLTPADDINHIEKSKFTVPFVCGSRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHTRQMQGELRRVKSMSPDELYTYAKEIAAPIDLVKECAQLGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFLSGDPAKRARAIVRAVTHYNDPKILAEVSENLGAAMVGRSVSSLEEKEKLATRGW", "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": "MPREKKKRGRRAEKSQSKRKWEDDEVPTSPKRQRTADEDNEAQAGDDYIPLDTRDTEKEQEQGQEDDTPFYGLLDAEEQEYFSKASQTLELNSFEDDDDKRLFIESVYAEARGKELKIACRQVKTLFEKFTGHFLHLVQHRFASHCCECLFIRAAPIVTSEMEKPKDRKKERKQTIENNGEEGGQDEPLNQRSAMELFLGVISELEGNWGYLLTESFASHTIRVLLLILAGEPLAGQSNARVLASRKKENVDSITPTSQSELTIQGSRQVPVEFNNTLRRMISDLSAGLNSTYLQALATHPIGSPVLQVILSIELGCMGTEKLKDKNSVFRRLIPDDTLETKEEGVNFLNSLFYDPVGSRLLETIVRVAPGKFFKTFYKNIIRERIGSLARNEIASYVVIKVLERVSREDLESAIESILPEIPSLVQRSRLNVIKTIIDRSIIRSADTASLAKALESAYGEDGLARLKAILGVETKDKDAEDLAKVKPKAGTSPQHIHGSLLAQSMLQASGTLAAMIQSSFLTAPTETLIQIANNPTASRALQEALKPSKLNTQFRRQFLPRFYGQMCDLSLDSSGSHVADALWDATSDLIFIKQRLAQELADNEPALRDSFLGRAVWRNWSMDLYKRKRGEWMSKAKGLDNTKVSPSTADSSAGPAKSKLDLARARYAARAEQQEKPDGKDQGSRGKKQALSAPSGLLKAQ", "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": "MRKHAKKIIRIIKMKLKLVAVAVTSLLAAGVVNAAEVYNKDGNKLDLYGKVHAQHYFSDDNGSDGDKTYARLGFKGETQINDQLTGFGQWEYEFKGNRTESQGADKDKTRLAFAGLKFADYGSFDYGRNYGVAYDIGAWTDVLPEFGGDTWTQTDVFMTGRTTGVATYRNTDFFGLVEGLNFAAQYQGKNDRDGAYESNGDGFGLSATYEYEGFGVGAAYAKSDRTNNQVKAASNLNAAGKNAEVWAAGLKYDANNIYLATTYSETLNMTTFGEDAAGDAFIANKTQNFEAVAQYQFDFGLRPSIAYLKSKGKNLGTYGDQDLVEYIDVGATYYFNKNMSTFVDYKINLLDDSDFTKAAKVSTDNIVAVGLNYQF", "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": "MANREVPVTDRYPLLNLLPNYQTPPRPIPPQQPHAPKKQSRRRLESDLDSVQSQSPLSPTECPWTILTTHSTVTVQATTQDGTSVVVTLRL", "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": "MAPSVTIDNISDFSPITTTTKTTSFNLRTLLLAPPSIASHEEKLRNVLATHDRSVTDLQMLDRLSAGLVTLPESTYDLVLILTDADGTRAESTELLTRDVFGKITQALKTGAKLQAQDGTFGQEIDGAEYREAILAGLVTEGGVMLKPDHSASVAVPLRLRRKDNSKTTAVSNAGPPVSTVEVPVSGKRKSVDMTEDVPEKDVPKNDVPKGVGFIDFSDDFDAEDDDDELIDEDTLLTEEDMKKPLAIPPECAPRAGKRRRACKDCTCGLAEKLAKEDAEKRATADSQLQALKLDADDLAEVDFTVKGKVGSCGNCSLGDAFRCDGCPYIGMPAFKPGEEVRLLNNDVQL", "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": "MANSGLQLLGYFLALGGWVGIIASTALPQWKQSSYAGDAIITAVGLYEGLWMSCASQSTGQVQCKLYDSLLALDGHIQSARALMVVAVLLGFVAMVLSVVGMKCTRVGDSNPTAKSRVAISGGALFLLAGLCTLTAVSWYATLVTQEFFNPSTPVNARYEFGPALFVGWASAGLAMLGGSFLCCTCPEPERANSIPQPYRSGPSTAAREPVVKLPASVKGPLGV", "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": "MTGMSNVSKLAGEPSGQEFLVFTLGNEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRVKFCEGDVEYDDNTVVIVLNLGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLSTEYLTGLGALGERMLILVNIEKLLNSEEMALLDIAASHVA", "text": "FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MEKHLPLIVNGQIISTEENRFEISFEEKKVKIDSFNNLHLTQMVNHDYLNDLNINNIINFLYTTGQRWKSEEYSRRRAYIRSLITYLGYSPQMAKLEANWIAMILCSKSALYDIIDTELGSTHIQDEWLPQGECYVRAFPKGRTMHLLAGNVPLSGVTSILRGILTRNQCIVRMSASDPFTAHALAMSFIDVDPNHPISRSISVLYWPHASDTTLAEELLSHMDAVVAWGGRDAIDWAVKHSPSHIDVLKFGPKKSFTVLDHPADLEEAASGVAHDICFYDQNACFSTQNIYFSGDKYEEFKLKLVEKLNLYQEVLPKSKQSFDDEALFSMTRLECQFSGLKVISEPENNWMIIESEPGVEYNHPLSRCVYVHKINKVDDVVQYIEKHQTQTISFYPWESSKKYRDAFAAKGVERIVESGMNNIFRAGGAHDAMRPLQRLVRFVSHERPYNFTTKDVSVEIEQTRFLEEDKFLVFVP", "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": "XNNIVFYSLGNVNSYQGG", "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": "MFDIKSIIRPNILTLEPYRCARDDFKTGILLDANENTHGPAIPTPDETELALELNRYPDPHQLELKQQVIDFREKHPNKYTKEKLSVENLCLGVGSDESIDMLLRCVCVPGKDKMLICPPTYGMYSICATVNDVVIEKVPLTVPDFQIDIPAILSKVKSDPNIKLLYLTSPGNPTGKLINVDSIITLLEELLNCWQGLIVVDEAYIDFTEPGSSMSTLVNQYPNLVVLQTLSKSFGLAGIRLGITFCSKELSWYLNAMKYPYNISSLTSNVALKATKQGLEIMENYVSKITEQRDIVLQKLLSLKYVGRNIGGLDSNFVLVEVLDKQGNPSNEVAKQLYNTLATGKSIVVRFRGSELNCVGGLRISIGTEEENKQLLEQFEAVLNDINQ", "text": "SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MMTFHPSPPQLTLIKSMLFIAALLPFGRLALFTLTDQLGANPIEFITRNTGDWTLYFLCMTLAITPLRRLSQWNWLIRLRRMLGLFAFFYACLHFTTFLWFDHFFDVNEMLKDVVKRPFITVGFSAFVLLIPLAITSTNGMVKRLGGKRWQWLHRLVYVIAALGILHYWWMKAGKHDFEQPIIFGTIVAVLLLVRVFWAWQKRSKNNALAGTSDCRTG", "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": "MSKTAIITGAAGGLGKGIAERLANDGFNIVLQDINEALLLETEKEFKEKGYQAVAYKSDVSKKKEQEELVQFAVTEFGQLDVMVNNAGVDAVTPILEIGEEELSKLFNINVFGTLFGIQAAANQFIKQKSKGKIINACSIAGHESYEVLGTYSATKHSVRSFTQTAAKELADKGITVNAYCPGVAKTEMWDRIDEEMVKLDDSLEIGDAFEAFSSEIKLGRYQEPSDVANLVSFLASNDSDYITGQSILTDGGLVYR", "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": "METWFLYFITKSISYALFMVLIVTFLESLALVGLFLPGIVLMSILGTLIGNGTLSFYPAWIVGIIGCMCGDWISYYCGFKFKKCITNLHLLKNNNVVLDKITNTLTNYPITTILLGRFIGPTRPLVPMVCGMLNISLKTFIIPNILGCILWPPIYFLPGIFTGIAISNTTNYSENTYFKIQFLAAILLIWLGIFLLWKLWKRYTDTGKKKIYISNVNLCLLLTISLSAGITIMIYIQSNSTLIFFRKILWKILISSQ", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DedA family."}
+{"protein": "MAGGPANWARAITGGSVVIGFGYLLLKTATPNEQQLYDSLSPDLKRRVDAQRSSQADSERSAKVKEEQSKRLV", "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": "MTNTVSTMILFGSTGDLSQRMLLPSLYGLDADGLLADDLRIVCTSRSEYDTDGFRDFAEKALDRFVASDRLNDDAKAKFLNKLFYATVDITDPTQFGKLADLCGPVEKGIAIYLSTAPSLFEGAIAGLKQAGLAGPTSRLALEKPLGQDLASSDHINDAVLKVFSEKQVYRIDHYLGKETVQNLLTLRFGNALFEPLWNSKGIDHVQISVAETVGLEGRIGYFDGSGSLRDMVQSHILQLVALVAMEPPAHMEANAVRDEKVKVFRALRPINNDTVFTHTVTGQYGAGVSGGKEVAGYIDELGQPSDTETFVAIKAHVDNWRWQGVPFYIRTGKRLPARRSEIVVQFKPVPHSIFSSSGGILQPNKLRIVLQPDETIQISMMVKEPGLDRNGAHMREVWLDLSLTDVFKDRKRRIAYERLMLDLIEGDATLFVRRDEVEAQWVWIDGIREGWKANSMKPKTYVSGTWGPSTAIALAERDGVTWYD", "text": "FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone. SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family."}
+{"protein": "MKNIFRRSVQIFHKDKKEGDKQDYTGSSGSSGNSGTDRSPTSSLSKKDKKHSKHHQNESYSGDNSPTLSRNHHDEIGHLQYTANHHIATSHHSHSHNHNHNHNHQLTQPIQQQQQTQHVNLASNNYYIRHIYTNNQYDETTQIVMNNGIPFIYNPNARKIFGVPLTQVPCRAGSNVPIIIEKLIDHIERTSLNSEGLFRIPGVDLTINQYIKLFDNGEDVDVSPIEPYTAAGLLKRFFRDLPVFVPQSINKRVVSLFIDEEGKKKPVDMEILSNLRVLVHQLPTVHFEVMQELTNLLGKLMSRSDQNKMTISNIAICLVPTLNCVPAIVTYSIQMHDFFYNEVFPQHHLYYMRPYEEKLVESAPTQPINIMTTSGGEKRYSSRPASITISGLLPSNGQNNSPSSSTITSTTITSPHDSTAPITFTVTTTFSPEQQQQMLQQQQQQQQQQEKQSSSSLSQSQQSIQPISDTNSTKSDRRTFRVDPNLDLTQYIEDTQYNVNRNYLYNGGPSGTTGTTPNGGSLSIGGGNGGNGGSSLSVGSGGGNGGSSLSVGSNTSVGVGGGGGGNNTTDQSKIYRRSVAYTNNEDTKAAIQQIKEKIDRYSKEKKTREEKEREKLLRYSIDLERYKDRTINNKQEKRASRDINKEIEREIEKKRLSPRERLNLFGLSSSSSSVNSTLTRSTANIISTIDGSGGSNRNSKNYGNGSSSSSNRRYSNTINQQLQMQLQQLQIQQQQYQQTQQSQIPLQYQQQQQQQQQQTTTTTTTSSGSNRFSSNRYKPVDLTQSSSNFRYSREIYDDDYYSNNNLMMFGNEQPNQTPISVSSSSAFTRQRSQSCFEPENLVLLQQQYQQYQQQQQQQQQIPFQANPQYSNAVIEQKLDQIRDTINNLHRDNRVSRDYTHYLREVEDLRSSLQKETVVSNEFIKNIELEDKLRREEEKNQRLIEEIHLLETYFILKEKSKAKRLSTTKDLLTRSRSPTLPSSINMSTSSLGSSSSSAYNNNNNNNNVPK", "text": "FUNCTION: Rho GTPase-activating protein involved in the signal transduction pathway. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MEVAIPKDLQQEASLAKKRYMDLCRQGQIFDARNRIIGGDTQAWDVQVRNQKIKEVTEKARDETFAAEMRHNDKVMCIMHDRELRHRKQLCRAINDFQQRFQKPETRREFDLSDPLALKKELPARVSDNDMRNTISGMQKFMGEDLNFQERKRIQKEQNREWSLQQHGEWERAQAEHKLAEHLHTQTELKFDEAARDLQRLEITTRKAVCAAVKEFNKKQVVELAERKRQVKQQEQEDNMSEITNLLHGDLLSENPQQAASNFGPRHVMLDRWKGMNREQLEEIWSTWKQQIHEKLRLQEEERQHNMDWDLRRTRKAHASLLQERQQQRLLREQRRALDCSNLSLAKQQYLQKRQLDAAPSSQPTEDYFSQFNTRSR", "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": "MSSISLIQPDRDLFSWPQYWAACFGPAPFLPMSREEMDQLGWDSCDIILVTGDAYVDHPSFGMAICGRMLEAQGFRVGIIAQPDWSSKDDFMRLGKPNLFFGVTAGNMDSMINRYTADRRLRHDDAYTPDNVAGKRPDRATLVYTQRCKEAWKDVPVILGGIEASLRRTAHYDYWSDTVRRSVLVDSKADMLMFGNGERPLVEVAHRLAMGEPISEIRDVRNTAIIVKEALPGWSGVDSTRLDTPGKIDPIPHPYGEDLPCADNKPVAPKKQEAKAVTVQPPRPKPWEKTYVLLPSFEKVKGDKVLYAHASRILHHETNPGCARALMQKHGDRYVWINPPAIPLSTEEMDSVFALPYKRVPHPAYGNARIPAYEMIRFSVNIMRGCFGGCSFCSITEHEGRIIQSRSEDSIINEIEAIRDTVPGFTGVISDLGGPTANMYMLRCKSPRAEQTCRRLSCVYPDICPHMDTNHEPTINLYRRARDLKGIKKILIASGVRYDIAVEDPRYIKELATHHVGGYLKIAPEHTEEGPLSKMMKPGMGSYDRFKELFDTYSKQAGKEQYLIPYFISAHPGTRDEDMVNLALWLKKHRFRLDQVQNFYPSPLANSTTMYYTGKNPLAKIGYKSEDVFVPKGDKQRRLHKALLRYHDPANWPLIRQALEAMGKKHLIGSRRDCLVPAPTIEEMREARRQNRNTRPALTKHTPMATQRQTPATAKKASSTQSRPVNAGAKKRPKAAVGR", "text": "SIMILARITY: Belongs to the UPF0313 family."}
+{"protein": "MSGGKGKVGSSEKASTSRSAKAGLTFPVGRIHRLLRKGNYAQRVGSGAPVYLTSVLEYLTAEILELAGNAARDNKKSRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVLPNIHQSLLPSKKSIKGASQEL", "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": "MTIFQKSFILLIIWNFSLFAFSDMKIEITHGINTAHPIAVIPFINNENITHELNNDNIEDIASIIAADLRNSGKFNTLPIAYLPYQPSKLTDIIPTFWEKLGINTVVLGAINIKNENYVISYQLIDTSNNPALVILDNQYEIEKKHLRYTAHTISDEIFEKLTGIKGVFCTRIAYILYTNNIKYAYELCTSDYDGHNQVSICRSSEPLMSPAWSPDGKKLAYVTFASGHSELIIQTLTNRSIDNIIQFPNHNGAPAWSPDGKKLAFSLSKTGSLNLYIMDLSSNNIQQITSNRYNNTEPSWFPDSQNLAYTSDQGGVPQVYKININNNRDSHRISWLNGSNQKPNISMDGTFMVMVNRNKGKQYISKLNFLTGEEETLTADSVLADTPSISPNGIMFMYSSIILNNSSSELYLDKKFTNIPDNNQSILSLASIDGKFKAHLNGSTGSIRFPTWSSLSCSY", "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": "MKIVVYHAEECDRKKCTSLKLGRKGKFKIVSSLNQLPRGALVLNPFSEKAVSPEDRDMVLRRGIAALDCSWKKVKKSSVIFQTARNHRSLPFLVAANPTNYGKPCILSTAEAVAATLYIVGLKDIASDIMSYFKWGPHFLDLNRELLEAYSRAENSLEVVEIQKKFIGG", "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": "MADAPGLIPIFLLGYLLSTECAVFLDRENATKILTRPKRYNSGKLEEFVQGNLERECIEERCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGICKDDINSYECWCQAGFEGRNCELDATCSIKNGRCKQFCKNSPDNKIICSCTEGYQLAEDQKSCEPAVPFPCGRVSVAYNSKKITRAETVFSNTDYGNSTELILDDITNSTILDNLTENSEPINDFTRVVGGENAKPGQIPWQVILNGEIEAFCGGAIINEKWIVTAAHCLKPGDKIEVVAGEHNIDEKEDTEQRRNVIRTIPHHQYNATINKYSHDIALLELDKPLILNSYVTPICVANKEYTNIFLKFGSGYVSGWGKVFNKGRQASILQYLRVPLVDRATCLRSTKFSIYNNMFCAGYREGGKDSCEGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT", "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": "MAASMARRLWPLLTRRGFRPRGGCISNDSPRRSFTTEKRNRNLLYEYAREGYSALPQLDIERFCACPEEAAHALELRKGELRSADLPAIISTWQELRQLQEQIRSLEEEKAAVTEAVRALLANQDSGEVQQDPKYQGLRARGREIRKELVHLYPREAQLEEQFYLQALKLPNQTHPDVPVGDESQARVLHMVGDKPVFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPARFKDLNLAGTAEVGLAGYFMDHTVAFRDLPVRMVCSSTCYRAETNTGQEPRGLYRVHHFTKVEMFGVTGPGLEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVTSASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPALQSYLGTDRITAPTHVPLQYIGPNQPRKPGLPGQPAVS", "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": "MGNVPGKEQQVRNARSVSEDYHREGQVRSKRPSAPREKKREPRVFVDPNEQVDGGYLVPQGVYTGPQDFDILVVKSLMTSRKLAPFFKGLQDYEEEWTDHQLMAAIRGFPIPSAASESPTTESTDTKDASASTSTPHAISTPSHLSPPTAPPQVAISPPRHTLSSNNPFRDPLEHMSHLRIDLDNTTFSQSAPTPSWMRSGEPDQEDGDELINPGILQSPPSREAPKPPPSRQRAKTLTNKEPPLMVKIYRDPIECPICFLYYPNSLNMTRCCAQPICSECFVQMKRAEPHPRHDEPEPDTLLGQLDLISEPTACPYCAMSDFGVVYSPRHGPGAKAAGANSADAAAAKGNGDESAIDDSGDSSDGIDTTNMDDVADKLMHMSGAKRRSSISVTNPNVVTVDRVRPDWSKTLAAARARAARKAATANALHATAFVEGGNGEVAGSSRSSRRTRQNHEQRQAARAQELEQIMLSEAMRLSMLESQEAEEKRSREQESK", "text": "FUNCTION: May negatively regulate the SNF1 kinase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIP5 family."}
+{"protein": "MTQSTVSSTIVEPYAEALMSVAQSNNLTNQIGEDVSFVLSLLQTSDDLKDFLVNPLTPADAQKAVLRQLAESRVQKQFFNFLLLLIDRRRIIFLEGICKYYQALLRKLNNTVLAEVTSTVELTDEQRHAITDKVKHMSQAAQVDLETSIDPDLIGGVIIKIGSQVLDASIRGQLRRMNSSITSLS", "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": "MTSRNYLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNIGVVEQIRQQLTALATASEGYTSVLLQGSGSYAVEAVLGSALGPQDKVLIVSNGAYGARMVEMAGLMGIAHHAYDCGEVARPDVQAIDAILNADPTISHIAMVHSETTTGMLNPIDEVGALAQRYDKTYIVDAMSSFGGIPMDIAALHIDYLISSANKCIQGVPGFAFVIAREQKLAACKGHSRSLSLDLYAQWRCMEDNHGKWRFTSPTHTVLAFAQALKELAEEGGVAARHQRYQQNQRSLVAGMRALGFNTLLDDELHSPIITAFYSPEDPQYRFSEFYRRLKEQGFVIYPGKVSQSDCFRIGNIGEVYAADITALLTAIRTAMYWTK", "text": "FUNCTION: Involved in phosphonate degradation. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. PhnW subfamily."}
+{"protein": "MARFSVCGGDDGEGPSNNNHQSRKRQRLPSIDENEEDAETSDAGSSGEEDEDETQNQGMRPESEDRGSTSDDSDREVVIEERRFGKFVNSQSSSSSKDSPLSVTLLDPDVLDCPICCEPLKIPIFQCDNGHLACTLCCTKVRNRCPSCTLPIGYVRCRAMEKVIEASRVSCLNAKYGCKESTSYGNRFSHEQVCVFTPCSCPILDCHYTGYYKDLNNHVRAEHKDDLISFVWNTRLTISLDLNKKTTILQEENDGHVIVVQVFRALHAVYVSVSCIAPLTPGVGRLSCRLAKITVDSLLKQGFMVKNIQKVTNEHPEDGFMLIPSYLFSGNDNLNLQIWIGHGRIFVHS", "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": "MKIPVLDKGFVELVDVMGNDLSAVRAARVSFNMELKDEEKDRRLVEYLMRHGHESPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLTYEFYIPPLQRFGQTRIVPEKVIEKISHVVNESYQTYMELLEAGVPREVARIVLPLNLYTRFYWTVNARSLMNFLNLRADSHAQWEIQQYAVAIAKIFREKCPWTYEAFIKYAYKGDLLREV", "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": "MKILISVCGEGFGHTTRCVAIGEALKNDYEISYIAYGKSKNFIEKYGFKVFETFPEIKLKGKDGKFDITSSILNKEYSPKKAIRREINIIREYNPDLIISDCKYSTVVAAKLLKKPVICISNQNYTRYKLKTDLIVYPTMKALNIINERCERFIVPDFPLPYTICEYNLKIIKNMEFIGPLIRYDVDDVDNYGEDYILSVIGGFEYRYKILEELGKIALKNNLNVKLVCGSYEVAKKLMRDLNLNSYKNENVEIIPITTNMKELIKNAELIVSHGGHSTIMEALSFGKPLIVIPDLDHPEQGNNAKKVHDLGCGIALSYKELYRLEEAILDIRNMKMYKRNASKMKELAKKYDGKKNIKKIIDEFFETRKNIRKYYLTDRIANKLINKFKLKIR", "text": "SIMILARITY: Belongs to the glycosyltransferase 28 family."}
+{"protein": "MHINQLLQHANSDLPLLQANFGLERESLRINKTNHRLAQTPHPTALGSRQFHPYIQTDYSESQMELITPVAHSSKEVLRFLGAITDVAERSIDQNQYLWPLSMPPQITEDEIEIAQLEDDFEFSYRQYLDKKYGKILQSISGIHYNMELGADLMNELFELSGYQSFIDFKNDLYLKVAQNFLNYRWFLTYLYGASPLAEKGFLNEELSQTVRSIRNSHLGYVNTDDIKVPFDSLENYISSIEHYVKSGALSAEKEFYSAVRLRGSKHNRDYLTKGITYLEFRCFDLNPFNNRGITQETIDSVHLFILAMLWLDTPKKLNQALDKAQKLNDKIALSHPLEKLPKENSASLIIEAMEALIKHFKLPSYYDDLLIAIKKQVENPKLTLSGRLFEHIKHASLEHFGQKKGQDYHNYAWQNYYALKGYENMELSTQMLLFDTIQKGIHFEILDENDQFLKLWHNDHIEYVKNGNMTSKDNYVIPLAMANKVVTKKILRENGYPVPAGAEFDNKDEALRYYSQIKNKPIVVKPKTTNFGLGISIFETAASHNDYEKALDIAFIEDYSVLVEEFIPGTEYRFFILDGKCEAVLLRVAANVVGDGHSTVRQLVAQKNRDPLRGREHRSPLEIIDLGDIELLMLQQEGYTLEDILPKGKKVNLRGNSNISTGGDSIDVTETMDPSYKQLAANMATAMGAWVCGVDLIIPDTNLKASKGKPNCTCIELNFNPSMYMHTYCYQGPGQVITGKILAKLFPEISTKI", "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": "MAKRTLGLAKAAKAKKQKKEQEHQEISASPDEESSSSNQLTIELPEEIDANNEISQLKGLHKTYLQSERDNELLVNGIIHECDRLLRENDSENKQPLPAVFHAIYAIALAELSKFHTEELDKVKEFFIAALERVELGLEKNPNDINLLVAKTKILLDQISLQYIAPLTLESDVKELDKEIDELLDAALSVYESVEARAKELKDYSIFDDSETLDILEALDDILDIVDNFGKENQGDDGSDEDDDEDDDEEEKSVELAETHPLYKIKNSDKYDQWWRDHTHLYLDNLEKLENGSPELKREVCHRLGQSYLQESEVPYSVFTTLKYDDEYDGIEELEGLTEKEAQKISQELITKALDYLKQAKDEEDPETWVSIAEAMISLGNLYEVDSKEQEDLYLEAEKILKRANNVTNGKFQEELDNLLP", "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": "MIMKTYFSGVSTLGVHSLATEDYGFFPLSVDQKTMERMKNVLDIPATQLNISNSSLIGSLCVGNSNGLLVPNITTEKELELIKMFLKENSLDVNLERLKAKNTAFGNLILTNNKGCIISEELSRFRKTIEDVLDVESGVGNYAELPTVGSNGVATDKGCLVHPLTDELELEWIQDILRVDYVERGTANRGVTSVGACILANTKGAVVGGDTSGPEILKIEEALDLID", "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": "MAFVTMKHLLAEAKREHYAVGQFNINGLQWTKAILQAAQKEQSPVIAAASDRLVDYLGGFKTISAMVGALMEEMAITVPVVLHLDHGSSAERCRQAIDAGFSSVMIDGSHHPIDENIAMTKEVADYAAKHGVSVEAEVGTVGGMEDGLVGGVRYADVAECERIVKETNIDALAAALGSVHGKYQGEPNLGFKEMEAISRMTDIPLVLHGASGIPQEQIKKAITLGHAKININTECMVAWTDETRRMFQKNGDLYEPRGYMTPGIEAVEETVRSKMREFGSAGKAVKQQVG", "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": "MSLGALISESRNPATMELDKLSTLAMLTCINDEDRKVPDAIRLVLPAVAQAVDLAADALKQGGRLIYLGAGTSGRLGVLDASECPPTFGVPHGMVIGLIAGGPGALLKAVEGAEDDIALGMRDLQDLQLTATDMVVGLAASGRTPYVIGALRYARELGCPTAAISCNPDSPIAQEAQVAISPVVGPEALTGSTRMKSGTAQKLVLNMLSTGAMVKLGKVYQNLMVDVKATNVKLVDRACRIVVEATGVSRAEAEHALRQTDFEVKPAILMLLKGVSAEQARQDLRQHHGYLRAAL", "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": "MELEKNERINALFAFYQPLLTAKQNDYLQLYYADDYSLGEIATEFSVSRQAVYDNIKRTEKILEGYEQKLHLYAEFEARNQQADRIRDYVLSHYPTDQTLRDLIDGMENLEAK", "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": "MSTNHLLEIKQYGQSIWMDNLTRDIIQSGELKDMVENQGISGITSNPAIFEKAIAGNAIYDADIEAGVRAGLPIYKIYESLVFADIRNACDILRPVYEASNRLDGYVSIEVPPTIAHDTEATISEARRYFQEIGRENLMIKIPGTEPGLPAVEQVIAEGMNVNITLLFSVESYVNTAWAYVRGLEKRLAEGKDISRIASVASFFLSRIDSNIDAKIDAKLKKGVDDIAVEAKLKAVKGKVAIANAKLAYQEYKKIIRSERWQELVAKGATVQRLLWASTSTKDPNYNDVMYIEELVGPDTVNTVPPATIKACADHCNVSDRLETDVNNAYTLIENLKDPDINIDLDTVMDELLVEGIDKFIQPFQSLMNSLEDKIKVLSPV", "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": "MSFAEKITGLLARPNQQDPIGPEQPWYLKYGSRWLGIVAAFFAILFGLWNVFSIITLSVSCLVAGIIQMVAGFVVMLLEAPCCFVCFEQVNVIADKVDSKPLYFRAGLYIAMAIPPIILCFGLASLFGSGLIFGTGVVYGMMALGKKASAEDMRAAAQQTFGGNTPAQTNDRAGIVNNAQPFSFTGAVGTDSNV", "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": "MKWQQRVRVATGLSCWQIMLHLLVVALLVVGWMSKTLVHVGVGLCALYCVTVVMMLVFQRHPEQRWREVADVLEELTTTWYFGAALIVLWLLSRVLENNFLLAIAGLAILAGPAVVSLLAKDKKLHHLTSKHRVRR", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MKRAAIRLWTLNKGLLTHGRGLSQGSQYKISEPLHIHQVRDKLREIVGVSTVWRDHVKAMEERKLLHSFLPKSQKVLPPRKMRDSYIEVLLPLGTDPELRDKYVTVQNTVRFGRILEDLDSLGVLVCYMHNHNHSTKMSPLSIVTVLVDKIDMCKHSLSPEQDIKFTGHVSWVGNTSMEVKMKMFQLHNDEKYWPVLDATFVMVARDSENKGPAFVNPLIPENKEEEELFKQGELNKSRRIAFSTSSLLKVAPSSEERNIIHELFLTTLDPKTISFQSRILPPKAVWMEDTKLKSLDICHPQERNVFNRIFGGFLMRKAYELAWATACSFGGSRPYVVTVDDIMFQKPVEVGSLLFLSSQVCFTQDNYIQVRVHSEVSSLDSREHMTTNVFHFTFMSEKEVPLIFPKTYGESMLYLDGQRHFKSMSTPVTLKKDYPVEP", "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": "MRVIRPVEHADIAALMQLAGKTGGGLTSLLANEATLAARIERALKTWSGELPKGEQGYVFVLEDSETGEVGGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPEWRKEGNGYLLSKSRFMFMAAFRDKFNEKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSEEAQAVIGEVHPQTAPARVVLEKEGFRYRHYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPALGDYPACLVANENYHHFRAALVRADPQTSRLVLTAAQLDALKCRAGDHVRLVRLCAEEKTV", "text": "FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. SIMILARITY: Belongs to the arginine N-succinyltransferase family."}
+{"protein": "MDPAVASLGILALTTASAIIGQTIEDVETNIGSQSNPNSQVQLAPQMGNLHRFFNKAIAGEPFAYCTFCGVSGAITVATLYLHLPAVIALAIGAAITTLIWLAYSTTAYLGRVSGSATFNQPVFLDMLTENLGPIAGHAFIVFFCMTGVAYLMTLPVKGFAHPFPIPVIGMIWGMTIGAIGSAVGDVYYGAEAEFVHKKFGGGIPVASHGDITRKGVLGARSPMEVGNFTVKYGSPITGMAFGLIVLSITRGVYNIE", "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": "MVPQAHGLLLLCFLLQLQGPLGTAVFITQEEAHGVLHRQRRANSLLEELWPGSLERECNEEQCSFEEAREIFKSPERTKQFWIVYSDGDQCASNPCQNGGTCQDHLKSYVCFCLLDFEGRNCEKSKNEQLICANENGDCDQYCRDHVGTKRTCSCHEDYTLQPDEVSCKPKVEYPCGRIPVVEKRNSSSRQGRIVGGNVCPKGECPWQAVLKINGLLLCGAVLLDARWIVTAAHCFDNIRYWGNITVVMGEHDFSEKDGDEQVRRVTQVIMPDKYIRGKINHDIALLRLHRPVTFTDYVVPLCLPEKSFSENTLARIRFSRVSGWGQLLDRGATALELMSIEVPRLMTQDCLEHAKHSSNTPKITENMFCAGYMDGTKDACKGDSGGPHATHYHGTWYLTGVVSWGEGCAAIGHIGVYTRVSQYIDWLVRHMDSKLQVGVFRLPLL", "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": "MALQADFDRAAEDVRKLKARPDDGELKELYGLYKQAIVGDINIACPGMLDLKGKAKWEAWNLKKGLSTEDATSAYISKAKELIEKYGI", "text": "FUNCTION: Binds medium- and long-chain acyl-CoA esters. SIMILARITY: Belongs to the ACBD7 family."}
+{"protein": "MADLDDIKDGKDFHTDKPQTNTLFALKGCGALDWGMQSRLARIFNPKTRKTVMLAFDHGYFQGPTTGLERIDINIAPLFEYADVLMCTRGILRSVVPPAINKPVVLRASGANSILTELSNEAVAVAMDDAVRLNSCAAAAQVYIGSEHEHQSIKNIIQLIDAGLRVGMPIMAVTGVGKDMARDQRYFSLATRIAAEMGAQIIKTYYVDKGFERIAAGCPVPIVIAGGKKLPEREALEMCYQAIDQGASGVDMGRNIFQSEDPVAMIKAVHAVVHHNETAERAYELFLSEKG", "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": "MRMVDIIEKKRDGKSLSKEEIEFFIKGYTNGDIPDYQASSLAMAIFFQDMNDEERAALTMAMVNSGDVIDLSKINGIKVDKHSTGGVGDTTTLVLAPLVAAVGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISEEDFIKLVNENQVAVIGQSGNLTPADKKLYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGNGAFMKTLEDAEALAHAMVSIGNNVGRNTMAIISDMSQPLGRAIGNALELKEAIDTLNGKGPEDLTELVLTLGSQMVVLANRANTLEEARQLLNEAIENGSALEKFKTFLENQGGDVSVVDAPELLPTATYQIEYKAQSSGVVSELIANEIGVASMMLGAGRQTKEDEIDLSVGIVLNKKVGDVVKEGESLLTIHSNRENVDDVIKKLDESIEIQAQATTPTLIHKIITE", "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": "MAFADYPVQSLMYITNRPEIVFTEGKGSWLTDHNGKRYLDFVQGWAVNCLGHSNDGMIEALNAQAKKLINPSPAFYNEPMAKLAGLLSAHSCFDKVFFANSGAEANEGAIKLARKWGKKHKSGAGKNRFEIITFDHSFHGRTLATMSASGKAGWDTIFAPQVPGFPKAILNDIASVEALITDETVGVMLEPVQGEGGVLPATQEFMQQLRALTRKHKLLLIVDEVQAGCGRCGTLFAYQLSNIEPDIMTLGKGIGGGVPLSALLCTDEVASFEAGDQGGTYNGNPLMTAVGCSVIEQLLAPGFLAGVQERGAYLRAQLLELSEAFGLAGERGEGLLRALLLGKDIGGQLVEAAREMNPTGLLLNAPRPNILRFMPALNVTTDEIDTMIGMLRTLLKAHG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily."}
+{"protein": "MENIEKLLMQEKILMLELDLVRAKISLARANGSSQQGDLPLHRETPVKEEAVHSALATFTPSQVKAIPEQTAPGKESTNPLMASILPKDMNPVQTGMRLTVPGDFLRPHQGIPIPRKSELSSTVAPLRAESGIQHPHINYYVVYNGPHAGIYDDWGCTKAATNGVPGVAHKKFATITEARAAADAYTTSQQTDRLNFIPKGEAQLKPKSFAKALTSPPKQKAHWLTLGTKKPSSDPAPKEISFDPEITMDDFLYLYDLVRKFDGEGDDTMFTTDNEKISLFNFRKNANPQMVREAYAAGLIKTIYPSNNLQEIKYLPKKVKDAVKRFRTNCIKNTEKDIFLKIRSTIPVWTIQGLLHKPRQVIEIGVSKKLVPTESKAMESKIQIEDLTELAVKTGEQFIQSLLRLNDKKKIFVNMVEHDTLIYSKNIKETVSEDQRAIETFQQRVISGNLLGFHCPAICHFIVKIVEKEGGTYQCHHCDKGKAIVKDASADSGPKDGPPPTRSIVEKEDVPTTSSKQVD", "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": "MKLNLYVLTPKRIIWDCEVKEIILSTNSGQIGVLPNHAPINTAVDMGPLRIRLLNDQWLTAVLWSGFARIVNNEIIILGNDAELGSDIDPEEAQQALEIAEANLSKAEGTKELVEAKLALRRARIRVEAVNWIPPSN", "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": "MTLADAQPQALNFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMIFAEPRYAMAELEEGDISAQLNDYNELKRLCEQIKRDRNPSVIVFIGTCTTEIIKMDLEGLAPKLESEIGIPIVVARANGLDYAFTQGEDTVLAAMAQRCPTQAPTAEADKEERNAIQKLMNFGRKQEDVKREESEYVDHPPLVMFGSVPDPIVTQLSLELKHQGIKVSGWLPAKRYTELPVIEEGYYVSGVNPFLSRTATTLMRRRKAKLIGSPFPIGPDGTRAWVEKICSVFNIEPKGLEEREAKIWQSVEDYLQLIRGKSVFFMGDNLLEISLARFLIRCGMTCHEIGIPYMDKRYQAAELDFLVKTCQEMGVPVPTIVEKPDNYNQLQRIHELKPDLVITGMAHANPLEARGISTKWSVEFTFAQIHGFGNTRDILELVTRPLRRNGALKDLGWEKLVEEARV", "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": "MEYFDMRKMSVNLWRNAAGETREICTFPPAKRDFYWRASIASIAANGEFSLFPGMERIVTLLEGGEMFLESTDRFNHTLKPLQPFAFAADQVVKAKLTAGQMSMDFNIMTRLDVCKAKVRIAERTFTTFGSRGGVVFVINGAWQLGDKLLTTDQGACWFDGRHTLRLLQPQGKLLFSEINWLAGHSPDQVQ", "text": "SIMILARITY: Belongs to the Ves family."}
+{"protein": "MSQTEHHISIEQEMRKSYLEYSLSVIIGRAIPDVRDGLKPVHRRILFAQQELGNSYTRPPKKCARIVGDVIGKYHPHGDSAVYDALVRMAQDFSMRDPLEEGQGNFGSIDGDAPAAMRYTEVRMSRLASEFLSDIDKETVDFRPNYDNSLEEPIVLPTKVPNLLLNGSSGIAVGMATNIPPHNLGELCNALLKIIDDPDVPIDNLLNIIHGPDFPTGGFIYVGQGLYDAYTKGRGTVKVRGKVEIEERKKGAQSIVIREIPFGLNKSSLVEKIAILVNERKIDGIADLRDESDRKGIRVVIELKKGVIPEIIINALYKFTPLETSFGINMLAVVDNRPQLLTIKSALTYFLDHRREVIVRRTRFELNKAEARLHILIGLIHALDHIDEVVNLIRSSSTPAEAKIRLIERFSLSEIQAQSILDMRLQRLTGLEREKLEEEMHELQTKIAWYESILGDTKILWGVIRDEVTGIKEMYTTPRRTEVIRETLTNIEIEDLIPDDDVVITLSRRGYIKRTNLAIYQQQRRGGKGVAGLHTSEDDFVQEFITTTNHQFLLLFTNKGRMHQLKVHQVPEGSRTAKGTHIANIVPLEKEEWVTTILTVREFSDNKFFLFATRKGMVKRSSASYYARSRRTGLLAVGLREDDELIMVKEVTNNDFIVLATAEGFAIRFSCEDVRNMGRGAAGVKGIALRPGDSVVACLILQEKQDTPAIMTVSNLGYGKRTSIDLYRVQTRGGKGIINFKVTQKTGLVIGAKPVSDDNALVLLTSTNKIIRMSVDEVRSAGRATMGVRLVKLDDGAYVVGFDTVDGTVDDSCDDATINT", "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": "MSALNLTVRVHPVVLFQVVDAFERRNAESHRVIGTLLGSVEKGVVEVTNCFCVPHKEHDDQVEAELSYALDMYDLNRKVNSNEAVVGWWATGNDVTNHSSVIHEYYARECNNPVHLTVDTSLQGGRMGLRSYVCIQLGVPGGKTGCMFTPIPVELTSYEPETFGLKLLQKTVGVAPANRPKTVPPMLDLAQISEASTKLQSLLDLILKYVDDVIAHKVTPDNAVGRQLLDLIHSVPHMSHEQFTQMFNANVRNLLMVITLSQLIKTQLQLNEKLTFLPTA", "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": "MSTFAILPVKRFEGAKGRLAGGLAAGPRRALAEAMYVDVLTALRRTQGVDRVLVLTADPGAQRVAEGYDAIPLDDPAEAGQNRAVMRGVAHARELGATRVLCLSGDTPMLDPADLDALLGRPRTADRYVVIVPDRHGEGTNGLLLCPPDGMKPSYGVDSCARHKALAEEAGLAVEIAEIPSVALDVDTPDDLDALRELIASRRGGAAHTRGMLNQLLRTNPKN", "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": "MGYFQGNDFRKITGGKKGKHRDKRKFELGSPPTETKLSTEELIEKERGMGGNIKIRVKYATFANIYDPQEKVSKKAKILSVIETPANKEYARRGIIVKGSIIQTELGKAKVTSRPGQDGTINAILIKE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family."}
+{"protein": "MSLSIDVTSLPSISSSIFKNESSSTTSTLSGKSIGRNELYVSPDAEAFNKYMLSKSPEDIGPSDSASNDPLTSFSIRSHAVKTNADAGVSMDSSTQSRPSSNVGCDQVDFSFNKAVKVNANLDSSISISTDQKREKSKKDHKNGKHYPKIEAESDSDDYVLDDSDSDDGKCKNCKYKRKYFALRMRMKHVAMQLIEDL", "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": "MVEQSKVPSSSLCPPDKIIFDEERGEYICTETGEVIEERIIDQGPEWRAFTPEEKEKRSRVGGPLNQTIHDMGISTVIDWKDKDAMGRSLDPKRRLEVLRWRKWQIRTRIQSSIDRNLAQAMNELERIGNLLNLPKAVKDEAALIYRKAVEKGLVRGRSIESVVAASIYAACRRMKMARTLDEIAQFTKANRKEVARCYRLILRELDIEVPVSDPKDYVTRIGTLLSLSGITMKHAAEIIEKAKNSGLTAGKDPAGLAAAAIYIAALLNDERRTQKEIAQVAGVTEVTVRNRYKELTQELKIQIPSQ", "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": "MKSQSIMSVERSAETSLTLEIPTSPLIIKITQQERNILSNVGNLLVKAFGNYENPDYIASLHLHAFQLLPERITRILSQFGSDFSAEQYGAIVFQGLIEVDQDDLGPTPPNWQGADYGKLNKYGFICSLLHGAVPSKPVQYYAQRKGGGLLHAVIPDEKMAATQTGSGSKTDLFVHTEDAFLSNQADFLSFLYLRNEERVPSTLYSIRSHGKMNPVMKKLFEPIYQCPKDANYNDEDVANSGPTASVLYGNRELPFIRFDAAEQIFNENAGQTSEALGNLMDFWDEAKTLINSDYIPNSGDLIFVNNHLCAHGRSAFIAGQRIENGEIIKCERRQMLRMMSKTSLIHIRSVTRTDDPYFIMEEHLGKIFDLD", "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": "MPLLQVEDLTKTFKGHASLFGRNQFNAVDKVSFTLERKQTLAIIGNNGSGKSTLVKMIAGIIPPTSGRILFNDRELQYQDAQSRAKHIRMVFQDANSAFNPRLNIGQILDEPLSLATDWTETQRNEKIFETLSLVGLYPDYTNLNIKHLSISQKQRVALARALILEPEIIIIDDAIGNLDASVRIQLLNLTLDLQQRLGISYIYVGQDLGVIKHIADTIIVMDEGKMIEYGSPQNLFTDPQTDVTRRLVESYFGKILDETAWVKDKNAH", "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": "MIYDSQIYTVLCIALLAGILAIRLGSTLYE", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaM family."}
+{"protein": "MIGPPVNLPKWLEENSHLLKPPINNYCVYNGDFTVMIVGGPNARTDYHINTTPEWFYQHRGAMTLKIVDPTEGNNTFRDIVIREGDMFLLPANTPHNPVRFADTVGIVLEQKRPAGSLDRMRWYCQREGCGAVVKEAAFHCTDLGTQIKEAVEAFKADEEGRRCKQCGEVAEWCPKPGSIRDPNLE", "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": "MSSEEGKLFVGGLNFNTDEQALEDHFSSFGPISEVVVVKDRETQRSRGFGFITFTNPEHASDAMRAMNGESLDGRQIRVDHAGKSARGSRGGAFGGRGRSYSRGGGDQGYGSGRYDSRPGGYGYGYGRSRDYSGSQGGYDRYSGGNYRDNYDN", "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": "MSDRSPATENPWQQLRRLTPARIALGRAGASLPTAAHLAFQFAHAQARDAVHLPFEPAALQDGLRRRGLDGLLLRSAARDRDTYLQRPDLGRRLRPECATRLRDWHAEHGGGRDLAIVVADGLSALAVQRHALPLLDCLLERLPAEGWSLAPISLVEQGRVAVADEIGELLGARMTVILIGERPGLSSPDSLGLYFTFAPRVGLTDAARNCISNVRPEGLSYAMAAHKLLYLMREACRRRLSGVELKDEAEVARLDGAGSGPGNFLLGEG", "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": "MFDIGVNLTSSQFVKDRDDVVTRALAAGVSGMLLTGTNLHESQQAQKLAQRYACCWSTAGVHPHDSSQWQSETEDAIVALARQPDVVAIGECGLDFNRNFSTPQEQERAFQAQLRIAAELQMPVFMHCRDAHARFLALLEPWLDKLPGAVLHCFTGTREEMQECIDRGLYIGITGWVCDERRGLELRELLPFIPAEKLLIETDAPYLLPRDLTPKPASRRNEPAHLAHILARVAHWRGEDPQWLAATTDANVKTLFGIAF", "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": "MDLPGPIHDFLLVFLGSGLILGGLGVVLRINPIYSAFSLGLVLVCISLFYILTNYHFVATAKLLIYVGAINVLILFVVMFMNSSEYYKDFNPWTIGNGLTSLVCTSILVSLISTILDTSWYGIIWTTRSNQIIEQDLIGNSQQIGIHLATDFFLPFEFISIILLVALIGAIDVTLQ", "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": "MAAGPRTSALLAFALLCLPWTREVGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILKQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF", "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": "MNEAVKTLDGWFCLHDFRSIDWAAWRELNPGNQELMLNELSHFLSDMEITKNIGEGEHTIYSILGQKADLVFFTLRDSLEALNEVENRFNKLAIADYLLPTYSYISVVELSNYLASHMAGGEDPYQNKGVRARLYPALPPKKHICFYPMSKKRDGADNWYMLPMEERQQLIRDHGLIGRSYAGKVQQIIGGSIGFDDYEWGVTLFSDDALEFKRIVTEMRFDEASARYAEFGSFFIGNLLLSEQLSKLFTI", "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": "MSGNESVVNYDHFIDKRRVRKAFERAAPLYDQAAVLQREVCDRMLSRLEYIKYMPDVVLDAGSGTGYGTCKLLERYPDASMLAIDIATGMHHQARQRMNSMIPRWRQLFGVGRNQRTSRVRYVAGDIEQLPLEDSCAGLVWSNLALQWCNDLKKTFDEMRRILKNGGLFMFSTFGPDTLKELRQAFRHADDYSHVNRFADMHDIGDMLVHSGFATPVMDMEYITLTYDEVISVMRDLKAIGAHNATGARHRGLTGKNAWQKAIGHYETLRTGGKLPATFEVVYGHAWKPAPRTSILTPETRRHIGLE", "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": "MKVGFFLLKFPLSSETFVLNQITAFIDMGFEVEILALQKGDTQNTHAAWTKYNLAARTRWLQDEPTGKVAKLRHRASQTLRGIHRKNTWQALNLKRYGAESRNLILSAICGQVATPFRADVFIAHFGPAGVTAAKLRELGVIRGKIATIFHGIDISSREVLNHYTPEYQQLFRRGDLMLPISDLWAGRLQKMGCPREKIAVSRMGVDMTRFSPRPVKAPATPLEIISVARLTEKKGLHVAIEACRQLKEQGVAFRYRILGIGPWERRLRTLIEQYQLEDVVEMPGFKPSHEVKAMLDDADVFLLPSVTGADGDMEGIPVALMEAMAVGIPVVSTLHSGIPELVEADKSGWLVPENDARALAQRLAAFSQLDTDELAPVVKRAREKVEHDFNQQVINRELASLLQAL", "text": "SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
+{"protein": "MAEEHNHNHEEENIIWITNEEGKEEAYEILFDFDSKDFDKSYVLYFPAGKGEDEEIEILASSYIQDEEGKQGQLKPVETDEEWDMIEEILATFLADEDEE", "text": "SIMILARITY: Belongs to the UPF0473 family."}
+{"protein": "MLSLILTIFFVHVAIYLVNTVGATTIDTLLWILYLKLPTSTSRNARQQSRLKREVVQLKREMNNTSSQDEFAKWAKLRRKHDKAMDEYEAMNKKLTAQKTSFDWSVKIARWLSTNGLKIFLQFYYSKTPVFALPAGWFPFYVEWVLSFPRAPRGSVSVQVWNSVCATAIAVMAEIVTSMLLQLRSRSASPASTAKAQKAQ", "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": "MASRAQRTGGRMILHNDLSGLRVVAVHAHPDDEAITTGGALHHLATRGADVTVVTCTLGEQGEVIGETWQQLVNGDADQLGGFRIHELLSSLRILGASGCFLGGAGRWRDSGMVGDPANDHPRSFVRSGDQAEEQLVEIFTMLRPHLVITYGPDGGYGHPDHIRAHEITHGAAGRVEGIQRILWAVTGRTDLQAGLDAISAVPTGWRAAGDDELACQDRVDFALELDDRAYHAKVESMRAHATQLWIADGGVSDTNPHAAFAEVTDRAAAPVVFALSNLIAQPVMRREHYQLGAGTAFPADAQGPADGLQW", "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": "MTISLFAIRDCLEKEDLLKEFISPEGWHLTLSDTLGQREVTALSYDSRDVTAETLFFCKGLNFKEIYLENAVKDGLEIYVSEVPYEVPAQLGIIVTDIKKAMAVLSMAFYDYPQNKLKLIGFTGTKGKTTAAYFTKYILDVATQQKTALLSTMNSTLDGKTFFKSALTTPESLDLYRMMATAVANGMTHFIMEVSSQAYKTNRVYKLFFDVGIFLNITPDHISPIEHPTFDDYFYCKRQLITHSKVIVLNHEADYFPLLKETAQQQKVPAIVYGSQPAPEVDYSFAVSSEDSLRFIVESPADALGLAGSYHLRLGGDFNKGNALSAAIASVLVGASKEECQQGIAATTVPGRMESLTNTNGATVYVDYAHNYDSLKNLLTFVREEHPDGRLIVLVGSTGDKAISRRKDFGRVLSELADVAVLTTDDPASEDPAKICQEIQAHITKEMPVYTVLDRGEAIAHALSLSTTADDAIVLAGKGADLYQKVNGVDEPYAGDFALAEAFINKKN", "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": "MVSQAKQPSNATFKNREKPQEVRKANIIAARAVADAIRTSLGPKGMDKMIKTSRGDIIISNDGHTILKQMAILHPVAKMLVEVSGAQDVEAGDGTTSVVIMTGALLGAAEKLLNKGIHPTIIAESFQRAAERSVEILLNMSTKISLDDKEALVRAASTSLSSKIVSQHSSFLAPLAVDCVLSIASHDSTNVDLNDIRLIKKVGGTIDDTEMVNGVVLTQNAVKTAGGPTRIEKARIGLIQFQISPPKPDTENNIVVNDYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLSKLGIMVVRDIERDEVEFLSKSLGCKPISDVELFTEDRLGSADVVEEVESDGSNIVTITGVKTTNKNPTVSVVIRGANNMVLDETERSLHDALCVIRCLVKERALIAGGGAPEIEVSYRLMKEARTMEGVEAFVWQEYAEALEVIPTTLAENAGLNSLNVVTELRLRHENGESNSGISVRRSGTSNTYEDHILQPVLVSTSAIRLASECVKSILRIDDITFSR", "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": "MTALAAGIAMLAGLGVGIGIGIATGKASESIGRQPEAFGRIFPLFLIGAALAEAVAIYSLVIAFMLISKI", "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": "MSRSRHVGKIRKRLEDVKNQWTRPARADFSDNESARLATDALLDGGPEAYWRALSQEGEVDFLSSAEAQYIQAQAKEPPDAPDSAGGAESGPRGLDSCSLQSGTYFPVASEGSEPALLHTWTLAEKPYLKEKSSATIYFQMDKHNNIRDLVRRCISRASQVLAILMDVFTDVEILCDILEAANKRGVFVCVLLDQGGVKLFQEMCDKVQISDIHLKNISIRSVEGEVYCAKSGRKFAGQIQEKFIISDWRFVLSGSYSFSWLCGHVHRNILSKFTGQAVELFDEEFRRLYASSKPLMGLKSPRLVAPFQPNKGPEAPNGRLSGTSDSASDRTSSNPFSSLSTGSNAHNQSLSTSSGPSSPLAPIPPTVPRLQPYHSTRRAVAPQPLLVPMRPHEGAPAPYSSLMAYRPTRLQLQQLGLVPRVTHPWRPFLQALPHF", "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": "MQFDYIIIGAGSAGNVLATRLTEDPNTSVLLLEAGGPDYRFDFRTQMPAALAFPLQGKRYNWAYETEPEPFMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLDNWAKEPGLENWSYLDCLPYYRKAETRDVGENDYHGGDGPVSVTTSKPGVNPLFEAMIEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPQGRRASTARGYLDQAKSRPNLTIRTHAMTDHIIFDCKRAVGVEWLEGDSTIPTRATANKEVLLCAGAIASPQILQRSGVGNAELLAEFDIPLVHDLPGVGENLQDHLEMYLQYECKEPVSLYPALQWWNQPKIGAEWLFGGTGVGASNHFEAGGFIRSREEFAWPNIQYHFLPVAINYNGSNAVKEHGFQCHVGSMRSPSRGHVRIKSRDPHQHPAILFNYMSHEQDWQEFRDAIRITREIMHQPALDQYRGREISPGTECQTDEQLDEFVRNHAETAFHPCGTCKMGYDEMSVVDGEGRVHGLEGLRVVDASIMPQIITGNLNATTIMIGEKMADMIRGKEALPRSTAGYFVANGMPVRAKKMSRDLN", "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": "MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFIRTILDKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASFNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDNAEAATEEFIKRAEVNGLAAQGKYEGSGEDGGAAAQSLYIANHAY", "text": "SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family."}
+{"protein": "MSDINATRLPIFWFIYFPCVSDVDSTLTRGER", "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": "MGDAEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGIVWDEGTLLEYLENPKKYIPGTKMIFAGIKKKGERQDLIAYLKQSTSS", "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": "MSNFTAEDKAAITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSPSAIMGNPKVKAHGVKVLTSLGEAIKNLDDLKGTFGQLSELHCDKLHVDPENFRLLGNVLVTVLAILHGKEFTPEVQASWQKMVAGVASALASRYH", "text": "FUNCTION: Gamma chains make up the fetal hemoglobin F, in combination with alpha chains. SIMILARITY: Belongs to the globin family."}
+{"protein": "MASAAAAAATARGPRYAPPDPTLPKPWRGLIDGNTGYLYFWNPETKAVQYDRPTAPPPSSPPAQQPPERPRNSDPAESQAQAGASRTQNAAPADDRARNDHLNDHFERRTEAAGSHAQNVPFTEQNTRSNPSSQPCSAAGVYPAQNVFSEAASGDRTSPEAYRAKHEITIVGNEAPAPFMTFQSTGFPPEILREVQQAGFSAPTPIQAQSWPIALRNRDIVAVAKTGSGKTLGYLIPGFILLKRLQHNSRDGPTVLVLSPTRELATQIQDEAKKFGRSSRISSVCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRVSLHQVSYLVLDEADRMLDMGFEPQIRKIVKQVQPKRQTLMFTATWPKEVRKIASDLLSNPVQVNIGNTDQLVANKSITQYVDVITPPEKSRRLDQILRSQEPGSKIIIFCSTKRMCDQLARNLARQYGASAIHGDKSQAERDSVLSEFRSGRCPILVATDVAARGLDIKDIRVVVNYDFPTGVEDYVHRIGRTGRAGATGVAYTFFCDQDSKYASDLVKILEGANQSVSQQLRDMVSRGGYGGRSRRWASSDDSYGGRGYDSGYTSRSTDNYNSGYGSQSGNGSSFHSSFHNSNSGNQFGDTSGFQTSFHNSSSNNQTSDNPSFHASSNNDQPGDGLSFHARFYSSSRGSDQSRTNNAGFRDRSRSPPSNRNHEDPGSKAVGVSNW", "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": "MDLLLLEKTLLGLFAAIIVASIVSKLRGKKFKLPPGPIPVPVFGNWLQVGDDLNHRNLSDYAKKFGEIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRIMTVPFFTNKVVQQYRYGWEEEAARVVEDVKKNPESATNGIVLRRRLQLMMYNNMYRIMFDRRFESEDDPLFVKLKALNGERSRLAQGFEYNYGDFIPILRPFLRGYLRICKEVKERRLQLFKDYFVDERKKFGSTKSMDNNSLKCAIDHILEAQQKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELETVLGPGVQITEPDTYKLPYLQAVIKETLRLRMAIPLFLPHMNLHDAKLGGYDIPAESKILVNAWFLANNPEHWKKPEEFRPERFLEEESKVEANGNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLPPPGKSKIDTSEKGGQFSLHILKHSTIVLKPRTF", "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": "MASVLIREAKEGDCGNILRMIRELAEYEKLSDQVKISEEALRADGFGENPFFHCLVAEILPAPGEPQGSCMVGYGLYYFIYSTWTGRNIYLEDIYVKPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVLDWNKKAVDLYKTLGARDLTEAEGWHSFRFEGEAMRELAGK", "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": "MNLYNIKHPEEQVTFSQAVRQGLGRDQGLFFPEVIPQLNNINELLELPLVERSQKILGALIDGELPQATLDAMVKNAFTFPAPLEKVEENIYALELFHGPTLAFKDFGGRFMAQALAAVRGDGKITILTATSGDTGAAVAHAFYGLENINVVILYPKGKISPLQEKLFCTLGGNIRTVAINADFDACQALVKQAFDDVELRQAIGLNSANSINISRLLAQVCYYFEAVAQLPKEKRDNVVVSVPSGNFGNLTAGLIAKTLGLPIKRFVASTNANDTVPRYLKSGNWDPKTTVATLSNAMDVSRPNNWPRVEELFKRNGWDLTDLGSGMLSDSETEDTLKAMQSKGYLCEPHGAIAYQVLKDQLKASETGIFLCTAHPAKFKESVERILGIQLPLPETLDKHNQLPLLSDEMDNDFAQLRAYLLKS", "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": "MTTAARPTFEPARGGRGKGEGDLSQLSKQYSSRDLPSHTKIKYRQATQDAPEEVRSRDFRRELEERERVVARDKNRDRPTREHTSSVSKKPRLDQIPAANLDADDPLTDEDGDEDSDEDSDDDTAALLAELEKIKKERAEEKDRKELEQKAEEERIRMENILSGNPLLNLTGPAAQSQASFKVKRRWDDDVVFKNCAKGVDEMKKQKRFVNDTLRSEFHKKFMEKYIK", "text": "FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC15 family."}
+{"protein": "MALLELRDVTRRFGDFTAVDCVNLSIEAGELFTLLGPSGCGKTTLLRMIAGFDVPDSGQILLDGQDIANTPPEKRPIHTVFQSYALFPHMTVADNVAFPLKMSGKTPAEIKKRVEKALEEVQLSRFTHRFPHELSGGQKQRVAFARGLINRPRLLLMDEPLGALDAKLREDMQRELISLQKEVGITFVFVTHSQDEALALSQRIAVMNQGQVEQIGEPSVIYSHPANRFIADFIGKINLMAARVTQVSDNDMTLEIDQLGTTTLPLKQGIKTGDQGVMAIRPEQVSVHALARHAELPHAHTGKVLDFLYVGDVTTYIVELDCGIRVEALLANSSPGRARFFEVGDPVIVSWTREAAQFLMN", "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": "MNEAVSPGALSTLFTDARTHNGWRETPVSDETLREIYALMKWGPTSANCSPARIVFIRTAEGKERLRPALSSGNLQKTLTAPVTAIVAWDSEFYERLPQLFPHGDARSWFTSSPQLAEETAFRNSSMQAAYLIVACRALGLDTGPMSGFDRQHVDDAFFAGSTLKSNLLINIGYGDSSKLFARLPRLSFEEACGLL", "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": "MGGCSSAFAVSTRMIRFSRGRVPAAILPVTSNDEPCCSCSPENNNKNNDGGGGGCDGGEHQKGKSWRRWQYRRCGGGGGGGGGRKNAILGDAADVKTAAGFAERYRLGAELGRGEFGVTRRCSDAATGEALACKTIRRKRLRRCRGDAEDVRREVEILRRISALGAGADSVVRLRDACEDSDGVHLVMELCEGGELFDRIFARGHYTERAAAKLARTIVGVVQLCHENGVMHRDLKPENFLFANKSEDSPLKAIDFGLSVFFKPGERFTQVVGSTYYMAPEVLNRSYGPEADVWSAGVILYILLCGVPPFWGDNDEKTVTAILQGGINFQREPWPKVSPHAKDLVSKMLDPDPSTRLTAKEVLEHPWLKNADRAPNVSLGEIVRSRLMQFSAMNKFKKKALGVVAKNLPVEEMDKYTQMFHKMDKDNSGNLTLEDLKLGLQINGHPVPETEIEMLLEAGDIDGNGTLDCEEFVTVLLHIKKMSNEEYLPKAFKFFDKDGNGFIEMEELMDALGDELGPTEQVVKDIIRDIDTDKDGRISYQEFESMMISGSDWRNASRRYSKANFSSLSRKLCKGNS", "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": "MSLDERIITQAILETYFEKFKSSLDLDVAIVGGGPSGMTAARLLAADGFNVALFERKLSLGGGMWGGGMTFNMIVVQEESVHLLTDVGVPVKRYKDNYFTADAVAATTTLASAACLAGAKIFNCMSVEDVMLREENGVKRVTGIVINSSPVEIAGLHVDPVVLGSKYLVEATGHAVEVLQTLVRKNDVRLNTPSGGIEGEQSMWADTAEINTVKNTREIFPGLYVAGMAANASYGSYRMGPIFGGMLLSGEKVAADIAAKLKG", "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": "MAENESNVVVDQGQTKLSDLWTKEDYWAIWLGFVILIAGMWLFLANPSPEFAQKVDKANGVMAAEAARAPFKTLAYYKAQDDKGKLQGMDTPSGKAIGAFLTTPGAWASDPLEAFVLSKEAADERNAAAKAKFESAKVKSDAALAAAQAAEAAAAGAAFADAALNTEAQAKIAEWRAEHAKMKAAEKKTKTKPFNIATSLPMLMVALGLFFAVGMKFMGHDVPKFLVGFIGVFFVAVLALMMGHQSTMKYWGIGAEAWAIIIGMLVANTVGTPSFIKPALQVEYYIKTGLVLLGAEVLFDKIIAIGIPGIFVAWVVTPIVLICTFIFGQKILKMPSKTLNIVISSDMSVCGTSAAIATAAACRAKKEELTLAIGLSLVFTAIMMIAMPAFIKAVGMPQVLGGAWMGGTIDATGAVAAAGAFLGEKALYVAATIKMIQNVLIGVVAFGVAVYWCARVECREGHSVGWIEIWHRFPKFVLGFLAASVLFSVISGSLGSDMSQIMVNQGVLKGLSSPLRNWFFCLAFTSIGLATNFRELAHYFKGGKPLILYVAGQSFNLVLTLAMAYVMFYIVFPEITAKI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0324 family."}
+{"protein": "MKISMIFLPHFLYYTVPTFYLFGLLIMHNAAQHNYVISLTTEQKRRKHITEEFGKQNIPFEFFDAITPDIIEETAKKFNITLDRSPKAKLSDGEIGCALSHIVLWDLALENNLNYINIFEDDIHLGENAKELLEIDYISDDIHVLKLEANGKMFFKQPKSVKCDRNVYPMTVKQSGCAGYTVTAKGAKYLLELVKNKPLDVAVDSLVFEDFLHFKDYKIVQLSPGICVQDFVLHPDNPFESSLQEGRDRVHGNQRKSSILEKIKNEFGRVKIKMFGKQVPFK", "text": "SIMILARITY: Belongs to the glycosyltransferase 25 family."}
+{"protein": "MAMVQPKSQKLRLFITHLGLLIFIAAIMFPLLMVIAISLREGNFATGSLIPDKISWEHWRLALGFSVEHADGRVTPPPFPVLLWLWNSVKIAGITAIGIVALSTTCAYAFARMRFPGKATLLKGMLIFQMFPAVLSLVALYALFDRLGQYIPFIGLNTHGGVIFAYLGGIALHVWTIKGYFETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDVDSYTLAVGMQQYLNPQNYLWGDFAAAAVLSAIPITLVFLLAQRWLVNGLTAGGVKG", "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": "MLTMGWSNILSLFGAMLILAALPSLSVLTVSSKSASGGFIHGLFAALGVVLGDIIFILIALWGLAFLRGAMGDFFVILKYISGIYLSWLGINTIRAKVNNQSLAKVDVKSLSSSFSAGLLITLADQKAVLFYLGFLPTFVDVNNIAYLDIAVIILTAILTVGGVKIFYAFLAHRSGLLISRQNKRIMNYLAGALMISVGVFLLISS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Rht family."}
+{"protein": "SLRKMHALGET", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MNVALIFAGGVGTRMQNSTKPKQFLELYNKPVIIYTLEKFEENKNIDAIVVVCVEPWIDYLRKLLFKFDIQKVKFVIPGGETGQESIFNGLCKIEEEFDHNSVVLIHDGVRPLINDEIINRNIEAVKSHGSAITTCPPVETFVLVDNEDVVKDVHDRSLSRLAKAPQSFYLRDILKVHRQAREDCYTEAIDSCSLMTKYGYDVRLVSGISENIKITSPIDFFIFKAIIDTQENLQVFG", "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": "MYKIIAIDIDGTVYSRKHGVHELTKLALKKAREKGIKIVIATGRTISTTRLIAKKLDLLNTSIPFIGQNGGQVFSYETNGKVKIRYTKKFTNKQVNQIFNIIKQHKAHAFCYTLDENIAYKNKGISIFFWWMKKRSQRNVKVYKPNKKLESQITKYICFGKKENMRQMRKKVEDLGFSAFSFSYVTNAKENIEINPIGVNKGYGLEYVAKELNIKPEEILFFGDGENDLEAIKFAGTGVAMKNSKLEIVKKAADDITSLTADQGGVGEYIFKYVLKEEIPKEFSIKK", "text": "SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family."}
+{"protein": "MAIILGADAHGNALKELIKSFLQEESYDIIDVTDINSDFIDNTLAVAKAVNEAEGRLGIMVDAYGAGPFMVATKLKGMVAAEVSDERSAYMTRGHNNARMITIGAEIVGPELAKNIVKGFVTGPYDGGRHQIRVDMLNKMA", "text": "SIMILARITY: Belongs to the LacAB/RpiB family."}
+{"protein": "MDRKVAVPEDGPPVVSWLPEEGEKLDQEGEDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFTCGIPVFFLEVALGQYTSQGSVTAWRKICPLLQGIGLASVVIESYLNIYYIIILAWALFYLFSSFTSELPWTTCTNTWNTEHCMDFLNHSGARTATSSENFTSPVMEFWERRVLGITSGIHDLGALRWELALCLLLAWLICYFCIWKGVKTTGKVVYFTATFPYLMLVILLIRGITLPGAYQGVIYYLKPDLLRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYRDSIALCFLNSATSFAAGFVVFSILGFMAQEQGLPISEVAESGPGLAFIAFPKAVTMMPLSQLWSCLFFIMLIFLGLDSQFVCVECLVTASMDMFPSQLRKSGRRELLILAIAVFCYLAGLFLVTEGGMYIFQLFDYYASSGICLLFLAMFEVICISWVYGADRFYDNIEDMIGYRPWPLVKISWLFLTPGLCLATFLFSLSQYTPLKYNNIYVYPPWGYSIGWFLALSSMICVPLFVIITLLKTRGSFKKRLRQLTTPDPSLPQPKQHLYLDGGTSQDCGPSPTKEGLIVGEKETHL", "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": "MANIVVKKLERTPIDETPVEIVERKGIGHPDSICDGIAESVSVALCKMYKEKLGVVLHHNTDQVELVGGYAYPKLGGGCMINPIYVLLSGRATAEVLDKETGKIVKLPVNTTAVNAAREYLKKALRNIDLEKDVVVDCRIGQGSVDLVEVFDRKRSEIPHANDTSFGVGHAPLSTTEKIVLETEKLLNSAELKAIVPGVGEDIKVMGLREGKKITLTIAMAVVDKYADSLEEYEKVKEMAHKKVVENAQKYLNGHELEVFINTADDEECIFLTVTGTSAEMGDDGSVGRGNRANGLITPFRPMSMEATSGKNPINHIGKIYNILSNIIASDVAELEEVKECQIRILSQIGKPITEPKILSIEVIPENGFTLDDVTKKATEVAEKWLDNIQNVTEKIVEGKVTTF", "text": "FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. SIMILARITY: Belongs to the AdoMet synthase 2 family."}
+{"protein": "MSSNTGDQFANLGKALSTTASVLFSSQPMEDTILSYSSPYKKLLHETITNAGGGSSLVKVRHDVKLSKGKNTGFQDIYSNSKEFFKNSYSDPKTTFKVLSYLSDDLLEDAPRDTIPQNKNMITENGEKRSAKSKKQEPTLFQGFEASLPVINETIELQQKLIMNSDMKPLTDSESIPVYAEEEEQEEEFSLPDHLKADKLLHSYSASFLKDASRSITDNLDLLEIQKNLAASEIRELDIKLEKLKMMRELVFKRVAKIEQHELFLEKHLNNVKDRIDMIIEYNMDKEYSSEDEENINGLSELSPKTGETNETYETAATTPLENKEEEHSPLLSKSIYQQLQDHEKKSDISERKKHSTSKKIKDVGVSHRNRRRKTYPTLQQFYDSGSKITSLPKAHDEDITCLDFDMPFGTMCSAGSLDHSVKVWDLSKKKQIATLHGHLASISCMQIDQYSTLITGGRDAVLKLWDIDKAMADEASNSSEDNDACLYTFDSHVDEITAISFDGDNLVSGSQDRTVRQWDLNSGKCTQTIDISFATGPMRSQRNIPLRNSVLLTKEPPAIGALQCFDAALATGTKDGIVRLWDLRSGKVVRMLEGHTDAITSLQFDSVNLVTGAMDRSIRIWDLRTGILSDVFAYEQPITSLHFDLDKIVISNNEPTVKIYNRKDGNHWFCGEDDPEQGNVDFVRYKHGYLVEGRSNGDINTWAI", "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": "GETISIYYDPGKFPALMPLKNGNYEERNGGVPQRGNITIHLQQFNEDLDKMTPDKNFGGIGVIDFERWKPIFRQNWGNTEIHKKYSIELVRYEHPKWSESMIEAEATKKFEKYARLFMEETLKLAKKTRKRAKWGYYGFPYCYNYTPNNPGPDCDAKAMIENDRLSWMYNNQEILFPSVYVRHELTPDQRVYLVQGRIKEAVRISNNLKHSPKVLSYWWYVYQDKMDIFLSETDVKKTFQEIVTNGGDGIIIWGSSSDVNSLSKCKRLREYLLNTLGPFAVNVTETVN", "text": "FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 56 family."}
+{"protein": "AYRKPPFNGSIF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
+{"protein": "MDRGTRRIWVSQNQGDTDLDYHKILTAGLTVQQGIVRQKIISVYLVDNLEAMCQLVIQAFEAGIDFQENADSFLLMLCLHHAYQGDYKLFLESNAVQYLEGHGFKFELRKKDGVNRLEELLPAATSGKNIRRTLAALPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKYLLIHQGMHMVAGHDANDAVIANSVAQARFSGLLIVKTVLDHILQKTDQGVRLHPLARTAKVRNEVNAFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLYPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDSLGLDDQERRILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITLASRPNLGSRQDDDNEIPFPGPISNNPDQDHLEDDPRDSRDTIIPNSAIDPEDGDFENYNGYHDDEVGTAGDLVLFDLDDHEDDNKAFELQDSSPQSQREIERERLIHPPPGNNKDDNRASDNNQQSADSEEQEGQYNRHRGPERTTANRRLSPVHEEDTPIDQGDDDPSSPPPLESDDDDASSSQQDPDYTAVAPPAPVYRSAEAHEPPHKSSNEPAETSQLNEDPDIGQSKSMQKLGETYHHLLRTQGPFEAINYYHMMKDEPVIFSTDDGKEYTYPDSLEEAYPPWLTEKERLDNENRYIYINNQQFFWPVMSPRDKFLAILQHHQ", "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": "MMKVLVVVALLVTHISYSSSEGIDDLEADELLSLMANEQTRKECIPKHHECTSNKHGCCRGNFFKYKCQCTTVVTQDGEQTERCFCGTPPHHKAAELVVGFGKKIFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 04 (U1-Lctx) subfamily."}
+{"protein": "MGENMEREMLRPKTIAMDQNSASARSNPEREIKTGRLEPASNSAPTMAIDLQAVTMIYRDKTVVDSLSFGVRAGECFGLLGPNGAGKSTITRMLLGMATPSAGKISVLGLPVPGKARLARASIGVVSQFDNLDMEFTVRENLLVFGRYFQMSTRAIEKLIPSLLEFAQLEAKADVRVSDLSGGMKRRLTLARALVNDPQLLILDEPTTGLDPPARHQIWERLRSLLIRGKTILLTTHMMDEAERMCDRLCVLEGGRMIAEGPPLSLIEDIIGCPVIEVYGGNPDELSLIVRPHVDRIETSGETLFCYTVNSDQVRAKLREFPSLRLLERPANLEDVFLRLTGREMEK", "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": "MKTTVILLLAIAIIFAIMTTLTSAKNEETMEEALKGLNELKERLKKQGIDTAALNLDEKLLT", "text": "FUNCTION: May have antimicrobial properties, like most ant linear peptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily."}
+{"protein": "MSISRRSYEQFDEMKSENQENNSKKKSSERLKKLDPDKFVEAYGAYGKYQIFTYVLVQTLNFFYSSSMYIMSFVQLNLEKQCEYKNETIPISETCQIETESSKAFGNLNGEYCGIAENTLVNVTNQKASTNLLVDFDLSCSHWFFQEFGLTIFTIGAVIAVPFMSMLADRYGRKPIIVTTAILAFLANMAASFSPNFAIFLILRAFIGACSDSYLSVASVATCEYLSEKARAWITVVYNVAWSLGMVWTLLVTLMTDDWRWRYFIVSLPGVYGFALWYFLPESPHWLITKNKTEKLKKYIKTANRVNNVSPEFNDCQQSSHHEEKHESFKALLGSKKLIWLLFANGFIEMVISLVYFAISFMSVELGGDQVQAFLYSSLIEIPAGLAVIPLMMKMGRKMIVIWCLVFQTLALIGVTVFLDSYEFKLVIMLVAKVMATIIYSVHPIWATEQFPTSVRSLCFSLMNIPQSMGIIMSPYVKHIVMSPNWIPFVVIALFSFISATLAFMLHETKNKKLPTDIESLSYPSETNDLSAYRRSKSSSSSVSALSKTSVRSKKTLSSESVSKKLDTVNFSDKEYRI", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
+{"protein": "MKRTINEVVGSTSVNTLDSSIAKKPVFLTKKQREELALKRRQDQISEQRVRREQLGRPEPETEDVSNGDTNRDKDRDRDRDRDRERDRDRERDRGRDRDRDRDRDRDRDRERERDRERDRRERDREPDRRNREKEREEEVKAREKARVEKLVEREKEKELDAIKEQYLGGKKPKKRVIRPSEKFRFSFDWENTEDTSRDMNVLYQNPHEAQLLFGRGFRAGMDRREQKKQAAKHEKEMRDEIRKKDGIVEKPEEAAAQRVREEAADTYDSFDMRVDRHWSDKRLEEMTERDWRIFREDFNISYKGSRIPRPMRSWEESKLTSELLKAVERAGYKKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLAYISRLPPMSEENETEGPYAVVMAPTRELAQQIEEETVKFAHYLGFRVTSIVGGQSIEEQGLKITQGCEIVIATPGRLIDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQVAGVLDAMPSSNLKPENEEEELDEKKIYRTTYMFSATMPPGVERLARKYLRNPVVVTIGTAGKTTDLISQHVIMMKESEKFFRLQKLLDELGEKTAIVFVNTKKNCDSIAKNLDKAGYRVTTLHGGKSQEQREISLEGFRAKRYNVLVATDVVGRGIDIPDVAHVINYDMPKHIEMYTHRIGRTGRAGKSGVATSFLTLHDTEVFYDLKQMLVQSNSAVPPELARHEASRFKPGTVPDRPPRHSDTVYIN", "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": "MTKRAPKSGPLSPSCSGGSSRNLELAVKSSEGARRSTRLRLQPLRKPKTSPKKKPVKLQTKMPKKPATAFFFFLDDFRKQYQEENPDVKSMREIGKTCGEKWKTMTYEEKVKYYDIATEKREEFHRAMTEYTKRMESGAHDESETDSDYSE", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HMGB family."}
+{"protein": "MTQQTAQQEQQKSEVKIYSREELKQKTLAELQKIGKELGLTRTTGLKKEELIEKILKAQLEKSRLVFVKGVLEILPEGYGFLRMPENNYMPSWNDVYVAPSQIKKFGLRTGDTIEGFARLPRENEKYKALIRMESVNGLPPDPEILKRRPQFEKLTPLHPMERFKLEYDPNELSTRVVSLIAPIGKGQRGLIVAPPKAGKTVLLQKIAQAIIRNHPEVYLIILLIDERPEEVTEMRRIVKDKAEVVASTFDEPPERHMQVAEIVVEKAKRMVELKKDVVILMDSLTRFTRASNAVTPPTGRVLTGGIEITAFQRPKKFFGAARNIEEGGSLTIIATALVETGSKMDDVIYEEFKGTGNMEIHLDRRLMERRIFPAINIEKSGTRKEELLLEPWELQRIWVLRKFLSTMDPVEAMEFLLEKLRRFKTNEEFLKAMNA", "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": "MENLTTAQFLHRATLLKKPPPPPWNLNSSFLTSTSYSIPRPSSLRRSLPLSINGDATQPTSLLHHHRFLSSLTRRLSLSGSCPLRLLQEDGDWSKDHFWAVIRFLRQSSRLHEILPVFDTWKNLEPSRISENNYERIIRFLCEEKSMSEAIRAFRSMIDDHELSPSLEIYNSIIHSYADDGKFEEAMFYLNHMKENGLLPITETYDGLIEAYGKWKMYDEIVLCLKRMESDGCVRDHVTYNLLIREFSRGGLLKRMEQMYQSLMSRKMTLEPSTLLSMLEAYAEFGLIEKMEETCNKIIRFGISLDEGLVRKLANVYIENLMFSRLDDLGRGISASRTRRTELAWCLRLLCHARLVSRKGLDYVVKEMEEARVPWNTTFANIALLAYSKMGDFTSIELLLSELRIKHVKLDLVTVGIVFDLSEARFDGTGVFMTWKKIGFLDKPVEMKTDPLVHAAFGKGQFLRSCEEVKNQSLGTRDGESKSWTYQYLMELVVKNQKTVP", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. P subfamily."}
+{"protein": "MTTKSKHIILSLTFLLLFLSTVFSSHVTQRFTSSDDITELVVTALNQTISNVNLSSSNFSDLLQRLGSNLSHRDLCAFDDCLELLDDTVFDLTTAISKLRSHSPELHNVKMLLSAAMTNTRTCLDGFASSDNDENLNNNDNKTYGVAESLKESLFNISSHVSDSLAMLENIPGHIPGKVKEDVGFPMWVSGSDRNLLQDPVDETKVNLVVAQNGTGNYTTIGEAISAAPNSSETRFVIYIKCGEYFENIEIPREKTMIMFIGDGIGRTVIKANRSYADGWTAFHSATVGVRGSGFIAKDLSFVNYAGPEKHQAVALRSSSDLSAYYRCSFESYQDTIYVHSHKQFYRECDIYGTVDFIFGDASVVFQNCSLYARRPNPNQKIIYTAQGRENSREPTGISIISSRILAAPDLIPVQANFKAYLGRPWQLYSRTVIMKSFIDDLVDPAGWLKWKDDFALETLYYGEYMNEGPGSNMTNRVQWPGFKRIETVEEASQFSVGPFIDGNKWLNSTRIPFTLDL", "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": "MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALATLPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISQEGSDLSVVERAEIWLFLKVPKANRTRSKVTIRLFQQQKHLQGSLDAGEEAEEVGLKGEKSEMLISEKVVDARKSTWHIFPVSSCIQRLLDQGKSSLDIRIACEQCQETGASLVLLGKKKRKEEEGEGKKRDGEGGAGGDEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFYVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS", "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": "MAGLASGATTACRATPMSAATTGLPLRVRGIAKRYGDSDVLRGIDLEIAPSACVAIVGRSGCGKSTLLRVIAGLETADVGTVDSGRAPLAAQRDAVRLMFQDARLLPWKRVIDNVALGLGRAGRAQAQQALDAVGLGTRGNAWPSALSGGQRQRVALARALVHRPRLLLLDEPLGALDALTRIEMQQLIVQLWRQHGFTLVLVTHDVAEASALADRIVVLEHGKVGLDVAVPVPHPRAPGLPALASIQAQVLSRLLGTTQVPEPAAPKAQTRHGPPRGATAQDTSPLQRIL", "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": "MLAARLIILLSFYWLSASAIDPADPLFVDLPHGKIRGRDNGFYYSYESLPYAEPPVGELRFEAPQPYKQQWTDTFDATQPPVTCMQWNQFIFGDNKLAGVEDCLTVSIYKPKNTSQSSFPVVAHMHGGAFMFGEARQNGHENMMREGKLILVKISYRLGPLGFASTGDAGLSGNFGLKDQRLALLWIKQNIASFGGEPENIIVVGHSAGGASVHLQMLREDFAQVAKAGISFGGNAMDPWVIHQSARGRTFELGRIVGCGQASDSTELKNCLKSKPAGEIVSAVHSFLVFAYVPFAPFGPVVESPDAPEAFISQHPVDIIKSGKFAQVPWAVTYNTEDGGYNAAVLLEKQASSGRELIFDLNDHWFDWAPYLLFYRDSMTTIKDMDDYSRKLRQEYLGDRRFSVESYWDLQRLFTDILYKNATELALDLYRKHGKSPVYAFVYDNPANTGIGQFFSKRTDVHFGTVHGDEYFLIFENLARGPEMRSDEEIISRNFLNMINDFVVSGNGTMTFGNCVLQDNVGSNKFQLLSITKNGCENLQLESFP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
+{"protein": "MRTHFMKNQSVKRNQHVSTPAIPASICADGLISELVHNEDHPGMTQLLLLPLLQQLGTQSRWQLWLTSQQKLSRDWLLRSGLPLDKVMQSPYCGTITTVEAMIKALQTGNYSVVLGWLADEISETERKRLQQAAKSGQALGLIMRSECNVLPSARPLHGLRIQSSLYH", "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": "MTNFDSKKLNKHWTIEDSISTYGIDKWGDQYFSINSLGNISITPNRNSKKTIDLFKLVNEIKSREINTPLILRFNDILKDRITELNNAFSQAIETYNYKNIFQGVFPIKCNQQKNVLEKIIEYGDYWDFGLEVGSKSELLIGLSLLENKKSLLICNGYKDKKYIEIAILARKLGKQPIIVIEQIDEVQRIIEAVKNLRSTPILGIRSKLSSKSSGRWGKSVGDNSKFGLSIPEIMLTIKELKEASLINEMKLLHFHIGSQISDISVIKDALQEASQIFVELSKLGAPMKYIDVGGGLGIDFDGTKTSSNTSTNYSLQNYANDVVATIKDSCEVNNIQHPIIISESGRAIVSHCSVLIFDVLGTSHVSSQIKVSHQKKTSLIIKNLIDTHNQLKNLRNKKEDLSEIIELWNDAKKFKKDCLVAFRLGFISLGERAYAEELTWACAKEISSHLDNEKIIHPDLSEITETLSSTYYANLSVFKSIPDTWAINQIFPIIPIHRHLEEPICKGNFADLTCDSDGKLNNFIDNGKIKSLLNLHRPEENNDYLIGIFMAGAYQEALGNFHNLFGNTNVIHIDINEDNTYKIKNIIKENSKSEILELLDYSSDNLVESIRINTEFAINNKTLSIEEARKLIDQIETSLRKSSYLSE", "text": "FUNCTION: Catalyzes the biosynthesis of agmatine from arginine. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily."}
+{"protein": "MTKTKGKVVGINGNMISVSFEGLVTLNEVGYVEVGSKKLKSEVIRIRGEVAQLQVFEITKGIKVGDIVEFTGDLLSVELGPGLLGQVYDGLQNPLPELAEQAGYFLERGIYLNALSRTAKWHFTPSAKEGDTLKRADLLGTVPEGSFTHRIMIPFNMYGTYKLKSIKPEGDYTVDDTIAEVTDERGNVIPLTMSFKWPVKRAIDCYAERLKPTETLVTKMRTMDTFFPVAKGGTYCIPGPFGAGKTVLQHATSRNADVDIVIIAACGERAGEVVETLTEFPELKDPKTGRTLMERTIIICNTSSMPVAAREASVYTGVTLAEYYRQMGLDVLLLADSTSRWAQALREMSGRLEEIPGEEAFPAYLESYIAAFYERAGIVRLSDGSKGSVTIGGTVSPAGGNFEEPVTQATLKVVGAFHGLSRERSDARKYPAIHPLDSWSKYPSVLPLEQVKYGRSFLRRGTEVEQMMKVVGEEGTSIEDFIIYLKGDLLDAVYLQQNSFDKVDDAVSVERQQHIYNILIEILGTSFKFVSKDEARSYFSKLKLMFIDYNYSPWGSDAFKSHEDGIKKHIAEKADSLDERAKKLLKQAV", "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": "MAAAAASLRGVVLGPRGAGLPGARARGLLCSARPGQLPLRTPQAVALSSKSGLSRGRKVMLSALGMLAAGGAGLAMALHSAVSASDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPEHDHRKRMGLKMLMMMALLVPLVYTIKRHKWSVLKSRKLAYRPPK", "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": "MKSFNIDHFIASVLQWILNIALIILSIVLSIFLINETITFIQYIFSAKKYTSYKLVESIIVYFLYFEFIALIIKYFKSNYHFPLRYFIYIGITALIRLIIVSHEEPMETLLYAGAILVLVIALYISNMRDLRKE", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsiE family."}
+{"protein": "MVAEVCSMPAASAVKKPFDLRSKMGKWCHHRFPCCRGSGTSNVGTSGDHDDSFMKTLRSKMGKWCCHCFPCCRGSGKSNVGTWGDYDDSAFMEPRYHVRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQEVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKISSENSNPEQDLKLTSEEESQRLKVSENSQPEKMSQEPEINKDCDREVEEEIKKHGSNPVGLPENLTNGASAGNGDDGLIPQRKSRKPENQQFPDTENEEYHSDEQNDTQKQLSEEQNTGISQDEILTNKQKQIEVAEKEMNSELSLSHKKEEDLLRENSMLREEIAKLRLELDETKHQNQLRENKILEEIESVKEKLLKTIQLNEEALTKTSI", "text": "SIMILARITY: Belongs to the POTE family."}
+{"protein": "MARTKQTACKSTGRKAPRKQLATKAAHKSAPAMGGVKKPHCYRPGTVALHEIHRYQKSTELLICKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVSIMPKDIQLTRRIRGERA", "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": "MNNNKGGFLRSSVFYIFIFLAVVGMVYGLFGNDKTTTKTITSSEFIKALNDKELKSVTVQPGNSIYNVTGTYKKAQTATKDKGLSLFQPTQKVTKFTSTLLPNDASLKSVTDAATKTKTELVTKQAENSGFWLNLLVSLVPVLLIVAVFYLMMNQAGGGKGGQGGMMSFGKSKAKPSDPKDNKVRFADVAGAEEEKQELVEVVEFLKAPKKFVNLGARIPKGVLLEGPPGTGKTLLAKAVAGEASVPFFSMSGSDFVEMFVGVGASRVRDLFENAKKSAPAIIFIDEIDAVGRRRGTGMGGGNDEREQTLNQILIEMDGFEGSEGVIILASTNRSDVLDPALLRSGRFDRKILVGAPDVKGREAILNVHAKNKPLADNVDLKAIAQQTPGYVGADLENLLNEAALLAARRNKSKVDAADIDEAEDRIFQGPAKTNHNMSESERRTTAYHEAGHALVGLVRSEASVVRKVTIVPRGRIGGYALMTPKNDRYNLKYSEAKEQLAGLMGGRASEIFMFNEASSGASNDFQQATGLARQMVTAFGMSDKLGMVQLEGNASVGYADQAGNRAYSEETARLIDEEVRRLAREAFDDAIAILRDNKDKLTAIAEALLEVETLDEKQIKDIYLTGTFTRKDIQDDTELAKAKSFEEAKAAADAKDSQAEQRFEKQDEEKSSDDHSESKNEDTDSTDKSETDDNNTENK", "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": "MTRLDSVERAVADIAAGKAVIVIDDEDRENEGDLIFAAEKATPEMVAFMVRYTSGYLCVPLDGAICDRLGLLPMYAVNQDKHGTAYTVTVDARNGVGTGISASDRATTMRLLADPTSIAEDFTRPGHVVPLRAKDGGVLRRPGHTEAAVDLARMAGLQPAGAICEIVSQKDEGSMAQTDELRVFADEHDLAMITIADLIEWRRKHEKHIERIAEARIPTRHGEFRAIGYTSIYEEVEHVALVRGEIAGPNSDGDDVLVRVHSECLTGDVFGSRRCDCGPQLDAAMAMVAREGRGIVLYMRGHEGRGIGLMHKLQAYQLQDAGEDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPAKRVGLDGYGLHIIERVPLPVRANAENIRYLMTKRDKMGHDLAGLDDFHESVHLPGEFGGAL", "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": "MMCGAPSATQPATAETQAIADKVKSQLEEKENKKFPVFKALEFKSQLVAGKNYFIKVQVDEDDFVHIRVFESLPHENKPVALTSYQTNKGRHDELTYF", "text": "FUNCTION: This is an intracellular thiol proteinase inhibitor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cystatin family."}
+{"protein": "MSGIDFKQKISFQRPFSKPSSAEDEYEITRVFESDRGRIVNSAAIRRLQQKTQVFPLERNAAVRSRLTHSLEVQQVGRYIAKEILNRFKQDKKITAYGLDKLLDPFESIVEMACLMHDIGNPPFGHFGESAINDWFTKRMDPNGGSGSEPQSRDQCQVEVLKLREGETELNILRSKIRHDLSQFEGNAQAIRLVHSLLKLNLTYAQVGCILKYTKPAYWSAPIPASHNYLMKKPGFYLAEENYVKELRRELNMEEFDRFPLTYIMEAADDISYCIADLEDAVEKNIFSVEQLYDHMSQEWGAVTPGDLFDKVVGAAFRQLGREQGRRSSEDQFFMYLRVNTVGKLVPHAAQRFIENLPAVFSGSFNQALLEDSSAACKLLQIFKRVAVKHVFNHPEVEQLELQGYRVISGLLDIYSPLLAMPETAFTQLVADDRHRKYPIETRLFHKLSIKHRLAYAESAERIRNLPSEQYEIYEYYYRARLIQDYISGMTDLYAYDEYRRLMAAE", "text": "FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs. SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily."}
+{"protein": "MASFDAAERRNLDRHICMRCNARNSPDADRCRKCGYTNLRPKAKERRAA", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL40 family."}
+{"protein": "MSPSCSSCVNVLLIMCLMLLSLSADAYKNYTVGESTGWFDIQERPSANYQKWADSKSFSLGDFLIFNTDSNHSVVQTYDFKTYKDCDYDNNENNDTTEWSAANPSATSPVPVSISVPLVKEGSNYFFSGNYDGEQCKFGQHFMINVTHGQGLPDSSSPDDAAAPGPSESSQSGDDEVAPDTIVPANFDHPKDIESADDDKEVHSKKSSSSTTKTSLFCFVFMGLFASF", "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": "MAGVMKLACLVLACMIVAGPITANRALTCGTVNSNVAPCIGYITQGGTLPGACCTGVSKLNSMARTTPDRQQACRCLETAARALGPNLNAGRAAGIPKACGVSVPFPISTNTNCNNVK", "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": "MAEENIIFVGKKPTMNYVLAVVTQFNNNANKIIIKARGKTISKAVDVAEITRHKFIPDAKYEEIRLDTETLQGERGSSNVSSIEITLSR", "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": "MICSQYGPVVVGWDGSKTFVNPSRCSKRVGLAEFLELINIDEIDKRLLYLLGIPRGYVTTYKLYAEVLGTSPRHVGWLMARNPLPVILPCHRVVKSDFSLGGYTGGVEVKKKLLAYEGALCGDRPCRVVRPRMIDDVRDALFKSLGLA", "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": "MTGPATRKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNAPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFRERELIYDLFEAATGMRMMHNFFRIGGIAADLPHGWIDKCLDFCDYFLTGIAEYQKLITRNPIFLERVEGVGIIGGEEAINWGLSGPMLRASGIQWDLRKVDHYECYDEFDWEVQWQNEGDSLARYLVRISEMTESIKIIQQALEGIPGGPYENLEIRRFDRVKDTVWNEFDYRFISKKPSPTFELSKQELYARVEAPKGELGIFLIGDKGVFPWRYKIRPPGFINLQILPQLVKRMKLADIMTILGSIDIIMGEVDR", "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": "MDSDFHVKPEIRILGIDDSALLNEKVMIVGTVFRGGDWIDGVLRSEITRDGLDATEVMVTMIKNSRHHNQLRVIMLDGITYGGFNVVDIEELYRETGLPVIVIMRSCPDFEKIRSALKHFSDGEERWKIIKKAGKIEKLITGRNGTPIYIQKAGIGAKNVEKIIRLTSIRSSIPEPLRVAHLIATGITLGESRGKA", "text": "SIMILARITY: Belongs to the UPF0215 family."}
+{"protein": "MQVIVALAALGSLAAPALGFSIPRGVPVSQSMIDVKLSSTGNSMVKATITNNGNRALNLLKFHTIMDSNPTRKVSIESEDGKEIQFTGMMPTYKEKDLKPSYFISLPPKGTVEHSFDIARTHDLSRGGKFTLKAEGMVPIAEENGTEITGAAKYHSNELHMTIDGEKAASVENAFGIVKRGPLTRINKRTSIDMQSCGNSQELQALTAALKASAQLSSMSAQAVSQNQDKYMEYFKDPQYMQTVQSRFQAVAQESSSTTGGGTTYHCSDTMGGCEEGVLAYTLPSQNEVFNCPIYYSDLPPLSNECHAQDQATTTLHELTHNPAVQEPFCEDNGYGYERATALSAEKAVQNADSYALFANGKLNLITLMLIIDPD", "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": "MVDITAAELKAAEAIFGDRLELAERYVEHLATSGTERGLIGPREVPRLWSRHVLNCAVIEREIARGSHVADVGSGAGLPGLCLAIARPDLELTLIEPLERRVIWLQEVVDDLGLTNVTVMRTRAELAVGMVNADVVTARAVSALSNLAGLTIPLLGGKGEVVAIKGRSAGEEIEKAAKAIRKLGGVQTSVVVVGEDLLEEPTTVVRIIVNKSQKIA", "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": "MTSGTRTPTWKERENNKRRERRRRAIAAKIFAGLRIHGNFKLPKHCDNNEVLKALCNEAGWTVEDDGTTYRKGCKPMDRMDLMNGSTSASPCSSYQHSPRASYNPSPSSSSFPSPTNPFGDANSLIPWLKNLSSNSPSKLPFFHGNSISAPVTPPLARSPTRDQVTIPDSGWLSGMQTPQSGPSSPTFSLVSRNPFFDKEAFKMGDCNSPMWTPGQSGNCSPAIPAGVDQNSDVPMADGMTAEFAFGCNAMAANGMVKPWEGERIHGECVSDDLELTLGNSRTR", "text": "SIMILARITY: Belongs to the BZR/LAT61 family."}
+{"protein": "MKIKNFIYFLIYFIFLFKVINGQNKTCKISVLLSGDKSDLGYNYMMNEARVLAESQLHMYPFSIYYEHLEESTLEAEHAIQDSVDKGANLIVVSSVIHFSLGVKYATKYKDEPIYWIIRGSKLVPTLPKVVILNFNSFELHYLLGYYAGLATKTGVVGFVSPGIGINTLSCDNSFYIGAKYARSNITFLDIHTGSWYNPEVSYKAAQKLIENGADVIGMSQDDMSVQKAIMDSGGLGLGVTGYPGHYQFGSDVAYSYLTNWTNLFITYANHVINDDWPAFDSFFTNLSRKDAIFMDDFSFRVPIDIQTKTKIELENLMNTSYAPYKSDPILESIGLQFSGNWINDTQFRANTKILPSYGDSTVDYPESLKIGVTVVSGFCIFLCLISMIIVIKFKEAKVIKSSSPIFCLLILFGCIVIFVGCIMFARSPTDGSCRSRVWLLSLGYTIFLGNLMVKNWRIWLLFDNPKLKKRAITNWKLYPWVSGIVIIDIVILSIWQALGDIVAESRTGIDSLTKYEYRNVCASSDQGSIALYLLLVFHGLILLVACFISFKIKVVDIEEFNESKPITTSVYIITFCLFIVIPIMVSSPTVTTQTTIICICALITTMLSIILLFGTKFFKMITVGLELGQTFVTSTKSSSHSQRTKSSKSSNGSGPKINGFGGNVLNLDDDSDEISSEKEKKKPIESNPKDHMAVFTSDEETSKASKFSSEQFSREQINDNIILENNNDNEEKQKDEEEIKEEKLLVSEIQAKRLSLEQNGQTEIDSNDV", "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": "MYKIQLLSCIALTLALVANGAPTSSSTGNTMKEVKSLLLDLQLLLEKVKNPENLKLSRMHTFDFYVPKVNATELKHLKCLLEELKLLEEVLNLAPSKNLNPREIKDSMDNIKRIVLELQGSETRFTCEYDDATVNAVEFLNKWITFCQSIYSTMT", "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": "MKERIHEYCHRLHLPVMAERWSAMAEYASTHNISYSEFLFRLLEAEIVEKQARSIQTLIKLSKLPYRKTIDTFDFTAQPSVDERRIRELLTLSFIDRKENILFLGPPGIGKTHLAISIGMEAIARGYKTYFITAHDLVNQLRRADQEGKLEKKLRVFVKPTVLIIDEMGYLKLDPNSAHYLFQVIARRYEHAPIILTSNKSFGEWGEIVGDSVLATAMLDRLLHHSIIFNLKGESYRLREKRLQEEKQKDQ", "text": "SIMILARITY: Belongs to the IS21/IS1162 putative ATP-binding protein family."}
+{"protein": "MTVVPVKLNELKNKLVIIDQTLLPNEEKFLELDNPEEIWEAIKKLRVRGAPAIGIAAAFGLYVSTLKSKAANVAQFKKEFEEVRDYFATSRPTAVNLFWALKRMTRRFEQEEDKTVDKIKQALLDESEKIFAEDQEMSKAIGKHGLSLLKPGMGLLTHCNAGGLASSGYGTALAPIYLGHEKGYNFKVYADETRPLLQGARLTTYELYKAGIDVTLICDDMASLVMKEGKIDAVLVGCDRVAANGDTANKIGTSGLAVLAKEYGIPMYILGPTSTIDLDASTGEDIKIELRDEEEVVNGFGRRTALKGVKAYNPAFDVTDAKYITAIITEKGIVMQPYKESLKKLFE", "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": "MSVIKSIKAREILNSRGNPTVEVDLYTEKDGVVSSFRAAVPSGASTGIYEAVELRDGDKSRYLGKGVLKAIKNILEVIQPAVIGKSVSDQAAIDKLMIDLDGTPNKGKLGANAILAVSLAVCRAGAADRNLPLYKYISEIAGTKMRLPVPAFNVINGGSHAGNKLAMQEFMILPVGAKDFNEAYRMGSEVYHNLKNVISGRYGQDAINVGDEGGFAPPIQSNKEGLELLKLAIEKAGYTGLVKIGMDCAASEFKVENGYDLDFKTKNNDGSAVISGEKLGDLYREFIKEYPIISIEDPFDQDDWESYTKLTASVDIQIVGDDLLVTNPERIKTGIEKKACNALLLKVNQIGSVTESIRAALDSKNASWGVMVSHRSGETEDTFIADLVVGLGTGQIKTGAPCRSERLAKYNQLVRINEELGENHNYAGLTFRKF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the enolase family."}
+{"protein": "MDDRTREYLKGRFGDYYRRASPALPPDANLREWGHIPWTPGSGTTMLRHQSLYDLGDVDTFFADNAPRHAYFSAARYDDPGASTMSQKGWRSADLVFDLDADHLPGVDPDATSYPEMLAECKQALLRLLDFLEDDFSFDDLTVVFSGGRGYHVHVRDESVRELDSEARREVVDYVRAIDLDTEGLIRTVSERGTTKRVLRTEGGWGARVHEALIEYADDLREMDAEDARERLMELDGIGEGRAETILGAFDRNPTAVREGNVEAGGPGVRRLVSALAARVTATDTAPIDEPVTTDTRRLIRLPRTLHGGSGLVVTPIDRDDLDAFDPLRDAVPDRFVGREIRIETDVDRTVELNGERVRVEPGRNTVPEFAGVFLMARGEARKAPER", "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": "MSEEISFVKEIDTGVEGLPKPEVKIENIVATVILENQLDLNLIETKIQDVDYNPDQFPGLVYRLESPRVTVLIFKSGKMVITGAKSINQLIHVVKKLLKAFADQGIPISGKPQIQIQNIVASANLKVYIDLEKAALEFENSLYEPEQFPGLIYRMDEPRVVMLIFSSGKMVITGAKMENEVYDAVKKVARKLKEADAIIGIAE", "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": "MTDSIPKKPFKKGSLVFVDRENYIKSIEALASDDDLPNYVFEGPGEILSVKDEYAQVRWRRPVPDVWLKLDQLKEYTQ", "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": "MDSGIYETPINYKKSNVSAVSVNNTIFVTGGLFINNSNSTIVVNNMEKLDIYKDKQWSIIEMPMARVYHGIDSTFGMLYFAGGLSVTEQYGNLEKNNEISCYNPRTNKWFDISYTIYKISISSLCKLNNVFYVFSKDIGYVEKYDGAWKLVHDRLPAIKALSTSPY", "text": "SIMILARITY: Belongs to the poxviruses Kelch family."}
+{"protein": "MSILIKNGYVIYGDSLKIIKADIYIENNKISKIGKDLTKSADHVIDAKGRVISPGFINAHTHSPMVLLRGLADDISLMEWLQNYVWPVEKKLKRVHIYWGALLGTLEMIKTGTTTFVDMYFHMEEVAKAVEEIGLRAYLSYGMVDLGDEEKRSIEIRETLKLLKFIESLSSPRVEFLFGPHAPYTCSPKLLTWVREKADETGKMITIHLSETKDEVKQIKEKYGKTPVELLDELGFLKNDVIAAHGVWLTDKEIEILAKRDVTIVHNPASNMKLGSGVMSLEKLLKAGVNVALGTDGAASNNNLDMIEEMKLAALLHKVHTLNPTLADAKTVFKMATQNGAKALRLNAGVIKEGALADVIVIDFNKPHLRPITNIISHIVYSANGNDVETTIVDGKVVMLDREVLTIDEEKILDKVQKIVDKLR", "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": "MSSKVGGGKGGKSKTSSEAKVLTTRSSKAGLQFPVGRIHRFLRNKNANNVRIGAKAAVYVASIMEYLTAEVLELAGNAAKDLRVKRITPRHLQLAIRGDEELDLLIRATIAGGGVLPHIHKSLVAKNAPLKKPKALDA", "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": "MSRFFANGSDSESESSEEEVQATNFNKASAFQFSDDEEEVKRVVRSTKEKRYENLTNIIKTIRNHKKIKDIPNTLSSFEDLTKAYTKALPVISKEENGITPRFYIRCLAELEDFINEVWEDREGRKNLSKNNSKSLGTLRQKVRKYIKDFEDDLSRFREAPDQESEAEDEEAAQDSDGGDAGDDSDAGIKREPAEAAPKVAKTVPAKAAPADDDDSDDSIDWDSDSETETESSDDENQYQNMRERFLKRTTEKEEKDDDKRKDKRKEQKIKIRKRPEDDEDGEWETVVKGHVVEKPKMFEKDAEIDIPLVLAKLVEIMSARGKKRTDRRLQIDLLFELRDISDQHNLGTAVSVKIHFNIISAIFDYNQKISEPMKLEHWALLLEVMQSMLKLLLVNPDIHMSESVAEEHEELATSPFYVRGCPLAAVERLDDEFTKLLKECDPHSNDYVSRLKDEVNVVKTIELVLQYFENDGNNNERCRIYLRKIEHLYYKFDPEVLKKKRGEIPQNTQTSVDVMDRLCKFIYAKDDTDRIRTRAILAHIYHHAMHDNWFQARDLVLMSHLQDNIDAADPATRILYNRMMANLGLCAFRQENIKDAHHCLVDLMVTGKPKELLAQGLLPQRQHERSAEQEKIEKQRQMPFHMHINLELLECVYLVSAMLLEIPYIAAHEFDARRRMISKTFYQQLRSSERQSLVGPPESMREHVVAAAKAMRCGNWQACANFIVNKKMNTKVWDLFYESDRVREMLTKFIKEESLRTYLFTYSNVYTSISIPSLAQMYELPVQKVHSIISKMIINEELMASLDDPTETVVMHRSEPSRLQALAMQFVDKVTNLVDVNEKVFDMKQGNFFQRGNMGNRGDRGYNRNQDGNWGGQLRDIKRIRGQRIQRGRKHQQQQQQQVQTIDEE", "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": "MFCEQCEQTASGNGCHQWGACGKSPEVNAVQDLLVYCLRGLAPVVLKAKELGISTHQADVFTGEALFATMTNVNFDKKRFTKYIRDCITIREQLKAAINQPVAWTDICCYQPNFNESLVEQGQNVALTLISQATNNLDIFSLKLTVLYGIKGCASYNFHAQELGQEDEKVYSFIQEALASLDRNDLSLNDWVNLALKVGETNLKAMELLDAGHTSTYGHPTPTSVPLNPRLGKALLVSGHDIKQLAAILQQTANTGLTIYTHGELLPAHGYPILKQKYPHLYGHYGTAWQNQTKDFAKFPGAIIVTTNCLMPPHETYDEKLFTIGPVGYQGINYLASDETGTPDFTPAIEKALSMPGFTTEETPRNVMVGFAHDAVLKVADTVIEAVQQGKIRHFFLVGGCDGAKPGRTYYTEFVEKVPKDCIVLTLACGKFRFFDKQLGSIGTLPRLMDVGQCNDAYSAIKIALGLANAFNIEVNQLPLSMILSWYEQKAIAVLLTLLYLGIKDIRLGPTLPAFITPNLFKLLSETYNLQSITTPEKDLAACLA", "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": "MSGVWVFRNGVVKLVENPPASANSGGGGGGGGGGGGGGIRRKALLHMPTGEVVTSYASLERKLAALGWERYYSGGGGAAAAAAMMLQFHKRSSVDLISLPKDFSQFGSVHMYDIVVKNRDAFRVIDV", "text": "SIMILARITY: Belongs to the FPF1 family."}
+{"protein": "MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSAPKEMADAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDVVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCEEIAQLAEDCGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENFA", "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": "MPTWGARPASPDRFAVSAEAENKVREQQPHVERIFSVGVSVLPKDCPDNPHIWLQLEGPKENASRAKEYLKGLCSPELQDEIHYPPKLHCIFLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEELAERLSWDFTPGPSSGASQCTGVLRDFSALLQSPGDAHREALLQLPLAVQEELLSLVQEASSGQGPGALASWEGRSSALLGAQCQGVRAPPSDGRESLDTGSMGPGDCRGARGDTYAVEKEGGKQGGPREMDWGWKELPGEEAWEREVALRPQSVGGGARESAPLKGKALGKEEIALGGGGFCVHREPPGAHGSCHRAAQSRGASLLQRLHNGNASPPRVPSPPPAPEPPWHCGDRGDCGDRGDVGDRGDKQQGMARGRGPQWKRGARGGNLVTGTQRFKEALQDPFTLCLANVPGQPDLRHIVIDGSNVAMVHGLQHYFSSRGIAIAVQYFWDRGHRDITVFVPQWRFSKDAKVRESHFLQKLYSLSLLSLTPSRVMDGKRISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESEKWMAIIRERLLPFTFVGNLFMVPDDPLGRNGPTLDEFLKKPARTQGSSKAQHPSRGFAEHGKQQQGREEEKGSGGIRKTRETERLRRQLLEVFWGQDHKVDFILQREPYCRDINQLSEALLSLNF", "text": "SIMILARITY: Belongs to the N4BP1 family."}
+{"protein": "MAGENTSRRTGSARLDEVIPEFELVSTDVKILAEKYLQDERIYRIWFEYLIPDEIDLIFPTTDGKLNYLSFTKRLASAIRYGRIKTAVSNNSSSNSYGSTEHVCDHGTSLCGRSERFASVINRFLDLHQILKDC", "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": "MIRKDLSQIPTYVPGKRNDHALKLSSNEVTHRPLPSAAQAMAEAAAGANRYPDMGVTELRGALSEHLGVPAEQIAVGCGSSALCQQLVQITCTPGDEVVFPWRSFEAYPIFVQVVGATPVAVPLTSDGFNDLDAMAAAITPKTKLVFVCNPNNPSGTVVRREAFLEFMAKVPADVVVALDEAYTEYVRDEDTIFATEILSEFPNLVGLRTFSKAFGLAGVRVGYAFGPHELIDALNKVALPFGVNAVGQAGALASLNNLDELMEHTEEVVAVRDRVADHIGAAHSQANFVWIPAESRSETPFEIAEKLAAHDVLVRAFPEGVRITVTNEEESDRLLAAWDASFA", "text": "FUNCTION: May catalyze the transamination reaction in phenylalanine biosynthesis. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MYPAHLLVLLAVCVSLLGAASIPPLPLNLVQFSYVITCANHNRRSSLDYADYGCYCGAGGSGTPVDELDRCCKIHDDCYGEAEKQGCYPKMLIYDYDCGSNGPYCKNVTKKCNRKVCDCDVAAAKCFARNAYNNANYNIDTKKRCK", "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": "MLIKTIFIIFLMFFSVNVFSKNVWIIENIQFKGLKYFSKDEVLKNIFFNIGSNISENDIKHSIKSLFQTGKFETIKIVHSGKTIIFEIKERPIISNITFSGNKIIKDSILKKYLTELGIKEGNFFNPFLNTVFVKNLKEFYSNVGRYNSDIKIFKKISSNNKIDLQIFIHESNLVEINHIKIIGNNHFPRDKILSLFKLKDCKSWWNFLEKRFYYSQQLEEDLKNLSNFYLNQGYYYFNIHRKKVRFLKDKNKVNITVYISEGKKYKISNFFLNGNLLQYYQSIKNFINIHNNEFYNKEKITLIVKKIQRFLSEKGYIDPKIIIYPQINFKEKKIILNFNIDIQKRYFVNKINFRGNELTQDIVLRREMKQIEGEWFNLKLIELGIKSLEKLKFLSDITVQKEILFNKENGVDITYTLKEQPTGTLNFGLGYGRDSGLSFNASISQDNLFGSGNSLKASIIKNDNQKYADISIMHPYFIDDGTNLDTRIFYNDFKYNINSFYNIVKTTSGFESDLSFLINAFNRVNIGFGYTHNGLLNKEEKFFSKNGNKSSDKFLKTSLVDDFTLNYSLTHDTLKYFYFPISGNQTYISGKNTIPGSDNKFYKFLFDSEQYIPLEEEKKFIFLTHIRAGIGNSLNKEKLPFYENFHAIDSNNIRGFRANTIGPKKIYINSNLEECLGYNKKSIFCESVDSIGGNAMIISNLELITPIPLIKTEYSKFLRSSFFLDAGNIWDTRWDKEQNIHFSQFPDYTILNNIQASIGISLQWFSPIGPLVFSYAYPIYKNKNNQLEAFQFNFGKNW", "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": "MELVPSARAELQSSPLVNLSDAFPSAFPSAGANASGSPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKLKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTQPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDINRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRTPCGRQEPGSLRRPRQATTRERVTACTPSDGPGGGAAA", "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": "MVNVVLGAQWGDEGKGKLVDLLVGKYDLVARCAGGNNAGHTIVVDGVKYDFHMLPSGLVNPKSLNLLGNGVVIHVPSFFKELEDLETKGLNDARERLFISSRAHLVFDFHQRTDKLRELELSGASTDGKNIGTTGKGIGPTYATKASRSGIRVHHLVNDNPESWTVFENMYRRLLETRKKRYGDFEYDAEGELARFKKYKEDLKPFVVDSVVFMHKAIEAKKKILVEGANALMLDIDFGTYPFVTSSNTGIAGVISGLGIPPKVIDECYGVVKAYTTRVGEGPFPTEQLNEDGEKLQEIGAEYGVTTGRKRRCGWLDLVIMKYSTLINGYTSLNITKLDVLDTFKEIPIGIGYYYKGQKLDLFPEDLIKLGKVEVEYKVLPGWQQDITKVTKYDDLPENAKKYIKFIEDFVGVPVEWVGTGPSRDNMVHKEIQRI", "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": "MTVRLILAKGREKSLLRRHPWVFSGAVARLEGKAQPGETIDVCDSQGKWLARAAWSPSSQIRARVWSWQQDESIDIDFFVRRLNAAQQLRDWLALRDNLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALITALQRCYPDCAIYDRSDVSVRKKEGLELTQGVVLGDAPPPLLPITEHGMKLLVDIQTGHKTGYYLDQRDSRQATRRYAQGRRVLNCFSYTGGFAVSALMGNCKEVISVDTSQAALDVARQNVELNGLDVSKAHFQRDDVFKLLRRYRDEGEKFDLIIMDPPKFVENKNQLMGACRGYKDINMLAMQLLNPGGMLMTFSCSGLMATDLFQKILADAAVDAQREVQFIEQFRQAADHPVISSYPEGMYLKGFACRVI", "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": "MSGGKPRGLNAARKLRNNRREQRWSDLHYKKRALGTAFKSSPFGGSSHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKVTAFVPNDGCLNFVDENDEVLLAGFGRKGKAKGDIPGVRFKVVKVSGVGLLALWKEKKEKPRS", "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": "MHTSPMEQPGTGDAGGLNVYVVELSRQLAALGVEVEVFTRAVSSKLPTSAELAPGVTVRHVDAGPFEEIHREDLPAWLCAFTADVLRAEAGHEPGYFDVIHSHYWLSGQVALAVARRWGVPFVHTSHTLAKIKNGALAVGDRPEPPGRLLGEQEVIAGSTRLIASTADERGHLIDLYDADPDRVDVVAPGVDLETFRPGDPAQSRARLGLDRDGDLLLFVGRIQPLKAPDLLLHAAAELLRRDPTRRSRLTVAVVGGPSGSGLEQPDALVKLAADLGISDLVRFQPPAPQHELAHWYRAATAVVVPSHSESFGLVALEAQACGTPVVAAAVGGLRTAVADGVSGLLVAGRDPARYADTLDRLLRQPHWRSRLAAGAVGRAAGFGWSATARGVLRSYRHALSPAAVAV", "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": "MLHLLGQDSRALARKAGISLEDARRITGAVIGRGAPLRSARNVRRAVLDRVEALATPGELRRVACTDAKDGFRRYLLELGDGARVEAVRIPLFDTHHTVCLSSQAGCALGCSFCATGALGLARSLRAWEIVAQLLHVRADSTRPITGVVFMGQGEPFLNYDAVLEAAYTLCDPAGGRIDGRRISISTAGVVPMIRRYTAEGHKFRLCVSLNAAIPWKRRALMPIEEGFPLDELVDAVREHAAQRGRVTLEYVMIAGVNTGDEDAAALGRLLAGIPVRLNPIAVNDATGRHRPPDEAEWNAFRDALARELPGQPIVRRYSGGQDEHAACGMLSSRTR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family."}
+{"protein": "MIEINRVNKIFYQGAKEINALKDINLHIAQGTIFGVIGSSGAGKSTLIRCVNMLERPTNGEVVVDGVDLTKLSSSELSKARRNIGMIFQHFNLLASRTVFDNVALPLELAGKSKHDIQKKVTELLDLVGLADKHHTYPANLSGGQKQRVAIARALSTDPKVLLCDEATSALDPATTKSILELIKDLNRKLSITILIITHEMEVVKNICHEVAIIGGGELVEKGAVSDIFAHPKTALAQEFIRATLDLSIPEDFKARLKDTYVEGSYPLIRLEFTGSTVDAPVISQISREFDIDISILSSDIDYAGGVKFGLMLAEVFGNQESTQKAIEFLRNHHVKVEVLGYVV", "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": "MSETEKIEEAAPPYLCEEPPEGAVKDHPQQQPGMISRVTGGIFSLTRGAVGATIGGVAWIGGKSFEVTKTAVTSVPSIGVGIVKGGVSVVTGSVAAVGSAVSNKVSGKKKDKSD", "text": "FUNCTION: May play a role in bone development. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM263 family."}
+{"protein": "MVVKNSIKFNSQSERKSLEETKVPPIFGLPPDALDDKKPTSDFAVPIIDFAGVHKSREAVVEKIKAAAENWGIFQVINHGVPLSVLEEIQNGVVRFHEEDPEVKKSYFSLDLTKTFIYHNNFELYSSSAGNWRDSFVCYMDPDPSNPEDLPVACRDAMIGYSKHVMSLGGLLFELLSEALGLNSDTLKSMGCMKGLHMICHYYPPCPQPDQTLGTSKHSDNTFITILLQDNIGGLQILHQDCWVDVSPLPGALIINIGDFLQLMTNDKFISVDHRVLTNRVGPRISIACFFSSSMNPNSTVYGPIKELLSEENPPKYRDFTIPEYSKGYIEKGLDGTSHLSHYRI", "text": "SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
+{"protein": "MERKSSLKVRVQKLGTSLSNMVMPNIGAFIAWGVAASLFIATGYLPNKALDTNVVGPMLKYVLPLLIGYTGGYNIHKQRGGVIGAIASFGAIAGSTVTMFIGAMIMGPLSAWILKKFDEKVQPKIRTGFEMLVNNFSLGLIGFALMVLAFFVIGPVVAQLTEWVGIGVEAIVKVHLLPLANLIIEPAKILFLNNALNHGIFTPLGTEQVAKVGKSVLFLLEANPGPGLGVLIAYAMFGKGSAKSSSWGAMIIHFFGGIHEIYFPYVMMKPAMFLAVIAGGLTGTFTFQTLGAGLTAPASPGSIIAIMGMSPKGWGPHLVVLAGVFAAAVASFLVASIILKSDNSDDDSLETAQAVTQAAKAESKGQAVTEPNLHSDITTDNIHQIIFACDAGMGSSAMGASILRDKVKKAGLDISVSNQAISNLQDTANTLIVTQEELADRAGQKTPRAVHVAVDNFLATSKYDDIIASLTNGKASGSENAAHSTQADSAEIDLNQIDAVVFAYGIAKGSATMGQETLRSIFKQNNVKIPVSTASYAHLSDYNAKNILLVTTIAQQGQAQQAAPNAQILVVDSLVTTPEYDKLVARMHK", "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": "MAVQQRRVSKSRKGMRRSHDHLTISNTVACNECGKALLPHRACRDCKTYRSIKLSIK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
+{"protein": "MNILNLKIIMFLLISNIIVVGGAWATSTCPDWPATRIAVEINALEQQLNKWSAAYHQQGHSPVTDDIYDQLQDKLRVWQSCRGLPDKTESQPIPGKGQFLHPVAHTGLKKLKDETALTRWMAGRKNLWVQPKVDGVAVTLVYHGGKLVQLLSRGNGVKGQNWTEKAPFISAIPQYIANAPALLTLQGELFLLMDGHQQAKSGGVNARSTVAGALMRKSPSPLLAQVGVFIWAWPDGPTTMKEKVALLQVMGFPFTAKYSEPVMSHLDVVQWRQFWFQAPLPFVTDGVVVRQEEEPAGRYWQATPGQWSMAWKYPPLQHIAEVKDIHFTLGRTGKGTVVLEVLPIKIDDKWIRRVNIGSVTRWKQWDIAPGDHITLALAGHGIPRLDNVVWRVHQRNTITAPNWDKFHQLSCFQRLPHGCEPQFLSRLIWLSGPGGLDIGGIGGGFWQKLIHHELINDLVGWLLLTPEQIASIPGIGNARAEKIYQQFQRAKQQPFSRWLLALGFPQVVSVDAQWQVVLRRSLSEWATMAGIGQMRAKQIKHFLDHPDVQALADFLSTQKVVGFELTE", "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": "MYQRALLFSALATAVSAQQVGTQKAEVHPALTWQKCTAAGSCTDQKGSVVIDANWRWLHSTEDTTNCYTGNEWNAELCPDNEACAKNCALDGADYSGTYGVTADGSSLKLNFVTSANVGSRLYLMEDDETYQMFNLLNNEFTFDVDVSNLPCGLNGALYFVSMDADGGLSKYPGNKAGAKYGTGYCDSQCPRDLKFINGEANVEGWKPSDNDKNAGVGGYGSCCPEMDIWEANSISTAYTPHPCDGMEQTRCDGNDCGGTYSSTRYAGTCDPDGCDFNSFRMGNESFYGPGGLVDTKSPITVVTQFVTAGGTDSGALKEIRRVYVQGGKVIGNSASNVAGVEGDSITSDFCTAQKKAFGDEDIFSKHGGLEGMGKALNKMALIVSIWDDHASSMMWLDSTYPVDADASTPGVARGTCEHGLGDPETVESQHPDASVTFSNIKFGPIGSTYKSV", "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": "MISPQEKQDKVIRATDLDALSCRYSANNKSYFSKPDPFIDSLISSYKMHLPLCTGYTNMSANRTLRSVFNEQKLPLINRGTYLRTESIDVITQEFIKEFKKCQVISLGGGSDTRCFRILEEHGEDVRYCEIDFHESVKIKKLAIINDKKLADIVKYDEESQSITSKEEFARLESNIHTENYHLIGYDLRELTGALDSGAILEYVDTSLPTLILSECVLCYLNPKENERIIEFWKNAFASKALLALLIYEPMSLNDAFGTTMTHNLSNRGINLLTFNEYPNLEARYKFLSEKCQSSNVKLTDMSNVGGYDSDNTTKAWINSKDLARINRLELVDEIEEIRLLLKHYCLCYCEFSHSPSLKTINKWKWILE", "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": "MSVSRIYIANVSYSSSEEDLREFLKDFNFSSVLIPCHTVRRFRRNEARSFGIAYVDFTSSEEAVRAVEELNGKEFGGRVLRVRTHNPYQPPKPIKERFGTKLQQLKKFAKYEDTAASGERAPTDAQDHPDQPQEGHMSPDVVLVNGTTDEEQQLANVINDPVTNADAPGTEQNISKEKAISEDTVYCAFLPKETTDNDLRNYFTDYGSREIWIFRTKNVSNSRFRFRNRNHTAALVTLSTELPLNKVIEELLGKKLLGTKISIKPAYIYKINEVKKIAEQSHMLATEYRHQNGNSDVVIGTPNEALLNSTQVASQIIGSNPEIEVSNQNSSSIANVAETNGNVGDTPITKLDSRNNIKIVNIGNPQDKTKKNQPNDNKELNKIDLETKNDSLHLESICDPIISIDMSGMTKQSVGSNKKKNKKKKSARGKEVRKLSVSNTTTQ", "text": "FUNCTION: May be involved in the modulation of rDNA transcription. SIMILARITY: Belongs to the RRT5 family."}
+{"protein": "MISNFGHIVKTYLSNFPKDDYPVLDTFKFVSIWLGLVLDQSQTSMRSMFKRLNLRGETVDISTFSKASKKRDVGVFREIIFSLKKELSKRKEIKQGELEIFPLDSTIVSITSKLMWNLGFHQVKVFSGINLSTGIPGGIVIHFGQGHDNKYGNETIEETPENGVAVMDRGFCDLQRIKRLQKENNKYHVLRIKNNIKLEKLANDNYMVGTGKNKIESRVVIFTHDNSEFRLVTNLPIESKEIEGVSDEKIAEIYKKRWQIELLWKFLKMHLKLNRLIAKNENAIGIQIYTCIIAYLILKLLVIPKEAGTTMLDKLRYLQAFMCEKISYVHWLRELALR", "text": "SIMILARITY: Belongs to the transposase 11 family."}
+{"protein": "MSTDARANHRIKSIEIDEESLAAASRDQEQERQVAIFDLLEGNYFEPAEAGDGPYDVRLSLIENRLAFDIASAGHARRHLLSLSPFRGVIKDYFLICDSYYSAIRNSSPQQIEALDMGRRGLHNEGSNLLRERLEGKVKTDLDTARRLFTLICALHWRG", "text": "SIMILARITY: Belongs to the UPF0262 family."}
+{"protein": "MKKTAIAITVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFIDNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGSVENGAYKAQGVQLTAKLGYPITDDLDVYTRLGGMVWRADTKAHNNVTGESEKNHDTGVSPVFAGGVEWAITPEIATRLEYQWTNNIGDAHTIGTRPDNGLLSLGVSYRFGQGEAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA", "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": "EVPADAVTESDPTAVALKYHRNAAESERVAAARPGLPPEEQHCENCQFMLPDQGADEWRGCSLFPGKLINLNGWCASWTLRAG", "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": "MKKAGLLFLVMIVIAVVAAGIGYWKLTGEESDTLRKIVLEQCLPNQQENQNPSPCAEVKPNAGYVVLKDRHGPLQYLLMPTYRINGTESPLLTDPSTPNFFWLAWQARDFMSQKYGQPVPDRAVSLAINSRTGRTQNHFHIHISCIRPDVREQLDNNLANISSRWLPLPGGLRGHEYLARRVTESELVQRSPFMMLAEEVPEAREHMGSYGLAMVRQSDNSFVLLATQRNLLTLNRASAEEIQDHQCEILR", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Cdh family."}
+{"protein": "MAGNMLANYVQVYVMLPLDVVSVDNKFEKGDEIRAQLKKLTEAGVDGVMIDVWWGLVEGKGPKAYDWSAYKQVFDLVHEAGLKLQAIMSFHQCGGNVGDVVNIPIPQWVRDVGATDPDIFYTNRGGTRNIEYLTLGVDDQPLFHGRTAVQMYADYMASFRENMKKFLDAGTIVDIEVGLGPAGEMRYPSYPQSQGWVFPGIGEFICYDKYLEADFKAAAAKAGHPEWELPDDAGEYNDTPEKTQFFKDNGTYLTEKGKFFLSWYSNKLIKHGDKILDEANKVFLGCRVQLAIKISGIHWWYRVPNHAAELTAGYYNLDDRDGYRTIARMLTRHHASMNFTCAEMRDSEQSEEAKSAPEELVQQVLSAGWREGLHVACENALGRYDATAYNTILRNARPKGINKNGPPEHKLFGFTYLRLSNELLEGQNYATFQTFVEKMHANLGHDPSVDPVAPLERSKPEMPIEMILKAAQPKLEPFPFDKNTDLPVKDHTDVGDEVLVAPV", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 14 family."}
+{"protein": "MTLKLIWDKFYVSIIFVITCLVLGIVLMCTVLGNSNNYSEVNINEGDSLWAIADEYASKSDMPKADFVAWVEKENNLTEGHVKAGDSVVIPVHETKLQNSDSTIQLANQ", "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": "MQLHRINTMDLKHSLRDLCMNPRHTSWAAPLLILGDAVLCALIIWRVPYTEIDWTTYMQQISLYISGERDYTLIKGSTGPLVYPAAHVYIYNILYHLTDEGRDIFLGQILFAILYLATLTVAMTCYRQAGAPPYLLVPLVLSKRLHSVFMLRLFNDGIAAFAMWVSIFLFMNKKLAAGVIVWSTGVAIKMTLLLLAPAIAMVLVLSLSFGPSIRLGFLAVLIQVLFGIPFLRNNPAGYVSRAFELTRQFMFKWTVNWRFVGEELFLSRKFSLALLALHLLLLGLFVATVWLEPSGSNLPSFLQRLIQRRYRTASLSKSFVMTAMLSSLAIGLLCARSLHYQFFAYLACATPFLLWQAGFHPILVYVVWAAQEWAWNAYPSTNASSLVVVLSLAAQVFGVLGNSFSRKHLDQSSQKEHMQ", "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": "MTFEEITNKILVKDKDYEMPFSKGLLTRSLTAAGMKPSESYILAREIERDLTDQGLRKISKDELRRRVYYALINRDYEDIAEKYLLWRRVLKKHSIIILVGGASGVGTSTIAFELASRLGIPSVIGTDSIREVMRRSISKDLVPMLYESSYTAWKALRHSSAEEYDTKEMHLLGFERHVEPVLIGIESIIDRSLTEGMSVILEGTHIVPGLLGEKYHSMQNVIILNLTLSSEEIHKQRFVARAKVSDRPLERYLSNFEIIKEINEYIVKKSRENKVPVIENVSISETVQKCLEIVTDRFVDLNEESEADSEIY", "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": "MDLGTTKYIIYTELIADGYVEKHDVIGAIFGQTEGLLSNELDLRDLQKSGRIGRIDVELENINGKSFAKITLPSSLDKVETSILAATLETIDRVGPCFATVKITEVEDIRVSKRQYITNRARSILRKLMDEMIDTYEITEEIKESLRTEEIMEYGPENLPCGPNIIHSDSIIVVEGRADVLNLLRCGIKNTVAVEGTSVPKSIMELTKKKTTTAFTDGDRGGELILKELLQTCDIDYVARAPYGKEVEGTSKKELMKCLRAKVPVEQIVGNNCNGSGVIESNTPKEIVEPITPKHFEKVETPAVIEPVFKEDAIEEETIIVEPVKKAETEIIDVDATNETQSEKKFSGVKEIVDSIKNTGNVKFVVDGTEKTNTFKEFLTNIHEIKKMDFFAADMPISQKIVDLLYDKTPIIVGKEINVTKKPVNLRLFSFDEIVA", "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": "MACNSSGCESGCYDREKDNGSKIVDDAVSGGGNHESVCVKCKCNAPMTFGDGGFDDGRFCADCFRNNVFGKFRLAVTSHAMITPSDNVLVAFSGGSSSRVSLQFVHELQIKALKNYEASRDRSLPVFGVGVAFVDETAAFPALSTEMIDAIEWVRYTVSCLSPPAKDLHVVPVESIFGSDSLDARDRLLKLLDSVPDDTGKEDLLLHLKMLSLQKVAAENGYNRLVLGSCTSRIASHVLTATVKGRGYSLSADIQHVDARWKVPIVLPLRDCVRLEITRLCLLDGLKTVELACRSQCGINDLVSSFVALLQEENPSRECTIVRTAAKLTPFYFNKIPETDDSNVPMATQRRLKRFNLKYDGSMTTEAFCPICNGPLNRSDSSELDTFEEGQESDVLYAACCSSCRFQILPQDGSSLEQFSSFLPDHMISQVKHQKVDSQAYLREKIKDCLLLDDEEVV", "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": "MNAHTGTVRGKERYRSGVMEYKRMGYWEPDYTPKDTDVIALFRVTPQEGVDPIEASAAVAGESSTATWTVVWTDRLTAAEKYRAKCHRVDPVPGTPGSYFAYIAYDLDLFEPGSIANLSASIIGNVFGFKPLKALRLEDMRFPVAYVKTFQGPATGIVVERERLDKFGRPLLGATVKPKLGLSGRNYGRVVYEALKGGLDFTKDDENINSQPFMHWRDRFLYCIEAVNRAQAASGEVKGTYLNITAGTMEDMYERAEFAKELGSCIVMIDLVIGYTAIQSMAKWARRNDMILHLHRAGHSTYTRQKSHGVSFRVIAKWMRLAGVDHIHAGTVVGKLEGDPNTTRGYYDVCREDFNPTKLEHGLFFDQSWASLNKMMPVASGGIHAGQMHQLLDLLGEDVVLQFGGGTIGHPMGIAAGAIANRVALEAMILARNEGRDYVHEGPEILAKAAQTCTPLKSALEVWKDVTFNYQSTDTPDFVPTALETV", "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": "MNKDDDKEGMAMFSALIEGIKPITQDKRHFRTPLKTKQEIELKEQQLHANSYFSDTYQPLLPVQGPMRWLDEGVDSLELKRLRRGDYQPDLLLDLHGYRQSEAKLELAALIQACVKQQSQCCCVMHGYGTGILKQQVPMWLVQHPMVKAFHQAPKEWGGDAALLVLIDIGDQPHRR", "text": "SIMILARITY: Belongs to the UPF0115 family."}
+{"protein": "MFQRDIKITTPNGLHTRPAALLVKEAKKFISEINIISNGKSANAKSLFKLQTLGLVQNSLITISAHGIDEKVAVEDLAKFLTTLK", "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": "MIYDFKAEIIKAKNSSFSKSGSHHWLLQRVTGVILALCSFWLIYFMFTNKNNDINIIMWEFKKPFNIVILLITVTISLYHSVLGMRVVIEDYINCHKLRNTLIIIVKLFCILTIVSFVVAIFYSG", "text": "FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "LQGLLLWLLLSVGGVWASRGPLRPLCRPINATLAAENEACPVCITFTTTICAGYCPSMVRVLPAALPPVPQPVCTYHELHFASIRLPGCPPGVDPMVSFPVALSCRCGPCRLSNSDCGGPRAQSLACDRPLLPGLLFL", "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": "MAARAPAARTLLCPAFRRTHSHDPADRQSPVPFRRLWPPCPRPRRGLPAATTSRSPSSRPTPQLHIALPTRRAGRHAPDLAALFEAVGVRHVPGVVTTIHADAARWTSPHRRRPVHPALRPLRPGRRSRLFTPPIPGLAEHAFNVDAGGVTTSTGERIRPPPSSGRGAAANPVGAADSPASMTVRARSADPFLAGDRHATASSSTGDVALAARRPRQRCRHVPASTL", "text": "SIMILARITY: Belongs to the NifX/NifY family."}
+{"protein": "MRMLLHLSLLGLGAAYVSAIAVENTMNRLVAETLTLLSIHRTLLIGDGNLMISTPVHTNHQLCIEEVFQGIDTLKNQTARGDAVEKLFQNLSLIKEYIDRQKKNCGGERWRVTQFLDYLQVFLGVINTEWTMES", "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": "MKIATLAVVSAFAATAIAGPIRPDGVVNDKFLIELGPGETQWVTKQQKHEMRAHINSIYKAGQGFVDITDEFGTDFTTAEVVPANYPKSALHAAVVNPMIAGLSKENLMRDLNTLVKFNNRYYESPTGVESATWVFNEVQKIIQASGVKGAKVEKFTNKFKQFSVIATIPGASKNTVIVGAHQDSINLKDPMKGRAPGADDNGSGSVVVLEAFRNVLKSKAIQAANATNTLEFHWYAGEEGGLLGSNNIFKKYKADGRKVKAMLNQDLTGFTKKGNPEQFGLITDNTNAELNEFCKTIVEKYATIKIIEAKCGYACSDHASAHRNGFPSSFIAETNFRNTNPYLHTADDVIANLDFNHMLEHAKVVVGFMGELAMTPNL", "text": "FUNCTION: Probable extracellular aminopeptidase which contributes to pathogenicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily."}
+{"protein": "MTLHCQEPKIRSLDMLSNSEIKPSENSQKTKVLLTKANNASNERAPPPLSHFIAGGVAGMLGAIATAPLDVVKTRLQSDFYKDRFLKQTAKSKSPLTAAYRHFMDTCIILKNVKVHEGTRALFRGLGPNLIGTIPARSINFFSYGNGKRILADLFNNGQENSQIHLMAAAIAGVITSAATNPIWLVKTRLQLDKKSGQAAQYRSSIDCIIKTIRLEGFRGLYKGLSASLLGVGESTLQWVLYEKFKHAVAIRQLRRKELGIQETIYDKVLDWGGKLGGAGIAKFMAAGIAYPHEVVRTRLRQSPSINGTPKYTGLIQCFKLVWMEQGIVGLYGGLTAHLLRVVPNACILFGSYEVIMHFIG", "text": "SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MSIQAPPRLLELAGQSLLRDQALSISAMEELPRVLYLPLFMEAFRRRHFQTLTVMVQAWPFTCLPLGSLMKTLHLETLKALLEGLHMLLTQKDRPRRRKLQVLDLRDVDENFWARWPGAWALSCFPETMSKRQTAEDRPRMGEHQPLKVFIDICLKEIPQDECLRYLFQWVYQRRGLVHLCCSKLVNYLTPIKHLRKSLKIIYLNSIQELEIHNMSWPRLIRKLRCYLKEMKTLGKLVFSRCHHSTSDNELEGRLVTKFSSVFLGLEHLQLLKIKLITFFSGHLEQLIRCLQNPLENLELTYGYLLEEDVKCLSQYPSLGYLKHLNLSYVLLFRISLEPLGALLEKIAASLETLILEGCQIHYSQLSAILPGLSRCSQLTTFYFGRNCMSMGALKDLLRHTSGLSKLSLETYPAPEESLNSLVRVNWEIFTPLRAELMCTLREVRQPKRIFIGPTPCPSCGSSLSEELELHLCC", "text": "SIMILARITY: Belongs to the PRAME family."}
+{"protein": "MVALYCGGGLRPLMLSWSRDLPCIWRALHTSAVCFKNRAARVRVGKGNKPVTYEEAHAPHYIAHRKGWLSLHTGNLDGEDHAAERTVEDVFLRKFMLGTFPGCLADQLILKRRANQVEICALVLRQLPAHKFYFLVGYSETLLSHFYKCPVRLHLQTVPSKVVYKYI", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
+{"protein": "MDIETAACFSIAFIATPILIVLVRLLFILPSLRLPTSVKKKKKLIQECQLSILLGSGGHTGEMMRIISKLDMGKVSRTWIYTSGDNASLAKAQDYERKSGTSSQYIPIPRARTVGQSYISSIPTTIYSFLFSAIAMLKHRPAVILLNGPGTCVPVAYILFLYKLLGLCNTKIIYIESLARVNKLSLSGLLLLPISDRFIVQWESLYQQYSRVEYYGILI", "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": "MSLKMKGKKYTDLDFVPTISDSEEDVPDLDSDEEKPKPETKGKKKNKSVDEESADMNSGFRFNTDDGEINTNFDGWEFLGDEKDEEKKDVDLDKIIRKKGGLIGMAHVDEAEKSESEESESDDEDLAMDGFGMGAQEQPEGEEEDEDASNSEQESNDEEEDDDEETYDVGDAGDAEEKVEEDTAEEMQAFYAPESESENAKKEVHKTFNDLALSRPVMKGLSNLGYVKPSPIQSATIPIALLGKDIIAGAVTGSGKTAAFMIPIIERLLYKPAKVASTRVIVLTPTRELAIQVADVGKKIGQFVSNLTFGLAVGGLNLRQQEQMLKTRPDIVIATPGRFIDHIRNSASFNVDSVEVLVIDEADRMLEDGFQDELNEIMSLLPSKRQTLLFSATMNSRIKQLISLSLKRPVRIMIDPPKQAATKLTQEFVRIRKRDHLKPSLLFNLIRKLDPNGQKRIVVFVARKDMAHKLRIILGLLGMAVAELHGSLTQEQRLDSVNKFKSLQVPVLICTDLASRGLDIPKIEVVINYDMPKSYEIYLHRVGRTARAGREGRSITFVGEASAERSIVKDAIRGVNDSEIPGSKAVGRNVDWNQVEETNKIVENMDQTVQDILVEEKEEKEILRAEMELKKGENLLKHKDEIQSRPKRTWFQSEKEKKNSKIMGALSKTKKEVNSKKRKRNEAMEDGHKRSYKKTQSDRTADQERTMKKQAKANGKKKGKSKGKR", "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": "MSTEYRTGREGEFTYRGHDLDELQEMSLEDVAELLPARQRRTITRGLSEEHHKVLAEARESGTEETANNPIRTHLRDMPVLPEFVGLTFAVYTGQEFERVEVQPEMIGHYLGEFQLTRSSVEHGQAGIGATRSSKFVPLK", "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": "MIQIIYVASPESQQIHVWKLDSIYGLLELIQVIYTHGQAQPMAVHPNKRFLYVGIRPNFGITTYRIDQIGLLADHGTIGIFSSPTHLISDKKGAFLYCTSYRNNTVSVIPISMSGMLLDSPIQIIEGLLGCHSANIDKFKKLLWVPCLKENAIRLFNINSFGMLTSYDPSIIKINVGSGPRHMIFCDFDCYAYVINELTSTVDVIKYNNFQKIPSIVQTVSIIPKNISINRCWAADIHITPNGRWLYCTDRSINIISCLEISKKTKKLKFVGYQLTEEQPRGFAIDYQGKFLVVAGQKSNCISLYKIDSDNGTLTMLSRYSSGKGPMWVSIITLNCK", "text": "FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate. SIMILARITY: Belongs to the cycloisomerase 2 family."}
+{"protein": "MSHAVKIYDTCIGCTQCVRACPLDVLEMVPWDGCKAGQIASSPRTEDCVGCKRCETACPTDFLSIRVYLGDETSRSMGLAY", "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": "MTALLDTFVSKIIENSDYAELDATYLSNRILALVGEDNAQQDTNQSNLIALKDELVDLAVVNGKVGDLAEEKDCLGAELMNFITPIPSQVNKAFWDTNAKSPQKAIKDFYELSKRNNYIKVTAIAKNIAFTTSSVYGDIDITINLSKPEKDPKAIAAAKLAKTSNYPKCQLCMENEGYQGRINYPARANHRIIRMNLGDEKWGFQYSPYAYFNEHCIFLNTEHVPMVISQNTFRQLLDIVDIFPGYFAGSNSDLPIVGGSILSHNHYQGGRHIFPMEIAELDSVFRFKDFPDVTAGIVKWPMSVIRLRGANKYSLVELAEIIRLAWRNYSDDTMNILAFTGDTPHHTVTPIARKRDGQFELDIVLRDNHTTAEYPDGVYHPHIDVQHIKKENIGLIEVMGLAILPPRLKKELAEVEKYVLNQYNEMADYHKDWADAIKASHPETSSETVSEIVKQAVGRTFVRVLEDAGVYKRNRQGQAAFMRFVESIGVK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase type 2 family."}
+{"protein": "MSLIREIAGGPYALAAGPDGAMWVTLVHDGAIARVGADGAVDRFPVADGSRPSLISAGPDGALWFTRNGDDRIGRLTTAGELTEFPLSEGSAPFGICAGADGALWFTEMGSGGIGRITVDGETSGWASVGGTPSMITRGPDDAVWFTLNQGNAIGRLHPRDGVTMRELPTRGAGPVGITATHDDAIWFTEILADKLGRIPLDGALQEIDLPGKPHAVVADPSGGVWVSLWGADRLARVSADGDIETFDLPPGSEPHGLAFGPDGGLWVALESGFVLRMPD", "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": "MAEHLASIFGTEKDRVNCPFYFKIGACRHGDRCSRLHNRPTVSPTIVLANMYQRPDMITPGVDAQGQPIDPEKMQEHFEDFYEDIYEELSKFGEVETLNVCDNLADHMIGNVYVQFREEEQAVAAHNALQGRFYSGRPIIVEYSPVTDFREATCRQFEENSCNRGGYCNFMHVKQIGRELRRKLYGGRSRRSHGRSRSPSPRHRRGNRDRDDFRRERDGYRGGGDGYRGGGGGGGGDGYRGGDSYRGGGGGGRRGGGSRYDRYDDGGRRRHGSPPRRARSPVRESSEERRAKIEQWNREREEKP", "text": "FUNCTION: Necessary for the splicing of pre-mRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family."}
+{"protein": "MDRKYLANAIRALSMDGVQQANSGHPGAPMGMADIAEVLWRSHLNHNPSNPEWADRDRFVLSNGHGSMLIYSLLHLSGYELSIDDLKNFRQLHSKTPGHPEYGYAPGIETTTGPLGQGITNAVGMAMAEKALAAQFNKEGHDIVDHFTYVFMGDGCLMEGISHEACSLAGTLGLGKLIAFWDDNGISIDGHVEGWFSDDTPKRFEAYGWHVIPAVDGHDADAINAAIEAAKADPRPTLICTKTIIGFGSPNKSGSHDCHGAPLGAEEIAATRKELGWEHGPFEIPQEVYAEWSAKETGAAKEAAWNEKFAAYEAAYPELAAEFKRRVNGELPAEWEEKASQIIADLQANPANIASRKASQNALEAFGALLPEFMGGSADLAPSNLTMWSGSKSLEANDFSGNYIHYGVREFGMTAIMNGIALHGGFVPYGATFLMFMEYARNAMRMAALMKIQNIQVYTHDSIGLGEDGPTHQPVEQIASLRLTPNMNTWRPCDQVESAVAWKLAIERKDAPTALIFSRQNLAQQPRSAEQVADIAKGGYILKDSEGKPELILIATGSEVELAVKAAEQLTAEGKKVRVVSMPSTDAFDKQDADYREAVLPSDVTARIAIEAGIADFWYKYVGFDGRIIGMTTFGESAPADQLFEMFGFTVENVVNTAKELLA", "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": "MLEPFFKNYFNQSLTKYNSQVDAINNFGPMLSNLSDDEIRQRVQILKQQLLSNKNEADIICEVFAIVREATFRTLDIKHFDVQLIGGLVLNDGQIAEMKTGEGKTIVALLPTFLNALYGKGVHVVTVNDYLARRDAETVGRVHRFLGLTVGLIQEDMSPEERKQNYQCDVVYVTNNELGFDYLRDNMAFTQEEVVQRPLFYCVVDEVDSILIDEARTPLIISGPSEAPTQKYLQTSQLARVLQKNIHYIIDEKNQVVKLTDEGTLFCEQALKIADLYSPSDPWISYVLNSIKAKELFIRNTHYIVNVEEEVIIVDEFTGRTMAGRRWSDGLHQAIESKENLPIQDESQTLASITYQNLFLLYDKLSGMTGTAKTEELEFEKIYGLKVIPIPTHRDVKRKDFPDLVYKNQYLKWQAIANECIKMNEIDRPVLIGTTTIEKSELLAALLSEYNVPYRLLNARPENIESEAEIVSQAGCRGAITISTNMAGRGTDIALGGNLESLLKVKLKKFISDLVSADFSTVLKSAQFDEFLVSFVPVFETFGLSKLNESSVREDLLEYLNEGIIPDRSDITDFITAYNSFLKERAAILLEEKTLITKLGGLHVIGTERHESRRIDNQLRGRSGRQGDPGSSRFFLSLDDKLLRLFGGDQILNLLQNIGLEDDAPIQSPILTKSLESAQKKVEVYYFDSRKQLFEYDQALTMQRNGIYSERKRVLEKESLRDWIIEYGERSLYDITLAFSTNTNLALDKFFALKTQELLGMPYQVKWESAKGDINVLLNNLKHQFQVSYTLKEAQLEAIEPGIMRELERSFLLQQIDFSWKEHLQKISALRDSIRWRSYGQRDPLTDYKKESYSTFVTMLNRIRHQVIYFIFRSKITIDFE", "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": "MQKTSILILALFAIAEAVPTTGPIRVRRQVLGGSLASNPAGGADARLNLSKGIGNPNHNVVGQVFAAGNTQSGPVTTGGTLAYNNAGHGASLTKTHTPGVKDVFQQEAHANLFNNGRHNLDAKVFASQNKLANGFEFQRNGAGLDYSHINGHGASLTHSNFPGIGQQLGLDGRANLWSSPNRATTLDLTGSASKWTSGPFANQKPNFGAGLGLSHHFG", "text": "FUNCTION: Hemolymph antibacterial protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the attacin/sarcotoxin-2 family."}
+{"protein": "MKHIIHASGNVNGTARNNSDCPHVALPEEIFFIISITGVLENLIIILAVIKNKNLQFPMYFFICSLAISDMLGSLYKILESILIMFRNMGYFKPHGSFETTTDDIIDTMFILSLLGSIFSLLAIAVDRYITIFHALQYHSIVTMHRTIAVLSIIWTFCIGSGITMVLFSHHVPTVLTFTSLFPLMLVFILCLYVHMFLMARSHARNISTLPRGNMRGAITLTILLGVFIFCWAPFILHILLVTFCPNNPYCTCYISLFHVNGMLIMCNAVIDPFIYAFRSPELRSAFRRMISYSKCL", "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": "MRFLPCIATLAATASALAIGDHVRSDDQYVLELAPGQTKVVTEAEKWALRAEGKRFFDITERASSLELASNKKQKLAVTYPDSVQHNETVQNLIKSLDKKNFETVLQPFSEFHNRYYKSDNGKKSSEWLQGKIQEIISASGAKGVTVEPFKHSFPQSSLIAKIPGKSDKTIVLGAHQDSINLDSPSEGRAPGADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVEFHFYAGEEGGLLGSQDIFEQYSQKSRDVKAMLQQDMTGYTKGTTDAGKPESIGIITDNVDENLTKFLKVIVDAYCTIPTVDSKCGYGCSDHASATKYGYPAAFAFESAFGDDSPYIHSADDTIETVNFDHVLQHGRLTLGFAYELAFADSL", "text": "FUNCTION: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily."}
+{"protein": "MASLIQVRDLLALRGRMEAAQISQALNTPQPMINAMLQQLESMGKAVRIQEEPDGCLSGSCKSCPEGKACLREWWALR", "text": "FUNCTION: May function as a transcriptional regulator that controls feoABC expression. SIMILARITY: Belongs to the FeoC family."}
+{"protein": "MAYSIPTPSQLVYFTENYADYIPFVNRLINARSNSFQTQSGRDELREILIKSQVSVVSPISRFPAEPAYYIYLRDPSISTVYTALLQSTDTRNRVIEVENSTNVTTAEQLNAVRRTDDASTAIHNNLEQLLSLLTNGTGVFNRTSFESASGLTWLVTTTPRTA", "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": "MGSLLQGFTKSLAMTFLSEIGDKTFFAAAILAMRYPRRLVLAGCLSALIVMTILSATLGWAAPNLISRKWTHHITTFLFFGFGLWSLWDGFKEGGGSEELAEVEAELDSDLKKTNDQSKNSKIEDEQKKQKRPFLTAFFSPIFLKAFSINFFGEWGDKSQLATIGLAADENPLGVVLGGIVAQTLCTTAAVLGGKSLASQISERIVALSGGMLFIIFGIQSLLTPVDA", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GDT1 family."}
+{"protein": "MDRHALGGGGALEIEKTPEAAEDMESEPALAAAREAERVPPWREQVTARGMVAALLIGVVYTVIVMKLSLTTGLIPTLNVSAALLAFLALRGWTHALDRLGIASRPFTRQENTVIQTCAVACYTIGYGGGFGSFLLGLNKKTYELSGASTPGNVPGSYKEPGIGWMTGFLLSTSFVGLLTLLPLRKVLVIDYKLTYPSGTATAVLINGFHTPQGDKNAKKQVRGFLRYFGISFLWSFFQWFYTGGDVCGFLQFPTFGLKAWKHTFFFDFSLTYVGAGMICSHLVNLSLLFGAILSWGIMWPLIGKQKGNWYSAKASESSMSGLFGYKSFICIALLVGDGFYNFVKVIVVTLKSVRERSRRRGLNNRVADADTMAIDDMQRNEVFNRDNIPTWMAYTGYTLLSVIAVVLIPVMFRQVKWYYVIIAYLLAPALGFCNAYGTGLTDMNMGYNYGKIALFIFAAWAGKDDGVVAGLVGCGLVKQLVLISADLMHDFKTGHLTLTSPRSMLVGQVVGTLMGCVVAPLTFFLFYKAFDVGDPNGYWKAPYALIYRNMAIIGVEGFSALPRHCLQLCAGFFAFAVLANLARDFLPRRYGRYMPLPMAMAVPFLVGASFAIDMCAGSLVVFLWHRFDGKRAALLVPAVASGLICGDGIWTFPSSLLALAKVKPPICMKFIPGN", "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": "MTTPASPTTGVQLLDVPPELAGQRIDNFLIARLKGAPKTLIYRILRKGEVRVNKGRIKPDYRLQAGDQVRVPPLRLAERDEPAPLAQGLLERMEAAIVYEDKALIVVNKPAGIAVHGGSGVSAGVIEVFRQLRPDAKDIELVHRLDRDTSGLLMIAKKRSMLRHLHEALRGEKIVDKRYHALVRGHWPAGKKNVRAPLLKNNLRSGERMVEVNVEGKDALTEFRVLRRFGDFATLVEARPITGRTHQIRVHAKHAGHAIAGDPKYGDEDFSREIRELGGKRLFLHAAQLRVPLPDGQVLELEAPVDEMWQRSLERLND", "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": "MKTLLVLALLLLSVSVQAKVYDRCEFARILKKSGMDGYRGVSLANWVCLAKWESNFNTKATNYNPGSQSTDYGIFQINSRYWCNDGKTPKAVNACHISCKVLLDDDLSQDIECAKRVVRDPQGIKAWVAWKAHCQNKDVSQYIRGCKL", "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": "MNGSWITILSLLVISQLASSKVTLIGKNTFLSFDDVEANFTPVVRRSGEYGLLYAAEPLDACSYLTNMAEKGSKFRPSYVLIVRGGCSFEEKIRNAQEAGYKAAIVYNDRYEELLVRMAGNSSGVYIHGVLVTRTSGEVLKEYTSRAEMELLLIPGFGISSWSIMAITFVSLLVISAVLASYFSVRRHRIRQHVRDLHHGGQGHSRMPKDLLQSMPTEVYTGVLEEGSTSVTCAICIDDYRVGEILRILPCKHKYHAVCIDSWLGRCRSFCPVCKQNPRTGNDVPPASETTPLISPGPNSITSLQSFYDLPIVVRVYL", "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": "MLLWFLSGSLLLFGTFDVWYFLRGLWVALRCCFQSPIRDVLAEQVVHGRVLLHDMDFMCHMNNARYLRECDFARFAHGTRIGLFMAARALKATMVVGATTIRYRRSLALGEGFELRTRIVSWDEKSFYLEQRFVSKSDGFISAVMLCRQNVIRGSPQNILEFLCKRKVDCPDISEDLQHWIRFISASSQALRAESGLDDKTK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the THEM6 family."}
+{"protein": "MAKKESFFKGVKSEMEKTSWPTKEELFKYTIIVVSTVIFFLVFFYALDIGINALKQLFLG", "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": "MTRSIFIHTLLALSALTSVHGANSPGCGKNPTLANGVHQINGREYTLKIPDDYDANNPYHLIFGLHWRGGNMDNVVSGDSIQPWYGLESRAQGSAIFIAPNGLNAGWANTNGEDVAFIDAIMEQVESDLCVDQSSRFATGFSWGGGMSYSLACSRAKEFRAVSVLSGGVISGCDGGNDPIAYLGIHGINDPVLPFDGGVELAERFVGNNGCQPASIEKPQSGSNGWKRTDFYGCSKPVSFIAYDGGHDGAPLGVQSSLAPDATWEFFMAA", "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": "MAGPGYDRVDSKDDEPPNIQIPSRTYGFPPEAFDWSRLPDFDTNFLPPEHVEAFIQALSAPDPIPPTPDGGATGSSSYRLNSPAWHRGSTTSFDLDLARRPESSGVGFHDEDRTARDSPAGAATAAAAGVATPGPPLSRRASSNSLFISARNDWAPISQRRVARAKTAPQSSSRNDKKKKRARSKDETREGYLYPLLKWPLLGVVTCWLVGLSVVHVLARLYITVYERYWAWRGERGRLRRAMRATARYSDWVAAARRMDDFLGNDSWKVDDAFAYYDNKTVRRVLAEMRRSRRRAEEAGGRDTEQGREAIEDLKVLIEACVKNNFAGIENPRLYSQTYYGTKNLVQNFIDEVERSLKFLVETERLSKEEKRVMFKGICANYGRTALCLSGGATFAYYHFGVVKALLEEDYLPDIITGTSGGALVAALVATRTNEELKELLIPALACRITACREPISVWFRRWWATGARFDSVDWARQCAWWTRGSLTFREAYERTGRILNVSCVPADQHSPTILCNYLTSPDCVIWSAVLASAAVPGILNPVVLLMKTRSGQLLPYSFGHKWKDGSLRTDIPIKALNLQFNVNFTIVSQVNPHINLFFFSSRGSVGQPVTHRRGRGWRGGYLGTVLVQFTKLDLTKWLRVLRSLELLPRPLGQDWSLLWLQDFGGTVTVWPRCLLSDFARILSDPDPARLARMIHEGQQSAFPKLRFVANRLRVERLVERGRRENRRGGGLGDGGVGSSGGAGGGAGGGQAEAVAGQAAGPGTGQRRPSFESILSEDDLRSLLKKRRVERGGIGSGETESEDETSDLDADFYEGITYDGGDDDAGLEFGAAGMRQPGVATPAGLGGVERGDLS", "text": "FUNCTION: Probable lipid hydrolase. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PLPL family."}
+{"protein": "MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPGEEDQAVSVSFGDPEGSSLQEESLRDLVCYCRKRGCKRREHMNGTCRKGHLLYMLCCR", "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": "MNIEELPLPSLLRDFLISKRGIRTLYPPQEEAIRAGLLNGENILMVSATASGKTLLAEVAAVNNVLVNDKKSLVAVPLKALAFEKLNDFNTYSELGIRVAASTGDYNSEDKWLGSYDVIITTYEKLDSLLRLKPSWIWNVGQLIIDEIHFINDDERGPIIESIVAKLRMLNLNPQIIGLSATIGNPEELANWLNAKLVKSDWRPVSLREGVYHKGVVTYVNDGEKRISGQGDSLINLTVDTLNDGGQVLVFSSSRQGAVRIARKLAEYICSSPVRYIDPGEAGKLAEEVRETSSSRILAEELTGLIKCGVSFHHAGLELEVRRVIEEGFRRGVLRVLASTTTLAAGVNLPARRVIVNEYRRYEPGYGFIEIPVMEYKQMAGRAGRPGLDPYGEAIIIVSSKDEVDYVIDKYIKSPPEYVKSNFMNPTSLKFHTLSAVASQYAETIDELVKFTSNTFAGFQGKLSAMIQANSVRRMISRIIDELVDYGFIIRNGDKLEATEVGAVVNRMYLDPDTAHVFIMGLRNLNSDADLNAYSLMLVVKSPKIPKVKVRRNELDELAQQAASMWSSIPLKPSDVDELVNYPEDYEDFLSEFKTAMALLEWINESNEDQIMKTYDVQPGDLRVLSDQAEWLIGALQELARTLGLSGNVVNGLRALRYRVKYGVNDELLELVVNLEGVGRVRARALYAAGYRSIEDLAKANVSDLTRIRGIGDKIAGSIIEQAHQLVKDGRVIKFNESTVKGKTRRGGGGLLDHMY", "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": "MKVIKTLSIINFFIFVTFNIKNESKYSNTFINNAYNMSIRRSMAESNPSTGAGGSGSAGGSGSAGGSGSAGGSGSAGGSGSAGSGDGNGANPGADAERSPSTPATTTTTTTTNDAEASTSTSSENPNHNNAETNPKGKGEVQKPNQANKETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPIAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAAPSLLSNSSNIASINKFVVLISATLVLSFAIFI", "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": "MGNISASITSQSKMGKDFDAVGFVKDFAAGGISAAVSKTAVAPIERVKLLLQVQHISKQISPDKQYKGMVDCFIRIPKEQGFSSFWRGNLANVIRYFPTQALNFAFKDKYKQVFLGGVDKNTQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADTGKGGQREFTGLGNCLTKIFKSDGIVGLYRGFGVSVQGIIIYRAAYFGFYDTARGMLPDPKNTPIYISWAIAQVVTTVAGIVSYPFDTVRRRMMMQSGRKATEVIYKNTLHCWATIAKQEGTGAFFKGAFSNILRGTGGAFVLVLYDEIKKVL", "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": "MSTTTTQIQPKPIPALYTVYILRSQPRHASLYIGSTPHPPRRLSQHNGLAKGGAYRTSKISLRPWNMVCLVSGFPSMIAALKFEWALNNPHKSLHIPAEKRAEAVKGLGRRKTGHLKRPRKSLVGVMEALRMLVGVRSFGRWPLRVHFFEEDVWRVWERGGWKAKSGGGGVGELGDLKVEVVTDFGSPTAPQGAGVIGMGEEAENDPHDDDDGDDAQDENKHGIYALPLDYAPIKDYVAKSQEIWEFERQGSCVVCKEAMVAGRGLYAICPNTSCEAVGHLDCWSRCLLKQETRRMKIDEGDEILPVKGECPKCHGEVLWGDMMKELTLRIRGQAEVEKLLKKKKRRRAAKGKEKGKGKVADEKGNNAEGRNTKGNREVKTTPQRVVEDSEDSEFLDIACLQ", "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": "MWLLFRSKHKKLVLRCFPSGKLGETEPNGSPLAYLSYYAASNSSKLRKVAHFLGSRVRHSYYHKRDNEVIIGLKICKTLVQKCRDNINVMASEVVNMLLVASSSKNLEVLSACVDCFATFCDNSGKGSPATFGNEFHSAFNNLVNSFFELSKGIDCVDPQQSKMLGLKAFHALTACKFAGTEGGMRYQPHFAIHCVLINSWSESDQEKKSFIDLVRSTAKSYKPLPPSSTGVSLPEHDEAGDNIDVAIKKLCIRILFNIYTQTDPLFMAESTKSLIHFFAAKSDTPVNLEYISVVLNQILDWTPVELRHSIFFCCLRCLSSSRIVNSETNVMVPYMIYSILNSKNSISGLSVIDVLRDLGSHLINAVNSFDADDQTWYNMCESPSEKLPRRLYLLLVCITCLTKHQYYDEEFADVWREIDTLANSETSSAIQMVALTAFHKLQNEKLNTKKESSAPLSLVTDFLLHSWPKSAERLHTSQSPFVRIKTAEVFYEFLCFLRPSLINFDTILRKSAITSFSVLWDFIYETSWHIERWLKVFSVQSEFYILKLIIQRLYQLYGPVSVTAVLPAMYRGLRPFENDPPRCIAEAVTAYYIIYIGENLKITTLQSSGRKWLDSLSSSLPSSLLNRGSSTHSWEKLTNASTEEVMLPLDMVVNELLEKSPKVFPEDSRLLFAEQSRHPKYTDIIQKLKKPSREKSFTSSSEYSLPFISPASDYQQNPLLHATKSLVSIHQQSQRGEMVSTLKQALSRPHTASTVVRSPSEINLTRQTSNRVPLLDMLNLNRAMSPTPIQSPPYVRT", "text": "SIMILARITY: Belongs to the EFR3 family."}
+{"protein": "MKIKKIKLLKALALTGAFGIVATVPVIVSSCSSTDNNGGTGDNNTGGGGSGTDQQQGTTYTPAIKSDVTLSGALSKIYDTTNTGDSRKNTNTLIAEDIKANPENYFTNGEDLKKVEGWSVTVDGSFDSNSVWTGDAYSKWSAVADTHKGVYKSTSKQLNINSLKDLKSQLDTSAKIKAICDESNLVFSTADADSYKIQNELGFTGGDLLHINVTATQAGKTLNMDLGIPVSDLNLKITDLKVSVTASNNSTGNNVAAVSDLTTNFTYNIGIKEEVTAPTEKPNLAKTDKGEVMKVLKALGYTQTGDETKLDNDKVSNSLGLYNCEFTAVSATPVEGSEDKFTIKLKAKPLTDYVWEDGTNTEKEISFEATFTMTGN", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the p35 lipoprotein family."}
+{"protein": "MAASLWMGDLEPYMDENFISRAFATMGETVMSVKIIRNRLTGIPAGYCFVEFADLATAEKCLHKINGKPLPGATPAKRFKLNYATYGKQPDNSPEYSLFVGDLTPDVDDGMLYEFFVKVYPSCRGGKVVLDQTGVSKGYGFVKFTDELEQKRALTECQGAVGLGSKPVRLSVAIPKASRVKPVEYSQMYSYSYNQYYQQYQNYYAQWGYDQNTGSYSYSYPQYGYTQSTMQTYEEVGDDALEDPMPQLDVTEANKEFMEQSEELYDALMDCHWQPLDTVSSEIPAMM", "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": "MEERPERLISEDGLRLDGRKPDEMRPLKIQAGVLKRADGSAYLELGANKIVAAVYGPRELHPRHKQKPDRAVVRFRYNMAPFSVDERKRPGPDRRSIEISKLSKEALEPAIFTEYYPRTAIDIFVEVLQADAGTRCAGISAASVALADAGIEMRDLVAACAAGKVEGKVVLDPMYYEDGYGEADVPLAMMPKEGKITLLQMDGDMTPGEFKQAVKLAKKGCKIVYKEQRRALKEKYGGD", "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": "MAAGRGRGGSRPFSVRGGRGRGQKGGRGSRRPTFEASRVAEAHHEDSSEDGSVHLGSDLDAEDQLEAPDESSSSSSDDEEDENRTEKPYNTLLQLLNTGQGVGGPARKRRKMDHNSKKVDVEVKGSDESDAEGLLLESEGEESSEGEEMEDMPMDEVRTENSGDENDASDPFEIHFSNVDSTLLSQKIKAISSKGWQSHKSELPGKLRLMASQPNTEGHIIQVLPATQGVDNLKLKQKLAKHAGDHISKLDSLASSLVPYIFGYQDLLFGARTLSNSATFRDLYCLHVLNHILKTRDRVLKNNSRLQKEPESDLELRDQGFTRPKVLIILPTRQACVRVMESITKLYQAEQQENKARFYETFSAADDKSWEHKPDDFRELFGGNDDDMFRLGLKFTRKTIKYFSQFYNSDIILASPLGLRMVMDKEDGEKQDFDFLSSIEIAIVDQADALLMQNWEHTEYVFSHLNLQPKESHGCDFSRVRNWYLDDQAKYVRQTLTFSSFITPEINALFSSRMQNTAGKIKATPTYEGAILDIPLPVPVKQTFSRFNSSSPVKDPENRFKYFTSTVLSSLIRSFTGRGGTPRASGTLIFIPSYLDFVRIRNYLATSSQTEHLSFGAISEYTSVRDVARARTHFFSGRHSVLLYTERTHHFRRYQIRGVKRIIMYGVPENPVFWGEVVGFLGLDPAGAAEAAEGGVRALFSKWDALKMERIVGTKRLGNMLMEKGGDTFSFV", "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": "MKFNFWKGLWKPKSLTPTLSHRLYRRMYTPQPPLNREMTVLDRSKFTVSLNLALAKFPDPKYIAQFAKECKADILQLRSINHVQKTDDNGRAVLLRHDLDLEGGEDVASKVMSQLSPRGKELLTEAQADITKIVKDLDYDFWRADEIFYSVLPVTEKDEIPSGFSMVGHVAHLNLRSEWKDYDRLIGQVILDKNPRVKTVVNKVDSIDTKFRTFKMDVLAGEDNTEVEQHESGCRFQFDFAKVYWNSRLHTEHDRLVSLFRGEASSRERKQQERAKRENHEKSTETAVEPDNTPATAVCDVFAGVGPFAVPSGRTSLFVMANDLNPYSYEALEHNVKLNKVSEYVKCFNLDGAEYVQQSMKLLDEHRRTQPTINPVQVRKRKAGQPVVKQDIPNHYSHYVMNLPDSAIEFLWSFKGLYTTVDGLSQDTPLPHVHVHCFHKWEAGEEEPSKEETKAALLERVYKQIDVRLDPNEVGMHWVRKVSPKKDMFCISFELPKEVAWAPQVNKE", "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": "MPKGEPFKIKMVEPIRLIPREDRERALKEAHYNPFFLRSSDVYIDLLTDSGTGAMSQFQWSAMMLGDESYAGASSYYRLKETVTDITGYEYVIPTHQGRGAEKVAFSQLITRPGMYVLSNMFFDTTRGHVQLAGGRPVDLLIDVPTEEYHPFKGNMDTERLEQFIREHGAENIACIVMTVTNNSAGGQPVSMANIRETYQIARKYGVLVLFDVARYAENCHFIRMREEGYADKHPIDIAREMFSYGDGLMMSAKKDALVNIGGLLAFRDEELFTKVGAAVVPFEGFLTYGGLAGRDLEAMAVGLREALDPDYLAYRVGQVQYLGEMLRNAGIPIQWPVGGHAVFIDAAKFLPHVPWDQFPGHALTLALYLEGGVRTVEVGSLMIGRDPETGENVRGPFEFTRLAIPRRVYTNLHLEDVAETVINAFQKREEIRGVKFAREPKVLRHFTAWFDPA", "text": "SIMILARITY: Belongs to the beta-eliminating lyase family."}
+{"protein": "MLIAVEGIDGAGKTTIAAYIAELLKEKGYKVKVLKEPGDSKFGKKIKSSEERLSPEEELELFLKDREIDARENILPALQSGYAVVMDRYYFSNIAYQSARGIDARLIREMNEKIAPKPDLTILLDVEPEIALERVRKRGKLSPFEKLDYLRKVRKCFLENADETTVVVDASKPLEEVKEEVRKVIESFLNLKKNSN", "text": "SIMILARITY: Belongs to the thymidylate kinase family."}
+{"protein": "MLKIGIVGCGFIGGQICRAIDGGEVSAELYALCDSSESKALELAASLKTCKPSYMKIEELIRGVDLIIESASQNAVRFIVPQALKAGCDVMILSVGALADEELRDTLFGLAKEHNCKLYFPSGAVVGIDGLNSASAAGISSVTLSTRKPPAGLMGAPYVVEHGIELEKLEKKTVLFEGPASEAVKAFPANVNVAATISLAGIGFERTRVKVIADPSLFRNVHEIIVEGEFGKFSTRVENLPSPENPKTSYLAALSAVSTLKKILNPVQIGT", "text": "FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. SIMILARITY: Belongs to the L-aspartate dehydrogenase family."}
+{"protein": "MSTILFYTRALIIGATKSQGVFGKTGTLVANISSNRGIISIVPRTNPPQKLLKMQEEENSLLEEARKVVPALSFGKHKGQAGRVGVIGGSEEYTGAPYFAAISAMKAGADLAHVFCSKSASTVIKSYSPELIVHPLLDVPNAVTLLDEWLPRIHSHVIGPGLGRVDATLNTVKEILIKLKKQEIPIVIDADGLFLITRDPSIIHGYTKAILTPNVVEFQRLSKSMNLNWESKDLNGSIMETVALSKALGGVTIVRKGEVDIVAAGDEVVTMDEIGSPRRCGGQGDLLSGVMALFSYWTHNSTCTPPPTLLAGYAACFLTKRCANQAFQKHGRSTATTDLISEINSVFVNNFENPTDPKS", "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": "MASERLPNRPACLLVASGAAEGVSAQSFLHCFTMASTAFNLQVATPGGKAMEFVDVTESNARWVQDFRLKAYASPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPICAVGHGVAALCCATNEDRSWVFDSYSLTGPSVCELVRAPGFARLPLVVEDFVKDSGACFSASEPDAVHVVLDRHLVTGQNASSTVPAVQNLLFLCGSRK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C56 family."}
+{"protein": "MSKVSRDTLYEAVREVQAGSISKRRKFLETVELQISLKNYDPQKDKRFSGTVRLKTTPRPKFSVCVLGDQQHCDEAKAAEIPHMDIEALKKLNKNKKMVKKLAKKYDAFLASESLIKQIPRILGPGLNKAGKFPSLLTHNENLNTKVDEVKSTIKFQMKKVLCLAVAVGHVRMSEDELVYNIHLAVNFLVSLLKKNWQNVRALYIKSSMGKPQRLY", "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": "MNGTEGPNFYVPFSNKTGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVGLTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGFNFGPIFMTLPAFFAKAAAIYNPVIYIMMNKQFRTCMITTLCCGKNPLGDDEVSASASKTETSQVAPA", "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": "MAIGDRAMFTVLLLFIASISGFSVVRCVTDPSDVQALQVLYTSLNSPSQLTNWKNGGGDPCGESWKGITCEGSAVVTIDISDLGVSGTLGYLLSDLKSLRKLDVSGNSIHDTLPYQLPPNLTSLNLARNNLSGNLPYSISAMGSLSYMNVSGNSLTMSIGDIFADHKSLATLDLSHNNFSGDLPSSLSTVSTLSVLYVQNNQLTGSIDVLSGLPLKTLNVANNHFNGSIPKELSSIQTLIYDGNSFDNVPASPQPERPGKKETPSGSKKPKIGSEEKSSDSGKGLSGGVVTGIVFGSLFVAGIIALVLYLCLHKKKRKVRGSTRASQRSLPLSGTPEVQEQRVKSVASVADLKSSPAEKVTVDRVMKNGSISRIRSPITASQYTVSSLQVATNSFSQENIIGEGSLGRVYRAEFPNGKIMAIKKIDNAALSLQEEDNFLEAVSNMSRLRHPNIVPLAGYCTEHGQRLLVYEYVGNGNLDDTLHTNDDRSMNLTWNARVKVALGTAKALEYLHEVCLPSIVHRNFKSANILLDEELNPHLSDSGLAALTPNTERQVSTQVVGSFGYSAPEFALSGIYTVKSDVYTFGVVMLELLTGRKPLDSSRTRAEQSLVRWATPQLHDIDALSKMVDPSLNGMYPAKSLSRFADIIALCIQPEPEFRPPMSEVVQQLVRLVQRASVVKRRSSDDTGFSYRTPEHEHVDISF", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MARVKRGVIARKRHKKILKLAKGYYGARSRVFRVAKQAVIKAGQYAYRDRRQKKRQFRALWIARINAGARNNGLSYSRLIAGLKKASIEIDRKVLADLAVNEKAAFAAIVEKAKATLA", "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": "MGGRRRKKRTNDTKHVRFAAAVEVWEADDIERKGPWEQVAVDRFRFQRRIASVEELLSTVLLRQKKLLEQQ", "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": "MSVSVCPCGSGNLLDACCGHYHAGTPAPDAQALMRSRYSAYVLGLIDYLVATTLPAQQAGLDRNAIAAWSAQSTWLGLEVENAEVLGGQPEHAFVTFTARWHDLEGDHQHRERSAFVQHDGRWYFIDPTVELKAGRNDPCPCNSGQKFKKCCASYWGNRA", "text": "SIMILARITY: Belongs to the UPF0225 family."}
+{"protein": "MDKILEAVVTSSYPVSVKQGLVRRVLEAARQPLEREQCLALLALGARLYVGGAEELPRRVGCQLLHVAGRHHPDVFAEFFSARRVLRLLQGGAGPPGPRALACVQLGLQLLPEGPAADEVFALLRREVLRTVCERPGPAACAQVARLLARHPRCVPDGPHRLLFCQQLVRCLGRFRCPAEGEEGAVEFLEQAQQVSGLLAQLWRAQPAAILPCLKELFAVISCAEEEPPSSALASVVQHLPLELMDGVVRNLSNDDSVTDSQMLTAISRMIDWVSWPLGKNIDKWIIALLKGLAAVKKFSILIEVSLTKIEKVFSKLLYPIVRGAALSVLKYMLLTFQHSHEAFHLLLPHIPPMVASLVKEDSNSGTSCLEQLAELVHCMVFRFPGFPDLYEPVMEAIKDLHVPNEDRIKQLLGQDAWTSQKSELAGFYPRLMAKSDTGKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQPLMTKLQWLFGFLEHSQRPAISPENFLSASWTPWFSPGTQQDCSEYLKYLLDRLHEEEKTGTRICQKLKQSSSPSPPEEPPAPSSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLAFPPPERCRRRRLGSVMRPTEDITARELPPPTSAQGPGRVGPRRQRKHCITEDTPPTSLYIEGLDSKEAGGQSSQEERIEREEEGKEERTEKEEVGEEEESTRGEGEREKEEEVEEEEEKVEKETEKEAEQEKEEDSLGAGTHPDAAIPSGERTCGSEGSRSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLPLAGGRGQAYDLCSVVVHSGVSSESGHYYCYAREGAARPAASLGTADRPEPENQWYLFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYRQRPREGPEAELGSSRVRTEPTLHKDLMEAISKDNILYLQEQEKEARSRAAYISALPTSPHWGRGFDEDKDEDEGSPGGCNPAGGNGGDFHRLVF", "text": "SIMILARITY: Belongs to the peptidase C19 family."}
+{"protein": "MWNPEAYLSFADHRGRPFFDLLARVGADAPRRVVDLGCGPGNLTVVLRHRWPEAVVEAWDNSPEMVAAARERGVQANLGDVRGWSPQPDTDVVLSNATLQWVPEHPELLTRWAGALAAGSWLAMQVPGNFDAPSHQAVRRLADREPWAPLLHDIPFRVGKVVETPADYAALLTDAGCSVDAWETTYIHELTDAHPVLEWITGTALRPVRSRLTDEQWDRFRAELIPLLDEAYPVRADGRTFFPFRRVFVVARTG", "text": "FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. Tam family."}
+{"protein": "MKAFSCLLAVIATAASLFQHVDASHARDKLNNISRVERPVIHTPSRRVHAHSHFDLTFDLYPRRNRIKLQLEPNHDVLSHNARVTFLDTEGNVDRIERIERRDHSVFKGWAWTQAKSGVWERVGWARIIMHRDGEDPLFEGVFTVMHDHHQVIAKSKYVRKRHQQDPPLDNTPGEYMLLFRGSDIAQTQSTGNVERSIMSSPSCDADTLAYDSNSNFMFPPLPEENNTSIWNYFMTSIGKRQMTDTGGVVPGSRDLKETIGSTSGCPNTRKVALIGVVADCTYTNTFASEMDARADIISVVNAASVVYEHSFNISLTLGEINILPKNCPATASSATPFNQQCDDRAGGGSFTLADRLNTFSAWRGKKTDDFAFWTLMTDCTTENQVGLAWAAQLCVKGVQGNPDSRNSSSQAVAGANVVSKTDNTWQVFAHEAGHIFGAVHDCDSMLCQNPANPDNSRCCPATASTCDARGRFMMNPTSGSQITNFSPCSIGQICSRMARRTILTNCLTTNRGVDTISGQQCGNGIVEDGEDCDCGDEESCKGNTCCDPKTCKYTSGSQCDDANEECCKGCKFASSSTICRTSSGPCDPEEKCSGNSGDCPHDIHSKDGGTCGTDLQCASGQCTSRDLQCQMHLGNQVAGSRTVAFDSYGCEVACKDPDRPNVRYEGSLTFLDGTPCGGGGTCKNGQCSGSTFGNEVSDWVSRHKPIVIGVAVGAGCLLLLAIASCICGRSRRQRPRNRKMPPINMRPMAPAYNGWNGAPPNAQQSSPGGHPPYNNIPPPINAPPPAYPGHMPPTRYA", "text": "FUNCTION: Probable zinc protease. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MPIGKLRRSKAISFRGPASPSLKFKSFETLQGKPLGEMGQNGHKQEEDMAAQRPHFPAEAGAEQEMKCHVAETPAQNSQVPSTTMENGFYSFANISDNTTNKNTNRYSYLSDNTACQLLAPATGTDYYKSLTPTMKPITERQNHAGTTMSLDTIPTAENISFQITLPTVPPSVISSRSSLINRQRSLSMRYSSPSSMSSLGSTPTKLTTLKRSNAIRCKGGLLQFFSQYAVKTGKKLVKWKIALRKRLFKFQRRSTKNKKNSSPTTSHLKRVNGYVSNVRRSFSTQSRLALVPEIVRRTPSRRHLTANTGMKDATPASPSRTSIRRTPSSIKRAASTLSSNYVYRDGSDTSSQAPELKSTGSSLAPAPSQMVRSTALTSLNSIVRQPSIVVNNKVIPLSRFPGEKMQLPIREEDEEEEEPSTKTDDYVIDTSKRMSTIGEIQASRISSSSGSISSHSSSIQSSHFDDASNSCPLNDSIESDSDIECTRTAWNHFLRTVIAERIRMRLQLAKLQELALLKDDSLDILYAVLRKTLDEPADKSSSTYDPDIMPENNSETGLGNGFRSSDQLSRLKEGSRKRNTSSSTMLALPEALATVRRSITMPVGLNYI", "text": "SUBCELLULAR LOCATION: Bud neck. SIMILARITY: Belongs to the AIM44 family."}
+{"protein": "MAMASAACSCTDGTWWVYALPALLGSDTLCAHPALLAGLIFLATVSVALLAWATSPGGPAWTNGRGASASLLSWDPVVCPCSAASSRCPGAAAPRPRRDGPRRRPRAKELMAFSVGDTPAVVSSCPATAREVLAHPSFADRPVKRSARELMFARAIGFAPNGEYWRRLRRVASTHLFSPRRVASHEPGRQGDAEAMLRSIAAEQSASGAVALRPHLQAAALNNIMGSVFGTRYDVTSGAGAAEAEHLKSMVREGFELLGAFNWSDHLPWLAHLYDPSNVTRRCAALVPRVQTFVRGVIDEHRRRRQNSAALNDNADFVDVLLSLEGDEKLGDDDMVAILWEMVFRGTDTTALLTEWCMAELVRHPAVQARVRAEVDAAVGAGGCPTDADVARMPYLQAVVKETLRAHPPGPLLSWARLATADVPLCNGMVVPAGTTAMVNMWAITHDAAVWADPDAFAPERFLPSEGGADVDVRGVDLRLAPFGAGRRVCPGKNLGLTTVGLWVARLVHAFQWALPDGAAAVCLDEVLKLSLEMKTPLVAAAIPRTA", "text": "SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MDRETILNAVKEARKNAKPRNFNQSVDLIVNLKELDFSRPENRIKQNVILPHGRGKESKIAVIAKGDLAAQADEMGLTVIRQEELEELGKNKKNAKKLANENDFFIAQADMMPLVGKTLGPVLGPRGKMPQPVPANANLKPLVERFKKTVSINTRDKPSFKVLAGTEKLNDEELAENIDAILSTVARQYEKGLYHVKNAYTKLTMGPSVPIKE", "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": "MDNRGSSQKGSLLLLLLLVSNLFLCKSVASLPICPSGAVNCQVSLRDLFDRAVILSHYIHNLSSEMFNEFDKRYAQGRGFITKAINSCHTSSLSTPEDKEQAQQIHHEVLLNLILRVLRSWNDPLYHLVTEVRGMQEAPDAILSRAIEIEEQNKRLLEGMEKIVGQVHPGIKENEVYSVWSGLPSLQMADEDTRLFAFYNLLHCLRRDSHKIDNYLKLLKCRIIYDSNC", "text": "FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
+{"protein": "MIIYINDKPCNAKVGDLLLNTAKLNKAHIGYICGGNGICQSCFVYVLEGAECLSEPGEDEKAFISDKLFAEGGRLACRTTIVKEGTIRVLTRAEKFRRIVLGLNVPGFITYAQTIGYNVTNKLPSGVSSIVSRVQSGRLNPVDTIGKIASGLSPASQLVYNNFIEAFPFMQAPVNMVSGVAKSAIDNASGALCTISGGRLHLPGSTCTAHDKPAEAIERITISAK", "text": "FUNCTION: Could play a direct role in the oxidation or reduction of the quenching species formed in the chlorosome. SUBCELLULAR LOCATION: Chlorosome."}
+{"protein": "MALQIPSLLLSAAVVVLMVLSSPGTEGGDSERHFVFQFKGECYFTNGTQRIRSVDRYIYNREEYLRFDSDVGEYRAVTELGRPDAEYYNKQYLEQTRAELDTVCRHNYEGVETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLISNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class II family."}
+{"protein": "MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHRFLVALYDPDRFLCSGILLNEEWVLTAAHCDRRNIRIKLGMHSKTVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVSNSEHIAPLSLPSSPPSVGSVCRIMGWGRISPSKETYPDVPHCANINLLDYEVCLAAYPEFGLPATSKTLCAGILEGGKDTCVGDSGGPLICNGQFQGILSWGNDVCGYILQPALYTRVFDHLDWIQSIIAGNTDVTCPP", "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": "MTDTTGNPLLSLDDIHFTYPGTTAPVLRGATLHLAQGDRLGLLGHNGSGKTTLLHIAMGLLRPESGTVHHRNAVAHDEASLAALRRDIGFLFQNADDQLFCPTVLEDVAFGPLNLGLSPEQARERATQTLQGLGLEGFGARVTHRLSGGEKKMVALASVLSMQPTALLLDEPTNDLDPATRQRLIDVLNRMSATHIIISHDWDFLARTCTTFLTVDDGIVCTSRHTPHVHTHIHHGGEVAHEHPSRGCCHQHDGSHHHAGHDDDHPHTSQTTE", "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": "MKNLVILSGAGISAESGIKTFRDAGGLWEGHDIMEVASPYGWKKNPQKVLDFYNQRRRQLFEVYPNKAHKALAELEKHYQVNIITQNVDDLHERAGSSRILHLHGELLSVRSEKDPNLVYRWEKDLNLGDLAQDKAQLRPDIVWFGEEVPLLKEAVSLVKQVHLLIIIGTSLQVYPAASLYTHANKDALIYYIDPKAKNARLPQNVQCINENAVHAMQDLMPKLIEMASQEMLK", "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": "MVNSTHRGMHTSLHLWNRSSYRLHSNASESLGKGYSDGGCYEQLFVSPEVFVTLGVISLLENILVIVAIAKNKNLHSPMYFFICSLAVADMLVSVSNGSETIVITLLNSTDTDAQSFTVNIDNVIDSVICSSLLASICSLLSIAVDRYFTIFYALQYHNIMTVKRVGIIISCIWAACTVSGILFIIYSDSSAVIICLITMFFTMLALMASLYVHMFLMARLHIKRIAVLPGTGAIRQGANMKGAITLTILIGVFVVCWAPFFLHLIFYISCPQNPYCVCFMSHFNLYLILIMCNSIIDPLIYALRSQELRKTFKEIICCYPLGGLCDLSSRY", "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": "MEYMAESTDRSPGHILCCECGVPISPNPANICVACLRSKVDISQGIPKQVSISFCKQCQRYFQPPGTWIQCALESRELLALCLKKIKAPLSKVRLVDAGFVWTEPHSKRLKVKLTIQKEVMNGAILQQVFVVDYVVQSQMCGDCHRVEAKDFWKAVIQVRQKTLHKKTFYYLEQLILKYGMHQNTLRIKEIHDGLDFYYSSKQHAQKMVEFLQCTVPCRYKASQRLISQDIHSNTYNYKSTFSVEIVPICKDNVVCLSPKLAQSLGNMNQICVCIRVTSAIHLIDPNTLQVADIDGSTFWSHPFNSLCHPKQLEEFIVMECSIVQDIKRAAGAGMISKKHTLGEVWVQKTSEMNTDKQYFCRTHLGHLLNPGDLVLGFDLANCNLNDEHVNKMNSDRVPDVVLIKKSYDRTKRQRRRNWKLKELARERENMDTDDERQYQDFLEDLEEDEAIRKNVNIYRDSAIPVESDTDDEGAPRISLAEMLEDLHISQDATGEEGASMLT", "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": "MGSRNSSSAGSGSGDPSEGLPRRGAGLRRSEEEEEEDEDVDLAQVLAYLLRRGQVRLVQGGGAANLQFIQALLDSEEENDRAWDGRLGDRYNPPVDATPDTRELEFNEIKTQVELATGQLGLRRAAQKHSFPRMLHQRERGLCHRGSFSLGEQSRVISHFLPNDLGFTDSYSQKAFCGIYSKDGQIFMSACQDQTIRLYDCRYGRFRKFKSIKARDVGWSVLDVAFTPDGNHFLYSSWSDYIHICNIYGEGDTHTALDLRPDERRFAVFSIAVSSDGREVLGGANDGCLYVFDREQNRRTLQIESHEDDVNAVAFADISSQILFSGGDDAICKVWDRRTMREDDPKPVGALAGHQDGITFIDSKGDARYLISNSKDQTIKLWDIRRFSSREGMEASRQAATQQNWDYRWQQVPKKAWRKLKLPGDSSLMTYRGHGVLHTLIRCRFSPIHSTGQQFIYSGCSTGKVVVYDLLSGHIVKKLTNHKACVRDVSWHPFEEKIVSSSWDGNLRLWQYRQAEYFQDDMPESEECASAPAPVPQSSTPFSSPQ", "text": "FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex."}
+{"protein": "MEPGRNQLFVVILLTSACLVYCSQYVTVFYGIPAWKNASIPLFCATKNRDTWGTIQCLPDNDDYQEIILNVTEAFDAWNNTVTEQAVEDVWHLFETSIKPCVKLTPLCVAMNCSRVQGNTTTPNPRTSSSTTSRPPTSAASIINETSNCIENNTCAGLGYEEMMQCEFNMKGLEQDKKRRYKDTWYLEDVVCDNTTAGTCYMRHCNTSIIKESCDKHYWDAMRFRYCAPPGFALLRCNDTNYSGFEPKCTKVVAASCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMRCKRPGNKTVLPITLMSGLVFHSQPINTRPRQAWCRFGGRWREAMQEVKQTLVQHPRYKGINDTGKINFTKPGAGSDPEVAFMWTNCRGEFLYCNMTWFLNWVEDKNQTRRNYCHIKQIINTWHKVGKNVYLPPREGELACESTVTSIIANIDIDKNRTHTNITFSAEVAELYRLELGDYKLIEITPIGFAPTDQRRYSSTPVRNKRGVFVLGFLGFLATAGSAMGARSLTLSAQSRTLLAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLKHQAQLNSWGCAFRQVCHTTVPWVNDSLSPDWKNMTWQEWEKQVRYLEANISQSLEEAQIQQEKNMYELQKLNSWDILGNWFDLTSWVKYIQYGVHIVVGIIALRIAIYVVQLLSRFRKGYRPVFSSPPGYLQQIHIHKDRGQPANEGTEEDVGGDSGYDLWPWPINYVQFLIHLLTRLLIGLYNICRDLLSKNSPTRRLISQSLTAIRDWLRLKAAQLQYGCEWIQEAFQAFARTTRETLAGAWGWLWEAARRIGRGILAVPRRIRQGAELALL", "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": "MEGEQQQQQQQSVAAVRPSLGKAPSPSFRLRNGSLNAVRLRRVFDLFDRNGDGEITVDELAQALDALGLEADRAGLAATVGAHVPDGAAGLRFEDFESLHRALGDALFGSLDVPEDGGGGGGGDEEMKEAFKVFDVDGDGFISASELQEVLKKLGMPEAGSLANVREMICNVDRDSDGRVDFGEFKCMMQGITVFGA", "text": "FUNCTION: Potential calcium sensor."}
+{"protein": "MFKREEIIEMANKDFEKAWIETKDLIKAKKVNESYPRIKPAFGKTHPVNDTIENLRQAYLRMGFEEYINPVIVDERDIYKQFGPEAMAVLDRCFYLAGLPRPDVGLSDEKISQIEKLGIKVSEHKESLQKILHGYKKGTLDGDDLVLEISNALEISSEMGLKILEEVFPEFKDLTAVSSKLTLRSHMTSGWFLTVSDLMNKKPLPFKLFSIDRCFRREQKEDKSHLMTYHSASCAIAGEGVDINDGKAIAEGLLSQFGFTNFKFIPDEKKSKYYTPETQTEVYAYHPKLKEWLEVATFGVYSPVALSKYGIDVPVMNLGLGVERLAMISGNFADVREMVYPQFYEHKLSDRAVASMVKLDKVPVMDEIYDLTKELIDSCVKNKDLKSPCELTIEKTFSFGKTKKNVKINIFEKEEGKNLLGPSILNEIYVYDGNVIGIPESFDGVKEEFKDFLEKGKAEGVPTGIRYIDALCFKITSKLEEAFVSNTTEFKVKVPIVRSLSDINLKIDDIALKQIMSKTKVIDVRGPVFLNVEVKIE", "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": "MKLTCVVIVAVLFLTAWTLVMADDSNNGLANLFSKSRDEMEDPEAAKLEKNYCQEKWDYCPVPFLGSRYCCDGLFCTLFFCA", "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": "MMRARVPLLLLGILFLASLSASFAISLREHNESQDNPFYFSSDNSWQTLFKNQYGHIRVLQSFDQHSERLQNLEDYRLVEFMSKPETLLLPQQADAEFLLVVRSGSALLALVKPGGTIIYSLKQQDTLKIPAGTIFFLINPQNNEDLRIIKLAMTVNNPQIQDFFLSSTEAQQSYLYGFRKDILDASFNSPIEEINRLLFAEEGRQEGVIVNIGSDLIQELSRHAKSSSRKSLDHNSLDISNEWGNLTDIVYNSLDVLLTYVEIKEGGLFVPHYNSKAIVILVVEEGVAKVELVGPKREKESLELETYRADVSEGDVFVIPAAYPVAIKAISNVNFTSFGINANNNYRILLTGKGGPTGKEDNIISAGINPDVLGLMFPGSGEDVQKLFNNQNLSHFVNGSYHKNAQPQPHEQEQQKQQKGRKGAFVY", "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": "MPGGRASSSYGLSVTDDKDARIWERIKDHPCFSEQAHHYFARMHVAVAPACNIQCNYCNRKYDCTNESRPGVASVKLTPDQALRKVLAVASKVPELSVIGVAGPGDACYDWRKTAATFEGVAREIPDIKLCISTNGLALPDHVDELADMNVDHVTITINMVD", "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": "MAEPLFLQSQMHKKIWGGNRLRKEFGYDIPSETTGEYWAISAHPNGVSVVKNGVYKGVPLDELYAEHRELFGNSKSSVFPLLTKILDANDWLSVQVHPDNAYALEHEGELGKTECWYVISADEGAEIIYGHEAKSKEELRQMIAAGDWDHLLTKIPVKAGDFFYVPSGTMHAIGKGIMILETQQSSDTTYRVYDFDRKDDQGRKRALHIEQSIDVLTIGKPANATPAWLSLQGLETTVLVSSPFFTVYKWQISGSVKMQQTAPYLLVSVLAGQGRITVGLEQYALRKGDHLILPNTIKSWQFDGDLEIIASHSNEC", "text": "SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family."}
+{"protein": "MIYQSLFSHQASLPSEQLPFTVILLNDWGLIRVTGKDRVKYLQGQITLDVPLLKENQHILGAHCDPKGKILSTVRLFHYLKGLAFITRKSLLHDELMELRKYAVFSKVEIDIAESTVLLGIAGDQARKVLKNCFEKLPTETEPVVHEDDYSLLHFSSPRERFLLVSQAFKEGDFLIQKLQDQAVFRSSEQWLALDIESGFPIIDAKNKTQFIPQAANLKALGGISFTKGCYTGQEVVARTEYRGVNKKALYWLTGKACRVPDVGEALEIQMEEDYRRTGVVLAAVKLQDGSLWVQAILNHDFQKDSILRVKGDENGRLMISHRSFKKFEPSSNPIA", "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": "MACGATLKRSMEFEALMSPQSPKRRRCAPLPGSPATPSPQRCGIRPEIQQGQQQPLGGDLRLTPEQILQNIKQEYTRYQRRRQLEGAFNQGEAGVSNEVQASCSSLTAPSSPGSLVKKDQPTFSLRQVGILCERLLKDHEDKIREEYEQILNIKLAEQYESFVKFTHDQIMRRYGARPTSYVS", "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": "MIASIVFFIVLVDGVATGSPNALVTDFDCRPGMKHCGVCQQLISGSTGANALCSYKGVGDFIVNNFSMGPVDWLWPSTAPSYAVVSESWGCVDDGAAFCDTTGNFRDHRGRVAREGRDGLGTVLIRPAGNGGPIDDCGADGFTQAIGTVVTTVTDYTRSERCAAVLVTVPPPNETVWYDGKCGFIPSSSSAAPPILGNMLLALIRAHPTLTLRMIQRILVRAAKPVTVTGWRGRGWWLNRVTDRWTHRNFGFGEVSPSRLEIEARRELSTSRAPVAWSTLDTCDLSEVEWVRVRLGIAPAVFRGGVTVEISSPSGTIIEILGKRPLDFSRDEFEGEFVTPFWGEPGRGKWTVSCTGGVILTTEGTCHGIR", "text": "SIMILARITY: Belongs to the peptidase S8 family."}
+{"protein": "VDINNGESVFTANCSACHAGGNNVIMPEKTLKKDALEENEMNNIKSITYQVTNGKNAMPAFGGRLSETDIEDVANFVISQSQKGW", "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": "MTNNAAAPLYSLRGLPLIGWRDMSHALNYLFADGQLKQGTLVAINAEKLLTAEDNPEVRALIAAAEFKYADGISVVRSIRKKFPQAQVSRVAGADLWEALMARAGKEGTPVFFVGGKPEVLAQTEAKLRTQWNVNIVGSQDGYFTPEQRQALFARIHASGAKIVTVAMGSPKQELLMRDCREVHPHALYMGVGGTYDVFTGHVKRAPKIWQNLGLEWLYRLLSQPKRITRQMRLLRYLRWHYTGDL", "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": "MKRERFKPPEPDDPLCCCGDIDQQREYCCCDCEELDDACERLLRGEPDKPDVFSRFISRMADRLGVSCCTVGPLRLELSVLPPMVLIPGLLRVAAINCLLGVIILTALPLLVLWYYYMTHRRKRRTLFFLSLALFSLAYMYYLFLTEIVPRGDVTHLQVVTATTGMMLTLISLVRTKQGPGFVKSQSLALGINSSLATNRSTNLTLDTDLRNGVSHLKGEKDVKKKCPVCQLVRPPRAGHCRICGACVLRMDHHCVWINSCVGQANHRQFILTLLLFLLTSFYGISLVLRSICPKQSLFTAMLYCPGVYNQYSTALCFTCVWYSVIITGGLLHLFILQIINVSCNVTEREAQIALRNKTGRRRFCGLVVETGDHSRGFLQNWIQFLTMNMDEIGSSLNLTDMV", "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": "MNNYTIKDITRASGGFAMLAVDQREAMRLMFAAAGAKTPVADSVLTDFKVNAAKILSPYASAVLLDQQFCYRQAVEQNAVAKSCAMIVAADDFIPGNGIPVDNVVLDKKINAQAVKRDGAKALKLLVLWRSDEDAQQRLNMVKEFNELCHSNGLLSIIEPVVRPPRCGDKFDREQAIIDAAKELGDSGADLYKVEMPLYGKGARSDLLTASQRLNGHINMPWVILSSGVDEKLFPRAVRVAMEAGASGFLAGRAVWSSVIGLPDTELMLRDVSAPKLQRLGEIVDEMMAKRR", "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": "MKYPKQIRTYCPYCKRHTIHKVERVKRRPRSELSAGQRRFRRVLKGYGGFPRPKPEGREKPVKKLDLRFVCTVCGRAHTRGKGFRVKRFELVEV", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family."}
+{"protein": "MDPQQKGLVNTCFVTTRIPSWAGARQNVTGSDLEGKPVPSDVLESGRPLAAPRIRTLYEEQQLNMLAVNVLLDELKIQVAAMQNSVTAIQREVNDLKQRIARD", "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": "MESTLGSDLARLVRVWRALIDPRLKPLELTQTHWVTLYNINRLPPEQSQIQLAKAIGIEQPSLVRTLDQLEEKGLITRHTCANDRRAKRIKLTEQSSPIIEQVDGVICSTRKEILGGISSDEIAVLSGLIDKLEKNIIQLQTK", "text": "FUNCTION: Transcription regulator that can specifically activate or repress expression of target genes. SIMILARITY: Belongs to the SlyA family."}
+{"protein": "MEEPQSDLSIELPLSQETFSDLWKLLPPNNVLSTLPSSDSIEELFLSENVTGWLEDSGGALQGVAAAAASTAEDPVTETPAPVASAPATPWPLSSSVPSYKTYQGDYGFRLGFLHSGTAKSVTCTYSPSLNKLFCQLAKTCPVQLWVNSTPPPGTRVRAMAIYKKLQYMTEVVRRCPHHERSSEGDSLAPPQHLIRVEGNLHAEYLDDKQTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDPSGNLLGRNSFEVRICACPGRDRRTEEKNFQKKGEPCPELPPKSAKRALPTNTSSSPPPKKKTLDGEYFTLKIRGHERFKMFQELNEALELKDAQASKGSEDNGAHSSYLKSKKGQSASRLKKLMIKREGPDSD", "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": "MQKIALCITGASGVIYGIKLLQVLEELDFSVDLVISRNAKVVLKEEHSLTFEEVLKGLKNVRIHEENDFTSPLASGSRLVHYRGVYVVPCSTNTLSCIANGINKNLIHRVGEVALKERVPLVLLVREAPYNEIHLENMLKITRMGGVVVPASPAFYHKPQSIDDMINFVVGKLLDVLRIEHNLYKRWRG", "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": "MKLIIFTGLVLFAIVSLIEAQAENEKACLPQYQVCTDAPGNCCSDLVCDCYGRYKSGARIGRNCFCLQKGVIYKRED", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 08 (U8-Lctx) subfamily."}
+{"protein": "MSVLTPLLLRGLTGSARRLPVPCARVHSKPPREQLGTMDIAIGLTSCFVCFLLPSGWVLSHLENYKKRE", "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": "MYFILTKDSFKDSPFLKFITVLLPYLHPPVLHLLLLHTNWRKTHKSKHTILYCLVNLLLLAFAVANILSIVALIVDKQKRTDDLLLHSIILPSFFIPPAYLLSTSCCLVPGQIGFTDTGINVIIDILILICPAISLVLVDEKSKYYPYSTAIPSILILVRLFREKCSPPKQSSPPIPTWRVAAFVFILVLAVLVYGLLGSGSIITLYDHFHPPKGADATSS", "text": "SIMILARITY: Belongs to the UPF0328 family."}
+{"protein": "MRPLMLQGHERSITQIKYNREGDLLFSSSKDQKPNVWYSLNGERLGTYDGHQGAVWCLDVDWESRKLITGAGDMTTKLWDVEYGTVIASIATKSSVRTSNFSFSGNQAAYSTDKAMGQNCELFIIDVRNADSTLSEQEPTLRIPMVESKITSMQWGPLDETIITGHDNGNIAIWDVRKGQKVVDSGVDHAAGINDMQLSKDGTMFVTASKDNTAKLFDAESLMCLKTYKTERPVNSAAISPIFDHVVLGGGQDAMEVTTTSTKAGKFDSRFFHLIYEEEFARLKGHFGPINSLAFHPDGKSYASGGEDGFVRVQSFDSTYFENIFE", "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": "MFSCFNNLGLDYCYQCMHGPEGCMVPSRQGDGGELYAHSEELEAKLRGLAKKESLEIEKSLENDKKTYGSHIKILILGGPSSGKSTIFKQMQIIHSNGFKTEQELIQYRGLIDTNIRQTYRQLVSGARVVGISLESLESLVHDINKVYAPMAADEFSIRTIPDVVEPLTAFWNSREIQEVYKRRYEFELLDSTKYYLENLNRISKSDYLPNEEDIVHSRKATVSINSIVFQYTGVSLLMVDVGGQRSERKKWLHLFDDAKVVIFVIDLTGYAKKSEESRTELSRFPNFFNEIGNDAFDMKVALKIFNDVAGSHALANAVFLLFFNKVDLFKELLPQVSLQPCFSKFAEENSYDNTSKFICDKFIRAAKPKKSVFPHFTTATNTENIKMVFRACMESVFKANSKATGLS", "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": "MDMNFDLYMNGVVEQARNEIESAGYEQLTTAEDVDKVLKQDGTTLVMINSVCGCAGGIARPAASHALHYDVLPDRLVTVFAGQDKEATQRAREYFEGYAPSSPSFALVKDGNITEMIERHQIEGHDVMNVINQLQTLFNKYCEER", "text": "SIMILARITY: Belongs to the UPF0403 family."}
+{"protein": "MANIKSAIKRAELNVKANEKNSAQKSAMRTAIKAFEANPSEELFRAASSSIDKAESKGLIHKNKASRDKARLAAKLG", "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": "MGSNQDDQAFLFAMQLASASVLPMVLKTAIELDLLETIAKAGPHGSVSSSELVAQLPKVNNPEAPVMIDRICSLLASYSVLTCTLKETADGCAERFYGLAPVCKFLIKNDAGVSLAPLLLMNQDKVLMESWYYLKDPVLDGGIPFNKAYGMSAFEYHGKDQRFNKVFNSGMFNHSTMTMKKIVELYNGFSGLKTLVDVGGGTGASLNMITSKHKSLKGINFDLPHVIADATTYQGIEHVGGDMFESVPKGDAIFMKWILHDWSDAHCLQVLKNCYKSLPENGKVIVAECILPEAPDTTPATQNVIHIDVIMLAHNPGGKERTEKEFEALAKGAGFKGFNKAACALNTWVMEFCK", "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": "MAHTTPRSHPPPHSLLQNLTTQSLLLSHLFTLIASPPNPNTSTQTQLNQVYSALQLSTLDLSGLVKEVGHHQEAYRRLVEKKNEVAGLEMRVRGLVKRLEEGRKELEGMIDQGERSLEDIEKSEREPVPAKTLMAHAQSLSKHSSAPVSSLLAPVDKAQYAPWPTEMSMRMGLLFQLEGSMSGMGERGVVGEEQKAPQKVEERREHVEHEESDRRYDPNAVFQLDLNSDESDED", "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": "MWELLVFLLFAVAYFLWPKAKCPGAKYPKSLPSLPLVGSLLFLPRSGHPHKNFFKLQKKYGPIYSFRLGTKTTVMVGDHQLAKEVLVKKGKEFSGRPHVVTLDILSDNQKGIAFADHGASWQMHRKLALATFALFKDGDQRLEKIICREISLLCDNLAMQDGQSIDLYLPLFLAVTNIICLICFNSSFKNGDPALKIIQNYNEGILKTLGKDNLVDIFPVLKIFPNKTLEKMKNYVKNRDELLREILEKHKENFSNDSITNMLDVLIQARMNSDNNGAASDQDSKLLSDKHILTTIGDIFGAGVETTTSVVRWTVAFLLHHPQLYKKLQEEIDQNIGFSRTPTMSDRNQLILLEATIREVLRIRPVAPTLIPHKAIMDSSIGEFAVDKGTNVIINLWALHHNEKEWYRPDQFMPERFLDPTRSQLISPSLSYLPFGAGPRSCLGESLARQEVFLFMAWLLQRFDLEVPDDGQLPHLEGNPTVVFLIAPFKVKVKVRQAWREAQAEGST", "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": "MKHLLSLVCTLGAATLAASAAAEAGSMPSANGLDFVIDGEASYFAGSNAYWLSFLTNNADVDLALDHFAESGLKILRIWGFSDVTAEPSDNKVYFQLHQNGSSTVNTGPNGLERLDYIISGAEKRGIKLVIPLVNYWDDFGGMNAYISAYGGDKPGWYTNDKIQAAYHAYVKAVVSRYVDSPAIFAWELANEPRCSGCDTSIINQWATKTSSFIKSLDPNHMVAMGDEGMGLPGDSNYPYSYYEGNDFALNLAIPDIDFGTLHLYTTDWGVSNNSWGNKWVQDHAAVCKSAGKPCLFEEYGMKGNHCTYELAWQKTALATPGMAADLFWQFGENLSSGQTHNDKYTVYYGSNEWKCVVSDHVAAVAVRRYRLPVGGGQHGP", "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": "MLSKQIPLGIYEKALPAGECWLERLRLAKTLGFDFVEMSVDETDERLSRLDWSREQRLALVNAIVETGVRVPSMCLSAHRRFPLGSEDDAVRAQGLEIMRKAIQFAQDVGIRVIQLAGYDVYYQEANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMNSISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGIGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFETLKQSGYCGPYLIEMWSETAEDPAAEVVKARDWVKARMAKAGTVEAA", "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": "MPKRKSPENAEGKDGAKLTKQEPTRRSARLSAKPVPPKPEPKPRKTSAKKEPGTKINRAAKGKKEEKQEAGKEGTAPSANGDTKAEEVLSTNASH", "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": "MTQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWTGFRARETAALEAVTAPSTVIATGGGIILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQVISEIRSALAQTINC", "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": "MKFLTPLVLSSLASAAALNRRADMCGQWDTTTTDKFTLYNNLWGEGNADSGSQCTGLDSDDGNTIAWHTSWTWTGGAGQVKSFANVAYNFEATQLSQLSSIPSTWKWENTGSDIVADVAYDLFTSSSADGDEEYEIMIWLAALGGAGPISSTGSAIATPTVGGQSWSLYSGPNGQMTVFSFVASSTTEDFSADLNDFLKYLQEEQGMPSSQYLTHVQAGTEPFSGSNVKFTTSSYSVSVA", "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": "MNTVRVTFLLVFVLAVSLGQADKDENRMEMQEKTEQGKSYLDFAENLLLQKLEELEAKLLEEDSEESRNSRQKRCIGEGVPCDENDPRCCSGLVCLKPTLHGIWYKSYYCYRK", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 01 (HNTX-16) subfamily."}
+{"protein": "MGNGVKEGPVRLHEDAEAVLSSSVSSKRDHRQVLSSLLSGALAGALAKTAVAPLDRTKIIFQVSSKRFSAKEAFRVLYYTYLNEGFLSLWRGNSATMVRVVPYAAIQFSAHEEYKRILGSYYGFRGEALPPWPRLFAGALAGTTAASLTYPLDLVRARMAVTPKEMYSNIFHVFIRISREEGLKTLYHGFMPTVLGVIPYAGLSFFTYETLKSLHREYSGRRQPYPFERMIFGACAGLIGQSASYPLDVVRRRMQTAGVTGYPRASIARTLRTIVREEGAVRGLYKGLSMNWVKGPIAVGISFTTFDLMQILLRHLQS", "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": "MARIQTVLGSITPNLLGRTLTHEHVAMDFEHFYKPPPADFQSELEQKISMATLGYVRLYPYSSKENVRFYDEEALEASRKDVLLYKKHGGGAIVENSSYGLKRNLEFIVDLAKTTGVHFIAGTGHYIHATQDASHKNLTVEQMTDLYSKDILTGIEVNGRMVKSGFIGEVASVYPVQEFERHSLLAAGEIQEVLGCGVSLHPHRVSKAPFEILRLYLEAGGRANKCVMSHLDRTLFDMDELLEFAKMGCYLQYDLFGTECSYYQLNSAVDMISDGQRIDNIIKLINEGLVDRLLMSHDIHTKHRLTSYGGHGYHHIHMNILPRMFQRGVTLDQVEQMTVTNPANWLSFSA", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family."}
+{"protein": "MNREITFFGRFEADILADRKTITIRDSSESDFRSGEVLRVCRNEDGVFFCHIKVKSVTPVTLDGLSERHAEQENMSLDELKKVIKAIYPGLDRFYVIEFTRC", "text": "FUNCTION: Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C). SIMILARITY: Belongs to the N(4)-acetylcytidine amidohydrolase family."}
+{"protein": "MKNAFKDALKVGRPQIGLWLGLANSYSAELLAGSGFDWLLIDGEHAPNNVQTVLTQLQAIAPYPSQPVVRPSWNDPVQIKQLLDVGAQTLLIPMVQNADEARNAVAATRYPPAGIRGVGSALARASRWNRIPDYLHQANDAMCVLVQIETREAMSNLASILDVDGIDGVFIGPADLSADMGFAGNPQHPEVQAAIENAIVQIRAAGKAPGILMANEALAKRYLELGALFVAVGVDTTLLARGAEALAARFGAEKKLSGASGVY", "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": "AAAAAGRGRSFSPAAPAPSSVRLPGRQAPAPAAASALAVEADPAADRVSSLSQVSGVLGSQWGDEGKGKLVDVLAPRFDIVARCQGGANAGHTIYNSEGKKFALHLVPSGILHEGTLCVVGNGAVIHVPGFFGEIDGLQSNGVSCDGRILVSDRAHLLFDLHQTVDGLREAELANSFIGTTKRGIGPCYSSKVTRNGLRVCDLRHMDTFGDKLDVLFEDAAARFEGFKYSKGMLKEEVERYKRFAERLEPFIADTVHVLNESIRQKKKILVEGGQATMLDIDFGTYPFVTSSSPSAGGICTGLGIAPRVIGDLIGVVKAYTTRVGSGPFPTELLGEEGDVLRKAGMEFGTTTGRPRRCGWLDIVALKYCCDINGFSSLNLTKLDVLSGLPEIKLGVSYNQMDGEKLQSFPGDLDTLEQVQVNYEVLPGWDSDISSVRSYSELPQAARRYVERIEELAGVPVHYIGVGPGRDALIYK", "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": "DPMLQDSQGFNALHLATHSSNAMLVLYLLMAGEMPVDTADTLGHTSLMWAAYQGDSLSVQILLKHGARVDTKDREGFTPLHWAVVKGNRECLSKILMAGADIKAGDKSGKTPVDMIKELKGTMIWDKALSDAKLSSDGQTRRTPFDKLMVLFPWYIALPLAVAQFLFGHIGAIKFLLRTRTPNDMLQTPYYTAVFQSTAFWVGFVWLRYLLGNTSHLLWMNIAFFVGYTSALYFFYGAVMADPGWTKANSSYESQREAVVQMADRGLLDARHFCVSCIAQRPLRSKHCKFCNRCVAKFDHHCPWIYNCIGAKNHRAFLIFLALFLSSVPIYAYLSFEYLHVLSPSYVPVSSDPCLLGDTLCGYFQYDAFTTTLAFWSLFQMTWPGLLFLVQLYQVGQAKTTNEAMNFQRHSYLGKSMTIRQRILRSLTEIDSEMAGAGHPLQEESINLLEANGTATNDEDEVTLFAQEESKPVGFGDHEGHNHGARRAGGGGMWNLLVGTARRRRQQGEDRDVNPFDFGLWQNCVGFWSDGTQGPMRGVNWYSFYEAEARGGAATSRRM", "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": "MSNMNQTIMDAFHFRHATKQFDPQKKVSKEDFETILESGRLSPSSLGLEPWKFVVIQDQALRDELKAHSWGAAKQLDTASHFVLIFARKNVTSRSPYVQHMLRDIKKYEAQTIPAVEQKFDAFQADFHISDNDQALYDWSSKQTYIALGNMMTTAALLGIDSCPMEGFSLDTVTDILANKGILDTEQFGLSVMVAFGYRQQDPPKNKTRQAYEDVIEWVGPKE", "text": "SIMILARITY: Belongs to the nitroreductase family."}
+{"protein": "MPLVFFARVADVSLGTFRTIVIFRGHKFLASFIGFFEIIIWLVASAQVLTNLDQWYLALAYASGFSVGNYAGISIENRFAIGNELIRCISFNRDVLAGKLREEGFKVVSFDGDMGEAYPVELLLVIEKRRNVPSLIQLIKDLDPTAVYSVSDVKSVYEGPDIFPRRSLLHSTLMLLGKR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0316 family."}
+{"protein": "MGTVHARSLDPLPMNGPDFGSPDDADLVEVEPEKKQEILENKDVVVQRVHFEGLGRTKDDLIAHEIGQVFKAKNLIEVMRKSHEAREKLLRLGVFRNVEVLIDTSEGEDAVPNGLDVTFEVTELRRLTGSYNTMVGNNEGSMVLGLKFPNLFGRAEKMTFQFSYGTKETSYGLSFFKPQVGNFERNFSVNLYKVTGQFPWSSLRETDRGVSAEINFPIWKTSHTLKWEGVWRELGCLARTASFAIREESGHTLKSSLSHTMVIDSRNASILPKRGALLKINQELAGYTGGDVSFLKEDFELQLNKQLAWDSVLSTSLWGGMLVPVGDRPSSIADRFYLGGPTSVRGFSMYSIGPQSEGDYLGGEAYWAGGVHLYTPLPFRPGRGGFGDLFRTHFFLNAGNLCNLNYGEGPRAHLQRLAECIRWSYGAGLVLRLGNIARLELNYCIPMGVQSGDRICDGVQFGAGIRFL", "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": "MSVRLADVIDVLDQAYPPRLAQSWDSVGLVCGDPDDVVDSVTVAVDATPAVVDQVPQAGLLLVHHPLLLRGVDTVAANTPKGVLVHRLIRTGRSLFTAHTNADSASPGVSDALAHAVGLTVDAVLDPVPGAADLDKWVIYVPRENSEAVRAAVFEAGAGHIGDYSHCSWSVAGTGQFLAHDGASPAIGSVGTVERVAEDRVEVVAPARARAEVLAAMRAAHPYEEPAFDIFALVPPPVGSGLGRIGRLPKPEPLRTFVARLEAALPPTATGVRAAGDPDLLVSRVAVCGGAGDSLLATVAAADVQAYVTADLRHHPADEHCRASQVALIDVAHWASEFPWCGQAAEVLRSHFGASLPVRVCTICTDPWNLDHETGRDQA", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family."}
+{"protein": "MVDQNPKRSNEPPVWLMFSAGGMVSGLAFPVLILILGILLPFGIISPDNIIAFSHHWFGKLVILALTIFPMWAGLHRLHHGMHDIKVHVPNGGLIFYGLAAVYSFIVLFAVIAI", "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": "MNNQSPLLKFLTTAPVITTIWLFITAGILIEFNRFFPDLLFHPLP", "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": "MLTSTLLAAATTPLEWSPTIGIIMVIANVIAITFGRQTIKYPSAEPALPSAKFFGGFGAPALLATTAFGHILGVGIILGLHNLGRF", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the PsaG/PsaK family."}
+{"protein": "MNLSRRDFMKTNAAVAAAAVAGLAIPVKNVEASPDKIIKWDKAPCRFCGTGCSVLVGTQNGRVVASQGDPDADVNRGLNCIKGYFLPKIMYGKDRLTSPMLRMTNGKFDKHGEFTPVSWDQAFTIMAEKFKKALKEKGPNGAGMFTSGQSTIFEGIAKSKLFKAGLRSNNIDPNARHCMASAAVAFMRTFGMDEPMGCYDDIEKADAFVLWGSNMAEMHPILWSRISDRRLSHPDVKVAVLSTFEHRSFELADLGVIFTPQSDLAIMNYIANYLIQHDAIDHDFIQKHTKFKRGETDIGYGLRETHELEKAAKNVKTAGKMHDSDFEEYKKLVAPYTLEKAHEISGVPKEQLEALAKMYADPKLNIVSFWTMGFNQHTRGVWANHLIYNIHLLTGKISKPGCGPFSLTGQPSACGTAREVGTFAHRLPADLVVTNPKHVEKAEKLWKLPKGVIQTQVGYHAVAQDRALKDKKMNVLWQMCTNNMQGGPNINQERFPGWRDEENFVIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWYQQVKAPGESKSDVWQLVEFSKYFTTDEMWPAEVLAANPEYKGKTLYEVLFRNGQVDKFQVPTDKPGYMNDEAEHFGFYLQKGLFEEYAVFGRGHGHDLADFETYHKARGLRWPVVDGKETLWRYREGYDPYVKEGEGVAFYGYPDKKAIILAVPYEPPAEAPNAEYDLWLTTGRVLEHWHTGTMTRRVPELHRSFPNNLVWMHPLDAKKRGLRHGDKVKISSRRGEMISHLDTRGRNKVPQGLVYTTFFDAGQLANYLTLDATDPISKETDFKKCAVKVEKA", "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": "MGGALSTDGAEQRASSVEELNQRLAHRFAAKCFEPLELTHLKENFFSRALDQHGIRYWNEEILSEFLGIPDGAGSAAAATSDGSLDAGPVIFRMVSYLGAFPFQNTMAPTVLTFESMVKVVVLLTERYGKVLKRGKKDRMKLLFGSLADVGRRDIITVLKEATEDSLESIGPSDPRSASPSTHNTGFLVDQPVNDEDEEDDDDLAIAALESLDAIEVFKHDQRIDKTVYESKISLTTFRRLLTLLLVTAPLRPLGRVSKFTTGLSKPSLDAVHEQVDSILAALDPGEASDGIGYKSFSKLVSTSLPYLFDPLTPLFEHLLFSKNLDLSRKRDSQTTNGLTSKPVPTPPSTPPLSPPLSPVISTGGFDSCILNPALLSHLSFFVSTNVHIPNIFRNRTHLHPVFSSTEHGESLTSFSHHVMTWQAPSILLVRGAVVSESSEEQLTTIGAYLPQPWKQTSSYSSRRSSEAPDPSTLPCLFELSPVHTVLQGSPSFSSLKSNMPVTHFSTKTGIAIGCMIPPSSRKSFGSDLHPKPAGGGSLLIDSALENATFIVSNGLNGPGVFLPPGISPVLSSTSLTASVPSMSSSNQNFTKSISIYNLEVWGIIPSTSLATQLDGSGSPIEKRDAISLQRAQWDFEAREAERRQAINMKVGGGESDAQTGRALLEMAGIIGDSYYSGHHRH", "text": "FUNCTION: May be involved in a process influencing telomere capping. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RTC5 family."}
+{"protein": "MDDNYLDSIFEKYLHAKKIFKNKEVLRHSYTPRELPHRREQIENLAHILVPVLRGETPSNVFVYGKTGTGKTVTIKFVTEELKKISQKYNVPVDVIYVNCEIVDTQYRVLANIVNHFREESGVEVPLVGWPTDEVYSKLKAVIDAKERFVIIVLDEIDKLIKKSGDDILYSLTRINTELHRAKVSIIGISNDLKFKDYLDPRVLSSLSEEEVVFPPYDANQLRDILMQRAKDAFNEGVLDDGVVPLCAALAAREHGDARRALDLLRVAGEIAEREGASKVTERHVWKAQEKIEQDTMEEVIKTLPLHSKVLLYAIVLLDENGELPANTGDVYSVYKSLCDHIDLEPLTQRRVSDLINELDMLGIINAKVVSKGRYGRTKEIRLNVTPYKVKNIYRHDHQLQTVLTISMSRQRRLL", "text": "FUNCTION: Involved in regulation of DNA replication. SIMILARITY: Belongs to the CDC6/cdc18 family."}
+{"protein": "MFKSGFITIVGRPNVGKSTLTNLLMGEKLSIVSNKPQTTRNNIQTILTGDDYQMIFVDTPGIHKPKHKLGEYMVNSATDSIKDVDLVLFLSNPCEEVGRGDKFIIEQLKNQKAPVIFVLNKVDESSPEKVAKTLELFSKEYDFAEMIPISAMKAKNTDKLLELMVKYLPEGPKYYPDDMITDVQERFVVAEIVREKALKNLSQEVPHGIAVDVIQMKQDDNGKYNIEVDLICEKASHKGIIIGKNGQTLKKIGSTARYELERFLRAKVNIKIWVKVRKEWRDNTSLLKELGYKKLK", "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": "MEAEAAAKRARESGDAAAAGAGEQAGISAVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDYQNVMVFQSSTYGKVLVLDGVIQVTERDECAYQEMITHLPLCSIKDPKKVLVIGGGDGGVLREVSRHSSVEQIDICEIDKMVVDVSKQFFPHLAVGFEDPRVSLHIGDGVAFLKNAPEGTYDAVIVDSSDPIGPAQELFEKPFFQSVARALRPGGVVCTQAESIWLHMHIIEDIVANCRQVFKGSVNYAWTTVPTYPSGVIGFMLCSTEGPTVDFQHPIFNIEDNEFSTKSKGPLKFYNSEIHSASFCLPSFAKRVIGSKAN", "text": "SIMILARITY: Belongs to the spermidine/spermine synthase family."}
+{"protein": "MSTKPELKRFEQFGEMMVQLYERYLPTAFDESLTLLEKMNKIIHYLNEIGKVTNELIEEWNKVMEWILNDGLEDLVKETLERWYEEGKFADLVIQVIDELKQFGVSVKTYGAKGDGVTDDIRAFEKAIESGFPVYVPYGTFMVSRGIKLPSNTVLTGAGKRNAVIKFMDSVGRGESLMYNQNVTTGNENIFLSSFTLDGNNKRLGQGISGIGGSRESNLSIRACHNVYIRDIEAVDCTLHGIDITCGGLDYPYLGDGTTAPNPSENIWIENCEATGFGDDGITTHHSQYINILNCYSHDPRLTANCNGFEIDDGSRHVVLSNNRSKGCYGGIEIKAHGDAPAAYNISINGHMSVEDVRSYNFRHIGHHAATDPQSVSAKNIVASNLVSIRPNNKRGFQDNATPRVLAVSAYYGVVINGLTGYTDDPNLLTETVVSVQFRARNCSLNGVGLTGFSNSDNGIYVIGGSRGGDAVNISNVTLNNSGRYGVSIGSGIENVSITNISGIGDGINSPVALVSTINSNPEISGLSSIGYPTAARVAGTDYNDGLTLFNGAFRASTTSSGKIHSEGFIMGSTSGCEASVSKSGVLTSSSSKTSSERSLIAGSSTSEAKGTYNTILGSLGAVADEQFAALISASQSRASGNHNLILSSYGINTTGSYKVNGGFEKINWELDSLNGRIKARDTVTGGNTWSDFAEYFESLDGQVIETGYLVTLEKGKIRKAEKGEKIIGVISETAGFVLGESSFEWQGAVLKNEFGGIIYEEVTTEDGVKFKRPLPSPDFDPNKNYIPRSQRREWHVVGLLGQIAVRIDETVKQGHGIDAVGGVATDGDNFIVQEITTPYTKEKGYGVAIVLVK", "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": "MLETTNGEASPEDPPLNLKSLSQPPQKRSRTVEDFNRFCSFVLTYAGYIPTPATEERPWTPPSSVSPHRTEESDGWDSSPQLPVPSDPPQPPATSDISTIETFVMKAKSQGGGGNSIMKTGGPIGGSGEQVKKGSRRKRRQLHRGGVTMSDTDTDEEERDKRPAGSLPAPQLPPSAESSRDGGGSSSDTDTQVMDEDIMVESGDDSWDLVTCYCEKPFAGRPMIECNICCTWVHLSCAKIRKSNVPDVYYCQKCRGGRGSGGTALKEEP", "text": "FUNCTION: Acts as a negative regulator of autophagy. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the PHF23 family."}
+{"protein": "MKVIFMGTPEFAVPALKKLITHHEVKAVFTQQPKAKGRGLNLAKSPIHQLAFEHQIPVYTPSTLRNDEIINLINKVNADIIVVIAYGFIVPKAILEAKKYGCLNIHPSDLPRHRGAAPLQRTIIEGDRKSSVCIMRMDTGLDTGDILMKEDFDLEERITLEELHNKCANLGAELLIKTLANIDNIVPITQPSDGVTYAHKLTKEEGKINWHESAYKIDCKIRGMNPWPGAYFSYNDKIIKILEAEYLNADHHFTSGTVISDKLEIACGSGILRVKKLQQESKKALNIEEFLRGTNILKDTVLK", "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": "MSKSLAGLAVLAALFIAVDAFRPSGLTNGHATFYGGSDASGTMGGACGYGDLYSAGYGTMTAALSTALFNDGASCGECYRITCDHAADSRWCLKGASVVITATNFCPPNFALPNNNGGWCNPPLKHFDMAQPAWEKIGIYRGGIVPVVFQRVSCYKKGGVRFRINGRDYFELVNIQNVGGAGSIKSVSIKGSKTGWLAMSRNWGANWQSNAYLDGQALSFSITTTDGATRVFLNVVPSSWSFGQIYSSNVQF", "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": "MHKAILNSDLIATKAGDVTVYNYDGETREYISTSNEYLAVGVGIPACSCLDAPGTHKAGYAICRSADFNSWEYVPDHRGETVYSTKTGESKEIKAPGDYPENTTTIAPLSPYDKWDGEKWVTDTEAQHSAAVDAAEAQRQSLIDAAMASISLIQLKLQAGRKLTQAETTRLNAVLDYIDAVTATDTSTAPDVIWPELPEA", "text": "SIMILARITY: Belongs to the tfa family."}
+{"protein": "MALAAARRLLLHAGSRLGRREAVDGARRFANKRVLVETEGPAGVAVMKLRNPPVNSLSLECLTEFTISLEKLENDKSIRGVILTSECPGIFSAGLDLLEMYGRNPAHYAEYWKNVQELWLRLYTSNMILVSAINGASPAGGCLLALCCDYRVMADNPKYTIGLNESLLGIVAPFWFKDMYVNTIGHREAERALQLGTLFSPAEALKVGVVDEVVPEDQVHSKARSVMTKWLAIPDHSRQLTKNMMRKATADNLIKQREADIQNFTSFISKDSIQKSLHMYLEKLKQKKG", "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": "MTLRSLILEMRSRPHRVVHDLAAAAAADSTSVSSQDYRWSEIPEELLREILIRVEAADGGGWPSRRSVVACAGVCRGWRLLMNETVVVPEISSKLTFPISLKQPGPRDSLVQCFIKRNRITQSYHLYLGLTNSLTDDGKFLLAACKLKHTTCTDYIISLRSDDMSRRSQAYVGKVRSNFLGTKFTVFDGNLLPSTGAAKLRKSRSYNPAKVSAKVPLGSYPVAHITYELNVLGSRGPRKMQCLMDTIPTSTMEPQGVASEPSEFPLLGTRSTLSRSQSKPLRSSSSHLKETPLVLSNKTPRWHEQLRCWCLNFHGRVTVASVKNFQLVAAGASCGSGTGMSPERQSERIILQFGKVGKDMFTMDYGYPISAFQAFAICLSSFETRIACE", "text": "SIMILARITY: Belongs to the TUB family."}
+{"protein": "MTTLATLIFLVTLLFVLWQPKGLDIGITALTGAFIAVITGVVSFSDVFEVTGIVWNATLTFVSVILISLILDKVGLFEWSAIHMLHASKGNGLKMFVYIILLGAIVAAFFANDGAALILTPIVLAMVKNIGFSKRAIFPFIIASGFIADTTSLPLIVSNLVNIISADYFHVGFVRYFSRMIIPNLFSLLASIIVLWLYFRKAIPKTFDDNNIKHPKDAINDLKLFKISWIVLVILLFGYLISEFTKIPVSIFTGIIAFIFLMLARKSNAVNIKQVIKGAPWNIVLFSIGMYIVVFGLRNAGITLILAKILEYISNYGLFSTILGMGFISAFLSSIMNNMPTVLIDAIAIGQSNVHGMLKEGLIYANVIGSDLGPKITPIGSLATLLWLHVLTQKDVKISWGTYFKTGIIITIPVLFITLIGLYLTLIIF", "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": "MAATMVLDPKPSSTPPPTLPNPYTTDSQSTDSEDDLYTRLKTLDRQIEFIDIQEEYVKDELKNLKREQLRSQEEVKRIQSVPLVIGQFMEMIDQNNGIVGSTTGSNYYVRILSTINRELLKPSASVALHRHSNALVDVLPPEADSSISLLSQSEKPDVTYNDIGGCDIQKQEIREAVELPLTHHELYKQIGIDPPRGVLLYGPPGTGKTMLAKAVANHTTAAFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEVDAIATARFDAQTGADREVQRILMELLNQMDGFDQTVNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFQVCTAKMNLSDEVDLEDYVSRPDKISAAEITAICQEAGMHAVRKNRYVILPKDFEKGYRTNVKKPDTDFDFYK", "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": "MQQEKELVKQKAKELLLDLLSIYTPSKNETNATKFFEKISNEFNLKLEILPDSNSFILGEGEILLASHVDTVPGYIEPKIENEVIYGRGAVDAKGPLISMIIAAWLLNEKGIKVMVSGLADEESTSIGAKELTLKNFNFKHIIVGEPSNGTDIVVEYRGSIQLDIMCESTPEHSSSAKSNLIVDISKKIIEVYKQPENYDKPSIVPTIIRAGESYNVTPAKLYLHFDVRYAINNKRDDLINEIKDKFQECGLKIVDETPPVKVSINNPVVKSLTRALLKQNIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLEHTNQEKITFDEIYIGVKTYMLAIEELWQKS", "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": "MTIRYPNGKRYDQASQPHKTPIKKHTYSNRGMSLEEELNDTNQYYLTHNIACVHKKPTPLQIVKVDYPARSAAVVKEAYFKQPSTTDYNGVYKGKYIDFEAKETKNKTSFPLQNFHLHQIEHMKQVVAHNGIAFVIIKFTLFDEFYLLDAKHIIAFWNRQNTGGRKSITKQEIEEHGSLLSCGYHPRIDYIRVLDTVYFS", "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": "MKTFFAKFIVALFAFTYFSAFAEPVTLNNSPVRSFVQWYSSKTGKSVIVNPDVKGNITVFNADVNNANIDDFFKSVLNANGLVVVAGNPAVVSTPLTKLASQPSNEETYDDESDGVAYEAVPQSAAPAVPADLTVRNFNVTRVRSSDVLPLAKIFVDSNGGGNVVDYPGNNSLVVSGSAQVMPALSDFITSIDVAREQVLIQSLMFETSVSNGVDLSFALALASGGKVAGGFNTSALGTALSTAGGSFGIFNGNILALSLQAVQSDSNSKVISTPRILTQSGQSGYISVGQNVPFVTGKVTGEAASVNNPFQTIERRDVGVSLKVTPVVMGNGQLVLTIDTKADSLSNQAIASDIITNQRQIQTTVQIKDGQTLLLGGLISSNQFDSDRSVPFMSKIPLIGWLFRSHSDSKDDRTMFVLLTAHVIRAL", "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": "MKQNRKNLPIILASSSPARIELLNRIKIIPSQIIPADIDETPNLRELPAPLAIRLAYEKAIKIASQIEESAIIIAANTVAAVGRRILPKATTYEEVKNCIKMLSGRRHRIYTGLCIIKKENDQLTVRQKIVQTIVKFKKLSDEEINFYCSLDEGIDKAGGCKISGYAEAFISFISGSYSNVMGLPLFETVNALTSLGFRCSSIMPAKMNYCHSAT", "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": "MTLLSSHLLVFSAVHHRAPPTTTTRNSPTTNHTVRFLCSPGVPPAVRLDQRLPRFVVPGAGAEDLLYNAGATVGVLGGGYALVRAFDELTRRNILQQGLSRKLVHILSGLLFLVSWPIFSNSPKARYFAAFVPLVNCLRLLVNGLSLASDEGLIKSVTREGDPLELLRGPLYYVLILILSALVFWRESPIGVISLAMMCAGDGIADIIGRRYGSMKIPYNEHKSLAGSMSMLVFGFLVSIGMLYYYSVLGHVQLDWASTLPRVAFISFVATLVESLPITKVVDDNISVPLATMAVAFFTFHH", "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": "MEQRRLASTEWVDIVNEENEVIAQASREQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARREAEEELGIAGVPFAEHGQFYFEDKNCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEITARCDEFTPDSLKALALWMKRNAKNEAVETETAE", "text": "SIMILARITY: Belongs to the Nudix hydrolase family."}
+{"protein": "MSSYYSVDAILTDAQKVPCTFELTVPGLGFLEGNMSGDMKQGSKVELPLWLGEMLALSQSLNTSSLVTLDPPSALSPRVLNALKADPRTVDLRALAPHFYDLGARILELFEEEKMIEVLSDTFKARAAVIADQAHNPRGALGEGADFMRGLDENERQLFRAAHDSAKAARTWMTDLKRK", "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": "MGKPVDDLLNSLMNLLDSETPSGGGCHLCDGLLSRELGKMLRKALSELEGVELSSVKSGVSLPAILIEREDRIRANHNPPKMRSLKVTLTRLLDVAISSLTGLKVSQEPDAILIFDFERGDVKLELAPVFIFGRYRKLQRGISQSRRKCPECGGRGCEACGWKGKIPQGSVEGIVGEVMREFFSAEDYVLHGAGREDVDARMLGEGRPFVMELLSPKRRSADLREVESEINRRAAGLIEVKNLEFSRREKIRILKERSPNVKKLYRALVEVEGGVEEGELELLKGLEGAVIRQRTPKRVLWRRADITRLKRVYEVNFRRIDDKKFELFVLCDGGLYVKELISGDDGRTSPSVTEILGKKSFCSELDVLEVMVE", "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": "MSSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD", "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": "MKLIASVLNPVHNFDARSTAMLSLLTFKNCFLSNGRVLIFQLKPCRKLQTTRFVLAESVASNNDILFNATASMRKNKDAAKLMTDRIHYVSPAKRKQTRTPSTGHQNRKRTTLKWNTGSERAQAAANFTLRQVFKMNERGVVKVVNQTTNKLEETSILIWAGELDLQKHGLAIVDVEQRGTFSIPLVKLVESKTALKKYSDELAKQKEEELTRLGFSSKRTGRKNENDSNEDNLKQIKVSWQISDADLNKQKANEIISQLKKGYKVFLYMNGKDALNKSNWAEDITDEEPAHTRKHSDRELERRQHIVEQLQVIVNEFSLSPTVEGSIETRLIMKLSPKPVASKKEDRMALKEQRKRERQEKLERKLEKKKLRNSENY", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM23 family."}
+{"protein": "MDVTKSLLCFISFVAFLLFSSVAEANKAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQGQEGTLWWHAHSSWLRATVYGSLLVFPPAGSSYPFTKPHRNVPLLLGEWWDANPVDVLRESIRTGGAPNNSDAYTINGQPGDLYKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNAPFGNTTTTAILQYKSAPCCGVGGGSGTKKGNSFKPIMPILPAYNDTNTVTRFSQSFRSLRRAEVPTEIDENLFVTIGLGLNNCPKNFRSRRCQGPNGTRFTASMNNVSFALPSNYSLLQAHHHGIPGVFTTDFPAKPPVKFDYTGNNISRSLYQPDRGTKLYKLKYGSRVQIVLQDTGIVTPENHPIHLHGYDFYIIAEGFGNFNPKKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAFLVENGNGVLQTIEQPPHDLPVC", "text": "FUNCTION: Lignin degradation and detoxification of lignin-derived products. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "MSTTPTYNHPVINERSKRMVWVDLEMTGLDISKDVILEMAIVITDAELNVIEKGPNLVIHRSDEVLKNMNDWCIEHHGKSGLTEDVRNSKISLEEAEKIMLEFVRKHTDKGICPLAGNTVHEDRRFLLKEMPTFAEHLHYRIIDVSTIKELSRRWYPYIPSPKKVCGHRALQDIEESIEELKSYRVTVFK", "text": "FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. SIMILARITY: Belongs to the oligoribonuclease family."}
+{"protein": "MALLRKINQVLLFLLIVTLCGILYKKVHKGTMLRNEADDDSETPEEMEDEIPVVICAAAGRMGAAMAAINSIYSNTDANILFYVVGLRNTLSRIRKWIEHSKLREINFKIVEFNPVVLKGKIRPDSSRPELLQPLNFVRFYLPLLIHQHEKVIYLDDDVIVQGDIQELYDTTLALGHAAAFSDDCDLPSSQDIHRLVGLQNTYMGYLDYRKKTIKDLGISPSTCSFNPGVIVANMTEWKHQRITKQLEKWMQKNVEENLYSSSLGGGVATSPMLIVFHGKYSTINPLWHIRHLGWNPDTRYSEHFLQEAKLLHWNGRHKPWDFPSVHNDLWESWFVPDPAGIFKLHHPNS", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 8 family."}
+{"protein": "QDAAKGEAVFKQCMTCHRADKNMVGPALGGVVGRKAGTAAGFTYSPLNHNSGEAGLVWTQENIIAYLPDPNAYLKKFLTDKGQADKATGSTKMTFKLANDQQRKDVAAYLATLK", "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": "AYGEAANVFGAPK", "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": "MAFKLSTKHLADIGAQTEKSIRIPSYDRNDVKEGIVHVGVGGFHRAHLAVYVDKLMQSHGVRDYAICGVGLQPADASMRDVLASQDHMYTVIERSAAGSTAHVVGSIRNFLFAPDDREAVIAKMAHPDTHIVSLTITESGYYYNENTHELQSEHPDIQHDLDPANAAKPKTTFGFLYAAMVRRREQGLKPFTVLSCDNMLKNGSITRNMLQSFAKLKDPSMADWIAQYGGFPNAMVDRITPRTSDPDIKELADKFKIDDAWPVVTEPFMQWVVEDKFADGRPPFDLVGVQVVKDVKDVEQFEKHKLRLLNASHSAMGYPGQLAGFKYVHEVMEHPLYRKFIWQMMQEEVKPLLPEIPGVDIDAYCNTLMERFSNPTIMDQLPRIALNSSGKMPQFVMPSIAEAIWVTGPFRRLVFVAACWFRYVLGVDDKGNKFEVDDPMREELQSKAQAGGTKPHEILSIKSLFGDDLRGDERFLKEVTQAMEDIARDGVMATMPKFVNDA", "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": "MLKLFSAFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKMLPVHAPTSGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKIETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPSGGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDARFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPADLLPQQLYWFSKGQQHDKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARQARLEREKAARLERHKSAAVQPAAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAAREARKAQARAKQAELQQTNDAATVADPRKTAVEAAIARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQVDPRKAAIEAAIARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAVPEEQVDPRKAAVEAAIARAKARKLEQQQTNAEPEEQVDPRKAAVAAAIARAQAKKAAQQKVVNED", "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": "MGGPRAWALLCLGLLLPGGGAAWSIGAAPFSGRRNWCSYVVTRTISCHVQNGTYLQRVLQNCPWPMSCPGSSYRTVVRPTYKVMYKIVTAREWRCCPGHSGVSCEEASSASLEPMWSGSTMRRMALRPTAFSGCLNCSKVSELTERLKVLEAKMTMLTVIEQPVPPTPATPEDPAPLWGPPPAQGSPGDGGLQDQVGAWGLPGPTGPKGDAGSRGPMGMRGPPGPQGPPGSPGRAGAVGTPGERGPPGPPGPPGPPGPPAPVGPPHARISQHGDPLLSNTFTETNNHWPQGPTGPPGPPGPMGPPGPPGPTGVPGSPGHIGPPGPTGPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGEKSHWGEGLHQLREALKILAERVLILETMIGLYEPELGSGAGPAGTGTPSLLRGKRGGHATNYRIVAPRSRDERG", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
+{"protein": "MAVARTGVLGVQWLQRASWNMMPLGARTASHMTKDMFPGPYPRTPEERAAAAKKYNMRVEDYEPYPDDGMGYGDYPKLPDRSQHERDPWYSWDQPDLRLNWGEPMHWHLDMFNRNRVDTSPIPVSWNVMCMQLFGFLAFMIFMCWVGEVYPVYQPVGPKQYPYNNLYLERGGDPSKEPERVVHYEI", "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": "MTEFQDPFLKSGEPVKFDKKYIDSTIRPGDIGIADQWAVKPVSDPFVGNLETPVNSGYFTKAFINNLPFYRSGISPNFRGLEVGAAFGYLLYGPFAMTGPLRNTDFALTAGLLSTIGAVHILTALFVLYTAPGKDPNVQPSDCTVENPPTDLFTRTGWTDFTSGFWLGGCGGAVFAWLLCGTLHLDTIMPIVKGVWAAG", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaL family."}
+{"protein": "MEIELGHYLALSAFVFICGVLGVLTRRNAIIIFMSIELMLNAVNLSFVAFSHYLSDIAGQMMVFFVMTVAAAEAAVGLAIVISLFRNKQTVNIDEINLLKG", "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": "MAYVINEACISCGACEPECPVNAISSGDDRYVIDADTCIDCGACAGVCPVDAPVQA", "text": "FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions."}
+{"protein": "MILIIYAHPYPHHSHANKQMLEQAGTLENVEIRSLYHLYPDFNIDVAAEQEALSRASLIVWQHPMQWYSVPPLLKLWMDKVLTHGWAYGHGGTALHGKHLLWAVTTGGGENHFTIGSHPGFDVLSQPLQATALYCGLKWLPPFSMHCTFICDDDTLQAQARQYKQRLLAWQEVNHG", "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": "MLIRFKINEIECEVDEEKEDLTILQACTANGIEIPRFCYHEKLTIAGNCRMCLVYVTNEEKLLAACGIPLDENFDDESIETEIDEILKAREGVMEFLLINHPLDCPICDQGGECDLQEQTIAYGLDTGRFYIKKRAVEVKAFGRLIKGIMTRCIHCTRCVRFLTEIAGVNELGVLGRGYNMEIGTYKKNVIIESELSGNIIDLCPVGALTSAVYAYKGRPWELKNIKGIDIFDTVLTPINYQVKGGEIFRILPRINDRLNEEWITDKVRFHYESYKIIEKMRKDTPSYKIQANKFIELSWKTALKMVFKVLLNKKNKVDLIIGSKINSTNLRIYKELMNRLGSKNYITENGLLFKKFNYDFRENYINSNDLYNVDQNDLVLLCGINLRVESPLLNIKLRNINFGDDEIETRKKIGIIGNKFDWKQESEYLGSTVNSMLKVFEGRFPYCQQIKKSKAPLILVGSSLLSRIAISLQEIRAAFEIASNIKPENVLLITQGANFGMALEEGIFKENFSKGGNVLYSIDSNEYKVSKTINYIIYQGILNDTFENKIDLYLPSKHYFEDFESDREIYVNTFGQRSEIEKLRISKGNKIKENSMIGYIQLMYLNKKEMNRKEKEQKEIKITYRGIKQKEKRQVKINKNLTINNIIDNYYMTDINSRLSKNLMITGQLRKEKKIMEAGSWKNKTCI", "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": "MDIAIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGVSEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVPSGVDAGHSERAIPVSREEKPSSAPTS", "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": "MKPENKLPVLDLISAEMKTVVNTLQSDLPSWPATGTIAEQRQYYTLERRFWNAGAPEMATRAYMVPTKYGQVETRLFCPQPDSPATLFYLHGGGFILGNLDTHDRIMRLLASYSQCTVIGIDYPLSPEARFPQAIEEIVAACCYFHQQAEDYQINMSRIGFAGDSAGAMLTLASALWLRDKQIDCGKIAGVLLWYGLYGLRDSVTRRLLGGVWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTREVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQFFTAQL", "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": "TTCTSTQQTAAYVTLVSILSDSSFNQCATDSGYSMLTATALPTDAQYKLMCSSTACNTMIKKIVSLNAPNCDLTVPTSGLVLNVYEYANGFSTKCASL", "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": "MSCHPQTPQSPSQFSPNTSDLMMSMTGSVTSTTTTLPTPAHSVNGSSIPSELTQDTAMGDDSPHKRKRDGDDMGSRAQKKVHVEDRKLGIDDLHMDVGEKYLLCRTPHPRPRPHVSEDLFEMYGLTGLAIEVARVRPNGEKNALRKTYKGHIKRLGVQGHFDEDKQDPNREYSLSHLMKLPQDVWDLQHVRGQDIRDGFTNEVQQKLSRAMTMGRGVVPRDQWDSSVLGEMGPGKGERQALSARPTAPNTPLPSAGPQGLPRPKTGTPLMQDASRSMRTIKKRSYGDSSFEGYGESYDDGADTGYSTGEGDMSSGQKRRKKVLIND", "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": "MTPNSMTENGLPAWDKQKPRPDRGQDWKLVGMSEACLHRKSHVERRGALKNEQTSPHLIQATWTSSIFHLDPDDVNDQSISSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKSLHPSYSCKYEGKCIIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPDSETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED", "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": "MLKRFFLLLSSLLLVCNVQAGLFNNKPQYLTAAEAFIFSSSQQDGQLQLHWQIADGYYLYQKEIQLSAQNATLGDVTFPTAEKYQDEFFGEVAIFRDQLKLPVKLTDLKENPSLKIRYQGCTKGFCYPPETVVIPLNPSLQGNNSANSAALPSTIATPNAPQTELAENLSNNYLSIFGFLLLGIGLAFTPCVLPMLPLLSAIVIGHKNRPNTSRALLLSFTYVQGMALTYTLLGLTVAAIGLPFQVALQSPAVLISLAVLFTLLAASMFGLFEIRLPNTWQQKLNALSQQQQGGAVGNVFIMGIIAGLVASPCTSAPLSGALLYVAQSGNLLIGGLALYLLALGMGLPLILITVFGNQILPKSGEWLFKVKTAFGFVMLALPIFLISRILPSHYEPFLWSTLALAFLGWLISSLNYSTMLKQAVRILLFIAFGLTAYPWANLVWQTTSNTAQPTTPHLAMEKITSLTELEQKLTAYQGKKVMLDLYADWCVACKEFEKYTFTDPQVQQQLATMAVLQIDMTKNSAENTALMKHFNVLGLPTILFFDENGHEMTNVRITGFLTANQFLAWLNRL", "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": "MADTKKNDNYAIDMDKLDAESDRFRPPPQPQPRHSSSSHSQSISNSPVLPILSYCASSILMTVTNKYVLSGVQFNLNFFLLCVQSVVCIIAIQTCKSMGLINYRDFNSDEAKKWFPISLLLIGMIYTGTKALKFLSIPVYTIFKNLTIILIAYGEVLWFGGSVTGMALFSFGLMVLSSVIAAWADIKHALDTSGFSGAEATSKISTLNAGYIWMLINCLCTSTYILGMRKRIKLTNFKDFDTMFYNNLLSIPILMIGSFIVEDWSSENINKNFPIETRNSLIFAMIFSGLSSVFISYTSAWCVRVTSSTTYSMVGALNKLPIALSGLIFFGDPVTVPSVSAIVVGFISGIVYSLAKVKQNAKPRTGVLPTTNPVSASTQSMRDGLKS", "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": "MTSLPLGVKVEDSAFGKPAGGGSGQAPGAAAATAAAMGTDEEGAKPKVSPSLLPFSVEALMADHRKPGAKESSLAASESAQAAGGLAQPLGVPPGSLGAPDAPSSPRPLGHFSVGGLLKLPEDALVKAESPEKPERTPWMQSPRFSPPPARRLSPPACTLRKHKTNRKPRTPFTTAQLLALERKFRQKQYLSIAERAEFSSSLSLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPPAAFGLSFPLGGPAAVAAAAGASLYGASGPFQRAALPVAPVGLYTAHVGYSMYHLT", "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": "MKIINIGVLAHVDAGKTTLTESLLYNSGAITELGSVDKGTTRTDNTLLERQRGITIQTGITSFQWENTKVNIIDTPGHMDFLAEVYRSLSVLDGAILLISAKDGVQAQTRILFHALRKMGIPTIFFINKIDQNGIDLSTVYQDIKEKLSAEIVIKQKVELYPNVCVTNFTESEQWDTVIEGNDDLLEKYMSGKSLEALELEQEESIRFQNCSLFPLYHGSAKSNIGIDNLIEVITNKFYSSTHRGPSELCGNVFKIEYTKKRQRLAYIRLYSGVLHLRDSVRVSEKEKIKVTEMYTSINGELCKIDRAYSGEIVILQNEFLKLNSVLGDTKLLPQRKKIENPHPLLQTTVEPSKPEQREMLLDALLEISDSDPLLRYYVDSTTHEIILSFLGKVQMEVISALLQEKYHVEIEITEPTVIYMERPLKNAEYTIHIEVPPNPFWASIGLSVSPLPLGSGMQYESSVSLGYLNQSFQNAVMEGIRYGCEQGLYGWNVTDCKICFKYGLYYSPVSTPADFRMLAPIVLEQVLKKAGTELLEPYLSFKIYAPQEYLSRAYNDAPKYCANIVDTQLKNNEVILSGEIPARCIQEYRSDLTFFTNGRSVCLTELKGYHVTTGEPVCQPRRPNSRIDKVRYMFNKIT", "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": "MTQPNPNKQIVELNRTSLFWGLLLIFVLAILFSNYFFN", "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": "MLPRAAWSLVLRKGGGGRRGMHSSEGTTRGGGKMSPYTNCYAQRYYPMPEEPFCTELNAEEQALKEKEKGSWTQLTHAEKVALYRLQFNETFAEMNRRSNEWKTVMGCVFFFIGFAALVIWWQRVYVFPPKPITLTDERKAQQLQRMLDMKVNPVQGLASRWDYEKKQWKK", "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": "MNLKQFPRHSLTFGPTPIHPLSRLSESLGGKVELYAKRDDCNSGLAFGGNKTRKLEYVIPDVLAQGADTLVSIGGIQSNHTRQVAAIAAHLGLKCVLVQENWVNYSDAVYDRVGNIQMSRIMGADVRLVSEGFDIGIRPSWEEAMESVRKAGGKPYPIPAGCSEHPLGGLGYVGFAEEVREQEAGLGFRFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPEPTRAQILRIARHTAELVGLGRDITEADVVLDTRYGGPEYGLPSAGTLEAIRLSARLEGMMTDPVYEGKSMQGMIDMVRRGEFPQGSKVLFAHLGGVPALNAYSFLFKDG", "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": "MARLSGVERPDDSGLRERKARAVEEPVKQPVESADGAAAAAQAKKKTIGRTPDGTAFTVPHTRDMVSQLLSPSEPKNLSDILVLSIIGLHIVLLYLLPSFLRIPIFAVLFLSWRAAYNIGIGWLLHMQSNHSTMVLWARQTKIFVNPATGDNPHPQLYSFIKRELETKIPEDYSFEDAPIEYNTWLVFRRVVDLILMCDFTSYCLFAIACGSRPAEENFLVLILRWVVGLGLVLFNLWVKLDAHRVVKDFAWYWGDFFYLVDQELTFDGVFEMAPHPMYSVGYAGYYGISLMAASYKVLFISILAHAAQFAFLVLVENPHIEKTYNAPPPRKRTIESHAGLAGEEKSSRRPSDSSEMVPPPSPVALPSSTHNLVGVKNLDLHRITDSSIILIQVLFFALTMLTPSTPIYQFFFVLNAAIWRLWYSVGIGYILNCQSHRREWTRHFVKFGETKEEAWNQWKGTYHLSMTLCYASFIAAAWKMYTLPENWGYGLAILKHVLGAGLIALQIWTSVSIYDSLGEFGWFFGDFFFDEAPKLTYSGIYRFLNNPERVLGLAGVWGAALITSSRAMIFLALLSHTLGIAFIQLVERPHMQKLYGRGLRQDAGLVRSIKRSLPPSFKQLHGSVDRILDESIEFIEEVLDTARPKLAAGVTTFVKDTSELFHKYPARITITRIEPDLAGYDMNDYSINVDTSDCITIRDGAEDKSEVLVFEYGSPIKVNWTAPLNHSKRDWVGLYMIGQNPSREVTNVSSWGRWVATNHGSFDSVLSEKGLIASDVVVSKPGTSNTSKKPSVKSGSGKKSSTSTSSHEVASGQMVFSGDKLWWTQGVFEFRYHHNGKHNVMATSRPFEIRIPKFDDGQIPSHVSSNGNGFMTTAIEQALLPIVQNCFDRDPEISPQTAEEPFGCETEGDLKYAKRVVYAVHQMFGIEFATEVVRADGNVQNLAWRICNAKKVLAPYSMRKSNGASTPTGESEEMK", "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": "MPWEEIEHTADAAFRVWADTPEDLLVEAAKALFDLITDLDAVEPEEEVEIEAEGGDLVELLHDWLEEIHFRHEIDGMLFSDFEVKELKKEEGWKVRGVARGEPYDPDRHPFHTEVKAVTYHNMKVEREDGRWVAEYVVDL", "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": "MAEKPEVLDAVLKETVDLENIPIEEVFENLRCTREGLTATAAQERLSIFGYNKLEEKKESKFLKFLGFMWNPLSWVMEAAAIMAIALANGGGKPPDWQDFVGIITLLIINSTISFIEENNAGNAAAALMARLAPKAKVLRDGKWDEEDASVLVPGDIISIKLGDIIPADARLLEGDPLKIDQSALTGESLPVTKGPGDGVYSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAVGMIIEIIVMYPIQHRKYRPGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLAQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLTVDKALIEVFAKGIDADTVVLMAARASRIENQDAIDTAIVGMLADPKEARAGIREIHFLPFNPTDKRTALTYLDGEGKMHRVSKGAPEQILNLAHNKSDIERRVHTVIDKFAERGLRSLGVAYQEVPEGRKESAGGPWQFIALLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGQTKDESIAALPIDELIEKADGFAGVFPEHKYEIVKRLQARKHICGMTGDGVNDAPALKKADIGIAVDDATDAARSASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVLGFMLLALIWKFDFPPFMVLIIAILNDGTIMTISKDRVKPSPLPDSWKLAEIFTTGVVLGGYLAMMTVIFFWAAYKTNFFPRIFGVSTLEKTATDDFRKLASAIYLQVSTISQALIFVTRSRSWSFVERPGLLLVFAFFVAQLVATLIAVYANWSFAAIEGIGWGWAGVIWLYNIVTYIPLDLIKFLIRYALSGKAWDLVLEQRIAFTRKKDFGKELRELQWAHAQRTLHGLQVPDPKIFSETTNFNELNQLAEEAKRRAEIARLRELHTLKGHVESVVKLKGLDIETIQQSYTV", "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": "MSEHVNKYTEYEARTKAIETLLYERGLITPAAVDRVVSYYENEIGPMGGAKVVAKSWVDPEYRKWLEEDATAAMASLGYAGEQAHQISAVFNDSQTHHVVVCTLCSCYPWPVLGLPPAWYKSMEYRSRVVADPRGVLKRDFGFDIPDEVEVRVWDSSSEIRYIVIPERPAGTDGWSEEELTKLVSRDSMIGVSNALTPQEVIV", "text": "FUNCTION: NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. SIMILARITY: Belongs to the nitrile hydratase subunit alpha family."}
+{"protein": "MNTSKASKKRKAVTRDVEEEAGVFSGDELNTGNLDGALSDNAHDLSSDEDESDSEVELIDDFSDEEDEEEEDVLDSDEIPSDGEDSAKKKSNAAPGELGAVIDDDDDDDDDESPSEEEQLNYRIEKDANGNDRFVYDEINPDDNSDYSDVDENANTIGNIPLSFYDQYPHIGYDINGKKIMRPAKGEALDALLDSIEIPKGWTGLTDPSTGKPLELSQEELELLRKVQMNEIPEDGYNPYEPIVEWFTSQQEIMPLSAAPEPKRRFVPSKHEAKRVMKIVKAIREGRILPFKPPTEEDEEDDTIVKYDLWADEAERKDHPMHIPAPKLPPPGYEESYHPPPEYLPSRKERKTWEEADPEDRDREFLPNDFGSLRRVPGYENFVKEKFERCLDLYLAPRVRRSKLNIDPESLLPKLPSPEELKPFPTACATVFRGHKGRVRTLAVDPSGLWLASGGDDGTVRVWELLTGRQLWSVKLSEEDPVNVVRWRPGKDALILAAAAGDDIFLAVPPIVDPAMEKASLDILDAGWGYAASVPPPTPAEANKKNNPPKWMRPSSSLADSGVCAVIPLRYVAKSLSWHRRGDYFVTVCPGSSTPASVAIAIHTLSKHLTQYPFRRRIKGGGPPQAAHFHPSKPILFVANQRSIRAYDLSRQLLVKILQPGARWISSFDIHPTSSTASGGDNLIVGSYDRRLLWHDLELSQRPYKTLRYHRKAIRAVKFHPGGRYPLFADASDDGSLQIFHGSVTGDMLSNATIVPLKVLKGHKITGELGVLDVDWHPREPWCVSAGADGTCRLWM", "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": "MGGGGNLVDGVRRWLFFQRRPSSSSSSNNHDQIQNPPTVSNPNDDEDLKKLTDPSKLRQIKVQQRNHLPMEKKGIPNAEFFTEYGEANRYQIQEVVGKGSYGVVGSAIDTHTGERVAIKKINDVFDHISDATRILREIKLLRLLLHPDVVEIKHIMLPPSRREFRDVYVVFELMESDLHQVIKANDDLTPEHHQFFLYQLLRGLKYVHAANVFHRDLKPKNILANADCKLKICDFGLARVSFNDAPTAIFWTDYVATRWYRAPELCGSFFSKYTPAIDIWSVGCIFAEMLLGKPLFPGKNVVHQLDIMTDFLGTPPPEAISKIRNDKARRYLGNMRKKQPVPFSKKFPKADPSALRLLERLIAFDPKDRPSAEEALADPYFNGLSSKVREPSTQPISKLEFEFERKKLTKDDIRELIYREILEYHPQMLEEYLRGGNQLSFMYPSGVDRFRRQFAHLEENQGPGGRSNALQRQHASLPRERVPASKNETVEERSNDIERRTTAAVASTLDSPKASQQAEGTENGGGGGYSARNLMKSSSISGSKCIGVQSKTNIEDSIVEEQDETVAVKVASLHNS", "text": "SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
+{"protein": "MVAYSILTLISLGLGSHCASALQYGYNQVPVHKDSDVVAGAFPPINGTHLQSPAFTTPGTVPRDFSDGKAGPTRDEIMDNFLRRLARSNGWMAYHEADFMSEEGRKFPYLYLSGTNSSLENPGSGKKLRVWLQGGVHGNEPAGDQSMLALLGEMAQNQQWTAKVLEKMDILVLPRYNPDGVFYFQRYLATNFDPNRDHVKLARQQTRDIKQLFTKFNPHIATDMHEFSAGRAFGPKKDVIYAADALFSAAKNLNIDEGIRQLSEKLFAKRMGKDIEAAGLRWDPYITQGDSTNSKLLLLEAGTDAKIGRNAMGLTQCVAFLCETRGIGIADQHFERRTLSGLVMAKSIIQTAVDNFDEVYNTIERGIDRFTHSKGSIVLTDKSPISARTFGMLNSTDGKLIDYPIDFASTTPATPVLTRSRPRAYLIPQSWTDVVKRLEVLGLKAEKLPYSYTGRVEALNVTSVAFDKEYYEGVVTATVETKLVEQNMRLPAGTYLLSTTQKNAALAFVALEPEYMDSFASFGIIPVSKGDQYPIFRLK", "text": "FUNCTION: Extracellular metalloprotease that contributes to pathogenicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M14 family."}
+{"protein": "MDRTATASWEVMSRRGEQQQQLMMQAPASHNGGSGGGEPARSRWAPKPEQILILESIFNSGMVNPAKDETARIRRLLERFGAVRDANVFYWFQNRRSRSRRRARQLQQACGAALHQLPSAAAAAGAGGGGDYYHHHHQPSSSPFLMHGGGGGGVVTSTTAAPAVAASGHFLADEVDGGGDDDLFAISRQMGLMARHGGGDHHYSSYADSDATQLSYQPTGTIQVFINGVAYDVPSGGALDMAGTFGRDAMLVHSSGEVLPVDEHGVLINSLQMGECYYLVSKSI", "text": "FUNCTION: Transcription factor which may be involved in developmental processes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WUS homeobox family."}
+{"protein": "MGKYSIDPENPIKSCKARGSYLRVHFKNTRETAQAIKKMHIRKAYRYLKDVIAKKQIIPFRRFCGGVGRKAQAKAFKHTQGRWPVKSAEFLLGLLKNAESNADVKGLDVDSLVIDHIQVNRAPYMRRRTYRAHGRINPYMSSPCHIEMIVSEKEQVVPRAEEEVEVKKVSKKKLAREKLKARE", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL22 family."}
+{"protein": "MLAMKLFTCFLQVLAGLAVHSQGALSAGNNSTEMEVVPFNEVWGRSYCRPMEKLVYIADEHPNEVSHIFSPSCVLLSRCSGCCGDEGLHCVALKTANITMQILKIPPNRDPHSYVEMTFSQDVLCECRPILETTKAERRKTKGKRKQSKTPQTEEPHL", "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": "MAVALWYCPPANSPCYDTVNSLILSLQTLFPDAVLFEPHVTITSQLRCDSADDAAAVLAAACAALRACRPQLDARGSPVVRFDAVAVGRRYFDKVHLACAHDRFLYGVAQVIRELFVQDPPDPAAAADWVHSSFRPHLSLVYSDLYHVDQALLRVLRQRIGDALGAALLPHPPAPGLQALWALQPPLDGWSIPGSFKVVRCEGPVRDWHVLAAADL", "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": "EAGIECDCGSPENPCCDAATCKLRPGAQCADGLCCDQCRFIKKGKICRRARGDNPDDRCTGQSADCPRNRFHA", "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": "MISMNRLSILLFVFAFGLTMMSNTALSYKHSVWIRNFLHEKNDLIIHCKSTNHDMVYHRLHPTGSYHLLVDDDSDYFWCHLWQGPNFKHHQVFGVNHGDVWEAREDGIYFSQIKYARDLRQHVFMYGWNVPLTLSRASSLGLCCVSLSLLLSSLVLFYFYLVLVLKFIFFIMNFKNLIFICVGIFLFSL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant self-incompatibility (S1) protein family."}
+{"protein": "MPFTLGQRWISDTESELGLGTVVAMDARTVTLLFPSTGENRLYARSDSPVTRVMFNPGDTITSHEGWQLHIDEVKEENGLLVYVGTRLDTEETNVTLREVLLDSKLVFSKPQDRLFAGQIDRMDRFALRYRARKFQSEQYRMPYSGLRGQRTNLIPHQLNIAHDVGRRHAPRVLLADEVGLGKTIEAGMILHQQLLSGAAERVLIIVPETLQHQWLVEMLRRFNLRFALFDDERYTEAQHDAYNPFETEQLVICSLDFARRNKQRLEHLCDAEWDLLVVDEAHHLVWSTDAPSREYMAIEQLAERVPGVLLLTATPEQLGMESHFARLRLLDPNRFHDFEQFVEEQKNYRPVADAVAMLLAGNKLSNDELNRLGDLIGEQDIEPLLQAANSDRDDAQAARDELVSMLMDRHGTSRVLFRNTRNGVKGFPKRELHTVKLPLPTQYQTAIKVSGIMGARKSPEDRARDMLYPEQIYQEFEGDTGTWWNFDPRVEWLMGYLTSHRSQKVLVICAKATTALQLEQVLREREGIRAAVFHEGMSIIERDRAAAWFAEEDTGAQVLLCSEIGSEGRNFQFASNLVMFDLPFNPDLLEQRIGRLDRIGQAHDIQIHVPYLEKTAQSVLVRWYHEGLDAFEHTCPTGRAIYDSAYASLINYLAAPEETDGFDDLIKSCREQHEALKAQLEQGRDRLLEIHSNGGEKAQQLAQSIEEQDDDTNLIAFAMNLFDIVGINQDDRGDNLIVLTPSDHMLVPDFPGLPEDGCTITFERDVALSREDAQFITWEHPLIRNGLDLILSGDTGSSTISLLKNKALPVGTLLVELVYVVEAQAPKQLQLNRFLPPTPVRMLLDKNGNNLAAQVEFETFNRQLSAVNRHTGSKLVNAVQQDVHAILQLGETQIEKSARALIDNARREADEKLSGELSRLEALRAVNPNIRDDELAAIDSNRQQVLESLNQAGWRLDALRLIVVTHQ", "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": "MPQAKLKDLLEFPCAFTFKVVGANRADLIDDVVVVVQKYAKGDYNPRQQLSSKGTYNSVSIDIIAEHIEQVEVLYVELAKIDGVRMVL", "text": "SIMILARITY: Belongs to the UPF0250 family."}
+{"protein": "MFGTPSRRTFLTASALSAMALAASPTVTDAIAAPGPDSWSALCERWIDIITGRRAARTSDPRARAIIAKTDRKVAEILTDLVSGSSRQTVLISADLRKEQSPFITKTARAIESMACAWATPGSSYHKDPEILSACIEGLRDFCRLRYNPSQDEYGNWWDWEDGASRAVADVMCILHDVLPPEVMSAAAAGIDHFIPDPWFQQPASVKPTANPVQPVVSTGANRMDLTRAVMCRSIATGDEKRLRHAVDGLPDAWRVTTEGDGFRADGGFIQHSHIPYTGGYGDVLFSGLAMLFPLVSGMRFDIVESARKAFHDQVERGFIPVMYNGQILDDVRGRSISRINESAAMHGISIARAMLMMADALPTHRAEQWRGIVHGWMARNTFDHLSEPSTLVDISLFDAAAKARPVPESSTPSYFASMDRLVHRTADWLITVSNCSDRIAWYEYGNGENEWASRTSQGMRYLLLPGDMGQYEDGYWATVDYSAPTGTTVDSTPLKRAVGASWAAKTPTNEWSGGLASGSWSAAASHITSQDSALKARRLWVGLKDAMVELTTDVTTDASRAITVVEHRKVASSSTKLLVDGNRVSSATSFQNPRWAHLDGVGGYVFATDTDLSADVATRKGTWIDVNPSRKVKGADEVIERAYASLHVTHHDRPVAWALLPTASRSHTMALATRPGVEPFTVLRNDATVQAVRSAGALLTKDPTVVTTLAFWKPATCGGVAVNRPALVQTRESANQMEVVIVEPTQKRGSLTVTIEGSWKVKTADSHVDVSCENAAGTLHVDTAGLGGQSVRVTLARQVTQTPSGGGRHDRA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 8 family."}
+{"protein": "MNLASISQSYMSHNENERSIVPYIPPPYHPTAPALAVSASQMETMSLGILNQAMSSSAGASGALKDEKAAYGAVAEALRDPEPIRKIKRQVGIQTLKTLKVELSGMRRKKLILKIIMFICANVTMATSLVGGMSIVDEDIAKHLAFDGKGDWVSKTVHGLNLLCTTMLLAANKISEKVREEIARTKRDIAKRQSYVSAATMSWDGDSVTQLRDVKYGD", "text": "FUNCTION: May play a role in the release of virions from infected cells. SIMILARITY: Belongs to the orbivirus NS3 family."}
+{"protein": "MSEIVSVSGGPTKPEIIAVSLSKLGLKDGDRFADVGCGTGSVSIEAARIARNLTIYAIDARKEALLATETNFKNFGIENARILAGEASDILGSEKTIDSIDCAFVGGTKNIGSILAKLVEKKARSIVVNAVRIETVVRTIEAMKSLDIFDEVIHVAVSRSFPIAGETMFKPENPVYIVVGKKQS", "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": "MTWGFLKQGIFRERSRVGKQKFYHCVSRYFHYLPPVLAILLPVGSWPFLSEQQWRYSYFLFPVVSSLGWLFAIGLRERQLRAAAGQLLETKIRKLTERDEGLKNIRETIEKRQKEANRLKLHNDKLVERLGQAREVVIQAKGRYDHMEEKSRKLHEENKQLQMQLEAAVRERNEKILENQELRQELKETLAYQQELHDEYQATFVEQHNMLDKRQAYIGNLEAKVQDLMCELRNLLQLEVGAKTELPGRPMASRDVVAQLVLEFRKIVFRVETTEAADSLTALRYTRTDPSAHNYSLACRQLFDDLREENLGMLFIYAPFAQRVLFANALFKDWTGHGLEDFLNKEGDVVLEGFAQWERDLLTESRTERSGKIVIKTKAFGATPFYYCVVTLDKGPLAEHVLGVLYPAKASFFTNLSYI", "text": "SIMILARITY: Belongs to the UPF0242 family."}
+{"protein": "MGNLCSLFTPPKPVKKRKPITKRQSSIGASSSGSGLNSNRWNNRVRSSSSRRDNKFEDALIQEHALAAAAVLFRQQNGGGGSLPFDRSASQRYQGSCSKKNQLPRSSSSRSRSSTDPLLQPHQFLNQGIKLDDLETNHFVLVHGGSFGAWCWYKTIALLEEDGFKVTAIDLAGCGINSININGIASLSQYVKPLTDILEKLPIGEKVILVGHDFGGACISYAMELFPSKISKAVFLAAAMLTNGQSTLDMFSLKAGQNDLMRKAQIFIYTNGNENPPTAIDLDKSLLKDLLFNQSPSKDVALASVSMRSIPFAPVLEKLSLSDANYGSVRRYYIETLEDNAIPVTLQENMINSSPPEKVYRLKGADHAPFFSKPQALHKLLLEIARISPA", "text": "FUNCTION: Putative methylesterase. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase family."}
+{"protein": "MKSILQQPIWRYYDQSISAKQRSPLESFATDDTLCQLVGQLVSPPTIRTWVHEASVVLGIQDHRLPYVQQGMDLLESRGYQPIVRNSGGLAVVLDEGILNISIVLSEQMDSLSINDGYDVMVDLVKGLFPEVAEKIEAYEIVGSYCPGSYDLSIEGKKFAGISQRRLRQGVAVQIYLCIEGSGSQRAALIRDFYEESLQQEETKFNYPQIVPEVMASLSELVDLHLTVEGVVIRLQQLLHRLAGEVHPESFHDEELTLYGFYLKRVFERNAKMLERHE", "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": "MYYGFDVGGTKIEFGAFNEKLERVATERVPTPTDDYPLLLETIAGLVAKYDQEFACEGKIGLGLPGMEDADDATVLTVNVPAAKGKPLRADLEAKIGRSVKIENDANCFALSEAWDEELQDAPSVMGLILGTGFGGGLIYEGKVFSGRNNVAGELGHMRLPLDAWFHLGDNAPLLGCGCGKKGCLDSYLSGRGFELLYAHYYGEEKKAIDIIKANAAGDEKAAEHVERFMELLAICFGNIFTANDPHVVALGGGLSNFELIYEEMPKRVPKYLLSVAKCPKIIKAKHGDSGGVRGAAFLNIKG", "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": "MSNTDSVRVKLLFFAKSRELAGVSGTDDFLVPHAEIKCSELLDLICNRYNLSIIRNNVILAHNEQYCADLSETIRIRNGDELAVIPPISGG", "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": "MYAELKDGMGTRDVFDGWNVQKVWQKEDEAWINRTQNSGMKLQNPAFAQGKNWERPVICQDIFWSRDGSSIVTIHDDYGIRQYVMSLEGNTDQLVPYSRMFKSQSIVTGRVHPLYSLYNDTEDFNVLLTACKDLPLQMYSLQDTEGPCLNHYNVINNETGNWEIPHAINWSNEDHFLIGSVKNRVSLFSCYRSSPIWTSQSKRGNSTSKSIVSCFSERPYGEFSNAKHTIFGTYKNELHLLDHRTQHPQFLHRSAQGRGYIQLLESFNGHYLYALKRNTNLIDVLDTRESHRPVNQLQLPFTMGNQKHKASITSTNGLTIGTDDGKIVCWSSNAIEFGVIDRNGLTCDNGAGEKPELTHEMGLNSSRINIVQQSPTDFGVCALSYSPDKMTYRPDVHASSGIYVTELTTDWFGL", "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": "MGFGTLVAIGVIVFAVVVITIILCLTCSCCCLYKACRRPQPVVTTTTATTVVHAPYPQQQGVPPSYPAAPYQGYQPVAIQPQPGMPVAPYPAQYPPPYPMQPPDPPAYHETVAAGAGAPYPISQPPYNPAYMDPQKPTY", "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": "MISRYSRRPVSHNLEIRGLSRSCLDQHPLPEEADNGTAHSSRLLHNLQEDMSLYSRSEESSASSVRSGCQTLTTDDTVPSWSGIHSYTGTGISTERSSVFSWGYDEFDKAASRQVQQMFEEIDELLYERKCETQLKGLQDECQEWAFRFPHLRILGTQVVCPTDEGFQWYATPAQTPSPSSSFQSKENTVSELYVQGRRAVLCRPTVEVTNPSIRTSGNNEDELPSVIEAEGLIEEYLAYDCRDMDEECEREYVSRRRRRRRCLPPVSPYRCRQEAVLDMLFDDVWRELIGWIEELVRKHWDGYVLDDEKSTVALSPKCPDPQNPFMLPSNVSTVLPPLSQTRTQQLTTNLQAQTSRVPVGPAVAHHNLNDLIMIHGIPLQQRNLGTLDRLNQSDCRDSEDKVSHRPGSSVIPAGKPRPRRALDQSTSSLTRPPQSARRRNPPPRNLMPITSSVTQPITTMEEVVRGTRLTTPSDRLTSPPMHLSRNTLLPPIGTGDIDHVYSGQHTRLIQKQRGSSSRAHSAVTDEGISLQPRDKLHLLDVFSRPNTTHTFRSDTPYHRSFTGIDNIGQGRPGRASVGVDSLGIGVTGISLGISSSSFIDSFSHRPMGHFPIGHEEEPDAKASGQARSHNRGGSTARSSRPGL", "text": "SIMILARITY: Belongs to the FAM149 family."}
+{"protein": "MSELLATYILADPGCDAEKRAEQIAIGLTVGSWTDLPLLKQEQLKKHKGRVVNVEETESELGEKQATVTIAYPEANFTNDIPAVLTTVFGKLSLDGKIKLADLEFSRSFKQSLPGPKFGVYGIRKKIGEFERPLLMSIFKGVIGRDMEDLKEQLRQQALGGVDLIKDDEILFETGSAPFEKRITEGKKVLEEAFEETGRKTLYAVNLTGRTMELKAKARKAAELGADVLLLNVFAYGLDVLQSFAEDDDIPLPIMAHPAVSGALTSSPHYGFSHSLLLGKLNRYAGADFSLFPSPYGSVALPKRDALAIYDECTKEDVFKPTFAVPSAGIHPGMVPLLMKDFGIDHIINAGGGIHGHPNGAAGGGRAFRAVIDAVLEAEPVEEKAKRSPDLKLALEKWGRVEVSV", "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": "MEELILGVVQGLTEFLPISSSGHLAIFTAIFNATPDVGYFAFLHLATFLAVLIFVKSEVFEIVNGISKKDKEYINLASKLVLSTIPAVIVGLCFGDFIESVFSSTFLIGVFLSITGILMLLSDKLNKNLKTIKSIPYLDALIVGIFQAFSVLPGISRSGTTLFAALFLGMKKEDAVKYSFLMSLPVTFGAGILELQKVAFSTEQIFGFFISFLTGLLGLYLVKKMVIGGKLKIFGYYCVLASFFVLMFL", "text": "FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UppP family."}
+{"protein": "MGILDGESKKARVGMERQDERLRSLSEANDRLMAKNHALAKALTRATQELTKAKAQLNQLAGPPMTFATMIRVHAANTDEQGVQHASAEVISGTRRMIVPVAANVQASRLEAGRTVLLNENMVIVDQHDTDTLGSVRTVRQVLDDGRLLVADSGGNVTLVRRAGTLAKENVNTGDRVSVDSSVRFALTLIPVEDDADLVLEETPDVTFDDIGGLDEQIERIRDAVQMPFLHRELFERYDLKPPKGVLLYGPPGNGKTLIAKAVANALAEGSGAGSGVFLSVKGPELLNKFVGESERLIRMIFRRARERAADGRPVIVFIDEMDSLLRTRGSGVSSDVETTIVPQFLSELDGVESLDNVMVIGASNRIDMIDPAVLRPGRLDVKIRVERPKAKQAEQIIRHYLTDDLPLTPGIEAKALTSVLVADIYAVSEHRHLCDVCDEHGQWSPVYLADVVSGAVLKNVVDRAKTKAVKISIESAEPAAIGVNLLAKAVQEEFEETRDAVLDADPVQWSRINGFEAGHVTRIRPTAQ", "text": "SIMILARITY: Belongs to the AAA ATPase family."}
+{"protein": "MSLLTEVETYVLSIVPSGPLKAEIAQRLEDVFAGKNTDLEALMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQRRRFVQNALSGNGDPNNMDRAVKLYRKLKREITFHGAKEVALSYSTGALASCMGLIYNRMGTVTTEVAFGLVCATCEQIADSQHRSHRQMVTTTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAEAMEVASKARQMVQAMRTIGTHPSSSAGLKDDLLENLQAYQKRMGVQMQRFK", "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": "MEPSTAARAWALFWLLPPLLGAVCASGPRTLVLLDNLNVRETHSLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDLGQHTLIVADTENLLKAPTIVGKSSLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVIFSGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVFKEEGVLRVGPVSHHRVGETAPPNAYTVTDLVEYSIVIQQLSNGKWVPFDGDDIQLEFVRIDPFVRTFLKKKGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYERFIPSAYPYYASAFSMMLGLFIFSIVFLHMKEKEKSD", "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": "MTHPSDTGSAPVLALRDVSKSFGAVRALRDVSLELFPGEVHALAGENGAGKSTLIKTLAGVHRPDAGHVLLDGAPVVFHGPGDARDAGIAVIYQEPTLFPDLSIAENIFMGRQPRRALGRIDHKATHDATAALMLRLGVELDPDRPARGLSIADQQIVEIAKALSFDARVLIMDEPTAALTGSEVARLFGVVRTLRDQGAAVLFISHRLEEIFHICARVTTLRDGAWIASEPLEGMTEDDLVRRMVGRDLDELYPKQEVTPGERALSVRRLTREGVFTDVSFEVRRGEIVALAGLVGAGRTEVARAVFGVDRWDAGEVEVDGKPLVNGAPSTAMAAGLALVPEDRRAQGLVMDMSIERNIGLTGLRTTVKAGLVDRGAERSRSLDWAVKLQVKYARIADTVATLSGGNQQKVVLAKWLATGPKVLIVDEPTRGIDVGTKAEVHRLLSQLAADGVAVLMISSDLPEVLGMADRVLVMHEGRLTAEISRTDATEETVMAAATGRAAA", "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": "MKPVPLVLLLTSVLLTTHIPLSTCRPRDLSLMNSQLDDVLLNGAGDGAMSYLVGEKLLQYLQRNLGAQKAGGVLHLPHFPTAQLHSPHEDNSLEELTEFSKRNDDPPISIDLTFHLLRNMIEMARNENQREQAGLNRKYLDEVGK", "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": "IIGDEINGAITTADNIAGKIGII", "text": "FUNCTION: May act as an antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Frog skin active peptide (FSAP) family. Septenin subfamily."}
+{"protein": "MTQFASPVLHSLLDTDAYKLHMQQAVFHHYYDVQVAAEFRCRDDDLLGIYADAIREQVDAMQHLRLQEDEFQWLSGLPFFKPDYLNWLREFRYNPAQVCVTNDNGKLNIRLTGPWREVIMWEVPLLAVISELVHHYRSPNAGVDQALDALESKLVDFTALTANLDMSRFHLMDFGTRRRFSREVQQAIVKRLQQESWFVGTSNYDLARRLALTPMGTQAHEWFQAHQQISPDLATSQRAALAAWLNEYPDQLGIALTDCITMDAFLRDFGIEFASRYQGLRHDSGDPVAWGEKAIAHYEKLGIDPLTKTLVFSDNLDLPKAVELYRHFASRVQLSFGIGTRLTCDIPQVKPLNIVIKLVECNGKPVAKLSDSPGKTICHDKAFVRALRKAFDLPQVRKAS", "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": "HAGDLGNIVAGSDGV", "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": "MTSKISTTYEEEGRQSKIQPRAFVITRSGPSSKSSSFSARQSYASSRQSITPGVYQQLSSSGITDFRGTREKEKREMQNLNERLASYIEKVHFLDAQVKKLEAENEALRNRKSESLQPIRDAYENELAQARKVIDELSSTKGVSEAKVAGLQDEIASLRELIVTYENQSKDYRKKIESLGNQIGEYEGELHTLRIRCGSLEDENAKVRELLDKIQEQNRRLRADLDTETAAHIEADCLAQTKTEEAEFYKDLLDQLELLKPEPIQIKGMDYAEFWKSELSKCVREIQSAYDEKIDMIQQDTEAKYSAQLNSLRSGNVKDGMQLQHVQEEVKKLRTQAGEKNAMYAELAAKFASLQAERDSIGRQCSELERELEELRIKYNQDIGDLSNELSAVLAQLQILTDAKITMELEIACYRKLLEGEESRVGLRSLVEQAIGVQGRGTASLKDTIQQSTSSGSMTIQRSSKGPIAFNSVDQSGSNIVIENTTSGARAKTQSLRGWRIDKTVAGRVAASIQLKDYEIPPNTKYTIWAKGAKDRATADNEQIADIFSLGVGSCTWTIVDEAGNEKATLIAKFSG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the intermediate filament family."}
+{"protein": "MDQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHATQAFHLTNDTLGAFMRDNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDVVYSIDGGFEAWQRQFPAEVAYGA", "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": "MVQRGSKVKILRPESYVYNEVGTVAS", "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": "MGVLDIVKAGVISGDELNKVYDYAKAEGFAIPAVNVVGTDSINAVLEAAKKVNSPVIIQFSNGGAKFYAGKNCPNGEVLGAISGAKHVHLLAKAYGVPVILHTDHAARKLLPWIDGLIEANAQYKKTHGQALFSSHMLDLSEESLEENLSTCEVYLQKLDALGVALEIELGCTGGEEDGVDNTGIDNSKLYTQPEDVALAYERLGKISDKFSIAASFGNVHGVYKPGNVSLQPEILKNSQKFVKDKFALNSDKPINFVFHGGSGSELKDIKNAVSYGVIKMNIDTDTQWAFWDGVREYELKNRAYLQGQIGNPEGDDKPNKKYYDPRVWLRSGEESMIKRLEIAFEDLNCINKN", "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": "MATKNSPSPKPMGTAQGDPGEAGTLPAPEAAGIRDTGSTQLKTKPKKIRKIKALVIDLGSQYCKCGYAGEPRPTYFISSTVGKRSAEMAADAGDNFKETYVGHELLNMEASLKLVNPLKHGVVVDWDCIQNIWEYIFHTAMKIMPEEHAVLVSDPPLSPTSNREKYAELLFETFGIPAMHVTSQALLSIYSYGKTSGLVVESGHGVSHVVPISEGDLLPGLPSRVDYAGCDLTNYLMQLLNEAGHKFSDDHLHIIEHIKKKCCYAALLPEEEMSLGLDELHVDYELPDGKIITIGQERFRCSEMLFKPSLVGCTQPGLPELTATCLARCQGTGFKEEMAANVLLCGGCTMLDGFPERFQRELSLLCPGDSPTVAAAPERKTSVWTGGSILASLQAFQQLWVSKEEFEERGCAAIYSKC", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family."}
+{"protein": "MERALGVGIGPLAAGTVGLLILLKVIQRLRRRPNIQDKVVVITGASSGLGKECARVFHAAGARLILCGRDQRRLQEVVEELGNKTYGKTKTYTPCTVTFDLSNTSVVCSAAAEILKRHGHVDVLINIAGVSYRGNILDTHVSVQREVMETNYFGPVALTQAILPSMVDRGSGHIVVISSVQGKISIPYRSAYAASKHAMQAYYDCLRAEVDSLGLHVSVLSPGYVRTNMSINAVTGDGSKYGVMDRTTATGADPVDVAKDILKAVCQKKKDVVMAGLGPTTAIYLRTLWPALYFRVMASRARKQTGKEE", "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": "MWRYISKHAYSRKFRNSHDSALLGFSQYSSSFGKTRPLQCLCEESTTHPNLGLSQNSIFSRISRKVRHLEGICEESSKNPHLGLSQNSTFSSVKGDFRICGKRGSGSLGRLRSYGSAAEAIVSTSEEDIDEIQELIEEMDKENEALKANLQPKQPKTIGGMGVGKYNFLRRRQIKVETEAWEEAAKEYQELLMDMCEQKLAPNLPYMKSLFLGWFEPLRDAIAAEQKLCDEGKNRGAYAPFFDQLPAEMMAVITMHKLMGLLMTGGGTGSARVVQAASYIGEAIEHEARIHRFLEKTKKSNALSGDLEETPGDMMKERERLRKKVKILMKKQKLRQVRKIVKQQDDEKPWGQDNLVKVGCRLIQILMETAYIQPPNDQLDDGPPDIRPAFVHTLKTVETMKGSRRYGVIQCDPLVRKGLDKTARHMVIPYMPMLVPPQSWLGYDKGGYLFLPSYIMRTHGAKQQREAVKRVPKKQLEPVFQALDTLGNTKWRVNRKVLGIVDRIWASGGRLADLVDREDVPLPEAPDTEDEAEIRKWKWKVKGVKKENCERHSQRCDIELKLAVARKMKDEDGFYYPHNLDFRGRAYPMHPYLNHLGSDLCRGILEFAEGRPLGTSGLRWLKIHLANVYGGGVDKLSYEGRVAFSENHLEDIFDSAERPLEGKRWWLGAEDPFQCLATCINIAEALRSPSPETAISYMPIHQDGSCNGLQHYAALGRDKLGAAAVNLVAGDKPADVYSGIAARVLDIMKRDAAKDPANDPNVMRARLLINQVDRKLVKQTVMTSVYGVTYIGARDQIKKRLKERGVIEDDNELFAAACYAAKTTLTALGEMFEAARSIMSWLGDCAKIIAMENHPVRWTTPLGLPVVQPYRKLGRHLIKTSLQILTLQRETDKVMVKRQRTAFPPNFVHSLDGSHMMMTAIACKESGLSFAGVHDSYWTHACDVDQMNKILREKFVELYDAPILENLLESFQQSFPDLQFPPLPERGDFDLREVLESPYFFN", "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": "MTVAETRARNLSIPAPSQITRPALEGVKETMVLNMGPHHPSTHGVLRLVVELDGETVVDVAPDIGYLHTGIEKTMESKTYQKAVVLTDRTDYLAPLSNNLSYVLAVEKLLGCEVPERATVARVLLVELQRIASHLVWLGTHALDLAAMSVFLYGFREREQILDIFELVSGARMMTSYFRVGGLAYDLPIEFDAAVEAFLAIMPGRIDEYEALLTDNPLWIERTQGIGAIDSEAAIALGLTGPGLRATGVAWDLRKTMPYCGYETYSFAVPTATHGDIYDRYLVRMAEMRESVSICRQALQRLRDIGPGPYMTLDRKIAPPPKSEITQSMEALIHHFKLWTEGFKPPRGDALAAVESPRGELATYIVSDGSAKPYRVHFRAPSFVNLQSLPHMARGHLVADLVALIASLDPVLGEVDR", "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": "MNERTSDAFDALLVLSFGGPEGHEEVRPFLENVTRGRGIPPERLDDVAVHYHHFGGISPINALNREIIANVEKELASRNRELPVYFGNRNWKPFGNEAAEQMADDGVKNALVLATSAWGGYSGCQQYQEDIRGMIKHLESQGQSVTFTKLRQFYDHPRFVSTMAQLVQDSYAKLPDELRDEARLVFTAHSIPLAADNAAGTPQDGSLYSSQVKEASALIAKAVGVSDFDVVWQSRSGSPHTPWLEPDIVDHAVELNEKGQKALVVCPVGFISDHMEVIWDLDSELMEEAEKRNMVVERVATVGPTDEFAALVVDLIEEAELKRVIERLGKLPARGSSINGAPCSEGCCGTAKHQTARVNPNARSAAPAAN", "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": "MSVTLINNENNARYEFETIECTRGPKAVDFSKLFETTGFFSYDPGYSSTAGCQSKISYINGKKGELYYRGHRIEDLVAKYKYVDVCRLLLTGELPKNQDESLEFELELRHRSFVHESLLNMFSAFPSNAHPMAKLSSGVSILSTLYSTHQNMHTEEDYQTMARRIVAKIPTLAAICYRNEVGAPIIYPDIARSYVENILFMLRGYPYSRLKHTTQGEVGITPLEVEAFDKILTLHADHGQNASSTTVRNVASTGVHPYAAISAGISALWGHLHGGANEKVLLQLEEIGDVKNVDKYIARVKDKNDNFKLMGFGHRVYKSYDPRAKILKGLKDELHQKGVKMDERLSEIAAKVEEIALKDEYFIERNLYPNVDFYSGTILRALKIPVRFFTPVFVIGRTVGWCAQLLEHVKSPQARITRPRQVYVGD", "text": "SIMILARITY: Belongs to the citrate synthase family."}
+{"protein": "MQVNENPNKVPVELNRTSLYLGVLSVLVLGILFSSYFFN", "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": "MRKGNSLHRNLDTIFGNEVYSNNLTHQEFLSVRNQHLWEKLRDIPLYEAVHTWLSSLTNHTSRSYRGSILALERIGLISLKMPLQQFALLNHNIILDAIKQIPTTVVCWSEGTKQVRAACYISLTKFLNRVTSGIISIAQPSHQESNKTFYKIRDLVKTNAMNQVERVLFLEELSKINYRDWLIAQTILQGAKRVTEALSVTTDHICFENGVISFNQIKSRGVFKTTIITYPQKFMKLLQDYVGERKGLVFITKKGRGVGLKQLAGTFAKAGIKAHIPFKVTPHVLRATAVTEYKKMGCSDSDIMKITGHSSSKMIYAYDKSTIADNASKKVSLI", "text": "SIMILARITY: Belongs to the 'phage' integrase family."}
+{"protein": "MSESLHLTRNGPILEITLDRPKANAIDAKTSFAMGEAFLNFRDDPELRVAIITGGGEKFFSAGWDLKAAAEGEAPDADFGPGGFAGLTEIFDLDKPVIAAVNGYAFGGGFELALAADFIVCAENASFALPEAKLGIVPDSGGVLRLPKLLPPAIVNEMVMTGRRMSAEEALRWGIVNRVVSQSELMDSARELAQQLVNSAPLAIAALKEIYRATSEMPVEEGYRYIRSGVLKHYPSVLHSEDALEGPQAFAEKRDPVWKGR", "text": "FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
+{"protein": "MEKSWFNLILSKGELEYRCGLSKSMDSRLGPVENTTVNEDPTRNDTDKNIHDCSDSSSYYSKVDHLVDVKDIRNFISDDTFLIRDSNQDRYSIYFDSENQIFELNNDHSFLSELESFFYSYHNSSYMNNGSKNDEPHYHFNLYDNDTNCGWNNHINSCIDSYLRSQICIDSSILSGSDNSNDNYISNYICGEGGNSSEGKNFDIITRENGNDLTLKESSNDLDLYKDLWVQCECENCYGVNYKKSLNSKMNICEQCGYHLKMRSSDRIELSIDPGTWGPMDEDMISLDPIEFQSEEELYKDRIDFYQRKTGLTEAIQTGTGQLNGIPIAIGVMDFQFMGGSMGSVVGEKITRLIEYATNNFLPLILVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYVSILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNKTIPEGSQAAEYLFHKGLFDPIVPRNPLKGVLSELVQLHGFFPLNQNSIK", "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": "MADAITVLTAIGITVLMLLMVISGTAMIVKELNPNDIFTMQSLKFNRAVTIFKYIGLFIYIPGTIILYATYIKSLLMKS", "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": "MDRIIEKLDRGWWVVSHEQKLWLPGGELPHGEAVNFDLVGQHALHIGEWQGESVWMVRQDRRHDMGSLRQVLDQDPGLFQLAGRGIQLAEFYRSHKFCGYCGHPMHASKSEWAMLCSHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPQSLMTAFMADYADGDIVVDKKELLTADWYRYDNLPLLPPPGTVARRLIEDTVAMCRAEFE", "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": "MSQLLTARQAEELHKSIIAYLASVNLTESSAALRAELGDSVSIDDATLKKYEGLLEKKWTSVVRLQKKNQDPTSWLPRSPARHILEGHREPVTCVAFHPVFSSLASGSDDTTIKIWDWELGELERTVKGHTKAVLDVDYGGPRGGTLLASCSSDLTIKLWDPSDNYKNIRTLPGHDHSVSSVRFIPSGAAGSPMSGNLLVSASRDKTLRIWDVTTGYCVKTLSGHVDWVRAVAPSLDGRFLFAAGDDRIPRLWDLSSAETKSTFLGHEHVIECVAIAPAASYPHLAVLSGLKKPPPVSSSAEFFATGSRDKTIRLWDSRGNLIKTLVGHDNWVRALAFHPGGKHLLSVADDKTIRCWDLTQECKCVRVISDAHGHFVTCLRWAPPLIKDGGANGESETNGAPAATATTNGVRPDPNAANKISIRCVIATGSVDRKVRIFAT", "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": "MARAKKSKDSQPLDLNNCQPLEHLQPVPKTRSASIISVESTDSEGGVVEVLAPPQVREFDDLTAFEAFVRDETWDNDFDYFHGRLNYYPPFIMKECHDNLDKIKPTANKNSRKFKRNLQHHVARHLIKDLEKCCGYELHMDKFDTIETPNRITWKFKDESDHGFSKEEEDEYNRHWRLELSVSCNNENPMVEVDYKAIPI", "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": "MTNNLKKTVYLIRHGQAQHNVGPDEDHNIRDPVLTSEGIEQCEALAKELESKQIPIDGIVCSPMRRTLQTMEIALKKYLAEGGPDKVPVYISPFFQEVGHLPCDIGLELDKLNKLYPKYNFQSCQDGIYPEKRDIYASDVTISAIRSKEALEYLAALPQQQIAVITHSAFIRFLLKKMVKAADIDFLPPQLSFKNCEFRIYDLVQTTTGELKLVESSSA", "text": "SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
+{"protein": "MSAAAASSAAGDSAKQPLLHHQRGNPPHVASVSSPSLPSAPPGALAGGRRFPGGLDVPNLKKRGGGTRSWIRVEAATASVQTLEVDKATMMRRCELPARDLRLLDPLFVYPSTILGRERAIVVNLEQIRCVITADEVLLLNSLDSYVLQYAAELQRRLLQRAEGDELPFEFRALELALEAACSFLDAQAAELEIEAYPLLDELTSKISTLNLERVRRLKSRLVALTRRVQKVRDEIEQLMDDDGDMAEMYLSEKKLRTEASFYGDQSMLGYNSVGDGTSFSAPVSPVSSPTESRKLEKAFSLCRSRHDSVKSSDNTATEHIQELEMLLEAYFVVIDSTLNKLTSLKEYIDDTEDFINIQLDNVRNQLIQFELLLTTATFVVAIFGVVAGIFGMNFETSVFSIQNAFQWVLIITGVIGAFIFCGFLWFFKYKRLMPL", "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": "MRILKPHLRSTSIQCYLCLLLNSHFLTEAGIHVFILGCISAGLPKTEANWQFVIRDLEKIDNIIQSIHIDTTLYTESDAHPSCKVTAMKCFLLELRVISLEFKHHVLNETVENLIFLANDRLSSNGDITETGCKECEELEEKNIKEFLQSFVHIVQMFINTS", "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": "MNHLQRRQLFLENLLVGVNSTFHQMQKHSISTCCRSLQRILDHLILLQTTHSPVFRLDRMQLRQMQTLACLWIHRHNHDLQVTLDAIKWISP", "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": "MSSKSQLPFSTRASNHPNPLARKLFEVAEAKKSNVTVSADVTTTKELLDLADRLGPYIAVIKTHIDILSDFGPETINGLNALAEKHNFLIFEDRKFIDIGNTVQKQYHGGALKISEWAHIINCAVLPAEGIVQALAETAQAEDFPHGSERGLLILAEMTSKGSLATGEYTSASVDYARKYPSFVLGFVSTRALTEVSSTVTAADNEDFVVFTTGVNLSSKGDKLGQQYQTPQSAIGRGADFIIAGRGIYTAPDPVEAAKQYQQQGWEAYLARVGGASQ", "text": "SIMILARITY: Belongs to the OMP decarboxylase family."}
+{"protein": "MAFEELLSQVGGLGRFQMLHLVFILPSLMLLIPHILLENFAAAIPGHRCWVHMLDNNTGSGNETGILSEDALLRISIPLDSNLRPEKCRRFVHPQWQLLHLNGTIHSTSEADTEPCVDGWVYDQSYFPSTIVTKWDLVCDYQSLKSVVQFLLLTGMLVGGIIGGHVSDRFGRRFILRWCLLQLAITDTCAAFAPTFPVYCVLRFLAGFSSMIIISNNSLPITEWIRPNSKALVVILSSGALSIGQIILGGLAYVFRDWQTLHVVASVPFFVFFLLSRWLVESARWLIITNKLDEGLKALRKVARTNGIKNAEETLNIEVVRSTMQEELDAAQTKTTVCDLFRNPSMRKRICILVFLRFANTIPFYGTMVNLQHVGSNIFLLQVLYGAVALIVRCLALLTLNHMGRRISQILFMFLVGLSILANTFVPKEMQTLRVALACLGIGCSAATFSSVAVHFIELIPTVLRARASGIDLTASRIGAALAPLLMTLTVFFTTLPWIIYGIFPIIGGLIVFLLPETKNLPLPDTIKDVENQKKNLKEKA", "text": "SUBCELLULAR LOCATION: 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": "MALLQLERISAQYPGSPEPVLSDISLTLGPQQLLVALGPSGSGKTSLLNLIAGFVEPSAGRITLDNVPVKGPSAERGVVFQDDALLPWQDVLANVAFGLELAGVAKDKREQRAREMLALVDLSGFEHRRIWQLSGGQKQRVGLARALAADPRVLLMDEPFGALDAFTREQMQELLLQVWQRTAKPVFLITHDIEEAVFLATDLILLAPNPGQIVERLHLDFGQRYAAGESARAIKSDPRFIETREHVLAKVFSQRSAVQRQERA", "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": "MAQKMLEDQDMLDQLLSGVHDSDLDFSESEEEEEEEESSSESESDEDSDMEVEPARQEAGPPEQCQQQPQQRAREQQPPPQQQQPQQREQGPPQQQQQQRTPKRGEESGDARPRARAPSGDAGPGPSGQARLPQQQQPQQPQQPPPKPPRQEVTVRAPGDRQQPQSQAAQPIPVIGGGCAPFQLRAPIAAAAATGWGGEQAPAQPLFQHVSPLNRRGDEDRRSGRDRRRREGRERDRESRSKGRNWYRPYPRGSSGARREGGGRDAGQGQGTRNPGPSQGGCEAGPSQAQAAQAARAPRQEQGERRQMLPQGQNLGPRPQQCPPQQCPPQPCPPFPLEALPILRAKFEPSCAVSYTNLVKSIQKIAMPPFLMRRREASPPCHFSKIPQATPGLVIPAAARTGEAKFEKFTDAFVQKVIDRGMSPQDCINKTVSLRKLDAKFDPLKTFTAKTVNFGQWLDVRKDSIINSGMSTQVVFLEELCAWAKLNLQHGCNLEERDLILHTAETVCSQLMYKLKPIMSCLEPNKPYASMAKQMAYLVCGAGRIQDAGMLLREVKVGSPLTMLVAFSLCVPVMITCRNRNPSLFNYCKSFLDMYQPGLLCALFNTMTSKLNTTCTEEECYASVRAAIGSVVNTRGLLFVPGI", "text": "SIMILARITY: Belongs to the herpesviridae UL69 family."}
+{"protein": "MATPVRDETRNVIDDNISARIQSKVKTNDTVRQTPSSLRKVSIKDEQVKQYQRNLNRFKTILNGLKAEEEKLSETDDIQMLAEKLLKLGETIDKVENRIVDLVEKIQLLETNENNNILHEHIDATGTYYLFDTLTSTNKRFYPKDCVFDYRTNNVENIPILLNNFKKFIKKYQFDDVFENDIIEIDPRENEILCKIIKEGLGESLDIMNTNTTDIFRIIDGLKNKYRSLHGRDVRIRAWEKVLVDTTCRNSALLMNKLQKLVLMEKWIFSKCCQDCPNLKDYLQEAIMGTLHESLRNSVKQRLYNIPHNVGINHEEFLINTVIETVIDLSPIADDQIENSCMYCKSVFHCSINCKKKPNRELRPDSTNFSKTYYLQGAQRQQQLKSSAKRTKVLEQDTKKVKQSVQQQKTGNY", "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."}
+{"protein": "MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEGGSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSVCTYENWAKAKRCVVCDHPRPNNIEAIELAETEEASSIINEQDRARWRGSCSSGNSQRRSPPATKRDSEVKMDFQRIELAGAVGSKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEVRLLNRPSAFDVGYTLVHLAIRFQRQDMLAILLTEVSQQAAKCIPAMVCPELTEQIRREIAASLHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELATRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYTRWKDWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYGNRGAGANLNTDDDVTITFLPLVDSERKLLHVHFLSAQELGNEEQQEKLLREWLDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDRYRQIRPCTSLSDGEEDEDDEDE", "text": "FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys- 29'-linked and 'Lys-33'-linked diubiquitin (PubMed:22157957, PubMed:23827681, PubMed:25752573, PubMed:25752577). Also cleaves 'Lys- 63'-linked chains, but with 40-fold less efficiency compared to 'Lys- 29'-linked ones (PubMed:18281465). Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription (PubMed:18281465). Acts as a regulator of autophagy by mediating deubiquitination of PIK3C3/VPS34, thereby promoting autophagosome maturation (PubMed:33637724). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987). Required in the stress fiber dynamics and cell migration (PubMed:21834987). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Enriched in punctate localization in the cytoplasm. SIMILARITY: Belongs to the peptidase C64 family."}
+{"protein": "MGPEKFARAKPHINIGTIGHVDHGKTTFTAAITATLANDGESFAKAYSDIDGAPEERARGITINTAHVEYQTRDRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPHIVVFLNKQDQVDDDELLELVELEVRELLSTYDFPGDDIPICPGSRLQAIEAISSNPTLKRGDNPWVDKIYALMDAVDAYIPTPERDVEKTFLMAIEDVFSITGRGTVATGRIERGVIKVVDNVEIVGIGDTKTTTITGIEMFQKTLEEGFAGDNVGILLRGVTRENIERGMVLAKPGTITPHTNFESEVYVLTKEEGGRHTPFFTGYSPIFYVITTDVTGSIDQFTADDGSIVEMVMPGDRIKMTAELIYPVAIEEGMRFVIREGGRTIGAGVVSKIVK", "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": "MLLALLRQHIRPYRRLVAMLMMLQLVSTLASLYLPTVNAEIVDDGVAKGDTATIVRLGAVMLGVTGLQVLCAIGAVYLGSRTGAGFGRDLRSAMFEHIITFSERETARFGAPTLLTRSTNDVRQILFLVQMTATVLVTAPIMCVGGIIMAIHQEAALTWLLLVSVPILAVANYWIISHMLPLFRRMQSLIDGINRVMRDQLSGVRVVRAFTREGYERDKFAQANTALSNAALSAGNWQALMLPVTTLTINASSVALIWFGGLRIDSGQMQVGSLIAFLSYFAQILMAVLMATMTLAVLPRASVCAERITEVLSTPAALGNPDNPKFPTDGVTGVVRLAGATFTYPGADCPVLQDISLTARPGTTTAIVGSTGSGKSTLVSLICRLYDVTAGAVLVDGIDVREYHTERLWSAIGLVPQRSYLFSGTVADNLRYGGGPDQVVTEQEMWEALRVAAADGFVQTDGLQTRVAQGGVNFSGGQRQRLAIARAVIRRPAIYVFDDAFSALDVHTDAKVHASLRQVSGDATIIVVTQRISNAAQADQVIVVDNGKIVGTGTHETLLADCPTYAEFAASQSLSATVGGVG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MSVNDYSLFDEATDELVSSERKLIAVDCHDDDSQVINVKVEDIFCDMSDKVVLKLQFRLCYKYRKLLDITLLGCRMKVYTELKTPSERSLKSILQKKMNIISDGNYLIGIRMFFININQLINTCKWITRIEDVYPICTLYHVNNTPVIDI", "text": "SIMILARITY: Belongs to the nanovirus U1 protein family."}
+{"protein": "MADLEEGFALTAVPLGSGPDGPLGVEQSGKTDQFLVTDSGRTVILYKVSDQKPLGSWSVKQGQIITCPAVCNFQTGEYIVVHDNKVLRIWNNEDVNLDKVFKATLSAEVYRIHSIQGTEPLVLFKEGAVRGLEALLAEPQQKIETVISDEEVIKWTKFFMVFRHPVLIFITEKHGNYFVYVQKFNSRILSKYTLLLGQEEKCVIQSFSTSVGRKFISLMSLSSDGCVYETLIPIHPSEPEKNQRLVQSQLLKSVVSGSARNGVALAILDQDHIAVLGAPLPASKECLSVWNTKFQTLQTSKELPQGTSGQLWYYGENLFMLHGKFLTVVPFKCEVSSLAGALGKLKHSQDPGIHATPHFVNWETSQGCGLGSQNSEQSKRILRRRKVEVSVQPEVPASTQLLATIQKDSEKHIEVELRKFLATKRTPDFHTIIGDVIIGLLGRCKAEPSFYPCNCLMQLVQTHVLSYSLCPGLMEFALEKTDVQILQLCLQQFPDIPESVTCACLKVFLSIGDDTLQDTDINMESVSDYMDPVQDGEMEEQTAFLQNGFSPEEDNCDSCAQKLKEKPQAAADESTSCPVTPKRAALLNAVLHSAYSETFLLPHLKDIPAQHSTLFLQYLYFLYLKCSENATMTLPGTHPPTLSQIMDWICLLLDANFTVVVMIPEAKRLLLSLYKFVKSQISICSELNKIEVSFRELQKLNQEKNNRELYSIEVLELF", "text": "FUNCTION: Ribosome biogenesis factor. May be required for both optimal rDNA transcription and small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus."}
+{"protein": "MSDSVAGDFPPDPLLASGAFISSAGDGTLDSSAKRRPIQGGIGISGSGESVRIGMANGTDQVNHQTESKSRKRAAPGDNWLPPGWRVEDKIRTSGATAGSVDKYYYEPNTGRKFRSRTEVLYYLEHGTSKRGTKKAENTYFNPDHFEGQGSNRVTRTATVPPPPPPPLDFDFKNPPDKVSWSMANAGEEGWIPNIGDVKVQDSVRRDWSTAFTFITSRNPSKVSA", "text": "FUNCTION: Transcriptional regulator that binds CpG, CpNpN and CpNpG (N is A, T, or C) islands in promoters regardless the DNA methylation status. Plays probably a role in gene silencing. May associate with histone deacetylase proteins (HDAC). Required for nucleolar dominance that consist in the silencing of rRNA genes inherited from one progenitor in genetic hybrids. Recruited to rRNA genes in a DRM2- dependent manner. Maintains gene silencing by interacting with RNA binding proteins (e.g. NTF2, RPS2C, HDA6 and AGO4) and by regulating DNA methylation status (PubMed:28229965). SUBCELLULAR LOCATION: Nucleus Chromosome Nucleus, nucleolus Note=Associated with heterochromatin, and particularly at perinucleolar chromocenters and nucleolus organizer regions (NORs) in a DRM2-dependent manner."}
+{"protein": "MSGCGPWLPHDLLWGMTPAQLPGDAPAWAHAVLEAGQPVVVRRALTAPGQVAVGLRGVSREQRYPALLDLQAVQRGVRPEQLCHVPPQGPWPALQALQHLRDELDAQEWIWGVSGSAGFELASGVAALHQHSDLDLILRTPELLPRARARELLALLDGAGCPVDMQLQVPGGALALREWAGPAARVLLKSASGARLVSDPWNPQEQAA", "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": "MGFWENNKDSITSGLKSAGKYGYQGTKYVAKTGYKASKKHYNNSKARRERKSGKKNSSDEEYESEDEMEYERKPTDIRSLKDPKSFPPPPLKPGQKTYAGQQQQQMPNGQASYAFQGAYQGQPGAGSMEQSQYAQPQYNQYPQQQLQQGVVPQQPPIYGEQVPPYGSNSNATSYQSLPQQNQPQYAIPSQVSLNSASQQSTGFVSQNLQYGTQSSNPAPSPSFQNGLQCHQQPQYVSHGSTNLGQSQFPSGQQQQPTTQFGQQVLPSPAQPHPQPQQQQQGQPLPPPRGQVILPAPGEPLSNGFEQQQQQQQQQQQQQPLNQNNALLPQMNVEGVSGMAAVQPVYGQAMSSTTNMQDSNPSYGASPMQGQPPVGGQPPVPVRMQPQPPQPMQQGNIYPIEPSLDSTSSTPHFEVTPFDPDAPAPKPKIDIPTVDVSSLPPPPTHRDRGAVLHQEPAPSGKIQPNTTSSAASLPAKHSRTTTADNERNSGNKENDESTSKSSILGHYDVDVNIMPPPKPFRHGLDSVPSEHTRKNALERAVPILPPRNNVEPPPPPSRGNFERTELVLSTNAANVQEDPISNFLPPPKPFRHTETKQNQNSKASPVEIKDEVLPGHPSEEDRNVEPSLLPQSKPQSKSQSQFRRAHMETQPIQNFQPPPKPFRRSQSSNSSDSSYTIDGPEANHGRGRGRIAKHHDGDEYNPKSENSTENGRLGDAPNSFIRKRAPTPPAPSRSEKLHEGAITSEFDSSKDANKYEKSIPPVTSSIQAQQSTKKAPPPVVKPKPRNFSLKANEYPKELTREATGQDEVLNSITNELSHIKLRKTNVNLEKLGGAKKVKDSSPVPSDLDEKYVSASGSITPPRPPPSRSSPKKVPPVVPKKNDNLKKKPPVVPKKKPLLKSLEPRPIEMERAYSGDISAADDNLNPFERYKRNVVPQEDDRLHKLK", "text": "SUBCELLULAR LOCATION: Membrane raft; Peripheral membrane protein Note=Localizes within detergent-insoluble glycolipid-enriched membranes. SIMILARITY: Belongs to the AIM3 family."}
+{"protein": "MEYRKRVDALVFFSLLLLGYFAAHAHGKAKEGIMQGNGARCVVGFPPCKDNKCYCCIGGRTHARYSTMAECSHACF", "text": "SIMILARITY: Belongs to the MEG family."}
+{"protein": "MAARMAFADKPNHFINFPLAQFSGFMGKYLKLQSQLVEMGLDCKLQKVPHVSITLLDIKADQYKQVEFAIQEIIDDLAAYEGDIVFDNPHMLGRCLVLDVKGFEELHEDIVEILRRRGCTADQSRQWIPHCTVAQFDEEKEIKEMQFYFKLPFYLKHNNLLTDARLELVKIGSSKVGGFYCSELSIWCGERLCYKPPTPKFSDIFGYCCIDKIRGDLEIGDLPPDDEEAWAELSYHYQRNTYFFRHVHDNSIYFRTVCRMKGCMC", "text": "FUNCTION: Not essential for virus replication in transformed murine cells. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the coronaviruses ns2a protein family."}
+{"protein": "MQILKIPWFGHKTENKTVECYAVTINKDGTRLASGGLDGNVKIWDLTTINVFYKMADQPHKSKKDSTSTKLEESLPDKSLRRPLCSMSRHNGVVTSLKFSPDGRWLASGSDDKICLIWEKDNTQIAKSFGTDEHDLEHWTVRKRLVAHDNDIQDICWSPDGNLLVTVGLDRSVIIWNALTFEKIKRYDIHQSMVKGIVFDPANKFFATASDDRTVRIFRYYKKLNEYNNYEFQMEHVVVDPFKKSPLTSYFRRMSWSPDGQHIAVPNATNGPVPSVAIINRGNWGSDISLIGHEAPVEVCSFSPTLFQIADTPANEEIKFQTVVATGGQDRTLAIWSTCNSRPIVVCSDIVDSSITDICWSPDGETLYFSCLDGSITGVKFGARELGQPVKEDLIDQQLNRYGADRESTILPESVEQLQLEEQSKDSRAISIRRMMPIQEAKPEQTPPISTPASAAIDIERLRKQTVTMTKSGKKRVAPLLVSTSAAPKNVLQKPLEKKRRTKSSSKISQAAYLLPKMGVQTTVHGIKKKAESMSNDTEVEENNDNDDIGENVMANTNSVSDAALKRQRNRRKRKLMELKYPSSFKYISNLPEGLFNNHTLQNIEINKIYKAHSKHKDISAEISSSTAVEIDEDLVFSVVFRVFDHMRKENEVLGQTSGRIRTTIEVRNGKPWDDDISDRDFDDATKVIVTEEGNDKREYCLFFPFRVQHVLPIILNDVLKYYVLCSFHGSVQIISADTGSYRCPTFELGESVVTMRHSQGYMLVLTSSGLFYSWDLKAMKVTMTGISIAAILNNYEIGGKIVVSPIVRGLEINPQDGSPLVLLDMTNDIYGYSIDLQCWVKTVDSWYYGVGADKDLDVVLTGLVKKSKMSYEEDKVTEKIFTYKFDSSNDLEDAMRKRGQELLDLI", "text": "FUNCTION: Required for replication-independent chromatin assembly and for the periodic repression of histone gene transcription during the cell cycle. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat HIR1 family."}
+{"protein": "ANPCNPAQLTPCAGPALFGGAVPPACCAQLRAQQGCLCGYARSPNYGSYIRSPNAARLFAICNLPMPRCR", "text": "FUNCTION: Potential phospholipid transfer protein. SIMILARITY: Belongs to the plant LTP family. B11E subfamily."}
+{"protein": "MSEIILTPKEQPEVPLEAPNIKPDVFAGKSIDEIKNIQIMYGNEVVKLGDFFEVSGEPADAASDIKIIIDGDVYNTKRIGQEMTAGEILVKGNVNMYVGAGMKGGRITVEGNAASWAGQDMRGGELEILGNAADYVGSSYRGDWRGMSGGVITVHGNAGNEIGEYMNGGKIIIKGDVNIMPGIHMNNGLIIIEGNAVARVGGEMAGGTIIVKGMIQEFLPGFKYLGVEKDIEVNGETFPGAFYKFEGDHAIKGAKGIVYAAVGCNGHIEP", "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: Belongs to the FwdC/FmdC family."}
+{"protein": "MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR", "text": "FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser- 392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Interaction with SIRT6 prevents translocation into the nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily."}
+{"protein": "SGSAKVAFSAIRSTNH", "text": "FUNCTION: The cerebellin peptide exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release. FUNCTION: Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber- Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post- synaptic components. On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2. NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). NRXN1-CBLN1-GRID2 complex mediates the D- Serine-dependent long term depression signals and AMPA receptor endocytosis (By similarity). Essential for long-term maintenance but not establishment of excitatory synapses (By similarity). Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells (By similarity). SUBCELLULAR LOCATION: Secreted Postsynaptic cell membrane."}
+{"protein": "MAENRCLIRLNRHTLAVTIIFKKQCADYGPRLTMQGSKHGSDGAQYAFPTWRKCLILTDACFVVFTSSSALCSMFPATAQIAAELSTTVETLHIANACVQIAMGISLFVWQPIRSFIGRRNAYLLAILTLFCFSIGAALAINASMFIAMRIIVGITGTFLLVAGQELLAETFDPVARGAAFGYMQIGNTTGLTIGPCIGGIIVSFTRWRIIYWLQVGLAGLGLILSSLFIPNEKGKSETVHGSISRLAALNPVNLLKPLVYPNIVITGSERCPEIQHILTSKQDIACGFLVFFQFIVLTSIPHIINPRFHFTTPLVSGLFYLAPGGGFVLGSLVGGIVSDRTTKRYIAKRNGIRLPQDRLNGSLPMWLGFMPVSMVIYGWTLDLEVGGMAVPIISVFFAAGGIVVAFNGLNTYTAEALPEHRFAAISGKYIIQYGFGAVSTAAVVPLIDAIGVGLVFTICAIISVIGGVGVFLVAKYGLQMQNHRFSSRV", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of 2,4'-dihydroxy-3'-methoxypropiophenone. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family."}
+{"protein": "MKILFVLISILYAVYCFSSEEDVDSAYLANELEPVEDINSEQYAALEPKEEQERSCAGMGQDCKDDCDCCLNIATCNCWFGRYFCSCTFGDYQTCLRKKGKCKRNRPQSCPRSNLNRKKG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 05 (agouti) family."}
+{"protein": "MKVGVLTGGGDCPGLNAVIRAVVRKGVQEYGYDFTGFRDGWRGPLEGDTVPLDIPAVRGILPRGGTVLGSSRTNPLKQRDGIRRIKDNLAALGVEALITIGGEDTLGVATRLADEYGVPCVGVPKTIDNDLSATDYTFGFDTAVGIATEAIDRLHTTAESHMRVLVVEVMGRHAGWIALHSGLAGGANVILIPEQRFDVEQVCSWVTSRFRASYAPIVVVAEGAMPRDGDMVLKDESLDSYGHVRLSGVGEWLAKQIEKRTGNEARTTVLGHVQRGGTPSAFDRWLATRFGLHAVDCVHDGDFGKMVALRGTDIVRVPIAEATARLKTVDPALYEEVGVFFG", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily."}
+{"protein": "IKCTLSKDCYSPCKKETGCPRAKCINRNCKCYGCS", "text": "FUNCTION: Blocks voltage-gated potassium channels rKv1.1/KCNA1 (IC(50)=13 nM), rKv1.2/KCNA2 (IC(50)=16 nM) and rKv1.3/KCNA3 (IC(50)=2 nM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 06 subfamily."}
+{"protein": "MAEPNQHYEVIIAGGGIAGVTLALMFEKLDISYFLLEGRDTLESDRGAGIGLQPNGLRILDQLGLVEDIEEATIPLEKWFSYDSEGNLMNDSDAMGQYRDKIGYPVAFIERRKLLPIMVRHIQRTECVKTSARVASIEESEDHVTVTTTDGLSLTADIVVGADGVRSAVRTHIDSKLPEPLTADDYISVACSTVYGMSAPTEGIAPGERFAVYRENQTVIGFTGKDGIVFWFVFENLNRNVPLSQAPRYTEAEAEALCLSVAHTQVTPKLKFGEIYKNSVVAVKIGVEEGVAKGWHTDRAVIVGDAACKTTPAGGQGANQAIESCAVFVNKLMAARKASQSGDKLSSDVVKSVLASYAQERAQPATTALERSQMVGKALLCTPGPATTLVKDMLKLSNEDWLLRAFMALSAAPYLEDVELTARGHLYNKAVEEARAEMARRQRVAKEVKEAEEKESKQAASIKESEQRNEFVGLRNPVQAATGVVEVGS", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:19400779). The first stage is catalyzed by the polyketide synthase bik1, which catalyzes the formation of the intermediate SMA76a also knowm as pre-bikaverin (PubMed:19400779). FAD- dependent monooxygenase bik2 might then be responsible for the oxidation of pre-bikaverin to oxo-pre-bikaverin which is in turn methylated by the O-methyltransferase bik3 to me-oxo-pre-bikaverin (PubMed:26382642). A further cycle of oxydation and methylation by bik2 and bik3 leads to the final product of bikaverin, via a nor-bikaverin intermediate (PubMed:19400779, PubMed:26382642). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
+{"protein": "MRWVWALLKNASLAGAPKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKNAMRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVPSTEPKNTSTYRVS", "text": "FUNCTION: Kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the PDK/BCKDK protein kinase family."}
+{"protein": "ITFSKIYRSCKSDSDCGNQKCARGRCV", "text": "FUNCTION: Not toxic to mice by intracerebroventricular injection. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the u18-CNTX family."}
+{"protein": "MDSASADASVTGSGNAKGSSAERVNGGGKFYKLEILVSDPQKRAGEAGLGPYVSYQISTRTDNPSYHGNQKASFDDIIVVHRRYNDVVLLHDILQNDHPTCIIPPLPDKKVLQYIAGDRFGRRFTQRRCHSLQNFLRRVSQHPILSTSKVLEIFLVGNEWDTYRKNIAGTLQNAQKEDVTDAVMNAFKKVHNQNEEFTEIRDRSDKLDNSVNRINKVFHRVVKKNEAIIEDYSKLGLTLQELQELVSSDNDKLADSLKVFIEGVTQFSYGLQDLNMFIDYEYLIDLKDLSHYIGSMKQTMRLKDQKQIDYEELSDYLTKSIKEKNNLISGYGGGNFLTSKLEELAGYNQEASRRDKINKLESTISSLTTELETAKKVADTFEQETLKEVKKFEEIKNDELKISLNNLADENIKFYERMLETWEKVDQSLR", "text": "FUNCTION: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans- Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy. SUBCELLULAR LOCATION: Cytoplasm, cytosol Preautophagosomal structure membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Note=Endosome and other perivacuolar punctate structures. Associates to phosphatidylinositol 3-phosphate, necessary for peripheral membrane localization to the perivacuolar punctate structures. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "MIADDDEKWLAAAIAAVKQNAFYMQRAIDSNNLKDALKFSAQMLSELRTSKLSPHKYYELYMRVFNELGTLEIFFKEETGRGCSIAELYELVQHAGNILPRLYLLCTIGSVYIKSKDVTATDILKDLVEMCRAVQHPLRGLFLRSYLAQVTRDKLPSIGSDLEGDGDAHMNALEFVLQNFTEMNKLWVRMQHQGPSREKEKREKERNELRDLVGKNLHVLSQLEGVDLGIYRDTVLPRILEQVVNCKDELAQCYLMDCIIQVFPDDFHLQTLDVLLGACPQLQPSVDIKTVLSGLMERLSNYAASSVEALPNFLQVEAFSKLNYAIGKVVEAQADLPAAASVTLYLFLLKFTLHVYSDRLDYVDQVLGSCVTQLSATGKLCDDKAAKQIVAFLSAPLEKYNNVVTILKLTNYPLVMEYLDRETNKAMAIILVQSVFKNNTHIATADEVDALFELAKGLMKDFDGTIDDEIDEEDFQEEQNLVARLVNKLYIDDPEEMSKIIFTVRKHIVAGGPKRLPLTIPPLVFSALKLIRRLRGGDENPFGDDASATPKRILQLLSETVEVLSDVSAPDLALRLYLQCAQAANNCELETVAYEFFTKAYLLYEEEISDSKAQVTALRLIIGTLQRMRVFNVENRDTLTHKATGYSARLLRKPDQCRAVYECAHLFWADECENLKDGERVVLCLKRAQRIADAVQQMANASRGTSSTGSVSLYVELLNKYLYFLEKGNQQVTGDTIKSLAELIKSETKKVESGAEPFINSTLRYIEFQRQQEDGGMNEKYEKIKMEWFE", "text": "FUNCTION: Plays a role in vesicular protein sorting. Component of the membrane-associated retromer complex which is essential in endosome-to- Golgi retrograde transport. Also involved in the efficient sorting of seed storage proteins (By similarity). The VPS29-VPS26-VPS35 subcomplex may be involved in recycling of specific cargos from endosome to the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the VPS35 family."}
+{"protein": "MNPAHLLVLSAVCVSLLGAANIPPQHLDLYQFKEMIRYTIPCEKTWGEYADYGCYCGAGGSGTPIDALDRCCYVHDNCYGDAANIRDCDPKTQSYSYKLTKRTIICYGAAGTCARVVCDCDRTAALCFGNSEYIEGHKNIDTARFCQ", "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": "MDPCDCAKTGPCNCGATCKCTNCQCTTCKKSCCSCCPSGCSKCASGCVCKGNSCGSSCCQ", "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": "MLFLHSVVQGTGTLCTLAAWILLALVMTGCQSSTTSKFQLFSLATNVAQINVGYFNMCVLSANATLICKPQFTGCPGLTSISLTDVRSKFLINEVHPWMIVFSFCVCGVSFLMGVVSSLPLIGRLEFLRNIRISLSFFSFFSILVTALFAHVAVSSFVMAVGNGTQNRVTASLGKKAMIFLWCSMGLVTLTGITDSIILLVTSRTKKIRKTILEKSKVLTPSSSFSSKSSTTKY", "text": "FUNCTION: Cell membrane protein which plays a relevant role in coordinating membrane organization and cell wall remodeling during mating. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell tip Note=Localizes to the tip of shmoos which requires fus1, actin and lipid rafts. SIMILARITY: Belongs to the SUR7 family."}
+{"protein": "MSHDWTDNRKNLMLFAGRAHPELAEQVAKELDVHVTSQDAREFANGEIFVRFHESVRGCDAFVLQSCPAPVNRWLMEQLIMIDALKRGSAKRITAVMPFYPYARQDKKHRGREPISARLIADLLKTAGADRIVTVDLHTDQIQGFFDGPVDHMRGQNLLTGYIRDNYPDGNMVVVSPDSGRVRIAEKWADALGGVPLAFIHKTRDPRVPNQVVSNRVVGDVAGRTCVLIDDMIDTGGTIAGAVALLHNDGAGDVIIAATHGVLSDPAAQRLASCGAREVIVTNTLPIGEDKRFPQLTVLSIAPLLASTIRAVFENGSVTGLFDGDA", "text": "FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) and of the decaprenylphosphoryl-arabinose (DPA), an essential precursor for the mycobacterial cell wall biosynthesis. Catalyzes the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P) to yield phosphoribosyl diphosphate (PRPP) and AMP. It can also use GTP, CTP and UTP as diphosphoryl donors (PubMed:22745722). 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. SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily."}
+{"protein": "MATTRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGAAGGGLPVSTVREVALLRRLEAFEHPNVVRLMDVCATSRTDRDIKVTLVFEHIDQDLRTYLDKAPPPGLPVETIKDLMRQFLSGLDFLHANCIVHRDLKPENILVTSNGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPREVSLPRGAFSPRGPRPVQSVVPEMEESGAQLLLEMLTFNPLKRISAFRALQHSYLHKEESDPE", "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 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": "MSGSKGVWGAPPGNNNRQLYSLDAGSSGSGVSASSAQRHSILDPHDSVMDLLNGQQSCAFDSRLIQNQDLIDRKGKSNNIDHNDINTHTHSKGLTDSWQAIDRDEYSFLNAGNHNNYHNTSNGDFNQQFGGVLSSDTSEEEVEINAAPSPNLSASQQHNQFLAYPLSSTGFGDQGNSETTVHQFSDGDPVKSTKTGQFSKAELGAGTGEDETIMVNLGHSWAGSFFVMPKLSLSESMKRFKILILSDGDSANSFYNRLSRYHRLMFDVGKLNEASKEEALKYTAFMIIFSDSKKVTTILNRMWKKYGDFTLIPICQKGQKQSVTEKVKTFANSNKIKLMSYPVVISDHYEIHGLLRHLHSLYVEVDSDYETDIPKKTKPRKGAKKKPAPHLAKRWWFWPISIALGVGIGCCVTFYFSKFETSSYNSSVGVIQTADKEIDAIVDAIEGNSPSILEESSPQSISDFLGQVCKLVKDTAIQINELLKQFLSAHLMTSAWIQSIGKEFMQPDSQSTISKVTALDLVMF", "text": "FUNCTION: Mitophagy-specific receptor that recruits the autophagic machinery to mitochondria and regulates selective degradation of mitochondria. Mitophagy 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. Recruits ATG11 to the surface of mitochondria. Promotes also autophagy- dependent peroxisome degradation (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Vacuole membrane; Single-pass membrane protein Preautophagosomal structure membrane; Single-pass membrane protein Note=Is recruited to the preautophagosomal structure during mitophagy and imported into the vacuole along with mitochondria during starvation. SIMILARITY: Belongs to the ATG32 family."}
+{"protein": "MKPSLLVFTVYLLWLKDCHCAPTWKDKTDMHGNLKGFSEAGDIDVDEEVKKALIGMKQMKIMMERREEEHTNLMKTLKKCKEEKQEALKLMNEVQEHLEEEESLCQVSLTDSWDECKSCLESNCMRFHTTCQPSWSSMKNTVEQFFRNIYQYLFPFDEDNEKDLPVGEKFIEEDAQVAQIENVFNQLTVDVRFLFNRSLNVFKQMQQEFDQTFQSYFMSDTDLMQPNFLPALSKEPRKKADPVQSWDIPSFFQLFYNFSLSIYHSISTTITKTLNAIEDLPKQDNDSNHGSLSSKTLPVQHRGPYGEFGQNLSECFQFHARCQKCQDYLWEDCPDVPELHTKVDEALELVNISHQQYAQVLQMTQHHLEDTTYLMEKMREEFGWVADLANQAPGAENIFDSTKMVPNIHEGNFSKQDETMIDLSILSSPNFTLKIPLEESAETSNFISYMLEKAVQHFKKHFKTW", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the clusterin family."}
+{"protein": "MNSNVENLPPHIIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIHGGACSTSSGRAEATQDLASGASASSADPMIPGVLGGAEGPMAKKHAGERDKKLAAKKKLDKKRALRRL", "text": "FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes 'Lys-11'-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 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. Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination. 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": "MLRWLIGGGREPQGLAEKAALQTIGEDQGQNPYTELLVLEAHRDIVRFLVRLDDFRFASAGDDGIIVVWNAQTGEKLLELRGHTQKITAVIAFPPLDSCEASSQLLLTASADRTVGVWDCDTGRQIQRVTCFQSTVKCLTVLQRLDIWLSGGSDLGVWNRKLDLLCKTSHLSDTGISALVEIPGNCVAAAVGRELIIFRLVTPTEELPEWDIIEVKRLLDHQDNILSLANINDTGFVTGSHVGELLIWDALDWTVQACERTFWSPTAQLDAQQEIKLFQKQNDISINHFTCDEENIFAAVGRGLYVYNLQLKRVIACQKTAHDSNILHIDKLPNRQLISCSEDGAVRMWEVREKQQLAAEPVPTGFFNMWGFGRVNKQASQPVKKQEENVTTCSLELIGDLIGHSSSVEMFLYFEDHGLVTCSADHLIILWKNGERESGVRSLKLFQKLEENGDLYPESP", "text": "FUNCTION: Non-catalytic component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy. The C9orf72-SMCR8 complex promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation. As part of the C9orf72-SMCR8 complex, stimulates RAB8A and RAB11A GTPase activity in vitro, however WDR42 is shown not be an essential complex component for this function (By similarity). The C9orf72-SMCR8 complex also acts as a negative regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and inhibiting its protein kinase activity. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MARRTDRAPLLDWAEGPGVSPAPETEQGERWAQGYGAAWERRPAGELTPLPQLEDDHIAAVFVVTFDPRSGNIVEWCRPHDIDLEGVEFKSMASGSHRVQSDFIYFRKGGFFGLACFANMPVESELERGARMKSVGVLSPSYTLLYRYMHFLENQVRHQLEIPGHYTPLEAFYEDKKGVLPVGPQTCQPALHWLPPVHKHLYPEMKITHPAGCMSQFIKFFGEQIFVLWKFALLRKRILIFSPPPVGVVCYRVYCCCCLANVTLPGIGATAPESKPFFYVNVADIQTLDGEGSYVACTTEKIFEQKQDLYDVYVDNQNVKTHREHLQPLLRVNSADKEKYQRLNDQRQLLMYSQEVDGDCGSCEEDLFILFFMEQNNRIFQTLLEVASSQDKTLTAEHARSMGLDPHGDRTFLMDLLEVYGFDLMLVIDNPCCP", "text": "FUNCTION: Probable guanine nucleotide exchange factor (GEF). May promote the exchange of GDP to GTP, converting inactive GDP-bound small GTPases into their active GTP-bound form. SIMILARITY: Belongs to the DENND11 family."}
+{"protein": "MMNFFNFRCIHCRGNLHIAKNGLCSGCQKQIKSFPYCGHCGSELQYYAQHCGNCLKQEPSWDKMVIIGHYIEPLSILIQRFKFQNQFWIDRTLARLLYLAVRDAKRTHQLKLPEAIIPVPLYHFRQWRRGYNQADLLSQQLSRWLDIPNLNNIVKRVKHTYTQRGLSAKDRRQNLKNAFSLAVSKNEFPYRRVALVDDVITTGSTLNEISKLLRKLGVEEIQVWGLARA", "text": "FUNCTION: Involved in transformation (competence for DNA uptake). SIMILARITY: Belongs to the ComF/GntX family."}
+{"protein": "MSQVVNIKPHEKYYGVYIVELEDGSVKLATKNLVPGHRVYGERLYRWGGEEYREWNLYRSKLAGALANGLAEQPIREGHSILYLGVATGTTASHISDIVGPTGRIFSVEFAPRVMREFVLVADIRKNLYPILGDARKPKEYRHLVEMVDGIYADIAQPEQAAIVADNADYFLKDNGYLLLAIKARSIDVTKEPSEIYRREINTLKERGFEIIDVVHLEPYDKDHAMVYARYKRK", "text": "FUNCTION: Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin family."}
+{"protein": "MQFRASIAAAAGLFALANARIYGIAFPETVKAGDEVEAVITTENYIQAVQDIAIAFGIATEASAYPETLGNALGSFYLGPEESNTLENITETVTIPAGLAPGQYVVAAGLYSLYGASSSPTLSHYNVTVTVGNVTSETYVGSQR", "text": "FUNCTION: Secreted effector that induces necrotic lesions in Nicotiana benthamiana (PubMed:22352720). Interacts with the host receptor-like kinases (RLKs) BAK1/SERK3 and BKK1/SERK4, inhibits their kinase activity and suppresses INF1-induced pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) in N.benthamiana (PubMed:30584105). Also interacts with the host receptor-like cytoplasmic kinase (RLCK) BIK1 and inhibits its kinase activity, thereby inhibiting PAMP-induced ROS generation (Probable). In PTI, phosphorylation relaying by RLKs and RLCKs is critical for the initiation of downstream signaling (Probable). SUBCELLULAR LOCATION: Secreted Host cytoplasm. SIMILARITY: Belongs to the NIS1 effector family."}
+{"protein": "MGRSPCCEKAHTNKGAWTKEEDERLVAYIKAHGEGCWRSLPKAAGLLRCGKSCRLRWINYLRPDLKRGNFTEEEDELIIKLHSLLGNKWSLIAGRLPGRTDNEIKNYWNTHIRRKLINRGIDPTSHRPIQESSASQDSKPTQLEPVTSNTINISFTSAPKVETFHESISFPGKSEKISMLTFKEEKDECPVQEKFPDLNLELRISLPDDVDRLQGHGKSTTPRCFKCSLGMINGMECRCGRMRCDVVGGSSKGSDMSNGFDFLGLAKKETTSLLGFRSLEMK", "text": "FUNCTION: Transcription repressor involved in regulation of protection against UV. Mediates transcriptional repression of CYP73A5, the gene encoding trans-cinnamate 4-monooxygenase, thereby regulating the accumulation of the UV-protectant compound sinapoylmalate. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MFRGATLVNLDSKGRLAVPTRYREMLYGESQGQMVCTIDLHQPCLLLYPLPEWEIIEQKLSRLSSMNPAERRVQRLLLGHASECQMDSAGRLLIANTLRQHADLKKEVMLVGQFNKFELWDEQTWYQQVKDDIDAEQSTQEPLSERLQDLSL", "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": "MEELLMSFKLKAIYPLTGGYNRHSINEFYEENVRPTEIKGLWRWWNRVLFNTVSYVKEGKLYTYDSIDRLFEDVFGSENKKSAVRLEVITDEGSDNHFELSNVELDNVIDCLKANREEKVNLDFRDNTLIIEIEGSTKIPISFKSNLDIDKIKDLVYKNKLLSFELLGFKSIKIDTKISDKEVIKEILRDLITNYLEYFNIKQEVTFTLNIYLDKSLKHKQNFDAKLKFALHSLLVFILLGGIGRKTSRGFGGLSIVNAECHDGLCGEIYGIVNNMESEKEKKDLATVLPNIIFSQTIEQYFSELINNESYKLRSWNNNSDFFVYYFIKDINILRINRIDTNVNRNGIENILNRISNELSASGNCLKDLIMQEMRRRAFALAFLGNRKFRNIHEIYPRILEFLYANYIKREFVNLIGKERRLSNLRFKILEINNTYYIISYLLYSSYLKDPNSSIKDTLYQFARCVI", "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 CMR complex degrades RNA complementary to the crRNA (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an unpaired 3' flag on the target RNA, and is stimulated by ATP. Some cleavage of the guide crRNA can also be observed. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CRISPR system Cmr1 family."}
+{"protein": "MKKVITYGTFDLFHYGHMKLLERAKNLGDYLIVGLSTDEFNLQKQKKSHHSYEHRKFILETIDLVNEVIPEKNWEQKISDIQKHDIDTFVIGDDWKGKFDFLKEYCEVIYLPRTDGISTTQIKKDMASL", "text": "FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to sn- glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit by TarB and TarF. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylyltransferase family."}
+{"protein": "MDTDLISNLPDDVLGKILSLVPTKLAAATSVLSKRWRNLLPLVDSLDFDETMLFYPDNKDGEDEASSYESGQRRRHSFSHFVDKTLALLSNAPLTEKFSLKCYHEDDGARINRWIRTALERGCLELNLEAANYLPIDSQYFTSNTLVKLTISDGFYPGGHLLPFGGVFFPALKTLTLVSVCFTSVEMINFFIHGCPALEELFLCVWMQYMSSPNVKRVTITSDFDDDIQRPSMVLKTPSLVYLDYSSYVAGNYYVVLDSLVEARLDLRLYEPIIYDEDGLWNAEVFGNITNLIEAIRTIKILHLSPSSLEVFYYCCDLPVLEDLVNLSIESDKEKGWEVMPRLLNKSPNLQTLVVKGLVHRVTYCCGDACACIRMKDREIVSCLSRCRVKVLKILGYGGSFRELKQMRHFLGKLKCLETVKVGVKEGSKKSNYLVANVMALPRVSSKCKIQFI", "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."}
+{"protein": "MAPPTRRLLNAALLLLLLLMATSHQPSGTVVARELRCQCLKTLPRVDFENIQSLTVTPPGPHCTQTEVIATLKDGQEVCLNPQAPRLQKIIQKLLKSDKSS", "text": "FUNCTION: Ligand for CXCR2 (By similarity). Has chemotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family."}
+{"protein": "MDLLGDQHFAAQQPPLFDATPSSLKEDAEELIAETIAAWDSIVSQIQTENATFLTFYSSTSPSKDLRDASTAVGRLFNDAEIELYSRQDMFERVDQVLQQQDKQVVASLDEESLYYIQKLHRRFHQNGCGIAEEGQRVTFKTKMKRLGHLVQQCNKNLNEDKSGVWLGLDELDGIPQSLISRLKQGDGENSDHLWLPTKVPFSSPAITNAKSEATRKRIYCAIQNRMEMNVPLFREIVLLRDETARLLGYADHATLKTADKMMQTPQAVEALLSEIRTAVAPLAAQDVEELLEIKRNEAESRGTTADELYFWDLAYYSARRGEAEKKISSSISEYFELNTTLAKLLSIIEHLFGTRFRRVNAAGRDEAAGSLIWHKDVQMYSVWNVDGPKEFLGTLFSATGEPPRPPTPPQSLVIPTALQGYENTDGSLFLASSALVMNYVRPTDTRPTLLSLDEVRKLFHEIGHLLHSQWTQTKYAALHHVDRDFVEAPSMMLEQFFWVEQHIKDVSFHYSHINSKMKDMWKATLVDQDETNPPEKPAQLSDDVVFNLARANQSKAIQGQLKEVFFATYDMLVHKPASRAALEALNLTELFNKTRSDVYKVRGGEALGEGWEWGHGQTVFRNILNRYDAGYYSYLLGRVFAMDIFDAGFKEKTTSREAGRRYRDMVYRVGGRQAEMKTMTDYLGHEPSTHPYLAWLQGTRIGDSGPTVAVPT", "text": "FUNCTION: Oligopeptidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock (PubMed:34608734). Within the pathway, phomG and phomG' are probably involved in the processing of the phomA and phomA' precursors (Probable). The pathway starts with the processing of the precursor phomA by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG to produce 10 identical copies of the hexapeptide Tyr-Val-Ile- Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1 and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa is required for the hydroxylation of C-beta of Tyr. PhomYc, phomYd, and phomYe are responsible for the biosynthesis of 2,3- dehydroisoleucine (dIle), 2,3-dehydroaspartic acid (dAsp), and 3,4- dehydroproline (dPro), respectively. While dIle formation by phomYc is indispensable for the installation of dAsp by phomYd, the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM acts as an S- adenosylmethionine-dependent alpha-N-methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl- phomopsin A to phomopsin A and phomopsin A further to an N,N- dimethylated congener called phomopsin E (Probable). SIMILARITY: Belongs to the peptidase M3 family."}
+{"protein": "MATVEVLTSEVVAPAEETPAGAVWLSNLDLAARRGYTPTVYFYRRNGDDEAAFFAADAVRDGLARALVPFYPLAGRLGLAGGGEDGRVQIDCTGEGAVFVTARSGHYALDDLMNEFVPCDEMRDLFVPPTPPPNPPCALLLVQVTHLRCGGVVLGMALHHSVVDARSAAHFAETWASIVRGAPAGDAPVPPCFDHKLLAARPARAVLYDHPEYKPEPAPAPAHAATASTYASAIITLTKQQVGALKAACAGASTFRAVVALVWQCACRARSLPPDKANLFLLYKYISEDWVDIQLNIQQRDNCIYAPTLKANCCFTPTF", "text": "FUNCTION: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to putrescine, to produce coumaroyl putrescine. SIMILARITY: Belongs to the plant acyltransferase family."}
+{"protein": "MLVIFLGILGLLANQVLGLPTQAGGHLRSTDNPPQEELGYWCTYMESCKFCWACAHGICKNKVNMSMPLIIENSYLTSCEVSRWYNQCTYSEGNGHYHVMDCSDPVPHNRPHRLLMKIYEKEDL", "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": "MKIYIQPLSVNSHTVEVLANSLPKIFNAEVFVLPASDVSLKCYNASRRQYNSTCILRMLPPIKVTLGVTGKDIYAKGMNFVFGEAELGGARAVLSVFRLTTADSELYRERVVKEAVHEIGHVLGLKHCSNNCVMRFSNSVQDVDRKPVSFCRECASKIRY", "text": "FUNCTION: Probable zinc metalloprotease whose natural substrate is unknown. SIMILARITY: Belongs to the peptidase M54 family."}
+{"protein": "MATIAMYLGQLLEFIHHYVGNYGVAIIVFTVFIRILLLPFYIQQMAMMKKMKEIQPLVEELKKKYGKDPQKLNMETMKLYQEKKINPFGGCLPMLLPLIILWPLFTMLRTYPAFSTASFLWMHSLAERDPYYIIPILATVTTYISSAMVATDKSQNSMNIMMSLFMGWITVTLPAGVGIYWVTSNIFQIVQQYIFMRETKTLKGES", "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 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily."}
+{"protein": "MNSWDAGLAGLLVGTIGVSLLSNGLVLLCLLHSADIRRQAPALFTLNLTCGNLLCTVVNMPLTLAGVVAQRQPAGDRLCRLAAFLDTFLAANSMLSMAALSIDRWVAVVFPLSYRAKMRLRDAAFMVAYTWLHALTFPATALALSWLGFHQLYASCTLCSRRPDERLRFAVFTSAFHALSFLLSFIVLCFTYLKVLKVARFHCKRIDVITMQTLVLLVDIHPSVRERCLEEQKRRRQRATKKISTFIGTFLVCFAPYVITRLVELFSTAPIDSHWGVLSKCLAYSKAASDPFVYSLLRHQYRRSCKELLNRIFNRRSIHSVGLTGDSHSQNILPVSE", "text": "FUNCTION: Orphan receptor. Displays a significant level of constitutive activity. Its effect is mediated by G(s)-alpha protein that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MVEPASPDSDEGISLLEFHGNGDRSWQLNFDDFQVSPEHKEKKSPSKLHNCLGCLGPEDNVADYYQQQVEMLEGFTEMDELAERGFVPGMSKEEQDNLAKSETLAIRISNIANMLLFAAKVYASVTSGSLAIIASTLDSLLDLLSGFILWFTAFSMQTPNPYQYPIGKKRMQPLGILVFASVMATLGLQIILESLRTMLSSHKEFNLTKEQESWVVGIMLSVTLVKLLLVLYCRSFTNEIVKAYAQDHFFDVITNIIGLIAVILANYIDYWIDPVGAIILALYTIRTWSMTVLENVNSLVGKSARPEYLQKLTYLCWNHHKAIRHIDTVRAYTFGSHYFVEVDIVLPADMPLQVAHDIGESLQEKLELLEEIERAFVHLDYEYTHKPEHARSHC", "text": "FUNCTION: Cation/proton antiporter involved in endogenous manganese tolerance probably through vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Prevacuolar compartment membrane. Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily."}
+{"protein": "MAGKVHRLSGEEREQLLPNLRAVGWHELDGRDAICKEFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYDKVHITLSTHDCGGLSERDINLASFIEQIAASLS", "text": "FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity (By similarity). Also acts as a coactivator for HNF1B-dependent transcription (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family."}
+{"protein": "MRVSRFNPRNRGFTLIELMIVVAIIGILAAIAIPNFIKFQARSKQSEAKTNLKALYTAQKSFFSEKDRYSDFANEIGFAPERGNRYGYRVSAAAGDCEVRNAADLPVPAAGVPCISNDSFRFGANSAIDDPTPVVARFVPQGAAGWNTTLGVQPTIADCPNCNFFAGARGNADNEATFDDWVIAGFEGSGQVGPCSEAGNVASGTPYNTRNDVACDGAAQ", "text": "FUNCTION: Major component of the type IV pili that are required for social gliding motility through cycles of extension and retraction. Extended pili are composed of thousands of copies of PilA and retract upon binding to extracellular polysaccharides and thereby pull the cell forward. SUBCELLULAR LOCATION: Fimbrium. Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the N-Me-Phe pilin family."}
+{"protein": "MTIKPSDSVSWFQVLQRGQHYMKTWPADKRLAPVFPENRVTVVTRFGIRFMPPLAIFTLTWQIALGGQLGPAIATALFACGLPLQGLWWLGKRAITPLPPTLLQWFHEVRHKLSEAGQAVAPIEPIPTYQSLADLLKRAFKQLDKTFLDDL", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0208 family."}
+{"protein": "MPTSSQDNRILVLGIGNILWADEGFGVRAVEEFHRRYAVPDNVTILDGGTQGLYLVNYLEEADRLIVFDAIDYGLEPGRLKLVRDDEVPRFTGAKKMSLHQTGFQEVISAADLLGRCPKHLVLIGCQPLDLEDWGGPLTPPVRDQIAPSIDLACQVLAEWGVTVSRRSAPLAESERLLANDIDHANYEMRPA", "text": "FUNCTION: Not known. Could be involved in the processing of hydrogenase. SIMILARITY: Belongs to the peptidase A31 family."}
+{"protein": "AIPPSYADLGKSARDIFNKGYGFGLVKLDVKTKSASGVEFTTSGSSNTDTGKVNGSLETKYKWAEYGLTFTEKWNTDNTLGTEIAIEDQIAKGLKLTFDTTFSPNTGKKSGKIKSAYKRECLNLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFSVGYKTGDFQLHTNVNDGSEFGGSIYQKVSDNLETAVNLAWTAGSNSTRFGIAAKYKLDSTASISAKVNNSSLVGVGYTQTLRPGVKLTLSALIDGKSINAGGHKLGLGLELEA", "text": "FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity). The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (By similarity). The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol (By similarity). Binding of ceramide may be required to trigger the Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane Membrane Note=May localize to non-mitochondrial membranes. SIMILARITY: Belongs to the eukaryotic mitochondrial porin family."}
+{"protein": "MKRVLVLLLALAFGHALERGRDYEKDKVCQELSTLGKDDFRSLSLILYSRKFPSSTFEQVSQLVKEVVSLTEECCAEGADPNCYDTRTSELSIKSCESDAPFPVHPGTSECCTKEGLERKLCMAALSHQPQEFPAYVEPTNDEICEAFRKDPKGFADQFLFEYSSNYGQAPLPLLVGYTKSYLSMVGSCCTSAKPTVCFLKERLQMKQLLLLTTMSNRVCSQYAAYGKEKSRMSHLIKLAQKVPTANLEDVLPLAEDLTEILSRCCKSTSEDCMARELPEHTLKICGNLSKKNSKFEECCYETTPMGIFMCSYFMPTAEPLQLPAIKLPTSKDLCGQSATQAMDQYTFELSRRTQVPEVFLSKVLDTTLKTLRECCDTQDSVSCFSTQSPLMKRQLTSFIEKGQEMCADYSENTFTEYKKKLAERLRTKMPNASPEELADMVAKHSDFASKCCSINSPPRYCSSQIDAEMRDILQS", "text": "FUNCTION: Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ALB/AFP/VDB family."}
+{"protein": "MTSKVVAAAASAFLSRTNELGNLQKSCIRILSFCESNSSRIGLHIHCPVIKFGLLENLDLCNNLLSLYLKTDGIWNARKLFDEMSHRTVFAWTVMISAFTKSQEFASALSLFEEMMASGTHPNEFTFSSVVRSCAGLRDISYGGRVHGSVIKTGFEGNSVVGSSLSDLYSKCGQFKEACELFSSLQNADTISWTMMISSLVGARKWREALQFYSEMVKAGVPPNEFTFVKLLGASSFLGLEFGKTIHSNIIVRGIPLNVVLKTSLVDFYSQFSKMEDAVRVLNSSGEQDVFLWTSVVSGFVRNLRAKEAVGTFLEMRSLGLQPNNFTYSAILSLCSAVRSLDFGKQIHSQTIKVGFEDSTDVGNALVDMYMKCSASEVEASRVFGAMVSPNVVSWTTLILGLVDHGFVQDCFGLLMEMVKREVEPNVVTLSGVLRACSKLRHVRRVLEIHAYLLRRHVDGEMVVGNSLVDAYASSRKVDYAWNVIRSMKRRDNITYTSLVTRFNELGKHEMALSVINYMYGDGIRMDQLSLPGFISASANLGALETGKHLHCYSVKSGFSGAASVLNSLVDMYSKCGSLEDAKKVFEEIATPDVVSWNGLVSGLASNGFISSALSAFEEMRMKETEPDSVTFLILLSACSNGRLTDLGLEYFQVMKKIYNIEPQVEHYVHLVGILGRAGRLEEATGVVETMHLKPNAMIFKTLLRACRYRGNLSLGEDMANKGLALAPSDPALYILLADLYDESGKPELAQKTRNLMTEKRLSKKLGKSTVEVQGKVHSFVSEDVTRVDKTNGIYAEIESIKEEIKRFGSPYRGNENASFHSAKQAVVYGFIYASPEAPVHVVKNKILCKDCHEFVSILTRLVDKKITVRDGNQVHIFKNGECSCKREETSFV", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. PCMP-H subfamily."}
+{"protein": "MNKLIRRAVTIFAVTSVASLFASGVLETSMAESLSTNVISLADTKAKDNTSHKSKKARKNHSKETLVDRKEVAPVHESKATGPKQDSCFGRMYTVKVNDDRNVEITQAVPEYATVGSPYPIEITATGKRDCVDVIITQQLPCEAEFVRSDPATTPTADGKLVWKIDRLGQGEKSKITVWVKPLKEGCCFTAATVCACPEIRSVTKCGQPAICVKQEGPENACLRCPVVYKINVVNQGTAIARNVVVENPVPDGYAHSSGQRVLTFTLGDMQPGEHRTITVEFCPLKRGRATNIATVSYCGGHKNTASVTTVINEPCVQVSIAGADWSYVCKPVEYVISVSNPGDLVLRDVVVEDTLSPGVTVLEAAGAQISCNKVVWTVKELNPGESLQYKVLVRAQTPGQFTNNVVVKSCSDCGTCTSCAEATTYWKGVAATHMCVVDTCDPVCVGENTVYRICVTNRGSAEDTNVSLMLKFSKELQPVSFSGPTKGTITGNTVVFDSLPRLGSKETVEFSVTLKAVSAGDARGEAILSSDTLTVPVSDTENTHIY", "text": "FUNCTION: In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the major outer membrane protein. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan (By similarity). SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MGIARILSAVLFLSVLFVVTFPTLLSADHHDGRIDTCRLPSDRGRCKASFERWYFNGTTCTKFVYGGYGGNDNRFPTEKACMKRCAKA", "text": "FUNCTION: Serine protease inhibitor that inhibits trypsin and blocks voltage-gated potassium channels (Kv). FUNCTION: Dual-function toxin that inhibits both serine proteases and voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family. 01 (intermediate) subfamily."}
+{"protein": "MSKGTPSMGKCHKRTHVRCRRCGRLSYNFNRKTCVACGFGRSKRLRSYKWMRKAGY", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family."}
+{"protein": "MSTADLMRRWVIALLLAAAGVAAEDSCSRNEFQCRDGKCIASKWVCDGSPECPDGSDESPETCMSVTCQSNQFSCGGRVSRCIPDSWRCDGQVDCENDSDEQGCPPKTCSQDDFRCQDGKCISPQFVCDGDRDCLDGSDEAHCQATTCGPAHFRCNSSICIPSLWACDGDVDCVDGSDEWPQNCQGRDTASKGVSSPCSSLEFHCGSSECIHRSWVCDGEADCKDKSDEEHCAVATCRPDEFQCADGSCIHGSRQCDREHDCKDMSDELGCVNVTQCDGPNKFKCHSGECISLDKVCDSARDCQDWSDEPIKECKTNECLDNNGGCSHICKDLKIGSECLCPSGFRLVDLHRCEDIDECQEPDTCSQLCVNLEGSYKCECQAGFHMDPHTRVCKAVGSIGYLLFTNRHEVRKMTLDRSEYTSLLPNLKNVVALDTEVTNNRIYWSDLSQKKIYSALMDQAPNLSYDTIISEDLHAPDGLAVDWIHRNIYWTDSVPGSVSVADTKGVKRRTLFQEAGSRPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIHSLVTENIQWPNGITLDLSSGRLYWVDSKLHSISSIDVNGGNRKTILEDENRLAHPFSLAIYEDKVYWTDVINEAIFSANRLTGSDVNLVAENLLSPEDIVLFHKVTQPRGVNWCETTALLPNGGCQYLCLPAPQIGPHSPKFTCACPDGMLLAKDMRSCLTEVDTVLTTQGTSAVRPVVTASATRPPKHSEDLSAPSTPRQPVDTPGLSTVASVTVSHQVQGDMAGRGNEEQPHGMRFLSIFFPIALVALLVLGAVLLWRNWRLKNINSINFDNPVYQKTTEDELHICRSQDGYTYPSRQMVSLEDDVA", "text": "FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane, clathrin-coated pit Golgi apparatus Early endosome Late endosome Lysosome Note=Rapidly endocytosed upon ligand binding. SIMILARITY: Belongs to the LDLR family."}
+{"protein": "MGSLDTNPTAFSAFPAGEGETFQPLNADDVRSYLHKAVDFISDYYKSVESMPVLPNVKPGYLQDELRASPPTYSAPFDVTMKELRSSVVPGMTHWASPNFFAFFPSTNSAAAIAGDLIASAMNTVGFTWQASPAATEMEVLALDWLAQMLNLPTSFMNRTGEGRGTGGGVILGTTSEAMLVTLVAARDAALRRSGSDGVAGLHRLAVYAADQTHSTFFKACRLAGFDPANIRSIPTGAETDYGLDPARLLEAMQADADAGLVPTYVCATVGTTSSNAVDPVGAVADVAARFAAWVHVDAAYAGSACICPEFRHHLDGVERVDSISMSPHKWLMTCLDCTCLYVRDTHRLTGSLETNPEYLKNHASDSGEVTDLKDMQVGVGRRFRGLKLWMVMRTYGVAKLQEHIRSDVAMAKVFEDLVRGDDRFEVVVPRNFALVCFRIRAGAGAAAATEEDADEANRELMERLNKTGKAYVAHTVVGGRFVLRFAVGSSLQEEHHVRSAWELIKKTTTEMMN", "text": "FUNCTION: Involved in serotonin biosynthesis (PubMed:17763868, PubMed:32595985, PubMed:19439571). Catalyzes the decarboxylation of L- tryptophan to produce tryptamine, which is converted to serotonin by tryptamine 5-hydroxylase (PubMed:17763868, PubMed:32595985). May play a major role in serotonin biosynthesis during senescence (PubMed:19439571). Accumulation of serotonin attenuates leaf senescence (PubMed:19439571). Catalyzes the decarboxylation of 5-hydroxy-L- tryptophan to produce serotonin (PubMed:32595985). SIMILARITY: Belongs to the group II decarboxylase family."}
+{"protein": "MAARGRLVVARGNRSFSSIIRKYSLKRETNKKVIKNVIKLLTMVILMGTVVIWIMMPTSTYKKIWLKSMRAKLGKSIYFGKPGVNLLVYMFPMILLASLGSIYLHLKKQTRVNQFNSRMDRKKIDKFGALKRPMLVKAGLGIVTVTEVMFLMMFMALLLWSLANYFYHTFVTITPQSLPTDGDNLWQARLDSIAVRLGLTGNICLGFLFYPVARGSSLLAAVGLTSESSTKYHIWLGNLVMTLFTSHGLCYCIYWISTNQVSQMLEWDRTGISHLAGEIALVAGLLMWATTFPAIRRRFFEVFFYTHYLYMVFMLFFVFHVGISYALISFPGFYIFMVDRFLRFLQSRNNVKLVSARVLPCETVELNFSKNPMLMYSPTSILFVNIPSISKLQWHPFTITSSSKLEPKKLSVMIKSQGKWSSKLHHMLASSNQIDHLAVSVEGPYGPASTDYLRHDSLVMVSGGSGITPFISIIRDLLYVSSTNAYKTPKITLICAFKNSSDLSMLNLILPNSTEISSFIDIQIKAFVTREKVSTCNMNIIKTLSFKPYVSDQPISPILGPNSWLWLATILSSSFMIFIIIIAIISRYHIYPIDQSSKEYTSAYTSLIYLLAISISVVATSTVAMLCNKKSYFKGLYQNVDALSPLMIESSPDQLLPEFTNIHYGERPNLNKLLVGLKGSSVGVLVCGPRKMREEVAKICSFGSAANLQFESISFNW", "text": "FUNCTION: Ferric chelate reductase involved in iron reduction in roots. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ferric reductase (FRE) family."}
+{"protein": "MSIQVFCDFDGTITNNDNIMSIMEKFAPPEAEEVKNRILSQELSIQEGVSQLFQLIPTNLHDEIIQFLIETAEIRNGFHEFIQFVNENNISFYVISGGMDFFVYPLLQGLIPKEQIYCNETDFSNEYITVNWPHPCDRHCQNHCGLCKSSLIRKLGDTNDFHIVIGDSITDLQAAKQADKVFARDFLITKCEENHISYTPFETFHDVQTELKHLLEVKL", "text": "FUNCTION: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5- methylthiopentene (DHK-MTPene). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MtnX family."}
+{"protein": "MYRKFGMAAMLVSILLLMTGCFNVNEPINAQSEGIWDSYFVYPLSWLMIYFANAFNGSFGLAIIVVTLLIRLLILPLMIKQLKSTRAMQALQPEMQALREKYSAKDQRTQQKLQQETMALFQKHGVNPLAGCFPVLIQMPILLAFYHAIMRTREIGDEHFLWFVLNQPDPILLPIIAGITTFLQQKMMMVTDNPQMKVLLYVMPVMILVFAMFLPSSLALYWVIGNLFMILQTYFITGPNVGAKKVAADVKVGGKKK", "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": "CCSKFGYCGLTDAYNFYTGQLTSFAHVTHETGNNAYCDPSKTQKPCAAGKKYYGRGPIQISXNYNYGPAGRAIGMDGLGNPDRVAQDALDDYKTALXFLVNGEEAVPGLSAANAVSYYRQYCQQLGVDPGPNL", "text": "FUNCTION: This protein functions both as an alpha-amylase inhibitor and as a chitinase. SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily."}
+{"protein": "MGLIMVFSSSIALGDGPKYVNAGRYYFFSRQLIFILIGLFAMAFTFLMPMKFWDSKAFWGYCICFLLLALVLVPGIGREVNYAYRWIPIGPFNFQPSEFAKLTMIVFTSAYTVRKQKSIHGLKGFLPIIIYLGIICFLLINEPDLGATMVVVAIVMSILLLGGLGFALFSLLFLSAVLLVIAAILTAPWRMQRFFAYLDPFSQEHAQNTGYQLTHSLIAVGRGGFFGEGLGLSIEKLHYLPEAHTDFIMAVVGEELGFVGIFFVILLFVLLVRKGLNVGRQAIAMDRLFNGLVAQGVVVWFGVQAIVNLGVCFGVFPTKGLTLPFISYGGSSIVISLMAFGLLLRVDYENRCLMRGQKPLGIGASYA", "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": "MAAFRDMVEVSNWLLSLLGANRAEAQQRRLLGSYEQMMERLLEMQDGAYRQLRETLAVEEEVAQSLLELKECTRQGDTELQQLEVELQRTSKEDTCVQARLRQLITELQELREMEEELQRQERDVDEDNTVTIPSAVYVAHLYHQISKIQWDYECEPGMIKGIHHGPTVAQPIHLDSAQLSPKFISDYLWSLVDTTWEPEP", "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. SIMILARITY: Belongs to the SPC24 family."}
+{"protein": "MAAAKWLIASLAFASSGLAFTPEDFISAPRRGEAIPDPKGELAVFHVSKYNFDKKDRPSGWNLLNLKNGDISVLTTDSDVSEITWLGDGTKVVYVNGTDSVEGGVGIWISDAKNFGNAYKAGSVNGAFSGLKLAKAGDKINFVGYGQSTTKGDLYNEAAAKEAVSSARIYDGLFVRHWDTYVGTQFNAVFSGSLTKNGDKYSFDGKLKNLVQPVKYAESPYPPFGGSGDYDLSSDGKTVAFMSKAPELPKANLTTSYIFLVPHDGSRVAEPINKRNGPRTPQGIEGASSSPVFSPDGKRIAYLQMATKNYESDRRVIHIAEVGSNKPVQRIASSWDRSPEAVKWSSDGRTLYVTAEDHATGKLFTLPADARDNHKPSVVKHDGSVSSFYFIGSSKSVLISGNSLWSNALYQVATPGRPNRKLFYANEHDPELKGLGPKDIEPLWVDGARTKIHSWIVKPTGFDKNKVYPLAFLIHGGPQGSWGDSWSTRWNPRVWADQGYVVVAPNPTGSTGFGQKLTDDITNDWGGAPYKDLVKIWEHVRDHIKYIDTDNGIAAGASFGGFMVNWIQGQDLGRKFKALVSHDGTFVGSSKIGTDELFFIEHDFNGTFFEARQNYDRWDCSKPELVAKWSTPQLVIHNDSDFRLSVAEGVGLFNVLQEKGIPSRFLNFPDETHWVTKPENSLVWHQQVLGWINKWSGINKSNPKSIKLSDCPIEVIDHEAHSYFDY", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S9C family."}
+{"protein": "MSSTEGKVICCRAAVAWEAGKPLVIEEVEVAPPQANVVRVKILYTSLCHTDVYFWEAKGQNPLFPRIYGHEAGGIVESVGEGVTDLKAGDHVLPVFTGECKECDHCKSEESNMCDLLRINTDRGVMLNDGKSRFSIKGKPIYHFVGTSTFSVYTVTHVGCLAKINPQSPLDKVCILSCGISTGLGATLNVRKPKKGSTVAVFGLGAVGLAAAEGARMAGASRIIGVDLNSNRFEEAKKFGITEFVNPKDHKKPVQEVIAELTNGGVDRSIECTGNIQAMIPAFECVHDGWGVAVLVGVPHKDAVFTTHPMNFLNERTLKGTFFGNYKPRTDIPSVVEKYMNKELEVDKFITHQLPFSQINKAFDYMLKGEGIRCIITMEE", "text": "FUNCTION: This protein is responsible for the conversion of alcohols to aldehydes in plants and is important for NAD metabolism during anaerobic respiration. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MAASSSSTTRLIPLLLVLTFCLALASASAWAAAAGDDDLLAAAREPGMAEWLRGVRRRIHRHPELAFEEVRTSELVRAELDAIGVPYQWPVARTGVVATIAGGGGGDGPVVALRADMDALPVQELVDWEHKSQENGKMHACGHDAHTAMLLGAAKLLQKRKNELKGTVKLVFQPAEEGSAGAYYVLQEGVLDDVSAMFGMHVDPALPVGVVAARPGPFAATSGRFLATITGKGGHAAFPHDAIDPVVAASNAILSLQQIVAREIDPLQGAVVSITFVKGGEAYNVIPQSVEFGGTMRSMTDEGLAYLMKRIKEIVEGQAAVNRCGGGVDFMEESMRPYPAVVNDEGMYAHARASAERLLGAGGVRVAPQLMGAEDFGFYAARMPSAFFTIGVGNATTSSARAAHTTHSPHFVIDEAALPVGAAVHAAVAIDYLSKHASSM", "text": "FUNCTION: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA). SIMILARITY: Belongs to the peptidase M20 family."}
+{"protein": "MKKISQSIITKRVLWTLFFLFIYCLGNQLVLPFVDLKNANIFGGAIGSLAFSSAMMGGNLRSMSLFSVGLSPWMSAMILWQMFSFSKKMGLKNLPIEIQDRRRMYLALGIAIVQSLAVSLNLPIVSGVNASLAIFMNTILLIAGTFFLVWLSDLNSLFGIGGSIVILMASMMANLPYQIMDSIEKLGIGWNVLLPLILFSLVFLYVSGVVQRARYRISINKINIHNRFKQYSYLDIMLNPAGGMPFMYAMSLVSIPQYVFMLIQFIHPENKWTSGAIKALTVGQPLWLVVYLVMLFVLGLAFAFVNVSGEQISERMRKSGEYIYGVYPGQETSAYINHLVLRLGFIGALYMLFMAGAPMLIILVNPDYLQLSMIPGTFLIFSGMIYNVNEEMKALKLNTSYTPLFENV", "text": "FUNCTION: Part of the accessory SecA2/SecY2 system specifically required for export of possible cell wall proteins. The central subunit of a protein translocation channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecY/SEC61-alpha family. SecY2 subfamily."}
+{"protein": "MSETAPAAPAAPAPVEKTPVKKKAKKTGAAAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKTAKKTPKKAKKPAAAAGAKKVSKSPKKVKAAKPKKAAKSPAKAKAPKAKASKPKASKPKATKAKKAAPRKK", "text": "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. SIMILARITY: Belongs to the histone H1/H5 family."}
+{"protein": "MLYLPCLLLWAFPQFWGQSEVQQNYTFGCLQISSFANRSWSRTDSVVWLGDLQTHRWSNDSDTISFTKPWSQGKFSNQQWEKLQHMFQVYRTSFTRDIKEIVKMMSPKEDYPIEVQLSAGCEMYPGNASESFLHVAFQGEYVVRFHGTSWQKVPEAPSWLDLPIKMLNADEGTRETVQILLNDTCPQFVRGLLEAGKPDLEKQEKPVAWLSRGPNPAHGHLQLVCHVSGFHPKPVWVMWMRGDQEQGGTHRGDILPNADETWYLQATLDVEAGDEAGLACRVKHSSLEGQDIILYWGGRQVSPVLIFLIVGVLVLVVCAVAYYIIRKRRRSYQDIM", "text": "FUNCTION: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T- cells. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Basolateral cell membrane; Single-pass type I membrane protein Endosome membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes."}
+{"protein": "MPRDRLKELQEKATVNTIHAYNYDPPARKYDVESQPLINQDADFEMFLERCSNIRGGLKSLEEDYDAVVQLHGALLSTPGADSENSNKLKSHNQMFFSKAEQIKNSLKILSEETSRIPTTACGIMRAKSDQVKSIYKTFENIMLNFNREQDEYKEKAKRKIVDYLKIRNMQLSDEEIENAVSSGNLSEVTKGVMLALNEKKALYDEVKSRADELKNLERQMGELAQMFHDLHIMVVSQAKMVDSIVNSVENATEYAKQARGNVEEARNLQKRARKMKVCIIIGSIIAVLILILFIQSAVCHFTPIC", "text": "FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones (By similarity). Acts in the intestine to regulate anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP). SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the syntaxin family."}
+{"protein": "MDKMRPRVVDVKEIEPNRKRGGDLRTLLTPVTVGATSGFMGLAIMRPGERISEHYHPYSEEFVYVVEGRLEVDLDGETFPLRADQGLMIPIDMRHRFRNVGDEEARMVFHLSPLAPKPSLGHVDTEAPAISDDVKAYPLVQEESGRPERPGVLS", "text": "SIMILARITY: Belongs to the SchB/CurC family."}
+{"protein": "MANQVIRCKAAVAWEAGKPLSIEEIEVAPPQAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKPILHFMGTSTFSEYTVVADISVAKIDPSAPLDKVCLLGCGISTGYGAAVNTAKVEPGSTCAVFGLGGVGLAVIMGCKVAGASRIIGIDINKDKFAKAKEFGATECINPQDFSKSIQEVLIEMTDGGVDFSFECIGNVKVMRSALEAAHKGWGVSVVVGVAASGEEISTRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTGNLSFDQINKAFDLMHSGNSIRTVLKM", "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": "MLLLISPINTEEALEAIEGGADIVDVKNPAEGSLGANFPWVIRRVREMTPEDMLVSATLGDVPYKPGTVSLAAMGALVSGADYIKVGLYGTRNYDEAVDVMKNVVRAVKDQSDAIVVAAGYADAHRVGAVEPMEIPRVAADSGADLAMLDTAVKDGKTLFDFMDMEKLESFVSAARDHGLKSALAGSVGREHLKPLHEIGCDVVGIRGAACVGGDRNTGRIHRDAVRELKELLDSF", "text": "FUNCTION: Catalyzes the formation of 4-(hydroxymethyl)-2- furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P). SIMILARITY: Belongs to the MfnB family."}
+{"protein": "MAVDIEYSYSSMAPSLRRERFTFKISPKLNKPLRPCIQLGSKDEAGRMVAPTVQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDIPFNITELLDNIVSLTTAESESFVLDFPQPSADYLDFRNRLQTNHVCLENCVLKEKAIAGTVKVQNLAFEKVVKIRMTFDTWKSFTDFPCQYVKDTYAGSDRDTFSFDISLPEKIQSYERMEFAVCYECNGQSYWDSNKGKNYRITRAELRSTQGMTEPYNGPDFGISFDQFGSPRCSFGLFPEWPSYLGYEKLGPYY", "text": "FUNCTION: Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes."}
+{"protein": "MALIRLGFGRQHFCLLKRRSFLMLKLAALVFAVVLFCEFLIYYLVIFRCDWPEVKTPASDSGQKTLKAMFLADTHLLGEVRGHWLDKLRREWQMERAFQTALRLLQPEVVFILGDIFDEGKWSSSQAWADDVERFQKIFRHPRHVQLKVVAGNHDIGFHYQMNAYKIKRFEKVFSPERLFSWKGINFVMVNSVALEGDGCHICSEAEAELIEISRKLNCSRKQERRSGPCPDPQLLPASAPVLLQHFPLYRRSDANCSGEDAAPLEERGIPFKERYDVLSQEASQQLLWWLRPRLILSGHTHSACEVLHGAEVPEISVPSFSWRNRNNPSFIMGSMTPTEYALAKCYLPYEDTVLATYCVAAGLLVVLILVHSELLPSPFLFGWNLLRKFKT", "text": "FUNCTION: Metallophosphoesterase required for transport of GPI-anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step for efficient transport of GPI- anchor proteins (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi- pass membrane protein Note=Also localizes to endoplasmic reticulum exit site. SIMILARITY: Belongs to the metallophosphoesterase superfamily. MPPE1 family."}
+{"protein": "MPIIPKPKSQTKGSVESSKKESRVKMETSDAKYMVGNEVKTIKFLDMRGNIATSARNSLNISPGVFAVNPFLGETLAEDTFNILDYAGLGNVDACASHLSRSQELREQVTEKTLREVPISDSYVLKVVSNLQATTVQNVVSFNKACAVMSFNILRHTTDEMYDWTKNEYVSLGLKEKAAKVNPNIINRLAGQINLSPQSPYYYLVTPGYEFLYDAYPAETIAMTLVKMAYRKTMNLPDSMKDSDICSSLNAKINKRHNLAVNNIDDIIKQIGKKHIEDMYNTLTQNIAMSGKESRNVETAQSFLALIESFKTTT", "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. SUBCELLULAR LOCATION: Virion. Host cytoplasm."}
+{"protein": "MPLYIHALACAFGLGSWVSINGLWVELPLIVNVLPEGWDLPSYLTVIIQFANLGPLLVTLAHKFCPGRLRENLAIYAVLSIGVVACILLAVFWNYTTVIFGQPRSTAFFILTFFLALVDCTSSVTFLPFMMQLPAKYITTYFIGEGLSGLVPGLVALAQGVGMSKCVNVTNVSDNVTDPGPSTFIVETQYLPPNFSTEIFFSFLAVMTTISLGAFLILNRLPRTFELSTENLVSDSDAVATVCRGLEDPMDPKTNCPEEVEQKQNEVLLPKPQHSSYQLAFIYVMVLWVNSATNGLLPSVQTFSCMPYGNMAYHLSAALSAVANPVACIIAMFFPKRSLVFLGILCLLGSTFGGYNMAMAAMSPCPLLQDTPLGDAIIVLSWVFFTGLLSYVKVMVGVILRDRSHSALVWCGAAVQTGSLLGSIIMFPLVNVYHLFKSGDICNTNCPL", "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. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the riboflavin transporter family."}
+{"protein": "MSEREKITIENIVASTSLAEHLDLSRIALALDGSEYEPEQFPGLIYRLQDPKTAVLIFRSGKVNCTGAKNIEDVKRTIKIIIDKLKAANIEVYDDPDIIVQNIVAVYDLESELNLTDIAMSLGLENVEYEPEQFPGLVYRVEEPRVVLLLFGSGKVVCTGAKEESEIEQAVIKVKKELQKVGLI", "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": "MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRGAAGAAPCFCPDKVDRGDLWMFRGDCPGGYGYTSDCYVWPNICCYPH", "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": "GRNGKSQSIIVGPWGDRVTN", "text": "FUNCTION: D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc. SIMILARITY: Belongs to the jacalin lectin family."}
+{"protein": "MASLRSVLKSQSLRHTVRSYSSQTMPPASPFAPRHFLSIADLSPSEFATLVRNASSHKRAIKSGSMPQNLQGSLLGKTVAMIFSKRSTRTRVSTEGAVVQMGGHPMFLGKDDIQLGVNESLYDTSVVISSMVSCIVARVGKHAEVADLAKHSSVPVINALCDSFHPLQAVADFQTIYEAFTPKAHHLSSLGLEGLKIAWVGDANNVLFDMAIAATKMGVDIAVATPKGYEIPPHMLELIKSAGEGVSKPGKLLQTNIPEEAVKDADILVTDTWVSMGQEEEKAQRLKEFDGFQITAELAKRGGAKEGWKFMHCLPRHPEEVSDEVFYSNRSLVFPEAENRLWAAISALEGFVVNKGKIE", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family."}
+{"protein": "MAVSTNELAILAIVLLVTAVVFYTKGTRRAPLPPGPRGIPFLGNLFQFNVMRPYPQYLKWAQKYGPVFSIKLGSQRIIVLSTSEAADELFVTRSKLYSSHESPHVGFDLVSDQQRMVFMPYSREWKIVRKNVHGILGPGPSKQMRKMQDLECRIMLHDLLCHGDTSIVEDFVEGPHGKVPERHWFSIIRRYTTSLMMTLVYGRRIHRIVDNPELHQVYEMMSNMTHVSQPGRYLVDALPILRWLPDIMAPWRAEGKRMHEWEMGFWGKLFADSRTAFLNGTGLNGFVQSYLSARAEAGLEDLPGKGATEDGAGWMRDKLITYTAVSIIEAGSDTTSTAVFSFVLLMLSNPDALRRAKEEMGAVVGSSRMPDWEDEDRLPWLTACIKETLRCAPPLPLGIPHKADEDDVYNGYLIPKGSTVIGNIWAIHMDPVRYPDPTAFKPERFYNPDGKLNWASGPDTHNRDHYIFGWGRRFCSGKYLAEASMFIVLSRLIWGFDFYAASDPQTGKVKLPDVNDVDTFTDGLVTAPKIYPVGFKPRSEKHAEMIKASYRDVQNDWQSMGLAGDER", "text": "FUNCTION: Cytochrome P450 monooxygenase that is able to use dehydroabietic acid as a substrate for oxidation. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MTTMYVSRVSTRPLSAQSAAQLSKAVAFFAQSYRLSSNACTAPTPSRRAFTSASKIQVKGRDLFPEPEHGQIKRTEPAWPHPPYTAEQMRSKVYFAHRKPRDFSDRVALGMVRFLRWCTDFATGYKHNVEAPKKASDSNALTATKPYQMSERKWLIRYVFLESVAGVPGMVAGMLRHLRSLRGLKRDNGWIETLLEEAYNERMHLLTFLKMYEPGIFMRTMILGAQGVFFNSFFLCYLFSPRTCHRFVGYLEEEAVLTYTLSIQDLENGHLPKWADPDFKAPDLAVEYWGMPEGNRSMRDLLYYIRADEAKHREVNHTLGNLKQDEDPNPFVSEYGKERGEKPGKGIESLKPVGWERDEVI", "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; Multi-pass membrane protein; Matrix side. SIMILARITY: Belongs to the alternative oxidase family."}
+{"protein": "PGPPPPAPEGRRRRGRGRNAAGQAVAAEASPAAVEMGNGAAAPGLQRPDAMGRFGRFGGKYVPETLMHALTELESAFHALATDDEFQKELDGILKDYVGRESPLYFAERLTEHYKRADGTGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKQRIIAETGAGQHGVATATVCRRFGLQCIIYMGAQDMERQALNVFRMRLLGAEVRAVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVREFHKVIGKETRRQAMDKWGGKPDVLVACVGGGSNAMGLFHEFVEDQDVRLVGLEAAGHGVDTDKHAATLTKGQVGVLHGSMSYLLQDDDGQVIEPHSISAGLDYPGVGPEHSFLKDIGRAEYDSVTDQEALDAFKRVSRLEGIIPALETSHALAYLEKLCPTLADGVRVVVNCSGRGDKDVHTASKYLDV", "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": "MIKVIFFDLDDTLVDTTKLAELARRNAIENMIRHGLPVDFETAYSELMELIKEYGSNFPHHFDYLLRRLDLPYNPKWVSAGVIAYHNTKFAYLREVPGARKVLIRLRELGYRLGIITDGNPVKQWEKILRLEIDDFFEHVIISDFEGVKKPHPKIFKKALKAFNVDAQEALMVGDRLYSDIYGAKNVGMKTVWFKYGKYSKEELEYREYADYEIEKLQDLLKVIENENGSNKEVHPAR", "text": "FUNCTION: Catalyzes the dephosphorylation of D,L-glyceraldehyde 3- phosphate in vitro. SIMILARITY: Belongs to the HAD-like hydrolase superfamily."}
+{"protein": "MKSIKRIGLCISLLILIIFVTSCDGDNKITGDSKEEQIKKSFAKTLEMYPIKNLEDLYDKEGYRDGEFKKGDKGTWVIRSEMKIQLKGENLESRGVVLEINRNTRTAKGNYIVREVVEDSDGMTHNHTKRYPVKMENNKIIPLKQIVDEKVKKEIEEFKFFVQYGNFKELENYKDGEVTYNPEAPIYSAQYQLKNSDYNVEQLRKRYNIPTQKAPKLLLKGSGNLKGSSVGYKNIEFTFVENKGENIYFTDSVYFNPSEDKYNY", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the staphylococcal tandem lipoprotein family."}
+{"protein": "MAKNTTNRHYSLRKLKTGTASVAVALTVVGAGLVAGQTVRADHSDLVAEKQRLEDLGQKFERLKQRSELYLQQYYDNKSNGYKGDWYVQQLKMLNRDLEQAYNELSGEAHKDALGKLGIDNADLKAKITELEKSVEEKNDVLSQIKKELEEAEKDIQFGREVHAADLLRHKQEIAEKENVISKLNGELQPLKQKVDETDRNLQQEKQKVLSLEQQLAVTKENAKKDFELAALGHQLADKEYNAKIAELESKLADAKKDFELAALGHQHAHNEYQAKLAEKDGQIKQLEEQKQILDASRKGTARDLEAVRQAKKATEAELNNLKAELAKVTEQKQILDASRKGTARDLEAVRKSKKQQVEAALKQLEEQNKISEASRKGLRRDLDTSREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSKLAALEKLNKDLEESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAGKASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTGETANPFFTAAALTVMAAA", "text": "FUNCTION: This protein is one of the different antigenic serotypes of protein M. Protein M is closely associated with virulence of the bacterium and can render the organism resistant to phagocytosis. SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. SIMILARITY: Belongs to the M protein family."}
+{"protein": "MNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGAMRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEELPDHQYYNDFPGKEPPLGGVVDMRLREGAARPTLPSTQMPSHLGATLPIGQHVTGDHEVRKQMLPPPPCPGRELFDDPSYVNIQNLDKARQAGGGAGPPNPSVNGSAPRDLFDMKPFEDALRVPPAPQSMSMAEQLQGESWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVDRKV", "text": "FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell junction, focal adhesion."}
+{"protein": "MWGCWLGLLLLLLAGQAALEARRSRWRRELAPGLHLRGIRDAGGRYCQEQDMCCRGRADECALPYLGATCYCDLFCNRTVSDCCPDFWDFCLGIPPPFPPVQGCMHGGRIYPVFGTYWDNCNRCTCHEGGHWECDQEPCLVDPDMIKAINRGNYGWQAGNHSAFWGMTLDEGIRYRLGTIRPSSTVMNMNEIYTVLGQGEVLPTAFEASEKWPNLIHEPLDQGNCAGSWAFSTAAVASDRVSIHSLGHMTPILSPQNLLSCDTHHQQGCRGGRLDGAWWFLRRRGVVSDNCYPFSGREQNEASPTPRCMMHSRAMGRGKRQATSRCPNGQVDSNDIYQVTPAYRLGSDEKEIMKELMENGPVQALMEVHEDFFLYQRGIYSHTPVSQGRPEQYRRHGTHSVKITGWGEETLPDGRTIKYWTAANSWGPWWGERGHFRIVRGTNECDIETFVLGVWGRVGMEDMGHH", "text": "FUNCTION: May be implicated in the adrenocortical zonation and in mechanisms for repressing the CYP11B1 gene expression in adrenocortical cells. This is a non catalytic peptidase C1 family protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "DTCCSIEDRREVQALWRSIWSAEDTGRRTLIGRLLFEELFEIDGATKGLFKRVNVDDTHSPEEFAHVLRVVNGLDTLIGVLGDSDTLNSLIDHLAEQHKARAGFKTVYFKEFGKALNHVLPEVASCFNPEAWNHCFDGLVDVISHRIDG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the globin family."}
+{"protein": "MKKKNIYSIRKLGVGIASVTLGTLLISGGVTPAANAAQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPKADAQQNKFNKDQQSAFYEILNMPNLNEEQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPKADNNFNKEQQNAFYEILNMPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNESQAPKADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKADNKFNKEQQNAFYEILHLPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKLNDAQAPKEEDNNKPGKEDGNKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDGNKPGKEDGNKPGKEDGNKPGKEDGNGVHVVKPGDTVNDIAKANGTTADKIAADNKLADKNMIKPGQELVVDKKQPANHADANKAQALPETGEENPFIGTTVFGGLSLALGAALLAGRRREL", "text": "FUNCTION: Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins (By similarity). In turn, Staphylococcus aureus is protected from phagocytic killing via inhibition of Ig Fc region. In addition, the host elicited B-cell response is prevented due to a decrease of antibody-secreting cell proliferation that enter the bone marrow, thereby decreasing long-term antibody production. Inhibits osteogenesis by preventing osteoblast proliferation and expression of alkaline phosphatase, type I collagen, osteopontin and osteocalcin. Acts directly as a pro-inflammatory factor in the lung through its ability to bind and activate tumor necrosis factor alpha receptor 1/TNFRSF1A (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor Note=Anchored to the cell wall by sortase A. SIMILARITY: Belongs to the immunoglobulin-binding protein SpA family."}
+{"protein": "MAVRSLWAGRLRVQRLLAWSAAWESKGWPLPFSTATQRTAGEDCRSEDPPDELGPPLAERALRVKAVKLEKEVQDLTVRYQRAIADCENIRRRTQRCVEDAKIFGIQSFCKDLVEVADILEKTTECISEESEPEDQKLTLEKVFRGLLLLEAKLKSVFAKHGLEKLTPIGDKYDPHEHELICHVPAGVGVQPGTVALVRQDGYKLHGRTIRLARVEVAVESQRRL", "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. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the GrpE family."}
+{"protein": "MSVRTSSRSNKGQNKYIEYLLQEETEAPKKKRTKKKVDSATEKNKKSDSSQEPRKDTENVRTDEVDEADEGYVRCLCGANNENYDAAEYSHGDMVQCDGCDTWQHIKCMTDGKDTIDGLMSEDSKYYCELCDPSLYAHLETSKEAEVSEDEDYHDDVYKPVNDHDDNDADVFLDEESPRKRKRSPDSAKGIHIKSKQVKKSNGSKKRNKSIDAAKSDTAENEMPTRKDFESEKEHKLRYNAEKMFSTLFSKFIVPETIEAKLYELPDGKDVISISQEFAHNLEEELYKACLNIEFGTLDKIYTEKVRSLYSNLKDKKNLELKAHVVEGKLPLNKLVNMNASELANPDLQEFKEKRDKVILENFIVEVPDKPMYVKTHKGDELIEDIAEPQEDILYSKDSIRLHNIDSIDSDKSKIEQTHAISKEPSPSTIINEESLNCAFLYPGLGLEFTGYLNYIGVSQKLRRDIFKEAIGDGKLYVEGRLPTTTAAPYLKEISCSRAILVYQLFPSNDSESKTTFADVVDSLENKGRIAGIKPKTRYEKDFYIVPSKGGEIPEILKDILGSHNDERSERFSRMKSDERTLFAFVVVKQEFIH", "text": "FUNCTION: Negative regulator of transcription elongation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BYE1 family."}
+{"protein": "MGKLQDGIAIKRINDAITTFKNYKLGELKQGGSMAINTLSNVRAHVGLAWPAILRNCLIHTSSHLGFMKFMIDIATTWKVGAFTLLGSVGDEDPFTDVDLIYTKTCLHLGLKDNDFLQFPEEFAYEANSFLEAQSMNAKVDMLTGVHNIEDKYVFRMQSISKFLKAYYTASEDVAYLTGFIKPDDSKDSILNAELLEAQVTSEVLRVRNLITTKIQKYINLYEDSQLPHFRQAALSYIQDWDVDGGVPAALPQPDTTDDERPVTKPGPSTPTVSKGVDEPEDEEMIRKKVETSKDAPSKADPPGNVSPRGVPALLEDDMSEMDMPDGFHDYLTREHENNFDLSQLGLAPSV", "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": "MADDRVAILTEDEEELKRKHLERFDRLSLEIQSPSQPPENDVPNDTAPTPSPQHELSCCERLFLRVNRHLLVSKVFYLFFYAAYGSLHPLLALYYKQLGMNPTQSGLLVGIRYFIEFCSAPFWGIVADRYRKGKAVLLFSMLCWILFNAGIGIVKPPIMACKEETIPTTTKVPTVHPTPSNETFFPNTSSTSQMRRRRDLIGQYPWRTILSSGQSSGYISEHRIKRDSNLSFTPAPEELANTTQTNQTSTTTQPKPSTSISTSTPSSTNTTSSSTTKSTTTNPNLPPPEYNMDQVNAIFLLILLVIIIGEFFSAPAITIVDTVTLHYLGPHRDRYGLQRMWGSLGWGLAMLCIGIWIDHTSTNLIIGNMECIMKNYKNYHIAFIVFGVLMVIALIVATQFKFDVQHHDTNEGQEVGNQQENVQPRGSPGTRSTDTPTIVQAEEFHFWDLMRLLCGVQYSTVLFVAWFMGFGYGFVFTFLYWHLQDLTGTTTLFGICSVLSHVSELAAYFTSHKFIELVGHIRVLYIGLACNTARYLYISYLENAWTVLPMEVLQGITHASVWAACISYLSAAVPPPLRTSAQGILQGLHLGLGRGCGAMVGGIFVNYFGVAETFRGIGMASLVILLIFSLIMYITGQNEKKEDKMLAENIPIPSSPVPIATIDLVQNTADVAAPARPEPKLPARKTQHQQEQEDLNKPAWVPSGSPWVSVALLVYQIREMVLLAKARPTVEVQPLQGTDEVRSDSQEDQSPPVFSDAVQNENTPSGLQDHSGSPTAQLDVPTRDTQPPSQHIS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. MFSD6 family."}
+{"protein": "VPETWDXXDYGAQT", "text": "SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQVLSEMTVADIRNNPVIAYEDDCVTRLIQDDVNETAYNQIKNWSISELREYVLSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGAKKMPVIKKANTTIGIPGTFSARLQPNDTRDDVQSIAAQIYEGLSFGVGDAVIGVNPVTDDVENLSRVLDTIYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICGSEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANFGADQVTMEARNYGLARHYDPFIVNTVVGFIGPEYLYNDRQIIRAGLEDHFMGKLSGISMGCDCCYTNHADADQNLNENLMILLATAGCNYIMGMPLGDDIMLNYQTTAFHDTATVRQLLNLRPSPEFERWLESMGIMANGRLTKRAGDPSLFF", "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 vitamin B12. FUNCTION: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds (PubMed:19762342). Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12. It is spontaneously inactivated by its substrate and reactivated by EutA (PubMed:15466038). SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the EutB family. SIMILARITY: Belongs to the EutB family."}
+{"protein": "MPLKSLKNRLNQHFELSPRYGSVKKIMPNIVYADGFNPSVGDVVKIEKSDGTECVGMVVVAEKEQFGFTPFNFIEGARAGDKVLFLKEGLNFPVGRNLLGRVLNPLGQVIDNKGVLDYERLAPVITTPIAPLKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMITRGCLAPIKVIALIGERGREIPEFIEKNLKGDLSSCVLVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSALSLLPQLMERAGKEENKGSITAFFSVLVEGDDLSDPIADQARSILDGHIVLSRELTDYGIYPPINILNSASRVAKDIISESQNLCARKFRRLYALLKENEMLIRIGSYQMGNDKELDEAIKKKALMEQFLVQDENALQPFEQSFQQLEEILR", "text": "FUNCTION: Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
+{"protein": "MNTATLSSILLESHKPAKLETIPEDSYSSIFVFKWLEYLCERVGHSNVPDVLEFYYNLGWVSDKAIAKLLKFSKGIGLDDDEIETSVGKLTIADHLVSLLFIERLNGKKVSSEALDKLEWEIRRIKKGAEQYYGI", "text": "SUBCELLULAR LOCATION: Archaeal flagellum. SIMILARITY: To M.jannaschii FlaE, also to FlaD."}
+{"protein": "MEDSVVDDVIKRLLGAKNGKTTKQVQLTEAEIKHLCSTAKQIFLTQPNLLELEAPIKICGDTHGQFSDLLRLFEYGGYPPAANYLFLGDYVDRGKQSVETICLLLAYKIKYKENFFLLRGNHECASINRIYGFYDECKKRYSVRVWKIFTDCFNCLPVAALIDEKILCMHGGLSPELKHLDEIRNIPRPADIPDHGLLCDLLWSDPDKDIEGWGENDRGVSYTFGADKVEEFLQTHDLDLICRAHQVVEDGYEFFANRQLVTIFSAPNYCGEFDNAGAMMSVDDSLTCSFQILKASEKKGNFGFGKNAGRRGTPPRKGGGKG", "text": "FUNCTION: Serine/threonine-protein phosphatase that possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily."}
+{"protein": "MKPGAFALNPHAASYVPISKRVDYGGGDDGLVFAAKSPTVEVSMPKKSSEMAYKQIRDDDLDLEMDIDMDIEYLLVTFSGLSQESITDVYLANGGDLEATIEMLNQLEIYSTESEENLPETLDIGDISESGPSTSKSTEVAASTSSVIPNAPVSA", "text": "FUNCTION: Promotes polyploidy in dark-grown seedlings. Regulates the endocycle leading to hypocotyl elongation."}
+{"protein": "MSTVHEILCKLSLEGDHSTPASAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIXIMVSRSEVDMLKIRSEFKRKYGKSLYNYIQQDTKGDYQKALLYLCGGDD", "text": "FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome Note=In the lamina beneath the plasma membrane. SIMILARITY: Belongs to the annexin family."}
+{"protein": "MNIDIVSMAWAALMVVFTFSLSLVIWGRSGL", "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 membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetN family."}
+{"protein": "MDIRNNDPGAVQYGNFFNYYQFSSAAERVKLLPDADIWLPALEDGETQKDKPYFILDVGCNCGVLTQLMHKYLEERLHRSVKVLGVDIDPRLIQRASEENESPKDVSYACVDVLDDEAFESVKTYMEVNNLEKFDAICCYSITMWIHLNHHDQGLRFFLQKLSNLAELLVVEPQPWKCYQKAERRLKKAGEIFPLFLELKWRSDVDLQIQKYLEESLDRRKIFKSAPTKWQRKICFYR", "text": "FUNCTION: Probable RNA methyltransferase. SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "METVRSAPPGDGAAEALLKELERQVQDVVRASSWWERHGVDCAILALSLLALPAGFLCLRAHNILAFATGITILGVCHYTLTVKGSHLATHSALTESKRWSKILMIFFLEVCTAFSAEFAKFNHVNLHHVYTNVVGLGDSSTWKVPLLNRYVYMFLGPLLVPIITPLVALEHLRKEEPRTALRTLGFICLGLYSQYWLFMNVSGFKNPSSALACMLLTRSLLAHPYLHVNIFQHIGLPMFSPDKKPRRIHMMTLGVLNLPRQLVLDWAFGHSLISCHVEHHLFPWLSDHMCLKVKPLVSKFLHEKQLPYNEDSYLARFQLFLSRYEEFMVHVPPITELVGVQ", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
+{"protein": "MKNFKLNRVKYKNIMSVGQNGIDIQLDKVQKTLITGRNGGGKSTMLEAITFGLFGKPFRDVKKGQLINSTNKKELLVELWMEYDEKKYYIKRGQKPNVFEITVNGTRLNESASSKDFQAEFEQLIGMSYASFKQIVVLGTAGYTPFMGLSTPARRKLVEDLLEVGTLAEMDKLNKALIRELNSQNQVLDVKKDSIIQQIKIYNDNVERQKKLTGDNLTRLQNMYDDLAKEARTLKSEIEEANERLVNIVLDEDPTDAFNKIGQEAFLIKSKIDSYNKVINMYHEGGLCPTCLSQLSSGDKVVSKIKDKVSECTHSFEQLSTHRDNLKVLVDEYRDNIKTQQSLANDIRNKKQSLIAAVDKAKKVKAAIEKASSEFIDHADEIALLQEELDKIVKTKTNLVMEKYHRGILTDMLKDSGIKGAIIKKYIPLFNKQINHYLKIMEADYVFTLDEEFNETIKSRGREDFSYASFSEGEKARIDIALLFTWRDIASIVSGVSISTLILDEVFDGSFDAEGIKGVANIINSMKNTNVFIISHKDHDPQEYGQHLQMKKVGRFTVMV", "text": "FUNCTION: Exonuclease that plays a role in viral genome replication, DNA recombination, and host DNA degradation. SIMILARITY: To phage T5 protein D13 and to yeast RAD52."}
+{"protein": "MNEEGCVPHNSDVVKQKSIDQRAPLSGEPKCVICSRYGEYICDETNDDVCSLECKQALLRRVDSARVFPATDECFYVRDPGSSSHDAQLLRRKLDIHVQGQGSAVPPPVLTFTSCGLPPKLLLNLETAGYDFPTPIQMQAIPAALTGKSLLASADTGSGKTASFLVPIISRCTTYHSEHPSDQRRNPLAMVLAPTRELCVQVEDQAKMLGKGLPFKTALVVGGDPMSGQLYRIQQGVELIIGTPGRVVDLLSKHTIELDNIMTFVLDEVDCMLQRGFRDQVMQIFQALSQPQVLLFSATISREVEKVGGSLAKEIILVSIGNPNKPNKAVNQLAIWVDAKQKKQKLFDILRSQNHFKPPAVVYVSSRVGADLLANAITVVTGVKALSIHGEKPMKERRDVMGSFLGGEVPVLVSTGVLGRGVDLLVVRQVIVFDMPSTIKEYIHVIGRASRMGEKGTAIVFVNEDDRNLFPDLVAALKSSGAAIPKELINLTSREMHNKKRRVGY", "text": "SIMILARITY: Belongs to the DEAD box helicase family. DDX59 subfamily."}
+{"protein": "MNETSNRDHQVTSKEILDVAFEKSKSKFTTPRQTIQDTEELQSYQQTKRKEFEQHINKNRLNLGQWTRYAKWEIENNHDFPRARSILERALDVNIQHVPFWIQYIQLELSHKNINHARNLMERAINTLPRVNKLWFLYVQTEEMLKNYPMVRAVFERWLDWHPDTSAWDAYINFEARYEEKENVRTIFKKYVHEFPNAGTWYKWIKYEMENNRDDVNTVRAVFESAVDTLLSNKSEENDDDEEFATIISSWTSWEVSCGEASRANEIFKLLLDNKTNKLEISDQTKSSIYTAFVEFEKNFGNKDSIEQSVLIKRRIKYEQEIQNDPYDYDSWWKYMTLLQNSSNKSDLENAFKKVTGNVVHDKHKSIKWRRYIMFWIWYAFWEEMTNNNPVSAREIWNNCLKVIPHKSFTFAKVWIGYSEFELRNSEDGLAKARKILGRAIGQTSINKPKIKIFKYYIDLEKKLGDWNRVRLLFQKWLEVSLLTTSSSELVIEKYVEFESSIEEYDRCDSILSSARQLSENPEYSSSFNLQRLLEITVEFYKEEMQYDKIREIYRALLDKDPNAHNWISFALFESSIPSAEQLEEYLQGDNEEFEATVDESQIESTRNIFEEAMTYFKDKDDKESRLVIIEAWRDFEEVNGSDESLSKVTKRLPVIVRKRRTVGSIEEEYIDYIFPDDESKKLPGKMSKFLANAKKWAQQN", "text": "FUNCTION: Involved in pre-mRNA splicing and cell cycle progression. Required for the spliceosome assembly and initiation of the DNA replication (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the crooked-neck family."}
+{"protein": "MRVVKVKKTVVIIGGGAAGMSAASRVKRLKPEWDVKVFEATEWVSHAPCGIPYVVEGISPTEKLMHYPPEVFIKKRGIDLHLNAEVIEVDTGYVRVREKDGEKSYEWDYLVFANGASPQVPAIEGVDLKGVFTADLPPDAVAIREYMEKNRVEDVVIVGGGYIGLEMAEAFVAQGKRVTMIVRGERILRRSFDKEVTDIIEEKLKQHVNLRLQEIVLRIEGKDRVEKVVTDAGEYRADLVILATGIKPNIELARQLGVRIGETGAIWTNEKMQTSVENVYAAGDVAETKHVITGRRVWVPLAPPGNKMGYVAGSNIAGKEIHFPGVLGTTVTKFLDVEIGKTGLTETEALKEGYDIRTAFIKASTRPHYYPGGKEIWLKGVVDNETNRLLGVQAVGAEILPRIDAAAAMLMANFTTKDAFFTDLAYAPPFAPVWDPLVVLARVLKF", "text": "FUNCTION: Catalyzes the CoA-dependent reduction of elemental sulfur (S(0)) to produce hydrogen sulfide. SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MRLDEYMDIERDERAERRRLAEEKSYGILDHLETFQDRFEETVQGDSLYGGVSPSIFVGRSNYPNVSTGILSPVGHDEDAASFETSAAWYDEGVSIDDVFQRRTSLLNSNRGTKVTNVADSWDGFLGTQREVAIADRPVTVEIGLDGKPSLDLDASADDVATPVGPRARARSADLAENPHVPKLVKKTLEDDDWNAEGAMTYLYRRGFDVYDINTILSAGALGQTEQRRLVPTRWSITAVDDTLGQYLRGQVKHAESVDGVEIYRNEFIGNAFWVILAPGRWEFELIELKAPGSVWNPDPEAGMYLAADREGYEGRTGYVNETAGAYHASRLGVLEHLQERGRQAKALVIRHVSDDYWGPVGVWQIRESIRHAFEGEMADAETFGDAVRDVTEYLPVSLADLRRKSTMAAGLQTDIFDFA", "text": "FUNCTION: Involved in DNA damage repair. Works together with the UvrABC proteins in repairing DNA damage resulting from exposure to the DNA damaging agent mitomycin C (MMC). SIMILARITY: Belongs to the Nre family."}
+{"protein": "MKLRVRLQKRTQPLEVPESEPTLGQLRAHLSQVLLPTLGFSSDTRFAITLNNKDALTGDEETLASYGIVSGDLICLVLEDDMPAPNLPSSTDTEHSSLQDNDQPSLAATPSQTNIPDEQGTDSSQGQATPFDAWTDDSMEGPSQNVEAESIQDAMSMEEVSGFHPLEPMLCNETEDGQVPHSLETLYQSAGCSNISDALIVLVHLLMLESGYIPQGTETKAVTMPEKWKSSGVYKLQYTHPLCEGGFAVLTCVPLGNLIIINATIKVNGGIKNVKSVQLQPGSYVAAGVEPGESAAKVYKDLKKLSRLFKDQLVYPLLAFTRQVLNLPDVFGLVVLPLELKLRIFRLLDVHSVLALSAVCHDLLIASNDPLLWRCLYLRDFRDGTVRGPDTDWKELYRKKHIQRKEAQRMRHAMFLPSAHPIPFCPIPVYPRAYLPTSLLPPGIIGGEYDERPILPSVGDPVTSLIPRPGELPGQFRPLRPRFDPVDPLPGPHSLLPGRAIPNNRFPFRPGRGRSADSRLPFL", "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 and plays a role in several biological processes such as cell cycle, cell proliferation, or maintenance of chromosome stability. Recognizes and ubiquitinates BIRC2 and the cell cycle regulator DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination. Mediates the ubiquitination and proteasomal degradation of UXT isoform 2, thereby impairing the NF-kappa-B signaling pathway. Inhibits NF- kappa-B pathway also by promoting the ubiquitinatioin of TRAF2 (By similarity). Affects the assembly state and activity of the proteasome in the cells including neurons by ubiquitinating the proteasomal subunit PSMA2 via 'Lys-63'-linked polyubiquitin chains (PubMed:27497298). Promotes 'Lys-48'-linked polyubiquitination SIRT7, leading to the hydrogen peroxide-induced cell death (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion Cytoplasm, cytosol Note=Predominantly cytoplasmic. A minor proportion is detected in the nucleus. Relocates from the cytosol to depolarized mitochondria (By similarity)."}
+{"protein": "MSSEIEVVEEIQSNPKENGESSSKGIEEESLKNDVYTAAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVVSKWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGKKEDLMITDKTGLTPAQLAAEKNHRQVSFFLGNARSLLEKRCDGSSPLGRLSKLGLAPVLWIMILLLLLVYTNSVVLASNLPKLTTGIGALAWLGFILATAGLFLFYRCSRKDPGYIRMNIHDPQTMKDDEPLLKIELNNPALLAGNWTQLCATCKIIRPLRAKHCSTCDRCVEQFDHHCPWVSNCVGKKNKWEFFLFLLLEVLAMLITGGVTLARVLSDPSAPSSFGAWMSHVASNHVGALSFLLVEFCLFFSVAVLTVIQASQISRNITTNEMANALRYSYLRGPGGRFRNPYDLGCRRNCSDFLVKGYNEDIECHEEDATQRPEGISMMQMQRNPNLQNGNGHVAIDVNPTHNSQSAHVHSANCSHSHNSKSKSDNVPLGLGLGLSRNPTRPVVSP", "text": "FUNCTION: Palmitoyltransferase involved in cell growth regulation (Ref.8). Contributes to the palmitoylation of CESA3, thus regulating cellulose biosynthesis (PubMed:35644016). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
+{"protein": "MELRVGNKYRLGRKIGSGSFGDIYLGTTINTGEEVAIKLECIRTKHPQLHIESKFYKTMQGGIGIPRIIWCGSEGDYNVMVMELLGPSLEDLFNFCSRRFSLKTVLLLADQMISRIDYIHSRDFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKFRDARSLKHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGALPWQGLKAANKRQKYERISEKKLSTSIVVLCKGFPSEFVNYLNFCRQMHFDQRPDYCHLRKLFRNLFHRLGFTYDYVFDWNLLKFGGPRNPQAIQQAQDGADGQAGHDAVAAAAAVAAAAAASSHQQQQHKVNAALGGGGGSAAQQQLQGGQTLAMLGGNGGGNGSQLIGGNGLNMDDSMAATNSSRPPYDTPERRPSIRMRQGGGGGGGGVGVGGMPSGGGGGGVGNAK", "text": "FUNCTION: Involved in circadian rhythms, viability and molecular oscillations of the clock genes period (per) and timeless (tim). Dbt reduces the stability and thus the accumulation of monomeric per proteins, probably through phosphorylation. No evident circadian oscillation is detected in head. Together with CkIalpha, regulates processing of ci by phosphorylating it, which promotes its binding to slmb, the F-box recognition component of the SCF(slmb) E3 ubiquitin- protein ligase (PubMed:16326393). SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily."}
+{"protein": "MNKIQHISFITKKNPLVSYERVGALQNRFVQHYLNYKANKVEQPPKPTIITSQVCPVYTLGRRESSINFTKGFPKAKVVKALRGGQTTFHGPGQILAYPIIDLKSFGLSPREYVSRLEQAIIATCKSFGIEKAHTTKNTGVWVTENDKIAAIGIHLRRNITSHGLALNVSTDLKYFNYIVGCGLYGKNTTSFKDQGVFTDLKSVEKVLVNNLDSFLMSK", "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 (By similarity). SIMILARITY: Belongs to the LipB family."}
+{"protein": "MIDHLKRTKIIATCGPALTKSLVSLKMLDDNEYAAIKKVAYANIEAIIKSGVSVIRLNFSHGTHEEQQVRIKIVRDVAKAMNIPVSIMLDTNGPEIRIVETKKEGLKITKDSEVIINTMSKMIASDNQFAVSDASGKYNMVNDVNIGQKILVDDGKLTLVVTRVDKQHNQVICVAKNDHTVFTKKRLNLPNAQYSIPFLSEKDLKDIDFGLSQGIDYIAASFVNTVADIKQLRDYLKLKNASGVKIIAKIESNHALNNIDKIIKASDGIMVARGDLGLEIPYYQVPYWQRYMIKACRFFNKRSITATQMLDSLEKNIQPTRAEVTDVYFAVDRGNDATMLSGETASGLYPLNAVAVMQKIDKQSETFFDYQYNVNYYLKNSTANKSRFWHNVVLPLTKKTVPKRKLVNSAFKYDFIVYPTNNINRIYALSNARLAAAVIILTNNKRVYTGHGVDYGIFCYLIDKNPNQLTKAELIELAWKAINHYQAYGDLEKLKQCLAVYNETIINL", "text": "SIMILARITY: Belongs to the pyruvate kinase family."}
+{"protein": "MEKARISIRQLFVMIIIFELGSSLLITPGSMAGRDAWIAVLLGCAIGLFLFYLYQGIYQCYPNSSPKEYMDDMLGTKLSWLFSFLYILYFAYIAARVLRDFGEMLLTFAYHDTPIIIVNALLMVVSIYAVRKGIEVLARAAELLFGAMYLLGAIGLVLIIVSGTIDPHNLKPVLANGISPVLHSVFTQTMYVPFGEVVLFVMIFPNLNDRKDVKKMGMIAMAISGLIVALTVAINISVLDVDLTLRSQFPLLSTIQTIKVEEFLDRLDVFFMLALIIGGFFKVSLYLYATVVGTSTLFKEKNPSQLAYPMGLGILILSITIATNFSEHLNEGLNVVPLYIHLPFQLLFPLFLFIVAVWKKKRREKSKGEEAKK", "text": "FUNCTION: Involved in the germination response to the combination of glucose, fructose, L-asparagine, and KCl. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Spore germination protein (SGP) (TC 2.A.3.9) family."}
+{"protein": "MAAGGPGAGSAAPVSSTSSLPLAALNMRVRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETHADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDVLLELGPSIEEDCQKYILKQQQEEAEKPLQVAAVDSSVPRTAELAGITTLDDPLGHMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFITVCDYTNPCTKSWFWTRLAKALSLP", "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": "MTQANLSETLFKPRFKHPETSTLVRRFNHGAQPPVQSALDGKTIPHWYRMINRLMWIWRGIDPREILDVQARIVMSDAERTDDDLYDTVIGYRGGNWIYEWATQAMVWQQKACAEEDPQLSGRHWLHAATLYNIAAYPHLKGDDLAEQAQALSNRAYEEAAQRLPGTMRQMEFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSKWKLTQDSSLLHQHVLKALPNVPWVDHTRVAAFGFRFGANVAVRLAYLESPRLKAVACLGPVVHTLLSDFKCQQQVPEMYLDVLASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLITSSSADGKLLEIPFNPVYRNFDKGLQEITDWIEKRLC", "text": "FUNCTION: Catalyzes the hydrolysis of esters. SIMILARITY: Belongs to the FrsA family."}
+{"protein": "MIRSRQKVLSLVTWTLKRSIVVNAVSASSVDPSFSTMANTTNVAANTNLNKTTTEPGNIRNAPQLSILQTLENAEFIALGTPPTLLTVHSPPSVPLFVRRGALTSIYGLKSTSNTTPTYGSSSSSSSSSSSSSSTATSFTSSLTSSTQPLIRNTLEFPLWWDRFRFNGGHILSYQKLISTVPFSTLISSSSSSLSSSSKYGDVKSFANLILDGSSDWAILNKTAIQAYTGNSLSISMHKLPKYISKSLAKFLNISRIETGLWSFWNSGYTLLSGRGHVGVVGSGGVYQLQLAEDEEILIRKSAILGVTVNGPFDLENCIIKNDVTTTLYLPQEGEQNHKVKVKLNVEERPQGKQVLVQPSAWDQIVLGSKLALNWTRLVWHYQKVFFNRISIILSRFLLGNAEFVKVVGPRNILIQASPHLKQTQKDTRRSFGGSNSEEITQLNEKLVFIEPQINPESGSKSKSNDYLSYVEIDPKKGAVFQNTPNFRDSI", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM24 family."}
+{"protein": "MTTFYTVVSWLIILGYWLLIAGVTLRILMKRRAVPSAMAWLLVIYILPLVGIVAYLSVGELHLGKRRAERARAMWPSTAKWLNDLKACKHIFAEENSAVASALFQLCERRQGIAGVKGNQLQLLTSSDDVMQALIRDIQLARHNIEMVFYIWQPGGMADQVAESLMAAARRGVHCRLMLDSAGSVAFFRSPWAGMMRNAGIEVVEALKVNLMRVFLRRMDLRQHRKMIMIDNYIAYTGSMNMVDPRYFKQDAGVGQWVDLMARMEGPVATAMGIVYSCDWEIETGKRLLPPPPDANIMPFEQASGHTIHTIASGPGFPEDLIHQALLTSVYAAREYLIMTTPYFVPSDDLLHAICTAAQRGVDVSIILPRKNDSLLVGWASRAFFSELLAAGVKIYQFEGGLLHTKSVLVDGELSLVGTVNLDMRSLWLNFEITLVIDDAGFGADLAEVQDDYISRSRLLDARLWVKRPFWQRVVERLFYFFSPLL", "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": "MKVLILACLVALALAREKEQLSVPTEAVGSVSSSEEITHINKQKLETIKHVEQLLREEKLQDKILPFIQSLFPFAERIPYPTLPQNILNLAQLDMLLPLLQPEIMEDPKAKETIIPKHKLMPFLKSPKTVPFVDSQILNLREMKNQHLLLPQLLPFMHQVFQPFPQTPIPYPQALLSLPQSKFMPIVPQVVPYPQRDMPIQALQLFQELLFPTHQGYPVVQPIAPVNV", "text": "FUNCTION: Important role in determination of the surface properties of the casein micelles. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-casein family."}
+{"protein": "MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSKDVSASVLATYVGGKQLYP", "text": "FUNCTION: Required for phyA-controlled responses to continuous far-red light (FRc) conditions, including the inhibition of hypocotyl elongation and the regulation of XTH15/XTR7 expression. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Cytoplasm, perinuclear region. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily."}
+{"protein": "MTENWKFRRRTFLKHGAQAATLAGLSGLFPETLRRALAVEPDIRTGTIQDVQHVVILMQENRSFDHYFGHLNGVRGFNDPRALKRQDGKPVWYQNYKYEFSPYHWDTKVTSAQWVSSQNHEWSAFHAIWNQGRNDKWMAVQYPEAMGYFKRGDIPYYYALADAFTLCEAYHQSMMGPTNPNRLYHMSGRAAPSGDGKDVHIGNDMGDGTIGASGTVDWTTYPERLSAAGVDWRVYQEGGYRSSSLWYLYVDAYWKYRLQEQNNYDCNALAWFRNFKNAPRDSDLWQRAMLARGVDQLRKDVQENTLPQVSWIVAPYCYCEHPWWGPSFGEYYVTRVLEALTSNPEVWARTVFILNYDEGDGFYDHASAPVPPWKDGVGLSTVSTAGEIEVSSGLPIGLGHRVPLIAISPWSKGGKVSAEVFDHTSVLRFLERRFGVVEENISPWRRAVCGDLTSLFDFQGAGDTQVAPDLTNVPQSDARKEDAYWQQFYRPSPKYWSYEPKSLPGQEKGQRPTLAVPYQLHATLALDIAAGKLRLTLGNDGMSLPGNPQGHSAAVFQVQPREVGNPRFYTVTSYPVVQESGEELGRTLNDELDDLLDANGRYAFEVHGPNGFFREFHGNLHLAAQMARPEVSVTYQRNGNLQLNIRNLGRLPCSVTVTPNPAYTREGSRRYELEPNQAISEVWLLRSSQGWYDLSVTASNTEANYLRRLAGHVETGKPSRSDPLLDIAAT", "text": "FUNCTION: Hydrolyzes sphingomyelin in addition to phosphatidylcholine. SIMILARITY: Belongs to the bacterial phospholipase C family."}
+{"protein": "MSSRYLLSPAAQAHLEEIWDCTYDRWGVDQAEQYLRELQHAIDRAAANPRIGRACDEIRPGYRKLSAGSHTLFYRVTGEGTIDVVRVLHQRMDVDRNL", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Its toxic effect is neutralized by coexpression with cognate antitoxin ParD1 (By similarity). FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli inhibits cell growth and colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin ParD1. SIMILARITY: Belongs to the RelE toxin family."}
+{"protein": "MTVQLGAFYLFPLFMAGFVQTNSNLEKMDCYKDVTGTIYDYDAFTLNGNEHIQFKQYAGKHVLFVNVATYCGLTAQYPELNTLQEELKPFGLVVLGFPCNQFGKQEPGENSEILLGLKYVRPGGGYVPNFQLFEKGDVNGEKEQKVFTFLKHSCPHPSELIGSIGYISWEPIRVHDIRWNFEKFLVGPDGVPVMRWVHETPISTVKSDILAYLKQFKTE", "text": "FUNCTION: May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids. Since the purified porcine enzyme has very little activity towards hydrogen peroxide or organic hydroperoxides the protective effect is not likely to be exerted by its enzymatic activity. Instead, may protect sperm from premature acrosome reaction in the epididymis by binding to lipid peroxides, which might otherwise interact with phospholipase A2 and induce the acrosome reaction. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glutathione peroxidase family."}
+{"protein": "MELTSEEYEELRGLLGTPDIGNADTLKKAFLKACKVHHPDKGGNEEAMKRLLYLYNKAKIAASATTSQVWYFLIIGYISLKNKNIYLPKIFWLRFQNMAPHSGNSGGKNSIKALMSKICIVMRN", "text": "FUNCTION: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus."}
+{"protein": "MAVSASPVISATSSGAGVPGGLFRAEPLYSTPREPPRLTPNMINSFVVNNHSNSAGGGGRGNTNTNECRMVDMHGMKVASFLMDGQELICLPQVFDLFLKHLVGGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCKLITRKDFETLFTDCTNARRKRQMTRKQAVNSSRPGRPPKRSLGVLQENARLLTHAVPGLLSPGLITPTGITAAAMAEAMKLQKMKLMAMNTLQGNGSQNGTESEPDDLNSNTGGSESSWDKDKMQSPFAAPGPQHGIAHAALAGQPGIGGAPTLNPLQQNHLLTNRLDLPFMMMPHPLLPVSLPPASVAMAMNQMNHLNTIANMAAAAQIHSPLSRAGTSVIKERIPESPSPAPSLEENHRPGSQTSSHTSSSVSSSPSQMDHHLERMEEVPVQIPIMKSPLDKIQLTPGQALPAGFPGPFIFADSLSSVETLLTNIQGLLKVALDNARIQEKQIQQEKKELRLELYREREIRENLERQLAVELQSRTTMQKRLKKEKKTKRKLQEALEFESKRREQVEQALKQATTSDSGLRMLKDTGIPDIEIENNGTPHDSAAMQGGNYYCLEMAQQLYSA", "text": "FUNCTION: Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator for SIX1 and SIX6. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. Is recruited with SIX6 to the p27Kip1 promoter in embryonal retina. SIX6 corepression seems also to involve NCOR1, TBL1, HDAC1 and HDAC3. May be involved together with PAX3, SIX1, and EYA2 in regulation of myogenesis. In the developing somite, expression of DACH2 and PAX3 is regulated by the overlying ectoderm, and DACH2 and PAX3 positively regulate each other's expression (By similarity). Probably binds to DNA via its DACHbox-N domain. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DACH/dachshund family."}
+{"protein": "MVLTGPLQRESVSMAKRVSMLDQHKKSSCARVRVAVRLRPYMDEKDEAKATTVCVRGLDSQSLEIVNWRNQLETMQYQFDAFYGDSASQREIYMGSVCHILPHLLIGQNASVFAYGPTGAGKTHTMLGNPNQPGVIPRAVRDLLQMSRTAASAPENENWTYTINMSYVEIYQEKVMDLLEPKNKDLPIREDKDHNILIPGVTQKMINSFADFDEHFIPASQNRTVASTKLNDRSSRSHAVLLIKVQKSQQVVPFRQLTGKLYLIDLAGSEDNRRTGNQGIRLKESGAINSSLFTLSKVVDALNQGLPRIPYRDSKLTRLLQDSLGGSAHSVMITNIAPEQTYYFDTLTALNFAAKSKQIINKPFSQETTQTVVQPAMKRPREETGHIAGSQKRKKSKNDSTESSPNSSMDTAGKQKLNLATLDPAVVERLLKLDKILTEKGKKKAQLLSTPKRERMALLKKWEESQMEIERLKEKQKELEQKAMEAEARLEKSNNSDLSDSSVSENTFRAPLRGRNTSTAKVKKVLRVLPMQGNSQLQSTVEEGIPVFEKKKKKKQVTCEGLENQPTWEMNMRTDLLESGKERILKLLNTGSVKELKSLQRIGDKKAKLIIGWREVNGPFKNVEELACLEGISAKQVSSFIKANIMSSIAS", "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": "MVKTAYVTGYKSYELNIFKENAPEIKYLKAFIENKLKSLIEEGLEWVLIQGQLGIEMWTAEVVISLKEEYPDLKLGVIAPFENHIERWNEQNQIQYQKIIEKADFTESVHHAPYEGPFQFKQTDQFMLDHTDMTVLLYDEEQEASPKYFKRMLVDFAEQTNYTCDIVTFDEINVFINDLQWSEEESFE", "text": "SIMILARITY: Belongs to the UPF0398 family."}
+{"protein": "MAAANPWDPASAPNGAGLVLGHFIASGMVNQEMLNMSKKTVSCFVNFTRLQQITNIQAEIYQKNLEIELLKLEKDTADVVHPFFLAQKCHTLQSMNNHLEAVLKEKRSLRQRLLKPMCQENLPIEAVYHRYMVHLLELAVTFIERLETHLETIRNIPHLAANLKKMNQALAKMDILVTETEELAENILKWRKQQNEVSSCIPKILAEESYLYKHDIIMPPLPFTSKVHVQTINAK", "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 HAUS2 family."}
+{"protein": "MESSRRPLGLTKPSAGXIIKIEAERISPSRLQLLNPIPGVWFPITLGFRALPNSRREKSFSLHKDKECLLPMESQLHSKRDIGTDTTDVPLKHLMASRSSYCPDGIFTILEQGPMLAQSMATISKELSGSQANRPRLGPLPILLKGTQVAMRLFLLGLRPVRYCLKVFMLKAQEGLHLLVDLVRGHNPVGQIIALEAVPTSASLPLL", "text": "FUNCTION: Structural protein that is not essential for the viral replication either in tissue culture or in its natural host. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the coronaviruses I protein family."}
+{"protein": "MSKVQSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKTGHQMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPQTCVDLWVGWGVPKERCIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQKAAGVLPDGMDVRAVNYLFKTPGGNLYHSGDSHYSNYYAKHGNEHQIDVALGSYGENPRGITDKMTSADILRMAESLNTKVVIPFHHDIWSNFQADPQEIRVLWEMKKDRLKYGFKPFIWQVGGKFTWPLDKDNFEYHYPRGFDDCFTIEPDLPFKSFL", "text": "FUNCTION: Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3- keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UlaG family."}
+{"protein": "MRTDVFLQRRKRRDVLLSIIALLLLIFAIVHLVFCAGLSFQGSSSARVRRDLENASECVQPQSSEFPEGFFTVQERKDGGILIYFMIIFYMLLSVSIVCDEYFLPSLEVISERLGLSQDVAGATFMAAGSSAPELVTAFLGVFVTKGDIGVSTIMGSAVYNLLCICAACGLLSSAVGRLSCWPLFRDCVAYAISVAAVIAIISDNRVYWYDGACLLLVYGVYVAVLCFDLRISEYVMQRFSPCCWCLKPRDRDSGEQQPLVGWSDDSSLRVQRRSRNDSGIFQDDSGYSHLSLSLHGLNEISDEHKSVFSMPDHDLKRILWVLSLPVSTLLFVSVPDCRRPFWKNFYMLTFLMSAVWISAFTYVLVWMVTIVGETLGIPDTVMGMTLLAAGTSIPDTVASVMVAREGKSDMAMSNIVGSNVFDMLCLGLPWFIQTVFVDVGSPVEVNSSGLVFMSCTLLLSIIFLFLAVHINGWKLDWKLGLVCLACYILFATLSILYELGIIGNNPIRSCSD", "text": "FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) to the melanosome in exchange for 4 cytoplasmic Na(+) (By similarity). Involved in pigmentation, possibly by participating in ion transport in melanosomes (PubMed:16357253). Predominant sodium-calcium exchanger in melanocytes (PubMed:16357253). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Melanosome Note=Enriched in late-stage melanosomes. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC24A subfamily."}
+{"protein": "MNDLMTKSFMSYVDLKKAAMKDLEAGGDGVELPEVGVTDERLKGFFQETEAVEEEMAAIRDALARLNAANEEGKSLHQPDALRALRGRVNADIIAVLRRARDIRARLEAMDRANAAQRRLSAGCREGTPLDRTRTALTAALRKKLKDLMLDFQALRQRIMSEYKDTVERRYYTLTGEVPEEEVIERIISEGRSEELLCAAVAEHGKGAVLATVHEIQDRHDAAREVERSLLELHQVFLDMAVVVESQGEQLDDIERHVNSATTYVQGGNKELRKAREHQRSSRKWLCIGIIILLLLVLLVIVPIATSFKRS", "text": "FUNCTION: Vesicle trafficking protein that functions in the secretory pathway. SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane protein Cytoplasm. Note=Localizes at the plasma membrane and in the cytoplasm. SIMILARITY: Belongs to the syntaxin family."}
+{"protein": "MGYLRSSFIFSLLAFVTYTYAATIEVRNNCPYTVWAASTPIGGGRRLNKGQTWVINAPRGTKMARIWGRTGCNFNAAGRGSCQTGDCGGVLQCTGWGKPPNTLAEYALDQFSNLDFWDISLVDGFNIPMTFAPTKPSAGKCHAIHCTANINGECPRALKVPGGCNNPCTTFGGQQYCCTQGPCGPTELSKFFKKRCPDAYSYPQDDPTSTFTCPSGSTNYRVVFCPNGVADPNFPLEMPASTDEVAK", "text": "SIMILARITY: Belongs to the thaumatin family."}
+{"protein": "MDVPARVSRRAAAAAARMLLRTARVPRECWFLPTALLCAYGFFANLRPSEPFLTPYLLGPDKNLTERQVYNEIYPVWTYSYLLLLFPVFLATDYLRYKPVILLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYTVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVVGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSSCHGVNGLKVQNGGIVTDTPAANHLPGWEDIESKIPLNLDEPPVEEPEEPKPDRLRVFRVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYAQGLWEKVMPSQNADIYNGGVEAVSTLLGASAVFAVGYIKLSWSTWGEMTLFLCSLLIAAAVYVMDTVQSIWVCYASYVVFRIIYMVLITIATFQIAANLSMERYALVFGVNTFIALALQTLLTLIVVDARGLGLCITTQFLIYASYFAAISVVFLANGIVSIIKKCRKQEDPSSSPQASTS", "text": "FUNCTION: High-affinity transporter for the intake of thiamine (PubMed:11481326, PubMed:11592824, PubMed:12393806, PubMed:22194418, PubMed:12031504, PubMed:24961373). Essential for spermatogenesis (PubMed:14567973, PubMed:14738878). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter (TC 2.A.48) family."}
+{"protein": "MVLLHVLFEHAVGYALLALKEVEEIILLLPQVEECVLNLGKFHNIVRLVAFCPFSSSQVALENANAVSEGVVHEDLRLLLETHLPPKKKKVLLGVGDPKIGAAIQEELGYNCQTGGVIAEILRGVRLHFHNLVKGLTDLSACKAQLGLGHSYSRAKVKFNVNRVDNMIIQSISLLDQLDKDINTFSMRVREWYGYHFPELVKIINDNATYCRLAQFIGNRKELNEEKLEKLEELTMDAAKAKAILDASRSSMGMDISAIDLINIESFSSRVVSLSEYRQSLHTYLRSKMSQVAPSLSALIGEAVGARLIAHAGSLTNLAKYPASTVQILGAEKALFRALKTRGNTPKYGLIFHSTFIGRAAAKNKGRISRYLANKCSIASRIDCFSEVPTSVFGEKLREQVEERLSFYETGEIPRKNLDVMKEAMVQAEEAAAEITRKLEKQEKKRLKKEKKRLAAIALASSENSSAPEECEETSERPKKKKKQKPQEVLQENGMEDPSVSFSKPKKKKSFSKEELVSSDLEETAGTGSLPKRKKSFPKEEPVTDPDESENKRVPKKKRKLSPKEEPLSSGPEEAAASKSSGSKKKKKLRKLSQES", "text": "FUNCTION: Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs. 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 Cytoplasm Nucleus, nucleoplasm. SIMILARITY: Belongs to the NOP5/NOP56 family."}
+{"protein": "MINIWTEKYRPKRLDDVIGEDENINTLKSFVKNGDLPHLIFAGPAGTGKTSTAIALTIELFGDDWKENFLELNASDERGIDIIRNNIKDFAKIRPSNKLGFKIIFLDEADQLTNEAQAALRRTMEMFYSTTRFIFSCNYSSKIIPPIQSRCVVLRFRPLDKEAMERKLREIAKNEKFDIDDDSLDAIYEISDGDMRKAINVMQAIQSTGEIKPSKIYEISGEINKNEYKNLISLSLNGAFSDAKSLLDKMLVDYGLSGIDIIRGMHSAIRNERIANRQKLEILIALAEFEFRISQGGSDNVQMDALLARISYIGSEIT", "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": "MDCPHQDVLHLIKYFRKEWPVVSDSERTTICGADNMLLTLQLALAEVNKQNGKEFSVSLSDVLLTWKYLVKHKLGLACEDTVVPKDYADIQKTYDLFLKNSNSLDLIDIYEKISTAGSSEAHFLSSEQLLDFLTNDVCLSEGTDFPIVSTPCKNNLDTVKVKPTLKRIFLAYLNLLVNAKNDFALAQVLNCPERGLGREAFTDLKHTSRLKNMSIFLVATSFIRTIELGGKGYAPSESDPLRKHLKGLSLFVHFIDRLNEIFGETHDPRTAGELLLSTIKMHLIKGRGSGDPLSEAATEVAQDLDLRIKYLINLVSEDKSSGTTGISPVRPKIRAINRGTASGGRETIKTLLKLLDEEAANPPSKNKADLLCADEENTLFGAFSLFTLFRSPEQTGSSPKALSQRVQKAINKDKPKLKHNLIRSQFACTYKDSNLTQTKQWDFPSMSQVPSCIHPAPKIVPVLCFDEEPLENDLQKGLKQSSGNIDLKTAEQVKNKPCKNVGNKRSKRKQVDIQSETTNGQENEPPQKKAVVELTSSKANKQGVSRNKASKNKLITGQAKLTSFFRV", "text": "FUNCTION: Required to suppress inappropriate homologous recombination, thereby playing a central role DNA repair and in the maintenance of genomic stability. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes to chromatin. SIMILARITY: Belongs to the PARI family."}
+{"protein": "MIEVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVSALPKGAVQPKYEDAMQYEFKVNGEAVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIHNDADSTASISACDGLKGYFKLQGETYPIEPLELSDSEAHAVFKYENVEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIKLAIVVDHGMYTKYSSNFKKIRKRVHQMVSNINEMCRPLNIAITLALLDVWSEKDFITVQADAPTTAGLFGDWRERVLLKKKNHDHAQLLTDTNFARNTIGWAYVGRMCDEKYSVAVVKDHSSKVFMVAVTMTHELGHNLGMEHDDKDKCKCDTCIMSAVISDKQSKLFSDCSKDYYQTFLTNDNPQCILNAPLRTDTVSTPVSGNEFLEAGEECDCGSPENPCCDAATCKLRPGAQCAEGLCCDQCRFKKKRTICRRARGDNPDDRCTGQSADCPRNGLYG", "text": "FUNCTION: [Disintegrin trimucrin]: Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). FUNCTION: [Snake venom metalloproteinase TM-3]: Potent fibrinogenolytic protease which cleaves mainly the Aalpha chain of fibrinogen (FGA) and slightly the Bbeta (FGB) and the gamma (FGG) chains (PubMed:8193588, PubMed:7488093). May possess hemorrhagic activity (PubMed:7488093). Compared to other SVMP, the substrate-binding pocket is relatively shallow (PubMed:12077431). Is less susceptible to tripeptide inhibitors than TM-1 (AC U3KRG1) and TM-2 (PubMed:9703966). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily."}
+{"protein": "MGLGVSAEQPAGGAEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSDQILQESEDFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPPSYHKKPPGTPPPSALPLGAPPPDALPPGPTPEDSPSLETGSRQSDYMEALLQAPGSSMEDPLPGPGSPSHSAPDPDGLPHFMETPLQPPPPVQRVMDPGFLDVSGISLLDNSNASVWPSLPSSTELTTTAVSTSGPEDICSSSSSHERGGEATWSGSEFEVSFLDSPGAQAQADHLPQLTLPDSLTSAASPEDGLSAELLEAQAEEEPASTEGLDTGTEAEGLDSQAQISTTE", "text": "FUNCTION: Key structural protein of the Golgi apparatus (PubMed:33301566). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (PubMed:33301566). Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (PubMed:33301566). However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis (By similarity). Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (PubMed:16489344). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936). SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum- Golgi intermediate compartment membrane. SIMILARITY: Belongs to the GORASP family."}
+{"protein": "MRNEMNLTFSALSQNESFARVTVAAFIAQLDPTLDELTEIKTVVSEAVTNSIIHGYDGNPDGKVHIEVTLDDHVVYLTIRDEGMGITDLEEARQPLFTTKPDLERSGMGFTIMENFMDDVMIDSSPEMGTTIRLTKHLSKSKALCN", "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": "MSEAEAQEPEPVPQPESEPEIQKPGIAAARNQANKKVLATQVQGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKFLRSVGDGETVEFDVVEGEKGAEAANVTGPGGVPVKGSRFAPNRRRFRRRFYRPRADTAGESGGEGVSPEQMSEGERGEETSPQQRPQRRRPPPFFYRRRFRRGPRPNNQQNQGAEVTEQSENKDPVAPTSEALASGDDPQRPPPRRFRQRFRRPFRPRPAPQQTPEGGDGETKAESGEDPRPEPQRQRNRPYVQRRRRQGATQVAATAQGEGKAEPTQHPASEEGTPSDSPTDDGAPVQSSAPDPGIADTPAPE", "text": "FUNCTION: Has a dual function in oocytes: as a DNA-binding protein, binds to the Y-box sequence (CTGATTGGCCAA) in the promoters of target genes to stimulate transcription. May also function at CCAAT-containing promoters that lack the consensus Y-box sequence. Also binds mRNA to promote accumulation of the transcripts it contributes to produce. SUBCELLULAR LOCATION: Cytoplasm Note=Either free or associated with ribonucleoprotein particles."}
+{"protein": "MLMLFLTVAMVHIVALMSPGPDFFFVSQTAVSRSRKEAMMGVLGITCGVMVWAGIALLGLHLIIEKMAWLHTLIMVGGGLYLCWMGYQMLRGALKKEAVSAPAPQVELAKSGRSFLKGLLTNLANPKAIIYFGSVFSLFVGDNVGTTARWGIFALIIVETLAWFTVVASLFALPQMRRGYQRLAKWIDGFAGALFAGFGIHLIISR", "text": "FUNCTION: Conducts the efflux of threonine. FUNCTION: Conducts the efflux of threonine. 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": "MEQVFLEINEKLPGLLTTGGSDATFAESSKLIERCNLALISFTGTPTAVMDDTIKLMKSILASNESYNIDYDQLMDLMSQMVIKYPFDRILELFTVEELALALNSPIERLNIMTCVVVEYSEPSGLFASTTLIDILLQKYLDEDSSVNLVNSIEKVWKKTAQDELIRRRILENNYNFLSEVKNNEPNSLVFTRLLELLKICFTYLKSTEFRNSLFLISKKMIMDAVKDNILVFISICEYFTSIFSIVQDQKSQNPSKIICVRNCENTIMLFGDLFQNRSEFPDIEQFALSYLFKMFKILSYFDDLIVFEKLDNGYIHIEDGNEYLTDFLSFISPQYLYKKHLNIIKSKGHVRPSEISIIRNLCMSSDCFDIIKKNITAEDILAMPYLEQMILLEKMSQYDYSVKFLAQHLPKVMGSLISKDVKELLDRETFDFRLQVINNLIEWDVEQLHIWYEPLTEAKAQCMGTFASKDVGTKIESSFS", "text": "FUNCTION: Involved in DNA mismatch repair in slow-growing cells. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC) (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the proteasome subunit S5B/HSM3 family."}
+{"protein": "MSGSKAESEEKAGSKQCPLVQVNEYKENEHIAYTSLRPIQITTLRKTAKVYLYPFSLSNSKLGLLKLSKSPVVNNSSKSVVHKKKDRKKTRRKVLTSKMKALSSKADSLLLKSSVDAYTESTRLGPKRTSDSATLSVDAESSDEDSAPGLDDFSGLSPYERKRLRNIRENANFFASLQLAESAARLRGMIKKRESPESKRKRPKKKENEIGCRRSMRLLKVDPLGVSLPASPTQPTLVEEEENPLLPPGPLEMIPENQDDSSELLKASLKTWAEMSQTSNEKTKKGLSSIKSYKANLSGMVISEATVRKVTKGAISSVALHPSEVRTLVAAGAKSGQIGLWDLTQQSEDAMYVFYAHSRYVSCLSFSPTNPAHLLSLSYDGTLRCGDFSSAVFEEVYRNEGNSPSSFDFLNDSSSLLVGHWDGHLSLVDRRTPGTSYEKFFNSSLEKIRTVHVHPLSRQYFVTAGLRDVHVYDARFLKSRGSQPLISLTEHSKSIASAYFSPVTGNRVVTTCADCKLRVFDSSSISSQLPLLSTIRHNTVTGRWLTRFQAVWDPKQEDCFIVGSMDHPRRVEVFHESGKNVHSLWGECLVSVCSLSAVHPTRYILAGGNSSGKLHVFMHQET", "text": "FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family."}
+{"protein": "MSEQAQTQQPAKSTPSKDSNKNGSSVSTILDTKWDIVLSNMLVKTAMGFGVGVFTSVLFFKRRAFPVWLGIGFGVGRGYAEGDAIFRSSAGLRSSKV", "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; Single-pass membrane protein Note=The C-terminus is located in the intermembrane space, while the location of the N-terminus has not been determined yet. As some programs predict the presence of 2 closely apposed membrane domains, it has been proposed that the protein may cross the membrane twice and that both termini may face the intermembrane space (PubMed:22114354). Enriched at crista junctions. SIMILARITY: Belongs to the MICOS complex subunit Mic10 family."}
+{"protein": "KRLLQDLNIKINQVIPEGGSVQDLQNLPKAWFNLVPYREVGLMTAIYLEKNFGMPYISTTPMGIVDIAECIRQIQKHVNNLALNQTFNYESYIDQQTRFV", "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": "DRPYSFGL", "text": "FUNCTION: May act as a neurotransmitter or neuromodulator and play a role in the integration of information within the brain. May be involved in the control of visceral muscles due to its ability to behave as potent inhibitors of peristaltic movements. May also fulfill a neurohormonal role on muscles of the gut and heart. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the allatostatin family."}
+{"protein": "MSKASDAVREPLVDKNMAGSKPDQPWMVYLSTFVAVCGSFAFGSCAGYSSPAQAAIRNDLSLTIAEFSLFGSLLTFGAMIGAITSGPIADLVGRKGAMRVSSAFCVVGWLAIIFAKGVVALDLGRLATGYGMGAFSYVVPIFIAEIAPKTFRGALTTLNQILICTGVSVSFIIGTLVTWRVLALIGIIPCAASFLGLFFIPESPRWLAKVGRDTEFEAALRKLRGKKADISEEAAEIQDYIETLERLPKAKMLDLFQRRYIRSVLIAFGLMVFQQFGGINGICFYTSSIFEQAGFPTRLGMIIYAVLQVVITALNAPIVDRAGRKPLLLVSATGLVIGCLIAAVSFYLKVHDMAHEAVPVLAVVGIMVYIGSFSAGMGAMPWVVMSEIFPINIKGVAGGMATLVNWFGAWAVSYTFNFLMSWSSYGTFLIYAAINALAIVFVIAIVPETKGKTLEQIQAIVNP", "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": "MARKRQRRRRRKVTRSQRAELQFPVSRVDRFLREGNYSRRLSSSAPVFLAGVLEYLTSNILELAGEVAHTTGRKRIAPEHVCRVVQNNEQLHQLFKQGGTSVFEPPEPDDN", "text": "FUNCTION: Atypical histone H2A which replaces conventional H2A during late spermatogenesis and is involved in the replacement of histones to protamine in male germ cells (PubMed:28366643). Core component of nucleosome: nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (PubMed:19506029). Nucleosomes containing H2AB1 only wrap 130 bp of DNA, compared to 147 bp for classical nucleosomes (PubMed:19506029). In condensing spermatids, the heterodimer between H2AB1 and H2BC1/TH2B is loaded onto the nucleosomes and promotes loading of transition proteins (TNP1 and TNP2) onto the nucleosomes (PubMed:28366643). Inclusion of the H2AB1-H2BC1/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition proteins (TNP1 and TNP2) (PubMed:28366643). Then, transition proteins drive the recruitment and processing of protamines, which are responsible for histone eviction (PubMed:28366643). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Specifically localizes to the pericentric regions in condensing spermatids (PubMed:17261847). SIMILARITY: Belongs to the histone H2A family."}
+{"protein": "MGTFFQKIADYSKDAVSAGKYLLQGLAVTFDHMRRRPITVQYPYEKLIPSERYRGRIHYEFDKCIACEVCVRVCPINLPVVDWVMNKETKKKELRNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELAAFDRHSLNFDNVALGRLPTSVTSDPSVMPLRELGYLPEGVMDPHELPKDSSRAGKLPIEIMDWMKNKESNKSEDNNLDININSLKVEKDSK", "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; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 23 kDa subunit family."}
+{"protein": "MGSSSFLVLMVSLVLVTLVAVEGVKEGIEKAGVCPADNVRCFKSDPPQCHTDQDCLGERKCCYLHCGFKCVIPVKELEEGGNKDEDVSRPYPEPGWEAKCPGSSSTRCPQK", "text": "FUNCTION: Antibacterial protein. Putative acid-stable proteinase inhibitor. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MFLHSVNLWNLAFYVFMVFLATLGLWDVFFGFEENKCSMSYMFEYPEYQKIELPKKLTKRYPAYELYLYGEGSYAEEHKILPLTGIPVLFLPGNAGSYKQVRSIGSIALRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKAILKLYKGQEFAPTSVAIIGHSMGGLVARALLTLKNFKQDLINLLVTQATPHVAPVMPLDRFITEFYMNVNNYWILNARHINLTTLSVAGGFRDYQVRSGLTFLPKLSHYTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTIRAFFDLIDADTKQITQKPKKKLSVLNHHFIRHPAKQFEENPSIISDLTGTSMWVPVKVSRWSYVAYNESDKIYFAFPLANHRKIYTHAYCQSTMLDTNSWIFGCINSTSMCRQGVDLSWKAELLPTIKSLTLRLQDYPSLSHIVVYVPSVHGSKFVVDCEFFKKEARSMQLPVTHLFSFGLSSRKVTLNTNGLYYNIELLNFGQIYQAFKVNVVSKCTGSKEEITSIYKLHIPWSYEDSLTIAQVPSSTDISLKLHVAQPENDSHVALLKMYTSSDCQYEVTIKTSFPQILGQVVRFHGGALPAYVVSSILLAYGGQLYSLLSTGYCLEYSTILDKEAKPYKVDPFVIMIKFLLGYKWFKELWDAVLLPELDAIVLTSQSMCFPLVSLILFLFGTCTAYWSGLLSSTSVQLLSSLWLALKRPAELPKDIKVMSPDLPVLTVVFLIVSWTTCGALAILLSYLYYVFKVVHLQASLTTFKNNQPVNPKHSRRSEKKSNHHKDSAVQSLRLCANDAEDSLRMHSTVINLLTWVVLLSMPSLIYWLKNLRYYFKLSPDPCKPLAFLLIPAIAILGNTHTVSVKSSKLLKTVSQFPLPLAVGVIAFGSSHLYRVPCFVIIPLVFHALCNFM", "text": "FUNCTION: Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI- anchored proteins from the endoplasmic reticulum to the Golgi (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GPI inositol-deacylase family."}
+{"protein": "MSLFRIFINQLEEDDEDMATSKKMITREEWEKKLNAVKLRKEDMNTLVMNFLVTEGYVEAAEKFQRESGTKPEIDLATITDRMAVKKAVQNGNVEDAIEKVNDLNPEILDTNPELFFHLQQQRLIELIRQGKTEEALEFAQEELAPRGEENQAFLEELEKTVALLVFDDASTCPVKELLDLSHRLKTASEVNAAILTSQSHEKDPKLPSLLKMLIWAQTQLDEKAVYPHINDLSTGKLEDPSE", "text": "SUBCELLULAR LOCATION: Cytoplasm Note=Associates predominantly in the form of large cytoplasmic complexes. SIMILARITY: Belongs to the GID8 family."}
+{"protein": "MFRQSLRSIARTRTGTIGVRTYAEAVNPDVLKVSLVAPHQAIFTNKEVSQVNLPASSGEMGVLANHVPTVEELAPGVVEVIESSGTASKYFVSGGFASILPGSKLSISTVEAHPLDAFSSENIKSLLAEAQKNASSADETVAAEAAIEIEVLEALQAAVH", "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(1) domain and the central stalk which is part of the complex rotary element (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 epsilon chain family."}
+{"protein": "MSYRRELEKYRDLDEDEILGGLTEEELRTLENELDELDPDNALLPAGLRQKDQTTKAPTGPFRREELLDHLEKQAKEFKDREDLVPYTGEKRGKVWVPKQKPMDPVLESVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYQALGSSSIVNKEGLNSVIKPTQYKPVPDEEPNATDVEETLERIKNNDPKLEEVNLNNIRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILRLVEALPYNTSLVELKIDNQSQPLGNKVEMEIVSMLEKNATLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLADLTGPIIPKCRSGV", "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. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus (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": "MLSVMVSSSLVLIVFFLGASEEAKPATTTTIKNTKPQCRPEDYATRLQDLRVTFHRVKPTLQREDDYSVWLDGTVVKGCWGCSVMDWLLRRYLEIVFPAGDHVYPGLKTELHSMRSTLESIYKDMRQCPLLGCGDKSVISRLSQEAERKSDNGTRKGLSELDTLFSRLEEYLHSRK", "text": "FUNCTION: Functional viral IL-10 homolog. Can bind to the human IL-10 receptor and compete with human IL-10 for binding sites. Requires both subunits of the human IL-10 receptor complex to induce signal transduction events and biological activities. IL-10 signaling pathway has several immunosuppressive activities that are exploited by the virus. Inhibits TLR-induced type I interferon production in host plasmacytoid dendritic cells (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-10 family."}
+{"protein": "MLLNWQGRHFMEINHSRITSYEIADYMIRTKSLLSAKELAAILEKEYPHLDVDKRDVYLRLKAIAVSKYSSVLIDDSTRPRRFQIHSLNPEFFRRSRAPRRFDEKLQNELYMTQDEKERREHQPWVMARQLFNKVARQHRHYGNATSARI", "text": "FUNCTION: Trans-activating factor involved in the late regulation of the P1 lytic growth cycle. May be the transcriptional activator of all late P1 functions."}
+{"protein": "MAAQPPTGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYLEVIKAEHVVVPIVTFNKHRQMINLTESKASLAAILEHSLFSTEQKLLAELNAIMGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDETAGRKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTRTVRITFGFNCRNKDHYGIMMYHKNRLIKAYEKVGCQLKANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTILALGEKLNDYWNEMKVKKNAEYPVNLPVEDIQKRPDQTWVQCDACLKWRKLPDGIDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLVHPTYEKTYKKTSKERFRIRQPEILPRILPQINPELLYQTSVSSQSFSPVKESVPRPHLSEVTSPFAARIINLNLASPASEPENSSMKRKLGVHSSILNAKTRRLSNPPVENSSYKNDDDEDVIILEENSTPKPAVDLEVKSDIEVKSEQSHTEQSGIHVDLVSSPKPCVQASSTSTSTSRSDPGITVSTQTDAPGLTVKKEESMEEDMGVRNGTATLSCVGTEAKVQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQSTETDAVFLLDSVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVSYVDGESLKLRSLRVNVGQLLAMIVPDLDLQQVNYDVDVVDEILGQVVEQMSEISST", "text": "FUNCTION: Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response. Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function. Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro. Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0. SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus matrix Nucleus, PML body Chromosome Note=Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent."}
+{"protein": "MDFLFGSRSSKTFKPKKNIPEGTHQYDLMKHAAATLGSGNLRNAVALPDGEDLNEWVAVNTVDFFNQINMLYGTITEFCTEETCGIMSAGPKYEYHWADGLTVKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFHSSAKTILKRLFRVYAHIYHQHFTEVVTLGEEAHLNTSFKHFIFFVQEFNLIERRELAPLQELIDKLTAKDERQI", "text": "FUNCTION: Coactivator of Warts (Wts) kinase in the Hippo/SWH (Sav/Wts/Hpo)signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. 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. 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. Mats is essential for early development and is required for proper chromosomal segregation in developing embryos. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm, cytosol. Cell membrane. Note=Colocalizes with wts and cyclin E at the centrosome. SIMILARITY: Belongs to the MOB1/phocein family."}
+{"protein": "MGEASSFVAVRLMRIIPILAILGATYYIFLTCFASFQATDVPVPEEWRNHDAVVDEVDEITETLTHDPDSRPTPHKLTIAEIEDLENKGEFMGFEDEDEIDVFINLDDDGDWEEDDLKKELGDELEGDFEDEEDEDFGDDDDDDDNDDDVDWSRFAYIQYVTNEDYLCNSVMIFEQLHRLGSKADRLLMYPKEMLEPDAAYSNKRGGQLLIRARDEYNVTLQPIEIQHRDGQDETWADSFTKLLAFNQTQYDRVLSLDSDSMVLQHMDELFQLPPCPVAMPRAYWLYNENPPKRILSSQVMLIQPDDVEFERIVQKMNSIGPNDYDMEIVNSLYLDSALILPHRKYDMLTAEFRNKDHTAYLGSEREKWDSSVALSEAKFVHFSDWPVPKPWINDVETRLANQPDCPEGETSCPDRDIWNGFYTDFTDNKKRVCESVGKTGQKWIHWRRM", "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": "MSNGGTPRSLPSSGQKSIQEICHPLSAEESARSRSPDVLNPGEKDLSLPNGTPVDTSSPASSSSLLNRLQLDDDLDAETRDLFVTVDDPKKHVSTMETYITYRVCTKTTRTEFDLPEYSVRRRYQDFDWLRIKLEDSQPTHLIPPLPEKFVMKGVVDRFSEEFVETRRKALDKFLKRVADHPVLSFNEHFNAFLSAKDLNKRQGLALLTKMGESVKYVTGGYKLRGRPVEFAAMGEYLDMFTQKLGTIDRIAQRIIKEQTEFLMELREYGPVYSSWSSFEEDLHEPLEGVSGCVSNCSSALEELTEDMSEDFLPVLREYVLYIESMKNVLKKRDQVQAEYETKLEAVVFREDKKTPMPTDVEKCQDRVECFNADLKADWDRWQNNKRQDFRQLLTGMADKNIQYYEKCLAAWESLIPLLQDKQDAKGETN", "text": "FUNCTION: Involved in the regulation of endocytosis and in several stages of intracellular trafficking. Together with snx4, involved in autophagosome assembly. SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "MADNSSDEYEEDNKEKKKPSQLTPQQGFSENDDDDDDDSSETDSDDDDDDEEHGAPLEGAYDPADYEHLPVSAEIKELFEYISRYTPQLIDLDHKLKPFIPDFIPAVGDIDAFLKVPRPDGKPDHLGLLVLDEPSTKQSDPTVLSLWLTENSKQHNITQHMKVKSLEDAEKNPKAIDTWIESISELHRSKPPATVHYTRPMPDIDTLMQEWSPEFEELLGKVSLPTVEIDCSLAEYIDMICAILDIPFYKSRIQSLHLLFSLYSEFKNSQHFKALAEGKKVFTPPPNSASQAGDAETLTFI", "text": "FUNCTION: Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. May play a role in chondrocyte maturation and skeletogenesis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Cell projection, cilium. Note=Expression is concentrated at the cilium basal body but is also detected along the length of the cilium. SIMILARITY: Belongs to the IFT46 family."}
+{"protein": "MSAATERERLTNANPNARGKDNSGAAIRQRFLKFYETRGHAVLPSSSLVPEDPTVLLTIAGMLQFKPVFMGQRERAHERATTTQKCVRTNDIENVGVTARHHTFFEMLGNFSFGDYFKKDACQWAWELATGEFGLNPERVWVSVFREDDEAFAIWRDVVGVPESRIKRMDEKDNFWAAGPTGPCGPCSELYYDFYPERGLEGADLDDDSRFIEFYNLVFMELNRDADGGVTPLKNKNIDTGMGLERMAQILQGVPNNYETDLIMPIINKAASMAGIDYNACNDVQKQQLKVIGDHTRAVSYMISDGVFASNIGRGYIVRRLLRRVVRNGRLLGIKPEEGASAFTPAIAEVAISMSEGCDPQVAKNSARILAELEREELSFQKTLGRGEEMLAELIETAKKTKTGLSGKDAFTLYDTYGFPLDITADVATEAGITVDLEGFESAMAEQRSMSQAAHQTVDVTAGNALARVADELGAKSTFIGYESTSSDVSNVLAIVCGGESVEEAPEGAKVDIVLDVTPFYAESGGQVGDNGVLHTADGATLEVSDVQKAGGGRIIVHTATVTKGSIKKGSQVTANVDENSRRRAKSNHTATHLLQSALKKVLGEDVSQAGSLCGFDRLRFDFNSPKAPTEAQLLEVENLVNGWISQSAALTAEEMPIAAAKDKGATMMFGEKYGDVVRVVDVPGISMELCGGTHVSNTAEIGGFKILSEAGIASGIRRIEAVAGAGVVELLQQRDAVVKQLASALRVPPEEITGRVSSLQEDLRATQKLAESLRGELAVAKAGALVSQAREVGEAKVLVARLDGVDPAALKVAAENLAAQLGDGAAIVLGSANGANVGLVALFDDKVQKDGGLKAGQVLGAAAKKCGGGGGGKPGFAQAGGRDATQLDAALDEALTTVTAALSPK", "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 tRNA(Ala) via its editing domain. SUBCELLULAR LOCATION: Plastid, chloroplast Mitochondrion. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
+{"protein": "MALAINVSSSSSSAISSSSFPSSDLKVTKIGSLRLLNRTNVSAASLSLSGKRSSVKALNVQSITKESIVASEVTEKLDVVEVEDFEELAKRLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKECGLHKGNIKENTNGNATANVNGTASVADIFNSENVVNLSRQGIENLMKLENRKEAWIVVLYAPWCPFCQAMEASFDELADKLGGSGVKVAKFRADGDQKDFAKKELQLGSFPTILVFPKNSSRPIKYPSEKRDVDSLTSFLNLVR", "text": "FUNCTION: Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'- phosphosulfate (PAPS). Uses glutathione or DTT as source of protons. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the APS reductase family."}
+{"protein": "MVGSRHPDQCAKRWHHSLDPNVKRGPWTMEEDSSLLEAVQKIGRDWKEIGRELFPSRSTTDIKNRYVILSRRRGPSPAIPENCSSIDIETHSSSLADSKPPIPAELLTPEVDFSIANTPCELDSSNLAPDTLSINMTLPSDLPSYLSLPLPDTAETDHALDESSTAWEIPDWTAFDNQCLFTPGASELEGSFTSRNHEEPPQPLPVPDIPGPSTLVLEDLRPETVNLVIDTLLRTNSKFGMRMYNTGS", "text": "FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MDRKYKDTSSEEEDSLNEDEMAWIPWYCNLKGNEFFATIDEDYINDDFNLTGLSSLVQFYDSALGIILDSDPDDPLSEDQQEALERSADILYGLIHARYILTPKGLAHMHEKFKKAEFGRCPRVFCQNQPVLPVGLADMQGVDTVKVYCPRCNDIFNPKYRRHSHIDGAYFGTTFPHLLLITYPELIPTKPPQQYIPKIYGFKIHKSARERQLQIQQKKNSLSNNNQNNQNNNINNNNNNNNNNNNNNNNNNNNQQNNNNQQNNNTNK", "text": "FUNCTION: Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. SIMILARITY: Belongs to the casein kinase 2 subunit beta family."}
+{"protein": "MDSFPEIEIAEYKVFDESNNNDDNVLNISYGVDENYLDGVGVSIASVVLNNNIPLAFHIICDSYSPCFVKYIERLAVQHHIKISLYLIKVESLEVLPQTKVWSRAMYFRLFAFDYLSKKVNTLLYLDADVVCKGSLQDLLQLDLTEKIAAVVKDVDSIQNKVNERLSAFNLQGGYFNSGVVFVNLKLWKENALTKKAFLLLAGKEADSFKYPDQDVLNILLQDKVIFLPRPYNTIYTIKSELKDKSHKKYSNIINDNTILIHYTGATKPWHAWANYPSVIYYKNARLNSPWKDFPAKDARTIVEFKKRYKHLLVQGHYFKGLLAGSAYLYRKLFHK", "text": "FUNCTION: Adds the glucose(II) group on the galactose(I) group of LPS. SIMILARITY: Belongs to the glycosyltransferase 8 family."}
+{"protein": "MEGWLGNLLAKSVKDKYIPVIVGRRDLWNKVFTPKSVNPDDNYEALEIVGDGVASYFFPSYFLKRFPQLNSPKGVKTVARLKIYYGSKKSFSSIADSLGFWKFIRSGPVPVNPSTRESLLEDTFEAFLGAVCMAVDDEYSIDGLGAVVAYKIMADIFDDMDISLEYTALFDTVTRLKELMDVKKDVLGGDAVYNHRGDTTVITLKGRVIGKATGAIKRDRAKEAAGQALDLLRREGHFREHDDDAVVKVAKGPAGDGLVVAQSALGGFTVFGAESGVVEGSGGTVAQALSRVVGTKRPSAVEVAGGDYKSLLKEYLESVGETDSVNYIHEGVTVTMTRKGKPVATANHLVKKVREQLASRDYYRTVHAKGV", "text": "FUNCTION: Digests double-stranded RNA. SIMILARITY: Belongs to the IIV-6 142R family."}
+{"protein": "MVEVMKFTKNKIAALLSLTLLGVYGCGSTPSSSDAEGAVEDVGGTIPDFESAAFFKKVKKDHRKAEVVSDQGVTSGSSALKVNFDSVSEANKFKYWPNVKVHPDSGFWNWNAKGSLSLDITNPTDSPANIILKLADNVGVMGSGDNQLNYAVNVPAGETVPVEMLFNGTKRKLDGYWGGEKINLRNIVEFQIFVQGPMDAQTVIIDNFNLVDATGDFIEASGQEVKVSGPIPTVASITSFDEGQPTFVAFDRSAAATVTELKTDMGGLLAVKLAATNAYPNITFKAPQPWDWSEYGDFSLAFDLESKADEPLQLFVRVDDAENENWGGTANGVVDSMSSYVTLAPGDDGTFYLPLGQTGSQIVSGMRAEPPKKSYNAQAISYGWGEKSLDTSNIVSFQLYLQNPTKDAEFNIKSVRLIPNIDADATRYEGLIDQYGQFTGSEWPKKITEDEELETMGKLAKMSLKSTSQMPGRSIYGGWADGPKLKGTGFFRTEKVDGKWSLVDPQGNLFFATGVDNIRMDDTVTITGHDFADKDKRSGKEVASEVRRSMFTWLPEDDDVLAENYDYANWVHSGALKKGEVFSFYGANLQRKYGGTFSEAEKVWKDITIDRMVDWGFTTLGNWADPMFYDNKKVAYVANGWIFGDHARISTGNDYWGPIHDPFDPEFVNSVKAMTKKLMTEVDKNDPWMMGVFVDNEISWGNTKNDANHYGLVVNALSYDMKKSPAKAAFTEHLKEKYWAIEDLNTSWGVKVASWAEFEKSFDHRSRLSKNMKKDYAEMLEMLSAKYFSTVRAELKKVLPNHLYLGAPFADWGVTPEIAKGAAPYVDVMSYNLYAEDLNSKGDWSKLAELDKPSIIGEFHFGSTDSGLFHGGIVSAASQQDRAKKYTNYMNSIADNPYFVGAHWFQYIDSPTTGRAWDGENYNVGFVSITDTPYVPLVEAAKKFNQDVYMLRYKK", "text": "FUNCTION: Hydrolyzes agarose to yield predominantly neoagarotetraose and neoagarohexaose. SIMILARITY: Belongs to the glycosyl hydrolase 50 family."}
+{"protein": "MIKARYFYLYKLIVRCRFFIAKYNTLFKQQVIEFYIQNGKNYSLISKHFQLDSRTLRHWINQFNHSRINGLAVLGKTRNYSLKFKLNVIQTVKNGQFL", "text": "SIMILARITY: Belongs to the IS150/IS1296 orfA family."}
+{"protein": "MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVGERARSLSITHIISSDLGRTKRTAEIIAQACGCDITFDSRLRELDMGVLEKRQIDSLTEEEEGWRRQLVNGTQDGRIPGGESMQELSDRVHAALASCLELPQGSRPLLVSHGIALGCLVSTILGLPAWAERRLRLRNCSISRIDYQESQWLASGWVVETAGDVSHLDAPALDELQR", "text": "SIMILARITY: Belongs to the phosphoglycerate mutase family. GpmB subfamily."}
+{"protein": "MILTVTPNPAVDHTIHFDEPLQTGVVHRTDDAVFTAGGKGINVAKYASALDADVTASGFLGGHFGKFVRDRLDADGIASDFVTVDADTRLNTTVLAADGEYKLNHNGPQIRAADVDELVETAQANEPDTLLVGGSLPPGMSLSDVDRLARAGDWKIAVDMGGEYLAELDADYYVCKPNRSELAAATGRTVETEADAVEAAEELHARGFEYVLASLGADGALLVTDDEVLSAPALDVEVVDTVGAGDAVMSGFLAAREHGLSDADALRMGVLTASRVVGVAGTRVPDLEDVLTNETHVEVTTVRTR", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l- phosphate to fructose-l,6-bisphosphate. Involved in the utilization of fructose as a sole carbon and energy source. SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
+{"protein": "MATSLSADSPQQLSSLSTQQTILLLLVSVLAIVHLGQWLLRQWRRKPWSSPPGPFPWPLIGNAASVGRASHLYFARLARRYGDVFQIRLGSCPVVVLNGESAIHQALVQQGGVFADRPPFASFRVVSGGRSLAFGHYSERWKERRRAAYGTMRAFSTRHPRSRGLLEGHALGEARELVAVLVRRCAGGACLDPTQPIIVAVANVMSAVCFGCRYNHDDAEFLELLSHNEEFGRTVGAGSLVDVMPWLQLFPNPVRTIFREFEQINRNFSNFVLDKFLRHRESLVPGAAPRDMMDAFILSAEKKATGDPGDSPSGLDLEDVPATITDIFGASQDTLSTALLWLLILFTRYPDVQARVQAELDQVVGRDRLPCMSDQPNLPYVMAFLYESMRFTSFLPVTLPHATTANTFVLGYYIPKNTVVFVNQWSVNHDPAKWSNPEDFDPARFLDKDGFINKALASSVMIFSVGKRRCIGEELSKTLLFLFISILAHQCNFKANQNEPSNMSFSYGLSIKPKSFKIHVSLRESMKLLDSAVEKLQAEEACQ", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (By similarity). 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) (By similarity). Exhibits catalytic activity for the formation of hydroxyestrogens from 17beta-estradiol (E2), namely 2- and 4-hydroxy E2 (PubMed:23821647). Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites (By similarity). May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (By similarity). Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system (PubMed:20972997). Additionally, displays dehydratase activity toward oxygenated eicosanoids including hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2 (By similarity). Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA- damaging products (By similarity). Plays an important role in retinal vascular development. Under ambient/hyperoxic O2 conditions, promotes angiogenesis and capillary morphogenesis of retinal endothelial cells and pericytes, likely by metabolizing the oxygenated products symptomatic of oxidative stress (By similarity). Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein Mitochondrion Note=Located primarily in endoplasmic reticulum. Upon treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), CYP1B1 is also targeted to mitochondria. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MDENGASFQVLCLATIGFHHLRGPEIEHLFPESMDFPKEWSILPFLSLPDGAHSSEKDFVYFTLPFPNDEGTVFGLSCTRQLNASSLKNIPSDVTRSSVQKAVVVITTSPPFGHIKDNLDIVTNAYFSQGDFSNLDVLRDFFHVLTRKEQDVHIALNINLKSFLCEWRQNALVLLKVLLLGKRILVYDKSAERLGNFQYSLLSLIPCMMSHLQDVSSPSAHSLEKSLHKPASLQTSDKRSLLAYTGFPLIIFGEGSMFSPYTPLQLVHVLEAKSSTSWLAGTTNTLIMLNQNKMAEVIVRSDTHQIEFVDPTIKNLTSLTYTDKSWMEDIISRVESSLEMELPGFEGSDDWIRNQFELYIFGMLATVKYYNFLKKQDDSILSQYHYLPSTSCISDYGETFLLEWMKTNTFRIWNNIADDDLFDVILPKHPCKEEHKVPISARIATLFSAVKITPKSRDGEDEGSKEPAV", "text": "FUNCTION: Functions in the late secretory pathway. Required for the generation of secretory vesicles as well as for actin polarization and polarized growth (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AVL9 family."}
+{"protein": "MFDYKLLSALAAVIEQAGFERAAQVLGLSQSAISQRIKLLEARVGQPVLVRVTPPAPTEIGRRLLNHVQQVRLLERDLQSLVPALDEEGLPERLRIALNADSLATWWAGAVGDFCAEHHLLLDLVVEDQTVGLKRMRAGEVAACVCASERPVAGARSLLLGAMRYRAMASPEFIVRHFPQGVRAEQLPRTPALVFGPDDFLQHRYLASLGVDGAFEHHLCPSSEGFIRLTEAGLGWGLVPELQVREQLERGLLLELLPDKPIDVPLYWHHWRNGGQLLGLLTEHLARLSAQWLVPWEQP", "text": "FUNCTION: Controls the transcription of genes involved in arginine and lysine metabolism. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MAPSDTPPSAEDLPSQGELALFAPPATAEDALVPASMVNAWIYCPRLAVLEWGRGEKARSVDLIAGLRAHQATESGPTPALPDPMVLREDQSLKTRKLSLSSERLGLTAELDLLDVEEGVVIPVEIKVGKRPSVDEGAYLPERAQVCAQALLLREAGYTCLEGALWFAESRERVTVDLTEALVTATLVATSDLRLTVASGRLPPPLDHSAKCPRCSLLPICLPDEIAWFRKGSIARTPPPPASPALPLYGQTPGARIGKKDRGGSVCLDRMAAWLSSRPVPCYAAIGMLNTASGASHPSVARHADGGASARSFRLPTAFRRPVRRSLPCYAAR", "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). This may be a 5' to 3' ssDNA exonuclease (By similarity). SIMILARITY: Belongs to the CRISPR-associated exonuclease Cas4 family."}
+{"protein": "MAQLPPKIPTMTTPNWPDFSSQKLPSIAATAAAAATAGPQQQNPSWMDEFLDFSATRRGTHRRSISDSIAFLEPPSSGVGNHHFDRFDDEQFMSMFNDDVHNNNHNHHHHHSINGNVGPTRSSSNTSTPSDHNSLSDDDNNKEAPPSDHDHHMDNNVANQNNAAGNNYNESDEVQSQCKTEPQDGPSANQNSGGSSGNRIHDPKRVKRILANRQSAQRSRVRKLQYISELERSVTSLQTEVSVLSPRVAFLDHQRLLLNVDNSAIKQRIAALAQDKIFKDAHQEALKREIERLRQVYHQQSLKKMENNVSDQSPADIKPSVEKEQLLNV", "text": "FUNCTION: Transcriptional activator. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MPRTQRNDNFIDKSFTVMADIILKMLPANKKAKEAFVYYRDGMSAQADGEYAEALDNYYEALTLEEDPNDRSYILYNIGIIHASNGEHEKALEYYEEAIQLNPRMPSALNNIAVIYHFQGEKAREDGQQAEAEALYDKAAEYWKQAIRLAPNNYIEAQNWLKITGRSEIDVFF", "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": "MTPASRSACRWALLLLAVLWPQQRAAGSGIFQLRLQEFVNQRGMLANGQSCEPGCRTFFRICLKHFQATFSEGPCTFGNVSTPVLGTNSFVVRDKNSGSGRNPLQLPFNFTWPGTFSLNIQAWHTPGDDLRPETSPGNSLISQIIIQGSLAVGKIWRTDEQNDTLTRLSYSYRVICSDNYYGESCSRLCKKRDDHFGHYECQPDGSLSCLPGWTGKYCDQPICLSGCHEQNGYCSKPDECICRPGWQGRLCNECIPHNGCRHGTCSIPWQCACDEGWGGLFCDQDLNYCTHHSPCKNGSTCSNSGPKGYTCTCLPGYTGEHCELGLSKCASNPCRNGGSCKDQENSYHCLCPPGYYGQHCEHSTLTCADSPCFNGGSCRERNQGSSYACECPPNFTGSNCEKKVDRCTSNPCANGGQCQNRGPSRTCRCRPGFTGTHCELHISDCARSPCAHGGTCHDLENGPVCTCPAGFSGRRCEVRITHDACASGPCFNGATCYTGLSPNNFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLVVLLVLLVMVVVAVRQLRLRRPDDESREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKLQNHTLDYNLAPGLLGRGGMPGKYPHSDKSLGEKVPLRLHSEKPECRISAICSPRDSMYQSVCLISEERNECVIATEV", "text": "FUNCTION: Involved in the Notch signaling pathway as Notch ligand (PubMed:11134954). Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting (By similarity). Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types (PubMed:22323600). During spinal cord neurogenesis, inhibits V2a interneuron fate (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MIRYKGFILFLLLMLIGCEQREELISNLSQRQANEIISVLERHNITARKVDGGKQGISVQVEKGTFASAVDLMRMYDLPNPERVDISQMFPTDSLVSSPRAEKARLYSAIEQRLEQSLVSIGGVISAKIHVSYDLEEKNISSKPMHISVIAIYDSPKESELLVSNIKRFLKNTFSDVKYENISVILTPKEEYVYTNVQPVKEIKSEFLTNEVIYLFLGMAVLVVILLVWAFKTGWFKRNKI", "text": "FUNCTION: Involved in the secretion of the Ipa antigens. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the YscJ lipoprotein family."}
+{"protein": "MQGPAGNASRGLPGGPPSTVASGAGRCESGALMHSFGIFLQGLLGVVAFSTLMLKRFREPKHERRPWRIWFLDTSKQAIGMLFIHFANVYLADLTEEDPCSLYLINFLLDATVGMLLIYVGVRAVSVLVEWQQWESLRFGEYGDPLQCGAWVGQCALYIVIMIFEKSVVFIVLLILQWKKVALLNPIENPDLKLAIVMLIVPFFVNALMFWVVDNFLMRKGKTKAKLEERGANQDSRNGSKVRYRRAASHEESESEILISADDEMEESDVEEDLRRLTPLKPVKKKKHRFGLPV", "text": "FUNCTION: Acts as a regulator of store-operated Ca(2+) entry (SOCE) at junctional sites that connect the endoplasmic reticulum (ER) and plasma membrane (PM), called ER-plasma membrane (ER-PM) junction or cortical ER (PubMed:26322679, PubMed:26644574). SOCE is a Ca(2+) influx following depletion of intracellular Ca(2+) stores (PubMed:26322679). Acts by interacting with STIM1, promoting STIM1 conformational switch (PubMed:26322679). Involved in STIM1 relocalization to ER-PM junctions (PubMed:26644574). Contributes to the maintenance and reorganization of store-dependent ER-PM junctions (PubMed:26644574). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Colocalizes with STIM1 at ER-plasma membrane (ER-PM) junctions, also called cortical endoplasmic reticulum (ER), in store-depleted calcium cells (PubMed:26644574). May translocate to ER-PM junctions in a STIM1-dependent manner in store- depleted cells (Probable). SIMILARITY: Belongs to the STIMATE family."}
+{"protein": "MNTFSQVWVFSDTPSRLPELMNGAQALANQINAFVLNDADGAQAIQLGANHVWKLNGKPDDRMIEDYAGVMADTIRQHGADGLVLLPNTRRGKLLAAKLGYRLKAAVSNDASTVSVQDGKATVKHMVYGGLAIGEERIATPYAVLTISSGTFDAAQPDASRTGETHTVEWQAPAVAITRTATQARQSNSVDLDKARLVVSVGRGIGSKENIALAEQLCKAIGAELACSRPVAENEKWMEHERYVGISNLMLKPELYLAVGISGQIQHMVGANASQTIFAINKDKNAPIFQYADYGIVGDAVKILPALTAALAR", "text": "FUNCTION: Required for anaerobic carnitine reduction. May bring reductant to CaiA. SIMILARITY: Belongs to the ETF alpha-subunit/FixB family."}
+{"protein": "MNRTTSRQTTSSSSYKRMFGGEGRPSVGMARSTLSSRQYSSPVRSSRMSYSVSAPPSIYASKNVRLRSSAPMPRLSSDTVDFALSDAINSEFKANRTNEKAEMQHLNDRFASYIDKVRFLEQQNKILLAELEQLKGKGASRIGDLYEDEMRDLRRQVDQLTNEKAHVEVDRDNMGEDIERLREKLQDEMIQKEEAEHNLQSFRQDVDNASLARLDLERKVESLQEEIIFLRKLHDEEVAELQAQIQDQHVQIDMDVAKPDLTAALRDVRVQYETLASRNLQDSEDWYKSKFADLSEAANRNTDAIRQAKQEANEYRRQVQALTCEVDSLKGTNESMERQMRELEESFGCEANNFQDTISRLEDDIRNMKDEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRITTPMPNFSSFNLRESMLEARPMIDNLSKKVVIKTIETRDGHVINESTQNHDDLE", "text": "FUNCTION: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Nucleus matrix. SIMILARITY: Belongs to the intermediate filament family."}
+{"protein": "MILQAWRSLQLLYLLEAISLLPCTEALLCYEATASAFRAVSLHNWKWLLLRSMVCNQREGCEETVVFIETGTSKGVLSFKGCSSAFSYPPQISYLVSPPGVSIASYSRVCRSYLCNNLTNLEPFVRLKASQPMSTLPSAKSCPSCVGKHDQECLPSFVTTENCPFAASSCYSSTLKFQAGNLNTTFLIMGCARDSHKLLADFQHIGSIRVTEVINVLDKSEAVSAGHCSQGISWSVLLCLLILLRD", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor."}
+{"protein": "MFSHLNQNTSGRHNSMDLNNSSISNFGTPVEQSTPALLFGKRKATVPSSYTASPLNTASAPCSDIFAVSAPAVPQHLKDTPGSKSVHWSPSLVQSGEKSAAQTQNTPANLSFGGNSSFSAPTKPAPQSIQTSSFGGQAMHAPPLRSLRDKVEPAKKISRRNTFTARSTPLSTPITQRVTSRLAEAEEQPMEEEADAADTWVTVFGFQPSQVSILLNLFSRHGEVVSHQTPSKGNFIHMRYSCVTHAQQAISRNGTLLDQDTFIGVVQCTNKDVINGSASGIVARSSNIAAAANRSASMYNSFVENDMADQSVNHNENSVLNSSNVFDANNSLNSSRISVRSGVGMRPLAADQRTNILQGTPSVRKAPDGLLNKFWNTIGLN", "text": "FUNCTION: Functions as a component of the nuclear pore complex (NPC) (By similarity). 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 (PubMed:35852146). Thereby required for nuclear import (PubMed:35852146). Required for the proper organization of chromosomes on the mitotic spindle during anaphase (PubMed:28122936). SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane. SIMILARITY: Belongs to the Nup35 family."}
+{"protein": "MVLGLRSKIIPLPDHKLGNIKLGSVTNAICHRPCRVRCSHSTASSMEEAKERIRETFGKIELSPSSYDTAWVAMVPSRYSMNQPCFPQCLDWILENQREDGSWGLNPSHPLLVKDSLSSTLASLLALRKWRIGDNQVQRGLGFIETHGWAVDNKDQISPLGFEIIFPCMINYAEKLNLDLPLDPNLVNMMLCERELTIERALKNEFEGNMANVEYFAEGLGELCHWKEMMLRQRHNGSLFDSPATTAAALIYHQYDEKCFGYLNSILKLHDNWVPTICPTKIHSNLFLVDALQNLGVDRYFKTEVKRVLDEIYRLWLEKNEEIFSDVAHCAMAFRLLRMNNYEVSSEELEGFVDQEHFFTTSSGKLMNHVAILELHRASQVAIHERKDHILDKISTWTRNFMEQKLLDKHIPDRSKKEMEFAMRKFYGTFDRVETRRYIESYKMDSFKILKAAYRSSGINNIDLLKFSEHDFNLCQTRHKEELQQMKRWFTDCKLEQVGLSQQYLYTSYFIIAAILFEPEYADARLAYAKYAIIITAVDDFFDCFICKEELQNIIELVERWEGYSTVGFRSERVRIFFLALYKMVEEIAAKAETKQGRCVKDHLINLWIDMLKCMLVELDLWKIKSTTPSIEEYLSVACVTIGVPCFVLTSLYLLGPKLSKDVIESSEVSALCNCTAAVARLINDIHSYKREQAESSTNMVSILITQSQGTISEEEAIRQIKEMMESKRRELLGMVLQNKESQLPQVCKDLFWTTINAAYSIHTHGDGYRFPEEFKNHINDVIYKPLNQYSP", "text": "FUNCTION: Involved in the biosynthesis of cis-abienol, a labdane diterpene that can be used as synthesis precursor of ambergris substitution fragance products. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "TVNANGEVKRQRTSYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKEHKMASMNIVPYHMSPYGHPY", "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. Deformed subfamily."}
+{"protein": "MRTLWIVAVWLTGVEGDLSQFGDMINKKTGTFGLFSYIYYGCYCGWGGKGKPQDATDRCCFVHDCCYGSVNGCDPKLSTYSYSFQNGDIVCGDDDPCLRAVCECDRVAAICSGENMNTYDKKYMLYSLFDCKEESEKC", "text": "FUNCTION: Snake venom phospholipase that inhibits ADP- and collagen- induced human platelet aggregation. This inhibition is completely inhibited by abolition of catalytic activity in case of collagen as inducer and partially inhibited in case of ADP as inducer. 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": "MLLSSPTTPSRGRTPSAVERLEADKAKYVKTHQVIVRRQEPALRGGPGPLTPHPCNELGASASPRTPGPARRGSGRRQPRPDSLIFYRQKRDCKASVNKENAKGQGLVRRLFLGATRDAAPSSPAPTERPGAPAGWAGSPDTPEATGKRAVCPTCSLPLSEKERFFNYCGLERALVEVLGAERFSPQSWGAEHGPQVATSPPPGSGDTSDWTSSDRDAGSPDCAGGGGGSEAAGSARDGRPTVSVVERNARVIQWLYGCQRARAPPRESEV", "text": "SIMILARITY: Belongs to the FAM110 family."}
+{"protein": "MHIRNPYRTPIDYQALSEAFPPLKPFVSVNADGTSSVDLTIPEAQRAFTAALLHRDFGLTMTIPEDRLCPTVPNRLNYVLWIEDIFNYTNKTLGLSDDRPIKGVDIGTGASAIYPMLACARFKAWSMVGTEVERKCIDTARLNVVANNLQDRLSILETSIDGPILVPIFEATEEYEYEFTMCNPPFYDGAADMQTSDAAKGFGFGVGAPHSGTVIEMSTEGGESAFVAQMVRESLKLRTRCRWYTSNLGKLKSLKEIVGLLKELEISNYAINEYVQGSTRRYAVAWSFTDIQLPEELSRPSNPELSSLF", "text": "FUNCTION: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product (PubMed:28763571, PubMed:31150155). The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD (PubMed:28763571, PubMed:31150155). 4-hydroxy-L- tryptophan is accepted as substrate by psiD as well (PubMed:28763571). The cytochrome P450 monooxygenase psiH then converts tryptamine to 4- hydroxytryptamine (PubMed:28763571). The kinase psiK catalyzes the 4-O- phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin (PubMed:28763571, PubMed:31150155). The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin (PubMed:28763571, PubMed:31150155). 4-hydroxy-6-methyl-l- tryptophancan also be converted the decarboxylase PsiD, kinase PsiK, and methyltransferase PsiM into respectively 6-methyl-norbaeocystin, 6- methylbaeocystin, and 6-methylpsilocybin (PubMed:31150155). SIMILARITY: Belongs to the methyltransferase superfamily. METTL16/RlmF family."}
+{"protein": "MEPEINCSEFCDSFPGQELDRRPLHDLCKTTITESQHSSTAASPLSPALLGIMWTFLSCGLLLVLFFLAFTIRCRKNRIVKMSSPNLNVVTLLGSCLTYISAYLFGIQDALEGSSVEALIQTRLSLLCIGTSLVFGPILGKSWRLYKVFTQRVPDKRVIIKDLQLLGLVAALVVADVILLVTWVLTDPIQCLQMLGVSMKVTGRDVSCSLTNTHFCASRYSDVWIALVLGCKGLLLLYGAYLAGLTNHVSSPPVNQSLTIMVGVNLLLLTAGLLFVVTRYLHSWPNLVFGLTSGGIFVCTTTVNCCVFIPQLKQWKAFEGENQTMRHMAKYFSTPSKSFHSQFDEDPSCHLRDEKSCMERLLTEKNAVIESLQEQVSNAKEKLVKLMSAECTYDSPEWAVPDAASARGLALPGPSECPAVSENESGAAARDSLHVPAACQHVQGPGASRRDTSPSPAQQDNMPLKQYCDHLDTGCNQKPKAEQSEGPERGDQEPMAPSQRLMADGVACEPHKPRQSPEGLPKKLPGVSSVVREKLQEVLQELDLGSEAPLSPLPCPQQLWKSTTSRSPQKLSPSKLGFSPYVVRRRRAAQRARSHIPGSVGLNVGHQANSTVSSSQSGLIVQNRDSPRLDHHNARSKVPRSSSVKPSPLSEPRRKQGTLEGSKQCETEPQEAGGACNVAFPCQSSASVQAQSPAAPCLPSSPALPRQRQPRPRLSPGCPSLSSGCYNLDSESSSSDEFFCRCHRPYCEICFQSSLDSNDSDTSDSDLEQASGLASWEKLWARSKPVVNFKDDLKPTLV", "text": "FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B receptor subfamily."}
+{"protein": "MAPASASGEDLRKLPTMAEVNGEQDFIDLTRETRPRTKDRSGLYVIDLTRAEGENRPIATLDLTLEPVTPSQKEPTSLQTCASLSGKAVMEGHVDRSSQPTARRIINSDPVDLDLVEENTFVGPPPATSISGGSVYPTEPNCSSATFTGNLSFLASLQLSSDVSSLSPTSNNSRSSSSSSNQKAPLPCPQQDVSRPPQALPCPLRPLPCPPRASPCPPRASSCPPRALSCPSQTMQCQLPALTHPPQEVPCPRQNIPGPPQDSLGLPQDVPGLPQSILHPQDVAYLQDMPRSPGDVPQSPSDVSPSPDAPQSPGGMPHLPGDVLHSPGDMPHSSGDVTHSPRDIPHLPGDRPDFTQNDVQNRDMPMDISALSSPSCSPSPQSETPLEKVPWLSVMETPARKEISLSEPAKPGSAHVQSRTPQGGLYNRPCLHRLKYFLRPPVHHLFFQTLIPDKDTRENKGQKLEPIPHRRLRMVTNTIEENFPLGTVQFLMDFVSPQHYPPREIVAHIIQKILLSGSETVDVLKEAYMLLMKIQQLHPANAKTVEWDWKLLTYVMEEEGQTLPGRVLFLRYVVQTLEDDFQQTLRRQRQHLQQSIANMVLSCDKQPHNVRDVIKWLVKAVTEDGLTQPPNGNQTSSGTGILKASSSHPSSQPNLTKNTNQLIVCQLQRMLSIAVEVDRTPTCSSNKIAEMMFGFVLDIPERSQREMFFTTMESHLLRCKVLEIIFLHSCETPTRLPLSLAQALYFLNNSTSLLKCQSDKSQWQTWDELVEHLQFLLSSYQHVLREHLRSSVIDRKDLIIKRIKPKPQQGDDITVVDVEKQIEAFRSRLIQMLGEPLVPQLQDKVHLLKLLLFYAADLNPDAEPFQKGWSGS", "text": "FUNCTION: [Isoform 5]: Inhibits the protease activity of CAPN3. FUNCTION: [Isoform 1]: Inhibits the protease activity of CAPN3. SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm Cytoplasm, myofibril, sarcomere."}
+{"protein": "MQEQKLQENDFSTLQTFKRLWPMIKPFKAGLIVSGVALVFNALADSGLIYLLKPLLDDGFGKANHSFLKMMAFVVVGMIILRGITNFISNYCLAWVSGKVVMTMRRRLFKHLMFMPVSFFDQNSTGRLLSRITYDSQMIASSSSGSLITIVREGAYIISLFAVMFYTSWELTIVLFIIGPIIAVLIRLVSKIFRRLSKNLQDSMGELTSATEQMLKGHKVVLSFGGQHVEEVHFNHVSNDMRRKSMKMVTANSISDPVVQVIASLALATVLYLATTPLIAEDNLSAGSFTVVFSSMLAMMRPLKSLTAVNAQFQSGMAACQTLFAILDLEPEKDDGAYKAEPAKGELEFKNVSFAYQGKDELALNNISFSVPAGKTVALVGRSGSGKSTIANLVTRFYDIEQGEILLDGVNIQDYRLSNLRENCAVVSQQVHLFNDTIANNIAYAAQDKYSREEIIAAAKAAYALEFIEKLPQVFDTVIGENGTSLSGGQRQRLAIARALLRNSPVLILDEATSALDTESERAIQSALEELKKDRTVVVIAHRLSTIENADEILVIDHGEIRERGNHKTLLEQNGAYKQLHSMQFTG", "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": "MVYSKTFRVEEKSITVSARGTIGVVFYRDFAYLPAVSLICFVPKEEFDIRFLFHALRAIKFKKQGSATGQLTVAQFKEYGIHVPSLKKQKEIAAILDPLYSFFTDLNEGLPAEIELRKKQLDYYQNFLFNWIQKQKELVEQASTN", "text": "FUNCTION: The C-terminal section of a specificity (S) subunit of a type I methyltransferase (MTase); this subunit dictates DNA sequence specificity. The single R subunit has multiple frameshifts and is probably not expressed. SIMILARITY: Belongs to the type-I restriction system S methylase family."}
+{"protein": "MQFLNMFFFDIYPYIAGAVFLIGSWLRYDYGQYTWRAASSQMLDRKGMNLASNLFHIGILGIFVGHFFGMLTPHWMYEAWLPIEVKQKMAMFAGGASGVLCLIGGVLLLKRRLFSPRVRATTTGADILILSLLVIQCALGLLTIPFSAQHMDGSEMMKLVGWAQSVVTFHGGASQHLDGVAFIFRLHLVLGMTLFLLFPFSRLIHIWSVPVEYLTRKYQLVRARH", "text": "FUNCTION: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MSQSRAPAREPSETPSQREQIRSHMKMVIQQLEGILKELKDVAHELREVVGQIDKLTSDLELDLDADDWTVATASSTSSSERGLCEAFRLDFLGQDSLSDSWDFCSFLESSSRRSARDDTKPPPTTASVYSQMNGGLPVPNGPLIITPDSSSEEASSSTHSQSQKTSRTAGTRERVRFSDKILYHALCCDDDEDEDEDEDGRDEEEDKLDTDSERSPLAGSPVPPLPELYNCREPPAGGSHTIPRKDALNPGCRKKLLRNSSTQTVSDKSTQTLLPYVPAKHRNKDL", "text": "FUNCTION: May be a component of the protein machinery at the inhibitory synapses, probably acting as a scaffold. SUBCELLULAR LOCATION: Postsynaptic density. SIMILARITY: Belongs to the INSYN1 family."}
+{"protein": "MSLERSTSPNPTERTSLLSDTASTISSRDDVEQSSLKQRRTPIPTGQLGGKVSMHSIIINAEGHLWPYINQFVNDIGVSDGNPRNVGFYSGLIESVFACGEVCSIFMLSRLSDRIGRRPVLLPSALGIAVFTALFGLSSSFTMMLTLRVCAGLLAGATPIVHSIVSELTDDTNNALVVPLYGLITPIGFAIGPLIGGTLEHAATKYPNVFGYELFRKYPYFLPSFVPCCMAIVGVTFGYFFLKETLPSLVKSKKRLERQRSSSSISSENSTLYGATEHIRDSTEETAADEEPDSKPKGITELIRDPSIRAIMASGTFLMFLYTSSDVIFSLYCFTAVEDGGVGLPPEKIGYAFSVAGLIAMLMQLCITPWVLRTFDKAKVYHFCMCSFPLVFALMGCLNPLAQTGYSEINKTLHPTTTGLLYAAIAILLLLARVCVMAFPISMMLVKQTADKHSLATANGLVQVAMTLARAFCPTISSSVFAYSTSHNILGGHFWVVVMVFISLVGVWQSTKIARVTKTKEQL", "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). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
+{"protein": "MAHVPARTSPGPGPQLLLLLLPLFLLLLRDVAGSHRAPAWSALPAAADGLQGDRDLQRHPGDAAATLGPSAQDMVAVHMHRLYEKYSRQGARPGGGNTVRSFRARLEVVDQKAVYFFNLTSMQDSEMILTATFHFYSEPPRWPRALEVLCKPRAKNASGRPLPLGPPTRQHLLFRSLSQNTATQGLLRGAMALAPPPRGLWQAKDISPIVKAARRDGELLLSAQLDSEERDPGVPRPSPYAPYILVYANDLAISEPNSVAVTLQRYDPFPAGDPEPRAAPNNSADPRVRRAAQATGPLQDNELPGLDERPPRAHAQHFHKHQLWPSPFRALKPRPGRKDRRKKGQEVFMAASQVLDFDEKTMQKARRKQWDEPRVCSRRYLKVDFADIGWNEWIISPKSFDAYYCAGACEFPMPKIVRPSNHATIQSIVRAVGIIPGIPEPCCVPDKMNSLGVLFLDENRNVVLKVYPNMSVDTCACR", "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": "MGVMAMLMLPLLLLGISGLLFIYQEVSRLWSKSAVQNKVVVITDAISGLGKECARVFHTGGARLVLCGKNWERLENLYDALISVADPSKQTFTPKLVLLDLSDISCVPDVAKEVLDCYGCVDILINNASVKVKGPAHKISLELDKKIMDANYFGPITLTKALLPNMISRRTGQIVLVNNIQGKFGIPFRTTYAASKHAALGFFDCLRAEVEEYDVVISTVSPTFIRSYHVYPEQGNWEASIWKFFFRKLTYGVHPVEVAEEVMRTVRRKKQEVFMANPIPKAAVYVRTFFPEFFFAVVACGVKEKLNVPEEG", "text": "FUNCTION: NADH-dependent oxidoreductase which catalyzes the oxidation of all-trans-retinol to all-trans-retinal. Plays a role in the regulation of cardiac and skeletal muscle metabolic functions. Maintains Ca(2+) intracellular homeostasis by repressing Ca(2+) release from the sarcoplasmic reticulum (SR) in myotubes, possibly through local alternations in NAD/NADH or retinol/retinal. Also plays a role in Ca(2+) homeostasis by controlling Ca(2+) overload in the cytosol and the SR in myotubes. Involved in glucose uptake into skeletal muscles and muscle performance by activating PI3K and mTORC2-mediated AKT1 phosphorylation signaling pathways, possibly through the action of its downstream catalytic product all-trans-retinoic acid. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane Note=The N-terminus region encompasses a short hydrophobic sequence bound to the sarcoplasmic reticulum membrane, whereas the C-terminus catalytic domain faces the myoplasm. In skeletal muscle, enriched in the longitudinal sarcoplasmic reticulum. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MAKSRNPSLGQVSDFDIRLLRIFKTIVECGSFSAAESTLGLSRSAISLHMGDLEKRLGMRLCQRGRAGFALTDEGREVYRATQTLLAALEGFRAEVNDLHQHLRGELNIGIINNLVTLPQMRITHALSALKGQGPQVRINIGMTTPNEIELGVLDGHLHVGVVPLISPLSGLEYLPLYDEHAQLYCSRGHALFERADGDIAVDEVLAADAVAPSYRLPAEAQARHQELNNSASASDREGMAFLILTGNFIGYLPSHYAADWVAAGMLRPLLPERFHYAIALTIVTRKGRRPNLVLERFLEAVAVS", "text": "FUNCTION: Involved in the degradation of beta-alanine. BauR activates the transcription of the bauABCD operon. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MGAVTTDVEVASSVPAQTIYKGFLLDMDNIIPKVLPQAIKSIEIISGDGGAGTIKKVTLGEVSQFTVVKQRIDEIDAEALKYSYSIIEGDLLLGIIESITSKFTVVPTDGGCIVKNTTIYTPIGDAVIPEENVKEATEQSGMVFKAIEAYLLANPGAY", "text": "SIMILARITY: Belongs to the BetVI family."}
+{"protein": "IPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFLKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGI", "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": "MASHSSTLFTSPSSFILFSSHRLKSSPNYFTYHFPRSVKRPHFDLRCSVSIEKEVPETERPFTFLRVSDGDQTQSSSYSVRARFEKMIRTAQDKVCEAIEAVEEGPKFKEDVWSRPGGGGGISRILQDGNVWEKAGVNVSVIYGVMPPEAYRAAKAATSEQKPGPIPFFAAGTSSVLHPQNPFAPTLHFNYRYFETDAPKDVPGAPRQWWFGGGTDFTPAYIFEEDVKHFHSV", "text": "FUNCTION: Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase family."}
+{"protein": "KEGYIVNYYDGCKYPCVKLGDNDYCLRECRLRYYKSAGGYCYAFACWCTHLYEQAVVWPLPNKTCN", "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 (PubMed:31734253). This toxin acts on human Nav1.2/SCN2A, Nav1.4/SCN4A and Nav1.6/SCN8A voltage-gated sodium channels (PubMed:31734253). Also, it reduces the peak of sodium currents in Nav1.5/SCN5A at all potentials (PubMed:31734253). In vivo, is lethal to mice when intraperitoneally injected at a dose of 5ug (PubMed:31734253). No activity is observed when injected into crickets or woodlice (PubMed:31734253). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
+{"protein": "MSRAAGHRPGLSAGQLAAATASPLLSLLLLLACCADACKGVPISPQRLQPEQELQLWNEIHEACASFLSIDSRPQASVALRELCRIVMEISQKPQEQSEKDNTKRFLFHYSKTQKLGNSNVVSSVVHPLLQLVPQLHERRMKRFKAEYQSPSVGQSKGYFLFRPRNGKRSTSFI", "text": "FUNCTION: [Neuromedin precursor-related peptide 33]: Does not function as a ligand for either NMUR1 or NMUR2. Indirectly induces prolactin release although its potency is much lower than that of neuromedin precursor-related peptide 36. FUNCTION: Stimulates muscle contractions of specific regions of the gastrointestinal tract. FUNCTION: [Neuromedin precursor-related peptide 36]: Does not function as a ligand for either NMUR1 or NMUR2. Indirectly induces prolactin release from lactotroph cells in the pituitary gland, probably via the hypothalamic dopaminergic system. FUNCTION: [Neuromedin-U-23]: Ligand for receptors NMUR1 and NMUR2 (By similarity). Stimulates muscle contractions of specific regions of the gastrointestinal tract. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NmU family."}
+{"protein": "MEHVVTCWRLKLLSWPVFLIWICLSLASVSLISWDQLPAFLIPSTGDSSLQTAKSRDSMKAPGRLLLLTLCILTFSAVCVFLCCWACLPLCLATCLDRHLPAAPRSTVPGPLHFSGYSSVPDGKPLIRELCHSCAVVSNSGQMLGSGLGAQIDGAECVLRMNQAPTVGFEEDVGQRTTLRVISHTSVPLLLRNYSHYFQHARDTLYVVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQVYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMIPALELCEEIVVYGMVSDSYCSEKSPRSVPYHYFEKGRLDECQMYRLHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWRAK", "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 (PubMed:10207017, PubMed:10601645). Prefers O-glycans to glycoproteins or glycolipids (PubMed:10207017). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
+{"protein": "MSSTSSDRPYDPLAPENEGVASSDVESTDSGEIRSYGPEEVLKNGSQIKDKGPALSKNSTQTSAVESAVAANRRLSKILTNTVDEPDVLEVDYSKCPPMGGGRPFPPTLPEKTQFEVTFDGPNDPLHPFNWPLRKKVMLCIILCLNCISITMGSSIFATGIRQICEIYHVIPVVAILGITLYVLGFAASPVIYAPLSEIYGRRGVLVISSFGFALFNFAVATAKDLQTIMICRFFAGFIGAAPLAVVPAAFADMFDTNIRGKAICLFSLGVFVGPILAPVIGSYITQHTTWRWLEYVIACFASAIFVAILFFFEESHHPSILVGKAKELRKLTGNWGIHAAHEDVELSVKEIAEKTITRPIIMLFTEPLLLIVTIYNSFVYGILYLLLEAYPIVFEQGYGFHTNGELPYISLIIGMAICGAFIWWMDEDYLRRYRKKGGLVPEARLLPMVVAGIVFPIGILWFCWTGNYPHKIHWIVPTIAGAFTGFGLIGIFLPCLNYIIESYLLIAASAVAANTFMRSGFGAAFPLFAGYMFNGMGVNYAGLLLGLLAVAMIPVPLLFLKYGPGIRKRSKYAYSL", "text": "FUNCTION: Multidrug resistance transporter involved in resistance to azole antifungal drugs such as the imidazoles miconazole, ketoconazole, and tioconazole; as well as the triazoles itraconazole and fluconazole (PubMed:26512119). Also plays a role in the resistance to other antifungal drug families such as the polyene amphotericin B, the pyrimide analog flucytosine, the fungicide mancozeb, and the polyamine spermine (PubMed:26512119). Decreases the intracellular accumulation of clotrimazole by mediating its extrusion from cells (PubMed:26512119). Plays a role in biofilm formation (PubMed:27780306). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily."}
+{"protein": "MQIFVKTLTGKTITLEVEGSDNIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIEPSLVILARKYKCDKMICRKCYARLHPRAVNCRKKKCGHSNNLRPKKKLLK", "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": "MAPSPRTGSRQDATALPSMSSTFWAFMILASLLIAYCSQLAAGTCEIVTLDRDSSQPRRTIARQTARCACRKGQIAGTTRARPACVDARIIKTKQWCDMLPCLEGEGCDLLINRSGWTCTQPGGRIKTTTVS", "text": "FUNCTION: Acts as a chemokine-like protein by regulating cell proliferation and migration through activation of G protein-coupled receptors (GPCRs), such as S1PR2 and FPR2 (By similarity). Stimulates chemotactic migration of macrophages mediated by the MAPK3/ERK1 and AKT1 pathway (By similarity). Blocks TNFSF11/RANKL-induced osteoclast formation from macrophages by inhibiting up-regulation of osteoclast fusogenic and differentiation genes (By similarity). Stimulation of macrophage migration and inhibition of osteoclast formation is mediated via GPCR FPR2 (By similarity). Acts as an adipokine by negatively regulating vascular smooth muscle cell (VSMC) proliferation and migration in response to platelet-derived growth factor stimulation via GPCR S1PR2 and G protein GNA12/GNA13-transmitted RHOA signaling (By similarity). Inhibits injury-induced cell proliferation and neointima formation in the femoral arteries (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TAFA family."}
+{"protein": "MEEREGGFRKETVERLLRLHFRDGRTRVNGDALLLMAELLKVFVREAAARAARQAQAEDLEKVDIEHVEKVLPQLLLDFV", "text": "FUNCTION: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks (By similarity). In complex with CENPS, CENPT and CENPW (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression (PubMed:19620631, PubMed:22304917). As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPS, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Chromosome, centromere, kinetochore Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPX being less stably bound at the kinetochore than CENPS. SIMILARITY: Belongs to the CENP-X/MHF2 family."}
+{"protein": "METSVSEIQIETKDEKRPEAASPQKERQERKTATLCFKRRKKVNKKKAKAGSKTAEETEKHAPEAGGSGQRQPAGAWASIKRLVTHRKPSESAEKQKPSEAEMQPEDGALPKKKTKSKLKIPCIRFSRGAKRSRPSKLTEDSGYVRVQGEADDLEIKAQIQPDEQATQAKSTQGLQEDVIVRDGKEIQESHISNNVISGEHVIGIELELEKESSALRMRTPGSEKEAKVILVKQGVQVQEASVLENSAADSPQPVTSTAPLSPATTHQLGLEEPSDSIRESAPSGKDDGRRKTAAEEKKSGETALGQAEEASSVSQADKSVLSQAEEATVGHTEEATVIQAQSQAKEGKLSQAEEATVAQAKETVLSQAEEVKLSQIEEPAISQAKKATVGQAKEAYVSQAEEAIVGHTEKATMGQAEEATVGHIEKTTVGQAEEATVGQAEEATVGQAEEATVGQAEEATVGQAEEATVGQAGEATVSHIEKTTVGQAEEAIVGQAEEATVGQAEEATVGQAEEATVGQAEEATVDQAEEATVGQAEEATVGQAGEAAVGQAEEAIVAQAEEATVGQAGEATVGQAEKATVGQAEEPIVGQAEETVLRHASDLKVNGVDAEKPRSEESKRMEPIAIIITDTEISEFDVKKSKNVPKQFLISMENEQVGVFANDSDFEGRTSEQYETLLIETASSLVKNAIELSVEQLVNEMVSEDNQINTLFQ", "text": "FUNCTION: Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. Plays a role in long term synaptic potentiation by regulating protein trafficking from the dendritic recycling endosomes to the plasma membrane and controlling both structural and functional plasticity at excitatory synapses. SUBCELLULAR LOCATION: Postsynaptic recycling endosome membrane; Lipid-anchor Note=Associates with lipid rafts."}
+{"protein": "MKFILPLFTSLPVALAWLPGIDKDIYSAAGTNIFNVTSASSKRWLPASKKIRGVNLGSHFVIEPWMASMAWSNMGCSGQRSEFDCVMALGQETADQAFADHWGSWITQDDINQMVQYGLNTIRIPVGYWLKEDLVYADSEHFPKGGIGYLEDVCGWASDAGMYIIIDLHGAPGAQQPKQPFTGQYAPNPGFYQDYQYDRALEFLEWMTTSIHQNNKFRNVGMLEIVNEPVQNADQASSMINSYYPSAFTRIRNTESSLGITSNNYLHIQMMNEKWGSGDPTQSLTDNYFAAYDDHRYVKWDSSVAVDKESYISASCVDDRGGNWPTIVGEWSLSVPDNVEHTADWEPSSNTDFYARWFAAQAIAYEKQEGWVFWSWKAQLGDYRWSYKDAVDAGVIPKDLDSIYDYSPC", "text": "FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
+{"protein": "MVYPIYMAKNKSYLHQINRLKIPPHSLEAEQSVLGGLMLDNEQWDSVSEHVVADDFFSKPHRLIFQEMQQLLDLGHPIDLITLSESLEQKGKLESVGRFSYLAELSKNTPSTANIIAYADIIRERAIVREMILVANKIANAGYDTQGRKSEELLDYAESSVFKIAEKRFKKDSGPKNIEQILDETVTSIEKLFLSPNDGVTGINTGYQDLNKKTSGLQPSELIIIAARPSMGKTTFAMNLCENAAMLYDKPVLIFSLEMPGEQIMMRMLASLSRVNQARIRTGQLNDEDWSRMSGTINVLLKKKNIYIDDSSALTPSEVRSRARRIYRENKGLTLIMVDYLQLMRVPSLSDNRTLEIAEISRTLKALAKELQVPVIALSQLNRSLEQRSDKRPVNSDLRESGSLEQDADLIMFIYRDEIYHENSDFKGVAEIIIGKQRNGPIGTICLTFNGHWSRFDNYCGPKYD", "text": "FUNCTION: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. SIMILARITY: Belongs to the helicase family. DnaB subfamily."}
+{"protein": "MIKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDAVTLRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFVGQDRTLKRLLLVSAGDVTDQQPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASGICADITHPFRITGKAEDNLRIVLSRLYESNTSWMPIVDEDGRYNGEISQDYIADYLSSGRTRRALNIHENS", "text": "FUNCTION: Part of the OsmU ABC transporter complex, which is involved in the uptake of osmoprotectants such as choline-O-sulfate and glycine betaine. 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": "MTTPQIDERAMEAGAAALQETIVDPGPLDVTALAVAAALAAGLHSAADDPAAALDKCIVLDELTEFAEKLVVHDRPGGIGTTVEYVEVYEDASGVRLGTATGNAVVLKMEPHMWQFHQSVSELADGSFEAVGVIDCTAMLRRMTQVLRVTGRSGRYAGKSGFMTLAISDPNQRPPHYSVQVVLC", "text": "FUNCTION: Involved in the biosynthesis of the spirotetramate antibiotics pyrroindomycins. Catalyzes the intramolecular cyclization forming the spiro-conjugate moiety in pyrroindomycins, via an exo- selective [4+2] cycloaddition reaction."}
+{"protein": "MNHTVQTFFSPVNSGQPPNYEMLKEEHEVAVLGAPHNPAPPTSTVIHIRSETSVPDHVVWSLFNTLFMNPCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTILLIVIPVLIFQAYG", "text": "FUNCTION: IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:26354436, PubMed:33270927, PubMed:33239446). Can inhibit: influenza virus hemagglutinin protein- mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS- CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein- mediated viral entry (PubMed:33270927). Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed:26354436). Exerts opposing activities on SARS-CoV-2, including amphipathicity-dependent restriction of virus at endosomes and amphipathicity-independent enhancement of infection at the plasma membrane (PubMed:33270927). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Late endosome membrane; Single-pass type II membrane protein Early endosome membrane; Single-pass type II membrane protein. Lysosome membrane; Single-pass type II membrane protein Cytoplasm, perinuclear region Note=Co-localizes with BRI3 isoform 1 at the perinuclear region. SIMILARITY: Belongs to the CD225/Dispanin family."}
+{"protein": "MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVDELPSNILLVRLLDGIKQRPWKPGPGGGGSTTCTNVLRAQGSTVVNCGSKDLQSPQCGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVNGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDTAECPSATAAQSSSASKHSDTKKNTRKRHSFTSLTMANKSSQASQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPTDVPYQAALGTMNPPLPPPPLLATTVLASTPSGATAAAVAAAAAAVAAGVGPRPAVGSTEQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWYKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQASRGVTMVSPSTAGGPAQKPQGNGVAGNPSVVPTAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAACIGPASVGLPHHSLASQPLPPMVGPAAHIAAVNINRTSVPLACAAGASSLASPNMTTAALETEPSGRTVTILPGLPTSPESAASACGNSSAVKPDKDSKKEKKGLLKLLSGASTKRKPRVSPPASPTLDVELGSGEVPLQGAVGPELPLGGVHGRVGSCPTDGDGPVAAGTAALAQDAFHRKTSSLDSAVPIAPPPRQACSSLGPVMNEARPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI", "text": "FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin- dependent and clathrin-independent endocytosis (By similarity). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway (PubMed:12514131). Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Cell projection, lamellipodium Golgi apparatus, trans-Golgi network Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. SIMILARITY: Belongs to the SH3RF family."}
+{"protein": "MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLIQHMNASNMSAAATAATLALPAGVTPVQQILTNSGQLLQVVRVANGAQYIFQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPTPAQAQITATGHQQPQAQPAQTQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDDVSDEEGQELFDTENVVVCQYDKIHRSKNKWKFHLKDGIMNLNGRDYIFSKAIGDAEW", "text": "FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIA subunit 1 family."}
+{"protein": "MESQGQWNPLLSFSRFINHHSNHLATRLEETKRLAGTLIQSHTRTKPAFAATLTPNHVAKSLAGTSVYTVSNSDNEFVLMSDAEGAKSIGLLCFRQEDAEAFLAQVRSRKKEFRGGAKVVPITLDQVYMLKVEGIAFRFLPDPVQIKNALELRAANRGSFDGVPVFQSDLLVVKKKNKRYCPVYFSKEDLEYELSKVSRSSKGVGVSQHIMVGSFEDVLKKMELSEKSSGWEDLVFIPPGKKHSQHMQEVIA", "text": "FUNCTION: Involved in protein precursor import into chloroplasts. Imported into the intermembrane space via the Toc translocon. May be involved in the import pathway used by proteins without a cleavable N- terminal pre-sequence. SUBCELLULAR LOCATION: Plastid, chloroplast intermembrane space; Peripheral membrane protein. SIMILARITY: Belongs to the Tic22 family."}
+{"protein": "MTSKKLVNSVAGCADDALAGLVACNPSLQLLQGHRVALRSDLDSLKGRVALLSGGGSGHEPAHAGFIGKGMLTGVIAGAVFTSPAVGSILAAIRAVAQAGTVGTLLIVKNYTGDRLNFGLAREQARAEGIPVEMVVVGDDSAFTVLKKAGRRGLCGTVLIHKVAGALAEAGVGLEEITDRVSVVAKAMGTLGVSLSSCSVPGSKPTFELSADEVELGLGIHGEAGVRRIKMATANEIVALMLDHMTSSSNASHVPVPPGSSVVLMVNNLGGLSFLELGIIADAAVCSLEGHGVKIARALVGTFMSALEMPGVSLTLLLVDEPLLKLIDAETTASAWPNVAKVWVTGRKRSRAAPTEPLAAPDSTTAAGEASKQMVLVLEWVCTTLLGLEEHLNALDRAAGDGDCGTTHSRAARAIXGWLKEGPPPASPAQLLSKLSFLLLEKMGGSSGALYGLFLTAAAQPLKAKTDLPAWSAAMDAGLEAMQKYGKAAPGDRTMLDSLWAAGQELQAWKSPGANMLQILTKAVKSAEAAAEATKNMEAGAGRASYISSARLDQPDPGAVAAAAILRAILEVLQSQGA", "text": "FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1- mediated cellular antiviral response."}
+{"protein": "MLKHFQRLGGALFAPVLLFPFAGLVVALTIILKNPDFVGELANTNGTFYKMITVIEEGGWTVFRQLPLIFAIGLPIGLAKKAHPRACLAVLATYLTYNYFISAILTFWGPSFGVDFTQNVGGVSGLTTIAGIKTLDTSIVGAIVISGITIYIHNKFFDTKLPDFLGTFQGTTLVSAIAFVVMIPCAYITCLVWPKIQMGISSLQALMVTSGTFGVWLYTFLERILIPTGLHHFIYGPFIFGPAVVDTGIQVAWAENLLNFANSTQPLKELFPQGGFALHGNSKIFGCIGIALAMYKTARPEKKKIVSGLLIPAALTAALVGITEPLEFTFLFIAPFLFVVHAVLAATMAAVMYAFGVVKYGSGIIEIAALNWLPLMKNHSGVMFTQLAIGVVFIGIHYLVFKFLIEKYNVKTSGREDEEEETKLYTKADWKAKNGEGKETNSSDLYSGKAKAFLEAFGGKDNIEQVNNCATRLRISVKDEKKVGPDIQFKAAGAHGVVRNGKAFQVIVGLSVPQVRESFENLMEQN", "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-glucoside transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MAAPGDPQDELLPLAGPGSQWLRDRGEGEDEAVTPKGATPAPQAGEPSPGLGARAREAASREAGSGPARQSPVAMETASTGVAGVSSAMDHTFSTTSKDGEGSCYTSLISDICYPPQEDSTYFTGILQRENGHVTISESPEELGTPGSSLPDVPGIESRGLFSSDSGIEMTPAESTEVNKILADPLDQMKAEAYKYIDITRPEEVKHQEQNHPELEDKDLDFKNKDTDISIKPEGVREPDEPAPVEGKIIKDHLLEESTFAPYIDDLSEEQRRAPQITTPVKITLTEIEPSVETTTQEKTPEKQDICLKPSPDTVPTVTVSEPEDDSPGSITPPSSGTEPSAAESQGKGSISEDELITAIKEAKGLSYETAESPRPVGQLADRPEVKARSGPPTIPSPLDHEASSAESGDSEIELVSEDPMAAEDALPSGYVSFGHVGGPPPSPASPSIQYSILREEREAELDSELIIESCDASSASEESPKREQDSPPMKPGALDAIREETGVRAEERAPSRRGLAEPASFLDYPSTEPQPGPELPPGDGALEPETPTLPRKPEEDASSHQSPAATKGPGPLGPGAPPPLLFLNKQKAIDLLYWRDIKQTGIVFGSFLLLLFSLTQFSVVSVVAYLALAALSATISFRIYKSVLQAVQKTDEGHPFKAYLELEITLSQEQIQKYTDCLQFYVNSTLKELRRLFLVQDLVDSLKFAVLMWLLTYVGALFNGLTLLLMAVVSMFTLPVVYVKHQAQIDQYLGLVRTHINAVVAKIQAKIPGAKRHAE", "text": "FUNCTION: Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein."}
+{"protein": "MMSDFGEELTKLAVAEDNPETSVLSKTGMHFPWLHKHVEAVVTGGKKRKDFAQTTSACLSFIQEALLKHQWQQAAEYMHSYLQTLEDSDTDKRQAAPEIIWKLGSEILFYHPKSNVETFNSFADRMKNIGVLNYLKISLQHALYLLHHGMLDDANRNLSKAETWRYGEKSSSQEVLINLVQAYKGLLQYYTWTRKKMELSKLDEDDYAYAAKTRTMLSQSCKTSTNICALVKTPGVWDPFVKSYVEMLEFYGDQDGAREMLTNYAYDEKFPSNPNAHVYLYEFLKREKAPRAKLISVLKILHEIVPSHTLMLEFHTLLRKSDTEEHQKLGLSVLFEVLDFAGCNKNITAWKYLAKYLKQILVGSHHEWVEEEWKSRRNWWPAFHFSFFWAKSDWKADTDLACEKAFVAGVLLGKGCKYFRYILKQDHETLKKKIKRMKKSVKKYTIVNPGVHT", "text": "FUNCTION: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (pre-initiation 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": "MVSLLRCQSFKPSSSLICSLALSAAFALSSSAFAEETKPAENKPATPVVSPPKATAQPANKNQVRFTKTGTFDGDSVVKLARKLASKPYVVLKDPLPAGLAKLSYDEYRDIRFNPVSSIWRDQGLPFQMQMFHRGFYFQDLIEIAIVEANQATHLAYEPKYFTAGEVITQALPNDDIGYSGFRIHNQLNTNGVYDELMVFQGASYFRALGKGNSYGLSARGLALKTADPEGEEFPIFRAFWVERPSYDSNLIVVHALLDSPSVAGAYRFSVRPGDNTQIDVEATLFPRVELSKVGLAPSTSMFLHSLNGRHDTDDFRPEVHDSDGLLMFNGRGEHLWRPLANPRQLQVSAFSDNSPQGFGLIQRERNYASYQDLEAHYERRPSLWIEPVGNWGQGAVVLTEIPTESEIHDNIVSFWKPRQPIPAGSEYHFAYRMNWGDEPVAKTNSVVVSRTASGRADIAKATPRRLFVVDYHLNGAMPDELPLAKVESSGGVIANVVIARNAANNGYRLAFELEPEDKDLIELRAELKFSTPRQVETWLYRWTL", "text": "FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the OpgD/OpgG family."}
+{"protein": "MTVAIGRSDSERGWFDVLDDWLKRDRFVFLGWSGLLLLPCAYLAVGAWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSMGHSILFVWGPEAQGDFTRWCQIGGLWTFTALHGALGLIGFTLRQFEIARLIGLRPYNAIAFSGPIAVFVSVFLLYPLGQAGWFFAPSFGVAAIFRFLLFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGSNTFPAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLGVNLRAYDFVSQEIRAAEDPEFETFYTKNLLLNEGIRAWMAVQDQPHENFVFSEEVLPRGNAL", "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, cyanelle thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family."}
+{"protein": "MSYKELSTILKILSDSSRLEILDLLSCGELCACDLLEHFQFSQPTLSHHMKSLVDNELVTTRKDGNKHWYQLNHAILDDIIQNLNIINTSNQRCVCKNVKSGDC", "text": "FUNCTION: Transcriptional repressor for the ars operon. ArsR is a trans-acting regulatory protein which controls its own expression. The repressive effect of ArsR is alleviated by oxyions of +III oxidation state of arsenic, antimony, and bismuth, as well as arsenate (As(V))."}
+{"protein": "MFTLNKFLLLLFFLGTINLSFCEEENAEEERIDEPDETDVEVEKRFLPIIAGIAAKVFPKIFCAISKKC", "text": "FUNCTION: Antibacterial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli. Has activity against C.albicans. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
+{"protein": "MQLRHIGDSVNHRVIQEHLAQEVGDVLAPFVALVFVRGQVLLRFFWNNHLL", "text": "SUBCELLULAR LOCATION: Peroxisome."}
+{"protein": "MVYKVFLSLCIGLALSASAALHAQKAVSGHAPIQVETPARSSGQKHVLQLVTPKLETVRIGIIGLGMRGPGAVERFSKIPGTQIVALCDVLPERVKKTQEILVKAGLPEAAAYSGSEDAWKKLCEREDIDLVYIVTDWKTHAEMGVYAMEHGKHAAIEVPAAMTLEEIWKLIDTSERTRKHCIQLENCVYDFFELTTLNMAHQGVFGEILHAEGAYIHNLEDFWPYYWNNWRLDYNRKHRGDVYATHGMGPACQLLDIHRGDRMKTIVAMDTKAVNGPAYIKNKTGEVVADFQNGDQTTSLIRTEKGKTLLIQHNVMTPRPYSRKYQAVGTDGFADKYPLEMYCLRPAQVDSDIAPDHEKLNAHGPVSEEVKKALMEKYKHPIHRELEETAKKVGGHGGMDYIMDYRLIYCLRNGLPLDMDVYDLAEWCCLAELSRISIENGSAPVAIPDFTRGNWDKVKGYRHAMAE", "text": "FUNCTION: Glycosidase. SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109 subfamily."}
+{"protein": "ATQTSPSPKGAAAXXXRVV", "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 inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
+{"protein": "ACYCRIPACLAGERRYGTCFYMGRVWAFCC", "text": "FUNCTION: Has bacteriostatic activity against L.monocytogenes, E.coli and S.aureus, microbicidial activity against L.monocytogenes and S.aureus and antifungal activity against C.neoformans. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MAATGTEKQGAKAYYVSTPIYYVNDAPHLGHAYTTVAGDVLTRWHRQRGEKVWYLTGTDEHGQKIMRTAEANGVTPQAWADKLVTESWKPLWEHLDIANDDFIRTTQKRHTDRVQEFVQDLYDKGEIYKGGYEGPYCVGCEEYKLPGELLDGEGEYAGQKLCPIHKKPVEILSEENYFFKLSEYSEKLLAHYEANPGFVQPESARNEVVNFVRQGLQDLSISRSTFDWGVPVPWDDKHVIYVWVDALLNYATAVGYNENPEKFESTFPADVHLVGKDILRFHAIIWPAMLMAQGLPLPGKIAANGWLMVGGEKMSKSNLTGIKPQDLTTHFGVDAYRWYFLRAIAFGQDGSFSWEDFSARYTSELANDYGNLASRVAAMVGKYFGGELPAATADGDAEQAIHDGLTKAVAEADRKIGEELDFQGGILAVFDFVKQVNGYITEQEPWKVAKDDSPEGKARLATILYTAAEALRAVAVLLNPIMPDTSQKLWDSLGAEPSLGALADQHVQDAADWGRLPAGATVTKGAVLFPRLEEKPAA", "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": "MDNEAVSALWSCASATCLSLDVKRHCSDANVDSQARTQSQATPMTNETDPRKLRHIAHTPRGSCFMTLLLLLLLALNFRHAHSCGPGRGLGRRRDRNLYPLVLKQTVPNLSEYQSGASGPLEGVIDRKSPKFKDLVPLYNSDILFRDEEGTGADRMMTKRCKEKLVMLATSVMNEWPGVKLLVTESWDEDHHHGEQSLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSSSISHVHGCFTPESTAQLESGAKKPLGELAIGDRVLSMDAKGQAVYSEVILFMDRNLEQMETFVQLHTDGGAVLTVTPAHLITVWQPERQTLDFVFADHVEELNYVLVVDDATGGELRPQRVLRVSSVRRRGVVAPLTREGTIVVNSVAASCYAVISSQSLAHWGLAPMRLWSTLQSWLPAKDKLRSSKVQEKSTPKVNSTAQLQNGLHWYANALYKVKDYVLPQSWRHD", "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": "MWGVFLLYVSMKMGGTTGQNIDQPTEMTATEGAIVQINCTYQTSGFNGLFWYQQHAGEAPTFLSYNVLDGLEEKGRFSSFLSRSKGYSYLLLKELQMKDSASYLCA", "text": "FUNCTION: V region of the variable domain of T cell receptor (TR) alpha 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": "MNYEFEREIGFINSQPSLAECLTSFPPVADTFQSSSIKTSSLSHSTLIPPPFEQTIPSLNPGSHPRHGAGGRPKPSPAGSRGSPVPAGALQPPEYPWMKEKKAAKKTALPPASAAAAAAATGPACLSHKESLEIADGSGGGSRRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQCKENQNSEGKCKSLEDSEKVEDDDEEKTLFEQALSVSGALLEREGYTFQQNTLSQQQAPNGHNGDSQSFPVSPLTSNEKNLKHFQHQSPTVPNCLSTMGQNCGAGLNNDSPEALEVPSLQDFNVFSTDSCLQLSDAVSPSLPGSLDSPVDISADSFDFFTDTLTTIDLQHLNY", "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. Proboscipedia subfamily."}
+{"protein": "MAVAVCGAVVPVVARLEGREFEYLMKKRSVTIGRNSSQGCVDVSMGHSSFISRRHLEIFIGGSGDGDDADVGDFYLRCLGKNGVFVDGVFQRRGAPPLQLPRVCTFRFPSTNIKITFTALAIDKKQKLEAPESPVKPVQPQISPLTIHIPDNIAHLISPLPSPTGTISAANSCPSSPRGAGSSGFKFGRVIPPDLIAEAAQSENDKDASGGDSPKDDSKPPYSYAQLIVQAITMAPDKQLTLNGIYTHITKNYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPGKGSFWRIDPASESKLVEQAFRKRRPRGVPCFRTPLGPLSSRSAPASPNHSGVFSAHSSGVQTPESLSREGSPIPLEPDASVIHPKLAVIQEARFAQSAPGSPLSSQPVLITVQRQLPQTIKPVTYTVAAPVTTATSQQAVMQTVHVVHQIPAVSVTNVTGLTPINTYTVGGQTMVAQAAVMAQPKLEHQENGDHKEVKVKVEAIPAIGHPALTTASRIIQTSSSAPLQTVTIVQTPLGQHQLPIKAVTQNGTHVVPITTAIQGQVTTANSSYSLIESPWQWRGNGTRAASPLHMLATHASASASLPTKRQNGDQSEQPDIKRGKTDEREVLAMTGLDAQSEMAMAASNEQENQK", "text": "FUNCTION: Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis and autophagy (By similarity). Recognizes and binds the forkhead DNA sequence motif (5'- GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context (By similarity). Acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen. Acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MARYRCCRSRSRSRCRRRRRKCYRRRRRCSRKRRRRVCCRRYTVMRCRRR", "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": "MTGMKKGKNKKKNVKNDERYKELDSLISNDSEIGNNSRWGGAKRICKLIGNEMRNNIYVYLLSILYLCVSVMNKVFSKRTLNKIGNYSFVTSEVHNMICTIVFQLLYFIYRKTSNPASRNESQKNFGWQFFLISLLDASTVIITMIGLTRTTGNIQSFIMQLIIPVNMYFCFIFLGYRYHLFNYLGAFIILITIAAVETVLSYETQSDNSIIFNLIMIFALIPLSFSNMTREVVFKKHKINIIRLNAMVALFQFFTSLLVLPVYNISFLKEIYMPFSEMGTNINDGLRCLFYGQSTIVENCGVGMVKMCDQCEGAWKTFITYSFFNICDNLLVCYIIDKFSTMTYTIVSCIQGPAITIAYYFKFLAGDVVRQPRLLDFLTLFGYLLGTIIYRIGNIILEKKKMLKALNTDGSEAELTSIETSTA", "text": "FUNCTION: May regulate endogenous transporter. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. Note=Localizes to the parasite digestive vacuole, the site of chloroquine action. SIMILARITY: Belongs to the CRT-like transporter family."}
+{"protein": "MFAGSVIRKLSHSEEVFARYEVFTSMTIQLRGVLDIDALSEAFDALVQAHPVLASHLETSSDGGWNLVADDLLHPGICVVDANNGAQSGCGGIQSETRLDQSVSLLNLRLTPREGGGELVLYIHHSMADGHHGAVLVDELFSRYTDVVTTGDPGPIIPQATPLSMEAVLQQRGVKKHALSGAERFMSVMYAYDLPATGTPAVLAEPGLPQAVPVTRLWLTKQETSDLAAFGREHRLSINAVVAAAILMTEWRLRETPHVPIPYVYPVDLRYVLAPPVAPTESTNLLGAAGYLAEIGQDTDIVDLATDIVATLRADLANGVVQQSGLHFGTAFEGTPPGLPPLVFCTDATAFPTMRTPPDLAIEDIQGRFYCSISVPLDLYSCGVYEGQLIIEHHGHIEEPAKALEAIRSLLCTVPSEYGWIME", "text": "FUNCTION: Catalyzes diesterification of phthiocerol, phthiodiolone, and phenolphthiocerol with mycocerosic acids, the final step in the phthiocerol, phthiodiolone and phenolphthiocerol dimycocerosate esters (PDIM) synthesis. Can directly transfer the mycocerosate bound to the mycocerosic acid synthase (mas) onto the substrate alcohols. SIMILARITY: Belongs to the acyltransferase PapA5 family."}
+{"protein": "MSKNFQEPIFDVAQLAHVELLSPKLEESIVFFTKYLGMEVTARAGNSVYLRAYEDFYHNTLKITESAEAGLGHVGWRASSPQALERRVLELEKSGLGRGWIDGDIGHGKAYQFTTPDGHQMEIFFEVEYYKPQPEQKTKLLNRPSKRPAQGVPVRRLDHINLMTSNPGVDTQFMIDTLGFRLREQIRDKGKILGSWISVSNLVHEIAFMQEPNQEKGKLHHLCYWYGIPQNLYDLADLLKDHEYFIEVPPNKHGISQAFCMYVYEPGGNRIELFGDAGYLITDPTWEPVIWEMEDVPGNGDTWIGTAFPDSWWLRGTPVTTKEVVKP", "text": "SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family."}
+{"protein": "MIARIIGEIGIEGARFIEENIDEQFKALRYLSKGIDSETFVKLVIANSLVSYQLTGKGEQWWWEFAKYFYGRDVKSIYLAYKEFLPNSRFNRRLIPQKLSRIRRVETFLSTLTEERIEEYYGDMSSLWGSIARALGVDKESKTVVFSVKMFGYAARIVLSTFNPYPMEIPIPEDSRIVKLTKKLTNEKPRKFWMKIARESGVPPLHIDSILWPLLGGASIDSAPPELRDKLAELIKIIR", "text": "FUNCTION: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double- stranded DNA substrates. SIMILARITY: Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family."}
+{"protein": "MYRLLIINPGSTSTKIGIYDDEKEIFEKTLRHSAEEIEKYNTIFDQFQFRKNVILDALKEANIEVSSLNAVVGRGGLLKPIVSGTYAVNQKMLEDLKVGVQGQHASNLGGIIANEIAKEINVPAYIVDPVVVDELDEVSRISGMADIPRKSIFHALNQKAVARRYAKEVGKKYEDLNLIVVHMGGGTSVGTHKDGRVIEVNNTLDGEGPFSPERSGGVPIGDLVRLCFSNKYTYEEVMKKINGKGGVVSYLNTIDFKAVVDKALEGDKKCALIYEAFTFQVAKEIGKCSTVLKGNVDAIILTGGIAYNEHVCNAIEDRVKFIAPVVRYGGEDELLALAEGGLRVLRGEEKAKEYK", "text": "FUNCTION: Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetokinase family."}
+{"protein": "MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQLDFSLPVPPRPVLPVTEI", "text": "FUNCTION: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. Can also acetylate demethylphosphinothricin but not PTT or glutamate. This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance. SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR subfamily."}
+{"protein": "MKSSVSWLFFSSIPLFSSLSIVAAEVTLDSSNNSYDGSNGTTFTVFSTTDAAAGTTYSLLSDVSFQNAGALGIPLASGCFLEAGGDLTFQGNQHALKFAFINAGSSAGTVASTSAADKNLLFNDFSRLSIISCPSLLLSPTGQCALKSVGNLSLTGNSQIIFTQNFSSDNGGVINTKNFLLSGTSQFASFSRNQAFTGKQGGVVYATGTITIENSPGIVSFSQNLAKGSGGALYSTDNCSITDNFQVIFDGNSAWEAAQAQGGAICCTTTDKTVTLTGNKNLSFTNNTALTYGGAISGLKVSISAGGPTLFQSNISGSSAGQGGGGAINIASAGELALSATSGDITFNNNQVTNGSTSTRNAINIIDTAKVTSIRAATGQSIYFYDPITNPGTAASTDTLNLNLADANSEIEYGGAIVFSGEKLSPTEKAIAANVTSTIRQPAVLARGDLVLRDGVTVTFKDLTQSPGSRILMDGGTTLSAKEANLSLNGLAVNLSSLDGTNKAALKTEAADKNISLSGTIALIDTEGSFYENHNLKSASTYPLLELTTAGANGTITLGALSTLTLQEPETHYGYQGNWQLSWANATSSKIGSINWTRTGYIPSPERKSNLPLNSLWGNFIDIRSINQLIETKSSGEPFERELWLSGIANFFYRDSMPTRHGFRHISGGYALGITATTPAEDQLTFAFCQLFARDRNHITGKNHGDTYGASLYFHHTEGLFDIANFLWGKATRAPWVLSEISQIIPLSFDAKFSYLHTDNHMKTYYTDNSIIKGSWRNDAFCADLGASLPFVISVPYLLKEVEPFVKVQYIYAHQQDFYERYAEGRAFNKSELINVEIPIGVTFERDSKSEKGTYDLTLMYILDAYRRNPKCQTSLIASDANWMAYGTNLARQGFSVRAANHFQVNPHMEIFGQFAFEVRSSSRNYNTNLGSKFCF", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. Cell outer membrane; Peripheral membrane protein; Extracellular side. SIMILARITY: Belongs to the PMP outer membrane protein family."}
+{"protein": "MMKIIIFLIVSSLVLIGVKTDNGYLLDKYTGCKVWCVINNESCNSECKIRRGNYGYCYFWKLACYCEGAPKSELWHYETNKCNGRM", "text": "FUNCTION: Inhibits sodium channels (Nav). Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family."}
+{"protein": "MSTIHSCLDLIRSQIQQSANGRNVLLVAVSKFHPVETLMEAYNAGQRHFGENYMQEFLKKVELMPDDVQWHFIGSLQSSKCKKIASVKNLYSIETIDTEKKARLVNSAREALQLPLNVYIQVNTSGEENKGGVTPSKVLELCKQVQDMKYLRLKGLMTIGSISNSQLSDHNPDFQVLSDLRESLQNELGIPLQLSMGMSSDYLLAIKYGSDSVRVGSSIFGSRPTEKPSDVHISASK", "text": "FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'- phosphate (PLP), the active form of vitamin B6. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family."}
+{"protein": "MASLSFVSSSHLTLRTPSIALRSTGSSPRTSVSFSVKAQSVALSQDDLKKLAAEKAVEAIKPGMVLGLGTGSTAAFAVDQIGKLLSSGELYDIVGIPTSKRTEEQARSLGIPLVGLDTHPRIDLAIDGADEVDPNLDLVKGRGGALLREKMVEAVADKFIVVADDTKLVTGLGGSGLAMPVEVVQFCWNFNLIRLQDLFKEFGCESKLRVDGDGKPYVTDNSNYIIDLYFKTPLKDGFAAAKEIGKFQGVVEHGLFLGMATSVIIAGKNGVEVMTK", "text": "FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ribose 5-phosphate isomerase family."}
+{"protein": "LQPGLEYQYRYSARV", "text": "FUNCTION: Forms stable clots in the presence of calcium. SUBCELLULAR LOCATION: Secreted, extracellular space."}
+{"protein": "MNTRENNLKALHAPRKINLREEAGLLGVDIVTDIGEAQPRNEPVFLGYQRRWFEDESQICIAEKSRRTGLTWAEAGRNVMTAAKPKRRGGRNVFYVGSRQEMALEYIAACALFARAFNQLAKADVWEQTFWDSDKKEEILTYMIRFPNSGFKIQALSSRPSNLRGLQGDVVIDEAAFHEALDELLKAAFALNMWGASVRIISTHNGVDNLFNQYIQDAREGRKDYSVHRITLDDAIADGLYRRICYVTNQPWSPEAEKAWRDGLYRNAPNKESADEEYGCIPKKSGGAYLSRVLIEAAMTPARDIPVLRFEAPDDFESLTPQMRHGIVQDWCEQELLPLLDALSPLNKHVLGEDFARRGDLTVFVPLAITPDLRKRECFRVELRNVTYDQQRQILLFILSRLPRFTGAAFDATGNGGYLAEAARLIYGPEMIDCISLTPAWYQEWMPKLKGEFEAQNITIARHQTTLDDLLHIKVDKGIPQIDKGRTKDEGGKGRRHGDFAVALCMAVRASYMNGFVIDEDSIQALPPRHRGDDVDNDDFDDYHQFERGGW", "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 full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by neck proteins. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the T4likevirus large terminase family."}
+{"protein": "MQNKRDSYNREDLLASSQGELFGEGYPQLPAPNMLMMDRITKMSETEGEFGKGLILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTAKKVTYEINMKRVVNRKLVMGLADGRVLVDGKEIYVAKDLKVGLFQDTSAF", "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. 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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioester dehydratase family. FabA subfamily. SIMILARITY: Belongs to the thioester dehydratase family. FabA subfamily."}
+{"protein": "MSSGGLLLLLGLLRVCAELTPVSSKDPYCNLPPDPGPCHDNKFAFYHHPASNKCKEFVYGGCGGNDNRFKTRNKCQCTCSEYP", "text": "FUNCTION: Beta-bungarotoxins are presynaptic neurotoxins of the venom. The B chain is homologous to venom basic protease inhibitors but has no protease inhibitor activity and blocks voltage-gated potassium channels (Kv) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family."}
+{"protein": "MAPISRETDFLVIGGGSGGIATARAAAGKYGIKSMVVEGKRLGGTCVNVGCVPKKVTFYAALVAETIHQAKDYGFSVEQTAPFDWPTFKQKRDAYVARLNGIYERNLANDKVEYVHGWAKLLSPNSVEVTLDDGTKSVVNAKKILIAVGGNPTIPPHIPGSEYGTNSDGFFDIDTLPKKVALVGAGYIAVEFAGMLNALGVETHLFIRHDTFLRSFDPMIQQVSVKEYERIGVKVHKKSQLTSVQKDAAGKLAINFKEGEGEQSISDVDHLIWAVGRTPAVEGLGLDKAGVKTNEKGYIEVDEYQNTSTENIYAVGDVCGQVELTPVAIAAGRKLAARLFGPEEFRTLKLNYDNVPSVVFAHPEIGSIGLTEPEAVAKYGAENLKIYKSSFTAMYYAMMKPEDKAPTAYKLICAGPEEKVVGLHIIGLGSGEILQGFGVAVNMGATKADFDNCVAIHPTSAEELVTLK", "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": "MHRASANSLLNSVSGSMMWRNQSSGRRPSKRLSDNEATLSTINSILGAEDMLSKNLLSYLPPNNEEIDMIYPSEQIMTFIEMLHGHKNFFKGQTIHNALRDSAVLKKQIAYGVAQALLNSVSIQQIHDEWKRHVRSFPFHNKKLSFQDYFSVWAHAIKQVILGDISNIINFILQSIDNSHYNRYVDWICTVGIVPFMRTTHTAPNLYNLLQQVSSKLIHDIVRHKQNIVTPVLLGLSSVIIPDFHNIKIFRDRNSEQISCFKNKKAIAFFTYSTPYVIRNRLMLTTPLAHLSPELKKHNSLRRHQKMCQLLNTFPIKVLTTAKTDVTNKKIMDMIEKEEKSSDAKKSLIKFLLNLSDSKSKIGIRDSVEGFIQEITPSIIDQNKLMLNRGQFRKRSAIDTGERDVRDLFKKQIIKCMEEQIQTQMDEIETLKTTNQMFERKIKDLHSLLETNNDCDRYNPNLDHDLENLSLSRALNIVQRLPFTSVSIDDTRSVANSFFSQYIPDTQYADKRIDQLWEMEYMRTFRLRKNVNNQGQEESITYSNYSIELLIVPFLRRFLNIYNLESIPEEFLFLSLGEILLAIYESSKIKHYLRLVYVRELNQISEVFNLTQTHPENSEPIFDSNIFSPNPENEILEKIKRIRNLRRIQHLTRPNYPKGDQD", "text": "FUNCTION: Forms a portal in the viral capsid through which viral DNA is translocated during DNA packaging. Assembles as a dodecamer at a single fivefold axe of the T=16 icosahedric capsid. Binds to the molecular motor that translocates the viral DNA, termed terminase. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae portal protein family."}
+{"protein": "MGGVRAVAALAFAGVVGLTFLVLGCALPRYGTWTPMFVITFYVLSPVPLLIARRFQEDMTGTNACIELALFITTGIVISAFALPIVLAHAGTIANSACFLVNTGSVIMFGTIIAYFYLHRDDDSGSWSQSLF", "text": "FUNCTION: Involved in endosomal protein transport. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OB-RGRP/VPS55 family."}
+{"protein": "MSQEKNEMFESEWSKEREREKQLASGLDTAEKALKAESEELQKSKSELICLYNEVHNLPGASESRDHFLIACDLLRRENSELETKVLKLSQEFAQLNHFTLRGKTAPSNLITSENICKDPESNEPVLEIEIQSPKEEREELCPKLGERKQKEIPEESVKEGSFPREGQKEEGSQQNQDMKDEEKEQRLTMKPEEVVRLREELSRINQSLLQSQSSGDSSDDSGAQYPSSGDKLKYNQQGEVQQLHQNLHRLQILCNSAENELRYERGKNLDLKQHNSLLQEENIKIKIELKHAQQKLLESTKMCSSLTAECKQSQQKIKELELEVLKQTQSIKSQNNLQEKLAQEKSKVADAEEKILDLQRKLEHAHKVCLTDTCISEKQQLEEKIKEATENEAKVKQQYQEEQQKRKLLYQNTDELHRQVRTLQDKENLLEMTCSQQQSRIQQQEALLKQLENEKRKYDEDVKSNQELSEKLSKLQQEKEALREEYLRLLKLLNVHVRNYNEKHQQHKIKLQKVKYRLTNEVELRDKRINEFEDEIGILQHKIEKKAIQDQITAQNDTLLLEKRKLQEQVIEQEQLIHSNKWTISSIQSRVLYMDKENKQLQEISLRLPATKKQKEIYSTEVCTCNNAELQHEDESVPKATEKWKHSEQMETTISDILESEVVNEILPLSNSSFSGKGLVESFVSLQETDDIKSKEAMASSKSPEKSPENLVCSQNSEAGYINVTSLKETHGIQEQDQKSEL", "text": "SIMILARITY: Belongs to the prefoldin subunit beta family."}
+{"protein": "MSLAEDWIDPNSSEDSDIQEDAELEYTADNPEKEQRGVFSLEKVQLQFPVSIRCLAVENNILVMALTSDKLMIVDLERPEDIIDIELPKKVLALGLTYKIFLDPSGHYIFVTTTAGDNCLFTPSHQGRVLTKLKGHTVEAVQWNLNGGNILELLIASKSGVLLELVLTLDSANLKRIEKSINTLYSFPFMESPMGILKNIQDDSMTIVTNKRILRFEPKTSRGKDQLYFSPAFQGSMKEILSFSEEETAQCFSYSPFPKNLAEPYTLALKTSKRIIYLDIMNPVNPDIQDYEFNESPKLSVPTVEMNMILTSFHLAFLDLDTLYIVNRVNGKESYQQRVNLSPHEEILGLCCDHEKNTYWLYTTDSLHELVVNNETREASLVFLEKGDFEKALECANTAKVRNTVLVGYAEFLMEHEEYERAATLYAETLKSVEEVALKFIELNQKDVLRLYLWKKLRSYKSTMKIQKSLLVNWLLELMLAKLNSLDEKERLELFPENVMQQRQQVQREFSTLLNQYKDEINREAAYNLANNYGKEEQLLQIATVMKDQSYIMHYWVQRENYEKALETLNEGVSQETLIQHATALLTHRPNETVSIWERQTDLDVHALIPSLLSYNQRSHVPVEENAAIRYLRYVTGVLGCVDPSIHNTLFCIYACHSSSNESYLMNYIEQQGNHPLYDMDLGIRLCLQFNCRRSAVKILVLMKLYSQGVELALEADDCELAATIANIPEEDVVLKKTLWQTIAKYMFSKKSGIKETLRFLENSEVLQLPELIRLLPEDIKLDDLSDNVCDELDHCMKRIEQLDFEIGQASEVAHEIQTNAENMRNRYIVLEPNESCWHCNQPLFSEPFVLFPCQHAFHRSCMLEKTYKLASEKNILKECQLCGPSYAVRLINEPFSTDF", "text": "FUNCTION: Required for vacuolar biogenesis. SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the VPS18 family."}
+{"protein": "MIITTWIVYILARKGAGLPFPPKVSSDVEVTETEAVSVVQHWLKKTEEEASQEIKEKMSTNFPPMQGQDVHVTRDVVKHHLSKSGLLANQSQEVLEERTRIQFIRWSHTRIFQVPSEARNEAMRDRIEQVRRSICHLSDEISQELRNRNSYSEC", "text": "FUNCTION: Essential for sperm motility and male fertility (By similarity). Plays an important role in sperm motility by regulating the organization and function of the mitochondria and is also required for correct sperm midpiece assembly (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane Mitochondrion Cell projection, cilium, flagellum Note=Localizes to the midpiece of the sperm flagellum."}
+{"protein": "MTSMILAVFIFLLTLVLVIWQPKNLSIGWSACGGAVLALIAGVVNFHDVLTVTGIVWNATLAFVAIILISLILDNIGFFEWAALHMAKAAKGYGVRMFVYVSLLGAIVAALFANDGAALILTPIVLAMVRALHFNEKLVFPFIIASGFIADTTSLPFVVSNLVNIVSADYFHITFIDYASRMVVPYLFSLLASIIVLYLFFRKSIPKRYDLTEVKKPVEAIKDQNMFRLSWYILGLLLIGYFASEFFSIPVSVVAGSIAIIFLIAAQKSPAVHTKKVVKEAPWAIVFFSIGMYVVVYGVRNAGLTDVLSDVIQAAADQGLFAGTIGMGFIAAILSSIMNNLPTVMIDALAIAGTDTHGMMREALIYANVIGSDLGPKITPIGSLATLLWLHVLSHKGMKISWGTYFKTGIILTIPTLLITLVGLYIWLLIIHSCF", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ArsB family."}
+{"protein": "MAKNAMLCLLILSVVLALAFATNKKDDEEPENHSTGIFGKVGRVVTVALAMSSRLGGANATRGGGAVYGRNLKSNQLPNNNWMAPPPPMAMRSAKVYDSKHSPAEYLKKFAQDFRRKTGTHSQRHHEETTLEQEKRGAPAGPDPIHHQDTTFEQEKRGAPAGPDPIHHQDTTLEQEKRVAGAGPDPIHHQDTKFEQEKRGAPAGPDPIHH", "text": "FUNCTION: Mimics host plant CLE extracellular signal peptides that regulate cell fate. May play a role in the differentiation or division of feeding cells (syncytia) induced in plant roots during infection. SUBCELLULAR LOCATION: Secreted Host cytoplasm Host extracellular space Secreted, extracellular space, apoplast Note=Present in secretory granules within the dorsal esophageal gland secretory cell and in the dorsal gland ampulla (collecting reservoir) at the base of the nematode stylet. Secreted into host root cells via the nematode stylet to transform the recipient cells into enlarged multinucleate feeding cells called giant-cells or syncytia. Secreted to the host apoplasm from its cytoplasm via a plant secretory pathway (By similarity). SIMILARITY: Belongs to the CLV3/ESR signal peptide family."}
+{"protein": "MDQEAMGNIVLLAIVTLISVVQNAFFAHKVEHESKTHNGRSFQRTGTPAFERVYTANQNCVDAYPTFLVVLWSAGLFCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGIFNYFLILFFGSDFENYIKTITTT", "text": "FUNCTION: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MAPEG family."}
+{"protein": "MRCLTIYTWTFRRLPFIPSTNSASFFSTLRFNMSTANNTQAIVIGGGLAGLSATNTILDLGGNVLLLDKNTAFGGNSVKAASGINAAPTQLQFDQHVSDSVNTFYNDSILSAKSKAKPELLRTLTSKSSSAVDWLSERFGLQMDQLSRLAGHSEPRTHRGTHPDYPFKPLAFVLVDQTEKFAASHPDRLQIKKNARVTRLLTNPNHDKVFGVEYMDLSDKSNHTVYGPVVLATGGYAADYSDDSLLKLYHPEALSLSTTNGPYCTGDGHKMVMSIGGSTVDLDLVQIHPTGFVDPKDPTALTKFLAAEALRGSGAVLLTSQGRRFCDELGYRDYVTGEMMKLKSPVYLVLNSAAAEEVANFIKFYSFKGLMKKMKAEELCSTLNCTKDELASTFSEYNRAAKGEIPDEFGRKYFGKTPLELTDTFTVGEVVPVLHYTMGGVQVDTQSRVLSTNGNVIDGLFAAGEIVGGIHGENRLGGSSLLACVVFGRLAGQGASSTMLRRFIASSTSTASS", "text": "FUNCTION: Irreversibly catalyzes the reduction of fumarate to succinate. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Nucleus. SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily."}
+{"protein": "MINNRENMSVSERLISSRQNRQLDEVRGRMIVTACALIMIAASVAITIFLGVKGLQSFLVNGVSPIEFLTSLNWNPTDSDPKYGVLPFIFGSFAVTILSALIAAPLGIAGAIFMTEIAPNWGKKVLQPVIELLVGIPSVVYGFIGLTVLVPFIAQFKSSGTGHSLLAGTIVLSVMILPTITSISADAMASLPKSLREGSYALGATRWQTIRKVLVPAAFPTLMTAVVLGMARAFGEALAVQMVIGNTRVLPESPFDTAGTLTTIITLNMGHTTYGSVENNTLWSMGLVLLVMSFLFILLIRYLSSRRKV", "text": "FUNCTION: Part of the binding-protein-dependent transport system YqgGHIJK. Probably 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. CysTW subfamily."}
+{"protein": "MAGRGSLVSWRAFHGCDSAEELPRVSPRFLRAWHPPPVSARMPTRRWAPGTQCITKCEHTRPKPGELAFRKGDVVTILEACENKSWYRVKHHTSGQEGLLAAGALREREALSADPKLSLMPWFHGKISGQEAVQQLQPPEDGLFLVRESARHPGDYVLCVSFGRDVIHYRVLHRDGHLTIDEAVFFCNLMDMVEHYSKDKGAICTKLVRPKRKHGTKSAEEELARAGWLLNLQHLTLGAQIGEGEFGAVLQGEYLGQKVAVKNIKCDVTAQAFLDETAVMTKMQHENLVRLLGVILHQGLYIVMEHVSKGNLVNFLRTRGRALVNTAQLLQFSLHVAEGMEYLESKKLVHRDLAARNILVSEDLVAKVSDFGLAKAERKGLDSSRLPVKWTAPEALKHGKFTSKSDVWSFGVLLWEVFSYGRAPYPKMSLKEVSEAVEKGYRMEPPEGCPGPVHVLMSSCWEAEPARRPPFRKLAEKLARELRSAGAPASVSGQDADGSTSPRSQEP", "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 by specifically phosphorylating their C- terminal regulatory tyrosine residue which acts as a negative regulatory site. It may play an inhibitory role in the control of T- cell proliferation. 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": "YTATRDNCCILDERFGSYCPTTCG", "text": "FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. 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 antibacterial immune response via both innate and T-cell mediated pathways. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "HLRNHSGWKPFRCDKCDYQCVNKSMLNSHLKSHSNIYQYRCADCTYATKYCHSLKL", "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": "MKIEIIETKIGLVKIIYDDTQTKIISVMFIDSSKIKPVKNSLSGLHKYFKGQNDYFTNLDLELKGTPFQRKVWKQILEIPFGETRTYSDIAMAIGNPKAVRAVANACGANPIAIIVPCHRVVGKNNDGGYEYGLEKKLWLLDFEKKNTQ", "text": "SIMILARITY: Belongs to the MGMT family."}
+{"protein": "MSFNTEVQPGICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDAVDERQRYTFGRQSVLELTHNWGSESDDSQYHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRGMKNVAFISDPDGYWVEIVQASLNGEMGRG", "text": "FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. SIMILARITY: Belongs to the glyoxalase I family."}
+{"protein": "MIVVLVDPRRPTLVPVEAIEFLRGEVQYTEEMPVAVPWSLPAARSAHAGNDAPVLLSSDPNHPAVITRLAAGARLISAPDSQRGERLVDAVAMMDKLRTAGPWESEQTHDSLRRYLLEETYELLDAVRSGSVDQLREELGDLLLQVLFHARIAEDASQSPFTIDDVADTLMRKLGNRAPGVLAGESISLEDQLAQWEAAKASEKARKSVADDVHTGQPALALAQKVIQRAQKAGLPAHLIPDEITSVSVSADVDAENTLRTAVLDFIDRLRCAERAIAVARRGSNVAEQLDVTPLGVITEQEWLAHWPTAVNDSRGGSKKRKGMR", "text": "FUNCTION: Required to maintain the full capacity of the mycobacterium to respond to oxidative stress via the degradation of oxidation-induced damaged nucleotides. Hydrolyzes all canonical (d)NTPs, as well as mutagenic dUTP and 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP). Also involved in the transcriptional activation of RelA in response to oxidative stress. SIMILARITY: Belongs to the nucleoside triphosphate pyrophosphohydrolase family."}
+{"protein": "MRRFAAGCLALALLVLPFVLTGARAAEDESEKEIERYRQMIEDPMANPGFLNVDRGEVLWSEPRGTRNVSLETCDLGEGPGKLEGAYAHLPRYFADTGKVMDLEQRLLWCMETIQGRDTKPLVAKPFSGPGRTSDMEDLVAFIANKSDGVKIKVALATPQEKEMYAIGEALFFRRSSINDFSCSTCHGAAGKRIRLQALPQLDVPGKDAQLTMATWPTYRVSQSALRTMQHRMWDCYRQMRMPAPDYASEAVTALTLYLTKQAEGGELKVPSIKR", "text": "FUNCTION: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the SoxA family."}
+{"protein": "MSFNKVPNIPGAPALSALLKVSVIGGLGVYALTNSLYNVDGGHRAVMFNRLTGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVESTTGSHDLQMVKIGLRVLTRPMGDRLPQIYRTLGENYSERVLPSIIHETLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEAKQVAAQEAERAKFIVEKAEQDRRSAVIRAQGEAKSAQLIGQAIANNQAFITLRKIEAAREIAQTIAQSANKVYLSSNDLLLNLQEMNLEPKK", "text": "FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the prohibitin family."}
+{"protein": "MAAAVDTFLFTSESVNEGHPDKLCDQISDAVLDACLAQDPESKVACETCTKTNLVMVFGEITTKANVDYEKIVRQTCRDIGFVSADVGLDADNCKVLVYIEQQSPDIAQGVHGHLSRRPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCPWLRPDGKTQVTVEYYNENGAMVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIARQAAKSIVAAGLARRCIVQISYAIGVPEPLSVFVDTYGTGKIPDKEILKIVKETFDFRPGMIAINLDLLKGGSRYLKTAAYGHFGRDDADFTWETVKPLKWEKPQA", "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 (By similarity). May be involved in the synthesis of betain in response to abiotic stress such as high salinity (PubMed:15695433). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AdoMet synthase family."}
+{"protein": "MHCVPLFCFLWFCHHLYYSQAVPIRKVQDDTKTLTKTIITRINDISHMYSISAKQRVTGLDFIPGLHPFQSLSDMDQTLAIYQQILSNLSSRNMVQISNDLENLRDLLHLLGSLKSCPFDEAGGLSALGNLEGVMEASLYSTEVVTLTRLQKSLYVMLQQLDLIHGC", "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": "MGRAEAGTPKAISNALKSKGLQRLRWYCSACQKQMRDENGFKCHTQSEGHIRQMNVIAMNPGKRIQDFSNQFLRDFISLLRTAHGEKKIHFNQFYQEYIRDKNHVHMNATRWHTLSEFCKFLGRQGMCRVEENEKGFFISYIDKNPANILRNEANKKRERQEKSDEEQRLRLLDEQIKRAYESAQNNEDNKDGSSREQPVLHEIDLSKKGNPIQLNLSSSSDSHSAQNEFFQTRNTPTFSFSSSSSQTSLKHKPKNVFAELNKSRKKNNKDSLDQGQNVKRPRSAVEDIIAQETMREKRRNIKL", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the KIN17 family."}
+{"protein": "MNTTTVSLERPNVHERRRENVATDINVNALVKNASKAIAPLWPIATFVARHPWMGLEHFSFEQVVHRLKLLRDIDLYPSMAMFRAAQRKGELNPKFLEMRLQRWLDEQPLTMPREEAERFCRAALLHEEIPNELLTSSSLKSLAAKMKDMRLRYDSNHLLTRPLSLLLEEQGKEKWARVLDHQMIKWCKLFLDESQALWAMPYREKGFYYAWRKLVINDPSLNKQQRERLKDLPHDPEEALRQALMLLGIPHGEMKGYLEAHLLSLPGWAGMLLWRSQQSGQAHLLLVDYLAIRLSLEWALIAPHLPFAKQKDDDEAFLLPLLAAWMHWGGWTPEKWLQLPQAEQQARLSFAYRFDKIVRGKLWLEAWEDTQEAQLKKRIASHSQNNEPKQAVAQLIFCMDVRSEPFRRHLEQAGPFETYGCAGFFGLPIKTRELDSSHAHASCPVIVEPRHEVQEFTSAENVKKYRGRRNALLSVSHTFKKMKQHLFASLLLPEVSGPLLGLHTLARSIAPSGAGRVFHQFQDNWAQKPATELSLNRESSLETTETTDLPVGFSTEEKVRYVYQLFKGMGLTSRFAPLVVVCGHESTTTNNPYASSLDCGACGGAAGGFNARVFAALCNLKEVREGLAKEGIVIPEDTVFVAAEHMTTVDDLCWLYVPTLSEAAQKAFDMLQGKLEEVSRNANNERLSKLPGLEGKKKDPLAEAHRRAEDWSEIRPEWGLAGNAALIIGRRELTKHCNLEGRVFLHSYDWRKDPSGEALANIITGPVTVAQWINLQYYASTVAPHYYGSGNKTTQTVTAGIGVMQGNASDLLAGLPWQSVMASDEEIFHSPLRLLVIIEAPQQNIERLFEDDPHFRRKVKNGWLRLVSIDPDSGEWKAWR", "text": "FUNCTION: Part of an energy-coupled inorganic carbon pump. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family."}
+{"protein": "MDPTCQESPAEDSNNEEDLDSTKAAPRIRDTPEDIVLEAPASGLAFHPTRDLLAAGDVDGDVFVFAYSCQEGETKELWSSGHHLKSCRAVVFSEDGQKLVTVSKDKAIHVLDVEQGQLERRISKAHSAPINSLLLVDENVLVTGDDTGGIRLWDQRKEGPLMDMRQHEEYIADMALDPAKKLLLTASGDGCLGVFNIKRRRFELLSEPQSGDLTSVALMKYGKKVACGSSEGTIYLFNWNGFGATSDRFALRAESIDCMVPVTENLLCTGSTDGIIRAVNILPNRVVGTVGQHAGEPVEELALSHCGHFLASSGHDQRLKFWDMTQLRTVVVDDYRRRKKKGGPLRALSSKAWSTDDFFAGLREDEEEAKAPEEVSGESDDDSD", "text": "FUNCTION: Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Cytoplasm. SIMILARITY: Belongs to the WD repeat WDR55 family."}
+{"protein": "MNDVVKVGMADLNVVTPPHTIRTAGLGSCVGVVLYDDVKKVAGMAHIMLPDSALGKKQEFNRAKYADTALDLLLSKLEAIGAKRYSLKAKMAGGAQMFSFASNNDMMRIGQRNVEAVKKKLRELSIPILAEDVGGSNGRTIEFNPETKRLSIRTVHQGEKEI", "text": "FUNCTION: Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). SIMILARITY: Belongs to the CheD family."}
+{"protein": "MTRYFCCGSYFPGYPIYGTNFHGTFRATPLNCVVPLGSPLNYGCGCNGYSSLGYSFGGSNINNLGGCYGGSFYRPWGSGSGFGYSTY", "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 7 family."}
+{"protein": "MGFSGSRANTALGAWSKWLTLCLAMTQPFSVTAKSAADYYVHSLPGQPEGPLLKMHAGHIEISPETSGNLFFWHFENRHIADKPRTVVWLNGGPGCSSEDGALMEIGPYRLIDKETLNYTEGSWDEFANLLFVDQPVGTGFSYGSTEHYVHELDEMASQFVTFLEKWFEIFPHYEPDDLYFAGESYAGQYIPYIARAILDRNKKQDVLANNRVWNLKGLLIGNGWISPQHQYPAYLPYVYQEGVVQGGTQEANLIEAKAAKCMKELNVEDTTGTVHIPDCEDILQAILDYTHKGKRCINMYDIRLTDEYSACGMNWPPDLKDVQPYLRRKDVVKALHINEEKQTGWTECAGAVGSSFKARKSKPAVELLPGLLEEGLPILLFSGQKDLICNHIGTEDMIKNMKWSGGTGFELSPGVWAPRQYWTFEGEPAGIYQQARNLTYVLFYNASHMVPFDYPRRTRDMLDKFLGVDITHIGGDPADSRIDGEKGPTTSVGAHPNSTAAAEREKEKLNTAAWKAYYKSGEVALIIVSTAAVVWGIFLWRSRRKHQSSGYRSIYPMLGLNSTGSLGRFSHKHSRGNGDIEAADFDETELDGQPSQAFLSRSSGDGETYAVGEESSDEEDGASDGQQLMFDQSRGEGRS", "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": "MKKFIILLSLLILLPLTAASKPLIPIMKTLFTDVTGTVPDAEEIAHKAELFRQQTGIAPFIVVLPDINNEASLRQNGKAMLAHASSSLSDVKGSVLLLFTTREPRLIMITNGQVESGLDDKHLGLLIENHTLAYLNADLWYQGINNALAVLQAQILKQSTPPLTYYPHPGQQHENAPPGSTNTLGFIAWAATFILFSRIFYYTTRFIYALKFAVAMTIANMGYQALCLYIDNSFAITRISPLWAGLIGVCTFIAALLLTSKR", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MQHFFTTFSTEGSKISLEALLNAREERAILQQQLITQYGQTLLCITLTAMGGVKKNALLDYVFTKALENLTALFTQLNITAVKEIIRPLETGHEAYFVLPIDARTLKVLMIELEESIPLARLWDLDVFNAKGNLLSRTDFDLSPRTCLVCGENAKICARTHKHEIDEIVDKIQSLAQNHDFAEHIGEQVYLALIQEARLSPKPGLVDAINNGSHKDMNLHTFEQSAISLKPFFTQFVLKGMMTAHLSENQILSEIRPLGLLAEKAMFKVTDGVNTHKGAIFSFGLVCTAIGRLLAQKSLVQSAVDFDVKLICSLVAQFTQGLTDELKNYPEHLPSTAGVRLFQKYGLTGVRGEAENGFNLIQTLLPQFDEYHQLEWEHRLLILLLNLMAINSDTNVVHRGGLAGLYFIQQTAQDLLTDQHLVTDKTALTQALMKFDTACIERNLSSGGSADLLALTIFFLSFRGN", "text": "FUNCTION: Bifunctional enzyme that catalyzes formation of 2-(5''- triphosphoribosyl)-3'-dephosphocoenzyme-A, and then the transfer of this prosthetic group precursor to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield the holo-acyl carrier protein. SIMILARITY: In the C-terminal section; belongs to the CitG/MdcB family. SIMILARITY: In the N-terminal section; belongs to the CitX family."}
+{"protein": "MGFERGGRGGARGGGRGGFGGDRGGRGGARGGSRGGFGGGRGGGAPRGRGGPRGGGRGGATRGRGGARGGAKGGAAGKKVIVEPHRHKGVFVARGGKEDLLATVNLVPGESVYGEKRISVENASKEEGGASTKTEYRIWNPFRSKLAAGILGGLETIYMKPGSKVLYLGAASGTSVSHVADIVGPTGSVYAVEFSHRSGRDLINMATRRTNVIPIVEDARKPMAYRMLLPMVDVIFADVAQPDQARIVGINAKLFLKQGGGLLISIKASCIDSTAPPEQVFASEVQKLREDKFFPKEQLTLEPYERDHAMVSCVYQQKEFVDN", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Note=Fibrillar region of the nucleolus. SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin family."}
+{"protein": "MVARGRTDEISTDVSEANSEHSLMITETSSPFRSIFSHSGKVANAGALEESDKQILEWAGKLELESMELRENSDKLIKVLNENSKTLCKSLNKFNQLLEQDAATNGNVKTLIKDLASQIENQLDKVSTAMLSKGDEKKTKSDSSYRQVLVEEISRYNSKITRHVTNKQHETEKSMRCTQEMLFNVGSQLEDVHKVLLSLSKDMHSLQTRQTALEMAFREKADHAYDRPDVSLNGTTLLHDMDEAHDKQRKKSVPPPRMMVTRSMKRRRSSSPTLSTSQNHNSEDNDDASHRLKRAARTIIPWEELRPDTLESEL", "text": "FUNCTION: Essential for meiotic chromosome segregation. MER1 and MER2 proteins must interact directly or indirectly. MER1 might be responsible for regulating the MER2 gene and/or gene product. MER2 is not required for mitosis and mitotic DNA repair mechanisms. Component of the MER2-MEI4-REC114 complex which seems to be required for meiotic double-strand break (DSB) formation. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to chromosomes."}
+{"protein": "MDIVCEFCDKSFDSKSKVNAHQRTKKCQQFRTITFVCRKCSSAILGYDNILFHVENCNGTTPILHKEIEDKIKVKNHNKEHDNKIFFGKGLNGKTVYIFNYEKSMLTYGSTNIISESIVSTIDNLVEKATLKSLNDAIQSFSKESFLQEILFKYPQPFSISDISKFFEYESRTVMAFLMAKDLNDLFEILFKECKLFPVCIVNDDIYVIDKVVRQNLDKWILEWKQIDYKEVSLSLKGFFLPVLNYAIKLFLNESNNNTTLKLLELIKEIADETKIRKLMSTFTKPIPVFEDIQNIFQNVKYIYNGSYKHTPMDTFIKNISYGSCFVKEKSIKTEHELYSLLMSLTKESEKTALIKKIKMNDNDDIVEIEKEMKLLKV", "text": "SIMILARITY: Belongs to the IIV-6 302L family."}
+{"protein": "MMTASVAGNRSGRSGNIARERSNRSRGAQKSDKERNLSKGSSRPKSNSSRVKKMRKSSLSKVQKNFAVFNDSAEHENKYETLAVAEADEKEVILLDEEEDTAMTTETKGVHAEETANVTGAEGVNAAANALDDNQDFIGFSDSEEEVASGEENGDADYAVEDAEDESSEPLPTNADYPWIQNHDHSRQREIADWLTLEIKDFVSYISPNKTEIQLRNDALKRIRDAVQDFWPDANLHCFGSYATDLYLPGSDIDCVVNSKSGDKDNKNALYSLASYLKRNGLATQVSVIAKARVPIIKFVEPASQIHIDLSFERTNGVEAAKIIRGWLHDTPGLRELVLIVKQFLHARRLNDVHIGGLGGFSIICLAYSFLKLHPRIICRDIEPLQNLGVLLIDFFELYGKNFGYDDVGIAVSEGDASYINKKEYPELTRNLRGTFNLVIQDPGDPANNISRGSFNIRDIKKAFAGAFELLTNRCFELDAATFKHRVGKSILGNVIKYRGAKRDFKDERALIVNKAIQENEEFHQRRGRIVHRDTAEFINISDDDDYELQPPPKRARVPAPAPAPADNVVVLDDPADDYVPAQPVDKLMGLDDTDDYLPAPASPTDTPKLDKAAKRNYWLSKGQTM", "text": "FUNCTION: Catalytic subunit of the TRAMP5 complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Polyadenylates RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. TRF5 is also required for proper nuclear division in mitosis and sister chromatid cohesion. Involved in the regulation of histone mRNA levels. May mediate mitotic chromosome condensation (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DNA polymerase type-B-like family."}
+{"protein": "MFLQKIVLYLSTACMFCYMLGKFLMLVILQFFSPSLAKKFILRMGEKITMTQNPRFNYEDWGLTFMSLAFIKTASSHMWLSLGEEAFVGGEAPDSPVVTMDREKTSISKYLKGNRPLVLSFGSCTUPPFMYKLDEFKQLVKDFSDVADFLVIYIAEAHSTDGWAFKNNYDINQHQSLEDRLSAAQVLVQSEPLCPVVVDEMTDVTTIKYGALPERLFILQAGKVLYKGGKGPWGYNPAEVRSFLEKIK", "text": "FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the iodothyronine deiodinase family."}
+{"protein": "MARSGFEVQKVTVEALFLREIRTRFGKFRLGYLWAILEPSAHLLILLGIFGYIMHRTMPDISFPVFLLNGLIPFFIFSSISNRSVGAIEANQGLFNYRPVKPIDTIIARALLETLIYVAVYILLMLIVWMAGEYFEITNFLQLVLTWSLLIILSCGIGLIFMVVGKTFPEMQKVLPILLKPLYFISCIMFPLHSIPKQYWSYLLWNPLVHVVELSREAVMPGYISEGVSLNYLAMFTLVTLFIGLALYRTREEAMLTS", "text": "FUNCTION: KpsM and KpsT constitute a system for the transport of polysialic acid across the cytoplasmic membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-2 integral membrane protein family."}
+{"protein": "MKRSTTQILTRLRELMLRAQVGDSCGISAYIVPSDDAHQSEYQCQHDERRSFVSGFDGSAGTAVITTETALLWTDGRYYQQAEKQLDSNWVLMRDGLSATPSIGAWLAKNLPKGSFVGVDPRLLSFRVWKPIETELSSAECQLVPIEGNLIDEVWGEDQPPQTSNKIITLKLEHSGVTIAKKWDVVRQQLKEKNADALVVSALDEIAWFLNLRGSDIDFNPVFFSYLIVTNDELLLFVDSGKLPTDFVQHQKENNVQISVLPYASIGIEISKIVSTRESKIWIAPTSSYYLTALIPKSRRIQEVTPICVLKAIKNDVEIAGFINSHIRDGVALCQYFAWLEDQVNKGAEVDEMSGADKLESFRSTKDKYMGLSFTTISASGPNGSVIHYHPKKETNRKINDKEIYLCDSGAQYLDGTTDVTRTLHFGEPTEFQKEAYTRVLKGQLSFGSTVFPAKVKGQVLDTLARKALWDVGLDYGHGTGHGVGHFLNVHEGPMGVGIRLMPDDPGLQANMFISNEPGFYQDGEFGIRVEDIVQIVPGQVAHNFSNRGALTFKTITMCPKQTKMIKKELLSDAEVKLLNSYHQQVWDTLSPILSREGDEFTLSWLKKEVQPI", "text": "FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M24B family."}
+{"protein": "MDTGGNSLASGPDGVKRKVCYFYDPEVGNYYYGQGHPMKPHRIRMTHALLAHYGLLQHMQVLKPFPARDRDLCRFHADDYVSFLRSITPETQQDQIRQLKRFNVGEDCPVFDGLYSFCQTYAGGSVGGSVKLNHGLCDIAINWAGGLHHAKKCEASGFCYVNDIVLAILELLKQHERVLYVDIDIHHGDGVEEAFYATDRVMTVSFHKFGDYFPGTGHIQDIGYGSGKYYSLNVPLDDGIDDESYHLLFKPIMGKVMEIFRPGAVVLQCGADSLSGDRLGCFNLSIKGHAECVKFMRSFNVPLLLLGGGGYTIRNVARCWCYETGVALGVEVEDKMPEHEYYEYFGPDYTLHVAPSNMENKNSRQMLEEIRNDLLHNLSKLQHAPSVPFQERPPDTETPEVDEDQEDGDKRWDPDSDMDVDDDRKPIPSRVKREAVEPDTKDKDGLKGIMERGKGCEVEVDESGSTKVTGVNPVGVEEASVKMEEEGTNKGGAEQAFPPKT", "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. HDA19 is involved in jasmonic acid and ethylene signaling of pathogen response. Part of a repressor complex including APETALA2 (AP2) and TOPLESS (TPL) that control the expression domains of numerous floral organ identity genes (PubMed:23034631). Involved in negative regulation of salinity stress response (PubMed:29018096). Represses the expression of stress tolerance-related genes, genes coding for late embryogenesis abundant (LEA) proteins that prevent protein aggregation, and positive regulators of abscisic acid (ABA) signaling, such as ABI5 and NAC019 (PubMed:29018096). SUBCELLULAR LOCATION: Nucleus Note=excluded from the nucleolus, but associated with the condensing chromatids. SIMILARITY: Belongs to the histone deacetylase family. HD type 1 subfamily."}
+{"protein": "MHSDAPTPVANELSEVSHLAEGDNASFSAGNFTVLQLPSDPSHCIDYAIPAGTLVIVDPNNPDNNRTVKLQAPAVFRPQCALGGTRAPAPRPEESFPDWSEYQKYHHNDRRDPFYGSVTPIAYTIAASTVTAWMLLIILFLSRKPSPLFQKIAVLITAVSLTVFLAQATDTLESQYNEGYQNAYELRHKIMGGWAFRILQVITCVITWLARLQVVIRLFDVPKINTRLAVVGSTLIFTNATIWACLNLIPPWSQYVRNAKSVLPVFGALCSLLLEVFYLVVVVIYSISKRKYAYSRTSIVMAAISWLAMILPMVFIVFDIAHYWIAGWSDFIRWTADAAASVVVWEWTNVIVYQERREQRQSVLGRQVYRDEILDFKGDNGGGTVGGGRTKYPSRMEEDDVPFRSSPNDHHFTSNIPTSAGEGQSFQFFKRARLPMYSRKIWKIARGESAASNNTHYEHAIIEEEEEESIERNRRTPTVQENGEEDDEETYDEENDQYSQDNHSSVHSFESSRPSQHPVPSSGGTRAVGHTHFPLPGQSEGAHTTSPAAAAAAAEPEPEPVAGPSGGAAAHGDSDDDSDNSDDSSLASFTVIQQTGFSVDNQGVPEYDADSAPPTFEPIPGFHRQDYSDAKG", "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 palH/RIM21 family."}
+{"protein": "MECVKQLCRNHLRLDNLTDPVRSVLTKGTTAEKVQLAACCLGVVCSIICLALGIAAAAVGVSCGGFALGLGIIAILLGIVLFATSALDVLENHGLVGCPFKLPCKSSPANEPAVQFFKGKNGSADQVILVTQ", "text": "FUNCTION: Inclusion membrane protein probably involved in early modification events of the chlamydial inclusion. SUBCELLULAR LOCATION: Secreted Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane; Multi-pass membrane protein Note=Secreted, probably by a type III secretion system (Probable). Localized in the inclusion membrane (PubMed:10447885, PubMed:26416906). Inclusion membrane staining is punctate (PubMed:10447885)."}
+{"protein": "MRIHHPLTLAALCVVLHESLGAAQHSNNVARLEHYRIAEIEHWEKRHLRSDSRGHRHHAHHGQVIDKENNNSQEQATTGNSVETNQVPSTEPTKDKTTPMKNALFKLFREKKLKTKNAGNGHAHDDDDDSDFSDDDVPTNAPTDAPTGAPTDAPTDAPTVAPTDAPTDAPTEAPTNAPTGTDAPTDAPTDAQVVPTFD", "text": "FUNCTION: Effector involved in the disease saprolegniosis in salmonids and other freshwater fish, resulting in considerable economic losses in aquaculture (Probable). Within the host fish cells, Htp1 is involved in the uptake of the S.parasitica effector Htp3 at a neutral pH (pH 7.5) and its release from vesicles into host cytosol where it degrades nucleic acids (PubMed:29904064). SUBCELLULAR LOCATION: Secreted Host cell Note=Host cell surface binding and uptake is mediated by an interaction with tyrosine-O-sulfate-modified cell surface molecules and not via phospholipids, as has been reported for RxLR-effectors from plant pathogenic oomycetes. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MAPKGKVGTKGKKQIYEENKETLSFYLRIILGATVLCGAINLGVFYSSSNFWTWATLVFSGIVYAGAYRSMRSMAQASFSEDGSLLDGGIDLNMEQGMAEHIKDIVLLTAIVQVLSCFSLYFWYFWLLAPGRALYLLWVNVLGPWFTADNSSTVPQEQNEKRQRRQERRQMKRF", "text": "FUNCTION: May function as a negative regulator of endoplasmic reticulum-stress induced autophagy. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM208 family."}
+{"protein": "MRAISPRMIRGEFRGRLGGFALDASFSVPATGITGLFGPSGCGKSTVLRCLAGLQHLPGSLCDVDGDVWQDDSTFLKPHQRPIGYVFQEASLFQHLSVKANLVYGAPRGDAGGAAGVIAFDEVIELLGLARLLDRAPRNLSGGERQRVAIGRALLSQPKLLLMDEPLSALDRLTKDEILPFLERLHARLSLPVIYVSHDITEIERLADHLILMRAGHVIGVGPLSDLQSDPALPLATARDAAVNFAAIAEAYDANYGLLTLRVDGGRLLVPSGPVEPGARRRIRIAAGDVSLAREAPRATSILNALSARIVSTSPVGPNEMLVVLGLGPNGNGARLLARVTRRSWDQLQLAEGIEVFAQVKGVALASERGVSEATK", "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": "FLGTINLSLCEQERDADEEKRDEPDESDVEVEKRFLPAALAGIGGILGKLFGK", "text": "FUNCTION: Non-amphipathic mildly cationic alpha-helical antimicrobial peptide with potent activity against Gram-positive (including methicillin-resistant Staphylococcus aureus (MRSA)) and Gram-negative bacteria, and some fungi, as well as against Trypanosoma and Leishmania (both promastigote and amastigote forms) (PubMed:23116712). Strongly and selectively perturbs anionic bilayer membranes by interacting with the polar head groups and acyl region of the phospholipids, with formation of regions of two coexisting phases, one phase rich in peptide and the other lipid-rich (PubMed:23116712). Shows low hemolytic activity (LC(50)=44 uM) and a low toxicity for human monocytes THP-1 and THP-1-derived macrophages (PubMed:23116712). Is not toxic to human hepatoma-derived cells (PubMed:23116712). SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Deeply inserts into the lipid bilayer. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily."}
+{"protein": "MATMEEIQREISAHEGQLVIARQKVKDAEKQYEKDPDDLNKRALHDRESVAASIQSKIDELKRQLADRLQQGRTSGQDRDPTGVEPGDHLKERSALSYGNTLDLNSLDIDEPTGQTADWLTIIVYLTSFVVPIILKALYMLTTRGRQTSKDNKGMRIRFKDDSSYEDVNGIRKPKHLYVSMPNAQSSMKAEEITPGRFRTAVCGLYPAQIKARNMVSPVMSVVGFLALAKDWTSRIEEWLGAPCKFMAESLIAGSLSGNPVNRDYIRQRQGALAGMEPKEFQALRQHSKDAGCTLVEHIESPSSIWVFAGAPDRCPPTCLFVGGMAELGAFFSILQDMRNTIMASKTVGTADEKLRKKSSFYQSYLRRTQSMGIQLDQRIIVMFMVAWGKEAVDNFHLGDDMDPELRSLAQILIDQKVKEISNQEPMKL", "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": "MLQSWEFVLLISCFLCFSSDALQRISLKKMPSIRETLQEMGMKVADVLPSLKHRFSYLDEGLHNKTASTILTNFRDTQYYGEISIGTPAQIFKVVFDTGSSNLWVPSHQCSPLYSACVSHNRYDSSESSTYKPKGTKITLTYGQGYIEGFLSQDIVRVADIPITQFFTEAIALPSIPFMYAHFDGVLGMGYPKQAIGGVIPVFDNIMSEKVLSENVFSVYYSRHSESNTGGEIILGGSDPSHYTGDFHYVSTSREGYWHVDLKGVSIENKIALCHDGCTATIDTGTSFISGPASSISVLMETIGATLSRGDYVIDCNQINLLPDISFHLGDMTYSLSSSTYVLKYSDETECTVAFSAIDIPPPRGPLWLLGATFIKQYYIEFDRQNNRIGFATSF", "text": "FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney (Probable). This protein is also found in snake venom and shown to specifically cleave human and porcine angiotensinogen into angiotensin I. It does not have general protease activity, no cleavage of alpha or beta casein. May be directly responsible for elevation of blood pressure in the victims of envenomation (PubMed:28734982). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MAFLQDGNHTAVTEFILLGLTDGPILRVILFTIILCIYLVTVSGNLSTILLIRVSSQLHHPMYFFLSHLASVDMGLSSSVTPNMLVNFLVKQNTISYIACSIQFGLAAFFGTVECFLLAAMAYDRFVAICNPLLYSTKISTESCIQLVVGSYIGGFLNASSFILSFFSFIFCGPNRINHFYCDLAPLVELSCSDVSVSVVVTSFSAGSVTVITVFVIAVSYSYILITILKMHSTEGRHKAFSTCTSHLTAVTLYYGTITFIYVMPKSSYSTDQNKVVSVFYMVVIPMLNPLIYSLRNNEIKGAIKRQLGKKMFC", "text": "FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MMIPSQSCFCFFFMVSFFLHTLASPTLRHCRHDQRNALLEFKHEFPRVNESNQIPYDVSLSSWNKSIDCCSWEGVTCDAISSEVISLNLSHVPLNNSLKPNSGLFKLQHLHNLTLSNCSLYGDIPSSLGNLFRLTLLDLSYNYLVGQVPPSIGNLSRLTILDLWDNKLVGQLPASIGNLTQLEYLIFSHNKFSGNIPVTFSNLTKLLVVNLYNNSFESMLPLDMSGFQNLDYFNVGENSFSGTLPKSLFTIPSLRWANLEGNMFKGPIEFRNMYSPSTRLQYLFLSQNKFDGPIPDTLSQYLNLIELDLSFNNLTGSFPTFLFTIPTLERVNLEGNHLKGPVEFGNMSSSSSLKFLNFAQNEFNGSIPESVSQYLNLEELHLSFNNFIGTIPRSISKLAKLEYFCLEDNNMVGEVPSWLWRLTMVALSNNSFNSFGESSEGLDETQVQWLDLSSNSFQGPFPHWICKLRSLEILIMSDNRFNGSIPPCLSSFMVSLTDLILRNNSLSGPLPDIFVNATKLLSLDVSRNKLDGVLPKSLIHCKAMQLLNVRSNKIKDKFPSWLGSLPSLHVLILRSNEFYGTLYQPHASIGFQSLRVIDVSHNDLIGTLPSFYFSSWREMSRLTGEDGDFRLSEAPYMGKVLNATAFFVDSMEIVNKGVETEFKRINEENKVINFSGNRFSGNIPESIGLLKELRHLNLSSNAFTGNIPQSLANLMKLEALDLSLNQLSGQIPQGLGSLSFMSTMNFSYNFLEGPVPKSTQFQGQNCSAFMENPKLNGLEEICRETDRVPNPKPQESKDLSEPEEHVINWIAAGIAYGPGVVCGLVIGHIFLSHKHECWFMEKFRRKKPKVVTRIARPSKH", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the RLP family."}
+{"protein": "MAADRNTGHTEEDKLDVLKSTQTVIHKALEKLGYPEEVYELLKEPMRLLTVKIPVRMDDGSVKIFTGYRAQHNDSVGPTKGGIRFHPNVTEKEVKAVKALSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAPDVFTNSQIMAWMMDEYSRIDEFNSPGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKLFNDTITNQELLELDCDILVPAAIENQITEENAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEMANNRRIDMRLAAYMVGVRKMAEASRFRGWI", "text": "FUNCTION: GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family (called gutB1). This 3 amino acid insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon source in the absence of arginine. It is unable to synthesize glutamate. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
+{"protein": "METTTPQSKSSVSHRPPLGREDWWSEEATATLVEAWGNRYVKLNHGNLRQNDWKDVADAVNSRHGDNSRKKTDLQCKNRVDTLKKKYKTEKAKLSPSTWRFYNRLDVLIGPVVKKSAGGVVKSAPFKNHLNPTGSNSTGSSLEDDDEDDDEVGDWEFVARKHPRVEEVDLSEGSTCRELATAILKFGEVYERIEGKKQQMMIELEKQRMEVTKEVELKRMNMLMEMQLEIEKSKHRKRASASGKKNSH", "text": "FUNCTION: Probable transcription regulator (By similarity). Promotes histone acetylation during ethylene signaling in an EIN2-dependent manner, thus regulating positively ethylene-responsive genes (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm."}
+{"protein": "MGVPAFFRWLSRKYPSVIIECNENKQVDADTGRNIYEDPTLPNPNGIEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFECIDRLFGIVRPRKLLYMAIDGVAPRAKMNQQRSRRFRAAKETTEKRLEIARIREELLSRGCKLPPEKEKGEHFDSNCITPGTPFMDRLSKCLHYFVHDRQNNNPAWKGIKVILSDANVPGEGEHKIMDYIRKQRAQPDHDPNTQHVLCGADADLIMLGLATHEPNFTIIREEFLPNKPRPCDICNGFGHEMDKCVGLGATAPTSANFKPDVPIGAEVKFIFVRLSVLREYLKQTLEMPNLPFEYSFERALDDWVFMCFFVGNDFLPHLPSLEIREGAVDRLVELYKKCVYKTRGYLTDSGDVNLDRVQLIMTDLGNAEDQIFKSRQRREEQFKARDKARKRQERNQDHGSLNQSAFGASAVGPNSQQRSVGNYKEEAAALRNRKRTSDMANLDDEDEEENNDEVRLWEDGFKDRYYESKFDVAPGNQQFRYAVALQYVRGLCWVLKYYYQGCASWNWYFPYHYAPFASDFVNIQGLSTMFEKGTKPFNPLEQLMGVFPAASSSHVPEPWAKLMSDPESPIIDFYPEDFKIDLNGKKFAWQGVALLPFVDEKRLFKALVPYYDQLTGEEVKRNKRGDNYLYISNQSPHYKKVKKISEKDDESVCKAISFDGMRGTLGKTELNTAISGVLKSPISGLSDINDNITVTTTFRDPEYDEDYIFEAKRLENAVDPPQVLPNEQSGNKHRPVIGFNSHLTRAYVPDSGHRMLNAGIRNQQGGGGNGGGGGGYGQGGGYGQGIGGNQGQSYQNNSRNYNYNYNNNYNQHQGGGYQNNYNNRQQQQYGHNQRFNQDNSNQQQRNFNNYNGPRNNNYQQQGGSRQQNQNYRRF", "text": "FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote the termination of transcription by RNA polymerase II (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1 subfamily."}
+{"protein": "MMSYIKQPHYAVNGLTLAGTGMDLLHSAVGYPTTPRKQRRERTTFTRAQLDILESLFAKTRYPDIFMREEVALKINLPESRVQVWFKNRRAKCRQQQQQSTGQAKPRPAKKKTSPARETNSEASTNGQYSPPPPGTAVTPSSTAGATVSIWSPASISPIPDPLSIATTPCMQRSAGYPMTYSQAPAYTQSYGGSSSYFTGLDCGSYLSPMHPQLSAPGSTLSPIASSTMGSHLSQSPASLSAQGYGASSLGFTSVDCLDYKDQTASWKLNFNATDCLDYKDQSSWKFQVL", "text": "FUNCTION: Transcription factor involved in anterior and eye development. Promotes the differentiation of both rod and cone photoreceptors cells in the retina. 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. Acts synergistically with nrl to activate the rhodopsin promoter (By similarity). Promotes the formation of anterior regions and represses the formation of posterior structures during development. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAIVALGVVYGDIGTSPLYTAQTFLAGQGGLGSVDREAVLGMLSLVFWSITLITTVKYVLIAMRIDNNGEGGIFALYSLIRKYGAWLAIPAMLGGAAFLADSVLTPAVSISSAVEGLQTLPPLEGLFDENPSLTLMITVVIIVILFSVQSRGTESIGKVFGSMVLVWFGFLAIVGVTNLSNDWSVFEALNPVYGIKFLFSPNNAAGIALMGTVFLSTTGAEALYSDMGHVGRGNIYFTWPFIKVALVLNYFGQGAWMLANSDNPQYTAMESLNPFFQMMSPNVRYLAVILSVSAGVIASQALITGAFTMVSEATRLNWMPHLQVRYPARTRGQLYIPVVNGVLCVSTLAVLAIFKDSEHISAAYGLALTITMITTTVLLGVYLWHSGKRVGAIVFTVLFLAIQAMFFIASMAKFLHGGWFTMLLTAAILFVMYTWNEGTKLERAQRRHMRPNDFLPALDKLHSDFRIPYFADNIVYLTSDSETKRLDTDIFFSIFADHPKRARAWWAVSVETTDEPFTREYSVEDFGTNYIYRVRFRLGFKVSQSIPAYIHQIMHDLSKTGELPKQKSIYPKVDADPDIGTIRYVLIHKALMPESKVSARGALSLQAKYAIRHMAGSPVKWFGLAPYNPLVEVQPLFVSTRRPPRLKRTDTAKTIPTPTPTRAVADPAAVPDPMDTTSGLGRLVQELDAAVSAEARKTAEAAAADAPAEQGDKGDKGKAENGKPAAKPQRSAKQKR", "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": "MTDQQSRPASPRRRSTQSIADRLALDALYEIAKTFAAAPDPVAEVPQIFNVLSSFLDLRHGVLALLAEPGEGAGVNPYVIAATAFQRSPEAPAADVLPDAVARIVFRSGVPFVSFDLAAEFGAEAVPKRLRDAGQTLIAVPLRDPERSHFVLGVLAAYRSHDHNRSGFSDADVRVLTMVASLLEQALRFRRRIARDRERALEDTRRMLQTVTEQRGPAAPVSLDGIVGSSPAIAEVVAQIKRVASTRMPVLLRGESGTGKELFARAVHAQSPRAKGPFIRVNCAALSETLLESELFGHEKGAFTGATALKKGRFELADGGTLFLDEIGEISPAFQSKLLRVLQEGEFERVGGAKTIKVDTRIVAATNRDLEDAVARGQFRADLYFRICVVPIVLPPLRNRKSDIKPLAQLFLDRFNKQNATNVKFAADAFDQICRCQFPGNVRELENCVNRAAALSDGAIVLAEELACRQGACLSAELFRLQDGTSPIGGLAVGRVITPTVRVSAPPPEPAPAPEPAPEAPPREEVPLRTKTAQLSREELLRALESAGWVQAKAARLLGMTPRQIAYALQKFEIELRKI", "text": "FUNCTION: Required for activation of most nif operons, which are directly involved in nitrogen fixation."}
+{"protein": "MWESKFAKESLTFDDVLLIPAQSDILPKDVDLSVQLSDKAKLNIPVISAGMDTVTESKMAIAMARQGGLGVIHKNMGVEEQADEVQKVKRSENGVISNPFFLTPEESVYEAEALMGKYRISGVPIVDNKEDRNLVGILTNRDLRFIEDFSIKIVDVMTQENLITAPVNTTLEEAEKILQKHKIEKLPLVKDGRLEGLITIKDIEKVIEFPNAAKDEHGRLLVAAAIGISKDTDIRAQKLVEAGVDVLVIDTAHGHSKGVIDQVKHIKKTYPEITLVAGNVATAEATKDLFEAGADIVKVGIGPGSICTTRVVAGVGVPQITAIYDCATEARKHGKAIIADGGIKFSGDIIKALAAGGHAVMLGSLLAGTEESPGATEIFQGRQYKVYRGMGSLGAMEKGSNDRYFQEDKAPKKFVPEGIEGRTAYKGALQDTIYQLMGGVRAGMGYTGSHDLRELREEAQFTRMGPAGLAESHPHNIQITKESPNYSF", "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. SIMILARITY: Belongs to the IMPDH/GMPR family."}
+{"protein": "MGQSLLPPSGGDDNIQPVDLKAALEERYLAYALSTIMHRALPDVRDGLKPVHRRIIHAMSEMGLRPNSSFKKCARIVGDVIGKFHPHGDQSVYDALVRLAQDFSQRYPVVDGQGNFGNIDGDNAAAYRYTEAKMTEVAALLLEGIDQDAVDFRPTYNEEDQEPTVLPGAFPNLLANGASGIAVGMATSIPPHNAHELCDAALHLIKHPDATVEDLLFDPANPQRGGIEGPDFPTGGVIVESRASMAESYRTGRGGFRVRARWAVEDLGRGGFQIVVTEIPYQVQKSRLIEKIAELLIARKLPLLEDIRDESAEDVRVVLVPKSRSVDANILMESLFKLTELESRIPLNMNVLSMGRVPRVMALNEVLSEWLAHRREVLQRRSRHRLAAIDRRLEILGGYLIAYLNIDEVIRIIREEDEPKAVMIERFGLTDVQAEAILNMRLRSLRKLEEFEIRTEFDSLSKEKAEIEALLASGDKQWQAVAWEIGEVKKKFAKATELGKRRSTFSDAPDADVEAIQQAMIEKEPITVVISEKGWIRALKGHIADTSSLQFKDGDGLKVSFPAQTTDKILIFTTGGKAYTLGGDKLPGGRGHGEPLRIMVDMENDQDVLTAFVHDPARKLIVSSTAGNGFVVTESDIVANTRKGKQVMNVTMPDEAKLVVPVKGDHLAVVGENRKMLVFPLVQVPEMARGKGVRLQRYKDGGVSDIRSFAIAEGLTWEDSAGRVFTKTRDELIEWMGDRAGAGRVVPKGFPRSGKFSG", "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. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 1 subfamily."}
+{"protein": "MEKSSQIHGSKPGDDNADEPENAAGQSQIRKQGADDLLDEIDGLLESNAEEFVRSYVQKGGQ", "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. SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family."}
+{"protein": "MRNFPVPYSNELIYSTIARAGVYQGIVSPKQLLDEVYGNRKVVATLGLPSHLGVIARHLHQTGRYAVQQLIYEHTLFPLYAPFVGKERRDEAIRLMEYQAQGAVHLMLGVAASRVKSDNRFRYCPDCVALQLNRYGEAFWQRDWYLPALPYCPKHGALVFFDRAVDDHRHQFWALGHTELLSDYPKDSLSQLTALAAYIAPLLDAPRAQELSPSLEQWTLFYQRLAQDLGLTKSKHIRHDLVAERVRQTFSDEALEKLDLKLAENKDTCWLKSIFRKHRKAFSYLQHSIVWQALLPKLTVIEALQQASALTEHSITTRPVSQSVQPNSEDLSVKHKDWQQLVHKYQGIKAARQSLEGGVLYAWLYRHDRDWLVHWNQQHQQERLAPAPRVDWNQRDRIAVRQLLRIIKRLDSSLDHPRATSSWLLKQTPNGTSLAKNLQKLPLVALCLKRYSESVEDYQIRRISQAFIKLKQEDVELRRWRLLRSATLSKERITEEAQRFLEMVYGEE", "text": "FUNCTION: TnsABC + TnsD promote high-frequency insertion of Tn7 into a specific target site known as att-Tn7 whereas TnsABC + TnsE promote low-frequency insertion into many different sites. FUNCTION: Required for Tn7 transposition. It may at least play a role in DNA sequence recognition. It seems to be required for specific binding to a region of att-Tn7."}
+{"protein": "MSIDWEQTFRKWSKPSSETESTKAENAERMIKAAINSSQILSTKDISVFPQGSYRNNTNVREDSDVDICVCLNTLVLSDYSLVPGMNDKLAELRTASYTYKQFKSDLETALKNKFGTLGVSRGDKAFDVHANSYRVDADVVPAIQGRLYYDKNHNAFIRGTCIKPDSGGTIYNWPEQNYSNGVNKNKSTGNRFKLIVRAIKRLRNHLAEKGYNTAKPIPSYLMECLVYIVPDQYFTGDSYKTNVENCINYLYNQIDSSDWTEINEIKYLFGSHQMWNKTQVKEFLLTAWSYIQKN", "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 (Probable). A type I-B(UU) CBASS system (PubMed:32839535). FUNCTION: Cyclic dinucleotide synthase that catalyzes the synthesis of 3',3'-cyclic UMP-UMP (c-di-UMP) as the major product, and of 3',3'- cyclic CMP-UMP as a minor product, that are second messengers for cell signal transduction. SIMILARITY: Belongs to the CD-NTase family. E02 subfamily."}
+{"protein": "MNIMITKIFFLVQLFYIVVSKSSAEENCETVASEVHVTKEEYDEMGRLLRSCSGEVSVNKCEGMCNSQVHPSISSPTGFQKECFCCREKFLRERLVTLTHCYDPDGIRFEDEENALMEVRLREPDECECYKCGDFSR", "text": "FUNCTION: Final heterodimeric neurohormone released at the end of the molting cycle, involved in the sclerotization (tanning) of the insect cuticle, melanization and wing spreading. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MTEALYFLDCYLKEFEATVEKVTEGKYIVLDRTAFYPESGGQPSDTGKLVRERDGAEFKVVYAGKFNGDISHEISPEGETGAEGLKVGDKVKGIIDWDRRYRHMRMHTATHVIANVIEKEAGAQITGNQLGLDQSRVDFSLEAFDREKFAEYEKIANEIIAENHSVNLYLVSRKEAEERLSRLTTLAKGFSEEITEVRLVEIEGVTIEACGGSHLKNTGEIKGIKIEKLQNKGKSNRRMYFSLLDQASGLK", "text": "FUNCTION: Functions in trans to edit the amino acid moiety from mischarged Ser-tRNA(Ala). Recognition depends, at least in part, on the acceptor stem of tRNA(Ala). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-M subfamily."}
+{"protein": "MACMHQAQLYNDLEELLTGPSVPIVAGAAGAAALTAYINAKYHIAHDLKTLGGGLTQSSEAIDFINRRVAQKRVLTHHIFQEQVQKQSNHPFLIFEGKTWSYKEFSEAYTRVANWLIDELDVQVGEMVAIDGGNSAEHLMLWLALDAIGAATSFLNWNLTGAGLIHCIKLCECRFVIADIDIKANIEPCRGELEETGINIHYYDPSFISSLPNNTPIPDSRTENIELDSVRGLIYTSGTTGLPKGVFISTGRELRTDWSISKYLNLKPTDRMYTCMPLYHAAAHSLCTASVIHGGGTVVLSRKFSHKKFWPEVVASEANIIQYVGELGRYLLNGPKSPYDRAHKVQMAWGNGMRPDVWEAFRERFNIPIIHELYAATDGLGSMTNRNAGPFTANCIALRGLIWHWKFRNQEVLVKMDLDTDEIMRDRNGFAIRCAVNEPGQMLFRLTPETLAGAPSYYNNETATQSRRITDVFQKGDLWFKSGDMLRQDAEGRVYFVDRLGDTFRWKSENVSTNEVADVMGTFPQIAETNVYGVLVPGNDGRVRSLNCHGRRRDRVDIRFAALAKHARDRLPGYAVPLFLRVTPALEYTGTLKIQKGRLKQEGIDPDKISGEDKLYWLPPGSDIYLPFGKMEWQGIVDKRIRL", "text": "FUNCTION: Acyl-CoA synthetase required for both the import of long chain fatty acids (LCFAs) (C14-C18) and the activation very long chain fatty acids (VLCFAs) (C20-C26) by esterification of the fatty acids into metabolically active CoA-thioesters for subsequent degradation or incorporation into phospholipids. The transport and fatty acyl-CoA synthetase activities are genetically separable and are thus independent activities. Esterifies VLCFAs in the peroxisome matrix. The VLCFAs are actively transported into peroxisomes by a PXA1-PXA2 heterodimeric transporter in the peroxisomal membrane. SUBCELLULAR LOCATION: Lipid droplet Cell membrane; Multi-pass membrane protein Peroxisome membrane; Multi-pass membrane protein Peroxisome. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MWPQPRLPPHPAMSEKTQQGKLAAAKKKLKAYWQRKSPGIPAGANRKKKVNGSSPDTATSGGYHSPGDSATGIYGEGRASSTTLQDLESQYQELAVALDSSSAIISQLTENINSLVRTSKEEKKHEIHLVQKLGRSLFKLKNQTAEPLAPEPPAGPSKVEQLQDETNHLRKELESVGRQLQAEVENNQMLSLLNRRQEERLREQEERLHEQEERLHEQEERLCEQEERLREQEERLCEQEERLREQEERLCEQEERLREQEERLCEQEERLREQEERLREQEERLCEQEERLCEQEERLREQEERLCEQEERLCEQEERLCEQEKLPGQERLLEEVEKLLEQERRQEEQERLLERERLLDEVEELLEQERLRQQDERLWQQETLRELERLRELERLRELERMLELGWEALYEQRAEPRSGFEELNNENKSTLQLEQQVKELEKSGGAEEPRGSESAAAARPVPGAPVPQGAWMCGQAGWTPQEHPGLSGEAVGTGEAAGGAEEAACHSFRAAENRELNITII", "text": "SIMILARITY: Belongs to the GOLGA6 family."}
+{"protein": "MSQDPHNGKGTFEVHKQPQPGLKVFRKGKYIDPKTFQMSPALIRARRPFFVRNMLALAGLTGFVAGIYGYTMYSLRTDDFGDVPIPPLDPEEIKKLQSKYSDDSKA", "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": "MKTSVLLFMLGLTFLFDGLAAINLQEGERTCYDIGELCSSDKPCCSGYYCSPRWGWCIYSTRGGR", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 31 (Jztx-15) subfamily."}
+{"protein": "MKHTLSVLVQDEAGVLSRISGLFARRGFNIASLAVGPAEQIGVSRITMVVQGDNRTIEQLTKQLYKLVNILNVQDVTNIPSVERELMLIKIQVNSQNRIEALEIVKIFRANVVDIAEDLIIVEVTGDPGKIVAIEQLLTKFGIIEIARTGKISLVRTSKINTEYLKDKVVAYNA", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the acetolactate synthase small subunit family."}
+{"protein": "MLLVTNDFPPRRGGIQSYLEAFVGELVRTHELTVYAPKWKGAEEYDEKAARSGYRVVRHPTTLMLPEPTVASRMKRLIGEHDIETVWFGAAAPLALLGPLARRAGARRIVASTHGHEVGWSMLPVARTALRRIGNDADVVTFVSRYTRSRFASAFGPSAALEHLPPGVDTDRFAPDPDARARMRERYGLGDRPVVVCLSRLVPRKGQDMLIRALPELRRRVPDTALAIVGGGPYLETLQRMASDLGVAEHVVFTRGIPAEELPAHHAMADVFAMPCRTRGAGLDVEGLGIVYLEASACGVPVVAGRSGGAPETVLDGKTGTVVDGTDVDAITTAVGDLLADPRRAAAMGVAGRHWALDNWQWRTRGARLAELLSGRREARQA", "text": "FUNCTION: Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM) (PubMed:10531370, PubMed:19638342). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 6 of a phosphatidyl-myo- inositol bearing an alpha-1,2-linked mannose residue (PIM1) to generate phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2) (PubMed:19638342). PimB also catalyzes the addition of a mannosyl residue from GDP-Man to the position 6 of phosphatidyl-myo-inositol bearing an acylated alpha-1,2-linked mannose residue (Ac1PIM1) to generate monoacylated phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2) (PubMed:19638342). The addition of the second mannosyl residue by PimB preferentially occurs before the acylation of the mannosyl residue transferred by PimA. Also able to transfer a mannosyl residue from GDP- Man to the position 6 of a phosphatidyl-myo-inositol (PI), but this reaction is very slow (PubMed:19638342). SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
+{"protein": "MTGRLIYLMGPSGSGKDSLLQAAREPLALRGCRIVRRVITRSAEAVGEDAQAVTPAQFDTLERASAFAMSWRANGLCYGIPVQIDEWLAQGYDVLVNGSRGYLAQARRRYPDLLAVLLGVQPEVLRQRLLARGRESPEEIEARLARNAEFAAGLEGPLFQLDNSGELDDTVRALLAWLGGDRACA", "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": "MLSNRAFGETIEDYEVQHLLGKGGFAIVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSKEMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRSSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSTPGALNMFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIQEEFKHHKLTYEQPGLFRQTSTGLAEPNWPGATKASSFRMEMGMVQNSKPAPVKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFFRFRPTYNEDRITDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYENLPSKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPSEGLKVYDRNGMFLSDHSCSESRSLIEHGNECFTHCVNISNALEVAQTKENSCFPVTIGRRPLTDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSVSTISSTRNTTGFETNCSRSNMLAAHQNIPIKRISVPDVGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKDDDLPFPVRDRVGQIPNIQLKLKTAPLLESGRKIDYNAMTPKTTTPCYNRMLL", "text": "FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily."}
+{"protein": "MSQIHKHTIPANIADRCLINPQQYEAMYQQSINVPDTFWGEQGKILDWIKPYQKVKNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVDDALKNPNVTSVEHVVVLKRTGGKIDWQEGRDLWWHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAIAMPS", "text": "FUNCTION: Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs 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": "AEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDYCGR", "text": "FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2 transcriptional activity. FUNCTION: Sequence-specific DNA-binding transcription factor (By similarity). Plays a role in hindbrain segmentation by regulating the expression of a subset of homeobox containing genes and in Schwann cell myelination by regulating the expression of genes involved in the formation and maintenance of myelin (By similarity). Binds to two EGR2- consensus sites EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in the HOXB3 enhancer and promotes HOXB3 transcriptional activation (By similarity). Binds to specific DNA sites located in the promoter region of HOXA4, HOXB2 and ERBB2 (By similarity). Regulates hindbrain segmentation by controlling the expression of Hox genes, such as HOXA4, HOXB3 and HOXB2, and thereby specifying odd and even rhombomeres (By similarity). Promotes the expression of HOXB3 in the rhombomere r5 in the hindbrain (By similarity). Regulates myelination in the peripheral nervous system after birth, possibly by regulating the expression of myelin proteins, such as MPZ, and by promoting the differentiation of Schwann cells (By similarity). Involved in the development of the jaw openener musculature, probably by playing a role in its innervation through trigeminal motor neurons (By similarity). May play a role in adipogenesis, possibly by regulating the expression of CEBPB (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family."}
+{"protein": "MRLVLFILLLPVCLATPFHQKGLFDFMLEDEGSADLASTDDPVISGFGPVCPFRCQCHLRVVQCSDLGLERVPKDLPPDTTLLDLQNNKITEIRDGDFKNLKNLHALILVNNKISKISPQAFAPLKKLERLYLSKNNLKELPENMPKSLQEIRAHENEISKLRKAVFNGLNQVIVLELGTNPLKSSGIENGAFQGMKRLSYIRIADTNITSIPKGLPPSLTELHLDGNKISKIDAEGLSGLTNLAKLGLSFNSISSVENGSLNNVPHLRELHLNNNELVRVPSGLGEHKYIQVVYLHNNKIASIGINDFCPLGYNTKKATYSGVSLFSNPVQYWEIQPSAFRCIHERSAVQIGNYK", "text": "FUNCTION: May affect the rate of fibrils formation. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily."}
+{"protein": "MSSTMFVKRNPIRETTAGKISSPSSPTLNVAVAHIRAGSYYEIDASILPQRSPENLKSIRVVMVSKITASDVSLRYPSMFSLRSHFDYSRMNRNKPMKKRSGGGLLPVFDESHVMASELAGDLLYRRIAPHELSMNRNSWGFWVSSSSRRNKFPRREVVSQPAYNTRLCRAASPEGKCSSELKSGGMIKWGRRLRVQYQSRHIDTRKNKEGEESSRVKDEVYKEEEMEKEEDDDDGNEIGGTKQEAKEITNGNRKRKLIESSTERLAQKAKVYDQKKETQIVVYKRKSERKFIDRWSVERYKLAERNMLKVMKEKNAVFGNSILRPELRSEARKLIGDTGLLDHLLKHMAGKVAPGGQDRFMRKHNADGAMEYWLESSDLIHIRKEAGVKDPYWTPPPGWKLGDNPSQDPVCAGEIRDIREELASLKRELKKLASKKEEEELVIMTTPNSCVTSQNDNLMTPAKEIYADLLKKKYKIEDQLVIIGETLRKMEEDMGWLKKTVDENYPKKPDSTETPLLLEDSPPIQTLEGEVKVVNKGNQITESPQNREKGRKHDQQERSPLSLISNTGFRICRPVGMFAWPQLPALAAATDTNASSPSHRQAYPSPFPVKPLAAKRPLGLTFPFTIIPEEAPKNLFNV", "text": "FUNCTION: Required for fertility. Involved in chromatid cohesion establishment, in chromosome structure during male and female meiosis (e.g. the synapse formation between homologous chromosomes, the recombination, and the cohesion of both chromatid arm and centromere), and in axial element formation. Regulates the switch from mitosis to the reductional meiosis division of megaspores prior to the female gametogenesis (megasporogenesis). SUBCELLULAR LOCATION: Nucleus Note=Localized in meiocyte nuclei just before meiosis, exclusively in meiotic G1 and S phase (at protein level)."}
+{"protein": "MKLCVTVLSLLVLVAAFCSPALSAPMGSDPPTSCCFTYTVRKLPRNFVTDYYETSSLCSQPAVVFQTKKGRQVCANPSDDWVQEYMDDLELN", "text": "FUNCTION: Monokine with inflammatory and chemokinetic properties. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
+{"protein": "MVNTQNQISQTSDLDYIVNQPYKYGFTTSVESEQFPRGISREVVKLISKKKNEPEYLLNFRLKAYEKWTKMKNPKWAHLKHPNIDFNSIIYYAVPKLKKELNSLDEVDPEILDTFNKLGISLNEQKRLSNVAVDAVFDSVSIATTFKKELAEAGVIFCSISEAIRNYPDLIQKYLGTVVPSGDNYFAALNSAVFSDGSFCYIPPDTVCPLELSTYFRINNEESGQFERTLIVADRGSKVSYLEGCTAPQYDTNQLHAAIVELIALDDAEIKYSTVQNWYAGNKDGKGGIYNFVTKRGLCSGKNSKISWTQVETGSAITWKYPGCILAGDNSQGEFYSVALTNNYQEADTGTKMIHIGNNTKSKIISKGISAGKSKNSYRGLVKIGPQSFNSRNYSQCDSLLIGQSSQANTFPYIQVQNPTAKVEHEASTSKISEDQIFYFLQRGINLEESVSLMISGFCKDVFNELPMEFAVEADRLLSLKLEGTVG", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the UPF0051 (ycf24) family."}
+{"protein": "MEASGGVGGAFLKDVVAYVEVWSSKGTENYSRTFAKQLEDMGATVSKTLNKQVTHVIFKDGYQSTWDKAQKTGAKLVSVLWVEKCRMAGALVDESLFPAVNTDEHLPNLSRKKHKCMQPKDFILKTPENDKRLQKKFEKMAEELQRQKAALDDDVPVLLFESPRSLVYSSPVNVMKRRLQDMKEKRENLSPTSSQMLEQSQQNPCVSLFETSLNISHQPLSSDESFASGSHSSFGDSCGDQERKLGRSANEMTTVTCPSSPVLRASSFYGSASPNHLRQPRPQKAPDSPSKESINCQKDATGAVADSERKQAAGVSQGVPDEKLCLSPTMSIIEEHQVRLGPKNSSAKRKRAADLGSSPKGKLKKRYKRKSALAIQLFKSDQSPPSTIRLIPGTPDVEASSYEDYFSPDNLKERNSERLPPEAQQLASPSLFHCRGLSKWERRNMLEMCDFTCIGEKHRSISSISDLISKSASSLEKPVKEEVNTASTCLLLVETSANDSPGLCSQPGPQLRDDTGPEGSSHPDTLSSSAHHITPLKGNSTETRDPGDGKGSPKEGSTPPASASPEDEVHICNLSLGEDCNVEKSVEEKENIATGYSESVKNGPGRPDPSDSSCTGLVRPQQKPKKSEKEEKPTRTLVMTSMPSEKQTLIIQVVSTLKGFSFAPEVCETTTHVLVGKSARTLNVLMGIARGCWILSYEWVLLSLELGHWISEEPFELSETFPAAPICRLERHLSTQQYQGTLFANQPKMFIAPASSPPRAKLCELVLLCGGQVSPAPQLASLIIGPYKGKKKARIQYLSEKWVLDSITQHKICDFNNYQLLQ", "text": "FUNCTION: Implicated in chromosome condensation and DNA damage induced cellular responses. May play a role in neurogenesis and regulation of the size of the cerebral cortex (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome."}
+{"protein": "MYRLISSIASKARVARNCTSQIGSRLSSTRNYAAKDIRFGVEGRALMLRGVEELADAVKVTIPPKGRNVIIEQSWGAPKVTKDGVTVAKSIEFKDRVKNVGASLVKQVANRPTQLNRCLGDGTTCATVLTRAIFTEGCKSVAAGMNAMDLRRGIKLAVDTVVTKLKSRARMISTSEEIAQVGTISANGDRELVTDCKAMESVGKEGVITIQDGKTLFNELEVVEGMKIDRGYISPYFITNQKNQKCELEDPLILIHEKKISNLNSMVKVLELALKSQRSLLIVAADLESDALAVLILNKLRAGIKVCAVKAPGFGENRKANMHDLATLTGAQVITEELGMNLEKIDLSMLGNCKKITVSKDDTVFLGWGAGDKKAIGERCEQIRSMVEASESDYDKEKLQERLAKLSGGVAVLKIGGASESEVGEKKDRVTDALNATKAAVEEGIVPGGGVALLYASKELDKLSTANFDHKIGVQIIQNALKTPVYTIASNAGVEGAVIVGKLLESDNPDLGYDAAKGEYVDMVKSGIIDPVKVIRTALVDAASVSSLLTTTEAVVTEIPTKEDASPAMGGGGGGMGGMGGMGGMGF", "text": "FUNCTION: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the chaperonin (HSP60) family."}
+{"protein": "MEKKNITLTILLTNLFIAFLGIGLVIPVTPTIMNELHLSGTAVGYMVACFAITQLIVSPIAGRWVDRFGRKIMIVIGLLFFSVSEFLFGIGKTVEMLFISRMLGGISAAFIMPGVTAFIADITTIKTRPKALGYMSAAISTGFIIGPGIGGFLAEVHSRLPFFFAAAFALLAAILSILTLREPERNPENQEIKGQKTGFKRIFAPMYFIAFLIILISSFGLASFESLFALFVDHKFGFTASDIAIMITGGAIVGAITQVVLFDRFTRWFGEIHLIRYSLILSTSLVFLLTTVHSYVAILLVTVTVFVGFDLMRPAVTTYLSKIAGNEQGFAGGMNSMFTSIGNVFGPIIGGMLFDIDVNYPFYFATVTLAIGIALTIAWKAPAHLKAST", "text": "FUNCTION: Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
+{"protein": "MFTMKKPMLLLFFLGMISMSLCQDERGADEDDGGEMTEEEKRGAFGDLLKGVAKEAGLKLLNMAQCKLSGNC", "text": "FUNCTION: Antimicrobial peptide. Active against a variety of Gram- negative and Gram-positive bacterial strains. Not active against fungi. Shows very weak hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
+{"protein": "MSATGLGPVRCAFVLLLALCSRPASSQDCSAPCQCPAGPAPRCPAGVSLVLDGCGCCRVCAKQLSELCTERDPCDPHKGLFCDFGSPANRKIGVCTAKDGAPCVFGGTVYQSGESFQSSCKYQCTCLDGSVGCVPLCSVDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKEHTVVGPALAAYRPEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNAFCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTTLPVEFKCPDGEVMKKSMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA", "text": "FUNCTION: Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes (By similarity). Mediates heparin- and divalent cation- dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells (By similarity). Enhances fibroblast growth factor-induced DNA synthesis (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the CCN family."}
+{"protein": "MSPVQLAEKNYERDEQFTKALHGESYKKTGLSALIAKSKDAASVAAEGYFKHWDGGISKDDEEKRLNDYSQLTHHYYNLVTDFYEYGWGSSFHFSRYYKGEAFRQATARHEHFLAHKMNLNENMKVLDVGCGVGGPGREITRFTDCEIVGLNNNDYQIERANHYAKKYHLDHKLSYVKGDFMQMDFEPESFDAVYAIEATVHAPVLEGVYSEIYKVLKPGGVFGVYEWVMTDKYDETNEEHRKIAYGIEVGDGIPKMYSRKVAEQALKNVGFEIEYQKDLADVDDEIPWYYPLSGDLKFCQTFGDYLTVFRTSRIGRFITTESVGLMEKIGLAPKGSKQVTHALEDAAVNLVEGGRQKLFTPMMLYVVRKPLEKKD", "text": "FUNCTION: Sterol 24-C-methyltransferase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:9593144, PubMed:20946868). ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol (PubMed:9593144, PubMed:20946868). 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). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family."}
+{"protein": "MSQRMQQGQPMIILGEDSQRTSGQDAQSMNITAGKAVAEAVRTTLGPKGMDKMLVDSGGQVVVTNDGVTILKEMDIDHPAANMIVEVSETQEDEVGDGTTTAVINAGELLDQAEDLLDSDVHATTIAQGYRQAAEKAKEVLEDNAIEVTEDDRETLTKIAATAMTGKGAESAKDLLSELVVDAVLAVKDDDGIDTNNVSIEKVVGGTIDNSELVEGVIVDKERVDENMPYAVEDANIAILDDALEVRETEIDAEVNVTDPDQLQQFLDQEEKQLKEMVDQLVEVGADAVFVGDGIDDMAQHYLAKEGILAVRRAKSSDLKRLARATGGRVVSSLDDIEADDLGFAGSVGQKDVGGDERIFVEDVEDAKSVTLILRGGTEHVVDELERAIEDSLGVVRTTLEDGKVLPGGGAPETELSLQLREFADSVGGREQLAVEAFAEALDIIPRTLAENAGLDPIDSLVDLRSRHDGGEFAAGLDAYTGEVIDMEEEGVVEPLRVKTQAIESATEAAVMILRIDDVIAAGDLSGGQTGSDDDDGGAPGGMGGGMGGMGGMGGMGGAM", "text": "FUNCTION: Molecular chaperone that assists in the folding or refolding of nascent or denatured proteins along with ATP hydrolysis (Probable). ATPase activity is highest in thermosome assemblies containing CCT1:CCT2, followed by assemblies containing CCT1:CCT2:CCT3. Required for thermosome ATPase activity. Not required for growth. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
+{"protein": "MDCVESYLSGDNSDESPVMHTWFSPSPSPSDSSSSPSSSASSSIGRNSDDGEKSSEDGGDDAGENEVESPYKGPLEMMESLEQVLPVRKGISKYYSGKSKSFTNLTAEAASALTSSSSMKDLAKPENPYSRRRRNLLCHQIWENNKTTPRGGISKKHVMSSSRSALTLAMAVAAGVMTGEGSSSGGDSSPGSSPTTSGSPPRQLHHHQHQMKKLPPLYPRSQGSFGNLTSSQSSLGFCAWRSFSVADFPRCFPATASGIGFNDS", "text": "FUNCTION: Promotes slightly the tolerance to zinc (Zn) and to oxidizing chemicals (e.g. diamide). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MNFKYIVAVSFLIASAYARSEENDEQSLSQRDILEEESLREIRGIGAKILGGVKTALKGALKELASTYVNGKRTAEDHEVMKRLEAVMRDLDSLDYPEEAAERETRGFNQEEIANLFTKKEKRILGPVIGTIGNVLGGLLKNLG", "text": "FUNCTION: Maximin-7 shows antimicrobial activity against bacteria and against the fungus C.albicans. It has little hemolytic activity (By similarity). FUNCTION: Maximin-H6 shows antimicrobial activity against bacteria and against the fungus C.albicans. Shows strong hemolytic activity (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
+{"protein": "MGLLDLCEEVFGTADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPVLTQDRDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAYLDFKGDMDQIMESVLCVQYTEEPRIRNIIQQAIDAGEVPSYNAFVKESKQKMNARKRRAQEEAKEAEMSRKELGLDEGVDSLKAAIQSRQKDRQKEMDNFLAQMEAKYCKSSKGGGKKSALKKEKK", "text": "FUNCTION: Acts as a dual histone chaperone and heat shock co-chaperone (PubMed:33857403). As a histone chaperone, forms a co-chaperone complex with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2 in histone H3-H4 heterodimer recognition and facilitate the assembly of histones into nucleosomes (PubMed:33857403). May also act as a histone co-chaperone together with TONSL (PubMed:33857403). May recruit histone chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers (PubMed:33857403). Also plays a role as co-chaperone of the HSP70 family of molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8 (PubMed:17182002, PubMed:33857403). As a co-chaperone, may play a role in the recruitment of HSP70-type molecular chaperone machinery to histone H3-H4 substrates, thereby maintaining the histone structural integrity (PubMed:33857403). Exhibits activity to assemble histones onto DNA in vitro (PubMed:33857403). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell membrane Note=Predominantly nuclear. Translocates to the cytoplasm and membrane after heat shock."}
+{"protein": "MAGCVARRALAVGSRWWSRSLATTRGSRPLCAVGGAGGLPPVATATTRRHLSSRNRAEGKVLETVGVFEVPKQNGKYETGQLFLHSVFGYRGVVLFPWQARLYDRDVASATPEKAENPAGHGSKEVKGKTHTYYQVLIDARDCPHISQRSQTEAVTFLANHDDSRALYAIPGLDYVSHEDILPYTSTDQVPIQHELFERFLLYDQTKAPPFVARETLRAWQEKNHPWLELSDVHRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEKTPPSGLHW", "text": "FUNCTION: Involved in DNA damage tolerance by regulating translesion synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG and abasic sites. May act by stimulating activity of DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta (POLD1). SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Note=Mainly localizes to the mitochondrial matrix; a small fraction localizes in the nucleus."}
+{"protein": "MANVKTEKSAKFAWNEENTQQAVTMYQQLINENGLEFANSDGLKEIAKTVGAASPVSVPSKLTSAKAYQKSDKPRKVGGGSSIRKAHYVRVIAKHAIDSGIIKDADDLASLESAKLETLDAVAQLLGVADEVKQAAGE", "text": "FUNCTION: Involved, together with A1 protein, in the second step transfer (SST) which allows the completion of viral DNA into the host cell. SIMILARITY: Belongs to the T5likevirus A2 protein family."}
+{"protein": "MSVYSKLPSQLKKPLVKKAVVLLIALYGVKKLSPYFFGKLKGRTSKQVKGADPLTSNGEPLVEAARKRKRSPAVNREFFDRLIRLLKILFPRLFCKELGLLGFHSLALISRTFLSIYVANLDGQIVKTIVKKDPRAFVVELTKWLLIAIPATFVNSAIRYLEGQLTLAFRTRLVTHAYMLYFSDQTYYRVSNMDGRLANPDQSLTEDVVMFAASVAHLYSNLTKPILDVVVTCYTLIKTAESKGANTTWPSVIAGIVVALTAKVLRAFSPRFGKLVAEEARRKGDLRYMHSRIIANSEEIAFYGGHKIEMLQLQRSYNSLSRQINLILFKRLWYVMLEQFLMKYLWSASGLVMVAVPIITATGYSKYDSEDVKQAALDMKEEDLVSERTQAFTTARSLLNAAADAVERIMVSYKEVTELAGYTARVYEMFEVFEDVRDGVYRRSATEVKPEETGAPQNVTHGMRVEGPLQIRGQVIDVEQGIKCENLPIITPTGDVVVSSLNMQVDEGMHLLITGPNGCGKSSLFRILSGLWPVYSGVLYKPSPDHMFYIPQRPYMSVGTLRDQVIYPHSVQEMQEKGITDRQLEEILQTVSLRYILEREGGWDAVSDWKDVLSGGEKQRMGMARMFYHKPQYALLDECTSAVSIDVEGKIFEAAKDAGISLLSITHRPSLWKYHSHLLQFDGEGGWRFEKLDASTRISLQDEKIRLETQLSGIPKMQQRLTELCRILGEDSSLPTPGDEEEDEEEDEKQTERDVQSAGKEKDLME", "text": "FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)- CoA from the cytosol to the peroxisome lumen. Coupled to the ATP- dependent transporter activity has also a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP- dependent transport into peroxisomes, the ACOT activity is essential during this transport process. Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (By similarity). Involved in oligodendrocyte patterning and myelination (PubMed:28911205). SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily."}
+{"protein": "KKDDYPVDTAKRNCKFPCNVIDKEGYCDNLCKGRKAEKGYCYRLNASCYCYGLPDDSPTKKSGRCNPNL", "text": "FUNCTION: Inhibits voltage-gated sodium channels (Nav). This toxin shows insect lethality against crickets. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family."}
+{"protein": "MEPQPGGARSCRRGAPGGACELGPAAEAAPMSLAIHSTTGTRYDLAVPPDETVEGLRKRLSQRLKVPKERLALLHKDTRLSSGKLQEFGVGDGSKLTLVPTVEAGLMSQASRPEQSVMQALESLTETQVSDFLSGRSPLTLALRVGDHMMFVQLQLAAQHAPLQHRHVLAAAAAAAAARGDPSIASPVSSPCRPVSSAARVPPVPTSPSPASPSPITAGSFRSHAASTTCPEQMDCSPTASSSASPGASTTSTPGASPAPRSRKPGAVIESFVNHAPGVFSGTFSGTLHPNCQDSSGRPRRDIGTILQILNDLLSATRHYQGMPPSLAQLRCHAQCSPASPAPDLAPRTTSCEKLTAAPSASLLQGQSQIRMCKPPGDRLRQTENRATRCKVERLQLLLQQKRLRRKARRDARGPYHWSPSRKAGRSDSSSSGGGGSPSEASGLGLDFEDSVWKPEVNPDIKSEFVVA", "text": "FUNCTION: Facilitates ubiquitin-independent proteasomal degradation of polycomb protein CBX4. Plays a role in inhibiting the activity of glucokinase GCK and both glucose-induced and basal insulin secretion. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus Cytoplasm, cytosol Note=Detected in the nucleus and nucleolus with no expression in the cytoplasm (By similarity). However, a later study finds expression in the nucleus and cytoplasm with no expression in the nucleolus (PubMed:24187134)."}
+{"protein": "MAALMESVVGRALKFSSTANFRSIRRGETPTLCIKSFSTIMSPPSKAIVYEEHGSPDSVTRLVNLPPVEVKENDVCVKMIAAPINPSDINRIEGVYPVRPPVPAVGGYEGVGEVYAVGSNVNGFSPGDWVIPSPPSSGTWQTYVVKEESVWHKIDKECPMEYAATITVNPLTALRMLEDFVNLNSGDSVVQNGATSIVGQCVIQLARLRGISTINLIRDRAGSDEAREQLKALGADEVFSESQLNVKNVKSLLGNLPEPALGFNCVGGNAASLVLKYLREGGTMVTYGGMSKKPITVSTTSFIFKDLALRGFWLQSWLSMGKVKECREMIDYLLGLARDGKLKYETELVPFEEFPVALDKALGKLGRQPKQVITF", "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. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
+{"protein": "MQNFEVIIGIEVHTALNTKTKMFSNAATSHKSIPNTLINEIDLALPGTLPTVNQEVVHKGLFLANALHMRTNHQFIAFDRKHYYYLDLPKGYQITQNYFPIGQNGYIQIIDEYNNLKRIRIKQIHLEEDTAKQTNIGNQIYLDYNRAGWPLIEIVSEADLRSAQETVLFLEELRKILLFNDISDAKMEDGSLRVDVNVSIRPQGAKKFGTKVEIKNINSISNVAKAIDYEIRRQLNLILLNQNVEQQTRRFDDNTNTTVFMRSKNDAINYRYIREANIAPIHLSDDYVKKMFLTKSCSINDLRQQLAQKGLVSSAIEQLLSDGPLFKAFKYVDKIVNNPLSVYKWLCLEFIGLINKNTQNIEEITPELLQKIARMILLFDQTLINGKQTKIILEKIYLTNKDPQILIKELGFEQITNENEITKLWHQILAKNQEMLLQYNERPDRVEKFFMGEIMKLTKAQANPTISFNVLKKILQK", "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": "MMPVILLLLLSLAIRCADGKAVQGDSDPSASLLTGDKNHDLPVKRDCTTCAGEECCGRCTCPWGDNCSCIEWGK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin V superfamily."}
+{"protein": "MRIDKNLPNYLTIARIMVIPVIILLFYINNSLARKLGALLFVLASITDFFDGYIARKYNLVTSFGKMFDPIADKLLVGCVTIMLLKKDNVDEIPCLLILAREFLVSGLREFLALVKVSVPVSRLAKLKTFLQMFALSILILGSKGSGIIYLDIVGEIILWIAAFLTIITGYSYFKACKTYF", "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": "MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTEEQPGEENQAVSISFGDPEGYALQDAAIRRARRCPPCPSCLSCPWCPRCLRCPMCKCNPK", "text": "FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MAKNKGLGRGLSSLLGEEVISIESEIVQIINIDKIRPNENQPRKNFEYDKIKELADSILNNGLLQPIIVDNNFQIIAGERRWRACKLAKVLEIPVIIKNLDARESMEIALIENIQRTDLTVMEEARGFKYLIENFNYTAEKLAERLGKSRSHIANLLRLNNLPQSIQDKVNENILSMGQARCLINHEHAEVIADYIINNDLNVRQTEELVRQWYKNEYTKSPNNNNKIGKRFLKDNATDNDLELLVKALSEKFGIKITIENYPLGGKLIFHYKDLEELDLILLKLN", "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": "MKQQYLLDYEATKASKNGMPVCKFDSCIPALQFCKENGIKMRGHVLVWHNQTPEWFFHKDYDVSKPLVDAATMERRLESYIKQVIEFCQKNYPGVVYCWDVVNEAILDDGSWREINNNWYTIMKEKYVEKAFYYARKYAKKDVALFYNDYNVFLPAKREAIYNLAQKLKEKGLIDGLGLQPTVGLNYPELDSDDIDSFKTTLETFAKLGLQIHITELNFEIKGDESNRTPENLKKQADRYYEMMKLLLKEDTDNGGPCNITCVTVFGICDDYPLYKNFKQCMYLWDKNCNPKPCFYSFLQAGLDWKASLLSK", "text": "FUNCTION: Could be a xylanase. SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family."}
+{"protein": "MKTPGVLLLILGLLASSSFAIIRIPLRKFTSIRRTMTEVGGSVEDLILKGPITKYSMQSSPKTTEPVSELLKNYLDAQYYGDIGIGTPPQCFTVVFDTGSSNLWVPSIHCKILDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDQSKARGIKVEKQIFGEATKQPGIVFVAAKFDGILGMGYPHISVNNVLPVFDNLMQQKLVDKNIFSFYLNRDPEGQPGGELMLGGTDSKYYHGELSYLNVTRKAYWQVHMDQLEVGNELTLCKGGCEAIVDTGTSLLVGPVEEVKELQKAIGAVPLIQGEYMIPCEKVSSLPTVYLKLGGKNYELHPDKYILKVSQGGKTICLSGFMGMDIPPPSGPLWILGDVFIGSYYTVFDRDNNRVGFANAVVL", "text": "FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. SUBCELLULAR LOCATION: Lysosome. Melanosome Secreted, extracellular space. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MYTKAVLLAFVGSAAAFNAPMMTVRRDAIATGAAAAVVAPLLRPAGAKMATDSKAPLIELFDERDGCKGPAANKASDVGEPGLCVKVSMQKVAMNAAAAKSVATNYMRK", "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": "MDLEEAEEFKERCSQCAAVSWGLTDEGKYYCTSCHNVTERSQEVINTDLIPNTQIKALNRGLKKKNNSEKGWDWYVCEGFQNILCQQAEALKNLGIGPELKNDVLHNFWKRYLQKSKQAYCKNPVYTTGRKPTVLEDNRSHSDWASEPELLSDVSCPPFLESGAESQSDIHTRKPFPISKASQSETSVCSGSLGGVEYSQRKEKGIVKMTVPQTLAFCYLSLLWQREAITLSDLLRFVEEDHIPYINAFQHFPEQMKLYGRDRGIFGIESWPDYEDIYKKTIEVGTFLDLPRFPDITEDCYLHPNILCMKYLMEVNLPDEMHNLTCHVVKMTGMGEVDFLTFDPIAKMAKTVKYDVQAVAIIVVVLKLLFLLDDNLEWSLSNLAEKHNEKNKKDKPWFDFRKWYQIMKKAFDEKKQKWEEARAKYLWKSEKPLYYSFVDKPVAYKKREMVVNLQKQFSTLVDSTATAGKKSPSSFQFNWTEEDTDRTCFHGHSLQGVLKEKGQSLLTKNSLYWLSTQKFCRCYCTHVTTYEESNYSLSYQFILNLFSFLLRIKTSLLHEEVSLVEKKLFEKKYSVTKKKSRSKKARRH", "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 as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRN7/TAF1B family."}
+{"protein": "MHSYIRPYQHVALRLPSELTKIVRLVPNTVVYLGKYGSFPANTIIGRPFYLTFEIIDVSGENNDNCLRIVPPAELHAETLIADGEGEGDDVEVNEEGIPIRTNREIVDDASTQKMTAEEIEALKKVSTGAGREIIEKLLESHSALDQKTAFSLAKYTLRKRKKFLKRFTVLPVDVSLLTNYMLEGKEAMKTMELRDESIGLIGCWGNVHHGGQSSFEGAVASKPNGRYLVIDETGGLVVAAMAERMGILYPHDQEDEDQELAEGSEENGERQQTNAMAQALARRRHMAASGNSITVIHANKQPSLSLLRYFGYDQDNPDESHPLYKHMKTVSWMQLLDPHADTIYANEPEVIPDETLATFKSNRRSAYYKKRSRWERVRRVVDEARAGNFDGLIVATLMEPASVLKHTVPLLAGSAPVVVYSPTVEPLTELADLYSTPRRTAYITRKREIIAQHSLQQSLQGQSQDNEKKPQEPDFSELDKDFALDPSLLLAPTIETSRVRAWQVLPGRTHPLMSGRGGAEGYIFHAIRVFPSHQNIQAAGNPSRKKRKVAAQQESATPAESGSGVDVEMQS", "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": "MGRTKVVGPAGRYGPRYGVSVRKRVRDILARRYQPHECPFCGSTGTVRRVSVGVWSCRKCGNTWAGAAYTPRSGLAKYFKRYIVRG", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL43 family. Putative zinc-binding subfamily."}
+{"protein": "MNNDNLHDKLTIWRQQQIELKGMLQLIPKFQSLNEIRYVVGLDISFDKSSPKAVSALVIYDLEQRMIIYKDYLCIEKLEEDYVPGFLSFREIKWYLPLLNHIPHQFRIDIILVDGNGVLHPVGFGLACHLGVLLNLPVVGVAKNYLHCVGLTESLDAHRETLKKHVLKKTTDHPILIHSIDQSSEILGAAVWTSSNSKRPVYVSIGNQMNLEQSIQLVQKCSSSHSRVPEPIRQADIYAKFVLSQSKRNKKN", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the endonuclease V family."}
+{"protein": "MLLRTAAASSLSLFNPNAEPSRSVPVLANNASRLVVRAAKGSTNHRALTGVIFEPFEEVKKELDLVPTVPQASLARQKYVDESEAAVNEQINVEYNVSYVYHALFAYFDRDNVALRGLAKFFKESSEEEREHAEKLMEYQNRRGGKVKLQSIVMPLSEFDHADKGDALHAMELALSLEKLTNEKLLHLHSVATKNGDVQLADFVESEFLGEQVESIKRISEYVAQLRRVGKGHGVWHFDQMLLHEGGHLA", "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. SIMILARITY: Belongs to the ferritin family."}
+{"protein": "MAANVGSMSQYWKRFDLQQLQRELDAAATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGRCAELQIHLTEATAKAVEQKELIARLEQDLSTIQSIQRPDAEGASEQGLEKIPEPIKEATALFYGPSMSSSGTLPEGQVDSLLSIISSQRERFRTRNQELEAESRMAQHTIQALQSELDSLRADNIKLFEKIKFLQSYPGRGIGSDDTELRYSSQYEERLDPFSSFSKRERQRKYLGLSPWDKATLGMGRLILSNKTARTIGFFYTLFLHCLVFLVLYKLAWSESVERDCAATCAKKFADHLHKFHESDNGAAAGDLWQ", "text": "FUNCTION: May be involved in intra-Golgi retrograde transport. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type IV membrane protein. SIMILARITY: Belongs to the CASP family."}
+{"protein": "IKCHNTLLPFIYKTCPEGQNLCFKGTLKFPKKTTYNRGCAATCPKSSLLVKYVCCNTNKCN", "text": "FUNCTION: Has low cytotoxic activity. SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Orphan group XV sub-subfamily."}
+{"protein": "MASTMTPYFGIVVSLIAYGIGTFLFKHSKQFFLFTPLFVAMVLGIGFLKVGNFTFEEYNTGGKIISFFLEPATIAFAIPLYKQADKLKKYWWQILSAIIVGSICSVVVVFIVAKAIHLDTAIMNSMLPQAATTAIALPLSESIGGIPAITSFAVIFNAVIVYALGALFLKTFRVKNPIAKGLALGTAGHALGVAVGIEMGEVEAAMASIAVTVVGVVTVVVIPLFMPLIA", "text": "FUNCTION: Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, 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 CidB/LrgB family. LrgB subfamily."}
+{"protein": "MSCSGSGADPEAAPASAASAPGPAPPVSAPAALPSSTAAENKASPAGTAGGPGAGAAAGGTGPLAARAGEPAERRGAAPVSAGGAAPPEGAISNGVYVLPSAANGDVKPVVSSTPLVDFLMQLEDYTPTIPDAVTGYYLNRAGFEASDPRIIRLISLAAQKFISDIANDALQHCKMKGTASGSSRSKSKDRKYTLTMEDLTPALSEYGINVKKPHYFT", "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). 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). TAF10 is also component of the PCAF histone acetylase complex, the TATA-binding protein-free TAF complex (TFTC) and the STAGA transcription coactivator-HAT complex (PubMed:18206972, PubMed:11564863, PubMed:9885574, PubMed:10373431, PubMed:12601814). May regulate cyclin E expression (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF10 family."}
+{"protein": "MGLLRLVFLLSWAASAGGLYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSQEDQFVHLDFQAHGRQFNLRMKKDTSLFSPDFKLEVGGETVNYDTSHIYTGQLFGEQGTLSHGSVVDGKSKGLLKPLKAHSYVEPSERFFKDQAVPFHSVMYHEDDIKYPHKYGSEGGCADSSVFKRMKEYQMSVQEEPEKHDHKEDHEDSGPVILRKKRAAQAEKNTCQLFIQTDHLFYKRYGETREAVIAQISSHVKAIDTIYQSTDFSGIRNISFMVKRIRINVTSDEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICERNKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGNECTPGEAKNLGFKENGNFIMYARTTSGDKLNNNKFSICSVRNISQVLDKKENSCFVESGQPICGNGLVEPGEQCDCGYSDQCKDECCYDANQPENLKCTLKPGKQCSPSQGPCCTTDCTFKRASENCREESDCAKMGTCNGNSAQCPPSEPRENLTECNRATQVCIKGQCSGSICERYDLEECTCGSTDEKDDKELCHVCCMEKMKPHTCASTGSEAWKAYFKGKTITLQPGSPCNEFKGYCDVFMRCRLVDADGPLARLKKAIFNPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQTTQQPSRQRPRENYQMGHMRH", "text": "FUNCTION: Controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MLSVAQSSALFLLQAICILYITKLTIPTPVSEINLVRQSDCVCVPIISRSGTDYITCFNNCQIEPINTKLYNSTCTKMVNITLVRCNNEVYVMTLPNLVSNRSHSWEVLINYLLRFISAIIVYLLLSISKQGIFLFFSIVHYSFKFIKNKKSCNICGNDFYFIHIDCPKPDFTKRSDFHMMFYIILFLSLFFVVTHADDNVYNYYEHGDLTEIQLLDKEHYSQDFVSDGFLYNFYVENSHLIYDISNISTITRPVKHNEVTSTWSCDGSSGCYKDHVGKYNKKPDYVLKKVHDGFSCFFTTATICGTCKSEHIAIGDHVRVINVKPYIHIVVKTANKTDKIVIDEFNKFIHEPYYIKPITQIHIDQHDFLVTGSKVYQGTFCERPSKSCFGPNYITSDKTVTLHEPKIRDTFTHDREYIIDYCDYPSNSDLESLELTDMVHHSDKIYSPYDFGLISIGIPKLGYLAGGFCESLVSVKKIEVYGCYDCQNGVKISVTYESSDSCHTLICKHDSTTHRYFVQQHTTTLNFHSFMSKKDTIIECNQMRKALNLDESSETSVYFESNGVKGSAKEPVNFDFIKNLLYIDYKKIIFVFLVAIISIGIFLRSPYMLLSSILKFRKRRKVVATNRSEQLVMDDDVDVFIGPPS", "text": "FUNCTION: Glycoprotein G2 and glycoprotein G1 interact with each other and are present at the surface of the virion. They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion (By similarity). SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane Host Golgi apparatus membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane Host Golgi apparatus membrane; Multi-pass membrane protein."}
+{"protein": "MARMHARRRGKSSSVRPARNEAPAWSNTDKAAIEKLIVDLRKEGTSASMIGLVLRDRYGVPDVKMVTGKSIGDILTENKVSSEIPEDLRDLMVKALGLRKHLGENPKDLHNKRQLHLVEAKIRRLVKYYIGTRKLPAGFTYKPENAEILLSR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
+{"protein": "MGSTRKGMLNVLIAAVLWGSSGVCAQYIMEQSQMSSQFLTMTRLIFAGLILLTLSFVHGDKIFSIINNHKDAISLLIFSVVGALTVQLTFLLTIEKSNAATATVLQFLSPTIIVAWFSLVRKSRPGILVFCAILTSLVGTFLLVTHGNPTSLSISPAALFWGIASAFAAAFYTTYPSTLIARYGTLPVVGWSMLIGGLILLPFYARQGTNFVVNGSLILAFFYLVVIGTSLTFSLYLKGAQLIGGPKASILSCAEPLSSALLSLLLLGITFTLPDWLGTLLILSSVILISMDSRRRARKINRPARHK", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EamA transporter family."}
+{"protein": "MAHTSDGWGAPYDNQTYVEAYEQLEIALLEPLDRILETANVEEFRPKFKNHQDPNDRKNKKNNDEEWRDSIYNIATDESDTDDHEQRKNFFQPPLQVQRNSFVKNTLMEFKRSSQIDISRLAVMGCGEMSLEKGICEYLGSFGTINVLSVDIDEPSLSIGQQLLGKHLERNAEILAVETGLPVLMRSYVGDILEPDHRFADVDAIVSMEVVEHIPLPNAKKFVENVLGTLMPRIFIFSTPNHEYNAVFGMEPGEFRHGDHKFEMNRKEFSNWLEELSIRFPHYQIDPPHYIGMTRGYENLSGASQAAVCRLQVDLNTTLPQEVTPYEMVGHLPCRLGSRLIAYNLVKEAFLDWLEKIELQEHEPRTDGYSPYWIFNVQNILHHLKAPVSFALTIDEKVAIKYIQGMTSRKVHAEYSHGFNGIVILQMHSKEELIKTVQDNTL", "text": "FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of PIWI-interacting RNAs (piRNAs) and small interfering RNAs (siRNAs) which are classes of regulatory RNAs that are involved in gene silencing in endogenous RNA interference (RNAi) pathways (PubMed:22536158, PubMed:22548001, PubMed:22829772). Methylation protects the 3'-end of small RNAs from tailing and trimming and could constitute a recognition signal for appropriate argonaute machineries (Probable). Methylates and stabilizes 26G-siRNAs (a class of 26 nucleotide siRNAs that possess a monophosphorylated guanine residue at the 5'-end) when they are bound by argonaute protein ergo-1 (PubMed:22536158, PubMed:22548001, PubMed:22829772). This occurs in the female germline and embryo, but not in the male germline (PubMed:22548001). Does not methylate 26G-siRNAs bound by argonaute proteins alg-3 or alg-4 (PubMed:22548001, PubMed:22829772). Methylates and stabilizes 21U-piRNAs, which are a class of 21 nucleotide piRNAs that possess a uracil residue at the 5'-end, in the male and female germline (PubMed:22536158, PubMed:22548001, PubMed:22829772). In addition, may play a role in exogenous RNAi (exoRNAi) pathways in the germline (PubMed:22829772). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Cytoplasmic granule Note=Nucleoplasm localization ceases following fertilization (PubMed:22548001). In embryos, diffusely localized in the cytoplasm (PubMed:22829772). In cells of the P-lineage (germ cell progenitor cells) in embryos, localizes to granules and at later postembryonic stages of development, localizes to perinuclear granules in the germ cells (PubMed:22829772). SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family."}
+{"protein": "MKLLPMDIPRVVIAGTSSKVGKTMISIGLMRLLVNRGYEVQPYKVGPDFIDPGFHHLATGRYSRNLDSFMLSRSAILETFIRNFRGADVAIIEGKTGLYDSSDAVSEKGSVAEVSKILKAPVVLVANVERLNRTAAAIILGYKLFDPDVLLKGVILNRVGSERHAGKVRTAVEKLAGVRVLGVVPRKKVKMPYRHLGLVTAYEREDMDELLDNIAEIVEKHVDVDKILEIAEKAPPLDSVFEDEKEDEEKKYVKIGVIRDQVFSFYYQDNLDELSKYAELVFVNSLTDKRLPDVDALYIGGGFPEVFAEGLEKNEKLRNEIYDFCQSGNPVYAECGGLMYLGESLETSEGEFEMVGFLPLKTKMYERFQAQGYSVYRTLKPCIIAKRNQKIVGHEFHYSRPTLTGKADFAFRVERGFGIDGRRDGILKENTLGCYIHVHFLSDKSIARRFVKKAMKKK", "text": "FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. SIMILARITY: Belongs to the CobB/CbiA family."}
+{"protein": "MTCICIFSIAFLLSFHLTTAQRSTGLQTYIVHVDKPDAQVLANSADLESYYNSFLPATVSGSEVPSRIIHSYHHVATGFAAKLSGEEVKEMEKKAGFVSAKLEKVLTLHTTHTPNFLGLYQNMGFWQESNYGKGVIIGLLDTGITPGHPSFSDVNMPSPPAKWKGKCEFTGNATCNKKIIGARNFISGSGVPPTDEEGHGTHTASTAAGNFVNDANVFGNANGTAVGMAPLAHIAMYKVCSEDGCSDADILAALDAAIDDGVDVLSLSLGGYSDPFYYDNIAIGAFAAIRKGIFVSASAGNDGPLNSTLSNEAPWILTVGASTHDRKIVATAVLGNGQQYDGESAFQPADFPHTLLPLVYPGTSDEEAAFCSSGSLDKFDVKGKVVVCDRGGDVARLEKSQTVKDAGGAAMILANLEIDGEGTFADAHVLPATHVGYAAGEMIKSYINSTSTPTAGILFKGTIIGFKSSPSVSSFSSRGPNLASPGIVKPDIIGPGVNILAAWPVSVENKTGTDLTFNIISGTSMSCPHLSGIVALLKSAHPDWSPAAIKSAIMTSADQSNLEGQPILDERNLPADIFATGAGHVNPSKASDPGLIYDIQLEDYIQYLCGLGYREKDIGLIVQETVKCESSISEAELNYPSFSIILGPKTQNYTRTVTNVGDASSTYTVNIAKTQGVDIVVEPATLVFTKMYQQATYTVSFTQSGDFTDRFVQGAISWSSNEYVVRSPISVKLE", "text": "FUNCTION: Required for arbuscular mycorrhiza (AM) development during AM symbiosis with AM fungi (e.g. Glomeromycota intraradices). SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast Note=Accumulates in the intercellular spaces and the periarbuscular space (PAS) during arbuscular mycorrhizal (AM) symbiosis. SIMILARITY: Belongs to the peptidase S8 family."}
+{"protein": "MGRRSTSSTKSGKFMNPTDQARKEARKRELKKNKKQRMMVRAAVLKMKDPRQIIRDMEKLDEMEFNPVQQPLLNEKVLRDKRKKLRETFERIVRLYERENPETYKELRKLELEYETKRGQLSLYFDSVKNAESVEVDSIPLPEMPHAPSSILIQDIPLPGAQPPSILKKSSALGKASSLSAAALAGVPRLPAGRKPPGPPPGPPPPQILQLYGNTRRTEASAGSDTEMMDGGRDSDSKSEADEESDSQEDSSAEREDSDRGERDEERERADKHTGRSVRFADMPSPNKKKRRVVKTKSITPLQAMMLRMAGQSVPEEEEEDEEEEYSESEDSEAEDQASTDAPQPLVNPRLPVPSAPMAAQQPPSLMQAPPITGPPPLGPPPAPPMRPPGPPSGPPPGPPPGAPPFLRPPGLPSALRGPMPRLLPPGPPPGRPPGPPPGPPPGLPPGPPPRGPPPRLPPPAPPGMPPPPPPPRAGPPRMAPPLSLFPPPLNPNVLSAPPSIVPRQKSPAASSNEGAPSGSALQMPPPPGTTANPLAPTIEKRATVAGSGGASAQGGGATISAKPQIINPKAEVTRFVPTALRVRRDRAGGTGRREEERPPANQQTPAHQAPPIAHAPTPPNLKTKDQVYEAFMREMEGLL", "text": "FUNCTION: Activates pre-mRNA splicing. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MSTQIFASSSQNEKIHKILRPTKKLQPSVWGERFLHYNISEQELRYKQQQVEELKAVVKKEIFGESAYDVSHQLKLINVVERLGLSYHFESEIENELESIYNKSVDQNYILKDENLHDASLRFRLLRQHGFRVSSADIFEKFKDEDGNFKECLVSDTIGLLSLYEASHLSCVGENILDEALDFTTTHLTEFLANKKEHDDPLSKEISQALERPLRKSLERLAARHFISIYANETSHNKVLLQLAKLDFNLLQSIHKKELSEISRWWKESDFVHKFPFARDRIVELYLWILAVYYEPQYYLARNILTKTIALASIADDIYDEYGTIEELELLTEAVERWDINFIDKLNPEYLQTFYKELLNSYEEFEQALSKEETYRVHYAKERFKELLRSSLEVAWWLKEGRVPSFDEYLKISLINCGYHMLIVSSLIGMKGSIVTKEVFEWLSIDRKIVRASVTICRLMDDIAEYKFEQEKNEEPSAVECYMKQYGVSEEEAYDELNKRVVNAWKEINEELLKPTGVASPILVRALNFSKFMDLFYKNGDGYTQVGKVTKHSVAALLIHPIP", "text": "FUNCTION: Sesquiterpene synthase that catalyzes the formation of germacrene A. Can use farnesyl diphosphate as substrate, but not geranyl diphosphate or geranylgeranyl diphosphate. Beta-elemene, the initially measured product in the assay, is derived nonenzymatically from germacrene A. SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily."}
+{"protein": "MKLFVLCIFAMMATLAMSRSWTYVQPKFLNKAFEVALKEEIIVRWDRKLAKWLRVNGGPLSHVQKKALYFVNRRYMQTHWANYMLWINKKTDALGRTPVVGDYRRLGAEIGRRIDMVFFYKFLSGRNMIPKYMPYMEQINRMRAADIPVKYMGK", "text": "FUNCTION: Dissolves the egg vitelline layer nonenzymatically during fertilization. It creates a hole of about 3 mu-m in diameter through which the sperm pass."}
+{"protein": "MSRLPDRSLLTRCEIFVYFGVYIAYIVVGLYKIYGLRDHIVKEAKFQFPEGWSLYPFSQRRRDDSNDELENFGDFIVSFWPFYLLHVAVQGFIRWKRPRLQCLGFIGVCALALSVNLDWSSMVLLVTLIASYYIVSLLSLKFLVWLLSAGWILCINVMQKNVWWTDRVGYTEYVLVIVTMSWSVLRGCSYSLSKIGAKQEDLTRYSLVQYLGYAMYFPCLTYGPIISYQRFAARREDEVQNWLGFVGGVLRSAIWWLVMQCALHYFYIHYMSRDVRMVEMMDSVFWQHSAGYFMGQFFFLYYVVTYGLGIAFAVQDGIPAPNRPRCIGRIHFYSDMWKYFDEGLYEFLFQNIYAELCGKRSSAAAKFGATALTFAFVFVWHGCYTYVLIWSILNFLCLAAEKVFKTFTAMPEYQRWTQRHLGAVGAQRLYAMLATQLFIPAAFSNVYFIGGQEIGDFLMRGAYLSGVGNYVALCFCSYCFFQCSELLLTKSDGRSKTKTF", "text": "FUNCTION: Required in hedgehog (hh) expressing cells for production of appropriate signaling activity in embryos and in the imaginal precursors of adult tissues. Acts within the secretory pathway to catalyze N-terminal palmitoylation of Hh; this lipid modification is required for the embryonic and larval patterning activities of the Hh signal. Not required for Wg signaling. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound acyltransferase family. HHAT subfamily."}
+{"protein": "MELNLEVIQREVIKPSSPAPHDRLQLSVIDFGIAEACVPMIFFYNLADLAEKSPDIVSTRLRSSLSQALSRFYPLAGKKEGVSISCNDEGAVFTEARTNLLLSEFLRNIDINSLKILIPTLAPGESLDSRPLLSVQATFFGSGSGLAVGICVSHCICDAASVSTFVRGWAATARGDSNDELSTPQFAEVAIHPPADISIHGSPFNALSEVREKCVTNRFVFESDKITKLKIVAASKSVPSPTRVEAVMSLIWRCARNASHANLIVPRATMMTQSMDLRLRIPTNVLSPDAIGNLQGVFFLKRGPGSEIEISEVVAEFRKEKEEFNEMIKENVNGGHTNTTLGQKIMSGIANYMSELKPNIDTYTMSSWCRKAFYEVDFGWGRPAWVGLGHQDIQDGVMYVLLVDAKDGEGVEVWVGIPEQDMAAFVCDQELLSYASLNPPVLI", "text": "FUNCTION: Probably involved in the modification of desaturated thalian- diol. SIMILARITY: Belongs to the plant acyltransferase family."}
+{"protein": "MRSLSLFTALLAGQAFAYPKPVLQSSTRRDWPTINEFLTELAEIMPIGDTVSAACDLIGDAEDVAADLFDISNTENDACGDVTVLFARGTCDPGNVGVLVGPWFFNSLETALPNKKVGVKGVPYPASVQGFLSGSVQPGIDMANQIKSVISSCPNTKLVLGGYSQGSMVVHNAASNLDAATMAKVSAVVLFGDPYDGRPVANYDASKVLVVCHDGDNICQGGDFILLPHLTYAEDADTAAAFVKPLVS", "text": "FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18987860). May degrade cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18987860). May also degrade suberin, a specialized macromolecule found in the cell wall of various plant tissues (PubMed:18987860). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family."}
+{"protein": "MEKRSSIKNRGVLRLPPGFRFHPTDEELVVQYLRRKVTGLPLPASVIPETDVCKSDPWDLPGDCESEMYFFSTREAKYPNGNRSNRSTGSGYWKATGLDKQIGKKKLVVGMKKTLVFYKGKPPNGTRTNWVLHEYRLVDSQQDSLYGQNMNWVLCRVFLKKRSNSNSKRKEDEKEEVENEKETETEREREEENKKSTCPIFYDFMRKDTKKKRRRRRCCDLNLTPATCCCCSSSTSSSSVCSSALTHTSSNDNRQEISYRENKFCLFL", "text": "FUNCTION: Transcription activator of the mannan synthase CSLA9. Recognizes and binds to DNA-specific sequence of CSLA9 promoter. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MASPGSGFWSFGSEDGSGDPENPGTARAWCQVAQKFTGGIGNKLCALLYGDSEKPAESGGSVTSRAATRKVACTCDQKPCSCPKGDVNYALLHATDLLPACEGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILTHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMLIARYKMFPEVKEKGMAAVPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEVKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHIDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWFVPPSLRVLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL", "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. SIMILARITY: Belongs to the group II decarboxylase family."}
+{"protein": "MAAASRSASGWALLLLVALWQQRAAGSGVFQLQLQEFINERGVLASGRPCEPGCRTFFRVCLKHFQAVVSPGPCTFGTVSTPVLGTNSFAVRDDSSGGGRNPLQLPFNFTWPGTFSLIIEAWHAPGDDLRPEALPPDALISKIAIQGSLAVGQNWLLDEQTSTLTRLRYSYRVICSDNYYGDNCSRLCKKRNDHFGHYVCQPDGNLSCLPGWTGEYCQQPICLSGCHEQNGYCSKPAECLCRPGWQGRLCNECIPHNGCRHGTCSTPWQCTCDEGWGGLFCDQDLNYCTHHSPCKNGATCSNSGQRSYTCTCRPGYTGVDCELELSECDSNPCRNGGSCKDQEDGYHCLCPPGYYGLHCEHSTLSCADSPCFNGGSCRERNQGANYACECPPNFTGSNCEKKVDRCTSNPCANGGQCLNRGPSRMCRCRPGFTGTYCELHVSDCARNPCAHGGTCHDLENGLMCTCPAGFSGRRCEVRTSIDACASSPCFNRATCYTDLSTDTFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLAVLLVLLGMVAVAVRQLRLRRPDDGSREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKQQNHTLDYNLAPGPLGRGTMPGKFPHSDKSLGEKAPLRLHSEKPECRISAICSPRDSMYQSVCLISEERNECVIATEV", "text": "FUNCTION: Involved in the Notch signaling pathway as Notch ligand (PubMed:11134954). Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting (PubMed:20616313). Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types (By similarity). During spinal cord neurogenesis, inhibits V2a interneuron fate (PubMed:17728344). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MTTFLQRDDFAVTARVLGALFYYSPESHETAPLVQALLNDDWQAQWPLDAEALAPVAVMFKTHSEESLPQAWQRLFIGPYALPSPPWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMQQNEPEDHFGSLLLLAAWLAENGRHHECEQLLAWHLFPWSSRFLDVFIDHAGHPFYQALGQLARLTLAQWQAQLIIPVAVKPLFR", "text": "FUNCTION: Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding- maturation pathway for the substrate protein. SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily."}
+{"protein": "MLSDELESKPELLVQFVQNTSIPLGQGLVESEAKDITCLSLLPVTEASECSRLMLPDDTPNHTNSSKEVPSSAVLRSLQVNVGPDGEETRAQTVQKSPEFLSTPESPSLLQDLQPSDSTSFILLNLTRAGLGSSAEHLVFVQDEADDSGNDFLSSESTDSSIPWFLRVQELAHDSLIAATRAQLAKNAKTSSNGENVHLGSGDGQPKDSGPLPQMEKKLKCTVEGCDRTFVWPAHFKYHLKTHRNDRSFICPAAGCGKSFYVLQRLKVHMRTHNGEKPFVCPESNCGKQFTTAGNLKNHLRIHTGEKPFLCEAQGCGRSFAEYSSLRKHLVVHSGEKPHQCQVCGKTFSQSGSRNVHMRKHHLQMGAAGSQEQEPAAEPLMGSSLLEEASVTSKNLVSMNSQPSLGGESLNLPNTNSILGVDDEVLAEGSPRPLSSVPDVTHHLVTMQSGRQSYELLNQGDLTERRT", "text": "FUNCTION: Transcription factor that binds to the sequence motif 5'- CATCCCATAATA-3', and is specifically required to silence expression of fetal hemoglobin in adult erythroid cells. Prevents expression of fetal hemoglobin genes HBG1 and HBG2 through CHD4: acts as a direct transcriptional activator of CHD4, a central component of the NuRD complex that represses transcription of fetal hemoglobin genes HBG1 and HBG2 in erythroid cells. May also activate transcription of matrix- remodeling genes such as MMP1 during fibroblast senescence. May activate transcription of the gap junction gene GJC1, perhaps in response to increasing glucose. However, recent studies suggest that ZNF410 is dedicated to regulate expression of a single gene: CHD4. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Directly binds to the sequence motif 5'-CATCCCATAATA-3'."}
+{"protein": "MTTVVAFILMFGVLVSIHEWGHLIFAKRAGMLVREFAIGFGPKIFSFTKNETLYTIRLIPAGGYVRVAGEDPEIIELKPGHHIGLEFNQAGEVSKIIVNNKSKHPYARVIEVENVDLDHKLIIEGYELDDDENRLSFNVNEKAMFVMDERETQIAPYNRQFASKSTGKRAMQLFAGPMMNFVLAIAIFLILGIIQGVPVEEAKLGEIQPDTPAEQAGFQQDDVITQIGDQSISTWEEFTSIVRENPGQELDMVIQRNGESQDISVVPGEAEAVNEVGDPITIGQIGVYQGFEKDVLGTFVYGIERTYDTTTMIIQNLFMLVTGQVSIELLSGPVGIYDATDQVVQTGFSNFLLWTAMLSINLGIINLVPLPALDGGRLLFVGLEAVRGKPIAPEKEGIFHFVGFALLMLLMIVVTWNDIQRLFL", "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": "MNSVEAVEKILNYSFVNKTLLKEAITQKSPLFDRLEFFGDSILEVAFTNYICHTYPNLKVKELRDLRTANVSNEKFARIAVNHNLHHFLLLQNPSLFKKVKNFAEAVRKEDDPVPYGGLVKAPKILADTLESIAATVFIDVNYDVKRLWEIFRSLLEPIYTPDDLLLQPKLPFLTLFRLADKHGSESTSGIRKMTTSTKILLRNKDCLDVDLEDVKGKSFEICSTELFSLSTVSENSLTDEMSQEEVVIDEDSPNVEPEDVKGKLFEICYTRKLQIQTGSSGNPLTYEMTTKQMVVDKDSLHVEPVNGRGELIEICTKNKWPRPIFSVQEEKGPKNEPKFVCSVKIEIPNIEGTFHMKGDIKSKKKQAENSLAYHMIRALESSLVSLVISNLQKPKSLDEKNNPLLFSSEMDSSVEAVEKILNYSFVNKTLLKELLTHNNSPLFQGLMFVGESALSLAFTKHLYLTYPMLEPKDLSVLRDANTCHDKYACVAVKKGIYQSFIGSVPKPEKMTTDFIELMGKEDDPYRVVKAPKILVNLLAGVAGAVYIDVKYNVQRLLEIFRVLLEPIYTLDDLRMQLKQPFLMLFRLADKHGKQIDFRYSKDGGSRKNIAQVYMDDMFIASGCAKRIDTAKLLAAEEAIQKLSECMPIEKIIHQDNLDGEVIQTGSSSLLTAFENPLTEEMTQEQMVIDEDSLDVEWKLFETEELQIQTGSSSMSTVSENPLPCEITPTKMVIGEVSPHVELEDVKGKSFEISSTETSSLPIAFENPLTNELTQEQMVIDENSPYVEPVDTKGKLFESCSVESSSLPTTSENPSTYEMTTKQMVVDKDSPHVEPEDEKGKLFEICAKNKWPNPIFSVEEERGQQNEQKIVCSVKIEIPNIEGTFHIKGDAKPTKKEAENSSADHMIRALESSVMSLVITNLQMHENLDGKKKNLQMKESLNENKTLLHSTKRRRRL", "text": "FUNCTION: Ribonuclease that cleaves double-stranded RNA (dsRNA)."}
+{"protein": "MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDEEDVKLLGMSGKRSAPGGGNKVPQKKVKLDEDDEDDDEDDEDDEDDDDDDFDEEETEEKVPVKKSVRDTPAKNAQKSNQNGKDLKPSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL", "text": "FUNCTION: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade. In complex with MYC enhances the transcription of MYC target genes. May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (PubMed:20513429). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Colocalizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. NEK2 is required for its localization to the centrosome during mitosis (By similarity). SIMILARITY: Belongs to the nucleoplasmin family."}
+{"protein": "MMRGLVSGAKMLSSTPSSMATSIATGRRSYSLIPMVIEHSSRGERAYDIFSRLLKERIICINGPINDDTSHVVVAQLLYLESENPSKPIHMYLNSPGGHVTAGLAIYDTMQYIRSPISTICLGQAASMASLLLAAGAKGQRRSLPNATVMIHQPSGGYSGQAKDITIHTKQIVRVWDALNELYVKHTGQPLDVVANNMDRDHFMTPEEAKAFGIIDEVIDERPLELVKDAVGNESKDKSSS", "text": "FUNCTION: Component of the mitochondrial ATP-dependent Clp protease (PubMed:11352464). Cleaves peptides in various proteins in a process that requires ATP hydrolysis (By similarity). Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the peptidase S14 family."}
+{"protein": "MRFKGLDLNLLVALDALMTKRSVTAAARSINLSQPAMSSAIARLRSYFQDELFRMQGRELITTPRAEALAPAIRDALLHIQFSIISWDMFNPAQSDRCFRIILSDFMTLVFFEKVVERVAREAPGVSFELLPPDDNPDELLRRGEVDFLIFPDVFMSSVHPKAKLFDQTLVSVGCLTNEQLLGDLSFERYMSMGHVAAQFGRALKPSVEQWLLLEHGYKRRIELVVPGFNLIPPLLSGTKRIAIIPLRLANHFAKSIPLRIVKHPLPLLSFTEAVQWPALHNKDQASIWMREILLDEAARIAAPRETAGCLGR", "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": "RIRKPIFAFPRF", "text": "FUNCTION: Conorfamide As2a: this amidated form is active on both ASIC channels and nicotinic acetylcholine receptors (nAChRs) (PubMed:31028742). Potentiates ASIC1a (EC(50)=10.9 uM) (PubMed:31028742). Inhibits desensitization of ASIC1a and to a lesser degree ASIC3 currents, resulting in a sustained opening of channels in the presence of low pH (PubMed:31028742). Inhibits with a slow reversibility human alpha-7/CHRNA7 nAChRs (IC(50)=689-3867 nM) and with a rapid reversibility human alpha-1-beta-1-delta-epsilon (CHRNA1- CHRNB1-CHRND-CHRNE) nAChRs (IC(50)=208 nM) (PubMed:31028742). FUNCTION: Conorfamide As2b: this non-amidated form is only weakly active on both ASIC channels and nicotinic acetylcholine receptors (nAChRs) (PubMed:31028742). Shows a very weak inhibition of peak current of rat ASIC1a and ASIC3 (PubMed:31028742). No inhibition or very weak desensitization of both rat ASIC1a and ASIC3 are observed (PubMed:31028742). Reversibly inhibits both human alpha-7/CHRNA7 nAChRs (IC(50)=2971-7036 nM) and human alpha-1-beta-1-delta-epsilon (CHRNA1- CHRNB1-CHRND-CHRNE) nAChRs (IC(50)=707 nM) (PubMed:31028742). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
+{"protein": "MSNDNCTGDIVTHLKNWNFGWNVILTIFIVILQFGHYKYSRLFYGLKMLVLWLLWPLVLALSIFDTWANWDSNWAFVAFSFFMAVSTLVMWVMYFANSFRLFRRARTFWAWNPEVNAITVTTVLGQTYYQPIQQAPTGITVTLLSGVLYVDGHRLASGVQVHNLPEYMTVAVPSTTIIYSRVGRSVNSQNSTGWVFYVRVKHGDFSAVSSPMSNMTENERLLHFF", "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": "MIHSLFLINCSGDIFLEKHWKSVVSQSVCDYFFEAQEKAADVENVPTVISTPHHYLISIYRDKLFFVSVIQTEVPPLFVIEFLHRVADTFQDYFGECSEAAIKDNVVIVYELLEEMLDNGFPLATESNILKELIKPPTILRSVVNSITGSSNVGDTLPTGQLSNIPWRRAGVKYTNNEAYFDVVEEIDAIIDKSGSTVFAEIQGVIDACIKLSGMPDLSLSFMNPRLLDDVSFHPCIRFKRWESERVLSFIPPDGNFRLISYRVSSQNLVAIPVYVKHNISFKENSSCGRFDITIGPKQNMGKTIEGITVTVHMPKVVLNMNLTPTQGSYTFDPVTKVLAWDVGKITPQKLPSLKGLVNLQSGAPKPEENPNLNIQFKIQQLAISGLKVNRLDMYGEKYKPFKGVKYITKAGKFQVRT", "text": "FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals (By similarity). SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. SIMILARITY: Belongs to the adaptor complexes medium subunit family."}
+{"protein": "MSSLAVDDAERRVGDYHPNLWDDALIQSLSTPYGASPYRDVAEKLIGEIKEMFASISIEDGDDEICYFLQRLWMIDNVERLGISRHFENEIKAAMEDVYSRHWSDKGIACGRHSVVADLNSTALAFRTLRLHGYSVCSDVFKIFQDQKGEFACSADQTEGEIKGILNLLRASLIAFPGERILQEAEIFATTYLKEALPKIQGSRLSQEIEYVLEYGWLTDLPRLETRNYIEVLAEEITPYFKKPCMAVEKLLKLAKIEFNLFHSLQQTELKHLSRWWKDSGFAQLTFTRHRHVEFYTLASCIAMEPKHSAFRLGFAKLCYLGIVLDDIYDTYGKMEELELFTAAIKRWDTSTTECLPEYMKGVYMAFYDCVNEMARQAEKTQGWDTLDYARKTWEALIDAFMEEAKWISSGYVPTFQKYLDNGKVSFGYRAATLQPILTLDIPLPLHILQEIDFPSSFNDLASSILRLRGDICGYQAERSRGEQASSISCYMKDNPGSTEEDALSHVNAMIGDKIPEFNWEFMKPSKAPISSKKYAFDILRAFYHLYKYRDGFSIAKIETKKLVMRTVLDPVPM", "text": "FUNCTION: Involved in sesquiterpene (C15) biosynthesis. The major product is alpha-farnesene. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
+{"protein": "MSASLINRSLTNIRTELDFLKGSNVISNDVYDQINKSLPAKWDPANAPRNASPASLEYVEALYQFDPQQDGDLGLKPGDKVQLLEKLSPEWYKGSCNGRTGIFPANYVKPAFSGSNGPSNLPPPPQYKAQELQQIPTQNSAASSYQQQPFPPPSTNYYQQPQQQPQQAPPPQQQQQQQQHQSSHSHLKSFGSKLGNAAIFGAGASIGSDIVNNIF", "text": "FUNCTION: Overproduction promotes the de novo induction of the [PSI+] prion form of SUP35. The prion-inducing effect depends on the association with the actin cytoskeleton. Also implicated in prion maintenance during heat stress. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, actin patch Note=When overexpressed, localizes to punctate structures which are reminiscent of cortical actin patches (PubMed:21777813). Transiently colocalizes with SUP35 aggregates during prionogenesis (PubMed:21777813). SIMILARITY: Belongs to the LSB1 family."}
+{"protein": "MKNKLIIGRYLPINSFVHHLDPRAKLMFVFLFIILIFFCHSPLTYLWVFALILFIMRLAKIQLWFLIKGLTPIFFFLIFTLMMHIFLTKGGYVLVEWHGITIETNGILEGLYISLRLIGIVMIATIMTLSTSPIDLTDAFERLLAPLKMFKLPVHQLSMIMSIALRFIPTLMDELDKIILAQKSRGSEISSGNIATRIKSFIPLLVPLFISAFQRAEELAVAMEVRGYDANVKRTSYRQLKWQLRDTISLTMIIPIAIILFVLKYSGV", "text": "FUNCTION: Transmembrane (T) component of an 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; Multi-pass membrane protein. SIMILARITY: Belongs to the energy-coupling factor EcfT family."}
+{"protein": "MAVTEAENPLLGEITCGTLLQKLQEIWDEVGESDEERDKLLLQIEEECLNVYKKKVELAAKSRAELLQTLSDATVELSNLTTALGEKSYIDIPDKTSGTIKEQLSAIAPALEQLWQQKEERVRAFSDVQSQIQKICEEIAGGLNNGPHVVDETDLSLKRLDDFQRKLQELQKEKSDRLQKVLEFVSTVHDLCAVLRLDFLSTVTEVHPSLDEANGVQTKSISNETLARLAKTVLTLKEDKMQRLKKLQELATQLTDLWNLMDTSDEERELFDHVTSNISASVHEVTASGALALDLIEQAEVEVDRLDQLKSSRMKEIAFKKQSELEEIYARAHIEIKPEVVRERIMSLIDAGNTEPTELLADMDSQIAKAKEEAFSRKEILDRVEKWMSACEEESWLEDYNRDQNRYSASRGAHLNLKRAEKARILVSKITAMVDTLIAKTRAWEEENSMSFEYDGVPLLAMLDEYTMLRQEREDEKRRLKEQKKQQEQPHTDQESAFGSKPSPARPVSAKKPVGTRVNGGGLNETPMRRLSMNSNQNGSKSKRDSLNKIASPSNIVANTKDDAASPVSRADPVMASP", "text": "FUNCTION: Microtubule-associated protein that stabilize microtubules (MT). Involved in the regulation of MT organization and dynamics. Confers MT resistance to the drug propyzamide and cold conditions. SUBCELLULAR LOCATION: Nucleus Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, phragmoplast. Note=During interphase, binds cortical microtubules. In M-phase, locates to the preprophase band. Decorates entire mitotic spindle during cell division. During the anaphase to telophase transition, accumulates in the midline where oppositely oriented phragmoplast MTs overlap. In the phragmoplast, colocalizes completely with the MTs. SIMILARITY: Belongs to the MAP65/ASE1 family."}
+{"protein": "MAARKNQKSPKPKVASSKLKNIKKSSKRNNSQSSTEPRKNATSLDSKKTTKKGVALPEIAERELTQEDIEFFNENPSSLKYLSSINPEDLGKKVEKGPRPDIYDLKKSQQFELDTSRLSSDEESVLDYSKDSEDEQDYELRPRVSSSWNNESYNRLPIKTKDGLLQNVVADVNNGEEFLSESESEASLEIDSDIKDEKQKSLEEQKIAPEIPVKQQIKNDKEALGIQAQQLLEEPVENLHLIRNIFEKFDSPYITIKKLSLLTLLAVFRDIIPGYKIRPLSEEEQGTKLSKEVAQRWEYEQTLLKHYAKFLQTLETILKSFSSTLDETQLSLYQVAVRCCTKLIEQASHFNLSEKLFALAVRQISHKTKRPGFDGIINSLKNIFEEDNLGKTSLKCVTILSRMFKQRNYDVLPDVYDLFLSVNILNDMKIKDEAWQDDTTNFKKRKKDLPYLTKKARKNYKETKKITQEMKEADAVITAQDKEKYQSEILKIIFITYFKTLQLKGKLIGNALEGVARLSHLLNIEFLGDLLQVLRELVMDDTVFLPKDKSGVQATREALLTVSTAFEIASAQGVGKLNLDLDLGLFVQRLYKIIFPFSLNPDADLNLKIKRLKDPDAPSKPFVVNATTEMEMLLKCFQVFFFKSKNISSSRLSSFSKRLAIASMQLPEHSASADLALLKKLLSRYSKLSRLLTSEEQIGDGIYNPFIEDPDLSNSSTAVLYEPFLLKNHYSPAVSQSAKELLKSTSL", "text": "FUNCTION: May be required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the CBF/MAK21 family."}
+{"protein": "MVAERYTVDLNKPLVFQVGHLGEEYQEWIHQPIVCVEGPRFFESDFWEFLTRTVWWAIPTIWLPVVCYVLSISASKGLTFPQIGLIVAFGVLTWTLLEYTLHRFLFHIQTKSYWANTAHYLLHGCHHKHPQDGLRLVFPPTATAILLVPLWKLLHLLATPATAPAILGGILFGYVMYDITHYYLHHGQPKEPTFKHLKKYHLNHHFRIQDKGYGITSSLWDKVFGTLPGIKAAAKKS", "text": "FUNCTION: Fatty acid 2-hydroxylase involved in the alpha-hydroxylation of the long-chain fatty acid (LCFA) palmitic acid. 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": "MEWVWALVVLAALGSAGAERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDEYGQMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIIDTDYDTYAVQYSCRLLNLDGTCADSYSFVFARDPNGFPPEVQRIVRRRQEELCLARQYRLISHNGYCDGKSDRNLL", "text": "FUNCTION: Retinol-binding protein that mediates retinol transport in blood plasma. Delivers retinol from the liver stores to the peripheral tissues. Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MIQYVYLKHMRKLWSLGKVRSTVLRFSTTNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSLCHGIDRSVVGDKYIDDDDLRSFSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELLATVIADLVRGEFLQLKNTMDPSSLEIKQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIKKAKDSLLCLPDSPARKALFALADKVITRKK", "text": "FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MAWSIALLTPPFFGPGRHVQAKEYREPRGCVMKMSSLKAPVLRIQATEYREPRGRVKMMSSLQAPLLTIQSFSGLRAPSALDYLGRPSPGFLVKYKLAKSSGREKASRCVPKAMFERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDSRVEVEKIIGRGSGFVAVEIPFTPRAKRVLELSLEEARQLGHNYIGSEHLLLGLLREGEGVAARVLENLGADPSNIRTQVIRMVGENNEVTASVGGGSSGNSKMPTLEEYGTNLTKLAEEGKLDPVVGRQPQIERVVQILARRTKNNPCLIGEPGVGKTAIAEGLAQRIASGDVPETIEGKTVITLDMGLLVAGTKYRGEFEERLKKLMEEIRQSDEIILFIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTIDEYRKHIEKDPALERRFQPVKVPEPTVEEAIQILQGLRERYEIHHKLRYTDEALVAAAQLSHQYISDRFLPDKAIDLIDEAGSRVRLRHAQLPEEARELEKQLRQITKEKNEAVRSQDFEMAGSHRDREIELKAEIANVLSRGKEVAKAENEAEEGGPTVTESDIQHIVATWTGIPVEKVSSDESSRLLQMEQTLHTRVIGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALAAYYFGSEEAMIRLDMSEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTLVLFDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTLLIMTSNVGSSVIEKGGRRIGFDLDHDEKDSSYNRIKSLVTEELKQYFRPEFLNRLDEMIVFRQLTKLEVKEIADIMLKEVVARLEVKEIELQVTERFKERVVDEGFDPSYGARPLRRAIMRLLEDSMAEKMLSRDIKEGDSVIVDVDAEGSVVVLSGTTGRVGGFAAEEAMEDPIPIL", "text": "FUNCTION: Molecular chaperone (PubMed:15304652, PubMed:21737456, PubMed:24599948). May act as a suppressor of FtsH-mediated thylakoid membrane biogenesis and may enhance photoinhibition (PubMed:15304652). Seems not involved in chloroplastic protein import (PubMed:15304652). Probable component of the TIC-associated stromal import motor involved in inner membrane translocation (PubMed:17376159). Has an ATPase activity, but no ADPase activity (PubMed:21737456). Interacts with transit peptides with a positional preference (PubMed:21737456, PubMed:22545953). Localization of the signal sequence at the N-terminal end of a protein seems mandatory for interaction to take place (PubMed:22545953). SUBCELLULAR LOCATION: Plastid, chloroplast stroma Plastid, chloroplast membrane. SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily."}
+{"protein": "MARPRSLVSPLLSGVFCQCDTVGGAPHTHDTPASPSLAAALAADPCGGLVCGGPEHETRLQILFQELDVNKDGGICINDLAVGLKRLGVHRTELELRKIVKAGDKDQDGQLDFEEFVHYLRDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVNISEQQAEKILKSMDKNGTMTIDWNEWRDYHLLHPAENIPEIILYWKHSTIFDVGENLLVPDEFTVEEKQTGMWWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSNNMSMLGGFTQMIREGGIRSLWRGNGINVIKIAPESAIKFMAYEQMKRIIGSDQETLGIHERLVAGSLAGVIAQSSIYPMEVLKTRMALRKTGQYQGMLDCGKKILLKEGVSAFYKGYVPNMLGIIPYAGIDLAVYETLKNAWLQRYATSSADPGVFVLLACGTISSTCGQLASYPLALVRTRMQAEASVEGAPQMTMSKLFKHIVKTEGAFGLYRGLAPNFMKVIPAVSISYVVYENLKLTLGVQSR", "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": "MYEAQYLWLFGLVLISGSVTERTTPKINFTTVVGLKTTPAMRSSSASSLGGSLPMVINTWNFTDANFLAWRILNVTQGGLRQTRNAVVEGCTRCEQQQCDRTVGYGGSPDELGETTLDAMIMDGSSMDVGAVAGLRGIKDAIRVARHVLEHTKHSMLVGDLASQFAQAMGFRSESLATPESKAMWMEWTAANCQPNFWRNVHPDPSISCGPYKPKATPLTRWKEDRARTEYSIGHLNHDTIGMIAIDAENNIHAGTSSNGARHKIPGRVGDSPIPGAGAYADNEVGAAVATGDGDIMMRFLPTLLAVEAMRAGKKPAEAAEVGIRRISKHYKDFSGAVIAVDRLGQYGAACYGMTEFPFVVSNPSKTDIPSRQESVKCITGKEAVNVV", "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": "MKATSKIMYSMATFLAIMAIIYLFATMHVEDSGYMVGYEWAGGVCMILGTLLTVMLGGYLHFTENRIDVLPEDWEEAEVADAAGTLGFFSPSSIWPLAMSGAIAVLGFGIVYMHYWLIAIGAVLLIYTTTMLNLQYGIPKEKH", "text": "FUNCTION: Part of cytochrome c oxidase, its function is unknown. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase bacterial subunit CtaF family."}
+{"protein": "MDFSRLHMYSPPQCVPENTGYTYALSSSYSSDALDFETEHKLDPVFDSPRMSRRSLRLATTACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGVSHGGTVSLQDAVTRRPPVLDESWIREQTTVDHFWGLDDDGDLKGGNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPVLNWASMHRTQRVDDPQDVFKPTTSRLKQPLQGDSEAFPWHWMSGVEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRDAVGQPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQLLPTVEHLQLELDQLKSELSSWRHVKTGCETVDAVQERVDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQILRNVTHHVSVTKQLPTSEAVVSAVSEAGASGITEAQARAIVNSALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALMSLFGIPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLSPTGNISSAPKDFAVYGLENEYQEEGQLLGQFTYDQDGESLQMFQALKRPDDTAFQIVELRIFSNWGHPEYTCLYRFRVHGEPVK", "text": "FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (PubMed:18039933, PubMed:18396275). The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration (By similarity). Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly (By similarity). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (By similarity). Helps to define the distribution of nuclear pore complexes (NPCs) (By similarity). Required for efficient localization of SYNE4 in the nuclear envelope (By similarity). May be involved in nuclear remodeling during sperm head formation in spermatogenesis (By similarity). May play a role in DNA repair by suppressing non- homologous end joining repair to facilitate the repair of DNA cross- links (PubMed:24375709). SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II membrane protein Note=At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles."}
+{"protein": "MSKEVSEEPEHVRPKDYTDPPPAPLFDVGELRLWSFYRALIAEFIATLLFLYITVATVIGYKVQSSADQCGGVGTLGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLLLARKVSVIRAVMYIVAQCLGGIVGVGIVKGIMKHQYNANGGGANMVASGYSTGTALGAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSIGAAVIYNQKKAWDDHWIFWAGPFIGALAAAAYHQYILRAAAIKALGSFRSNPSN", "text": "FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. 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": "MVGFGANRRAGRLPSFVLVVLLVVIVVLAFNYWSISSRHVLLQEEVAELQGQVQRTEVARGRLEKRNSDLLLLVDTHKKQIDQKEADYGRLSSRLQAKEGLGKRCEDDKVKLQNNISYQMADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQIKELRAQHEENIKKLADQFLQEQKETHKIQSNDGKELGRNDHGAPKNIPNVPENDANKNEDPSSNHLPHGKEQLKRVGDAGMPGVEENDLAKVDELPAALKKPPVLASQHESHQTISHLPTGQPLSPNMAPGSHLNQNENPSTSKQNPSNPLQHIIPGPNLDREPRIQTDTLKQATRDRANDFHKLKQSRFFDENESPVDPQHGSKLADYNGDDGNVGEYEADKQAELAYNEEEDGDGGEEDVQDDEERELQMDPADYGKQRFSDVL", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the GOLM family."}
+{"protein": "MTWCNDRSDVQTVERIIPSPGAAESPVASLPVSCHKTCPSCGHNFKFHEQAGIHDLPGLPAGVKFDPTDQEVLEHLEGKVRDDAKKLHPLIDEFIRTIDGENGICYTHPEKLPGVNKDGTVRHFFHRPSKAYTTGTRKRRKVHTDSDVGGETRWHKTGKTRPVLAGGRVRGYKKILVLYTNYGKQKKPEKTNWVMHQYHLGTSEEEKEGELVVSKVFYQTQPRQCGGSVAAAATAKDRPYLHGLGGGGGRHLHYHLHHNNGNGKSNGSGGTAGAGEYYHNIPAIISFNQTGIQNHLVHDSQPFIP", "text": "FUNCTION: Transcriptional activator that plays a regulatory role in the development of secondary cell wall fibers (PubMed:18952777, PubMed:22133261). Involved in the regulation of cellulose and hemicellulose biosynthetic genes as well as of genes involved in lignin polymerization and signaling (PubMed:22133261). Is not a direct target of SND1 (PubMed:18952777). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MITMPDYRPGMNGIIIGLLSSFGSAILIGCFFLIFYFFRCTTSGRIFLDRIGRPGEYDDEQQFLREEAEALETMDDMQRTEYLRAKAFIAANPPESLQTDISLSQYLAIQEKGVSAWEFEPELEIANCFVEARTEIEFFDSECTVMSNLPVPKQNEVYYWEAKIYDKPENTLISIGMATKPYPLFRLPGFHKYSVAYLSNGTRRYNQPFNATSYGPQVVQGDVIGVGYRPRSGTIFFTRNGKKLEDVVHGLKSQNFFPSIGANGPCIVHVNFGQAGFVFIEANVKKWGLAPMTGSLAPPPPYGSEQGSILLEAGTKDGFTSTLGRGRGYSHPVQTYSRQGLAAVDSSHNRTRSGNFRMFPPTSPGPVRSPTDISLAHLVPTEDAGEPSSSAAALVDQDGQPITGGFLSPDQPPPEYTSPVNSRPGSRRHSSDSENTPLIQLSGRSRGASSATARPIQSGGSHNRPRAGSHRPPSPPIPSYQDAVRQGAGRDRSDSTRSARDSS", "text": "FUNCTION: Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Single-pass type II membrane protein Endosome membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the SSH4 family."}
+{"protein": "MICLVILTCIIMSNSFVNNNNMVQAKMTWTMKAAEEAEAVANINCSEHGRAFLDGIISEGSPKCECNTCYTGPDCSEKIQGCSADVASGDGLFLEEYWKQHKEASAVLVSPWHRMSYFFNPVSNFISFELEKTIKELHEVVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTATPDAPESKVVAHAPFYPVFREQTKYFDKKGYVWAGNAANYVNVSNPEQYIEMVTSPNNPEGLLRHAVIKGCKSIYDMVYYWPHYTPIKYKADEDILLFTMSKFTGHSGSRFGWALIKDESVYNNLLNYMTKNTEGTPRETQLRSLKVLKEIVAMVKTQKGTMRDLNTFGFKKLRERWVNITALLDQSDRFSYQELPQSEYCNYFRRMRPPSPSYAWVNCEWEEDKDCYQTFQNGRINTQSGVGFEASSRYVRLSLIKTQDDFDQLMYYLKDMVKAKRKTPLIKQLFTDETETASRRPFI", "text": "FUNCTION: Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the alliinase family."}
+{"protein": "MDLRHLLFTLALVCANDSLSASDDLLQWPQISKCRSPELETFSCYWTDGKVTTSGTIQLLYMKRSDEDWKECPDYITAGENSCYFNTSYTSIWIPYCVKLANKDEVFDEKCFSVDEIVLPDPPVHLNWTLLNTSQTGIHGDIQVRWDPPPTADVQKGWITLEYELQYKEVNETKWKELEPRLSTVVPLYSLKMGRDYEIRVRSRQRTSEKFGEFSEILYVSFTQAGIEFVHCAEEIEFPWFLVVVFGVCGLAVTAILILLSKQPRLKMLIFPPVPVPKIKGIDPDLLKKGKLDEVNSILASHDNYKTQLYNDDLWVEFIELDIDDSDEKNRVSDTDRLLSDDHLKSHSCLGAKDDDSGRASCYEPDIPETDFSASDTCDAISDIDQFKKVTEKEEDLLCLHRKDDVEALQSLANTDTQQPHTSTQSESRESWPPFADSTDSANPSVQTQLSNQNSLTNTDFYAQVSDITPAGSVVLSPGQKSKVGRAQCESCTEQNFTMDNAYFCEADVKKCIAVISQEEDEPRVQEQSCNEDTYFTTESLTTTGINLGASMAETPSMEMPVPDYTSIHIVHSPQGLVLNATALPVPEKEFNMSCGYVSTDQLNKIMP", "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: 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": "MIRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEDTDTALKFEQLTAYVDELSAPYLEDAEIDFVTDQLGSQLTLKARTPKCAK", "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 (By similarity). SIMILARITY: Belongs to the NfuA family."}
+{"protein": "MATELKEYLVIIPDLPDVLAKRQVLLKPHNQDAAPLVKAGRVPFFGSTLAHHSPEGQQVAENGTVMIIKAESEEEIREIIRKDIFTIEGVWDFGKLSIWPFKIARMRNRRDNSWVVQKFGGTSIGKFPDKTSSDMLCTKFRKESLRNNEQITADCQELLDYTSAAKRFNLDINGKAKDKMVSFGEKLSCRLMVAMLRDRDIPAEYVDLSDIVPSNNLDQLKPEFFHEAAAVFGKRVEACNGRVPVITGFFGTVPGSLIDSGIGRGYSDLCAVLVAIGLHAERVQIWKEVDGIFTADPREVPDARCLPSITPSEAAELTFYGSEVIHHLALSLAIQAKPPVSIFVKNVQKPWGQGTVVVPSDGDDTSSWPIDYLDPSDSDSTSSTALPKMPTAVTIKRDITIFNILSNKQSMSHGFFVKVFTILAEHDISVDLISTSEVHVSMAINSSNMEPSQIKNVQCRLSEEGEVNVLPDMAILSLVGAELKNMTGIAGRMFAILGEQHVNIEMISQGASEINISCVIPDKDATRALNMLHDELFTKSAI", "text": "FUNCTION: Aspartate kinase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O- acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity). SIMILARITY: Belongs to the aspartokinase family."}
+{"protein": "PILAAVLQQSSGNVDFDSESPRKPEIQNEIVDLHNSLRRSVNPTASNMLRMEWYPEAADNAERWAYRCIESHSSYESRVIEGIKCGENIYMSPYPMKWTDIIHAWHDEYKDFKYGVGADPPNAVTGHYTQIVWYKSYRIGCAAAYCPSSPYSYFFVCQYCPAGNFIGKTATPYTSGTPCGDCPSDCDNGLCTNPCTRENKFTNCNTMVQQSSCQDNYMKTNCPASCFCQNKII", "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": "MILKRVTEALEAYKNGEMLIVMDDEDRENEGDLVLAGIFSTPEKINFMATHARGLICVSLTKDLAKKFELPPMVSVNDSNHETAFTVSIDAKEARTGISAFERHLTIELLCKDTTKPSDFVRPGHIFPLIAKDGGVLARTGHTEASVDLCKLAGLKPVSVICEIMKEDGSMARRGDKFLSDFALKHNLKTLYVSDLISYRLENESLLKMFCQEEREFLKHQTQCYTFLDHQQKNHYAFKFKGAKTHDLAPLVRFHPIKEDFDFLTTDAFEVFFKALEYLKHEGGYLIFMNTHSKENNVVKDFGIGALVLKNLGIKDFRLLSSCEDRQYKALSGFGLKLVETISL", "text": "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": "MDTCFFCGAVDLSDTGSSSSMRYETLSAKVPSSQKTVSLVLTHLANCIQTQLDLKPGARLCPRCFQELSDYDTIMVNLMTTQKRLTTQLKGALKSEFEVPESGEDILVEEVEIPQSDVETDADAEADALFVELVKDQEESDTEIKREFVDEEEEEDDDDDDEFICEDVDVGDSEALYGKSSDGEDRPTKKRVKQECTTCGKVYNSWYQLQKHISEEHSKQPNHICPICGVIRRDEEYLELHMNLHEGKTEKQCRYCPKSFSRPVNTLRHMRMHWDKKKYQCEKCGLRFSQDNLLYNHRLRHEAEENPIICSICNVSFKSRKTFNHHTLIHKENRPRHYCSVCPKSFTERYTLKMHMKTHEGDVVYGVREEAPADEQQVVEELHVDVDESEAAVTVIMSDNDENSGFCLICNTNFENKKELEHHLQFDHDVVLK", "text": "FUNCTION: Transcriptional activator that controls bicoid gene expression during oogenesis. Found in transcriptionally active cells. Binds to specific sites on polytene chromosomes of third instar larvae. Binds to the consensus DNA sequence 5'-YTAGAGATGGRAA-3'. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MEQRGRASQDEEQAIVGAETGSQPSLPVSPMRPIIAPSPAMVLPTPGHGMGIPQFGPVGLPAQASTPMLSSTPGPSYSSAPTPMPNPSAANLWPTYKLVAEIPNAHKKSISGIKFSPDGRYMGSGSADCSIKIWRMDFVYEKTLMGHRLGINEFSWSSDSKLIVSCSDDKLVKVFDVSSGRCVKTLKGHTNYVFCCCFNPSGTLIASGSFDETIRIWCARNGNTIFSIPGHEDPVSSVCFNRDGAYLASGSYDGIVRIWDSTTGTCVKTLIDEEHPPITHVKFSPNGKYILASNLNNTLKLWDYQKLRVLKEYTGHENSKYCVAANFSVTGGKWIVSGSEDHKVYIWNLQTREILQTLDGHNTAVMCTDCHPGQNIIASAALEPDMRIKIWRSQS", "text": "FUNCTION: Sex determining protein required in the germline to promote the spermatogenesis to oogenesis switch during the late larval stages of development. Acts with the sex determining factor tra-1, and redundantly with wdr-5.1, to regulate fog-3 expression, which in turn determines germ cell fate. Not required for methylation of histone H3 'Lys-4'."}
+{"protein": "MELIILVGIAIALLVVIITLYLLQKKNAAPETKPAAAPQRGVPQRAQEGVPRRAQIARNQRNRLRQNAPAAPAGQVAPAAGAPAARGDSDHEDEGQVDADDARVPQGAVLDEKMGAKKRAKMEAKEQKRLQREQELHDREQRKVKEAKEEAERKQQEDLEAEVERKRVEAERLAKEERERKEHEEYLKMKAAFSVEEEGFEEGDADEQDSLLAGFIQYIRDNKVVVLEDLAVAFKLKTQQVIDRIQELQADGTLTGVIDDRGKFIYVSEEELSAVAKFIKQRGRVSITELAESSNNLINLTPISAGGEEASS", "text": "FUNCTION: Substrate adapter for ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins. SIMILARITY: Belongs to the DDRGK1 family."}
+{"protein": "MQPSLIPSLLETAAARNGDGRVILYSQGNREDPRSITYRDLLETASKASVAVHNHQNYTPGAAVLLHFNNHLDNIVWFWAVLLAGCIPAITPAFSNNPVQRVANLEHLSSTLITDWCLTSQALLVEFAGQDAIEPVSVETLGWEKASPDSNTASVKAKPTDTALLLFTSGSTGKSKAVCLSHFQIVSAIAGKLSVVPLPEQSSFLNWVGLDHVAAIIEIHLQALYADLDQVHVPGSDVISDPIWFLDLMATHRVSRTFAPNFFLARIRDALVQNARSASPRQWDLSGLRYVASGGEANTTKTCDELSQLLKSFGAPLNVIVPGFGMTETCAGAIFNTNCPDYDKKHGLEYTSVGSCMPGIFMRVTNQQGDPLPPGEMGSLELAGPVVFRQYLNNPAATQESFTMDGWFKTGDCGTLDENGYLVLGGRAKETIIINGVKYSPHEIETAVEEHNIKGLSRSFTCCFSSLSPGAETEEIVLVYLPTYAPEDIPARAATADAISKVVLMSTGSRPHIIPLEQALLPKSTLGKLSRSKIKAAYERGEYRTHDSINRSLIARHRQATRASPKNDFEKGLLEIFLRSFKISEDEFDVQTPIFDVGIDSIELINLKRDIEQHLGFADATIPIIILLENTTVRELAAALDNLYRPKEYNPVVTLQAHGDKNPLWLVHPGAGEVLIFINLAKFITDRPVYALRARGFDEGEKPFDSIEDAVTSYYNGVKSKQPHGPYALAGYCYGSMLAFEVAKKLEENGDEVRFVGSFNLPPHIKMRMRELDWKECLLHLAYFLDLITQKRSRELAVELDGLDQDTILQAIIDEADKERYAQLSLSRPFLSRWADVAYELHRIAGDYDPDGRVASMDVFFSIPLAIAAASKSEWRNVHLSQWDDFTRSHVRFHDVPGEHYSMIGPEHVFAFQKILRSALAERGM", "text": "FUNCTION: Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of Asp-melanin, a pigment that confers resistance against UV light and hampers phagocytosis by soil amoeba (PubMed:29305695, PubMed:23841722, PubMed:27133313, PubMed:29270299). The nonribosomal peptide synthase melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (PubMed:29305695, PubMed:27133313, PubMed:29270299). The tyrosinase tyrP then performs hydroxylations of both aromatic moieties of aspulvinone E (PubMed:27133313, PubMed:29305695). The product of tyrP is highly unstable, and, due to the high reactivity of methides and ortho-diquinones, the polymeric Asp-melanin forms spontaneously (PubMed:27133313). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NRP synthetase family."}
+{"protein": "MGCVQCKDKEATKLTDERDGSLTQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHATGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFEALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSEKADGLCFNLTVIATNNTPQTVGLAKDAWEVARDSLFLEQKLGQGCFAEVWRGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSRRPIYIVTEYMSKGSLLIFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGDNL", "text": "FUNCTION: Tyrosine-protein kinase implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Role in CNTN1-mediated signaling. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane Perikaryon Note=Present and active in lipid rafts (By similarity). Palmitoylation is crucial for proper trafficking (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily."}
+{"protein": "MPISTKSSFYLPAVDISPYLQDPNSDAARKVIDDVRAACTSTGFFQLLGHGISPALQQSVFAAAAKFFALPSDVKSRCRNVGFRGYDPMASQSYELGVLPDLKEGFIAGKDIPLDDPRVASQRFFMGQNAWPPSELLPEANFRRPIEEYYQAMLKLCWVVLDLVAATLPYGPHVFDEFKENDPACPLRLLHYPPAPAPDVAKGRQLGSSAHTDFGAITLLLQDDHSGLEVQDCETGEWIGVPPNKDAYVVNLGDMMSRITRGHYKSSIHRVINQNLTDRYSVVFFFDGNLDYRLRPLDRVGQNWDEEDTLTVEEHMLERTTTTYNLKVK", "text": "FUNCTION: 2-oxoglutarate-dependent dioxygenase; 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:17586673, PubMed:19012408, PubMed:28238725, PubMed:19111642, PubMed:27913218). 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). 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). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
+{"protein": "MSDWDKPTVIGFRQQKPTVAKGSTLNAAQRAGLVISSESKGAGQSKGPADHQRIAKLDRDDAPKPPEKVSADVGKAVATARMAIKNAEGKSMTQKELATSVNAKPQDIADLESGRAVPDQALLGKLERKLNVKLRGAKNLIGTPLHPKKK", "text": "FUNCTION: Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters. Involved in induction of the ribosome quality control (RQC) pathway; a pathway that degrades nascent peptide chains during problematic translation. Required to prevent stalled ribosomes from frameshifting. SIMILARITY: Belongs to the MBF1 family."}
+{"protein": "MSSTRSPLKTKNENTISTKMNNMSFVDKENTPPSLSSTRILASKTARKIFDESEGQSKAKKGAVEEEPLLKENPHRFVIFPIQYHDIWQMYKKAEASFWTAEEVDLSKDLQHWDSLKDEERYFISHVLAFFAASDGIVNENLVERFTQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDSKEREFLFNAIETMPCVKKKADWALNWIGDKNARYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLINKPSEETVKKIIMNAVEIEQEFLTDALPVKLIGMNCDLMKQYIEFVADRLLLELGFDKVYRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSGTTDNTFTLDADF", "text": "FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small chain family."}
+{"protein": "MFLEAVYHRPRKNWSYAYNGTTVHLRIRTKKDDMTAVYALAGDKYMWDHTMEYVPMTKLATDELFDYWECEVTPPYRRVKYGFLLQQGHEKRWMTEYDFLTEPPRNPDRLFEYPFINPVDVFQPPAWVKDAIFYQIFPERFANGDTRNDPEGTLPWGSADPTPSCFFGGDLQGVIDHLDHLSKLGVNAVYFTPLFKATTNHKYDTEDYFQIDPQFGDKDTLKKLVDLCHERGIRVLLDAVFNHSGRTFPPFVDVLKNGEKSKYKDWFHIRSLPLEVVDGIPTYDTFAFEPLMPKLNTEHPDVKEYLLKAAEYWIRETGIDGWRLDVANEVSHQFWREFRRVVKQANPDAYILGEVWHESSIWLEGDQFDAVMNYPFTNAVLDFFIHQIADAEKFSFMLGKQLAGYPRQASEVMFNLLDSHDTARLLTQADGDKRKMKLAVLFQFTYFGTPCIYYGDEVGLDGGHDPGCRKCMEWDETKHDKDLFAFYQTVIRLRQAHAALRTGTFKFLTAEKNSRQIAYLREDDQDTILVVMNNDKAGHTLRCLSGMHSGPICGTTMS", "text": "FUNCTION: Hydrolyzes alpha-, beta- and gamma-cyclodextrins and the resulting linear maltodextrins, with the highest activity with beta- cyclodextrin (cyclomaltoheptaose). Soluble starch is hydrolyzed slowly, but it is nevertheless preferred over pullulan as a substrate. Is able to hydrolyze amylose and amylopectin, with a very strong preference for amylose, with maltose and glucose as the main products (PubMed:9606956, PubMed:10620329, PubMed:16536613). Maltose and glucose are the main hydrolysis products of cyclomaltodextrins, maltodextrins and starch, whereas panose is the main hydrolysis product of pullulan. Acarbose is partially hydrolyzed to glucose and pseudotrisaccharide. No activity with maltose as substrate (PubMed:9606956, PubMed:10620329). Has transglycosylating activity with high concentrations of maltotriose, maltotetraose and starch (PubMed:9606956). SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MSSSLPRSLLRLGHRKPLFPRYNTFVNSSVITHTSLLRTRLYSNGTGATSGKKDDKTRNKPKPLWPQVKSASTFTFSGILVIGAVGISAIVIYLILSELFSPSGDTQLFNRAVSMVEKNKDIRSLLQCDDGITGKERLKAYGELITNDKWTRNRPIVSTKKLDKEGRTHHYMRFHVESKKKIALVHLEAKESKQNYQPDFINMYVDVPGEKRYYLIKPKLHPVSNSKGFLGIRWGPRKD", "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 keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix. In the complex, it acts as an antagonist of TIM50 by reducing preprotein accumulation at the TOM23 complex and promotes dissociation of the PAM complex from the TIM23 complex. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM21 family."}
+{"protein": "MTKEEVEEEPLSPMARLFQSPGIENCIITMIGFKAKINPDIILDDLKHNVSKHPRFCSKLVIATHTNYDGERWMKTKVNVEDHVFVPDIDLQEINKDGDGFVDDYVSRLTLSPLDKSKPLWDIHILNVKTSDAEAVGVMRCHHSLADGMSLMSLLVACTRKTSNLESFPTIPAIKRREQMMSHRFGNKGWYSRSINAVYYAVRLIWNTIVDLLLLWATSLFFKDTETPISEGIGSGNNARRFYHRTVSLDDIKLIKNAMKMTINDVLLGVTQDALSRYLNQRYGDKNGEGVTTTSNLNNLPGKIRIRAGVAVNLRQDIGIQPLEDMLAKDSKCRWGNYDSLVFVPFSISLETDPLVPLLKAKSIMDRKKHSLVAPMHYSIIEFIINTFGTKVFNRTCSNTTTILSNIVGPVEEVSLHGNCITYIALTGYGHSQALMIHFISYANKMIITIAVDPAVIPDPHNICDEMEKSLKAMKDTLSGKSD", "text": "FUNCTION: Bifunctional wax ester synthase/diacylglycerol acyltransferase (By similarity). Involved in cuticular wax biosynthesis (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the long-chain O- acyltransferase family."}
+{"protein": "MSEAKSGPEYASFFAVMGASAAMVFSALGAAYGTAKSGTGIAAMSVMRPEMIMKSIIPVVMAGIIAIYGLVVAVLIANSLNDGISLYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK", "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: 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": "MKKNVQIKGTKDGISIFLSDKASISELQQELTQLLADQKQNPYSGEKLEVQVQIGNRLFSEEEELEISTIIHENSQMEISAFYSNVMSKDEAKKWKENDQIFSMATIIRSGQVVQVPGDFLLIGDVNPGGQIRSNGNVFVLGNIKGIIHAGFEGNENAVVAGKFLYPSQVRIADKVYGFDSEDYKEVTETDLFSAFVNDAGEIVIDGIHKIRKIRPEISNFQGGR", "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 (By similarity). SIMILARITY: Belongs to the MinC family."}
+{"protein": "MALGAAPAAQLALLALLGTLLPGPGGAGISIHPSKAIIPRGDSLTVNCSNSCDQKSTFGLETVLIKEEVGRGDNWKVFQLRDVQEDIELFCYSNCHKEQTIASMNLTVYWFPEHVELAPLPLWQPVGEELNLSCLVSGGAPRAHLSVVLLRGEEELGRQPVGKGEPAKVMFTVQSRREDHGTNFSCRWELDLRSQGLELFQNTSAPRKLQTYVLPSIDPHLEVPPIVEVGSRWPVNCTLDGLFPASDAKVYLVLGDQKLESNITYDGDSVLAKAWMEENEEGTHSLKCSVTLGEVSRRTQENVTVYSFPLPTLTLSPPEVSEWTTVTVECVTRDGAVVKLNGTSAVPPGPRAQLKLNASASDHRSNFSCSAALEIAGQVVHKHQTLELHVLYGPRLDQRDCPGNWTWQEGSEQTLKCEAQGNPIPKLNCSRKGDGASLPIGDLRPVRREVAGTYLCRATSARGRVTREVVLNVLHGQNILDIVIPVVAVTLILGALGTAGYVYNYQRKIQKYELQKARKAQEEAALKLNAQSTPP", "text": "FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family."}
+{"protein": "MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMTESVHTWQDHGYLATYINKNGSFANLRIYPHGLVLLDLQSYDGDAQGKEVDSLLNKVEERMKELSQDSTERVKRLPPIVRGGAIDRYWPTADGRLVEYDIDKVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYSGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVLDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDLSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVWKKAKP", "text": "FUNCTION: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM). SIMILARITY: Belongs to the spermidine/spermine synthase family."}
+{"protein": "MQDSMDDSLREAEGRQDDSEVSSGTTLGSSTPEDSGVTAKLRKKYQMASALLRRELEELSVYDAKTAGVSGRSSGSGSGGLALLGGRFHVAPLRIPARRRLQTLVVAWHTSSFIYMTVLVLFLAANPLMWWFMVPYMVYYVWNRSPANGGVVRRYSPRLRSLALWRYYCEYYPISLHKSEDLAPTFVPDPRGAEPREWKLRLWLWPTRVELLNLTLQWTRARPQVATGPRYIFGYHPHGVGALGAFGAIATEGCNWSKVFAGIPACLCTLVNQFQIPIYRDYLLGLGCTSVARKNVLKVLEQNYSVCIVVGGAQEALLSRVGSTELVLNKRKGFIKLALETGNVNLVPIYAFGETDCFNVLDTGNESYLRKFQLWIKKTYGFTIPFFFARGVFNYDFGFLPFRNPINVVVGKPVYVDKRRTNPTMEEIDHYHDLYVQELRNVFDKNKHKFGYAGKELKIVE", "text": "FUNCTION: Catalyzes the terminal and only committed step in triacylglycerol (TAG) synthesis by using diacylglycerol (DAG) and fatty acyl-CoA as substrates. Required for storage lipid synthesis. Major DAG esterifying enzyme in stationary phase when TAG production is particularly active. Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains. SUBCELLULAR LOCATION: Lipid droplet Endoplasmic reticulum membrane; Multi- pass membrane protein Note=Localizes to sites of lipid droplet biogenesis in the endoplasmic reticulum. SIMILARITY: Belongs to the diacylglycerol acyltransferase family."}
+{"protein": "MVLEDRKDGSSLPGRSGSFSKSSPSELDVVDPYKRISSPGSILDAEKVEKKPGGWRAVSFILGNETLERLGSIGLLANFMVYLTKVFHLEQVDAANVINIWSGFTNLTPLVGAYISDTYVGRFKTIAFASFATLLGLITITLTASFPQLHPASCNSQDPLSCGGPNKLQIGVLLLGLCFLSVGSGGIRPCSIPFGVDQFDQRTEEGVKGVASFFNWYYMTFTVVLIITQTVVVYIQDQVSWIIGFSIPTGLMALAVVMFFAGMKRYVYVKPEGSIFSGIAQVIVAARKKRKLKLPAEDDGTVTYYDPAIKSSVLSKLHRSNQFRCLDKAAVVIEGDLTPEGPPADKWRLCSVQEVEEVKCLIRIVPIWSAGIISLAAMTTQGTFTVSQALKMDRNLGPKFEIPAGSLSVISLLTIGIFLPFYDRVFVPFMRRITGHKSGITLLQRIGTGIVFAIFSMIVAGIVERMRRIRSINAGDPTGMTPMSVFWLSPQLILMGLCEAFNIIGQIEFFNSQFPEHMRSIANSLFSLSFAGSSYLSSFLVTVVHKFSGGHDRPDWLNKNLNAGKLDYFYYLIAVLGVVNLVYFWYCARGYRYKVGLPIEDFEEDKSSDDVEMTSKKSMK", "text": "FUNCTION: Low-affinity proton-dependent nitrate transporter. Not involved in dipeptides transport, but has a weak glucosinolate transport activity. Involved in phloem loading and nitrate remobilization from the older leaves to other tissues. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes at the plasma membrane, where it interacts with NLA. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family."}
+{"protein": "MQIPRSVGTHDGSFHADEVTACALLIMFDLVDKDKIIRTRDSEKLAQCEYVCDVGGRYSIADKRFDHHQVSYTGSWSSAGMVLDYLHHLGSLPHEEYEYLNSTLVHGVDEQDNGRFFSKEGFCSFSDIIKIYNPLEEGGNTDKEFFFALHFAIDLLTRLREKFRYDRICRDVVKQVMEKEDVCLRFDRPLAWQENFFSLGGENHPAAFVSFPCSDQWILRGIPPTLDRRMEVRIPFPEDWAGLLGDQLVKATGIPGAIFCHKGLFLSVWDSRESCEEALNLVLKQQGVV", "text": "SIMILARITY: Belongs to the MYG1 family."}
+{"protein": "MSSSIFGPLTGFLERVNSLNAPYQALSYDEQKAMTIWQRVKFYNWTFELCALGVLFLVYAFYKFGNSVNLKRGNQIFQSLHSFLANDLKFSRVGFNINDSKIFTVEHQNTWFSSFATGRSAIKSINLNLHLVARSNPFSMCLEYLLGFFFASLKSKQLEEFMEIVIRPNGILVTSESAHPNKNAHEILTKFRFVTSIVNKEFMNQARTENYFLSIAHTSENDKLPNNFVYMSDVNQLSGFMFHYSKPYEVLSQAGNLLKYISFTDLPVNPPRDDKEWESSIEPKAIIRCAVPQNENELKLLNQIISLVVEIYDGFTQDLVQQSPNLFITNDILKRTTNLRQQELNKIKKFMKETELELAKEKKLELEKAKRRQLKASGQQEKVDQKMKEKRERRLKNKQRTRFQ", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0674 family."}
+{"protein": "MSFLKNQLSRLLALILVVAIGLTACDSGTGLTGNYSQDTLTVIATLREAIDLPQDAPNRQEVQDTARGQINDYISRYRRKGDAGGLKSFTTMQTALNSLAGYYTSYGARPIPEKLKKRLQLEFTQAERSIERGV", "text": "FUNCTION: Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Photosystem II (PSII) complexes containing this protein are monomeric, are assembly intermediates lacking the calcium-manganese-oxide cluster and miss some of the lumenal subunits. Probably blocks binding of some of the small lumenal subunits. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Lipid-anchor; Lumenal side Note=Associated with PSII on the lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the Psb27 family."}
+{"protein": "MTKEYATLAGGCFWCMVKPFTSYPGIKSVVSGYSGGHVDNPTYEQVCTNKTGHVEAVQITFDPEVTSFENILDIYFKTFDPTDDQGQFFDRGESYQPVIFYHDEHQKKAAEFKKQQLNEQGIFKKPVITPIKPYKNFYPAEDYHQDYYKKNPVHYYQYQRGSGRKAFIESHWGNQNA", "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": "MNLSAKTVVLIAIGAALYGIGGLPMFGIPVFANTTLKPAMAVLALFSVLFGPLVGFLVGFIGHWVTDMFAGWGVWLTWVLGSGLVGLIIGFYPKITRGRLEMGKFTKCDFALFVFLAFLGNVIGYGCSAYLDSVLYAEPFTKVVAQLIIIAAGNTLLIAIVGHYILTAVAKRKQQSYNLKEAD", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0397 family."}
+{"protein": "MSRRVRQRVEDNGKYKVDSPSYTVIGVEDLAPKVQQYVNWTSLPYDTVFHLFTRLNYRDRASLASTCRTWRSLGASSFLWSSLDLRAHKFDLSMAASLATRCVDLQKIRFRGVDSADAIIHLKARSLLEISGDYCRKITDATLSMIAARHEALESLQLGPDFCERITSDAIRVIAFCCPKLKKLRVSGMRDVSSEAIESLAKHCPQLSDLGFLDCLNINEEALGKVVSLRYLSVAGTSNIKWKVALENWEKLPKLIGLDVSRTTIDHIAVSRLLKSSQSLKVLCALNCPYLEEDKSYSSNRFKGKVLLAVFTDTFDELASIFADNSKKPKNIFSYWRDLIRKDKSIDEIMLWIEWIISHTLLRIAESSNSQGLNDFWLNQGATLLLSLMQSAQEDVQERAATGLATFIVVDDENASIDCGRAEAVMRDGGIRLLLELAKSWREGLQSEAAKAIANLSVNAKVAKAVAEEGGISVLADLAKSMNRLVAEEAAGGLWNLSVGEEHKNAIAQAGGVNALVDLIFRWPHGCDGVLERAAGALANLAADDKCSMEVARAGGVHALVMLARNCKYEGAQEQAARALANLAAHGDSNGNNAAVGQEAGALEALVQLTQSPHEGVKQEAAGALWNLAFDDKNRESIAAFGGVEALVALAKSSSNASTGLQERVAGALWGLSVSEANSIAIGHEGGIPPLIALVRSEAEDVHETAAGALWNLSFNPGNALRIVEEGGVVALVQLCSSSVSKMARFMAALALAYMFDGRMDEYAMIGTSLESTSKSVTLNGARTMALDQIKAFIKTFMEHQIFSTGALSSAPSMLAQVSERARIPEAGHLRCSGSEIGRFVTMLRNPCLVLRACAAFALLQFTIPESRHAMHHASLMQNAGEARGLRSAAAAASMPREAKIFMKIVLRNLEHQQAESPEGMKVSYNRI", "text": "FUNCTION: Promotes lateral root initiation and development, independently of auxin (IAA) and abscisis acid (ABA). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the beta-catenin family."}
+{"protein": "MEPNPSDPVLTDRIQAIVTTEKSIDEMMKCAREIIQDLGKEKQIGKNKMEDNANNFKKLITQVENELSAQMQYLSHVCVGSSHQGSTFGVLQNSLLAQSGLSSLHSELFQIVRYLDPTSDEPQTTEEDEEDGSDDLNEDGADGAPSSTVTSSTTDGSGGGDDAASSSAPRSQEESGRQMTDDDDDMEQ", "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 11 family."}
+{"protein": "MGVLLPIFFGVLLLFTVTPPSMSQLPPTIMVPAPAPAPISPSDLCNGIFLSYDFILGRKIPPNDTADQPYRFESVLTVLNNGREELKEWRVFVGFQHNEILISATDALIVNGTELPALVGNGTIFGGYPVSDLKTAIQTAGDLKQMTAEIELVGTQFMVAPPAVPLPSNISLVNEGWLCPVPTLQSKRELTTCCIRDASIIVNTTITTKFLPRQPGDLTIMYDVIRAYDQNYLTEVTMENHNPLGRLDHWELSFDWMRDEFIQKMQGAYPTVVDATKCIFGPQSLIYTGLDFADVLTCERRPIIIDLPPTKKDDSTLGNIPSCCRNGTILPRIMDPSKSVSVFTMQVAKMPPDFNRSALFPPQNWRIKGTLNPDYSCGPPVRVTPTFYPDPSGMPTNKSSFASWQIVCNITQAKTEIPKCCVSFSAFFNDSIIPCNTCACGCVSETRRTCSAETPSLLIPPDALLLPFENRTALTLAWNALKHKTLPNPMPCGDNCGVSINWHMASDYRGGWTVRITIFNWGEIDFPNWFLAVQMKKPALLGFEKAYSFNASLLSVDGGVNNTIFMEGLPGLDYLVAEADEKDPKKKNIRIPGKQQSVIQFSKKLTPGINVAERDGFPAKVIFNGEECLLPDLLPMASGGRRNGAITVLSFITFYVAAFMVLL", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the COBRA family."}
+{"protein": "VFFAGP", "text": "FUNCTION: Cyclic hexapeptide that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:8441706). Cycloaminide B is non-toxic to mammals but shows immunosuppressive activity, probably through the inhibition of the action of interleukin-1 and interleukin-2 (PubMed:8441706). SIMILARITY: Belongs to the MSDIN fungal toxin family."}
+{"protein": "MRTWACLLLLGCGYLAHVLAEEPGIPRDVLDRLARSQIHSIRDLQRLLEIDSVGAEDAPEPSLRAPGVHTARHVAEKPPAPVPVRRKRTIEEAIPAICKTRTVIYEIPRSQVDPTSANFLIWPPCVEVKRCTGCCNTSSVKCQPSRVHHRSVKVAKVEYVRKKPKLKEVQVRLEEHLECACAASSAGPEHREEEAGRRRESGKKRKRKRLRPT", "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 lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity). SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon wounding. SIMILARITY: Belongs to the PDGF/VEGF growth factor family."}
+{"protein": "MKLFVCFLLLAVVVVSAVNASEEMRLKNLLKAVERDETPDECVTRGNFCATPEVHGDWCCGSLKCVSNSCR", "text": "FUNCTION: Probable insect neurotoxin with ion channel impairing activity (Probable). Does not show activity on 45 human receptors from 9 families (5-hydroxytryptamine, adrenergic, dopamine, muscarinic, histamine, neurotransmitter, opioid, sigma, and gaba(A) receptors) (PubMed:27227898). In vivo, does not cause paralytic or lethal activity when injected into sheep blowflies or crickets (PubMed:27227898). It is noteworthy that both sheep blowflies and crickets are evolutionarily distant from prey species (PubMed:27227898). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MKVLLCIAASCLMLLALNVSAENTQQEEQDYDYGTDTCPFPVLANKTNKAKFVGCHQKCNGGDQKLTDGTACYVVERKVWDRMTPMLWYECPLGECKNGVCEDLRKKEDCRKGNGEEK", "text": "FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CCL1, CCL3, CCL4, CCL8, CCL17, CCL18 and CCL22. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MQPKTFVHQLHAILLEPEVNKWIYWSPTDNTVFFLKPYDPNFSTHVLKRYFKHGNVNSFVRQLHMYGFHKLSHPSPDQSSANNGNVKELVEWKFTHPSGFFFKEANAGILNKIQRKSTGVGKDGKRKNILSPISVSYVDASRLNVLSQQSGPVSAREPSNMFMGSPVHYSTSQSPPHISIPQQQQSSGPYLISSLPPQQPTVNMMRRQSISARMMNSYDYPNQFSTQDSIVQPQQPQQVLSPQALSGPPMKKSGTLSSTDDLKTTSLPIVNYPMPYHPGAFAQQQQQQQQPLPTVPPYSSYSTPFPSMMNSLSNSASNSPALGVCNNNVTLPKKSNISERQALDNHIQTLKNSLSTITDLIEKHINSASQDENKTLTNDAMNKDLRTSLSLLQNSKEEIIQLESKWMSMQSVKTTALPLQETTNTSSTLTSLTSSIIPKSIPIITKGEVATKPASY", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HSF family."}
+{"protein": "MLYRSALRTSRAFTPRLALSHSRLVSSLVFLEHKAGKLSEASLSAVTAAKTLGNDTHGLLVGTKSEIENALDRAKEIKGLSKIYLARSDSYSHSLAEALASLLASIVSAKDVSHLFAAHTAVGKNVFPRLAGLLDSSLIADIIALESSGDTFTRPIYAGNAVLTIKSSPKDSVKIVTVRSTAFDKAPVAAGSAVIEDVDIITVDTPTQFVSEELTVSSRPDLASAARVVSGGRALKSKESFDAILNPLADSLGAAVGASRAAVDAGYADNSLQVGQTGKVVAPELYVAIGISGAIQHLAGMKESKMIIAINKDPDAPIFQVADVGLVADLFESVPQLVKELGNVKV", "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). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the ETF alpha-subunit/FixB family."}
+{"protein": "MYAASILILHLTWAVATIAANGAGHNGPVASGAGPNGLQCQPIAVSACQGLGYNMTALPNLAGHTNQLEAELQIAKLVPLIESGCSRRARFLLCSSLFPLCTPDVPRPVAACKLLCETVRGECMENAPPELMELWPSFLNCDGLPQPEKHELCMQIPQEVAVPGGSPSGPPTTGSPGVEDHPQTYRFWKSGASPTSDLAGVLCPQNFSGSPFNPEECVPQCQRDAFHTSSQKKTSETLILGLSAVCFVLTLFALVTFWAEPTRFGYPERPVLFLCLCYNLFSVCYLERIVFHNQARMHDVELQGRLMRPGCLLTPPCLASYITTSYLSLCAASWWLIFALCFYLSSHKKWSSEALEKRSGLFHVLAWVPPLAPPIAALLLEKVRPSELTGMCYAPGFVELPALVLLLLGLYFTLRASRSLLSLQQQLQPTLAHHRFGQIRKRFVLFSLLYFAPTTAGVVAALCERYADSVPSCSTPDDCLSPTPLSAWPALVRIFFQLVGGTLTGLWVWSRKTCESYRNRLGASGTPTSSLMNQSKAAGALPKKHLYTSGKSMLPTGGITPLYAGISFHNVPVYNPNQSRV", "text": "FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Required to coordinate the cytoskeletons of epidermal cells to produce a parallel array of cuticular hairs and bristles. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family."}
+{"protein": "MASHPEQQSSSSSADVSSSSWGKVERKFTNKSASEYYDPCQDFADRSLRCMKRNPDDRDMCHDYFQAYRDCKKQWLTQKKLGSSSTAK", "text": "FUNCTION: Required for the assembly of cytochrome c oxidase. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: Belongs to the COX23 family."}
+{"protein": "MNKLQLLGVVFAKVNECSLELSCVRYCDPNLLLTKRKEFLHNAFVCKYLCDSLLSELQHFSCTNGLTACKHLAIILENLCEHFYVINKALCSFEIHKDHQQYYRTLFDVDQCSLHDPIKISFVNKQDLEITLTDFNEIERFLCKLNLIFPLIDARSGMRIISQIYDRLRKFTGISPLARLEFYKSACGGCYLCYEELQMTPNNGSSVQKRLNGVLCEHVTYTKDLVFQENEYLEVLREDLKRDNLLREDMRTELDDMKKILSNKKERGFYVPEAEQLLHRYDVFTDDIPNYIYTLSDLTYWSKTSEKIIKTMNMTMQQLNVYNNNMIKLKRSISRALNDIEVRDCFDVFEKVVDKRHCMFLGSMFTSSAKIISLLATQCLTAFEEKAVFERLNECDALCSTVNTILERLKSASGDGKEGITKQDFQADELIKGYNVSDEVSVRKKTYLNKVADKGYSKIVASLSTEERSIKKLIDINFLGTLCIDMMVKLEKMFYKRSQIGQMVENGVHLLALCNYDNHLYIRNNLSRQSISTENVNGVIQHILSFLCGPIFTHRHDIFPMPPNIDMAYACDNANVLPHRKEELMQCVNDITSVHGWSISSYNTFFKIDSVDLNTAHAHVWGYVKEFIVAVTLYNELYGQRLRAFRVDENTIRECGLYLTYNSDIPLVLKTDKNVIYGSDIYSILYAHMHHA", "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": "MLMAGQRGAWTMGDVVEKSLEGPLAPSTDEPSQKTGDLVEILNGEKVKFDDAGLSLILQNGLETLRMENALTDVILCVDIQEFSCHRVVLAAASNYFRAMFCNDLKEKYEKRIIIKGVDAETMHTLLDYTYTSKALITKQNVQRVLEAANLFQFLRMVDACASFLTEALNPENCVGILRLADTHSLDSLKKQVQSYIIQNFVQILNSEEFLDLPVDTLHHILKSDDLYVTEEAQVFETVMSWVRHKPSERLCLLPYVLENVRLPLLDPWYFVETVEADPLIRQCPEVFPLLQEARMYHLSGNEIISERTKPRMHEFQSEVFMIIGGCTKDERFVAEVTCLDPLRRSRLEVAKLPLTEHELESENKKWVEFACVTLKNEVYISGGKETQHDVWKYNSSINKWIQIEYLNIGRWRHKMVVLGGKVYVIGGFDGLQRINNVETYDPFHNCWSEAAPLLVHVSSFAATSHKKKLYVIGGGPNGKLATDKTQCYDPSTNKWSLKAAMPVEAKCINAVSFRDRIYVVGGAMRALYAYSPLEDSWCLVTQLSHERASCGIAPCNNRLYITGGRDEKNEVIATVLCWDPEAQKLTEECVLPRGVSHHGSVTIRKSYTHIRRIVPGAVSV", "text": "FUNCTION: Involved in B-lymphocyte antigen receptor signaling and germinal center formation."}
+{"protein": "MELQSLIDTVSLQKLLLLGALLRLILIAYAFFHDQWFRVKYTDIDYMIVVDGARHMWNGGSPFDRTTFRYTPLLAALVMPSIWIANPMGKLIFASSDLGAAWYCYGVLKSFAKERSAKWMVSLFILFNPIVLSVSTRGNSDMLVTFMSLMVLSKFARRKCYQAAAVLGFAVHFKIYPIIYALPLTLGVWEQSVAASTNTWRRVVKTAVVVSICALMAAISFAVPTVLCYMKYGQQYLNEAFIYHVYREDHRHNFSPYWLLMYLNMARRHLGQGVDFSPRLVAFAPQAVVLSFVSYKLRRNTAHACCVQTVLFVAFNKVCTVQYFVWFIPFLAFLFCEPKEVEDDESGGSGAFKFFSWVKALGVVLMWAATIPLWVTTAVPLEFHGYSDFAQLWIVSCLFFLAMVVLASMLARIAYRVQCTKCSAKSIKVA", "text": "FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-PI during GPI precursor assembly (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGM family."}
+{"protein": "MKRAHPDYSSSDSELDETIEVEKESADENGNLSSALCSMSPTTSSQVLARKRRRGIIEKRRRDRINNSLSELRRLVPSAFEKQGSAKLEKAEILQMTVDHLKMLHTAGGKGYFDAHALAMDYRSLGFRECLAEVARYLSIIEGLDASDPLLVRLVSHLNNYASQREAASGAHGGLGHIPWGSAFGHHPHIAHPLLLPQNGHGNAGTAASPTEPHHQGRLASAHPEAPALRAPPSGGLGPVLPVVTSASKLSPPLLSSVASLSAFPFSFSSFHLLSPSTPTQAANLGKPYRPWGTEIGAF", "text": "FUNCTION: Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Downstream effector of Notch signaling required for 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 HEY2 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. 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": "MRTLKSLVIVSAALLPFSATAFAADAIQEQPPVPAPVEVAPQYSWAGGYTGLYLGYGWNKAKTSTVGSIKPDDWKAGAFAGWNFQQDQIVYGVEGDAGYSWAKKSKDGLEVKQGFEGSLRARVGYDLNPVMPYLTAGIAGSQIKLNNGLDDESKFRVGWTAGAGLEAKLTDNILGRVEYRYTQYGNKNYDLAGTTVRNKLDTQDIRVGIGYKF", "text": "SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the Omp25/RopB family."}
+{"protein": "MEGPAFSKSPKDKTIERAFLGVLGILFVTGGLASRDNPHQVYNITWEVTNGEQDTVWAVTGNHPLWTWWPDLTPDLCMLALHGPTHWGLDNHPPYSSPPGPPCCSGDAGAVSGCARDCDEPLTSYSPRCNTAWNRLKLARVTHAPKEGFYICPGSHRPRWARSCGGLDAYYCASWGCETTGRAAWNPTSSWDYITVSNNLTSSQATKACKNNGWCNPLVIRFTGPGKRATSWTTGHFWGLRLYISGHDPGLTFGIRLKVTDLGPRVPIGPNPVLSDQRPPSRPVPARPPPPSASPSTPTIPPQQGTGDRLLNLVQGAYLTLNMTDPTRTQECWLCLVSEPPYYEGVAVLREYTSHETAPANCSSGSQHKLTLSEVTGQGRCLGTVPKTHQALCNRTEPTVSGSNYLVAPEGTLWACSTGLTPCLSTTVLNLTTDYCVLVELWPKVTYHSPDYVYTQFEPGARFRREPVSLTLALLPEGLTMGGIAAGVGTGTTALVATQQFQQLQAAMHNDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLNQRQKLFESGQGWFEGLFNRSPWFTTLISTIMGPLIVLLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPIEYEP", "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 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). SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane; Peripheral membrane protein Note=The R-peptide is membrane-associated through its palmitate. 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 virion 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": "SGSCEVKTCWWSQPDFRVIGDFLKDKYDSASEMVVEKHRESRGWVETLRPKYTFFKPPTERDLVYYESSPNFCEPNPETGSFGTRDRICNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCIF", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. Required for normal embryonic mesoderm development and formation of caudal somites. Required for normal morphogenesis of the developing neural tube. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MANSTTVTEFILLGLSDACELQVLIFLGFLLTYFLILLGNFLIIFITLVDRRLYTPMYYFLRNFAMLEIWFTSVIFPKMLTNIITGHKTISLLGCFLQAFLYFFLGTTEFFLLAVMSFDRYVAICNPLRYATIMSKRVCVQLVFCSWMSGLLLIIVPSSIVFQQPFCGPNIINHFFCDNFPLMELICADTSLVEFLGFVIANFSLLGTLAVTATCYGHILYTILHIPSAKERKKAFSTCSSHIIVVSLFYGSCIFMYVRSGKNGQGEDHNKVVALLNTVVTPTLNPFIYTLRNKQVKQVFREHVSKFQKFSQT", "text": "FUNCTION: Odorant receptor. Activated by (-)-citronellal and to a lesser extent by (+)-citronellal. Not activated by carvone or limonene. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MAMTTRTLLLAAVCAAAALPRGWSPIKNIDDPHIQELGRWAITENNRVSPSDELTFHRVTGGEQQVVSGMNYRLEIEAASGGGDVTGSYGAVVFEQEWSNTRKLISFDKNHNF", "text": "FUNCTION: Specific inhibitor of cysteine proteinases. Probably involved in the regulation of endogenous processes and in defense against pests and pathogens (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cystatin family. Phytocystatin subfamily."}
+{"protein": "MISSCVTRCFGRGKCLPGPATASIYQTIRCISTNSNKAAEAPIFPKLEDVKMHELIGNNNFGKKTYYVERSRTGNLPVYSAYKNGGNKIITEIRKIEGDVIQLRNDLQEQLPFIPKKSWSVVMQSKKIIIKGNAVEAVKRVLTKKF", "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 mL49 family."}
+{"protein": "MKAIVFVLIFAVAFAVTATHQGEILCNLCTGLINTLENLLTTKGADKVKDYISSLCNKASGFIATLCTKVLDFGIDKLIQLIEDKVDANAICAKIHAC", "text": "FUNCTION: Forms pores in the cell membrane of host cells (PubMed:1881907, PubMed:7715451, PubMed:8515772, PubMed:7525351, PubMed:14970207). Has antibacterial activity against M.luteus, no activity against E.coli (PubMed:7715451). Implicated in the cytolytic activity of the parasite (PubMed:7715451). SUBCELLULAR LOCATION: Cytoplasmic granule."}
+{"protein": "MPEFLGPIAGFGVTLSTMFKKPETEFYPEEKRPTAPGYHGRHQLNRYADGLEKCIGCELCAWACPADAIYVEGADNTEEERFSPGERYGQVYQINYLRCIGCGLCVEACPTRALTMTNEYEMVDDNRAGLIYEKDRLLAPLKTDMTAPPHALRPGTTQDDYYRGDITAVPEQAAPEQAAPEQPAPEREPNPETEK", "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": "CRYICPLGAALAIPSKFRLFDWLKRRKECGNPCQLCAKECEIQAIHPDGRINGNECHYCLDCQMTYHNDNKCPPLINKRKKRGKKAADPQLIPAVEVSDA", "text": "FUNCTION: Transcriptional activator of the nitrous-oxide reductase gene NosZ. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein."}
+{"protein": "MGSERIMTTQQQFLDLLSDIEPSTTTVNDCSSAHNTLRDALKVHNEFSKVHVHTFLSGSYKRNTAVRPTTIGGITQRPDVDIIALTNHTINDDPQIVLDAVHTALKDIGYTDLTVNRRSVNVKLKKVDMDVVPIISDGYGGYLIPDIHLEEWLVTNPPAHTEWTVEVNKNANGRFKPLVKLFKWWRRENLSDLKRPKGFILECLVAKHMNYYESNYEKLFVYLLETIRDSYGIYASLGIIPHLEDPGVAGNNVFSAVTADEFKTFFEKVEEQAAIARNALNETDDDKALALWRQVLGNRFPRSASHKSANSADMASSLIRSALGAGLTFPSTPVYPNKPGGFA", "text": "FUNCTION: Cyclic trinucleotide synthase that catalyzes the synthesis of 2',3',3'-cyclic AMP-AMP-AMP (2',3',3'-c-tri-AMP or 2'3'3'-cAAA) as the major product, as well as another cyclic AMP(4) 2'-5'-linked minor product that acts as a second messenger for cell signal transduction. 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 II-C(AAAA) CBASS system (PubMed:32839535). SIMILARITY: Belongs to the CD-NTase family. D01 subfamily."}
+{"protein": "MALWYLFNKRSLGAAVLILVGLLMCNIQITGAQSNIGVCYGEIANNLPSEQDVINLYKANGIRKMRIYYPDTNIFKALNGSNIEIILEVPNQDLEALANSSIANGWVQDNIRSHFPYVKFKYISIGNEVSPTNNGQYSQFLLHAMKNVYNALAAAGLQDKIKVSTATYSGLLANTYPPKDSIFREELKSFINPIIEFLARNNLPLLANIYPYFGHIYNTVDVPLSYALFNQQETNSTGYQNLFDALLDSIYFAVEKAGGPNVEIIVSESGWPSEGNSAATIENAQTYYRNLVNHVKGGAGTPKKPGRIIETYLFAMFDENEKQGEITEKHFGLFYPNRAAKYQLNFMYSDS", "text": "FUNCTION: Implicated in the defense of plants against pathogens. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Note=Stylar secretory matrix. SIMILARITY: Belongs to the glycosyl hydrolase 17 family."}
+{"protein": "MKKPVVVILAVVVLLAAGIGGWLWYQSQQDRGLTLYGNVDIRTLNMSFRVGGRLESLAVDEGDTVKSGQLLGQLDKAPYENALMQAKASVSVAQAQYDLMLAGYRDEEVAQAEAAVKQAKAAYDYSQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLSQYRTGNRPQDIAQAKANLEQAQAQLAQAELDLHDTTLIAPSNGTLMTRAVEPGSMLSAGSTVLTLSLTRPVWVRAYIDEPNLSQAQPGREILLYTDGRPDKPYHGKIGFVSPTAEFTPKTVETPDLRTDLVYRLRIIVTDADDALRQGMPITVKFNDGEGHE", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the UPF0194 family."}
+{"protein": "MYTRFGPPIVFLISCYALILCGTVDALPRAPYFNDDINKTTTTSEDKTVGNTVVEEEKKTYTVGDSEGYQEASRLLQKSLNLSLDPCDDFFEYACRAWVDSHPIPDDLTSYSQFTATREKVLAEMRKLYEDNTSIPTSKSIALIKQIYNTCMDTEKHNAVGARDLLEKIKTYGYWPMVHNEKWRESTFDLTKLLSNTIQSRDVSVFFDFGPAEDSRNVSRRLLSFDQGSLGLGYSTRDYYLDEKKYEKQMKAYRKYTIGKVRYYTEDAGMAVNESKIESDVDEIIAFEKEWAQILVAEEDRRNYTKLYNVRRFDDLKEYMSIIDWKKLTLSTTPFLVHSYLKTNPSIIISDVEYLQKMNTLLQNTDPRIVTNYILLRWAGSWSQEIGKKYEDLQQEFAFQMYGRKQRQPRWKDCVSSAGGKLSYASGSMYVRKYFDANAKNTTLDMITDLQEAFRNMMHANDWMDAETKKYALEKADQMLKQIGYPDFILNDEKLDDWYKGLEGAPEDSFSQLVEKSIQWRNNFYYRRLLEPVNRFEFISSAAVVNAFYSPTRNAIAFPAGILQQPFFDARFPKALNYGGIGAVIGHEITHGFDDTGRQFDNVGNLRDWWDNTTSSKFNERTQCIIEQYADVKLRGTDLRINGKLTQGENIADNGGIKQAFKAYKSYLEKHGGQEARLPQFESLTNEQLFFVGYAQVWCGAKTPETKTLLLLTDPHSPETARVNTVLTNQPEFAEAFKCPAGSPMNPTKRCVVW", "text": "FUNCTION: Probable cell surface protease. Required to control the neuronal innervation of pharyngeal pumping. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase M13 family."}
+{"protein": "MDRCKENCVSRPVKSTVPFGPKRVLVTEQIPSQHPGSASSGQAQRVLCPSNSQRVPPQAQKPVAGQKPVLKQLPAASGPRPASRLSNPQKSEQPQPAASGNNSEKEQTSIQKTEDSKKRQWTLEDFDIGRPLGKGKFGNVYLAREKQSKFILALKVLFKVQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSNGELKIADFGWSVHAPSSRRTTLCGTLDYQPPEMIEGRMHDEKVDLWSLGVLCYEFLVGMPPFEAHTYQETYRRISRVEFTFPDFVTEGARDLISRLLKHNSSQRLTLAEVLEHPWIKANSSKPPTGHNSKEATSKSS", "text": "FUNCTION: Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (By similarity). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (By similarity). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (By similarity). Required for initial activation of CDK1 at centrosomes (By similarity). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity (By similarity). Required for normal axon formation (PubMed:19812038). Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization (By similarity). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizating p53/TP53 (By similarity). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (By similarity). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (By similarity). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cell projection, neuron projection Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Basolateral cell membrane Note=Localizes on centrosomes in interphase cells and at each spindle pole in mitosis. Associates with both the pericentriolar material (PCM) and centrioles. Detected at the neurite hillock in developing neurons. Colocalized with SIRT2 at centrosome. The localization to the spindle poles is regulated by AAAS (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily."}
+{"protein": "MSVPEVQWAQVVEKAGTPPVYKQVPVPKPGPDEILVKMRYSGVCHTDLHAMKGDWPLPSKMPLIGGHEGAGVVVAKGELVKDEDFKIGDRAGIKWLNGSCLSCEMCMQADEPLCPHASLSGYTVDGTFQQYTIGKAALASKIPDNVPLDAAAPILCAGITVYKGLKESGARPGQTVAIVGAGGGLGSLAQQYAKAMGLRTIAIDSGDEKKAMCEQLGAEVFIDFSKSADVVADVKAATPGGLGAHAVILLAVAEKPFQQATEYVRSHGSVVAIGLPANAFLKAPVFTTVVRMINIKGSYVGNRQDGVEALDFFARGLIKAPFKKAPLQDLPQIFELMGQGKIAGRYVLEIPE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MALIQTSLIWVAYAVAVAILFLIASTFVYVYQKPRDRAAAVTIVCIFTTLALLATVLLIPVDVALVSSTSRSSLGRKKDWATPDKVDSIVYTLRIVYYTLYSLDAVLCLLVIPFTYFWYEEYDQDAAEHGEQTAAQRIGGALKWTLGFLIFVVAIFLVGFFVPFAKQAKEDKRLDLDYFKHLLSENHGERALSFGLGFLITVGTVLFVLYTGAGMALLPVAMIKSAPSVSAPTLAANTASQLETNRERQRQLEGRNEGREGGLDSRDRRELEALVREERTLIRRERLAAESSGEDRHWIVKAWIKTEAFFRPLKLIGGLILLVFALVIFASMLITGIDKAKNSICGAHCGYILGHINIFQPLNWVLVKSAKVFPIDYVLFLLLVLFLFSASVVGIATAGIRFLWVTIFKIRKGQTSPQALLMATVLLTLITLAINYSVAMVVAPQYATWGPQTYCDMKTNSLDEQPDCAEHKDLIKPCSELATNPAAQQVCTPSVLSTFINRVTINFPFFGIVLFWAQFAFLGVYLIVFLTTLFKAPTLDQEQIDRDLEEEEDEGLLASTGRRFGAAWSDVTGRATKPANYGATERDERIQ", "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": "MAYDVARVRGLHPSLGDGWVHFDAPAGMLIPDSVATTVSTAFRRSGASTVGAHPSARRSAAVLDAAREAVADLVNADPGGVVLGADRAVLLSLLAEASSSRAGLGYEVIVSRLDDEANIAPWLRAAHRYGAKVKWAEVDIETGELPTWQWESLISKSTRLVAVNSASGTLGGVTDLRAMTKLVHDVGALVVVDHSAAAPYRLLDIRETDADVVTVNAHAWGGPPIGAMVFRDPSVMNSFGSVSTNPYATGPARLEIGVHQFGLLAGVVASIEYLAALDESARGSRRERLAVSMQSADAYLNRVFDYLMVSLRSLPLVMLIGRPEAQIPVVSFAVHKVPADRVVQRLADNGILAIANTGSRVLDVLGVNDVGGAVTVGLAHYSTMAEVDQLVRALASLG", "text": "FUNCTION: Is essential for optimal growth. FUNCTION: Is essential for optimal growth. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MAVGLAEHDKEAWGRLPFSLTIADISQDDEPLIYVNRAFEQMTGYSRSSVVGRNCRFLQGEKTDPGAVERLAKAIRNCEEVEETIYNYRADGEGFWNHLLMGPLEDQDEKCRYFVGIQVDMGQSESPDRATELDRQLAEVQHRVKNHLAMIVSMIRIQSSQAGGVGSQFDSLSRRVEALQLLYQEMDIAGAAKATDKIIPLGAYLGRIASAINHIDGRGAIKVNVQADTVDVPVETAGRIGLLVSEVLTNALQHAFSDRASGVVQLRSSVMSGEQLRVTVEDDGRGIPEDCDWPNEGNLGSRIVRQLVQGLGAELNVTRGGTGTIVNIDIPLSQQKTLIADERTKD", "text": "FUNCTION: Photosensitive kinase that is involved in increased bacterial virulence upon exposure to light."}
+{"protein": "MKKSWTWTWRVPAELLLLCAALGCLCVPGSRSERPRSLEPTVVNRSLAKSRHSRSVDATPMPIDCELSSWSSWTMCDPCQKKRYRHAYLLRPSQFNGEPCNFSDKEVEDCATSRPCRSQVRCEGFVCAQTGRCVNRRLLCNGDNDCGDQSDEANCRKIYKKCHHEMEQYWAIGSLASGINLFTNSLEGPVLDHRYYAGGCNPHYILDMRFRKPYNVESYTPQTQGKYKFALAEYESYSDFERNVMEKTYSKSTFNLGFKIPSIFEFGINTESDQLMNYISRTKRFSHTKSKFLHARSALEVAHYKLKPRNLMLHYDFLQRVQRVPLEYSYGEYRDLFRDFGHHFITEAVLGGIYEYTLIMNKEAMERADYSLNDVQACAKNDFKLGAAIEEVYVSLGVSTSKCRGILNEIKDRNKRDTMVQDLVVLVRGGASEHITALAYSDLPTADLMQEWGDAVQYNPAIIKIKVEPLYELVTATDVAYSSTVKQNMRQALEEFQGEVSPCRCAPCQGNGVPVQKGSRCDCICPVGFQGSACEITSRKNVPIDGRWSCWSRWSSCSGGQKTRRRQCNNPAPQDGGSPCSGPASETLAC", "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": "MSSQQQKQPCTPPPQLQQQQVKQPCQPPPQEPCIPKTKEPCHPKVPEPCHPKVPEPCQPKVPEPCHPKVPEPCPSIVTPAPAQQKTKQK", "text": "FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. Can function as both amine donor and acceptor in transglutaminase-mediated cross-linkage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cornifin (SPRR) family."}
+{"protein": "MDTQKIEAAVKMIIEAVGEDANREGLQETPARVARMYQEIFSGLGQTAEEHLSKSFEIIDDNMVVEKDIFFHTMCEHHFLPFYGRAHIAYIPDGRVAGLSKLARTVEVYSKKPQIQERLNIEVADALMDYLGAKGAFVVIEAEHMCMSMRGVRKPGTATLTTVARGLFETDKDLRDQAYRLMGL", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I family. SIMILARITY: Belongs to the GTP cyclohydrolase I family."}
+{"protein": "MRALAPSFRLLAGLLLLIVLSLSSANAQCNFANSCTGVELYGYILRGDCINEDGHPHATSINLNYYIGNDNGRLEYPGESFGSSCVKTALNDGHTLTASCKGADGQYHDSSMDLNYVVGNSYGYMEPCRASNADHVLKSSSE", "text": "FUNCTION: Mannose-binding lectin. SIMILARITY: Belongs to the cyanovirin-N family."}
+{"protein": "MCARGQVGRGTQLRTGRPCSQVPGSRWRPERLLRRQRAGGRPSRPHPARARPGLSLPATLLGSRAAAAVPLPLPPALAPGDPAMPVRTECPPPAGASAASAASLIPPPPINTQQPGVATSLLYSGSKFRGHQKSKGNSYDVEVVLQHVDTGNSYLCGYLKIKGLTEEYPTLTTFFEGEIISKKHPFLTRKWDADEDVDRKHWGKFLAFYQYAKSFNSDDFDYEELKNGDYVFMRWKEQFLVPDHTIKDISGASFAGFYYICFQKSAASIEGYYYHRSSEWYQSLNLTHVPEHSAPIYEFR", "text": "FUNCTION: Substrate-recognition subunit 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 (Probable) (PubMed:29911972). Binds proteins and peptides with a Pro/N-degron consisting of an unmodified N-terminal Pro followed by a small residue, and has the highest affinity for the peptide Pro-Gly-Leu-Trp (PubMed:29632410). Binds peptides with an N-terminal sequence of the type Pro-[Ala,Gly]- [Leu,Met,Gln,Ser,Tyr]-[Glu,Gly,His,Ser,Val,Trp,Tyr]. Does not bind peptides with an acetylated N-terminal Pro residue (PubMed:29632410). SIMILARITY: Belongs to the GID4/VID24 family."}
+{"protein": "MRIEVTIAKTSPLPAGAIDALAGELSRRIQYAFPDNEGHVSVRYAAANNLSVIGATKEDKQRISEILQETWESADDWFVSE", "text": "FUNCTION: Involved in SOS regulation. Inhibits RecA by preventing RecA to bind ssDNA. Can displace ssDNA from RecA (By similarity). FUNCTION: Involved in SOS regulation. Inhibits RecA by preventing RecA to bind ssDNA. Can displace ssDNA from RecA. SIMILARITY: Belongs to the DinI family."}
+{"protein": "MILSHRYTLIALAAAILSSGAHAAGASVTASWGNVAEPSLPADSAVCKTLAATITPVSGSIDTVDGNPSNSQPDASRIQTAIDNCPAGQAVRLVKGSAGESGFLSGSLKLKSGVTLWIDTGVTLFASRNPADFDNGVGTCGTATTSNTKSCNALIVARDTVGSGIVGDGIIDGRGGSLVTSGPNANRLTWWDIAYLNKTKGLNQQNPRLVQLYNGSAFTLYRVTVQNSPNFHIVTTGTAGVTAWGIKIVTPSLAYTVPGYKCAAGTTPDKVTPATCFTPETVKNTDGFDPGQSTNVVLANSYISTGDDHVAIKASGGATRNLLFAHNHFYYGHGLSIGSETDGGVSNMQVTDLAMDGNDSSGGNGLRIKSDISRGGKVNNIVYNGICMRNVKEPLVFDPFYSTAKGSLYPNFTNIVVKNFHDLGSAKGIARTMTFLGYEAKKRTNPLTLTLDNVVFDGTQPAFDVAHNGGPASPNGTHFTFGGNGPVSFANAIVTSSTTDVTVTGTPGTAAAVDCSNAFVPLKSVAPTSPI", "text": "FUNCTION: Contributes to the wilt disease production on tomato. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
+{"protein": "MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEDRQPSPEPVQENANSAYYDAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKHLEELEEKSATPPPAEPASLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVDAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMTQKLGSGRGTGQMEGRFTGQRR", "text": "FUNCTION: Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling. Plays an essential role in stress granule formation. Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (By similarity). Promotes formation of stress granules phase- separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, Stress granule."}
+{"protein": "MGYKCTRCKQKVEIDYEYTGIRCPYCGHRILVKERPTTIKRIKAE", "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": "MSERAADDVRGEPRRAAAAAGGAAAAAARQQQQQQQQQQPPPPQPQRQQHPPPPPRRTRPEDGGPGAASTSAAAMATVGERRPLPSPEVMLGQSWNLWVEASKLPGKDGTELDESFKEFGKNREVMGLCREDMPIFGFCPAHDDFYLVVCNDCNQVVKPQAFQSHYERRHSSSSKPPLAVPPTSVFSFFPSLSKSKGGSASGSNRSSSGGVLSASSSSSKLLKSPKEKLQLRGNTRPMHPIQQSRVPHGRIMTPSVKVEKIHPKMDGTLLKSAVGPTCPATVSSLVKPGLNCPSIPKPTLPSPGQILNGKGLPAPPTLEKKPEDNSNNRKFLNKRLSEREFDPDIHCGVIDLDTKKPCTRSLTCKTHSLTQRRAVQGRRKRFDVLLAEHKNKTREKELIRHPDSQQPPQPLRDPHPAPPRTSQEPHQNPHGVIPSESKPFVASKPKPHTPSLPRPPGCPAQQGGSAPIDPPPVHESPHPPLPATEPASRLSSEEGEGDDKEESVEKLDCHYSGHHPQPASFCTFGSRQIGRGYYVFDSRWNRLRCALNLMVEKHLNAQLWKKIPPVPSTTSPISTRIPHRTNSVPTSQCGVSYLAAATVSTSPVLLSSTCISPNSKSVPAHGTTLNAQPAASGAMDPVCSMQSRQVSSSSSSPSTPSGLSSVPSSPMSRKPQKLKSSKSLRPKESSGNSTNCQNASSSTSGGSGKKRKNSSPLLVHSSSSSSSSSSSSHSMESFRKNCVAHSGPPYPSTVTSSHSIGLNCVTNKANAVNVRHDQSGRGPPTGSPAESIKRMSVMVNSSDSTLSLGPFIHQSNELPVNSHGSFSHSHTPLDKLIGKKRKCSPSSSSINNSSSKPTKVAKVPAVNNVHMKHTGTIPGAQGLMNSSLLHQPKARP", "text": "FUNCTION: Acts as component of the STAGA transcription coactivator-HAT complex (PubMed:15932940, PubMed:18206972). Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation (PubMed:15932940, PubMed:18206972). Necessary for microtubule cytoskeleton stabilization (PubMed:22100762). SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform a]: Nucleus Nucleus, nucleolus Nucleus matrix Cytoplasm, cytoskeleton Note=In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus (PubMed:10441328). It is able to shuttle between the nucleus and cytoplasm (PubMed:16314424). SIMILARITY: Belongs to the ataxin-7 family."}
+{"protein": "MESTSQDRRATHVITIKPNETVLTAFPYRPHSSLLDFLKGEPRVLGATQILLALIIVGFGTIFALNYIGFSQRLPLVVLTGYPFWGALIFILTGYLTVTDKKSKLLGQGVTGMNVISSLVAITGITFTILSYRHQDKYCQMPSFEEICVFSRTLFIVLFFLPSDVTQNSEQPAPEENDQLQFVLQEEFSSDDSTTNAQSVIFGGYAFFKLTLSRSPLVSQPGNKGREFVPDEQKQSILPSPKFSEEEIEPLPPTLEKKPSENMSIQLDSTFKQMKDEDLQSAIVQPSQMQTKLLQDQAASLQVFPSHSALKLEDISPEDLPSQALPVEGLSEQTMPSKSTSSHVKQSSNLTANDLPPQGILSQDTSSQDMLFHDMTSQDMQSLDMLSQDTPSHAMPPQDIPSQDMLSQALSAHAILPEASTSHIVQFPEIQHLLQQPPDLQPENTEPQNQQILQMSYQDIRSEVMEETKEWKSEEELHRRKSSRRHSLNQQTKALQYLRRHSLDVQAKGQKSSKRHSLDQQSKGWQSPKQKSLDQQIKDWLSPKRHSVDKQAQLNQTKEQLPDQQAEDQQAKGEQYPEGQSKDGQVKDQQTDKEQNSKKQTQDQQTEDQPAQEKKSPKGQFQNVQAEGQQAQVEKVPKLLCQDSESQIQQYQFWQFHKGNLQAGQPRTVNLLAKNPLTG", "text": "FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MS4A family."}
+{"protein": "MKTPWKVLLGLLGIAALVTVITVPVVLLNKGTDDAAADSRRTYTLTDYLKSTFRVKFYTLQWISDHEYLYKQENNILLFNAEYGNSSIFLENSTFDELGYSTNDYSVSPDRQFILFEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWITWSPVGHKLAYVWNNDIYVKNEPNLSSQRITWTGKENVIYNGVTDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRIPYPKAGAENPTVKFFVVDTRTLSPNASVTSYQIVPPASVLIGDHYLCGVTWVTEERISLQWIRRAQNYSIIDICDYDESTGRWISSVARQHIEISTTGWVGRFRPAEPHFTSDGNSFYKIISNEEGYKHICHFQTDKSNCTFITKGAWEVIGIEALTSDYLYYISNEHKGMPGGRNLYRIQLNDYTKVTCLSCELNPERCQYYSASFSNKAKYYQLRCFGPGLPLYTLHSSSSDKELRVLEDNSALDKMLQDVQMPSKKLDVINLHGTKFWYQMILPPHFDKSKKYPLLIEVYAGPCSQKVDTVFRLSWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEATRQFSKMGFVDDKRIAIWGWSYGGYVTSMVLGAGSGVFKCGIAVAPVSKWEYYDSVYTERYMGLPTPEDNLDYYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQLSKALVDAGVDFQTMWYTDEDHGIASNMAHQHIYTHMSHFLKQCFSLP", "text": "FUNCTION: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:14719797). Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones such as brain natriuretic peptide 32. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Apical cell membrane; Single-pass type II membrane protein Cell projection, invadopodium membrane; Single-pass type II membrane protein Cell projection, lamellipodium membrane; Single-pass type II membrane protein Cell junction Membrane raft Note=Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids. Redistributed to membrane rafts in T-cell in an interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface (By similarity). SUBCELLULAR LOCATION: [Dipeptidyl peptidase 4 soluble form]: Secreted. Note=Detected in the serum and the seminal fluid. SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily."}
+{"protein": "MVMEVDEPAVAATTSQNQPQEHANDFDMDTSEGPIENDETFEPVDQINWKFNQVKGNIDADVHTEADVISCVEFSHDGEYLATGDKGGRVVIFQRDQSGKYVKGVRSREYNVYSTFQSHEPEFDYLKSLEIDEKINQIRWLKKKNAANFILSTNDKTIKLWKISERERKIGDDAWNLPRTNRINTSSFRGRLQIPSIVPMELIVEASPRRVYGNAHTYHVNSISVNSDQETFLSADDLRVNLWNLEITNESFNIVDIKPANMEELTEVITAAEFHPTQCNWFVYSSSKGSIRLCDMRDRALCDAYAKIFEEPEDPQSRSFFSEIIASVSDVKFSHNGRYLLTRDYLTVKVWDLNMESQPVETYPVHNYLRTKLCALYENDSIFDKFECDWSGDDKHILTGSYHNLFRSYARGNNQDAKTWEARPQEPHSQLRSRFVVPSAKRKRNNLSSSGETTEEDLSSDQLQFDRKILHTAWHPKDNIIALAATNNLYIFSDV", "text": "FUNCTION: Probable regulatory subunit of serine/threonine phosphatase let-92. Together with let-92 and constant regulatory subunit paa-1, positively regulates centriole duplication during early embryonic cell divisions by preventing the degradation of sas-5 and kinase zyg-1 (PubMed:21497766). In addition, during vulva development, may play a role with phosphatase let-92 and regulatory subunit paa-1 in the induction of vulva cell precursors by positively regulating let-60/Ras- MAP kinase signaling, probably by promoting lin-45 activation (PubMed:10521400, PubMed:14724126). In intestinal epithelial cells, may play a role in the late secretory pathway probably by regulating the exocyst, a protein complex involved in targeting secretory vesicles to the plasma membrane (PubMed:24192838). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family."}
+{"protein": "MQPTLLLSLLGAVGLAAVNSMPVDNRNHNEGMVTRCIIEVLSNALSKSSAPPITPECRQVLKTSRKDVKDKETTENENTKFEVRLLRDPADASEAHESSSRGEAGAPGEEDIQGPTKADTEKWAEGGGHSRERADEPQWSLYPSDSQVSEEVKTRHSEKSQREDEEEEEGENYQKGERGEDSSEEKHLEEPGETQNAFLNERKQASAIKKEELVARSETHAAGHSQEKTHSREKSSQESGEETGSQENHPQESKGQPRSQEESEEGEEDATSEVDKRRTRPRHHHGRSRPDRSSQGGSLPSEEKGHPQEESEESNVSMASLGEKRDHHSTHYRASEEEPEYGEEIKGYPGVQAPEDLEWERYRGRGSEEYRAPRPQSEESWDEEDKRNYPSLELDKMAHGYGEESEEERGLEPGKGRHHRGRGGEPRAYFMSDTREEKRFLGEGHHRVQENQMDKARRHPQGAWKELDRNYLNYGEEGAPGKWQQQGDLQDTKENREEARFQDKQYSSHHTAEKRKRLGELFNPYYDPLQWKSSHFERRDNMNDNFLEGEEENELTLNEKNFFPEYNYDWWEKKPFSEDVNWGYEKRNLARVPKLDLKRQYDRVAQLDQLLHYRKKSAEFPDFYDSEEPVSTHQEAENEKDRADQTVLTEDEKKELENLAAMDLELQKIAEKFSQRG", "text": "FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides. SUBCELLULAR LOCATION: Secreted Note=Neuroendocrine and endocrine secretory granules. SIMILARITY: Belongs to the chromogranin/secretogranin protein family."}
+{"protein": "MGSEPPSSPQVVEEGADEEDEELSGAEDADLRSSSGRGSLLTRRGITLRVLLKDGLVEPGDGVLSIHYLGKKFVGDLLNDGKIRWVETGQIFNSPSAWATHCKRLVNPAKKSGCGWASVRYRGQKLVQYKTTWLHKYQPSADMSLISEGEDDEMGDDDEEEGKTTIPVEDKNKKSKPELHEIGLTQRRDRERIPVRYCTLGTRDAARDPHTLVELSAFSAINRFQPFNVAVSSNVLLLMDFHCHLTSSEVVGYLGGRWDTNTQLLTVLRAFPCRTRLADKDAAPAVEEEICQNLFMRGLSLVGWYHSHPRGPALPSLQDIDSQMDHQLRLQGSSNGFQPCLGIICGPYYHGNQGVASTITPFWVVPPPEQRPNDHGIPVAVEVTYVQDNFLTTDVLNEMMLLVEFYRSAPDLVQFSQMWSPNTSILDKIKASLSGHAPKDQAYAQILEHVYNQLRNTQ", "text": "FUNCTION: Probable protease (By similarity). Acts as a sensor of N(6)- methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA, leading to its degradation (By similarity). SIMILARITY: Belongs to the peptidase M67 family."}
+{"protein": "MNQVELLSPAGNLKKLKIALNYGADAVYGGVSHFSLRNRAGKEFTLETFKEGIDYAHALNKKVYATINGFPFNSQLKLLEEHIDKMAELEPDAFIIAAPGVVKLALKIAPHIPIHLSTQANVLNLLDAQVFYDLGVKRIVCARELSLNDAIEIKKALPNLELEIFVHGSMCFAFSGRCLISALQKGRVPNRGSCANDCRFDYEYYVKNPDNGVMMRLVEEEGVGTHIFNAKDLNLSGHIAEILSSNAISALKIEGRTKSSYYAAQTTRIYRLAVDDFYHNTLKPSFYASELNTLKNRGFTDGYLMRRPFERLDTQNHQTAISEGDFQVNGEITEDGRFFACKFTTTTNTAYEIIAPKNAAITPIVNEIGKIYTFEKRSYLVLYKILLENNTELETIHSGNVNLVRLPAPLPAFSFLRTQVRV", "text": "FUNCTION: Involved in prephenate-dependent formation of 5- hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-carboxymethoxyuridine (cmo5U) biosynthesis. SIMILARITY: Belongs to the peptidase U32 family."}
+{"protein": "MQFIKYKSYILKFLLVSCIFCINGCDCTILCPNGLIAQEQRFVLFVSFFTMLLIIIPVIFMTIFFVLRYRESNFSKTYDPKWSHSNIIELLIWGIPIIIIVFLSIFSWKSVHDLDPKKPIVSNVQPIKINVISLDWKWLFIYPDQKIATINKLIIPINTPIIFNLTSGSVMNSFFIPSLGSQIYVMPGMKTNLNLIANKLGQFKGFSSNYSGKGFSNMKFDVLVTSDHIFFYEWVKKIQKSKYKLNSMYQFNQLAIPSDNNAIKYFSNLKENLFNVVIANVLKISL", "text": "FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
+{"protein": "MAEQSDKAVKYYTLEEIKKHNHSKSTWLILHHKVYDLTKFLEDHPGGEEVLREQAGGDATENFEDIGHSTDARELSKTFIIGELHPDDRSKIAKPVETLITTVDSNSSWWTNWVIPAISAVVVALMYRIYTAED", "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": "MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI", "text": "FUNCTION: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition (PubMed:1833066, PubMed:1827756, PubMed:8114739, PubMed:8302605, PubMed:19412162, PubMed:33854235). Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase (PubMed:1833066, PubMed:1827756, PubMed:8114739, PubMed:8302605, PubMed:19412162). Hypophosphorylates RB1 in early G(1) phase (PubMed:1833066, PubMed:1827756, PubMed:8114739, PubMed:8302605, PubMed:19412162). Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals (PubMed:1833066, PubMed:1827756, PubMed:8302605, PubMed:19412162). Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity (PubMed:15241418). Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (PubMed:9106657). Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner (PubMed:16569215, PubMed:18417529). SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus membrane Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members. SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily."}
+{"protein": "MLKRRQPKYCSFMDSIDNSTTIIRKNLNRFIRELTDDGKLDFESIPYQNLQKEVANQDEEGCENVIEVLLDTTSRSGCPDRKLILQLFNSFFLQFPIFRENLLNDPSEFLELMFETNPIRNPLPGSKKHGNELKVEAITVIKSWEKEKCVKNDARMKCLVVTLKKTKFVDYENGAKKIEAERKRKKILEERKMKMIENSVNVYSSKYHEIKNDAETLSMELTTTMQMLVPSFTTADPEVPSTSTSTPSAISDSKSFEIFIPDLTPEISVSSENDAIVEAFLGAKLSLIHRVQTLRKLVKRLQLLKQPGEKLAQEIIDYRDGIKNLVLKADELRIINPRPPKNKRKKSDDDFIDVDISIDDILMVQYAEKLEVDVKSKDESEKITESPEKHKIEMKNEKPVKIKTVPFGLDLKYWGEERKDVEVPKNNADCHRFWRSADEGTVAGKAQQSIYTQRQYTFIGKAPDNRKVCLAKMKSGKLCPRKDYYTCPLHGKIVDRDDEGRPINEEDRLEENYRKEQNHLKEADKIRQMIEKEYESKTKRRKKHDVDTTASEDVRNRLQKKLLDPKTIQRVSADLDASRKNRLEKNFGQQFSHF", "text": "FUNCTION: Factor involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage (PubMed:27043179). TC-NER allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (By similarity). SUBCELLULAR LOCATION: Chromosome Note=Accumulates at UV DNA damage sites. SIMILARITY: Belongs to the UVSSA family."}
+{"protein": "MAASMCDVFSFCVGVAGRARVSVEVRFVSSAKGKGLFATQLIRKGETIFVERPLVAAQFLWNALYRYRACDHCLRALEKAEENAQRLTGKPGQVLPHPELCTVRKDLHQNCPHCQVMYCSAECRLAATEQYHQVLCPGPSQDDPLHPLNKLQEAWRSIHYPPETASIMLMARMVATVKQAKDKDRWIRLFSQFCNKTANEEEEIVHKLLGDKFKGQLELLRRLFTEALYEEAVSQWFTPDGFRSLFALVGTNGQGIGTSSLSQWVHACDTLELKPQDREQLDAFIDQLYKDIEAATGEFLNCEGSGLFVLQSCCNHSCVPNAETSFPENNFLLHVTALEDIKPGEEICISYLDCCQRERSRHSRHKILRENYLFVCSCPKCLAEADEPNVTSEEEEEEEEEEEGEPEDAELGDEMTDV", "text": "FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 to form trimethylated histone H4 lysine 20 (H4K20me3) which represents a specific tag for epigenetic transcriptional repression (By similarity). In association with the NCoR corepressor complex, is involved in the repression of toll-like receptor 4 (TLR4)-target inflammatory genes in macrophages by catalyzing the formation of H4K20me3 at the gene promoters (By similarity). Plays an important role in embryonic stem (ES) cell self- renewal and differentiation (By similarity). Promotes ES cell maintenance by silencing differentiation genes through deposition of H4K20me3 marks (By similarity). Maintains genome stability of ES cells during differentiation through regulation of heterochromatin formation and repression of endogenous repetitive DNA elements by depositing H4K20me3 marks (PubMed:28951459). SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
+{"protein": "MAAASGVRRIKLGSQGLEVSAQGLGCMGLSIFDGTTKVETDLIALIHHAINSGITLLDTSDIYGPETNELLLGQALKDGMREKVELATKFGLLLKDQKLGYRGDPAYVRAACEASLRRLGVSCIDLYYQHRIDTTVPIEVTIGELKKLVEEGKIKYIGLSEACASTIRRAHAVHPLTAVQLEWSLWSRDVEEDIIPTCRELGIGIVAYSPLGLGFFAAGPKFIESMDNGDYRKGLPRFQQENLDHNKILYEKVNAMAEKKSCTPAQLALAWVHHQGNDVCPIPGTSKIKNLNQNIGALSVKLSIEEMAELDAMGHPDSVKGERSATYIVTYKNSETPPLSSWTS", "text": "SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MNSMSEYVKPRKNEFLRKFENFYFEIPFLSKLPPKVSVPIFSLISVNIVVWIVAAIVISLVNRSLFLSVLLSWTLGLRHALDADHITAIDNLTRRLLSTDKPMSTVGTWFSIGHSTVVLITCIVVAATSSKFADRWNNFQTIGGIIGTSVSMGLLLLLAIGNTVLLVRLSYWLWMYRKSGVTKDEGVTGFLARKMQRLFRLVDSPWKIYVLGFVFGLGFDTSTEVSLLGIATLQALKGTSIWAILLFPIVFLVGMCLVDTTDGALMYYAYSYSSGETNPYFSRLYYSIILTFVSVIAAFTIGIIQMLMLIISVHPMESTFWNGLNRLSDNYEIVGGCICGAFVLAGLFGISMHNYFKKKFTPPVQVGNDREDEVLEKNKELENVSKNSISVQISESEKVSYDTVDSKV", "text": "FUNCTION: High-affinity nickel transporter responsible for nickel uptake. Required for urease biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) family."}
+{"protein": "MSKCLQQLKRQLQHFGIDGCSLADGDIDYFFTVTGIDRGWGCGWRNIQMLISWLQYTNPNWFKRNFSSGNYEINSLQSLLLSAWMKGIDAEGYAQLGDNLHGKWIGATEVYSLFTGLFVNVALVDFDFRSEASASNALFLYVKKHFESSNDTSNVSPCYLQFQGHSIIIIGFCSSLETLVVLDPDRYQSVQKKFVNIADFNHCYMRKKRSLKFSQFQLVHFKQNIFLNDFSSKLEVRSTRISDF", "text": "FUNCTION: Deubiquitinase with endodeubiquitinase activity that preferentially cleaves 'Lys-48'-linked polyubiquitin chains (PubMed:29576528, PubMed:29476094). Shows only weak activity against 'Lys-63' and 'Lys-11'-linked chains (PubMed:29476094). Has a role in meiosis (PubMed:16303567). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C78 family. ZUFSP subfamily."}
+{"protein": "MSSSSYRDSYFQYRHLPAPHHILYAEWNQDILALPDEVANITMAMKDNTRTDAEEGRAPQDGERNSNVRESAQGKALMTSEQNSNRYWNSFHDEDDWNLFNGMELESNGVVTFAGQAFDHSLNGGTNSRNDGANEPRKETITGSIFDRRITQLAYARNNGWHELALPQSR", "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. SWM1 is required for APC/C activity in meiosis. SIMILARITY: Belongs to the APC13 family."}
+{"protein": "MDVNIAPLRAWDDFFPGSDRFARPDFRDISKWNNRVVSNLLYYQTNYLVVAAMMISVVGFLSPFNMILGGIVVVLVFTGFVWAAHNKDILRRMKKQYPTAFVMVVMLASYFLISLFGGVMVFVFGITFPLLLMFIHASLRLRNLKNKLENKMEEIGLKRTPMGIVLDALEQQEETITKFSDYISKMKE", "text": "FUNCTION: Regulates intracellular concentrations of taurine and glutamate. Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate in a PKC activity- dependent manner. Plays a role in the retention of SLC1A1/EAAC1 in the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Cytoplasm Cytoplasm, cytoskeleton Note=Also exists as a soluble form in the cytoplasm. Associated with microtubules. SIMILARITY: Belongs to the PRA1 family."}
+{"protein": "MKILIVDDFSTMRRIIKNLLRDLGFTNTAEADDGTTALPMLHSGNFDFLVTDWNMPGMTGIDLLRAVRADERLKHLPVLMVTAEAKRDQIIEAAQAGVNGYVVKPFTAQVLKEKIEKIFERVNG", "text": "FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheY is likely to be involved in changing the direction of flagellar rotation. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MKTKFTKKTVLKFFGILFAILLLSVLILFSVVIGRTFTFKVNRELGQWENTSTIYPYLSPEQREKLLDNFKVAVQIPTVSFSESDQNITALQEFDLLLRRVFPKVFSSSLVRHEVVGNYSHLFTVVGADAGLEPYMLLAHIDVVPANEAGGWDAPPFSAQEIDGFIYGRGTIDNKQSVMGILQALEYLLERGYTPRRTFYIGLGHDEEINGEEGAVKIVNLLKSRGVKLLYVLDEGLTIMDGVVDGLNEPAALIGVSEKGQTTVKLSVSTPPGHSSMPPRESSIGILASAVARLEKNRMPNLFGHGPERATFEHLAHKFGWSYRMIMSNLWLFSSLLSSVLEGQPDTNAFVRTTTAVTMFNSGVKINVMPAHAEAFVNFRIHSSQTVQGVLNRIESTVSDKRVKVEFINGFDPLPIGSYEDDTFGYQIIKKSVQDIFPQVTVTPGICVANTDSRHYTQLSPDIYRFAPSWYKPGDSARFHGVNERISIQNYEEIVLFYFQLMQNSDVRNLPTLRS", "text": "FUNCTION: Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase. It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction. Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure. PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M20A family."}
+{"protein": "MKFGGYFTKSVDDLKIDEELSKLIPENTMSDKIKNEIQKYGFLYPVIIDQNGFVIDGYTRVRIAKELGIKEVPVIVYIFDSPEERMRSAIQLNVIRRHLTHEQIEQLYQKYLSTGLSPKEAVKKLDKELKQENIRIKNLEPKMRAVEILQSEAPELFELLAKYQLDPQLLLQFYLSIKEFYDYFKQLPEEKKLEILRSERLLLQVEAEPALLKQFAEAEKFASSVTSVPTTEQEDNGDLESFYRGVDGNEEELIRSKEELNEALEQMGLGTEEEEAENQDEQLFSEFIEELKSGSVTAVPKSIEVYKKENGRLIKIEGEIYLKRKS", "text": "SIMILARITY: Belongs to the ParB family."}
+{"protein": "MALLAEHLLRPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVYDTNPTKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRFIQVFLQSICDGERDENHPNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKVRLFLVNYTATIDVIYEMYTRMNAELNYKV", "text": "FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides. FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GLTP family."}
+{"protein": "MALLATLLLSAALGALLSFALLAAAVASDYWYILEVADAGGLGGVQLFSHSGLWRTCEGQNSCVPLIDPFASAGLEVSPSVQHLLSLHRTVMVVLPLSLVLIVCGWVCGLLSSLSQSVPLLLATGCYFLLGGALTLAGLSIYISYSHLAFVEAARTYGVTHVQNVHISFGWSLALAWASCASEVLSGALLLAAARLLSLSQRPGVPHSVIL", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Endoplasmic reticulum. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family."}
+{"protein": "MVDIAEAMPTTASSLPSDEALRKFKCPECTKAFKFKHHLKEHIRIHSGEKPFECQQCHKRFSHSGSYSSHMSSKKCVQQASPSMVTPFNPYQLMMYRNIMLQLQTPQVSFLPSTAANNMDYMSLLQANLFQSLENGTSPTPTQEPSAPASPEPKIEVVDEPEVSSEVKTEVKTEVKTEDSVPEESITPAVSMSLSPAPEQNGNESMNNGGSGSDGKSSPDWRPLRSRSFLNDSQVAVLQNHFKRNPFPSKYELSAVAEQIGVNKRVVQVWFQNTRAKERRSNRLPSMPRGSVASAAAAAATSPTVWQTPVQLMAAWASQFSNGNNSLTASQDERNNENTDEVMDHDGLKDGKETPLDLTLSTDDTEPEWSPEKLIGFLDQTGGVIQELLRQAGNGFVTNQEDEEEKPIKAEESPVSSGSSSIWPSFIGQYPSILDSASLSVLEKALDQQKSSEDDASSLCSNESKLLKFPTTPLKEEEGLFSCDQCDKVFGKQSSLARHKYEHSGQRPYKCDICEKAFKHKHHLTEHKRLHSGEKPFQCDKCLKRFSHSGSYSQHMNHRYSYCKPYREQPASPSDVLNGGSVTVSPSSSNTPPPST", "text": "FUNCTION: Transcription factor (PubMed:12835394, PubMed:12835395, PubMed:25474681, PubMed:30291162). Down-regulates expression of genes involved in either the synthesis or reuptake of serotonin, dopamine and GABA (PubMed:12835394). Acts as a transcriptional repressor to regulate multiple, discrete, neuron-specific aspects of terminal differentiation, including cell migration, axonal development and gene expression (PubMed:12835394, PubMed:12835395, PubMed:25474681, PubMed:30291162). Promotes touch receptor neuron differentiation by repressing the expression of egl-44 and egl-46 (PubMed:30291162). As egl-44 and egl-46, probably acting as a heterodimer, repress expression of zag-1 in FLP neurons, together these proteins form a bistable, negative-feedback loop that regulates the choice between neuronal fates (PubMed:30291162). Required for axon guidance (PubMed:12835395). Involved in the proper development of the pharynx (PubMed:12835395). Required for pharynx isthmus peristalsis, probably via a role in the differentiation of the M4 cholinergic motor neuron (PubMed:25474681). Directly represses its own transcription by interacting with conserved E-box sequence motifs 5'-CACCTG-3' in its own promoter (PubMed:12835394, PubMed:12835395). May also act as a transcriptional activator of the homeodomain ceh-28 (PubMed:25474681). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MGYIPPPGDNDDNGKKSNKKTQNTSKPISSDSTPDGTTITIINPMSLIPRNPSFGLIWGPLTPASDNRPAMYTMVALQIAIGVRFFRYARTHLRRHPVPQAQFHAPPGLGVNSMISTTANQTYSAPPQQFLRRSKGDVFKSILAITTGSLLIFGSGLEIARMMLPYDPWYDEAQFYRKQAVRNGDKPNFWFGAYQYYQPMTYKEWHSKVSKWIDSVEKEIKVDETTFVIDKDGKARGGIGPAGVGYVNGAGQQSGAASAAAAVAKPLFQIRNRAKYQQIHAKLYNANETRMRELLANELNDTNVNELNKAERLDKILEGKSDLVNPNFNKPSISLGNHPMESDDEFEMVWLNFEPWDELKMETDYDIRLIPRYASVEELEQVDEGELFVVKKEELGETDNVVNESS", "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": "MELIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSMSGIIQPLTIYGPHGIREFVETALRISGSWTDYPLEIVEIGAGEIFDDGLRKVTAYPMEHPLECYGYRIEEHDKPGALNAQALKAAGVPPGPLFQELKAGKTIMLDDGRQINGADYLAVPVPGKALAIFGDTGPCDAALELAKGVDVMVHEATLDMAMEAKANSRGHSSTRQAAALAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFAVFSI", "text": "FUNCTION: Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities. SIMILARITY: Belongs to the RNase Z family. RNase BN subfamily."}
+{"protein": "MSTVGSSSEGRHSVRCFRHRNANTFLTYSKCPLEPEFIGEHLFRLTREYEPAYILVVRETHTDGTWHCHALLQCIKPCTTRDERYFDIDRYHGNIQSAKSTDKVREYILKDPKDKWEKGTYIPRKKSFVPPGKEPAEKKPTKDEVMREIMTHATSREEYLSLVQSSLPYDWATKLNYFEYSASRLFPDIAEPYTNPHPTTEYDLHCNETIEDWLKPNIYQVSPQAYKLLEPSCLSLEQAIADLEWLDDTTRMLQEKEREASTSAAQHGQVKHPGLEASDDTTTGKTISTGLHMMKKLSTMSLTTFPSSSVRAGNDSSAAKKTT", "text": "FUNCTION: Implicated in enhancement of V-sense gene expression. Acts a an inhibitor of C-sense gene transcription (By similarity). SUBCELLULAR LOCATION: Host nucleus Host cytoplasm. SIMILARITY: Belongs to the geminiviridae Rep protein family."}
+{"protein": "MEVFLEMLLTAVVALLFSFLLAKLVSVATVENDLSSDQPLKPEIGVGVTEDVRFGMKMDARVLESQRNFQVVDENVELVDRFLSEEADRVYEVDEAVTGNAKICGDREAESSAAASSENYVIAEEVILVRGQDEQSDSAEAESISSVSPENVVAEEIKSQGQEEVTELGRSGCVENEESGGDVLVAESEEVRVEKSSNMVEESDAEAENEEKTELTIEEDDDWEGIERSELEKAFAAAVNLLEESGKAEEIGAEAKMELFGLHKIATEGSCREAQPMAVMISARAKWNAWQKLGNMSQEEAMEQYLALVSKEIPGLTKAGHTVGKMSEMETSVGLPPNSGSLEDPTNLVTTGVDESSKNGIP", "text": "FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity. Can interact in vitro with arachidonyl-CoA, barely with oleoyl-CoA, but not with palmitoyl-CoA. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the ACBP family."}
+{"protein": "MATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILEIPGPGDNQHFGDLHQTELGPSGAGCQVGINQNGTGKLVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQQQCSKSYVDRHMESLSQSKSFRRRHNSWSSSSRHPNQATPKKSGLKNGQMKNKDDECFGDDIEEIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNERPTRYRHDENILESEPIVYRRITVPHNVSKEFCTDSGLVVPSISYELHKKLLSVAEKHGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRPTVALLCGPHVKGAQGIRCGRHLANHDVQVILFLPNFVKMLESITNELSLFSKTQGQQVSSLKDLPTSPVDLVINCLDCPENVFLRDQPWYKAAVAWANQNRAPVLSIDPPVHEVEQGIDAKWSLALGLPLPLGEHAGRIYLCDIGIPQQVFQEVGINYHSPFGCKFVIPLHSA", "text": "FUNCTION: Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping (By similarity). SUBCELLULAR LOCATION: Cytoplasm, P-body Note=Processing bodies (PB). SIMILARITY: Belongs to the EDC3 family."}
+{"protein": "MVKLTADLIWKSPHFFNAIKERELDLRGNKIPVIENLGATEDQFDTIDLSDNEIVKLENFPYLNRLGTLLINNNRITRINPNLGEFLPKLHSLVLTNNRLVNLVEIDPLASIPKLQYLSLLDNNITKKANYRLYVIHKLKSLRVLDFIKIKAKERAEAASLFSSKEAEEEVKKVSREEVKKVSETAENPETPKVVAPTAEQILAIKAAIINSQTIEEIARLEQALKFGQVPAGLIIPDPATNDSAPMEE", "text": "FUNCTION: This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the U2 small nuclear ribonucleoprotein A family."}
+{"protein": "MGISYSVDVDSEASAKAMLRERSISLKHSKAIAREISGETVADAKEYLQAVIDEERSVPFKQHNSGVGHRNDIDGWDAGRYPEKASKDFLKLLSNVSNNADQQGFDADEMVIEHVAPHKVGESQGRKPRAMGRATTWNATLCDVEIVVTETEEVTA", "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": "MKQFYIVDSSMLPEVVGKVIAARALLQNGEVKQVSEAVKQVGISRGTYYKYKDYVFLRDPEMASRKAVISLMLHHDRGILSEVLTTMSQVQASIVTINQNIPIHNWASVVMSFDISALQGTLDDLVTKLGDIRGVSDVHLVSVE", "text": "SIMILARITY: Belongs to the UPF0735 family."}
+{"protein": "MADLKRYWCDWALGPLSENPRMSQQQIFSPILWIPLLFLLMGLGASGKETPPTVISGMLGGSVTFSLNISKDAEIEHIIWNCPPKALALVFYKKDITILDKGYNGRLKVSEDGYSLYMSNLTKSDSGSYHAQINQKNVILTTNKEFTLHIYEKLQKPQIIVESVTPSDTDSCTFTLICTVKGTKDSVQYSWTREDTHLNTYDGSHTLRVSQSVCDPDLPYTCKAWNPVSQNSSQPVRIWQFCTGASRRKTAAGKTVVGILGEPVTLPLEFRATRATKNVVWVFNTSVISQERRGAATADSRRKPKGSEERRVRTSDQDQSLKISQLKMEDAGPYHAYVCSEASRDPSVRHFTLLVYKRLEKPSVTKSPVHMMNGICEVVLTCSVDGGGNNVTYTWMPLQNKAVMSQGKSHLNVSWESGEHLPNFTCTAHNPVSNSSSQFSSGTICSGPERNKRFWLLLLLVLLLLMLIGGYFILRKKKQCSSLATRYRQAEVPAEIPETPTGHGQFSVLSQRYEKLDMSAKTTRHQPTPTSDTSSESSATTEEDDEKTRMHSTANSRNQVYDLVTHQDIAHALAYEGQVEYEAITPYDKVDGSMDEEDMAYIQVSLNVQGETPLPQKKEDSNTIYCSVQKPKKTAQTPQQDAESPETPTYENFT", "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 (PubMed:19648922). May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T- cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Promotes recruitment of RORC to the IL-17 promoter (By similarity). May be involved in the maintenance of peripheral cell tolerance by serving as a negative regulator of the immune response. May disable autoantibody responses and inhibit IFN-gamma secretion by CD4(+) T- cells (PubMed:23914190). May negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells (PubMed:23225888). Can promote natural killer (NK) cell activation (PubMed:19648922). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell membrane."}
+{"protein": "MAELCRMDSTLTALDEEMLWDMLESHRCRIVQSICPSRLTPYLRQAKVLGQLDEEEILHSSRFTNSAMRVGHLLDLLKARGKNGAIAFLESLKFHNPDVYTLVTGLQSDIDFSTFSGLMETSKLTECLAGAISSLQEELAQEKAQKEVLLRRCQQLKERLGLAEAHAEGLRQLEVDHSRMKREVSTHFHEVLKLKDEMLNLSLHYSNALREKELAATRCHSLQEELYLVKQELQRASLVSSCERESRERSLKMASNLEPQGEELNRLKEENEKLRSMTFSLVEKDILEQSLDEARESKQELVDRIHSLRERAVAAERQQKQYWEEKEQTLLQFRKTQVDCELYKEKMTMLQGQVAELQKERDQAYTARDRAQMEISQRLVEKDALRRRVFELTEQVCELRTQLRRLQAEAPGGPKQEAGARELCLRGKQRLVRMHAVCPPDDSDCSLLSSTESRLWWDLNSTSSREQMDSFRSSSPMPPSQQSLYKRVAEDFLEDPESLSFPEVLEMRLQGATVDDTDTDLEFEMIDGADLSQTEDSLQGSSRSLNVSESSVPVRRRPARKILSQVTVLAFQGDALLEQIGVIGGNLTGIFIHRVTPGSAADEMALRPGTQIMMVDYKPTKPSLRATLENTTLEQAVGLLRRVNGSCYLSVKINTEGYKNLIQDLDAKVVTSGDSFYIRVNLAMQRGGDGELQTHCNDILHVTDTMFQGRSCWHAHHVNPYTMKDMEPGTIPNYSQAQQQLLALIQDMTQRCTVPRKPPGGPQKLVRIVSVDKAAVSPLTSSFDQSQWDSGKEEGGPSVCFWSESCFTLAPYTLVHPHRPARPRPVLFVPRLVGRILGKKLCLLQGFKQCSAEYLSQEEYATWSQRGDIIQEGESIGDHHWITRHAVESLMNMSTHALLDVRLDSVRVLHRMDMFPIIIHVSVNEKTAKKLRKGLHRLGSSEEQFLEVARQEEGELDRVPCLYSSLAPDSWSDLDSLLSCVRLAIADEQKKVVWTESPC", "text": "FUNCTION: Acts as a scaffolding protein that can activate the inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase signaling pathways. Forms a signaling complex with BCL10 and MALT1, and activates MALT1 proteolytic activity and inflammatory gene expression. MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and p38/JNK MAP kinases. May play a role in signaling mediated by TRAF2, TRAF3 and TRAF6 and protects cells against apoptosis. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MEKIEKIIEFEIARINSHLPRARRSLKELLEMKEAKVTLRDGSEHYFKREELKLLANLLDEDEISKLKLPIVIEISTLERDKIMIRGRVEVKVIKKVLGLEEGYLEENVLKLPRYYLAEIRRKLPTTTVHAFIVEW", "text": "SIMILARITY: Belongs to the UPF0216 family."}
+{"protein": "MTMRIDTDKQMNLLSDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHKGSGQEAMKKAGLLQTYYDLALPMGVNIADEKGNILSTKNVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGGMSKVRKFVTDTEVEETGTFNIQADIHQPEINCPGFFQLCNGNRLMASHQGNLLFANPNNNGALHFGISFKTPDEWKNQTQVDFQNRNSVVDFLLKEFSDWDERYKELIHTTLSFVGLATRIFPLEKPWKSKRPLPITMIGDAAHLMPPFAGQGVNSGLVDALILSDNLADGKFNSIEEAVKNYEQQMFIYGKEAQEESTQNEIEMFKPDFTFQQLLNV", "text": "FUNCTION: An FAD-requiring monooxygenase active on tetracycline antibiotic derivatives, which leads to their inactivation (PubMed:15452119, PubMed:16128584). Hydroxylates carbon 11a of oxytetracycline and tigecycline (PubMed:15452119, PubMed:26097034). Acts on many tetracycline analogs (chlorotetracycline, demeclocycline, doxycycline, minocycline, oxytetracyclinee), probably by monooxygenization (PubMed:15452119, PubMed:16128584). Tigecycline, a new generation tetracycline antibiotic, is rendered less effective against E.coli by this monooxygenation, is much weaker at inhibiting translation in vitro and binds Mg(2+) considerably less well (PubMed:16128584, PubMed:26097034). Expression in E.coli BW25113 reduces its growth rate about 5%. The reaction probably proceeds by FAD reduction by NADPH and, second, hydroxylation of antibiotic in a ping- pong mechanism (PubMed:23236139). Degrades chlortetracycline, probably by monooxygenation (PubMed:15452119, PubMed:28481346). Slowly oxidizes anhydrotetracycline, the final substrate in tetracycline biosynthesis (PubMed:26097034). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aromatic-ring hydroxylase family. TetX subfamily."}
+{"protein": "MVKFNSSRKSGKSKKTIRKLTAPETVKQNKPQKVFEKCFMRGRYMLSTVLILLGLCALVARAAYVQSINADTLSNEADKRSLRKDEVLSVRGSILDRNGQLLSVSVPMSAIVADPKTMLKENSLADKERIAALAEELGMTENDLVKKIEKNSKSGYLYLARQVELSKANYIRRLKIKGIILETEHRRFYPRVEEAAHVVGYTDIDGNGIEGIEKSFNSLLVGKDGSRTVRKDKRGNIVAHISDEKKYDAQDVTLSIDEKLQSMVYREIKKAVSENNAESGTAVLVDVRTGEVLAMATAPSYNPNNRVGVKSELMRNRAITDTFEPGSTVKPFVVLTALQRGVVKRDEIIDTTSFKLSGKEIVDVAPRAQQTLDEILMNSSNRGVSRLALRMPPSALMETYQNAGLSKPTDLGLIGEQVGILNANRKRWADIERATVAYGYGITATPLQIARAYATLGSFGVYRPLSITKVDPPVIGKRVFSEKITKDIVGILEKVAIKNKRAMVEGYRVGVKTGTARKIENGHYVNKYVAFTAGIAPISDPRYALVVLINDPKAGEYYGGAVSAPVFSNIMGYALRANAIPQDAEAAENTTTKSAKRIVYIGEHKNQKVN", "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": "MIDQNHDSEEQAQMQKLTRTVTLTVALTLVSGCSYFGVYKRDLAQGNLVTSAMAEQLQPGMTRQQVVNLMGSPMLEAPFDAQQWDYVYRLDKAYGGVEQRRLTLTFQGNRLADIDRHGDFSRPPSVADERGIGPTDSTNARGNLLNARPDDE", "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 BamE family."}
+{"protein": "MTASTRNGSPSPSPAAPTATEQESKSMTTTPANPPETKSQTNGKGSGTAQSSQKPASTSANAKDPLRPRRKKAKRACFACQRAHLTCGDERPCQRCIKRGLQDACHDGVRKKAKYLHDAPNEALLPGIRGNYYNQANTTRNIPNQRGNASNSNSNKVSRQSVSSANFYTPQAARSYNVYVQAKSQQSHVRPAVMQDASMNPSVFHAQSPSSTQNFDLSSNPQTQNLSSAMSQTASSVSGQNQDPFGAAFFDPSHPALFNFDIASMNFGNRYGALEFGMLGHMATGAGDTPPSDSATQRGSIGRSSGTFTAQNFGDSANNQSPFLFGDPVLNDWNPTGQGQANPRNIYNQNAVAGQMGEQNPHAFAIESAPMNFASPSSTESPQMTTTTPFDEANANFSSRTNLMHPTNTPQQSRISTPGLKHQGLHVGVKRRYRSPSSIYESVKEPYSYTSGFHSLTAFIQRRFSPQKTLQIAKALASIRPSFIATTKTLNQDDLIFMEKCFQRTLWEYEDFINACGTPTIVCRRTGEIAAVGKEFSILTGWKKEVLLGKEPNLNVNTGSSLSSASSVRGSSTFTPRNNNTHNSIDPHTGMPTVGGGGASGRTQPVFLAELLDDDSVIEFYEDFAKLAFGDSRGSVMTTCKLLKYKTKEDSAALFHGKEETQQGGVDGSSGTGTTTSGDVATTTATGTSTSNGANANTNGNNTNPNDPSSAASSSASSALQGPQQSPRQTWGKRGIAGEAGMNQLGFRDGKVECSYCWTVKRDVFDIPMLIVMNFLPCI", "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": "MALLAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVYDTNPAKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRFIQVFLQSICDGERDENHPNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKIRLFLVNYTATIDVIYEMYTQMNAELNYKV", "text": "FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides. FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GLTP family."}
+{"protein": "MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIRVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKCGVPWLYRFELMGTQRDIDNVRKGVNEFWQQLPRSA", "text": "FUNCTION: Probably involved in ribonucleotide reductase function. SIMILARITY: Belongs to the NrdI family."}
+{"protein": "MSEIIQDLSLEDVLGDRFGRYSKYIIQERALPDVRDGLKPVQRRILYAMYSSGNTHDKNFRKSAKTVGDVIGQYHPHGDSSVYEAMVRLSQDWKLRHVLIEMHGNNGSIDNDPPAAMRYTEAKLSLLAEELLRDINKETVSFIPNYDDTTLEPMVLPSRFPNLLVNGSTGISAGYATDIPPHNLAEVIQATLKYIDNPDITVNQLMKYIKGPDFPTGGIIQGIDGIKKAYESGKGRIIVRSKVEEETLRNGRKQLIITEIPYEVNKSSLVKRIDELRADKKVDGIVEVRDETDRTGLRIAIELKKDVNSESIKNYLYKNSDLQISYNFNMVAISDGRPKLMGIRQIIDSYLNHQIEVVANRTKFELDNAEKRMHIVEGLIKALSILDKVIELIRSSKNKRDAKENLIEVYEFTEEQAEAIVMLQLYRLTNTDIVALEGEHKELEALIKQLRHILDNHDALLNVIKEELNEIKKKFKSERLSLIEAEIEEIKIDKEVMVPSEEVILSMTRHGYIKRTSIRSFNASGVEDIGLKDGDSLLKHQEVNTQDTVLVFTNKGRYLFIPVHKLADIRWKELGQHVSQIVPIEEDEVVINVFNEKDFNTDAFYVFATQNGMIKKSTVPLFKTTRFNKPLIATKVKENDDLISVMRFEKDQLITVITNKGMSLTYNTSELSDTGLRAAGVKSINLKAEDFVVMTEGVSENDTILMATQRGSLKRISFKILQVAKRAQRGITLLKELKKNPHRIVAAHVVTGEHSQYTLYSKSNEEHGLINDIHKSEQYTNGSFIVDTDDFGEVIDMYIS", "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. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 2 subfamily."}
+{"protein": "MVNWQVIGQLVSTGAIMLLGPAIIILLALKKGNL", "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": "MIRTNFLLKQGRRHESKDKSSKRHKSEEHNDKEHSSDKGRERLNSSENGEDRHKRKERKSSRGRSHSRSRSRERRHRSRSRERKKSRSRSRDRKKSRSRSRDRKKSRSRSRDRKRRIRTRSRSRSRHRHRTRSRSRSRSRSRDRKKRIEKPRRFSRSLSRTPSPPPFRGRNTAMDAQEALARRLERAKKLQEQREKEMVEKQKQQEMAAAAAATGGSVLNVAALLASGTQVTPQIAMAAQMAALQAKALAETGIAVPSYYNPAAVNPMKFAEQEKKRKMLWQGKKEGDKSQSAEIWEKLNFGNKDQNVKFRKLMGIKSEDEAGCSSVDEESYKTLKQQEEVFRNLDAQYEMARSQTHTQRGMGLGFTSSMRGMDTV", "text": "SIMILARITY: Belongs to the RSRC2 family."}
+{"protein": "MTVAISNPAAPPVSARAYLSVIGGTCALLCTVGFVVAFGVFQGYYTEHLLRGMSEFDIPWIGSASIFLLYVSAPICGVLVDRFGPKVLLIAGSIGVLVAIFMISLCSQYYQIFLAQAVLLGISMGFVTWPPFAVVSRNLPHHRGLALGVITGGSSVGGIVWSIMIEELLTKRNLGFPWTVRVLGFTMLPLLAFACISITEPPKQSQPQPRPALEATVEGGSASPTPKPEYASLPLLRSTVFISICVGFGLAFLGLFNPFFYISSYAAGHGASAQTSSYMISIMNAATLFGRVIPGIVADRVGHYNVMIFVLLASGITSFCWTEVRSLTGLVIWSIAYGFSSGAILSLQGACAGKIATPQNQGKAIGFLQGSLAVTVLVGSPIGGQLLGHYGYLSLSMFTGATLVMGAVVMGYARLCLNRSPMEAHQFRFLLAPN", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor (PubMed:32083553). May be involved in the secretion of fumigermin (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
+{"protein": "MVRLNSAAGSRWWAPAMAILAVALSVEAAEVARYDNYRLYRVTPHSEAQLRSVAAMEQASDSLIFLETARKLGDRFDIVVAPHKLADFTETLESDYIPHELIEQNVQRAFDEERVRLTNKRAKGPFDWNDYHTLEEIHAWLDQLASEHPKEVELLDAGRSHQNRTMKGVKLSYGPGRPGVFLEGGIHAREWISPATVTYILNQLLTSEDAKVRALAEKFDWYVFPNANPDGYAYTFQVNRLWRKTRKAYGPFCYGADPNRNWDFHWAEQGTSNNACSDTYHGSEAFSEVETRSLAAFVEKLRGKLGAYIAFHSYSQLLLFPYGHTGEHSPNHQDLNEIAEATVKSLAKRYGTQYKYGNVYDAIYPASGSSVDWSYGAQDVKIAYTYELRPDGDAWNGFVLPPNEIVPTGEETLDSLITLLEESSARGYYDEKH", "text": "FUNCTION: Involved in the digestion of the blood meal. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M14 family."}
+{"protein": "MWNQKHDLESAQTPLYPMMSESPELRWSFIRKVYSIISIQLLVTIAVAATVVKVHSISVFFTTTTAGFALYILLILTPLIVMCPLYYYHQKHPVNYLLLGIFTVALAFAVGLTCAFTSGKVILESVILTAVVVISLTLYTFWAAKRGHDFNFLGPFLFGAVIVLMVFSFIQILFPLGKISVMIYGCLASIIFCGYIVYDTDNLIKRHSYDEYIWAAVSLYLDVINLFLSLLTLLRAVDS", "text": "FUNCTION: (Microbial infection) May prevent cell death upon A.alternata f.sp. lycopersici (AAL) toxin treatment. FUNCTION: (Microbial infection) Facilitates the development of the powdery mildew fungus E.cruciferarum. FUNCTION: Regulates the brassinosteroid (BR) signaling pathway that mediates cell elongation and organ morphogenesis (PubMed:19202280). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BI1 family."}
+{"protein": "MESSNDFSNKDSDTVSLSPVEFSNYQCEINPGFHEFLKKSGFEDVGFRFNVVTILGSQSSGKSHLLNSLFNASFQTMDASRGHSQTTKGIWGSLVLPKDTSVSATVVFDSEGTDSRERGEGRLTFEHRSSLFCLALSDVVIVNLWYNSMGNLTGSNYGLLKTVVEANLELVDTNNEENYKTVLFFCVRDWSPSLSPLNVVKDYVLNNYMRSIWNEISKPARFENMGVESLFEIRVFGLSNAVTQPELFEKDVKEVKKTWESLKPKEYSRRVPSDGFFVYSKNVWKTIIEQNHLDIPTQKEMLSSYRCSEIKTAILESATTSVPELTETDFSEYLMSLLNKVESEYFSQASRYDPKVSEKVGKELLSQLCGKFQPCFESALAGYVKKLAVESSSLLDKEFTVNSSGKELKVANARPYTVWPSFSKKCEELQSKQSEKLSEHLSRFKVSFNKTVSFEYEFDAQPLKDHLNLLVSTEFEVLRSRHLGLLKQQLDSMCNSTFVMVKNNLLDRSLTEDEFWDYFDELFDETHKNCMDQLTTSYQGLVNRASKAEFAQLSLVLLLKAARHNFDELQNNLEQLLLERFDKFFNYQEFKGELVPTEWHKQSAQELNNRYKESKEDALTLLKVLKKTKTKKMPSFDLNDVKKNQYFYSTLGEPVSDKYSTPVTEQFALEVTNSCSKKFLEMYKNAQVVQNAGTSISSWRNIPPIFWLVLLVLGWNELRSVFKVLLRFYVVIPLLIVFYFTFSYSATKLLGPKADQYVKPVRDKVLSLFTALLAWFVRTLHMIASKSSSFKQRPAT", "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": "MFVLPGYDAFLGFLLIAAAVPVLALVTNKLLAPRSQDGERQLTYESGMEPIGGAWIQFNIRYYMFALVFVIFDVETVFLYPWAVAFHRLGLLAFIEALIFIAILVVALAYAWRKGALEWS", "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 subunit 3 family."}
+{"protein": "MRCHYFVLLAVAAFLAGANVAVATTDAQLSDARAVRASFNTKRALRSHTKATDHGEERAYKPSLSVVESLNNWMQRASKNILPDDVILVMASKAMTKKTSSSDAVFAMLQLDQGLKGILSNPNLKQFAYYLVLTEKAPSQALITKLISQYGDDVVAKYLFDIKHKAINVSEKLKAEARFWQGAQYVKWFDEGVTPALVRQKYNVHPETWYKNPYEGVYWEYTGVYAKLASKSNKPLPVEV", "text": "FUNCTION: Effector that enhances P.infestans colonization of Nicotiana benthamiana leaves. SUBCELLULAR LOCATION: Secreted Host cytoplasm Host nucleus Host nucleus, host nucleolus. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSIMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTMKAQKELEEQTRKALELDQERKRAKEEAERLEKERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMSAPPPPPPPPVVPPTENEHDEHDENNAEASAELSNDGVMNHRSEEERVTETQKNERVNKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM", "text": "FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell projection, microvillus Note=Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively."}
+{"protein": "MNMEGPLRPRLVNCSDFQFGVVTTETIENALLHLAQQNEQAVKEAAGRTGSFRETRIVEFVFLLSEQWCLEKSVSYQAVEILERFMLKQAEDICRQATLQLRGKDTELQSWRAMKEQLVNKFILRLVSCVQLASKLSFHYKIVSNITVLNFLQALGYVHTKEELLESELDILKSLNFQINLPTPLAYVEMLLEVLGYNGCLVPATQLHATCLTLLDLVYLLHEPIYESLLRASIENSTPSQLQGEKFLSVKEDFMLLAVGIIAASAFIQNHECWSQVIGHLQSITGIASESIAEFSYAILTHSVGANTPGPQQPVPHKAARALRTAAAAASSNT", "text": "FUNCTION: Plays a role in the different steps of crossover formation during meiotic recombination (PubMed:24891606, PubMed:32640224, PubMed:32555348). Participates in the crossover differentiation step of crossover-specific recombination intermediates through its interaction with PRR19 (PubMed:32555348). In addition, stimulates crossover formation through the interactions with RFC3 and RFC4 and simultaneously regulates cell-cycle progression through interactions with CDC34 and subsequent ubiquitination of WEE1 (PubMed:32640224). May also participates in an active deselection process that destabilizes or removes excess pre-CO intermediates (PubMed:24891606). SUBCELLULAR LOCATION: Nucleus Cytoplasm Chromosome Note=Shuttles between the nucleus and cytoplasm in a stage-specific manner of prophase I cells (PubMed:32640224). Co-localized at crossover sites with PRR19 (PubMed:32555348)."}
+{"protein": "MKFARSGAAVSLLAAGTLVLTACGGGTNSSSSGAGGTSGSVHCGGKKELHSSGSTAQENAMEQFVYAYVRSCPGYTLDYNANGSGAGVTQFLNNETDFAGSDVPLNPSTGQPDRAAERCGSPAWDLPTVFGPIAITYNIKGVSTLNLDGPTTAKIFNGTITVWNDPQIQALNSGTDLPPTPISVIFRSDKSGTSDNFQKYLDGASNGAWGKGASETFNGGVGVGASGNNGTSALLQTTDGSITYNEWSFAVGKQLNMAQIITSAGPDPVAITTESVGKTIAGAKIMGQGNDLVLDTSSFYRPTQPGSYPIVLATYEIVCSKYPDATTGTAVRAFMQAAIGPGQEGLDQYGSIPLPKSFQAKLAAAVNAIS", "text": "FUNCTION: Functions in inorganic phosphate uptake, a phosphate-binding protein, although probably not the main uptake protein under phosphate starvation (By similarity). Part of the ABC transporter complex PstSACB involved in phosphate import (Probable). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Secreted Note=Present on the cell surface. SIMILARITY: Belongs to the PstS family."}
+{"protein": "MASLSGPISPTNLEMFKPGVEELNPSKLLLLSNHQEGMLYPTILGSLELLSFKRERSLNLQRDKVCLLHQESQLLKLRGTGTDTTDVPLKQPMATSVNCCHDGIFTILEQDRMPKTSMAPTLTESSGSLVTRLMSIPRLTFSIGTQVAMRLFRLGFRLARYSLRVTILKAQEGLLLIPDLLHAHPVEPLVQDRAVEPILAIEPLPLV", "text": "FUNCTION: Structural protein that is not essential for the viral replication either in tissue culture or in its natural host. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the coronavirus I protein family."}
+{"protein": "MTGAWGHLLRSLHLKTLSLWIPKTCFSLKARAFWTSVTRCGLHTKPSMPPCDFTPERYQSLAYSRVLEIHKQHLSPVHTAYFPEPLLLHQGHVEWLFDHEGNRYLDFFSGIVTVSVGHCHPKVNAAAQRQLGRLWHTSSVFFHPLIHEYAEKLSALLPEPLKVVFLVNSGSEANDLAMLMARAHSNSTDIISFRGAYHGCSPYTLGLTNVGIYKMDLPHGMGCQPTMCPDIFHGPWGGSHCRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPKGFLKEAFELVRERGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAVVTTPDIAKSLTKRMLHFNTFGGNPMACAVGSAVLEVIKEENLQENSQEVGTYMLLKLAKLRDEFEIVGDVRGKGLMIGIEMVKDKESRQPLPREEVNQIHHDCKCMGLLIGRGGLFSQTFRIAPSMCITKPEVDFAVEVFRSALIQHMERRAK", "text": "FUNCTION: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MDTKDFKRLEKMYSPRYLPGLDGLRAFAVIGIIIYHLNAQWLSGGFLGVDTFFVISGYLITSLLISEYYRTQKIDLLEFWKRRLKRLIPAVLFLICVVLTFTLIFKPELIIQMKRDAIAAIFYVSNWWYISQNVDYFNQFAIEPLKHLWSLAIEEQFYLLFPLVITFLLHRFKPRNIIQTLFIVSLISLGLMIVIHFITGDNSRVYFGTDTRLQTLLLGCILAFIWPPFALKKDISKKIVVSLDIIGISGFAVLMTLFFIVGDQDQWIYNGGFYIISFATLFIIAIAVHPSSLFAKFLSMKPLLIIGKRSYSLYLWHYPIIVFVNSYYVQGQIPVYVYIIEILLTALMAEISYRFIETPIRKKGFKAFAFLPKKKGQFARTVLVILLLVPSIVVLSGQFDALGKQHEAEKKEKKTEFKTTKKKVVKKDKQEDKQTANSKEDIKKSSPLLIGDSVMVDIGNVFTKKIPNAQIDGKVGRQLVDATPIVKSQYKDYAKKGQKVVVELGTNGAFTKDQLNELLDSFGKADIYLVSIRVPRDYEGRINKLIYEAAEKRSNVHLVDWYKASAGHPEYFAYDGIHLEYAGSKALTDLIVKTMETHATNKK", "text": "FUNCTION: Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan (PubMed:15661003, PubMed:32350117). O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance (PubMed:15661003). FUNCTION: Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acyltransferase 3 family."}
+{"protein": "MEEHYYVSIDIGSSSVKTIVGEKFHNGINVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPIIGTEVYDESNEIDFYEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHSLKVEAGVIAIQKSILINMIKCVEACGVDVLDVYSDAYNYGSILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQGLNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEARVEEIFFEVFDVLQDLGLTKVNGGFIVTGGSANLLGVKELLSDMVSEKVRIHTPSQMGIRKPEFSSAISTISSSIAFDELLDYVTINYHDNEETEEDVIDVKDKDNESKLGGFDWFKRKTNKKDTHENEVESSDEEIYQSEDNHQEHKQNHEHVQDKDKEESKFKKLMKSLFE", "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": "MKLTIIRLEKFSDQDRIDLQKIWPEYSPSSLQVDDNHRIYAARFNERLLAAVRVTLSGTEGALDSLRVREVTRRRGVGQYLLEEVLRNNPGVSCWWMADAGVEDRGVMTAFMQALGFTAQQGGWEKC", "text": "FUNCTION: Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD (PubMed:23170229, PubMed:25910242). Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA (PubMed:25910242). SIMILARITY: Belongs to the PanZ/PanM family."}
+{"protein": "MTDVTIKALASEIQTSVDRLIQQFADAGIRKSADDSVTAQEKQTLLTHLNREHGSAPDKLTLQRKTRSTLNIPGTGGKSKSVQIEVRKKRTFVKRDPQEAERLAAEEQAQREAEEQARREAEEAAKREAQLKAEREAAEQAKRELADKAKREAAEKDKVSNQQTDDMTKTAQAEKQRRENEAAELKRKSEEEARRKLEEEARRVAEEARRMAQENEKNWTEAPETPEETTDYHVTTSQHARQAEDDNDREVEGGRGRGRNAKAARPAKKGNKHAESKADREEARAAVRGGKGGKHRKGSALQQGFQKPAQAVNRDVIIGETITVGDLANKMAVKGSQVIKAMMKLGAMATINQVIDQETAQLVAEEMGHKVILRRENELEEAVMSDRDTGAAAEPRAPVVTIMGHVDHGKTSLLDYIRSTKVASGEAGGITQHIGAYHVETDNGMITFLDTPGHAAFTSMRARGAQATDIVVLVVAADDGVMPQTIEAIQHAKAAQVPLVVAVNKIDKPEADLDRVKNELSQYGVMPEEWGGEAQFIPVSAKAGTGIDDLLNAILLQAEVLELKAVRNGMASGAVIESFLDKGRGPVATVLVREGTLHKGDIVLCGFEYGRVRAMRNELGQEVLEAGPSIPVEILGLSGVPAAGDEVTVVRDEKKAREVALYRQGKFREVKLARQQKSKLENMFANMTEGEVHEVNIVLKADVQGSVEAISDSLLKLSTDEVKVKIIGSGVGGITETDATLAAASNAILVGFNVRADASARKVIDAESLDLRYYSVIYHLIDEVKAAMSGMLSPELKQQIIGLAEVRDVFKSPKFGAIAGCMVTEGTIKRHNPIRVLRDNVVIYEGELESLRRFKDDVNEVRNGMECGIGVKNYNDVRVGDMIEVFEIIEIQRTID", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily."}
+{"protein": "MEKDIKRQIQILEIITSEEKWFTTIEISKILRCCNKTIMKDISFIKDFLPEDWHIKIKKGKGVRIYLPYNKHRNEITFLLFRESLTFRILQHLFERETKTIATLAERLYIQVPSILPALKRVENYLKKFGLKLRKKPLRLEGDEVRIMIMYLDLYLKSYNDTEWPFEKLKKEVIFQYLGTLEESLGISLHVVSKRHLSFFIAILLKRKQQGYKVQLNRKFLYFNTETPDYVKIGRIFEKLEREFGVSLTVQDKILLTISIKSSKYVYKDINKEKEESVQYFKEGNLSIYELVKDFINSLEEKLKVDLISDEEFIFALVDYFKRTIYHLQYLCMFERPQKQTIQYMQTEHSETFSAVKEVYTEFVKKNEIADYVSVEEIAKVTMYIEASRLRYTSNYKKVLLVTGESESWAEYLAATLAKRFGDKIQISTVFFAKKSDHDVNADFIISTIPLDLGSTPIICINSIPTERDYTNIQYYLDLQDG", "text": "FUNCTION: AcpB and AcpA regulate cap gene expression and capsule synthesis. SIMILARITY: Belongs to the AtxA/AcpA family."}
+{"protein": "MFTNTPVGGKRERQNGAHPAWSTLGANSAQIHQNTADLASKMHKLRYTKIRSPPTRVSIESITPKQRFPAPNFEQAYHSNIRYEQEESDNEEFENVVKNGHEASTNVFYESDGDDEEFVNEEYENSIDEESDDEGYSLNEDTTATNASFRYPMNQRSTRKSQFYSSKFKPLLWFGITLFSTLLIITLLHKGQEFYSRSFSSDNSQPSNSPVPNIPPASNDTKTSLKPDIIKDFTDSPSKVGGNEEFDYSTGDLITKKEFDKILQQKVEQLKQSLKEEMSNYKSSVPFEVELNDDWKFFIESTVRKYLTDPVSMPNFALLSTGAEVLPALTSKRYVRRPSAFIPRFTSYFFDSLVVRGHEPSIALTPNNAVAMCWSFQGSEGQLGISLSRPVYVTNVTIEHVQHKIAHDLSSAPKDFELWVQGMSSKMFVLLGKARYSLTEDSIQTFSFESSNYIVAEPIQNVILKIKSNWGNPNYTCLYQVRVHGTVPNADEQPIPSLGEKAESTAENTGQDSS", "text": "FUNCTION: Associates with the spindle pole body and maintains a functional interface between the nuclear membrane and the microtubule motor proteins. Involved in chromosome segregation during meiosis where it associates with the telomeres. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane; Single-pass membrane protein."}
+{"protein": "MNLKPQNNLLTNENIDHVDIPENDIPMSITEHLEELRQRTLFVFLFFLFATTISFTQIKIIVAILQAPAVGIKFLQLAPGEYFFSSIKVAIYCGIVATTPFAVYQVILYILPGLTGKERKIILPLLISSVLLFITGGIFAYFVLAPAALTFLISYGSDIVEPLWSFEQYFDFILLLLLSTGLAFEIPIIQLLLGVSGTFSSSQMIRAWRYIIIIATIAGAILTPSTDPVTQLIMSSAVLLLYFGGIVILLVLKK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family."}
+{"protein": "HLLQFNKVIKFETRKNAIPFYAFYGCYCGWGGRG", "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 II subfamily."}
+{"protein": "MLQIGEDVDYLLIPREVRLAGGVWRVISKPATKEAEFRERLIQFLQEEGRTLEDVARIIEKSTPHPPQPRKRTKELRVRRVPQMVTPPLRLVVGTYDSSNGSDSELSDFDTSKVKGNRSSSGRTRKVRKMPVSYLGSKFLGSDVESEDDQELVEAFLRRGEKPSAPPPRRRVNLPVPMFENNLGPQPSKADRWREYVSQVSWGKLKQRVKGWAPRSGSEVGQTQQASTAAERAGEMRHSQASSDDDSSRNTGDRSDQMLGTRRWKPKIKWVSLRRCRKEQVPPFAQGTGMPAEEHPEAAENQGAEAAANQRAEPLASPRAEAAASPRAETAADPRVEAVASPRAEAAASPRAEAVADPRAEAAASPRAEAAASPRTEAAASLRAEAVASPRAEAAASPRAEAAADPRAEAAASPIAEAAANQKAELVDSPRAETAADPRAEAAASPRAEAVADPRVEAAASPIAEAAANQKAELVDSPRAETAADPRAEAAASPRAEAAADPRAEVAASPRAEAAASPRAEAEASPRAEAAASPKAEAEANLRVEAAAYLRAGVPPDQRAEAIDSQRAEGPANQRTGATENQRVEVLADQRAGVLHDQREEAGPQGIQEASAGSGSRAQKQVKTVRFQTPGRFSWFRMRRRVFWHTPRLPTLPRRVPRAGEARSLRVLRADIRADVEHREQEEQL", "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": "MADITVVNDTGELYNVINQKKSEGYLESELTIISKSKLHLNDLHDSEISLISTSGTFSDKMTKLLTGEDGEHAVLSRYNLAPDELEKYKQLILDDKMLVVGVRDHSSHQEVLENNSAYEEVDITHFAEASKGPKA", "text": "SIMILARITY: Belongs to the UPF0355 family."}
+{"protein": "MDDFSATHINYTLSIHLSGIFFAWHRHFVWLWERTLREECGYNGYQPYWDWALSANNISASPIFDGSPTSLSGNGDPINQEPFLQLEPTNITIPTGTGGGCVTNGPFANMTLNLPDLSMAGDEEFPSNAFDYKPHCFTRNLNSHMSSAFTSQADVDRLLNSPSITDLQANIDFSAWPELREARILGPHAAAHMSLGRTMDDFWTAPQDPSFMLHHAQVDRIWSLWQARGPESRRWALNGTSTINNRPTSPEVTLDTELVWGSLSESKTMREVMSTEAYHFCYEYGA", "text": "FUNCTION: Oxidase; 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 tyrosinase family."}
+{"protein": "MSQRQPQSPNQTLISITNDTETSSSAVSNDTTPKGWTGDNSPGIEALCAIYITYAVIISVGILGNAILIKVFFKTKSMQTVPNIFITSLAFGDLLLLLTCVPVDATHYLAEGWLFGKVGCKVLSFIRLTSVGVSVFTLTILSADRYKAVVKPLERQPSNAILKTCAKAGGIWIMAMIFALPEAIFSNVYTFQDPNRNVTFESCNSYPISERLLQEIHSLLCFLVFYIIPLSIISVYYSLIARTLYKSTLNIPTEEQSHARKQIESRKRIAKTVLVLVALFALCWLPNHLLYLYHSFTYESYAEPSDVPFVVTIFSRVLAFSNSCVNPFALYWLSKTFQKHFKAQLCCFKAEQPEPPLGDTPLNNLTVMGRVPATGSAHVSEISVTLFSGSTAKKGEDKV", "text": "FUNCTION: Role in sperm cell division, maturation, or function. 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": "MLQPNMPAPNFSGQAVVGKEFETISLSDYKGKWVILAFYPLDFTFVCPTEIIAISDQMEQFAQRNCAVIFCSTDSVYSHLQWTKMDRKVGGIGQLNFPLLADKNMSVSRAFGVLDEEQGNTYRGNFLIDPKGVLRQITVNDDPVGRSVEEALRLLDAFIFHEEHGEVCPANWKPKSKTIVPTPDGSKAYFSSAN", "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. FUNCTION: Antioxidant. Could be involved in protection against reactive oxygen species (ROS) generated by metabolic processes and/or protection of the parasite against ROS released by immune effector cells. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily."}
+{"protein": "MDNKRHQTSIGSELSEAQNRLSTVGMRIRQRIDRGYAYSGKNVSGMDDQVPIRDVASTIVPQFRTQVLYEQQQQPQQMHRPAMNGPAPMLVNQRTESSNLDCMQEEMLSNGKRRVF", "text": "FUNCTION: Mediates the nuclear localization of the ribonucleotide reductase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DIF1/spd1 family."}
+{"protein": "MARRWSGETRLGLVRRARRMNRALAQAFPHVYCELDFTSPLELTVATILSAQSTDKRVNLTTPAVFARYRSALDYMQADRAELENFIRPTGFFRNKAASLIRLGQALVERFDGEVPSTMVDLFTLPGVGRKTANVILGNAFGIPGITVDTHFGRLVRRWRWTAEEDPVKVEHAVGELIERDQWTLLSHRVIFHGRRVCHARKPACGVCVLAKDCPSFGLGPTEPLLAAPLVQGPEAGHLLALAGL", "text": "FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. SIMILARITY: Belongs to the Nth/MutY family."}
+{"protein": "MELDFGHFDERDKASRNMRGSRMNGLPSPTHSAHCSFYRTRTLQALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNVKTSANMKAPQSLASSNSAQARENKDFVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFRYAQDDFSLDENECRVMKGNPSAAAGPKASPTPQKTSAKSPGPMRRSKSPADSGNDQDANGTSSSQLSTPKSKQSPISTPTSPGSLRKHKVDLYLPLSLDDSDSLGDSM", "text": "FUNCTION: Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May participate along with PAFAH1B1/LIS-1 in a distinct overlapping signaling pathway that promotes neuronal migration. SUBCELLULAR LOCATION: Cytoplasm Cell projection, neuron projection Note=Localizes at neurite tips."}
+{"protein": "MPLQVSDYSWQQTKTAVFLSLPLKGVCVRDTDVFCMENYLKVNFPPFLFEAFLYAPIDDESSKAKIGNDTIVFTLYKKEAAMWETLSVTGVDKEMMQRIREKSILQAQERAKEATEAKAAAKREDQKYALSVMMKIEEEERKKIEDMKENERIKATKELEAWKEYQRKAEEQKKIQREEKLCQKEKQIKEERKKIKYKSLTRNLASRNLAPKGRNSENIFTEKLKEDSIPAPRSVGSIKINFTPRVFPTALRESQVAEEEEWLHKQAEARRAMNTDIAELCDLKEEEKNPEWLKDKGNKLFATENYLAAINAYNLAIRLNNKMPLLYLNRAACHLKLKNLHKAIEDSSKALELLMPPVTDNANARMKAHVRRGTAFCQLELYVEGLQDYEAALKIDPSNKIVQIDAEKIRNVIQGTELKS", "text": "FUNCTION: 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. Axonemal dynein assembly factor required for ciliary motility (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, neuron projection Dynein axonemal particle."}
+{"protein": "MAYRKRGARREANINNNDRMQEKDDEKQDQNNRMQLSDKVLSKKEEVVTDNQEEIKIADEVKKSTKEESKQLLEVLKTKEEHQKEIQYEILQKTIPTFEPKESILKKLEDIKPEQAKKQTKLFRIFEPRQLPIYRANGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQVLTEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGAVRRFIAEMRQRVQADRNVVNYPSILHPIDYAFNEYFLQHQLVEPLNNDIIFNYIPERIRNDVNYILNMDRNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLKELVSTEAQIQKMSQDLQLEALTIQSETQFLTGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVVPNDMFIRESLVACQLAIVNTIIYPAFGMQRMHYRNGDPQTPFQIAEQQIQNFQVANWLHFVNNNQFRQVVIDGVLNQVLNDNIRDGHVINQLMEALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLAYNYETLMACVTMNMQHVQTLTTEKLQLTSVTSLCMLIGNATVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKAIVEDFLKRLHIFDVARVPDDQMYRLRDRLRLLPVEVRRLDIFNLILMNMDQIERASDKIAQGVIIAYRDMQLERDEMYGYVNIARNLDGFQQINLEELMRTGDYAQITNMLLNNQPVALVGALPFVTDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWVPTSTTKVYKQVPQQFDFRNSMHMLTSNLTFTVYSDLLAFVSADTVEPINAVAFDNMRIMNEL", "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": "MVLLAAIDQGTSSSRFLVFEADTGELVTSHQIEVRQLFPHGGWVEMDPMELYDTVVSCISKTIEKLENLGISADEIKSVGVANQRETSIVWDKETGKPLYNAIVWLDTRTSSLADEAISRTASKSKDEFRAKTGLPIHPYFSALKLKWLFQNVPEVKKAYADGNLMFGTVDTWLIWKLTGAYVTDVSNASRTLLLDLHKRKWSTQLCEFFDLPIEILPEIRSSAEVYGHFDKGPLEGVPLSGCLGDQQAAMVGHQCLNAGQTKNTYGTGTFMLCNIGTRPIISKNGLLTTVGFQFGADSPVVYALEGSGSIGGNVVRFLRDNFKFISDAKEMEGLCRSVEDTSGAYFVPSFTGLYTPYWDSTARGTILGLTQVTQREHICLAALRAVAFQSAEMIAAVEQDLEGGTKVTTLKVDGGMIANKLFNEIQADIMGRDIVTPKITEISGWGAAVAGGIGAQQISLDEFLQQSSEDNRYTPQKDDNWRSAELARWKEAVKRSCGWAQ", "text": "SIMILARITY: Belongs to the FGGY kinase family."}
+{"protein": "MKFMVTEQKTLIYPVINLITGQHNYIGFKCRISTNNANYVVHRVFSIQNKLSREHTASTKTKSQVRGGGKKPWKQKGTGRARAGSIRSPLWRGGGVVFGPKPKNVFFKINKKEIRLALYTVLSNALPKTTVVSSLEGLPNFISTQALIKFLRSLNVSLDNRVLIVVEKKETPLFLSCRNIKNLALIQADHLNVKSVILAQSLVVTLQALKIIYKTFNDN", "text": "FUNCTION: Probably binds the 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL4 family."}
+{"protein": "MGAERRLLSIKEAFRLAQQPHQNQAKLVVALSRTYRTMDDKTVFHEEFIHYLKYVMVVYKREPAVERVIEFAAKFVTSFHQSDMEDDEEEEDGGLLNYLFTFLLKSHEANSNAVRFRVCLLINKLLGSMPENAQIDDDVFDKINKAMLIRLKDKIPNVRIQAVLALSRLQDPKDDECPVVNAYATLIENDSNPEVRRAVLSCIAPSAKTLPKIVGRTKDVKEAVRKLAYQVLAEKVHMRAMSIAQRVMLLQQGLNDRSDAVKQAMQKHLLQGWLRFSEGNILELLHRLDVENSSEVAVSVLNALFSITPLSELVGLCKNNDGRKLIPVETLTPEIALYWCALCEYLKSKGDEGEEFLEQILPEPVVYADYLLSYIQSIPVVNEEHRGDFSYIGNLMTKEFIGQQLILIIKSLDTSEEGGRKKLLAVLQEILILPTIPISLVSFLVERLLHIIIDDNKRTQIVTEIISEIRAPIVTVGVNNDPADVRKKELKMAEIKVKLIEAKEALENCITLQDFNRASELKEEIKALEDARINLLKETEQLEIKEVHIEKNDAETLQKCLILCYELLKQMSISTGLSATMNGIIESLILPGIISIHPVVRNLAVLCLGCCGLQNQDFARKHFVLLLQVLQIDDVTIKISALKAIFDQLMTFGIEPFKTKKIKTLHCEGTEINSDDEQESKEVEETATAKNVLKLLSDFLDSEVSELRTGAAEGLAKLMFSGLLVSSRILSRLILLWYNPVTEEDVQLRHCLGVFFPVFAYASRTNQECFEEAFLPTLQTLANAPASSPLAEIDITNVAELLVDLTRPSGLNPQAKTSQDYQALTVHDNLAMKICNEILTSPCSPEIRVYTKALSSLELSSHLAKDLLVLLNEILEQVKDRTCLRALEKIKIQLEKGNKEFGDQAEAAQDATLTTTTFQNEDEKNKEVYMTPLRGVKATQASKSTQLKTNRGQRKVTVSARTNRRCQTAEADSESDHEVPEPESEMKMRLPRRAKTAALEKSKLNLAQFLNEDLS", "text": "FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. SIMILARITY: Belongs to the CND3 (condensin subunit 3) family."}
+{"protein": "MPAQGHRLYVKAKHLSFQRSKHVIHPGTSLVKIEGCDSKEEAQFYLGKRICFVYKSNKPVRGSKIRVIWGTVSRPHGNSGVVRARFTHNLPPKTFGASLRVMLYPSNV", "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 eL33 family."}
+{"protein": "MSFSVKGRSLRGNNNGGTGTKCGRWNPTVEQLKILTDLFRAGLRTPTTDQIQKISTELSFYGKIESKNVFYWFQNHKARERQKRRKISIDFDHHHHQPSTRDVFEISEEDCQEEEKVIETLQLFPVNSFEDSNSKVDKMRARGNNQYREYIRETTTTSFSPYSSCGAEMEHPPPLDLRLSFL", "text": "FUNCTION: Transcription factor, which may be involved in the specification and maintenance of the stem cells (QC cells) in the root apical meristem (RAM). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WUS homeobox family."}
+{"protein": "MKTNDNYIEEVTAKVLTSGKYSTLYPPTVRRVTERLFDRYPPKQLEKEVRKKLHQAYGAYIGGIDGKRLEKKIEKIIHEIPNPTTDEATRTEWEKEICLKILNLHTSTNERTVAYDELYQKIFEVTGVPTSITDAGCALNPFSFPFFTEAGMLGQYIGFDLDKGMIEAIEHSLRTLNAPEGIVVKQGDILSDPSGESDLLLMFKLYTLLDRQEEASGLKILQEWKYKNAVISFPIKTISGRDVGMEENYTVKFENDLVGSDLRIMQKLKLGNEMYFIVSRL", "text": "FUNCTION: Specifically methylates the N(7) position of guanine 1405 in 16S rRNA. Confers resistance to various aminoglycosides, including gentamicin and kanamycin. SIMILARITY: Belongs to the methyltransferase superfamily. Aminoglycoside resistance family."}
+{"protein": "MKIIRFGVSVPEELLEKFDQIIAEKGYVNRSEAIRDLMRDFIVRHEWEAGDKEVAGTITMLYNHDEADVVKELLDLQHDYLNEIISSIHVHMDEHNCLEVVIVKGKAKRIKEIADRLLSLKGVKHGKLVMTGTGKELV", "text": "FUNCTION: Transcriptional regulator. SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family."}
+{"protein": "MSSPTTSSLDTPLPGNGPPQPGAPSSSPTVKEEGPEPWPGGPDPDVPGTDEASSACSTDWVIPDPEEEPERKRKKGPAPKMLGHELCRVCGDKASGFHYNVLSCEGCKGFFRRSVVRGGARRYACRGGGTCQMDAFMRRKCQQCRLRKCKEAGMREQCVLSEEQIRKKKIRKQQQESQSQSQSPVGPQGSSSSASGPGASPGGSEAGSQGSGEGEGVQLTAAQELMIQQLVAAQLQCNKRSFSDQPKVTPWPLGADPQSRDARQQRFAHFTELAIISVQEIVDFAKQVPGFLQLGREDQIALLKASTIEIMLLETARRYNHETECITFLKDFTYSKDDFHRAGLQVEFINPIFEFSRAMRRLGLDDAEYALLIAINIFSADRPNVQEPGRVEALQQPYVEALLSYTRIKRPQDQLRFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE", "text": "FUNCTION: Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles (By similarity). Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity). 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 (PubMed:20159957). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
+{"protein": "MNRVINFLNMVALSAMRRSELVGAFFVIAIVFMMITPLPTGLIDVLIAVNICISCLLIMLAMHLPRPLAFSTFPAVLLLTTMFRLALSVSTTRLILLNQDAGHIVEAFGQFVVGGNLAVGLVIFLILTVVNFLVITKGSERVAEVGARFTLDAMPGKQMSIDSDLRANLITVHEARKRRAELNKESQLFGAMDGAMKFVNGDAIASLIIVAINMIGGISIGVLQHNMAAGDALQLYTVLTIGDGLIAQIPALLISVTSGMIITRVPNTEAGVEANIGREIAEQITSQPKAWIIASVAMLGFAALPGMPTGVFITIAIICGAGGLLQLQRAKPKADEQRTAAVAPEMNGKEDLRTFSPSRQFVLQFHPGQDSAQIEALVSEIRKRRNRLVVQYGLTLPSFIIEHVDDIAPDEFRFTVYDVPMLKATFTQSHVAVEARQLEGENLPAAIPGNTDRQEDQWVWLPAEQSGELNPVSSTTLIIERMERALQSCAPQFIGLQETKAILSWLESEQPELAQEMQRVLTLTRFSAVLQRLASECVPLRAIRVIAETLIEHCQHERDTNVLTDYVRIALKSQIYHQYCGAEGLQVWLVTPESEGLLRDGLRQTQTETFFALSNETSQMLVQQLHIAFPVRAPEQAVLLVAQDLRSPLRTLLREEFYHVPVLSFAEISNAAKVKVMGRFDLEDDLEPLDNEHAA", "text": "FUNCTION: Involved in the secretion of harpin-pss; a proteinaceous elicitor of the hypersensitivity response in plants. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family."}
+{"protein": "MEQIQMVKVLEKCQVTPPSDTTDVELSLPVTFFDIPWLHLNKMQSLLFYDFPYPRTHFLDTVIPNLKASLSLTLKHYVPLSGNLLMPIKSGEMPKFQYSRDEGDSITLIVAESDQDFDYLKGHQLVDSNDLHGLFYVMPRVIRTMQDYKVIPLVAVQVTVFPNRGIAVALTAHHSIADAKSFVMFINAWAYINKFGKDADLLSANLLPSFDRSIIKDLYGLEETFWNEMQDVLEMFSRFGSKPPRFNKVRATYVLSLAEIQKLKNKVLNLRGSEPTIRVTTFTMTCGYVWTCMVKSKDDVVSEESSNDENELEYFSFTADCRGLLTPPCPPNYFGNCLASCVAKATHKELVGDKGLLVAVAAIGEAIEKRLHNEKGVLADAKTWLSESNGIPSKRFLGITGSPKFDSYGVDFGWGKPAKFDITSVDYAELIYVIQSRDFEKGVEIGVSLPKIHMDAFAKIFEEGFCSLS", "text": "FUNCTION: Transfers hydroxycinnamic moieties to the glucosyl groups of anthocyanin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the plant acyltransferase family."}
+{"protein": "MPIKVLFVDDHEMVRIGISSYLSTQSDIDVVGEGKSGKDAIEKAHELKPDLILMDLLMDDMDGVEATEQVKKDLPNIKVVMLTSYIEDNEVYRALDSGVDSYILKTTSASDIAEAIRKTYNNESVFEAEVLVKMRNRMKQRAELYEMLTEREMEILLLIAKGYSNQEIASASHITIKTVKTHVSNILSKLEVQDRTQAVIYAFQHNLIQ", "text": "FUNCTION: Member of the two-component regulatory system VraS/VraR involved in the control of the cell wall peptidoglycan biosynthesis. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MSKSKTFLFTSESVGEGHPDKICDQVSDAILDACLEQDPFSKVACETAAKTGMIMVFGEITTKARLDYQQIVRDTIKKIGYDDSAKGFDYKTCNVLVAIEQQSPDIAQGLHYEKSLEDLGAGDQGIMFGYATDETPEGLPLTILLAHKLNMAMADARRDGSLPWLRPDTKTQVTVEYEDDNGRWVPKRIDTVVISAQHADEISTADLRTQLQKDIVEKVIPKDMLDENTKYFIQPSGRFVIGGPQGDAGLTGRKIIVDAYGGASSVGGGAFSGKDYSKVDRSAAYAARWVAKSLVAAGLCKRVQVQFSYAIGIAEPLSLHVDTYGTATKSDDEIIEIIKKNFDLRPGVLVKELDLARPIYLPTASYGHFTNQEYSWEKPKKLEF", "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. SIMILARITY: Belongs to the AdoMet synthase family."}
+{"protein": "MKQPLILSFLLLGMVSAFHLETAHLENPKREESLKQEADGSREQGRELALTQETKQTEGEEVEGSQHQDIFEDEEAMESDPDALNKDSACPKEEDTTHFQGTPGCKSCNYVLVRTPETFDKAQRVCRRCYRGNLASVHSYSFNYQIQNLARKINQSIVWIGGILRGWFWKKFCWMDGSCWDFGYWAPGQPGSGGGHCVTLCTKGGHWRRASCKSHLPFICSF", "text": "FUNCTION: Possesses similar cytotoxic and cytostimulatory activities to PRG2/MBP. SUBCELLULAR LOCATION: Note=Localized to the eosinophil secondary granule."}
+{"protein": "METVLVINPGSTSTKLALFANHDCLAEETLRHSVQELAPFENVVSQTSFRKQMIAEFLETHNIIQLAAVVGRGGLLKPIPGGTYLVDQQMLEDLRTERFNTHASNLGAILANEFAEKYHVPAFIVDPVVVDELQPLARISGLKGIQRRSVGHALNQKAVARKIAEDLGKTYEQSNFIVVHLGGGISLGAHQKGRMVDVVNGLDGEGPYTPERSGALPLVEFAQWILEQELTISQVKKLIAGNSGLKSYLGETDLRHIQAQIAAGDQTANYYLKGMCYQIAKSIGEMAVVLEGTIDAIILTGGAAYSQTVVQEISQKVTWIAPIKVYPGEMEMAALYEGVNRVLTGEEQALNYSEAKIEQE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetokinase family."}
+{"protein": "MLPFVHEQIGTIIVNFFILTVVCAITLLVCLAVLTAIRLCVQCASGVNTLLFVPAFYIYNTGRNAYFKFQENRPPFPPEDWV", "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 betacoronaviruses E protein family."}
+{"protein": "METLKDKTLQELEELQNDSEAIDQLALESPEVQDLQLEREMALATNRSLAERNLEFQGPLEISRSNLSDKYQELRKLVERCQEQKAKLEKFSSALQPGTLLDLLQVEGMKIEGESEAMAEKFLEGEVPLETFLENFSSMRMLSHLRRVRVEKLQEVVRKPRASQELAGDAPPPRPPPPVRPVPQGTPPVVEEQPQPPSAMPPYPLPYSLSPSLPVGSTAHGALPPAPFPVVSQPSFYSGPLGPTYPAAQPGPRGAAGYSWSPQRSTPPRPGYPGTPTGASGPGYPLAGGRALSPGYPQQSPYPATGGKPPYPIQPQLPSFPGQPQPSVPLQPPYPPGPAPPYGFPPPPGPAWPGY", "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 (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein Note=Probably associates with membranes. SIMILARITY: Belongs to the VPS37 family."}
+{"protein": "MTEAMKITLSTQPADARWGEKATYSINNDGITLHLNGADDLGLIQRAARKIDGLGIKHVQLSGEGWDADRCWAFWQGYKAPKGTRKVVWPDLDDAQRQELDNRLMIIDWVRDTINAPAEELGPSQLAQRAVDLISNVAGDRVTYRITKGEDLREQGYMGLHTVGRGSERSPVLLALDYNPTGDKEAPVYACLVGKGITFDSGGYSIKQTAFMDSMKSDMGGAATVTGALAFAITRGLNKRVKLFLCCADNLISGNAFKLGDIITYRNGKKVEVMNTDAEGRLVLADGLIDASAQKPEMIIDAATLTGAAKTALGNDYHALFSFDDALAGRLLASAAQENEPFWRLPLAEFHRSQLPSNFAELNNTGSAAYPAGASTAAGFLSHFVENYQQGWLHIDCSATYRKAPVEQWSAGATGLGVRTIANLLTA", "text": "FUNCTION: Probably plays an important role in intracellular peptide degradation (PubMed:20067529). FUNCTION: Probably plays an important role in intracellular peptide degradation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M17 family."}
+{"protein": "MAPADGESSPPPHVAVVAFPFSSHAAVLLSIARALAAAAAPSGATLSFLSTASSLAQLRKASSASAGHGLPGNLRFVEVPDGAPAAEETVPVPRQMQLFMEAAEAGGVKAWLEAARAAAGGARVTCVVGDAFVWPAADAAASAGAPWVPVWTAASCALLAHIRTDSLREDVGDQAANRVDEPLISHPGLASYRVRDLPDGVVSGDFNYVISLLVHRMGQCLPRSAAAVALNTFPGLDPPDVTAALAEILPNCVPFGPYHLLLAEDDADTAAPADPHGCLAWLGRQPARGVAYVSFGTVACPRPDELRELAAGLEASAAPFLWSLREDSWTLLPPGFLDRAAGTGSGLVVPWAPQVAVLRHPSVGAFVTHAGWASVLEGVSSGVPMACRPFFGDQRMNARSVAHVWGFGAAFEGAMTSAGVAAAVEELLRGEEGAGMRARAKELQALVAEAFGPGGECRKNFDRFVEIVCRA", "text": "FUNCTION: In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MSEVKSRKKPGPKVAAPEPEKRSDGRKNPEARGGAGWADPRTGLSLLSLATSLGLAWLVFQQSEKFAKVENQYRLLQTESSEFQGLQSKISLISNKLESTENTLQEATSSMSLMTQFEQEVAGLQRSIHDIENSEEMLTQKLQNLNEKFQNITDLWKRTLVEMSDNTAVFKSEAKSTHSEVTLKINSAEQEIKLLTERLKDLEDSTLRNIRTVSRQEEEDLLRVEAQLSSDTKAVEKLEEEQRTLLARDEDLTDKLSSYEPKVEECKAHLPTIENAVHSVLRVSQDLIGTERKMEELTVQMFNMEDDMLKAVSEIMEMQNTLEGIQYDNSLLKMQNELVVLKGKVHDFMAYSSAGEKGTLEEYNLENKGTDDY", "text": "FUNCTION: Target of p53/TP53 with pro-apoptotic function. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein."}
+{"protein": "MAARVGAFLRNTWDKEPVLVVSFVIGGLAVILPPLSPYFKYSIMINKATPYNYPVPVRDDGNMPDMPSHPQDPQGPSLEWLKKL", "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. SIMILARITY: Belongs to the complex I NDUFA3 subunit family."}
+{"protein": "MTVSNSNGLPDIVTVQKRLYPLIFTEIVSEQPTKQPVATAYGFKAVPEADDGSGWTQFGFRLDRWYAQVESSKMKTEISLETLQDMQALGVSNSVIVDSLADQIADEINTSIIGALNSISTVGAALTLTGNTDFEKGQDLYTKVHLAASEIEKTTGCKGTYVVAGGKCFGYLTGCGVVQRVGESDVYKAWSGLYIVHDKYATSDYVTVGVKKDMGDYEISSLVFSPYQFDQANDGAIAYQYKGTDPKSFHPVYGVIARYALTVPPLEDNQTGAVEIDWSNLGALANSSKLSYTYAVTV", "text": "FUNCTION: Capsid protein that self-associates to form pentons, building the capsid in association with hexamers of the major capsid protein and one dodecamer of the portal protein. SUBCELLULAR LOCATION: [Capsid vertex protein]: Virion. Note=Part of the capsid icosahedric shell of the immature virion. SIMILARITY: Belongs to the Tevenvirinae capsid vertex family."}
+{"protein": "MDYQVSSPTYDIDYYTSEPCQKINVKQIAARLLPLLYSLVFIFGFVGNILVVLILINCKRLKSMTDIYLLNLAISDLLFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWVVAVFASLPRIIFTRSQREGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVMLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTQCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEVPERASSVYTRSTGEQEIFVGL", "text": "FUNCTION: Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQAQKKMDHGRDQFLRDHPCVSQKSLEDFIKLLVEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIVLHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAIFLKWHVPPGLVRSLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVVEPAGRPGSPAPAEKVETPSPPTASALDYPSENLAFIDESSDTQSERGCALPRAPRGRRRPNPSKKPSRPRGPGRLRDKAVPV", "text": "FUNCTION: Voltage-insensitive potassium channel (PubMed:9628867). Channel opening is triggered by mechanical forces that deform the membrane. Channel opening is triggered by raising the intracellular pH to basic levels (By similarity). The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (By similarity). Plays a role in the sensory perception of pain caused by pressure (PubMed:19279663). Plays a role in the perception of pain caused by heat (PubMed:19279663). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the two pore domain potassium channel (TC 1.A.1.8) family."}
+{"protein": "MTNTQTRVIKQINKTILATCSFIFLFGFFLSSATSTILIQTNEWSILTAAILISIVELFNYLKHKFQFNDRKSGYNCFFFINLAKLGLLYGLFIDAFKLGS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf20 family."}
+{"protein": "MSLLVVAPEWLTSAAAELQSIESALSAANAAAAVPTTGLAAAAADEVSTAVATLFAGFGQEYQAISTQLSAFQQQFALTLNSSAGSYSAAEAQSVSILDTLGQDVFGAINAPTEALLGRPLIGNGANGTATSPNGGAGGLLFGNGGIGYSQTGAGIVGGAGGSAGLIGNGGAGGTGGAGATGGAGGNGGWLFGSGGIGGTGGANALGTGGTGGLGGSAGLFGGGGNGGAGGLGISGDLGTGGAGGTGGFLLGDYGVSGAGGDGRTVPLEVVNVTEPVVNVNVNGGHSTPVLIDTGSAGLVMQVKDVGGPLGLLRMGLPSGISMSAYSGGLTYLFATYPTTVDFGNGIVTSTTGVDVVLFSIPTSPYALTTWLNALWSNPLTTPFDAYFQSAGVDGVLGVGPNAVGPGPSIPTQALGGGLGQGLLIDMKGGELVFGPNPLTPEFSISGAPIATLWVSVNGGAPVAVPSIIDSGGVMGTIPSSVIGGSTLPANTNITVYTDNTMTTEVYHYSTNDYQPTVISSGLMNTGFLPFWNQPVYIDYSPAGTGTTVFDMP", "text": "FUNCTION: Aspartic protease that processes the lipase LipY and other PE_PGRS proteins. Can also cleave itself. Cleaves LipY both inside the PE domain, before amino acid 98, and after amino acids 136 and 149. Involved in virulence. SUBCELLULAR LOCATION: Secreted Cell surface Note=Secreted via the ESX-5 / type VII secretion system (T7SS). SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily."}
+{"protein": "MSYGREDTTIEPDFIEPDAPLAASGGVADNIGGTMQNSGSRGTLDETVLQTLKRDVVEINSRLKQVVYPHFPSFFSPSDDGIGAADNDISANCDLWAPLAFIILYSLFVSHARSLFSSLFVSSWFILLVMALHLRLTKPHQRVSLISYISISGYCLFPQVLNALVSQILLPLAYHIGKQNRWIVRVLSLVKLVVMALCLMWSVAAVSWVTKSKTIIEIYPLALCLFGMAWLSTIL", "text": "FUNCTION: May be involved in proper membrane localization of Rab GTPases. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the YIP1 family."}
+{"protein": "MNVKHGTFKGGIHPPYRKESTAEVPLGFGKKPEMVIIPMSLHIGAPCTPIVKKGDTVFLGQRVGEPNGFVSVPVHASVSGKVIAVEERPHASGDRVMSVVIESDGLDTIDPSIKPYGTLEDMDADAIKKMVLNAGIVGLGGATFPTHVKLAIPPDKKVDCVVLNGAECEPYLTADHHLMTSQAEKVVMGLKLAMKSVGVEKGFIGVEDNKTDAIEALVKAIGNDSRLEVYSLHTKYPQGAEKQLIAAITGREVPSGALPADAGVVVMNVGTAAQIAESMITGLPLYKRYLTCTGDAIKNPQTIEIRIGVPFQSVIDQCGGFSSEPGKVISGGPMMGVTQFVTDIPVMKGTSGILCLTKESAKIATPSNCIHCGKCVGVCPIHLQPLNIAEYSQRNMWDKCESNNAMDCIECGSCSYICPAKRTLVSSIRVAKREIIAQRRKGN", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Couples electron transfer from reduced ferredoxin to NAD(+) with electrogenic movement of Na(+) out of the cell. Involved in caffeate respiration. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily."}
+{"protein": "MGLEDERKMLTESGDPEKEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDKRVSSRSRTEEDCTEELLDFLHARDHCVAYKLFNNLK", "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": "MSLMDNWKTDMESYDEGGLVANPNFEVLATFRYDPGFARQSASKKEIFETPDPRLGLRDEDIRQQIINEDYSSYLRVREVNSGGDLLENIQHPDAWKHDCKTIVCQRVEDMLQVIYERFFLLDEQYQRIRIALSYFKIDFSTSLNDLLKLLVENLINCKEGNSEYHEKIQKMINERQCYKMRVLVSKTGDIRIEAIPMPMEPILKLTTDYDSVSTYFIKTMLNGFLIDSTINWDVVVSSEPLNASAFTSFKTTSRDHYARARVRMQTAINNLRGSEPTSSVSQCEILFSNKSGLLMEGSITNVAVIQKDPNGSKKYVTPRLATGCLCGTMRHYLLRLGLIEEGDIDIGSLTVGNEVLLFNGVMGCIKGTVKTKY", "text": "FUNCTION: Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MARNIQSLERAAAMLRLLAGGERRLGLSDIASTLGLAKGTAHGILRSLQAEGFVEQEPASGRYQLGAELLALGNSYLDVHELRARALVWTDDLARSSGEAAYLGVLHQQGVLIVHHVFRPDDSRQVLEVGAMHPLHSTAHGKVISAFDPVAHSEVLEGDRATLTGRTVTEAAAFEEVLDLTRARGWALDLEETWEGVASLAAPVHDRRRMAVGAVGVTGPVERLCPDGAPATELVTAVRDCAAAVSRDLGAGRF", "text": "FUNCTION: May be an activator protein for the gylABX operon."}
+{"protein": "MAAPTAKVSRGWSGLALGVRIAVLRLPGLTQVRWSRYGPEYQDPQIDKEYYRKPLAQLTEEETYERELRKTQVIKAAPATKTSSVFEDPVISKFTNMMMKGGNKILARSLMTQTLEAVKRKQFEKYHAASAEEQATVERNPYTIFHQALKNCEPVIGLVPILKGGHFYQVPVPLAERRRRFLAMKWMITECREKKPRRMLMPEKLSQELLEAFCNRGPVIKRKHDMHKMAEANRALAHYRWW", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
+{"protein": "MEQEHVMTLKEWMEWNAHKQLQKLQSTHPELHVDIPEDIPLVPEKVPLKMRMRYRCYTLCATSTRIMFWILFFLLCFSIVTLSTIISILRYQWKEAITHPGPVLSWQVTNSHVTMGGNTSSSSRRRRDIQYHKLPVEVNISGIPQGLFFAPQPKPIFHKERTLGLSQVILIDSDTITQGHIKQQKAYLVSTINEEMEQLQKTVLPFDLPIKDPLTQKEYIEKRCFQKYGHCYVIAFNGNKVWPSQDLIQDQCPLPPRFGNNLKYRNHTIWKYYIPLPFKVSSNWTRVESYGNIRIGSFKVPDEFRQNATHGIFCSDALYSNWYPRDLPSSVQQSFAQAYITKVLMKRKKQPTLRDIAFPKELSPVGSGMLFRPINPYDICNMPRAVLLLNKTYYTFSLWEGDCGYYQHNLTLHPACKNFNRTRQDHPYACRFWRNKYDSESVQCYNNDMCYYRPLYDGTENTEDWGWLAYTDSFPSPICIEEKRIWKKNYTLSSVLAECVNQAMEYGIDEVLSKLDLIFGNLTHQSADEAFIPVNNFTWPRYEKQNKQQKTSCERKKGRRQRRSVSTENLRRIQEAGLGLANAITTVAKISDLNDQKLAKGVHLLRDHVVTLMEANLDDIVSLGEGIQIEHIHNHLTSLKLLTLENRIDWRFINDSWIQEELGVSDNIMKVIRKTARCIPYNVKQTRNLNTSTAWEIYLYYEIIIPTTIYTQNWNIKNLGHLVRNAGYLSKVWIQQPFEVLNQECGTNIYLHMEECVDQDYIICEEVMELPPCGNGTGSDCPVLTKPLTDEYLEIEPLKNGSYLVLSSTTDCGIPAYVPVVITVNDTISCFDKEFKRPLKQELKVTKYAPSVPQLELRVPRLTSLIAKIKGIQIEITSSWETIKEQVARAKAELLRLDLHEGDYPEWLQLLGEATKDVWPTISNFVSGIGNFIKDTAGGIFGTAFSFLGYVKPVLLGFVIIFCIILIIKIIGWLQNTRKKDQ", "text": "FUNCTION: The leader peptide is a component of released, infectious virions and is required for particle budding. 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 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. 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. SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host endoplasmic reticulum membrane; Single-pass type I membrane protein."}
+{"protein": "MAEEQAYHVSKGLECLKALRENPPDIEEIQEVSSLRDQTCNPGQENGTTGMQEEEDSQNLDESHEPTKGSNYVGHVPQNNPGCGERNTALVEAERPPREDIQPGPGIRCDHVYDHSGEEVKGIEDADSLVVPAGTVGNRGFERGEGSLDDSTEDSGEDYSEGNASSNWGYSFGLKPDRAADVSMLMEEELSALLRTSRNVGIQKRDGKTLQFPHNPEVRQGIRSVDPLKRGTEERSVSHGMGIVAGSTSGATQSALKSTGGSSEPSVSAGNVRQPAMNAKMTQKCKLESGTQLPPRTSNEAESDSEYDDELFSEIQEIRSAITKLTEDNQAILTKLDTLLLLKGETDSIKKQISKQNIAISTIEGHLSSIMIAIPGFGKDTGDPTANVDINPELRPIIGRDSGRPLAEVLKQPASSRGNRKDSGITLGSKGQLLRDLQLKPIDKESSSAIGYKPKDTAPSKAVLASLIRSSRVDQSHKHNMLALLKNIKGDDNLNEFYQMVKSITHA", "text": "FUNCTION: Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis. SIMILARITY: Belongs to the morbillivirus P protein family."}
+{"protein": "MASVEQPNKPKLKLYSYFRSSCSFRVRIALNLKGLDYEYVPVNLLKGEQFTPEFLKINPIGYVPALVDGEDVISDSFAILMYLEEKYPEHPILPADIHKKAINYQAANIVSSSIQPLQNLAVLNFIGEKVSPDEKVPWVQRHISKGFAALEKLLQGHAGRFATGDEVYLADLFLEPQIHAAITRFNVDMTQFPLLLRLHEAYSQLPEFQNAMPDKQPDSTSPTAS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Zeta family."}
+{"protein": "MIPLEHPILLESFAHIDRSVGPHNLSSQEYAIARRVIHSTADFDFLHLLRFAPDLPQAEFDPDLPEHQAIARGIESLRHGQTIVVDVNMVKQGIQGLVQRTFNNPIQTAIDFATIADPGKTRTETGMDRCIAQFPEAIYVIGNAPTALLTLCQAIAAGKAKPALVIGVPVGFIGVLEAKKALSLLPCPQIRVEGNKGGSPVAAGIVNALLMLAWREG", "text": "FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate. SIMILARITY: Belongs to the CobH/CbiC family."}
+{"protein": "MDSVYIYQWLYANYEVRGYGIALNNTVVCVRVPNFKQVVYVECTDPQHDPRSTFTQHGFRVYETPRACSLYGAKGVGTYFAARVPNYNAMRDVQETQGPFKIHESRVSKTMEFTARAGLPTVGWIQVSQRCVVTRTVTMAAKEYMVPNWRTDVRPAPDIEGVPPAKIVYFDIEVKSDHENVFPSDRDDEVIFQIGLVLCSGTTVLRTDLLSLPGRDYDASVYQYATEGELLHAFIAYIREHEVVAVCGYNIMGFDIPYIIKRCARTSMLGTFKRIGWDSHRLAIEKTAGVGHAKMTYIQWEGVLTIDLMPIIMMDHKLDSYSLDYVANHFVKAGKDPIRPRDIFHAYNTGLMARVGRYCVKDTQLCKQLVDYLNTWVALCEMAGVCNTSIMQLFTQGQQVRVFAQIYRDCTPMDVVDKVYVIPDGGCDSDVVSPSSYTGAYVYEPVPGVYKNVIPMDFQSLYPSIIISKNICYSTLVDQGGEEYAWQEHEGCEHDPQYAKQHALGVEIGVLQCNMAALPRRATQERARMRERISEMKIQYASMTPSVVKCNVFSFRFTHAHEGVLPRVLRNLLESRARVRARIKTTDDPDIRAVLDKKQLAYKISANSVYGTMGTQRGYLPFMAGAMTTTYCGRKLIEKAAHLLKTVVGATIVYGDTDSCYIQLGHDRASLDELWQMAVNASDTVSAFFERPVRLEFEQCIYTKFIIFTKKRYVYRAFTRDGKQRTGSKGVMLSRRDSAMCARNTYAAIMSAILEGSADVPFIAVRMMHDMMIPGALQDDDFVLTKSVQDIGNGDDNNHGSYKVRNPQKAQAAATQRVAPDDAEGYAIALRQEMVKQMPAQAQLAERMRLQGRAVVSGARIEYVVLKHQYGVPEGALGARLLDFERWRDMKVAYPLDRLYYMKSVVNACDQLLVTAGYGPVCSKVYAAHLQLAYVHKQLMRRMMPTV", "text": "SIMILARITY: Belongs to the DNA polymerase type-B family."}
+{"protein": "MARKKKTRRITDIMPIRKADKKIDITKARSGKKLTRYELDAKAREDKKKRKHKGLASGSRHSAVEEKANKLQNEIKDPKIGSKKKIPLVVEFVNKPEKGQVIPVIKQVKKQDPMKELENLENNEILNELLDALDAGKTISKSDQQFVDECLDRISELMEELGIEDEDESEDDLYRTFERMDINQFR", "text": "FUNCTION: A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis. SIMILARITY: Belongs to the YihI family."}
+{"protein": "MTDYRTQPINQKNADFVEQVADRIEEMQLEGRSLWQDAKRRFFRNKAAVASLIILAFIIIFITVAPWFFPFTYEDTDWNMMSAAPTMEGYHFFGTDASGRDLLVRTAIGGRISLLVGIAGAFISVTIGTIYGAISGYVGGKTDMLMMRFLEILSSFPFMFFVILLVTLFGQNIFLIFIAIGAIAWLGLARIVRGQTLSLKNKEFVEAAIVCGVPRRQIILKHIIPNVLGLVAVYASLEVPGLILFESFLSFLGLGTQEPMSSWGALLSDGAAQMEVSPWLLIFPAFFLCLTLFCFNFIGDGLRDALDPKDR", "text": "FUNCTION: Part of the binding-protein-dependent transport system for oligopeptides; 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. OppBC subfamily."}
+{"protein": "MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGQKPHEVMKFMDVYQRSFCRPIETLVDIFQEYPDEIEFIFKPSCVPLMRCGGCCNDESLECVPTEEFNITMQIMRIKPHQSQHIGEMSFLQHNKCECRPKKDKARQEKCDKPRR", "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. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin (By similarity). Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Also binds the DEAR/FBXW7-AS1 receptor (By similarity). SIMILARITY: Belongs to the PDGF/VEGF growth factor family."}
+{"protein": "MEKEGLGLEITELRLGLPGRDVAEKMMKKRAFTEMNMTSSGSNSDQCESGVVSSGGDAEKVNDSPAAKSQVVGWPPVCSYRKKNSCKEASTTKVGLGYVKVSMDGVPYLRKMDLGSSQGYDDLAFALDKLFGFRGIGVALKDGDNCEYVTIYEDKDGDWMLAGDVPWGMFLESCKRLRIMKRSDATGFGLQPRGVDE", "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": "MGLYAAAAAVLAGVESRQGSLKGLVYSSNFQNLKQLYALVCETQRYSAVLDAVIASAGLLRAEKKLRPHLAKVLVYELLLGKGFRGGGGRWKALLGRHQARLKAELARLKVHRGVSRNEDLLQESSRPGQAYQVPRFVRVNTLKTRPEDAIDYFKRQGFSYQGRASSLEDLRALKGQHFLLDPLLPELLVFPAQTDLHEHPLYRAGHLILQDKASCLPAMLLSPPPGSHVIDACAAPGNKTSYIAALLKNQGKIFAFDQDAKRLAAMATLVARAGVSCCELAEKDFLTVSPSDQRYSQVQYILLDPSCSGSGMLSRQLEEHGEGTPSKERLQALAGFQQRALCHALRFPSLQRLVYSTCSLCQEENEDVVQEALQHNSGTFRLAPVLPTWPHRGLSTFPGSEHCLRASPETTLTGGFFIAVFERAEVVPTPAPQTDAMDPEPLSQVPKRKRRRKAAVGASMQPST", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 3438 (m5C3438) in 28S rRNA (PubMed:31722427). m5C3782 promotes protein translation without affecting ribosome biogenesis and fidelity (By similarity). Required for corpus callosum and cerebral cortex development (PubMed:31174389, PubMed:31462248). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family."}
+{"protein": "MTLSRVHQQVIAFPAAKTDTMSYLPDPASINNHQIPTSSKVSYLTGKGKSMLRKKKTDSFTNGARDQDKLGPKLTETVKRKLSLGAKILQMGGLEKIYKRLFKVCDQEKLFKAYQCYLSTTAGPIAGLLFISSKKIAFCSERSIKVASPQGVLSRVHYKVSIPLCKINGVNQSQNTKKPSQKYLEIVTIDNFDFWFMGFVSYQKAFNCLEKALNNDEQ", "text": "SIMILARITY: Belongs to the GEM family."}
+{"protein": "MRTRITLALAVLLLLLAGCSPGAPADGPVTLRFQSLAWQPDSVAATKELVGEWNATHPDVKVEYIQGSWDSVHDQLLTSFEGGEAPDVIHDASDDLADFAYGGYLADLSGLLPARLASDIPRGSWETATFGRGVYGVPFLQEPRVLIADADRLRAAKVRIPTPGHPWSWPEFRQVAKKLTGPGRYGVAWPLKEPVSATLNLSLSAGGRLFHRGADDKVTVRFEAGDEVVARTIHDQVAVDREHAPASTLGSGGADTLPGLFGGRYAMVPLGFSYRQQIVRQAPEDFHWQVLPAPAGAGGLTQGVSPQTLSVSADCPHKKEAVAFIDFLLRPRNMVRLALGDWMLPTGTQALKDPALHTARHGWATGTALAARLRPAPAQSVRGYPEWKDKVATPAYQRYYSGASTLADVRHAWSGTATWCWPATSADPPPGVPRAGKRNIRDATSRLPSTP", "text": "FUNCTION: May participate in oleandomycin glycosylation and secretion during antibiotic production. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
+{"protein": "MPLSNGRNRRTRKLFKRPFRGHGLSNTSTILHTYKVGDYVTILCNSSIQHGLPYKAFHGKTGRVWNVNPHAIGVMVNKKVNNRIVVKRLHISPEHIRPSGCQKDFLERKAAVAAIRKQNIQLKKEGKPLLPLPAKRLPKQPRPAELIKGADIKFTTVAPLKFEELY", "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. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family."}
+{"protein": "CGDINAPCQSDCDCCGYSVTCDCYWSKDCKCRESNFVIGMALRKAFCKNK", "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": "MSSKSASKLKREAKKAERLAAKGESVKPSKKNGTKNGKDKEVDGVTKDLSELSTSDPIFERSASGVLTSQPMSRDIKIDSYTLSFHGRLLIENATIELNHGQRYGLLGDNGSGKSTFLESVAARDVEYPEHIDSYLLNAEAEPSDVNAVDYIIQSAKDKVQKLEAEIEELSTADDVDDVLLESKYEELDDMDPSTFEAKAAMILHGLGFTQEMMAKPTKDMSGGWRMRVALSRALFIKPSLLLLDEPTNHLDLEAVVWLENYLAKYDKILVVTSHSQDFLNNVCTNIIDLTSKKQLVYYGGNFDIYMRTKEENETNQMKAYLKQQEEIAHIKKFIASAGTYANLVRQAKSKQKIIDKMEAAGLVEKPEPPRQFSFEFDEVRKLPPPIIAFNDVAFSYDGNLDHALYRDLSFGIDMDSRVAIVGKNGTGKSTLLNLITGLLIPIEGNVSRYSGLKMAKYSQHSADQLPYDKSPLEYIMDTYKPKFPERELQQWRSVLGKFGLSGLHQTSEIRTLSDGLKSRVVFAALALEQPHILLLDEPTNHLDITSIDALAKAINVWTGGVVLVSHDFRLIGQVSKELWEVKDKKVVKLDCSIEEYKKSMAKEVQSRDTTAKVKHLI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MIEPQNNKNINNNIYNNNNNNFKMNQDENQLILNSKQLLEKIKISKKKNPQLKFIRVCWIDISNKIRTKAINIDWILNHEPKLIHVSITNVCMSLLCFEDSVTIEALKSENFGEAFLIPITTTKLNILPYCPSHIQIFGEFFYLDNESKKLKPWLLCPRNSLQRAIDRLKNKFGISLKGSFEEEFYLIKKGDNNNSSVASLLNSIEKLDHGTFANYHSLDCYGDILEKITNALEEQGLPIEQLLSESGSGQFEITIDYTDIMEACDRHIIVRQTINSIASYNGYIATFIPKPFDGLVGSGCHAHLSLWDTNDSNLTPDANGECGLSLVNQFFIGGLLKHSKSLTALFNTTPNSYKRLKPFYWSGCNVSWGLDNKESFIRIPSSPFSATDGCSNFEIKTIDHTSNPYLAMAGIIHAGFDGIENSIAPPPPTSLFDQSVLNNQLIPSNFEDAIQSLKENHYLCENIGNDISNAFIHVKLAENKILKELSDDDQILKLLELF", "text": "SIMILARITY: Belongs to the glutamine synthetase family."}
+{"protein": "MAVTFDISPEKEAGVLRLFHSQLFVTPPPLTRRDVDLSGKTAIVTGANGGLGLETAHQLLDLGCKVILAVRRVERGEAARQKLLEGRDAQATEIEVWPLDLSSYESVVGFAERAKTLSRLDIAILNAGLYKVNQTMTASTGYEESIHVNYLANALLITLLAPIFKNKKTGNTPGRIVLVSSDLAAWAKFKERKSNPILPTFKQKMTPKWDYLERYGTSKVLGQFFVTELAKRVSPDAVLVTTTNCGLCHGSELSREGQGHLIGYVFNVVSRLFGRSCSVGARVFVHAAANPVLGASVHGQYVEDAKLKPMSPLIYKPGDLQLGSKLWEETMDELSFAGAREIIDSLTK", "text": "FUNCTION: Short-chain dehydrogenase; 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 short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MAARSLSGAVKSLCSAASGSLSCSIVLRRSYVATSQNVTAAGLSKGGSTRVMVGKMEQRGLDQEAESAWGPDPVTGYYRPSNRAAEIDPAELRELLLKNKAKSF", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the LEA type 3 family."}
+{"protein": "MSVSRRVIHHGLYFAVLGPLIGVLFLVLYIFFAKEPLILLVIIQVLPLFLLMSITTGAIPAMLTGVMVACLPEKIGSQKRYRCLVGGIGGVVITEIYCAVIVHIKDMASSALFENILSGENLVVRIIPALLAGVVMSRIITHLPGLDISCPETDSLS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbrB family."}
+{"protein": "MVRPTRNRKPINYSQFEDSGNDSDDDFISSSTPVNKSKTVPKVLKQDKPKPNLKNLQKEEVLPTEPPKKRVALDDKVFQRGLEVALALSVKELPTLTNQVKKSKEKSTDKQGKEKTENTGKPPRVSNCSVASDDVEDLDKITEEGDASSVEGERKSPSQAKAPRRRAPSEGSDGSSANDTESESATGEGSESDPDFDESKESDEDFGVRRSKESKKKTVQKKPAGEKKERKSKPKCEASVTSVDPAPAAIKSGSPSLPQAVGLPSEATRKPAIMCSPSAESKRPKWVPPAASGSRNSSSNALAGTPAKSPSQSLRLGLSRLAPVKRLHPSATSSQVR", "text": "FUNCTION: Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination. Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51. Binds single-stranded DNA (ssDNA), double- stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation. Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair. WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2. Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination. SUBCELLULAR LOCATION: Chromosome Nucleus Chromosome, telomere Note=Colocalizes with RAD51 to multiple nuclear foci (PubMed:9192668, PubMed:21307306). Colocalizes with DMC1 on meiotic chromatin (PubMed:21307306)."}
+{"protein": "MPYRAELKRPDLKGSFPCSICQKVFCHSSSLSRHRMQAHFKSYTCTTCNNEIPSNDTLRSHMYRVHNITRMFMCRCCNWAFPDKTSLHIHMQSMLKNGTPGEAAVLAKSSDVVDSTSESGSPRQSPPFSPDLLMQKRMLQVAANNNNIGSIFPTLLKSPDSKSMFPLDLSNMGPSQFLSAWLANNPINTAALNLAAQQTPSKDSIQSSNISDYDDLEVQTTEEDIKFEVESSDVSPRSVIVKTEPTFKRELEHDADIDVEGDDGEPPLKMTIDDKNIHISHDQPSPTVSDSHISGGSSSHSGESLKCFDCQVARGKLVAVEDKCRAYEKTIRELQVQVDFLRKIQPNPMPPVMLPPPMMPMPSPGPNNLFQNPAMRMLLNNLIHMNRPSVVP", "text": "FUNCTION: Probable transcription factor that acts downstream of egl-15, to promote migration of the HSN motor neurons from the tail to the gonad primordium during HSN cell differentiation (PubMed:10049362). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLWPASEEFAALCRTQLELVVNSLGASSLAVYLSETLNDSPSWSPVAVYPEAASLLSLAIPPTLPPPTQVPETSLSHYPQQVVSSLANQLILPLMYQNWVLGVLVAQRQHRPWLAAEQAQLQQVAQTLAIACVLDQRQQWLSHSPAQPLDQRQQRFDDLLHQLRNPVAAIRTFVKLLLKRLEPDHKGRPLAEGIAKETERLMALLEDYRQQRNDIPALTGSQPLPLAGKPLDLAETLLPLISAAQARAEMEGKTFVVEIPPQLPPIWLEERVLQEVVGNLLDNAFKYTPKGGTIGLRLMLSSPALELTVWDTGCGIPKEAQPRLFERGYRGVQADSGIEGSGLGLAIAQDLLRPYGLSLRVTSPYAGDRGTAFTLAIPWQMKVEP", "text": "FUNCTION: Member of 2 two-component regulatory system(s) Hik2/Rre1 and Hik2/RppA. Transduces PQ (plastoquinone) redox signals to photosystem gene expression machinery during the adjustment of photosystem stoichiometry. Reduced PQ suppresses its autophosphorylation activity (i.e. kinase activity is higher under oxidizing conditions). As part of a two-component regulatory system with Rre1, controls expression of sigB and several other genes in response to hyperosmotic stress. May transfer phosphate to RppA in a possible Hik2/RppA two-component system. SIMILARITY: Belongs to the chloroplast sensor kinase protein family."}
+{"protein": "MSFLFNKRPKSTQDVVRCLCDNLPKLEINNDKKKSFEEVSKCLQNLRVSLCGTAEVEPDADLVSDLSFQIYQSNLPFLLVRYLPKLEFESKKDTGLIFSALLRRHVASRYPTVDYMLAHPQIFPVLVSYYRYQEVAFTAGSILRECSRHEALNEVLLNSRDFWTFFSLIQASSFDMASDAFSTFKSILLNHKSQVAEFISYHFDEFFKQYTVLLKSENYVTKRQSLKLLGEILLNRANRSVMTRYISSAENLKLMMILLRDKSKNIQFEAFHVFKLFVANPEKSEEVIEILRRNKSKLISYLSAFHTDRKNDEQFNDERAFVIKQIERL", "text": "SIMILARITY: Belongs to the Mo25 family."}
+{"protein": "MPPSVATHASLLLKAAAAAAHLHPKPFFSPRAAPPRIPSAPAPPAAGGSRYRPTTTTTAAATATSATAACRWFRWPPPAQAPVRGLCSLPHSGGGGGGGEGMGSEGVGRRRRVVAPAVNGVAKDGAPQPPPPKLLTLPTVLTIGRVAAVPLLISTFYMEGPWAATATTGIFLAAAVTDWLDGYIARKMQLGTPFGAFLDPVADKLMVAATLVLLCTKPLEISLLRDGPWLLTVPAIAIIGREITMSAVREWAASQNTKVLEAVAVNNLGKWKTATQMTALTILLASRDKSLPAQDALVTSGIALLYVSAGLAIWSLVVYMRKIWRILLK", "text": "FUNCTION: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family."}
+{"protein": "MPAAWMPVLRLGAYASRVPGPAGGDGAVPIAITCFTRGLDIRKEKADVLCPAGCPLEEFSVFGNIVYASVSSICGAAVHRGVISISGGPVRVYSLPGRENYSSVDANGIQSQTLARWSASFTVTKGKSSTQEATGQAVSTARPPTGKRLKKTPEKKTGNKDCKADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSNTGKALKHTAQKFFTADTGMRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVAFVDKAVCRNNGFFSYHMPNWFGTTKYVKPLVQKLCSHEQMMCSKTCYNSVNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRSIRYMSGGTATGDAISFTVRNVFGPVRDSPNKNFLVIITDGQSYDDVRGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHAFFTREFTGLEPIVSDIIRGICRDFLESQQ", "text": "FUNCTION: Plays a role in the control of cell shape and motility in the trabecular meshwork. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
+{"protein": "MPPKPAPGDNEGNASGSTPTPPPPPPARTAEEARLRLAEMEREREQEQLLEEMNSNTPAEDARNISRLTQLAALLRREQTNVHVTNMALEIGRPALQPPPNMRGDPTNMYSQVSSDFLWKIKPQRISNNMATSEDMVKIQVALEGLGVPTESVKEVIIRLVLNCANTSSSVYQDPKGVIEWDGGAIIADDVVGVITKHSTLRKVCRLYAAVAWNYMHLQQTPPSDWSAMGFHPNVKYAAFDFFDYVENGAAIRPSGGIVPKPTRAEYVAYNTYKMLALNKANNNDTFGNFDSAITGGRQGPAIHNNLNNANNKTL", "text": "FUNCTION: Required for genome encapsidation. Forms ribonucleoprotein complexes along with TGB1 helicase and viral RNA. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the potexviruses coat protein family."}
+{"protein": "MPPTPEVGLPLWLLAELTYRCPLQCPYCSNPLDFAAQGQELSTEQWFKVMAEAREMGAAQIGFSGGEPLVRQDLAQLIAEARRLGYYTNLITSGIGLNEARIADFKKAGLDHIQISFQASDEQVNNLLAGSKKAFAQKLEMARAVKAHGYPMVLNFVTHRHNIDKIDRIIELCIALEADFVELATCQFYGWAHLNRLGLLPTRAQLERAERITNEYRDKLKAEGNPCKLIFVTPDYYEERPKACMNGWGNLFLTITPDGTALPCHGARQLPVQFPNVRDHDLHHIWYESFGFNRFRGYEWMREPCRSCDEKEKDFGGCRCQAFMLTGDASNADPVCAKSTEHGIILKAREEAETAQLAIEQMTFRNDRNSRVIARG", "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": "MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAEPQP", "text": "FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:10578051). Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain- lengths of C8-C18 (PubMed:10578051). May play an important physiological function in brain (PubMed:10578051). SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytosol."}
+{"protein": "MKFLELADLDTVNNALSFDADDCRIRGKCELYTTKSTNSDKKLFKAIENRCQEDLFALSSSKSPEYAFSLTQQSPFGPLDQSSSRRTFMYIVATLNASYPDHDFSSLQPTDFYKEPSLSRVVDSVNSTLNNIGRGRLSVNGIWEIIDRHINLSDCSVYSYTPDSDSDPYGDDALIWGMSYFFFNKNMKRMLYLSLHGLGKEVSGRNRYGNDDDSVFTPLADDAEPSDFDDDWVANMDD", "text": "FUNCTION: Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the MAF1 family."}
+{"protein": "MRKEEIPDKSRTIPIDPNLPKWVCQNCHHSLTIVGVDSYAGKFFNDPPPSATQGSSIHGANSVLGSTRMDNSFVVLPRHKPPQSQGIPPRPRGASSPQPDATQSGKAMEESFVVVYKSEPVSDSGGSHNLSLEVGQNGPLHSNTSGFNATINVLTRAFDIARTQTQVEQPLCLECMRVLSDKLEKEVEDVTRDVEAYEACVQRLEGETQDVLSEADFLKEKKKIEEEERKLVAAIEETEKQNAEVNHQLKELEFKGNRFNELEDRYWQEFNNFQFQLIAHQEERDAILAKIEVSQAHLELLNKTNVLIDAFPIRNDGEFGTINNFRLGRLPAIKVEWDEINAAWGQACLLLHTMCNYFRPKFQCQVKIQPMGSYPRIVDSNNETYELFGPVNLFWSTRYDKAMTLYLMCLKDFADFANSKDQENNIPPDNCLNLPYKIEKDKVLGYSITQSFNKQESWTKALKYTLCNLKWALYWFVGNTNFQPLSATVSLPSNISAAGSLYAKRGPDSSKPSCKKT", "text": "FUNCTION: Required for normal plant development (PubMed:17339883, PubMed:17932459, PubMed:18227644). Required for pollen germination (PubMed:17339883, PubMed:17259285, PubMed:18227644). Required for autophagic activity. Required to limit the pathogen-associated cell death response (PubMed:17932459). May be involved in vacuolar protein sorting (PubMed:17259285). Binds to microtubules. May facilitate efficient recruitment of other ATG proteins to assemble scaffolds for autophagosome biogenesis (PubMed:26566764). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Note=Colocalizes with ATG8I in punctuate structures (PubMed:17259285). Localizes in punctuate structures and colocalizes with microtubules (PubMed:26566764). SIMILARITY: Belongs to the beclin family."}
+{"protein": "MESEAIQEDLQNLDVELKDVQGQISALIEHQDRLYERKSELKTLLKALAASGSPVASSGGSSAIENWSETFEWDSRADDVRFNVFGISKYRANQKEIINAIMTGRDVLVIMAAGGGKSLCYQLPAMLRGGTTLVVSPLLSLIQDQVMGLAALGISAYMLTSTSGKENEKFVYKALEKGEDDLKILYVTPEKVSKSKRFMSKLEKCHNAGRLSLISIDEAHCCSQWGHDFRPDYKNLSILKTQFPKVPMVALTATATQKVQNDLIEMLHIPKCVKFVSSVNRPNLFYSVREKSAVGKLVVDEIAEFIRESYSNNESGIVYCFSRKECEQIAGDLRERGISADYYHADMDANMREKVHMRWSKNKLQVIVGTVAFGMGINKPDVRFVIHHSLSKSMETYYQESGRAGRDGLPSECILFFRSADVPRQSSMVFYEYSGLQNLYDIVRYCQSKTKCRRSAFFRHFGEPSQDCNGMCDNCALSSEVKEVDVSDLSKLVVSMVQETQAKDQRVTMLQLGDKLRNKHKDLIAELKRDEVEHLVIKLIVDSVLKEEFQHTPYSTNAYVTMGPLANQLLQGRKTIKMETSSRQTKKLKRSITFSGLELKLDELRKEISAADGSILPHTVLSTQQIGSISSQKPVSLQELESIIGKLKTEKYGDRILEEVMRHEAVSEQLVEDPTKEETCKSRLRKRAKTQKDVVLVESSGEEEA", "text": "FUNCTION: 3'-5' DNA helicase that may play a role in the repair of DNA (PubMed:18419780, PubMed:19755539). Its DNA unwinding activity in vitro is dependent on magnesium, and ATP or dATP (PubMed:18419780, PubMed:19755539). Can use GTP/dGTP, CTP/dCTP or UTP/dUTP as nucleotide cofactors (PubMed:18419780, PubMed:19755539). Catalyzes Holliday junction branch migration and replication fork regression (PubMed:19755539, PubMed:23771268). Disrupts D-loop structures (PubMed:18419780). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the helicase family. RecQ subfamily."}
+{"protein": "MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGSLLVIFCVELACGVWTYEQELMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNFFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMMSLKNDNSQHLSCPSVELLKPSLSRIFEHTSMANSFNTHFEMEEL", "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) (By similarity). 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. 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": "MPVFKAPFNGYSVKFSPFYESRLAVATAQNFGILGNGRIHVLELAPGAPGVTESVSYDTADAVYDVCWSESHDSVLIAAIGDGSVKIYDTALPPPSNPIRSFQEHAREVQSVDYNPTRRDSFLTSSWDDTVKLWAMDRPASVRTFKEHAYCVYQAVWNPKHGDVFASASGDCTLRIWDVREPGSTMIIPAHDFEILSCDWNKYDDCILATSSVDKTVKVWDVRSYRVPLAVLNGHGYAVRKVKFSPHRRSLIASCSYDMSVCLWDYMVEDALVGRYDHHTEFAVGIDMSVLVEGLMASTGWDELVYVWQQGMDPRAS", "text": "FUNCTION: Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal (PubMed:15548601, PubMed:15637057, PubMed:17478547, PubMed:19594707, PubMed:20130089). Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol (PubMed:15548601, PubMed:15637057, PubMed:17478547, PubMed:19594707, PubMed:20130089). Cargo protein-binding triggers interaction with PEX5 and formation of a ternary complex composed of PEX5 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex (PubMed:15548601, PubMed:15637057, PubMed:17478547, PubMed:19594707, PubMed:20130089). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome matrix Note=The loss of PEX12, PEX13 or PEX14 prevents the targeting of PEX7 to peroxisomes. SIMILARITY: Belongs to the WD repeat peroxin-7 family."}
+{"protein": "MTGMTNVTKLASEPSGQEFLVFTLGDEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRIKFSQVDVDYNDNTVVIVLNLGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLSTEYLTGLGALGDRMLILVNIEKLLNSEEMALLDSAASEVA", "text": "FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. It physically bridges CheA to the MCPs (methyl-accepting chemotaxis proteins) to allow regulated phosphotransfer to CheY and CheB (By similarity). FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. It physically bridges CheA to the MCPs (methyl-accepting chemotaxis proteins) to allow regulated phosphotransfer to CheY and CheB. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MKRIITLTVVNRSGVLNRITGLFTKRHYNIESITVGHTETAGVSRITFVVHVEGENDVEQLTKQLNKQIDVLKVTDITNQSIVQRELALIKVVSAPSTRTEINGIIEPFRASVVDVSRDSIVVQVTGESNKIEALIELLKPYGIKEIARTGTTAFARGTQQKASSNKTISIV", "text": "SIMILARITY: Belongs to the acetolactate synthase small subunit family."}
+{"protein": "MAVSLDDDVPLILTLDEGGSAPLAPSNGLGQEELPSKNGGSYAIHDSQAPSLSSGGESSPSSPAHNWEMNYQEAAIYLQEGENNDKFFTHPKDAKALAAYLFAHNHLFYLMELATALLLLLLSLCEAPAVPALRLGIYVHATLELFALMVVVFELCMKLRWLGLHTFIRHKRTMVKTSVLVVQFVEAIVVLVRQMSHVRVTRALRCIFLVDCRYCGGVRRNLRQIFQSLPPFMDILLLLLFFMIIFAILGFYLFSPNPSDPYFSTLENSIVSLFVLLTTANFPDVMMPSYSRNPWSCVFFIVYLSIELYFIMNLLLAVVFDTFNDIEKRKFKSLLLHKRTAIQHAYRLLISQRRPAGISYRQFEGLMRFYKPRMSARERYLTFKALNQNNTPLLSLKDFYDIYEVAALKWKAKKNREHWFDELPRTALLIFKGINILVKSKAFQYFMYLVVAVNGVWILVETFMLKGGNFFSKHVPWSYLVFLTIYGVELFLKVAGLGPVEYLSSGWNLFDFSVTVFAFLGLLALALNMEPFYFIVVLRPLQLLRLFKLKERYRNVLDTMFELLPRMASLGLTLLIFYYSFAIVGMEFFCGIVFPNCCNTSTVADAYRWRNHTVGNRTVVEEGYYYLNNFDNILNSFVTLFELTVVNNWYIIMEGVTSQTSHWSRLYFMTFYIVTMVVMTIIVAFILEAFVFRMNYSRKNQDSEVDGGITLEKEISKEELVAVLELYREARGASSDVTRLLETLSQMERYQQHSMVFLGRRSRTKSDLSLKMYQEEIQEWYEEHAREQEQQRQLSSSAAPAAQQPPGSRQRSQTVT", "text": "FUNCTION: Intracellular channel initially characterized as a non- selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid adenine dinucleotide phosphate), it is also a voltage-gated highly- selective Na(+) channel activated directly by PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate) that senses pH changes and confers electrical excitability to organelles (PubMed:19620632, PubMed:23063126, PubMed:24776928, PubMed:23394946). Localizes to the early and recycling endosomes membranes where it plays a role in the uptake and processing of proteins and regulates organellar membrane excitability, membrane trafficking and pH homeostasis (PubMed:23394946) (Probable). Ion selectivity is not fixed but rather agonist-dependent and under defined ionic conditions, can be readily activated by both NAADP and PI(3,5)P2 (Probable). Required for mTOR-dependent nutrient sensing (PubMed:23394946) (Probable). FUNCTION: (Microbial infection) During Ebola virus (EBOV) infection, controls the movement of endosomes containing virus particles and is required by EBOV to escape from the endosomal network into the cell cytoplasm. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Recycling endosome 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": "MAVCTVYTIPTTTHLGSSFNQNNKQVFFNYKRSSSSNNTLFTTRPSYVITCSQQQTIVIGLAADSGCGKSTFMRRLTSVFGGAAEPPKGGNPDSNTLISDTTTVICLDDFHSLDRNGRKVEKVTALDPKANDFDLMYEQVKALKEGKAVDKPIYNHVSGLLDPPELIQPPKILVIEGLHPMYDARVRELLDFSIYLDISNEVKFAWKIQRDMKERGHSLESIKASIESRKPDFDAYIDPQKQHADVVIEVLPTELIPDDDEGKVLRVRMIQKEGVKFFNPVYLFDEGSTISWIPCGRKLTCSYPGIKFSYGPDTFYGNEVTVVEMDGMFDRLDELIYVESHLSNLSTKFYGEVTQQMLKHQNFPGSNNGTGFFQTIIGLKIRDLFEQLVASRSTATATAAKA", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the phosphoribulokinase family."}
+{"protein": "MPNYKLLYFNMRGRAEIIRYIFAYLDIKYEDHRIEQADWPKIKPTLPFGKIPVLEVEGLTLHQSLAIARYLTKNTDLAGKTELEQCQVDAVVDTLDDFMSLFPWAEENQDLKERTFNDLLTRQAPHLLKDLDTYLGDKEWFIGNYVTWADFYWDICSTTLLVLKPDLLGIYPRLVSLRNKVQAIPAISAWILKRPQTKL", "text": "FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Sigma family."}
+{"protein": "MPPKKAARPAQENISLGPQIREGELVFGVARIFASFNDTFVHVTDLSGRETTDRVIGGIKVKADRDESSPYAAMLAAQDVAARCKELGITALHIKIRATGGNGTRTPGPGAQSALRALARSGMKIGRIEDVTPTPSDSTRRKGGRRGRRL", "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. uS11 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
+{"protein": "MGFFIPQSSLGNLKLYKYQSDDRSFLSNHVLRPFWRKFATIFPLWMAPNLVTLLGFCFIIFNVLTTLYYDPYFDQESPRWTYFSYAIGLFLYQTFDACDGMHARRTGQQGPLGELFDHCIDSINTTLSMIPVCSMTGMGYTYMTIFSQFAILCSFYLSTWEEYHTHKLYLAEFCGPVEGIIVLCISFIAVGIYGPQTIWHTKVAQFSWQDFVFDVETVHLMYAFCTGALIFNIVTAHTNVVRYYESQSTKSATPSKTAENISKAVNGLLPFFAYFSSIFTLVLIQPSFISLALILSIGFSVAFVVGRMIIAHLTMQPFPMVNFPFLIPTIQLVLYAFMVYVLDYQKGSIVSALVWMGLGLTLAIHGMFINDIIYDITTFLDIYALSIKHPKEI", "text": "FUNCTION: Catalyzes the final step in the CDP-choline route leading to phosphatidylcholin (PC). Preferentially uses CDP-monomethylethanolamine as aminoalcohol substrate. Shows highest activity toward di- and mono- unsaturated diacylglycerol species as lipid substrates. The CDP-choline pathway only contributes to net PC synthesis if exogenous choline is present. In its absence, this pathway recycles choline from PC turnover and may contribute to maintaining the proper PC species composition. SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family."}
+{"protein": "MIIINKYIRMNKIAILFSFFILICCTGYSISYKINGINENKVLSLSSSPSPSSSSSSSQILEKGKEEIKKIKKTNKNKLLYNVAIVDLEPKLEIEQELLTRNNKKKMEMKEEMDIAMMMMKAADRTDQVSTSSSSSSFSEENKKSSSDDSAPAIQSNLTFSGYMTGGEQVCDPKSCNSPSVFTQNYLCNTSSAWANGYVFHDPVPPTGLFVVHKIVVTFTGMFNVIPPTSMVFSLVNGEENAGIFFISKSSPSQCPNCQISFSPRTLPDVDPNGLASYRYGSNNSIIFNLFETDVACIGKVTANIFYGPVAFKVNSVVPNTAPSTGGETVYFIGEQFYQSSQIQCKFGTVISTGTYINSTCASCVVPPMLQSNSTTPSDYNVTIQLSEDGGSSFCLNTTFFIYTAASIPFVKPTSPNYQKIIYIVVGVGIAVLLIIAVGIYFIIRLRIKNKRLNGSKHALPIGINDDERSPLLKTDYKTLFEIKPIDISEIVVQNRIGRGSCAEVFTGTWRGIIVAIKKAKLLNEDDEDFLNELAQEATIMSQLRHPNICQFLGTCNNPPEILIVMEYMPLGSLYRILHDPSISLDWPRMKSMALDIAKGMNYLHCCDPIVIHRDLKSHNLLVDEHYRVKISDFGLSTRFKKHLDKKTAMTPVGTPCWTAPEVLRNDPYTEKADVFSFAIVLWEIVTREDPYQGMPTFQIVISVGQHKLRPIVPPQVSAPFTRLITECWSEDPQQRPSFQEIVKRLEAM", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family."}
+{"protein": "MGCDDKCGCAVPCPGGTGCRCTSARSGAAAGEHTTCGCGEHCGCNPCACGREGTPSGRANRRANCSCGAACNCASCGSATA", "text": "FUNCTION: Binds 5 molecules of zinc. May have a role in Zn(2+) homeostasis during embryogenesis. SIMILARITY: Belongs to the metallothionein superfamily. Type 15 family."}
+{"protein": "MVEQLLLPLWNSLATVDDETLPLMSTALLIARDEYPDLDANLYDTLVQSYVEYLRSEVEEISLWPLKMAAVNRYLFQKLGYSGNHDEYYDPRNSYLNQVFERRLGNPISLAVIQIEVARRLGIPLDGVSFPGHFLVRLPVDDGILVMDPFNGGRPLDAEELRERVRPHLGGEVPDDRALAQILNPAPHRTILVRILRNLHSVYANTNRWDRAARCADRILKLVPNQPEALRDRGLAYLQLGHRSGARNDLTRYLQLYPSTHNVDMVRGHLVDLSNERIQTH", "text": "SIMILARITY: Belongs to the UPF0162 family."}
+{"protein": "MIDDQRDMQVDSVNQEENVDSGETKQNTVTEVPRTVLQDVEANIAALMQATKQRDPRLVYRSLRTTSNICHRLNADVLGQLIKKYYSFDNSLKNELLELIDMPQNGDDSSTSITNGNGNTIFPEVDMYLQLLLSMTLYYNEKYEVGAEYIKKVIARLQSYDRRTLDQIAAKLYFYYILFFEKCNRSVECRNTLLSVHRTASLRHDSETQAMVLTLLLRNYIQFNLYDQADRLVSKTSFLTNASNNLAIRYQYYLGRIRAIQLDYTTAHEHLVSAIRKAPNTVYAVQFLEAVYKLHIVVQLLMGEIPERRIFRQKSLEKTLVPYLRISQAVRIGDLCAFTDALSKYEAEFRFDGLYTLICRLRHTVIKTGLRMISLSYSRISLRDVCIKLGLDSEESAEYIVAKGIRDGVIDASIDHSNAFMASNEAMDIYSTEQPQQAFHERIQFCLALHNDSIKSMRYPMDAHKSELEGVEEARRRMDKEMAEADLDDDEPDLGEF", "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 S3 family."}
+{"protein": "MIEVVLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLHLEKNKELFSKDYSETHYSPDGRKITTNPSVEDHCYYRGRIENDADSTASISACNGLKGHFKLQGELYLIEPLELSDSEAHAVFKLENVEKEDEAPKMCGVTQNWESYEPIKKASDLNLNPDQQNLPQRYIELVVVADHRVFMKYNSDLNTIRTRVHEIVNFINGFYRSLNIHVSLTDLEIWSNEDQINIQSASSDTLNAFAEWRETDLLNRKSHDNAQLLTAIELDEETLGLAPLGTMCDPKLSIGIVQDHSPINLLMGVTMAHELGHNLGMEHDGKDCLRGASLCIMRPGLTKGRSYEFSADSMHYYERFLKQYKPQCILNKPLRIDPVSTPVSGNELLEAGEE", "text": "FUNCTION: Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I subfamily."}
+{"protein": "FFGSMIGALAKGLPSLISLIKK", "text": "FUNCTION: Antimicrobial peptide. Active against Gram-negative bacterium E.coli (MIC=12.5 uM) and against Gram-positive bacterium S.aureus (MIC=12.5 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
+{"protein": "MCKGLAALPHSCLERAKEIKIKLGILLQKPDSAVDLVIPYNEKPEKPAKAHKPSLEEVLQWRQSLDKLLQSNYGFASFKSFLKSEFSEENLEFWVACENYKKIKSPIKMAEKAKQIYEEFIQTEAPKEVNIDHFTKDITMKNLVEPSPHSFDLAQKRIYALMEKDSLPRFVRSEFYKELIN", "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: Cytoplasm Membrane."}
+{"protein": "MKTQRDSPSLGRWSLVLLLLGLVMPLAIVAQVLSYQEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQKSPEDCDFKEDGLVKRCVGTVILNQARDSFDISCDKDNRRSARLGNFFRKVKEKIGGGLKKVGQKIKDFLGNLVPRTAS", "text": "FUNCTION: [Antibacterial peptide LL-37]: Antimicrobial peptide that is an integral component of the innate immune system (By similarity). Binds to bacterial lipopolysaccharides (LPS) (By similarity). Causes membrane permeabilization by forming transmembrane pores (in vitro) (By similarity). Causes lysis of E.coli (By similarity). Exhibits antimicrobial activity against Gram-negative bacteria such as P.aeruginosa, S.typhimurium, E.aerogenes, E.coli and P.syringae, Gram- positive bacteria such as L.monocytogenes, S.epidermidis, S.pyogenes and S.aureus, as well as vancomycin-resistant enterococci (in vitro) (By similarity). Exhibits antimicrobial activity against methicillin- resistant S.aureus, P.mirabilis, and C.albicans in low-salt media, but not in media containing 100 mM NaCl (in vitro) (By similarity). Forms chiral supramolecular assemblies with quinolone signal (PQS) molecules of P.aeruginosa, which may lead to interference of bacterial quorum signaling and perturbance of bacterial biofilm formation (By similarity). May form supramolecular fiber-like assemblies on bacterial membranes (By similarity). Induces cytokine and chemokine producation as well as TNF/TNFA and CSF2/GMCSF production in normal human keratinocytes (By similarity). Exhibits hemolytic activity against red blood cells (By similarity). FUNCTION: [Antibacterial peptide FALL-39]: Exhibits antimicrobial activity against E.coli and B.megaterium (in vitro). FUNCTION: Antimicrobial protein that is an integral component of the innate immune system (By similarity). Binds to bacterial lipopolysaccharides (LPS) (By similarity). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (By similarity). Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (By similarity). The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram- negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (By similarity). SUBCELLULAR LOCATION: Secreted Vesicle Note=Stored as pro-peptide in granules and phagolysosomes of neutrophils (By similarity). Secreted in sweat onto skin (By similarity). SIMILARITY: Belongs to the cathelicidin family."}
+{"protein": "MGEGSRRPSGMLMSVDLEPVQLVGPDGTPTAERRYHRDLPEETLRWLYEMMVVTRELDTEFVNLQRQGELALYTPCRGQEAAQVGAAACLRKTDWLFPQYRELGVYLVRGIPPGHVGVAWRGTWHGGLQFTTKCCAPMSVPIGTQTLHAVGAAMAAQRLDEDSVTVAFLGDGATSEGDVHEALNFAAVFTTPCVFYVQNNQWAISMPVSRQTAAPSIAHKAIGYGMPGIRVDGNDVLACYAVMAEAAARARAGDGPTLIEAVTYRLGPHTTADDPTRYRSQEEVDRWATLDPIPRYRTYLQDQGLWSQRLEEQVTARAKHVRSELRDAVFDAPDFDVDEVFTTVYAEITPGLQAQREQLRAELARTD", "text": "FUNCTION: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched- chain alpha-ketoacids to acyl-CoA and CO(2). FUNCTION: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched- chain alpha-ketoacids to acyl-CoA and CO(2)."}
+{"protein": "MASSTVSVVLSLFLLLLTQAYSADIQSFSFKNFNSSSFILQGDATVSSSKLRLTKVKGNGLPTLSSLGRAFYSSPIQIYDKSTGAVASWATSFTANIFAPNKSSSADGIAFALVPVGSEPKSNSGFLGVFDSDVYDNSAQTVAVEFDTFSNTDWDPTSRHIGIDVNSIKSIRTASWGLANGQNAEILITYNAATSLLVASLVHPSRRTSYIVSERVDITNELPEYVSIGFSATTGLSEGYTETHDVLSWSFASKLPDDSTTEPLDIASYLVRNVL", "text": "FUNCTION: Metalloglycoprotein, containing Ca, Mg, Mn, and Zn and the carbohydrates galactose, glucosamine, mannose, and fucose. It agglutinates erythrocytes of blood group A1. SIMILARITY: Belongs to the leguminous lectin family."}
+{"protein": "MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS", "text": "FUNCTION: Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). SUBCELLULAR LOCATION: Membrane; Lipid-anchor Cytoplasm Microsome Mitochondrion Nucleus Cytoplasm, perinuclear region Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity)."}
+{"protein": "MHLTVFYLVALCTFASADDQPRYIINKLPYEQIKPFPAVEPDCRINEIALQFQPQLHISSGCHPYPAVDKNGYISTGLGVSHVFTDCDGSPEGSQVYGRAYVYKGYLAIMYAWYFPRDYMVSPVWIGHRNAWEHAVLWLGGLTEDPELLAVAAKSMWGYRTYAPPKSKYMKDDSFKLEYSWMVMSHHYLTATKDPGEFQDLIMWNNMTERARESLRLKSSSHFKSPLSDDRFFRALRKSYPF", "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": "MASELPMSPHLEQIHGEIRDHFRALANGFQRLDKIKDSSRQSKQLEELAEKMRDCKRLVKEFDRELKDGEARNSPQVNKQLNDEKQSMIKELNSYVALRKTYLNTLGNKKVELFDTGAGVSGEPTAEENVQMASTMSNQELVDAGMKRMDETDQAIERSKQVVHQTLEVGTQTASNLKGQTDQMGRVVNDLDTIQFSLKKASQLVKEIGRQVATDKCIMAFLFLIVCGVIAIIIVKIVNPNNKDIRDIPGLAPPAQSRKLLYFRE", "text": "FUNCTION: Vesicle trafficking protein that functions in the secretory pathway. SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the novel plant SNARE family."}
+{"protein": "MDFIFHEKQEGFLCAQHCLNNLLQGEYFSPVELASIAHQLDEEERMRMAEGGVTSEEYLAFLQQPSENMDDTGFFSIQVISNALKFWGLEIIHFNNPEYQKLGIDPINERSFICNYKQHWFTIRKFGKHWFNLNSLLAGPELISDTCLANFLARLQQQAYSVFVVKGDLPDCEADQLLQIISVEEMDTPKLNGKKLVKQKEHRVYKTVLEKVSEESDESGTSDQDEEDFQRALELSRQETNREDEHLRSTIELSMQGSSGNTSQDLPKTSCVTPASEQPKKIKEDYFEKHQQEQKQQQQQSDLPGHSSYLHERPTTSSRAIESDLSDDISEGTVQAAVDTILEIMRKNLKIKGEK", "text": "FUNCTION: Deubiquitinating enzyme that cleaves both 'Lys-48'-linked and 'Lys-63'-linked poly-ubiquitin chains (in vitro). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAKLSPLTLIFIAACLSRILHLTILSGLSKALPLFDTSPSLLLSSPPPALRWDAIHFASVAYNGYEYEQQVAFQPGWLAVMRLAGEGVRFIRAASVVELKDVILGGTIVANVAFVAATLVLYKLTKHIFNPTFAFLTSLLYLLPPTATPSAPYTEPIYSLLTFSGIYLLSIKRQMVLAGLCFAGATTIRSTGIFNSITLMCFAVFGDAHIFDLDPKDYCKIRKKLKPFLSAILVVAPFFMFQHYTETVFCTRELKRASTARPWCSNSPPVSYGFVQKLYWNVGPFEYWTVSQLPNFALAMPILFSSLAGVVKFFSHLVSSSQVLNHGTEEIPPPPILFELYSVHVLTMALLLFTSHTQITLRVCLGDPVVWWNAVKLGFDNVQIGEAPMGQVKVNKFGRYWIGWTVVWGAVAAVLWAGHYPPA", "text": "FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGV family."}
+{"protein": "MESTNKTWTELMTPLSQFWLESSSQAWKNWFDLMAKGGAGAMMGSAPQSFESLPQQFLQSQQFYGELLKLSFEAWQSLWPKLDNGSAPGAVQGYLKQLQTQIEQYTATTQALQGDMDGLWQCYIKEVQRFSQLWLSTWQSSVAPLGKLPTGDIHAWLDLNNLYGDALYNKNLSSFMRSPLLGPSREMNGKLLRAFDDWVKLSQAMADYQLLEADIQYRGFAALMEDLLARAKEDKPVKTWKEFQQRWAIAADQVFEEAFCEEKNLKVRGKFINALNRYRIQQQEILEAWLKMLNLPTRSEVDEIHQTIYQLRKEVKSLKKRLGETEANPG", "text": "FUNCTION: When expressed in E.coli with Synechocystis PhaC and C.necator PhaA and PhaB, confers the ability to synthesize up to 13% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source; all 4 genes are necessary for PHB production (PubMed:9683655). Cell-free in vitro coexpression with PhaE gives a heterodimer able to polymerize 3- hydroxybutyrate-CoA (PubMed:25629766). This subunit has no catalytic activity but enhances the activity of PhaC, the catalytic subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PHA/PHB synthase family. Type III PhaE subfamily."}
+{"protein": "MGKIESNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPQGDCLTAAGDKLQPLPPPLSPPPRPPPLSPVPSGCFEGGAGNCSSHGGNGGNGGSDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRKLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSPVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPLASSPTFCKTELNMACNSTQSDTCLGKENRLLEHNRSVLSGDDSTGSEPPLSPPERLPIRRSSTRDKNRRGETCFLLTTGDYTCASDGGIRKGYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL", "text": "FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Contributes to the regulation of the fast action potential repolarization and in sustained high-frequency firing in neurons of the central nervous system (PubMed:10561420, PubMed:10414303, PubMed:11124984, PubMed:10903572, PubMed:11506885, PubMed:15317859, PubMed:15917463, PubMed:17761775, PubMed:21414897). Homotetramer channels mediate delayed-rectifier voltage-dependent potassium currents that activate rapidly at high-threshold voltages and inactivate slowly (PubMed:10414303). Forms tetrameric 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 (By similarity). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNC1, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:10531438, PubMed:12000114). Channel properties may be modulated by either the association with ancillary subunits, such as KCNE1, KCNE2 and KCNE3 or indirectly by nitric oxide (NO) through a cGMP- and PKG-mediated signaling cascade, slowing channel activation and deactivation of delayed rectifier potassium channels (By similarity). Contributes to fire sustained trains of very brief action potentials at high frequency in thalamocortical and suprachiasmatic nucleus (SCN) neurons, in hippocampal and neocortical interneurons and in retinal ganglion cells (PubMed:10561420, PubMed:10903572, PubMed:11506885, PubMed:17761775). Sustained maximal action potential firing frequency in inhibitory hippocampal interneurons is negatively modulated by histamine H2 receptor activation in a cAMP- and protein kinase (PKA) phosphorylation- dependent manner (PubMed:10903572). Plays a role in maintaining the fidelity of synaptic transmission in neocortical GABAergic interneurons by generating action potential (AP) repolarization at nerve terminals, thus reducing spike-evoked calcium influx and GABA neurotransmitter release (PubMed:15917463). Required for long-range synchronization of gamma oscillations over distance in the neocortex (PubMed:22539821). Contributes to the modulation of the circadian rhythm of spontaneous action potential firing in suprachiasmatic nucleus (SCN) neurons in a light-dependent manner (PubMed:21414897). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Membrane; Multi-pass membrane protein Perikaryon Cell projection, axon Cell projection, dendrite Postsynaptic cell membrane Presynaptic cell membrane Synapse, synaptosome Synapse Apical cell membrane Basolateral cell membrane Note=Colocalizes with parvalbumin in globus pallidus neurons. Localizes in thalamocortical axons and synapses (By similarity). Localizes on the surface of cell somata, proximal dendrites and axonal membranes (PubMed:12000114, PubMed:10903572). Also detected throughout the neuropil (PubMed:12000114). Localized in starburst cell somata and proximal dendrite processes (PubMed:15317859). Colocalized with GABA in presynaptic terminals (PubMed:10531438). Clustered in patches in somatic and proximal dendritic membrane as well as in axons and presnypatic terminals of GABAergic interneurons; some of these patches are found near postsynaptic sites (PubMed:10531438). SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC 1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily."}
+{"protein": "MGFPVGYTEVFLPKLFVQTLSILGFIRTIVFSIFRFLGLSDFLEMDQTWPDYTSYPTRIPETRSPFSALLIREILPVIKFEELTNSGEDLPENCAVCLYEFEGEQEIRWLRNCRHIFHRSCLDRWMDHDQKTCPLCRTPFVPDEMQEEFNQRLWAASGVHDFHCPVTELL", "text": "FUNCTION: May be involved in the brassinosteroids (BRs) signaling pathway and regulate the growth and development of rosette leaves (PubMed:28887625). Seems to prevent over development of leaves and inflorescence stems (PubMed:12012249). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RING-type zinc finger family."}
+{"protein": "MSVHPRNQGKDDCCEKTHLDSQYSPGYYWLGNNTLKVPLVLHKENRQRLVSQILSKHKDQVKENSFILLESGKSTMQYDTDHEPLFKQERYFFWTFGSDIPDCFGIVGLDEQATSILCIPKLPAEYATWMGEIRSKEYYKSIFLVDQVLYVDEMMDYLKSKNASTIYTILGTNTDSGSTFVEPQYPGLRETFNVNNTLLFPEIAECRVIKSPKEVEVIRYCVDASVSAHKHVMRKVKVGLKEYQCESEFLHHVYNEWGCRNVGYTCICAANKNSAVLHYGHAGEPNSATISENGFCLFDMGAEYHSYTADITCSFPATGKFSPEQRVVYQAVLDASVAVMEAMRPGVSWVDMHKLAERCILAALLKAGILVGDLQDLIANKIGSVFFPHGLGHFLGLDTHDVGGYLGDCQPKVHSLRTTRTLKAGMVITSEPGCYFINHLLTQALSNPETAKFFNLTELDKYRNIGGVRIEDDILVTETGCDNLSKNLPRTIDEIEAFMLK", "text": "FUNCTION: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position. SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily."}
+{"protein": "MPTPSHLKNPLCFDFRAARRVPETHAWPGLDDHPVVDGGGGGGEDAVPVVDVGAGDAAARVARAAEQWGAFLLVGHGVPAALLSRVEERVARVFSLPASEKMRAVRGPGEPCGYGSPPISSFFSKLMWSEGYTFSPSSLRSELRRLWPKSGDDYLLFCDVMEEFHKEMRRLADELLRLFLRALGLTGEEVAGVEAERRIGERMTATVHLNWYPRCPEPRRALGLIAHTDSGFFTFVLQSLVPGLQLFRRGPDRWVAVPAVAGAFVVNVGDLFHILTNGRFHSVYHRAVVNRDRDRVSLGYFLGPPPDAEVAPLPEAVPAGRSPAYRAVTWPEYMAVRKKAFATGGSALKMVSTDAAAAADEHDDVAAAADVHA", "text": "FUNCTION: Catalyzes the 3-beta-hydroxylation of the inactive gibberellin precursors, leading to the formation of bioactive gibberellins. In vitro, converts the precursors GA20, GA5, GA44 and GA9 to the corresponding 3-beta-hydroxylated active products GA1, GA3, GA38 and GA4, respectively. Involved in the production of bioactive GA for vegetative growth and development (PubMed:11438692). Controls the elongation of the vegetative shoot and plant height by the regulation of active gibberellin levels (Ref.7). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
+{"protein": "MASHDKRDYQAELTDAALAADLATAAGELLLEIREEIGFDQPRALGDAGDRLANSLLLSRLRAERPGDAVLSEEAHDDRVRLQAGRVWIIDPLDGTREFSTAGRTDWAVHIALWQRTTGGVADGRREITDAAVALPARGNRVYRSDTVTAGAVTGGVPNILRIAVSATRPPTILHRIRQKLAIEPVAIGSAGAKAMAVVDGDVDAYLHVGGQWEWDSAAPAGVVLAAGMHASRLDGSPLRYNQLDPYLPDFVMCRADIAPILLGVIREVWQ", "text": "FUNCTION: Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'- phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathway by controlling the pools of PAP and PAPS in the cell. To a lesser extent, is also able to hydrolyze inositol 1-phosphate (I-1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F-6-P)) and AMP in vitro, but this might not be significant in vivo (By similarity). SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
+{"protein": "MADPEDPRDAGDVLGDDSFPLSSLANLFEVEDTPSPAEPSRGPPGAVDGKQNLRMKFHGAFRKGPPKPMELLESTIYESSVVPAPKKAPMDSLFDYGTYRQHPSENKRWRRRVVEKPVAGTKGPAPNPPPILKVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTENGHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQHIIRREIADEDVRHLSRKFKDWAYGPVYSSLYDLSSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLCAMIIFTLIAYYRPMEGPPPYPYTTTIDYLRLAGEIITLLTGILFFFSNIKDLFMKKCPGVNSFFIDGSFQLLYFIYSVLVIVTAGLYLGGVEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPSSESCSEDHSNCTLPTYPSCRDSQTFSTFLLDLFKLTIGMGDLEMLESAKYPGVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPLFLRRVFRSGEMVTVGKGTDGTPDRRWCFRVDEVNWSHWNQNLGIISEDPGKSDTYQYYGFSHTVGRLRRDRWSTVVPRVVELNKSCPTEDVVVPLGTMGTAEARERRHGQTPSSPL", "text": "FUNCTION: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:11081638). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:11081638). Also activated by phorbol esters (PubMed:19864432). Channel activity seems to be regulated by a calmodulin-dependent mechanism (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cell junction, adherens junction. SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV4 sub-subfamily."}
+{"protein": "MWLEATTHPGLEDLLLEELSALYPGEGAEVDARKGRVRIPRAWVGEEALGLRLAHHLVLFRARLLLSREDPLGALERAALALPWPELEGAGSFRVEARREGEHPFTSPEVERRVGEALHRAYGVPVDLKRPAVRVRVDVRGEEAFLGVQLTERPLSRRFPKAALRGSLTPVLAQALLRLADARPGMRVLDPFTGSGTIALEAASTLGPTSPVYAGDLDEKRLGLAREAALASGLSWIRFLRADARHLPRFFPEVDRILANPPHGLRLGRKEGLFHLYWDFLRGALALLPPGGRVALLTLRPALLKRALPPGFALRHARVVEQGGVYPRVFVLEKL", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Phe). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "MAARYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGKDIVVLGVEKKSVAKLQEERTVRKICALDEHVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIATLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTDEAIASDNDAIKLAIKALLEVVQSGGKNIELAVIRRNQPLKILESKEIETLVAEIEKEKEEEAEKKKQKKSS", "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 T1A family."}
+{"protein": "MDATAFHPSLWGDFFVKYEPPTAPKRGHMTQRAELLKEEVRKTLKAAANQIKNALDLIITLQRLGLDHHYENEISELLRFVYSSSDYDDKDLYVVSLRFYLLRKHGHRVSSDVFMSFKDEEGNFVVDDTKCLLSLYNAAYLMTHGEKVLDEAITFTRRQLEALLLDPLEPALADEVYLTLQTPLFRRLRILEAVNYIPIYGKEAGRNEAILELAKLNFNLAQLIYCEELKEVTLWWKQLNVETNLSFIRDRIVECHFWMTGACCEPRYSLSRVIATKMTALITVLDDMMDTYSTTEEAMLLAEAIYRWEENAAELLPGYMKHFYLYLLKTIDSCGGELGPNRSFRTFYLKEMLKVFVRGSSQEIKWRNENYVPKTISEHLEHSGPTVGAFQVACSSFVGMGDNITKESFEWLLTYPELVKSLMNIARLLNDTASTKREQTAGHHVSTVQCYMLKHGTTMDEACEKIKELTEDSWKDMMELYLTPTEHPKLVAQTIVDFARTADYMYKETDGFTFSHTIKDMIAKLFVDPISLF", "text": "FUNCTION: Sesquiterpene cyclase catalyzing the production of sixfold more beta-farnesene than alpha-bergamotene 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": "MSIPGVNASFSSTPERLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCGLAVTDLLGTLLVSPVTIATYMKGQWPGDQALCDYSTFILLFFGLSGLSIICAMSIERYLAINHAYFYSHYVDKRLAGLTLFAVYASNVLFCALPNMGLGRSERQYPGTWCFIDWTTNVTAYAAFSYMYAGFSSFLILATVLCNVLVCGALLRMLRQFMRRTSLGTEQHHAAAAAAVASVACRGHAAASPALQRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFINQLYQPSVVKDISRNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSGRDGSAQHCSESRRTSSAMSGHSRSFLSRELREISSTSHTLLYLPDLTESSLGGKNLLPGTHGMGLTQADTTSLRTLRISETSDSSQGQDSESVLLVDEVSGSQREEPASKGNSLQVTFPSETLKLSEKCI", "text": "FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MYNKVLIIDDHPVLRFAVRVLMEKEGFEVIGETDNGIDGLKIAREKIPNLVVLDIGIPKLDGLEVIARLQSLGLPLRVLVLTGQPPSLFARRCLNSGAAGFVCKHENLHEVINAAKAVMAGYTYFPSTTLSEMRMGDNAKSDSTLISVLSNRELTVLQLLAQGMSNKDIADSMFLSNKTVSTYKTRLLQKLNATSLVELIDLAKRNNLA", "text": "FUNCTION: Member of the two-component regulatory system BvgS/BvgA. Activates the transcription of virulence genes."}
+{"protein": "MSEVASRELRNDTAGVLRRVRAGEDVTITVSGRPVAVLTPVRPRRRRWLSKTEFLSRLRGAQADPGLRNDLAVLAGDTTEDLGPIR", "text": "FUNCTION: Probable antitoxin component of a type II toxin-antitoxin (TA) system. The cognate toxin is VapC5. FUNCTION: Probable antitoxin component of a probable type II toxin- antitoxin (TA) system. The cognate toxin is VapC5 (By similarity). SIMILARITY: Belongs to the phD/YefM antitoxin family."}
+{"protein": "MSNDFKVIINGQNIDNGQKIIFEKSQDVPKPIFDIGDNEYYTIAMVDPDAPSRENPIYKYFLHMLIVNNYQTLVSFQPPSPPKGSGYHRYFFFLLKQPKYIDQNIWKQQINNNSIRREKFNLSEFISDNKLTVIASTYFKTKR", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family."}
+{"protein": "MESKPSRIPRRISVQPSGSLSARMVSGNRGTSLNDSYHSRDSSFRLDSEYQSASASASASPYQSTWYSESEITQGARSRSQNQQRDHDSKRPKLSCTNCTSTSAGRNIGSGLNTLSDSSWRPGQVPRSSSMVLGSFGTDLMRERRDLERRRDSSISSLMDYSHRSGDFTAPAYVQERVPSSYSQGARPKENAANTLQLNSSTNHQLPSEHQTVPSSRDSSRSSFRSHFSPRQSESFRNSSHPAFSYLSSRNETPTISSSERAGSSQRPFQESSDNEGRRTTRRLLSRIASSMSSTFFSRRSSQDSLNTRSLSSENYISPRTLTSQSRNNGASSSEVNDGRASEASQGFRFLRRRWGLSSLSQNHSSEPDAENFNQESEGRNTGPWLSSSLRNRCTPLFSRRRREGRDESSRISPSDVPPRSHLFRRESNEVVHLEAQGDSLGAAASRPQASGASGNASASGSTPDLPQGGRNTGIAGILPGSLFRFAVPPALGSNLTDNVTITVDIIPSGWSSADGKSEKAKSAPSRDPEKLQKIKESLLLEDSDEEEEGDLCRICQMAAASSSNLLIEPCKCTGSLQYVHQECMKKWLQAKINSGSSLEAVTTCELCKEKLQLNLEDFDIHELHRAHANEQAEYEFISSGLYLVVLLHLCEQSFSDMMGNTIEPSTRVRFINLARTLQAHMEDLETSEDEF", "text": "FUNCTION: E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. 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 (By similarity). May be involved in T-cell proliferation by regulating LIF secretion (By similarity). May play a role in lysosome homeostasis (By similarity)."}
+{"protein": "MKIAIEGCMHGDLDNVYKTIQHYEQIHNTKVDLLLCCGDFQAVRNEKDMDSLNVPRKYREMKSFWKYYSGQEVAPIPTIFIGGNHEASNYLWELYYGGWAATNIYFLGFAGVVKFGNVRIGGLSGIYNERHYRSGHFERPPYNESTIRSVYHVRDYDVQKLMQLEEPLDIFLSHDWPVGITDYGDSESLMRQKPYFRQEIEEKTLGSKPAALLLEKLKPQYWFSAHLHCKFAAAVQHGNDGSVTKFLALDKCLPGKKFLQIIEIESEPGPFEVLYDEEWLAITRKFNSIFPLTRRYTNVSTAGTIQESREWVRKKLEERQFKPFEFARTVPAYNPSQRVFDSIPEIPQNPQTLSLLELLGLPYLLDSSPVTGERTDIPASLAPSDLPTYDSEEIPIDDIDEIEEMEEAKADDHTRDDA", "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. It may also participate in retrovirus replication via an RNA lariat intermediate in cDNA synthesis. Plays en essential role during embryogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the lariat debranching enzyme family."}
+{"protein": "MDIVSLAWAVLMVVFTFSLSLVVWGRSGL", "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": "MQPEGAEKGKSFKQRLVLKSSLAKETLSEFLGTFILIVLGCGCVAQAILSRGRFGGVITINVGFSMAVAMAIYVAGGVSGGHINPAVSLAMCLFGRMKWFKLPFYVGAQFLGAFVGAATVFGIYYDGLMSFAGGKLLIVGENATAHIFATYPAPYLSLANAFADQVVATMILLIIVFAIFDSRNLGAPRGLEPIAIGLLIIVIASSLGLNSGCAMNPARDLSPRLFTALAGWGFEVFRAGNNFWWIPVVGPLVGAVIGGLIYVLVIEIHHPEPDSVFKTEQSEDKPEKYELSVIM", "text": "FUNCTION: Forms a water channel with a broad specificity. Also permeable glycerol and urea. Mediates passage of a wide variety of small, non-charged solutes including carbamides, polyols, purines, and pyrimidines. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
+{"protein": "MKSLVLGLLVGSAIASGPLQHVLHAPPDPEPKPEPEPQVVKDPFEELRDTFDRLRNKAGDIWDDVMDNIPNIMSNMRPLTIPAKKFTRRPDSEWTHIVRGADLEALWVDDESGYKHRKIDGKLSQYDLRIKAVDPSDLGIDKVKQYSGYLDDNANDKHLFFWFFESRNDPFGDPVVLWLNGGPGCSSLTGMFFELGPASIDENITANYNPYSWNSNSSIIFLDQPVNVGYSYSSQAVSDTVTAAKDVYALLTLFFTQFRQYSAQDFHIAGESYAGHYIPVFASEILHHNNTNINLQSVLIGNGLTDPLSQYPFYRPMACGDGGYPSVLDSQSCQSMDNALPRCLSMIKSCYDIESTFTCLPASIYCNNALIGPYQKTGRNPYDVRTNCTGNDLCYPQLNYITEYLNKPHVMRSLGVEVDSYESCNMDINRNFLFHGDWMKPYHRLVPSLLARIPVLIYAGDADFICNWLGNKAWTEALEYPGHAKFAEAPMENLTMINSQGKNEVFGEVKSHSNLTFMRIFKAGHMTPFDSPQASLEFANSWLSGEWSEV", "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": "MTHLFEGVGVALTTPFTNNKVNIEALKTHVNFLLENNAQAIIVNGTTAESPTLTTDEKERILKTVIDLVDKRVPVIAGTGTNDTEKSIQASIQAKALGADAIMLITPYYNKTNQRGLVKHFEAIADAVKLPVVLYNVPSRTNMTIEPETVEILSQHPYIVALKDATNDFEYLEEVKKRIDTNSFALYSGNDDNVVEYYQRGGQGVISVIANVIPKEFQALYDAQQSGLDIQDQFKPIGTLLSALSVDINPIPIKALTSYLGFGNYELRLPLVSLEDTDTKVLRETYDTFKAGENE", "text": "FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). 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": "MVKKKIDNRIRVMIENGVKLGHRTMFIVIGDKARDQVPILYDILTKSTVKARPTVLWCYKNKDEAISNHGKKRAKKIAVGKVDVNEADLFDSFRVATTIHGRYYSETHAVLGRTYGVCVLQDFEALTPNLLARTVETVEGGGLIILLLKTLQSLKQLYTMSMDVHKRFRTEAHQTVTCRFNERLILSLADCKRCLVVNDDLTVLPLSSKTINVEPVNPAGAGRSPNEASLKELKESLLTVQPAGALVNLCKTYDQANAVAQFIEALVDKQLKPPMSLTAARGRGKSAALGLSIAAAVAFGYVNIYVTSPHPENLITLFEFVLKGFDALEYQEHADYTIIRSTNADYKKAIIRINITRSSRQTIQYIAPSDTHLLNAADLLLIDEAAAIPLPLVKKMIGPYLVFMASTINGYEGTGRSLSLKLISQLQKDNNARPPLKLEESIRYQENDDIEKWLINLLCLDASTVPSISSGCPTPDACELYYVDRDALFSYHKAAEAFLHRLVSIYVSSHYKNTPNDLQMMSDAPAHHLFCLLGPVQRMDALPEILVVIQVALEGQISAQSISDSLGRGKKAAGDLIPWNVAEQYGDRDFPKLCGVRIVRVATHPNYQRMGYGKRAIQLLKDYYARKHTNLEDGPVASKDAGKGIEEVEEEELSLLKEQIRPRSRIPTLLQRLHERVPEHVDYIGTSYGLTTELLKFWKNAGFVPVYLSQKSNELTAEHSCIMLHTPNATPWLGLYYQDFRRRVLKLMGKTFREFETKLCLALLKNKSVDTEGSALKVLDKPMLDVYFLPHDLQRLESYARQQSEFRLIIDLLTDIAQLYFQGRIDGLQLDLVQQGILLALGVQGKTVDALGLELNMPGNQLLAKFFDAMKRCNQCFRSVLEEHIEGGMLREADLSKGEELQPLTLSLDKELDQTAQKLSKQQRKELKRLKAEQLDEFQIKGTEEDWSKALETNGTGGGSGLLSVKSGVKRLDGPIETREDGDLAAPLSKKKKKNNPKQRRSQGKSLI", "text": "FUNCTION: RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs. Requires a tRNA-binding adapter protein for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (Probable). 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. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility (PubMed:11493925). 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 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily."}
+{"protein": "MGILLGLLLLGHLTVDTYGRPILEVPESVTGPWKGDVNLPCTYDPLQGYTQVLVKWLVQRGSDPVTIFLRDSSGDHIQQAKYQGRLHVSHKVPGDVSLQLSTLEMDDRSHYTCEVTWQTPDGNQVVRDKITELRVQKLSVSKPTVTTGSGYGFTVPQGMRISLQCQARGSPPISYIWYKQQTNNQEPIKVATLSTLLFKPAVIADSGSYFCTAKGQVGSEQHSDIVKFVVKDSSKLLKTKTEAPTTMTYPLKATSTVKQSWDWTTDMDGYLGETSAGPGKSLPVFAIILIISLCCMVVFTMAYIMLCRKTSQQEHVYEAARAHAREANDSGETMRVAIFASGCSSDEPTSQNLGNNYSDEPCIGQEYQIIAQINGNYARLLDTVPLDYEFLATEGKSVC", "text": "FUNCTION: Phagocytic receptor, strong negative regulator of T-cell proliferation and IL2 production. Potent inhibitor of the alternative complement pathway convertases. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MGFNVPVINRDSEILKADAKKWLEQQDNQKKCVLVIVSIALLLDNMLYMVIVPIIPKYLRDIHNYQVTFEGYHNETSQLANGTYLVREVGGRINFLDEELELGWLFASKALLQIFVNPFSGYIIDRVGYEIPMILGLCTMFFSTAIFALGKSYGVLLFARSLQGFGSAFADTSGLAMIADRFTEENERSAALGIALAFISFGCLVAPPFGSVLYSLAGKPVPFLILSFVCLADAIAVFMVINPHRRGTDSHGEKVQGTPMWRLFMDPFIACCSGALIMANVSLAFLEPTITTWMSEMMPDTPGWLVGVIWLPPFFPHVLGVYVTVKMLRAFPHHTWAIAMVGLAMEGIACFAIPYTTSVMQLVIPLSFVCFGIALIDTSLLPMLGHLVDTRHVSVYGSVYAIADISYSLAYAFGPIIAGWIVTNWGFTALNIIIFATNVTYAPVLFLLRKVHSYDTLGAKGDTAEMTQLNSSAPAGGYNGKPEATTAESYQGWEDQQSYQNQAQIPNHAVSFQDSRPQAEFPAGYDPLNPQW", "text": "FUNCTION: Involved in acetylcholine transport into synaptic vesicles. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Vesicular transporter family."}
+{"protein": "MQCFSFIKTMMILFNLLIFLCGAALLAVGIWVSIDGASFLKIFGPLSSSAMQFVNVGYFLIAAGVVVFALGFLGCYGAKTESKCALVTFFFILLLIFIAEVAAAVVALVYTTMAEHFLTLLVVPAIKKDYGSQEDFTQVWNTTMKGLKCCGFTNYTDFEDSPYFKENSAFPPFCCNDNVTNTANETCTKQKAHDQKVEGCFNQLLYDIRTNAVTVGGVAAGIGGLELAAMIVSMYLYCNLQ", "text": "SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MENQKMPISSVSNLKDLNMISRPVANFPPSIWGDRFINYACEDENEQAQKERQVEELKEQVRRELATAIDKPLQQLNIIDATQRLGIAYHFENEIEESLKHIYLHTYVENTCFEGSDDLYSVALWFRLLRQDDYRVSCDVFKKFRDSEGNFKNSLMEDAKGLLELYEATHLSVNGEEMLDDALEFTKTHLELVVSHLNYPLAEQVRHALYQPQHKGLPRLEAVYFFRIYEAYDSHNEALLKLAKLDFNLLQSLHMKELSHMAKWWKSLDFATKFPFARDRLVEGYFWILGVYFEPQYSLARKIIIKVFTMISTIDDIYDAYGTLDELKLFTKAIQRWDIGSLDQLPEYMKPCYKSVLDVYNEIEEEMDNQGSLFRMHYAKEEMKKIVEGYMDEAKWCHEKYVPTFQEYMSVALVTAGYTFLTTISYLGMGEIASKEAFDWLFSRPPIIEASESVCRLMDDMRSHEFEQERGHVASGIECYMKQYGVTEEEAHDKFHKRLVKAWKDINEGCLRPYPMPKPLLMRILSLTRVIDVIYKNEDWYTHVKKPMKDKIASLLIDPMIV", "text": "FUNCTION: Sesquiterpene synthase. SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily."}
+{"protein": "MIEVTFTPYDVLLFRESRPFDAGSESVARSIIPLPQTVAGAIRTLLFYKGLKNCVGVGEEEPEFTLVGIAIGTEKGRIYPLPFNIIKSEKFYKVVNPGRFLGKLILPPKGKYKSGYVTESILEKYLKGELKEVEENKVIRIEKEKRIGIKLSREKKVVEEGMLYTVEFLRIEKIYAWIEDPGCGIKDILSSYEFLTLGGESRVAFVEVDDKTPDIFNRELGSTKKALFYFSTPTIGKVGEIVQELEKRLNAKIDDYLLVSSRPTAISGWDMHEKKPKGTKFAIPPGSVLFVEFKEEVEVPPYIKLGKLKKLGYGLALGGIWE", "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), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation- dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'- 3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CRISPR system Cmr3 family."}
+{"protein": "MTVKTTVSTKDIDEAFLRLKDIVKETPLQLDHYLSQKYDCKVYLKREDLQWVRSFKLRGAYNAISVLSDEAKSKGITCASAGNHAQGVAYTAKKLNLNAVIFMPVTTPLQKVNQVKFFGNSNVEVVLTGDTFDHCLAEALTYTSEHQMNFIDPFNNVHTISGQGTLAKEMLEQSKTDNVNFDYLFAAIGGGGLISGISTYFKTYSPTTKIIGVEPSGASSMYESVVVNNQVVTLPNIDKFVDGASVARVGDITFEIAKENVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALENYKDHIKGKTVVCVISGGNNDINRMKEIEERSLLYEEMKHYFILNFPQRPGALREFVNDVLGPQDDITKFEYLKKSSQNTGTVIIGIQLKDHDDLIQLKQRVNHFDPSNIYINENKMLYSLLI", "text": "FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity). SIMILARITY: Belongs to the serine/threonine dehydratase family."}
+{"protein": "MPAVAGSLYMASQHKGVPPPLPPPPRPLPVINLGRLTMDSASRALAVRDIVLACRERGCFEVVNHGISRSCMNGALEAASEFFQLSTERKEEFASDDIRQPIRYDTSSRDGISMSRSFLKHYANPLDDWIKFWPTQPPTYREKMGEYAVETQRVSMQLMEAILQGLGLGPSYLQEKLEGGVQFVALNNYPQSSAKKADKIGLAPHSDYGFLTILLQSSPGLEVMHHEDDAWTSVPAIPGALHVHVGDHLEVLSNGQLKSLVHRAVLNPNESRISIASIHGLSMDEEVHCAEELVDEHHPKMYRGSSFQDFLDFLPANMNRYKRYVESLRIDKP", "text": "FUNCTION: Involved in melatonin degradation (PubMed:25728912). Catalyzes the hydroxylation of melatonin to produce 2-hydroxymelatonin (PubMed:25728912). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
+{"protein": "MDDLGTLVSSGQKVAVTWDGSSSKDALKEFVSKLQEAVAPQGTVSVENIERLLLSAHADSSFDAVLLGVVQGTQSVHSSEILAEVARILKPGGAVIIQELVAAGVDKGSPLRTPERLSSLLKLSGLTEATQLLQEPLSPEQKQTVVELLGYKGNDVSTIRMKAKKPNYELGSSRQLSLPKSKITEKSSVDQATVKLWTLSANDMNDENVDLLDSDELLDQEDLKKPVPSSLRASGCGEGSEKKRKACKNCTCGLAEELEAEKTPSTVPKAAPSACGNCYLGDAFRCASCPYLGMPAFKPGEKVLLNPTQLQDA", "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 NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 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. Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells. SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion intermembrane space. SIMILARITY: Belongs to the anamorsin family."}
+{"protein": "MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEEGALPPYSDHALVNNPPNTHRENHSSGTTDNSSPLLIKLLISFTSIILFNAPAVCYLKYKDAFFKNYGAVEWTLFGFWCFVCTLALIFLTYFYETWTKAVKVTVISLAQCVKVTAVFLAKCVKVTAVGLYNSREKWVVIIWLLWVVICYTLFLRAKFGNLNLDKALICSTCSISAALLLFLLYVRLPFWTLKHMFSGLFQVLGVQSCVVIVQKGLMHLFDKHIDGTGYEIEASSLFVIGNFLFFYEMECPGALKRMPKFIRNGIASFLGGIANAIGGANDNNDIPLEETEAESEV", "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": "MNWKTPSKKIYDSADLKNFEKSIAFEKLQKTLQQIILSVENHKIPPGILNVDIVTRPGRIGSIPLPSLIEPTTTTTTRENKIGPSNGNVEILIELFQYLNKLIDETPPLKGPTRFGNFACRDWHDKIDIIPILKKFKFPQELSSSNNSSSKSNIDGFLLESSYYLLNSFGSKIRLDYGTGHELSFLAFIGSLIEFKILNHPTTTEEINGKEILIIFANYYDLVRRLILVYNLEPAGSHGVWGLDDHFHLIYILGASQFINDKLAPIVQRSLSSQVINSCKLTNFYINAIAFIFRLKTGPFNEHSPIIFDIHNKVFSWTKVRQGLIKMYMVEVFNKFPVLQHFWCGEVLYPWKDHQGNDLPVNEKEETELDKPPETTLNSTTTTTTTTKVSSSTSKIPFTPAPWANTTTTHAVPRNTRNTRNPRS", "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": "MSNKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKSIVTLQRGSLNQVQRWDGKETTIKRKLVNGKMVAECKMKGVVCTRIYEKV", "text": "FUNCTION: May play a role in lipid transport protein in Schwann cells. May bind cholesterol. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
+{"protein": "SLLELGKMILQETGKMPSKSYGAYGCNCGVLGR", "text": "FUNCTION: Snake phospholipase A2 homolog that lacks enzymatic activity (PubMed:19944711, PubMed:20036276). May display myotoxin activity (Probable). In isolated heart decreases cardiac frequency (PubMed:20036276). Also decreases mean arterial pressure (PubMed:19944711). Does not show antimicrobial activity (PubMed:19944711). Does not change renal parameters (such as perfusion pressure, renal vascular resistance, urinary flow, glomerular filtration rate and sodium tubular transport) (PubMed:20036276). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily."}
+{"protein": "MSRGDGYPKNIFLLCRDSGVPFEDLRLQCVFCTKELTSPELAAFCIRELNVVWKSGAPYGACARCLLFEGIKRRLKYWQYSCFVEGVEAETNESIYTQLIRCYMCHKPLVREEKDKHRNEKRRLHKISGYWRGSCLYCWSRCMGQSPR", "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": "MPTVNKERNMSSIAYFILWVGIAVQLVTPITAAQLYPALSPLQIIIACILGNLIVAILLTLLGDIGVRYGIPYAVYIRASFGYLGAHIPGIVRAVPAVFWFGFQTWMGAYALDAIMEMLTGYSNLTLLIILFGVVQIINTAMGMEAITKFEWLASPSILIIGIILQVYIMKQHHLTFSEIFSHGGDGGVSMGYAVVVMMGTYITMALNAPDFTRFLKTKTGSSEPNWWKVNKGSFWAHTFGLIGS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family."}
+{"protein": "MSGDGEDELCRNALALVNELCFSVRGNHNNEKCIEFSYLLRDRDRTRHIETDISVSLLSVIVTFCGIVLLGVSLFVSWKLCWIPWRDKGLNPQRRDSQHHPHQHLHHHHSHFTDLTVERVDCGPEMPERSYLDLESYPESGIKLSQTSPDIPVDTSSGSKENNIPNAHSQQQVSAPPPATRFNSLPRPIPQQLSSPEFGTQADEKVEQVTSIGQIKPELYKQRSIDTEAKKHQKVNCGRINFMLRYTYTTEQLVVKILKALDLPAKDANGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFNVPFNELQNRKLHFSVYDFDRFSRHDLIGQVVLDNLLEFSDFSEDTTIWRDILEATSEKADLGEINFSLCYLPTAGRLTITIIKATNLKAMDLTGFSDPYVKASLICDERRLKKRKTSIKKNTLNPVYNEALVFDIPNENMEHVNVIIAVMDYDCIGHNEVIGMCRVGNATDGPGREHWNEMLANPRKPIEQWHQLIEEKVMNSYMTKSFAAGTGATKPVTIVVESPHSV", "text": "FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. Synapse. Note=Synaptic vesicles in neurons. SIMILARITY: Belongs to the synaptotagmin family."}
+{"protein": "MKRIAFVFSTAPHGSASGREGLDALLATSALTEALGVFFISDGVFQLLPGQKPDAVLARDYIATFKLFDLYDIDQCWICAASLRERGLKNVNFVVDATPLEPVALRRELGNYDVILRF", "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": "MVEQDPFEIAVKQLERAAQYMDISEEALEFLKRPQRIVEVSIPVEMDDGSVKVFTGFRVQYNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGVICNPKEMSDREKERLARGYVRAIYDVISPYTDIPAPDVYTNPQIMAWMMDEYETISRRKDPSFGVITGKPPSVGGIVARMDATARGASYTVREAAKALGMDLKGKTIAIQGYGNAGYYMAKIMSEEYGMKVVAVSDSKGGIYNPDGLNADEVLAWKKKTGSVKDFPGATNITNEELLELEVDVLAPSAIEEVITKKNADNIKAKIVAELANGPTTPEADEILYEKGILIIPDFLCNAGGVTVSYFEWVQNITGDYWTVEETRAKLDKKMTKAFWDVYNTHKEKNINMRDAAYVVAVSRVYQAMKDRGWIKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
+{"protein": "MEQQPSVPRSCTNVARETPMNLNIQSTTGTRYELSVPLNETVDGLKRRISQRLKVPKERLTLLHRETRLSSGKLQDLGISDGSRLTLLPSVEAGLMSQMSRPEQSVMQALESLTETQVNDFLSGRSPLTLALRVGDHMMFVQLQLAAQQSGGSHLQHRHVITRGADAGAPPQYRTLHTSTSALSHLASCTPGSTPPTTLSPTSSTHCDAPHSSPLTTSVFRSHGEGVSPCAEQVPCSTRGTEGTSSSPSSRSRKPGAIIESFVNHAPGVFSGTFSGTLHPHCQDGAGRPRRDIGTILQILNDLLSATRHYQGMPPSLTTLRCHTQCASQARNAKATSPQSTGPQQTTHPVGHCQAQTRTCKPSGDRLRQTENRATRCKVERLQLLMHQKRLRRKARRDSRAPYHWMPTRKSSRTSSNSSTSSGEGSLEIDFEDSLWKPDVKAELNSEFVVA", "text": "FUNCTION: Facilitates ubiquitin-independent proteasomal degradation of polycomb protein CBX4. Plays a role in inhibiting the activity of glucokinase GCK and both glucose-induced and basal insulin secretion. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Nucleus, nucleolus Note=Detected in the nucleus and nucleolus with no expression in the cytoplasm. However, a later study finds expression in the nucleus and cytoplasm with no expression in the nucleolus."}
+{"protein": "MSSISSAPQQQFSLRYHKASISYILPISSRYIYSADQSGLVIKWDLQIRRPKLQWQAHKDSILTILQWHQYIVTHSRDSTIKVWLEDILQFEMPVNALNYTNIVLYRDNYLITPATLDSNNVDVYKLKQHPIEVSRVIANISIFELVNKTRTNMHANKAGDGVDINVKYADEFAIDDKDNMQGRQDFGIIMKMLVIDMTIYIGFESGDIVGLHLEVPESKLTRGSNSTLLINREPRLKLEYQNTLLVPNPVISLANLNGLLVSGSTGTKVVIHSDPTRTVKFHLSGIHSIQTYQDRLVIGFWDGAIEYKGEIIQRPLPQIKGGLDINSNGDDENEEENLKSNVKLTSMTLSSFGNSSGSDTAKVQHVRKPKYSEMVKAKSMSDALFAGYEDGTIMGYALI", "text": "FUNCTION: Component of the ASTRA complex involved in chromatin remodeling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat ASA1 family."}
+{"protein": "MKISYRAFVRQVRHASTTASKGATTSVTSSAAGQLKSEPAARATFLERIQRGPGFQDFFAVKPASRLKTDEEEHVDTSVPYLNSIDFNGNGRKVHFEVYGCQMNTNDTEVVFSILKENGYLRCQEPEEADVIMLVTCAVRDGAEQRIRNRLKHLRAMKNKRSTRRHPLQLTLLGCMAERLKEKLLEQEQCVDVIAGPDSYKDLPRLLAISRHYGNSAINVLLSLDETYADVMPVRLNSESPTAFVSIMRGCDNMCTYCIVPFTRGRERSRPLASIVAEVKALAEQGVKEVTLLGQNVNSYRDRTAQEEQDSLKATPVPGFSTVYKPKTGGTPFAALLRSVAQAVPDMRIRFTSPHPKDFSDEVLEVIRDHPNVCKQLHLPAQSGNTQVLERMRRGYSREAYLELVQHIRQFLPNVGLSSDFICGFCGETEEEFQDTVSLIQQVQYNVAYLFAYSMREKTTAHRRYKDDVPINVKNERLQRMVQVFREGATQLHRKMEGQEQLILIEGKSKRSDAHWFGRNDANIKVIVPSIYVPISGDSTARKSFGVGDFLAVRIEESNSQVLKGTPLELSNITDFHSRQLIQ", "text": "FUNCTION: Potential regulator of CDK5 activity. SIMILARITY: Belongs to the methylthiotransferase family. MiaB subfamily."}
+{"protein": "MENKKTIYFLCTGNSCRSQMAEAWGKKYLGDNWNVYSAGIEAHGVNPNAIKAMNEVNIDITNQTSDIIDANILNRADLVVTLCSHADSVCPSTPPDVNRVHWGFDDPAGKEWSEFQRVRDEIGERIKRFSETGE", "text": "FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein phosphatase family. Thioredoxin-coupled ArsC subfamily."}
+{"protein": "MSKVLFVFGTRPEAIKMAPLVIEFKNNPAIEVKVCVTGQHREMLDQVLDFFEIEPDYDLNIMKQKQSLGSITCSILTRLDEILASFMPAHIFVHGDTTTTFAASLAAFYQNIKVWHIEAGLRTWNMNSPFPEEGNRQLTSKLAFFHAAPTLQAKDNLLRESVKEKNIIVTGNTVIDALLIGIKKITGSTGDVREIISLKNKLNLDKKIILVTLHRRENQGELLRTICDDIKQLALEHDDIEIVFPVHMSPRIREVVNEKLSGVVNIKLVEPLAYPGFIWLMNNAHFILSDSGGVQEEAPSLQKPVLVARDTTERPEVIENGAAMLVDPRIPNNIYSSCKKLLSDERLYEKMSQAGNPFGDGKASKKILDYFVSLEDIK", "text": "SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family."}
+{"protein": "MLQTNNYSLVLLIQLALLTFDLFVNSFSELLRSAPVIQLVLFIIQDIGILFNVIIILLMMFNTYVFQVGLVSLLLERFRAMLILSALYLTLSICFHCWVMNLRWMESNRFVWTDGLQVLFVFQRIAAVLYYYFYKRTTEYLGDPRLYEDSPWLRDAFARARQ", "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": "MAQPQNVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATLGVEVHPLHFHTNFGEICFNVWDTAGQEKLGGLRDGYYIQGQCGIIMFDVTSRITYKNVPHWWRDLVRVCENIPIVLCGNKVDVKERKVKAKAITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLVGNPNLEFVASPALAPPEVQVDQQLLAQYQQEMNEAAAMPLPDEDDADL", "text": "FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the small GTPase superfamily. Ran family."}
+{"protein": "MVLESIARVIKVQLPAYLKRLPIPDSIAGFIRLTVSEWLRLLPFLGVLALLGYLAIRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLHLAKAAYCRCWRSKTFPVCDGSHNKHNELTGDNVGPLILKKKEV", "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": "MKKVEKKDNFKKFKNDNIYKKDDKNINQELINEEKKIKNFNSSNNESSNEKKILFDIEMNITVELGKSKVKIKDLLNFSKGSMLFLQRKKEDPLKVFANNKLIALGEIVFSNNKYGIRIISINNSLNGINTSV", "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 membrane; Peripheral membrane protein; Cytoplasmic side Bacterial flagellum basal body. SIMILARITY: Belongs to the FliN/MopA/SpaO family."}
+{"protein": "MCPGLWGTCFWLWGSLLWLSIGRSGNVPPTTQPKCTDFQSANLLRGTNLKVQFLLFTPSDPGCGQLVEEDSDIRNSEFNASLGTKLIIHGFRALGTKPSWINKFIRALLRAADANVIAVDWVYGSTGMYFSAVENVVKLSLEISRFLSKLLELGVSESSIHIIGVSLGAHVGGMVGHFYKGQLGRITGLDPAGPEYTRASLEERLDSGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQDQPGCPAFIHAGYSYLICDHMRAVHLYISALENTCPLMAFPCASYKAFLAGDCLDCFNPFLLSCPRIGLVERGGVKIEPLPKEVRVYLQTTSSAPYCVHHSLVEFNLKEKRKKDTSIEVTFLGNNVTSSVKITIPKDHLEGRGIIAHQNPHCQINQVKLKFHISSRVWRKDRTPIVGTFCTAPLPVNDSKKTVCIPEPVRLQVSMAVLRDLKMACV", "text": "FUNCTION: Hydrolyzes the ester bond of the acyl group attached at the sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1- acyl-2-lysophosphatidylserines (lysophospholipase activity) in the pathway of phosphatidylserines acyl chain remodeling (PubMed:8999922). Cleaves phosphatidylserines exposed on the outer leaflet of the plasma membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines, which in turn enhance mast cell activation and histamine production (PubMed:11395520). Has no activity toward other glycerophospholipids including phosphatidylcholines, phosphatidylethanolamines, phosphatidic acids or phosphatidylinositols, or glycerolipids such as triolein (PubMed:8999922). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
+{"protein": "MIDSEALENERTKLKREIAELRAALNRKEQCLRDLETTISEATGDEDDVHPDTNGGVCHTQLSNDDIARYSRQLILPDFGVQGQLRLKNSSVLIVGMGGLGCPAAQYLAAAGCGKLGLIDYDEVERSNFHRQILHSEARCGMSKAESARIALLELNQHCEIRCHTRLLNSRNAMHIIRTYDVVLDCSDNVATRYLLNDACVMLRKPLVSGSALKTDGQLTVYCYGNGPCYRCIYPVPPPPEAVTNCGDGGVLGAVTGTIGAMQALEAIKVIVGLGDVLAGRLLIFDGSSCLFRNIRIRSKRPNCHVCSAQPLITELIDYELFCGMHATDKDNPLQLLASEERLDVEEYRNKVQQQPHLLIDVRQPAEFEICQLPDAVNVPLAEVLDDSYLKRFSKQLEDTQLPIILLCRRGNDSQIAVQHVRNRFPKHSIRDIIGGLHAWTHKVDPSFPIY", "text": "FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (- COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily."}
+{"protein": "MNKKKIISILKEKLNLKDIYVTEDNNHYEITAIGNVFKGLTQVKRQKKIYNPLIDLITENKIHAISIKSYSLEEWDKNQK", "text": "SIMILARITY: Belongs to the BolA/IbaG family."}
+{"protein": "MEERSVLMERYVIGRQLGQGTFGKVYYARNLSSGQSVAIKMIDKEKILKVGLMEQIKREISIMRLVRHPNVLQLFEVMATKSNIYFALEYAKGGELFHKMARAKLNEESARNYFQQLISAMDYCHSRGVYHRDLKPENLLLDENETLKVSDFGLSALAESRRQDGLLHTACGTPAYVAPEVLSRKGYSGSKADVWSCGVILFVLVANYLPFHDRNIIQMYRKIAKAEYRCPRHFSAELKELLYGILDPDPSTRMSISRIKRSAWYRKPIAISALNNETGKKSCTSEAPFSGPTICISSERNQEPPNLHNLNAFDIISLSTGFDLSGLFGERYGRRESLFTSRKPAAAVLVKLKELAKALNLKVTKTDNGVLKLATTKEGRKGRLELDAEVSEVAPFLLVELKKTNGDTLEYQRMMKEDIRPSLKDIIWTWQGDQQ", "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": "MAQKPDGGAGLRGFQAEASVEDSALLVQTLMEAIQISEAPPTSQATAAASGPNASPQSSQPPTANEKADTEVSAAAARPKTGFKAQNATTKGPNDYSQARNAKEMPKNQSKAAFKSQNGTPKGPHAASDFSQAAPTGKSAKKSEMAFKGQNSTKAGPGTTYNFPQSPSANEMTNNQPKTAKAWNDTTKVPGADAQTQNVNQAKMADVGTSAGISEADGAAAQTSADGSQTQNVESRTIIRGKRTRKVNNLNVEENNSGDQRRASLASGNWRSAPVPVTTQQNPPGAPPNVVWQTPLAWQNPSGWQNQTARQTPPAARQSPPARQTPSAWQNPVAWQNPVIWPNPVIWQNPVIWPNPIVWPGPIVWPNPMAWQSTPGWQSPPSWQAPPSWQSPQDWQGPPDWQVPPDWSMPPDWSFPSDWPFPPDWIPADWPIPPDWQNLRPSPNLRSSSNSRASQNQGPPQPRDVALLQERANKLVKYLMLKDYTKVPIKRSEMLRDIIREYTDVYPEIIERACFVLEKKFGIQLKEIDKEEHLYILISTPESLAGILGTTKDTPKLGLLLVILGIIFMNGNRATEAVLWEALRKMGLRPGVRHPLLGDLRKLLTYEFVKQKYLDYRRVPNSNPPEYEFLWGLRSYHETSKMKVLRFIAEVQKRDPRDWTAQFMEAADEALDALDAAAAEAEARAEARNRMGIGDEAVSGPWSWDDIEFELLTWDEEGDFGDPWSRIPFTFWARYHQNARSRFPQAFTGPIIGPSGTATANFAANFGAIGFFWVE", "text": "FUNCTION: Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl- conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rhythm regulation. May act as RORA coregulator, modulating the expression of core clock genes such as BMAL1 and NFIL3, induced, or NR1D1, repressed. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell membrane; Peripheral membrane protein Note=Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF."}
+{"protein": "MAGSEQQRPRRRDDGDSDAAAAAAAPLQDAELALAGINMLLNNGFRESDQLFKQYRNHSPLMSFGASFVSFLNAMMTFEEEKMQLACDDLKTTEKLCESEEAGVIETIKNKIKKNVDVRKSAPSMVDRLQRQIIIADCQVYLAVLSFVKQELSAYIKGGWILRKAWKIYNKCYLDINALQELYQKKLTEESLTSDAANDNHIVAEGVSEESLNRLKGAVSFGYGLFHLCISMVPPNLLKIINLLGFPGDRLQGLSSLMYASESKDMKAPLATLALLWYHTVVRPFFALDGSDNKAGLDEAKEILLKKEAAYPNSSLFMFFKGRIQRLECQINSALTSFHTALELAVDQREIQHVCLYEIGWCSMIELNFKDAFDSFERLKNESRWSQCYYAYLTAVCQGATGDVDGAQIVFKEVQKLFKRKNNQIEQFSVKKAERFRKQTPTKALCVLASIEVLYLWKALPNCSFPNLQRMSQACHEVDDSSVVGLKYLLLGAIHKCLGNSEDAVQYFQRAVKDELCRQNNLYVQPYACYELGCLLLDKPETVGRGRALLLQAKEDFSGYDFENRLHVRIHAALASLRELVPQ", "text": "SIMILARITY: Belongs to the TTC39 family."}
+{"protein": "MENQPKLNSSKEIIAFLAERFPLCFVAEGEARPLKIGIFQDIVERIQDEECLSKTQLRSALRLYTSSWRYLYGVKEGAQRVDLDGNSCGELEAEHIEHALQQLTEAKARVQAQRAEQRAKKREAENVAAGEKNERPTAKKPAPRRRANNTEGEKRQPPRPQKRPQQARKPVAKPVQAKPIQAAPIQIVDVSSLKIGQEIKVRVGKSSVDASVLEVAKDGVRVQLPSGLAMIVRAEHLQF", "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": "MASRGGGRGCGRGQLTFNVEAVGIGKGDALPPPTLQPSPLFPPLEFRPVPLPSGEEGEYVLALKQELRGAMRQLPYFIRPAVPKRDVERYSDKYQMSGPIDNAIDWNPDWRRLPRELKIRVRKLQKERTTIILPKRPPKTTEDKEETIQKLETLEKKEEEVTSEEDEEKEEEEEKEEEEEEEYDEEEHEEETDYIMSYFDNGEDFGGDSDDNMDEAIY", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPC7 RNA polymerase subunit family."}
+{"protein": "MSMKQLETSMSSVSLQEKKPTRIKIALHPQSKSEQNETDRASKIPTGRISTTQPQTYYRPTNLTKTPASQVSRRSSYTTDPPSPLTGITGFRNYSLDDFEIGKALGKGKFGKVYLVKDKKTGFVSALKCMEKKELVEGNVEKQFRREVEIQSNLRHTNVLRLFGHFHDKDRVYLILEYVVHGELYKLLRNQKRFTESTASSYIYQMSEALLYLHGKNIIHRDIKPENILLHFNDTIKISDFGWSVHAPSNRRSTLCGTMDYLPPEIVQSRPYDKNVDVWSLGILMYEFLCGAPPFEEPGGAQATYRRIVKLDLRIPPYVSADAADLIKRMLTLDPAKRFKLKDMHKHPWIVRLRPTWKYKVPKTASHERSA", "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 (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": "MIKLFICQKKYYLTAIFLLTIQSCASVEYKPLVTGATTAIAPNIWPKVVNGSLFQEKIPINYGYQPLFEDHRPHNIGDTITVVLQENISASNSSISNMSRDGSANFGLKIAPGQLNNILGVNFQDNTTSLDSFGRNNFSGKGSNSANNKFTGLITVTVKRVLPNGNLKVIGEKQVSINKGTEFIRFSGVINPTNINKNNFISSTQIADARIEYLSHGGLDDVQKMGWLQKLLLKISPI", "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": "MPMFIVNTNVPRSSVPEGLLSELTQQLAQATGKPAQYIAVHVVPDQLMTFSGSSDPCALCSLHSIGKIGGAQNRTYSKLLCGLLADRLRISPDRIYINYYDMNAANVGWNGSTFA", "text": "FUNCTION: Pro-inflammatory cytokine involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Does not have a cleavable signal sequence and is secreted via a specialized, non- classical pathway. Secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. SIMILARITY: Belongs to the MIF family."}
+{"protein": "MSGISNAENGKAIVSSGVLNSVSAFVRRHRTFVYTIGAVAVFATVGGVYHVQQKKASHKRSKKLKAHQDKAESKVNEGKNEAAKVVKEEDLKSSETGKDVETAAAAAAAAKKKKKNKKKVKAKKVGDSSVDKIATEESVKSMTKEERAKLAAELKTLGNKAYGQKEYANAIDYYTQAITCSHDPIFFSNRAACYAAIGDFEQVIKDTSEALSLDSSYVKALNRRSAAYEQLGKLDEALMDSTVSCIFDGFANESMTATVERLLKKVAEKKSSALLKERPPKLPAASFIQTYLDSFHAQPKPLFDNKFDGDAALAEAYEYLEKGEYQLSYDKAKESCLGSFSSPSVNARTHNLVGTFKFVSGDSKGSMENFNAAIKLDRKFIQPYIRLSAAYLDENDNEKMWKVLNDAESVDKTDSDLYYHRAQVRFVSGEFAEAISDYQKSIALDDSFIYSHIQLGVAQYKTHAIAESMKTFEDCKKRFPNSSEVYNYFGEILLDQQKFDDAVKNFDHAIELEKREHLTIMSAMPLINKALAVFQWKKDISQAENLCRQALSADPECDIAIASMAQFLLQQGKAREALEYFEKSAQLARTESEMVNAFSYAEATRTQIALTEKYPQLVGRLSNPM", "text": "FUNCTION: Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with tom20 and tom22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the tom40 translocation pore. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Tom70 family."}
+{"protein": "MAITLSATSLPISAADHHPLPLTVGVLGSGHAGTALAAWFASRHVPTALWAPADHPGSISAIKANEGVITTEGMINGPFRVSACDDLAAVIRSSRVLIIVTRADVHDSFVNELANFNGELATKDIVVVCGHGFSIKYERQLRFKRIFETDNSPITSKLSDQKKCNVNIKEMKASFGLSCFPIHRDDAGVIDLPEDTKNIFAQLFSARIICIPPLQVLFFSNCITHAVPAVMNIGRLRDPANSLTKRAEKWLLELDERTPRAEKGFFFYGEGSNTYVCNVQEQIDHERRKVAAACGLRLNSLLQECNDEYDTDYETLREYCLAPSPHNVHHACPDNMEHRYFSEELCSLEDVAAIAAIANIELPLTHAFINIIHAGKGKINPTGKSSSVIGNFSSSDLIRFGATHVFNKDEMVE", "text": "SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine dehydrogenases family."}
+{"protein": "MRRSCLMIRRRKRMFTAVTLLVLLVMGTSVCPVKAEGAARQMEALNRGLVAVKTDGGIFVSWRFLGTENASVLFNVYRDGQKLNAAPVKTTNYVDKNGSAGSTYTVRAVVNGTEQPASEKASVWAQPYHSVPLDKPAGGTTPKGESYTYSANDASVGDVDGDGQYELILKWDPSNSKDNSQDGYTGDVLIDAYKLDGTKLWRINLGKNIRAGAHYTQFMVYDLDGDGKAEVAMKTADGTKDGTGKVIGNANADYRNEQGRVLSGPEYLTVFQGSTGKELVTANFEPARGNVSDWGDSYGNRVDRFLAGIAYLDGQRPSLIMTRGYYAKTMLVAYNFRDGKLSKLWTLDSSKSGNEAFAGQGNHNLSIADVDGDGKDEIIFGSMAVDHDGKGMYSTGLGHGDALHTGDLDPGRPGLEVFQVHEDKNAKYGLSFRDAATGKILWGVYAGKDVGRGMAADIDPRYPGQEVWANGSLYSAKGVKIGSGVPSSTNFGIWWDGDLLREQLDSNRIDKWDYQNGVSKNMLTASGAAANNGTKATPTLQADLLGDWREEVVWRTEDSSALRIYTTTIPTEHRLYTLMHDPVYRLGIAWQNIAYNQPPHTSFFLGDGMAEQPKPNMYTP", "text": "FUNCTION: Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases oligosaccharide products (PubMed:16682770, PubMed:17449691, PubMed:19193638). Degrades rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin (PubMed:16682770, PubMed:17449691). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 11 family."}
+{"protein": "MGTIKNNFQLLWLILLIVVLVNGKSINKNNNNNKNEIINVTYDGRSLIINGERKLLFSGSIHYPRTSEEMWPIILKQSKDAGIDIIDTYIFWNIHQPNSPSEYYFDGNANITKFLDLCKEFDLYVNLRIGPYVCAEWTYGGFPIWLKEIPNIVYRDYNQQWMNEMSIWMEFVVKYLDNYFAPNGGPIILAQVENEYGWLEQEYGINGTEYAKWSIDFAKSLNIGIPWIMCQQNDIESAINTCNGYYCHDWISSHWEQFPNQPSFWTENWIGWFENWGQAKPKRPVQDILYSNARFIAYGGSLINYYMWFGGTNFGRTSGGPWIITSYDYDAPLDEFGQPNEPKFSLSSKFHQVLHAIESDLLNNQPPKSPTFLSQFIEVHQYGINLSFITNYGTSTTPKIIQWMNQTYTIQPWSVLIIYNNEILFDTSFIPPNTLFNNNTINNFKPINQNIIQSIFQISDFNLNSGGGGGDGDGNSVNSVSPIEQLLITKDTSDYCWYSTNVTTTSLSYNEKGNIFLTITEFYDYVHIFIDNEYQGSAFSPSLCQLQLNPINNSTTFQLQILSMTIGLENYASHMENYTRGILGSILIGSQNLTNNQWLMKSGLIGENIKIFNNDNTINWQTSPSSSSSSLIQKPLTWYKLNISLVGLPIDISSTVYALDMSSMNKGMIWVNGYSIGRYWLIEATQSICNQSAIENYSYIGEYDPSNYRIDCNKPSQSIYSVPIDWLFNNNYNNQYATIIIIEELNGNPNEIQLLSNKIIN", "text": "FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
+{"protein": "MEASGKLICRQRQVLFSFLLLGLSLAGAAEPRSYSVVEETEGSSFVTNLAKDLGLEQREFSRRGVRVVSRGNKLHLQLNQETGDLLLNEKLDREDLCGHTEPCVLRFQVLLESPFEFFQAELQVIDINDHSPVFLDKQMLVKVSESSPPGTAFPLKNAEDLDVGQNNIENYIISPNSYFRVLTRKRSDGRKYPELVLDKALDREEEAELRLTLTALDGGSPPRSGTAQVYIEVVDVNDNAPEFEQPFYRVQISEDSPISFLVVKVSATDVDTGVNGEISYSLFQASDEISKTFKVDFLTGEIRLKKQLDFEKFQSYEVNIEARDAGGFSGKCTVLIQVIDVNDHAPEVTMSAFTSPIPENAPETVVALFSVSDLDSGENGKISCSIQEDLPFLLKSSVGNFYTLLTETPLDRESRAEYNVTITVTDLGTPGLTTHLNMTVLVSDVNDNAPAFTQASYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQNPHLPLASLVSINTDNGHLFALRSLDYEALQAFEFRVGASDRGSPALSSEALVRVLVLDANDNSPFVLYPLQNSSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKQRLVVLVKDNGEPPCSATATLHVLLVDGFSQPYLPLPEAAPAQGQADSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGHLVDVRGTGSLSQNYQYEVCLAGGSGTNEFQFLKPVLPNIQGHSFGPEMEQNSNFRNGFGFSLQLK", "text": "FUNCTION: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination. Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MWMTPKRSKMEVDEALVFRPEWTQRYLVVEPPEGDGALCLVCRRLIVATRERDVRRHYEAEHEYYERYVADGERAALVERLRQGDLPVASFTPEERAARAGLGLCRLLALKGRGWGEGDFVYQCMEVLLREVLPEHVSVLQGVDLSPDITRQRILSIDRNLRNQLFNRARDFKAYSLALDDQAFVAYENYLLVFIRGVGPELEVQEDLLTIINLTHHFSVGALMSAILESLQTAGLSLQRMVGLTTTHTLRMIGENSGLVSYMREKAVSPNCWNVIHYSGFLHLELLSSYDVDVNQIINTISEWIVLIKTRGVRRPEFQTLLTESESEHGERVNGRCLNNWLRRGKTLKLIFSLRKEMEAFLVSVGATTVHFSDKQWLCDFGFLVDIMEHLRELSEELRVSKVFAAAAFDHICTFEVKLNLFQRHIEEKNLTDFPALREVVDELKQQNKEDEKIFDPDRYQMVICRLQKEFERHFKDLRFIKKDLELFSNPFNFKPEYAPISVRVELTKLQANTNLWNEYRIKDLGQFYAGLSAESYPIIKGVACKVASLFDSNQICEKAFSYLTRNQHTLSQPLTDEHLQALFRVATTEMEPGWDDLVRERNESNP", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum."}
+{"protein": "NSVNPCCDPQTCKPIEGKHCISGPCCENCYFLRSGTICQRARGDGNNDYCTGITPDCPRNRYN", "text": "FUNCTION: May bind to both alpha-IIb/beta-3 (ITGA2B/ITGB3) and alpha- V/beta-3 (ITGAV/ITGB3) integrins, and may inhibit platelet aggregation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin subfamily."}
+{"protein": "MAPYRSSLLCALLLLALCALSPSHAATTSRGRAQERAPQSRVSEARPSTMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESSTFSGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWDSFNNGDCFILDLGNNIYQWCGSGSNKFERLKATQVSKGIRDNERSGRAQVHVSEEGGEPEAMLQVLGPKPALPEGTEDTAKEDAANRRLAKLYKVSNGAGSMSVSLVADENPFAQGALRSEDCFILDHGRDGKIFVWKGKQANMEERKAALKTASDFISKMQYPRQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGPGLGYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSRDGGQTAPASIRLFQVRASSSGATRAVEVMPKSGALNSNDAFVLKTPSAAYLWVGAGASEAEKTGAQELLKVLRSQHVQVEEGSEPDAFWEALGGKTAYRTSPRLKDKKMDAHPPRLFACSNRIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVRQGFEPPSFVGWFLGWDDNYWSVDPLDRALAELAA", "text": "FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (By similarity). Plays a role in ciliogenesis (By similarity). SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton. SUBCELLULAR LOCATION: [Isoform 1]: Secreted. SIMILARITY: Belongs to the villin/gelsolin family."}
+{"protein": "MQPPPDEARRDMAGDTQWSRPECQAWTGTLLLGTCLLYCARSSMPICTVSMSQDFGWNKKEAGIVLSSFFWGYCLTQVVGGHLGDRIGGEKVILLSASAWGSITAVTPLLAHLSSAHLAFMTFSRILMGLLQGVYFPALTSLLSQKVRESERAFTYSIVGAGSQFGTLLTGAVGSLLLEWYGWQSIFYFSGGLTLLWVWYVYRYLLSEKDLILALGVLAQSRPVSRHNRVPWRRLFRKPAVWAAVVSQLSAACSFFILLSWLPTFFEETFPDAKGWIFNVVPWLVAIPASLFSGFLSDHLINQGYRAITVRKLMQGMGLGLSSVFALCLGHTSSFCESVVFASASIGLQTFNHSGISVNIQDLAPSCAGFLFGVANTAGALAGVVGVCLGGYLMETTGSWTCLFNLVAIISNLGLCTFLVFGQAQRVDLSSTHEDL", "text": "FUNCTION: Voltage-gated ATP nucleotide uniporter that can also transport the purine nucleotides ADP and GTP. Uses the membrane potential as the driving force to control ATP accumulation in lysosomes and secretory vesicles (PubMed:18375752, PubMed:23467297). By controlling ATP storage in lysosomes, regulates ATP-dependent proteins of these organelles (PubMed:35269509). Also indirectly regulates the exocytosis of ATP through its import into lysosomes in astrocytes and secretory vesicles such as adrenal chromaffin granules, mucin granules and synaptic vesicles (PubMed:18375752, PubMed:23467297). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Note=Localizes to mucin granules and vesicles. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family."}
+{"protein": "MDAFNYRGGELFAEGVALSAIAERFGTPTYVYSRAHIEAQYRTFADALEGMPHLVCFAVKANSNLGVLNVLARLGAGFDIVSGGELERVLAAGGSADKIVFSGVGKTREDMRRALEVGVHCFNIESTDELGSRLQIVAAELGVRAPISLRVNPDVDAGTHPYISTGLKENKFGIAIADAEDVYVRAAQLPNLEVLGVDCHIGSQLTTLEPFIDALDRLLALVDRLGDCGIYLRHIDLGGGVGVRYRDEEPPLVADYIKAVRERLDGRDLALMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMDVTAVRPRDTAARSYDIVGPICETGDFLAKGRELALEEGDLLAVHSAGAYGFVMSSNYNTRGRCAEVLVDGDQAFEVRRRETVAELFAGESLLPE", "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": "MDTIVLDQRGEVFSFFRSLDMLCYAIIAQQYFQDPTVLLLLLKVFVQLSYLTPKPFSQLNALPLFYPLLLNFLISLMVRMFFNLPTAGESLDGYLYGGSIINFIGEKNESSRIDFITSDLVLFCLQIFMALILIASNKRPTQASHIQASQSGLSNVDGDEEPSDLITEDSRDTQQGQRQEDLQRQLENERSRLIARFSHSLYSFQHGLSFGSPQNRNTPLQRQSADSYSTPVCIEVDSEDWKDLVWKSQYATENANTNSINNSPLSSNTTGVPNSVLTNPI", "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: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein."}
+{"protein": "MDPNCSCPTGGSCSCAGSCTCKACRCPSCKKSCCSCCPVGCAKCAQGCVCKGASDKCSCCA", "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": "MFCKHLSFVAITICFLLVLAKTENEIQQKNIKFDQRTWRNMRSNGYLALPRQGRSDNQPDYTCCGMPLTKYVGICPIGMECCPGLKKVLQKSGQRTIYSVCVADAY", "text": "FUNCTION: Evokes contractions in the radula protractor muscle, and may regulate feeding behavior and gut motility by controlling muscle contraction of the buccal mass. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SCP family."}
+{"protein": "MEAARPFAREWRAQSLPLAVGGVLKLRLCELWLLLLGSSLNARFLPDEEDVDFINEYVNLHNELRGDVIPRGSNLRFMTWDVALSRTARAWGKKCLFTHNIYLQDVQMVHPKFYGIGENMWVGPENEFTASIAIRSWHAEKKMYNFENGSCSGDCSNYIQLVWDHSYKVGCAVTPCSKIGHIIHAAIFICNYAPGGTLTRRPYEPGIFCTRCGRRDKCTDFLCSNADRDQATYYRFWYPKWEMPRPVVCDPLCTFILLLRILCFILCVITVLIVQSQFPNILLEQQMIFTPEESEAGNEEEEKEEEKKEKEEMEMEIMEMEEEKEEREEEEEETQKEKMEEEEK", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CRISP family."}
+{"protein": "MKFIIAFFVATLAVMTVSGEDKKHDYQNEFDFLLMERIHEQIKKGELALFYLQEQINHFEEKPTKEMKDKIVAEMDTIIAMIDGVRGVLDRLMQRKDLDIFEQYNLEMAKKSGDILERDLKKEEARVKKIEV", "text": "SIMILARITY: Belongs to the mite group 5 allergen family."}
+{"protein": "MELRPRLGATCLLGFSFLLLVTSSHGPNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDPSGKVRPEIINENGNPSYKYFYISAEQVVQGMKEAQERLTGDAFREKHLEDEL", "text": "FUNCTION: Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol- disulfide oxidase activity. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
+{"protein": "ATITVVNRCSYTVWPGALPGGGVRLDPGQRWALNMPAGTAGAAV", "text": "FUNCTION: Has antifungal activity. Inhibits the growth of Trichoderma viridae and Candida albicans. SIMILARITY: Belongs to the thaumatin family."}
+{"protein": "MSETFFHLLGPGTQPNDDSFSMNPLPITCQVNDEPSMAALEQCAHSPQVIALLNELQHQLSERQPPLGEVLAVDLLNLNADDRHFINTLLGEGEVSVRIQQADDSESEIQEAIFCGLWRVRRRRGEKLLEDKLEAGCAPLALWQAATQNLLPTDSLLPPPIDGLMNGLPLAHELLAHVRNPDAQPHSINLTQLPISEADRLFLSRLCGPGNIQIRTIGYGESYINATGLRHVWHLRCTDTLKGPLLESYEICPIPEVVLAAPEDLVDSAQRLSEVCQWLAEAAPT", "text": "FUNCTION: Not known. Could enhance the incorporation of nickel to the hydrogenase. SIMILARITY: Belongs to the HupH/HyaF family."}
+{"protein": "MRSIKTVHVISAHAEGEVGDVIVGGVKPPPGETIWEQSRFIARDETLRNFVLNEPRGGVFRHVNLLVPPKHPDADAAFIIMEPEDTPPMSGSNSICVSTVLLDGGIVPMQEPETHMLLEAPGGLVKVRAECRNGKAERIFVQNLPSFAAKLDAELEVEGLGKLKVDTAYGGDSFVIVDAEAMGFSLKPEEAHEIARLGVRITNAANKALGFDHPENPDWRHFSFCLFAGKVERTAEGLRAGAAVAIQPGKVDRSPTGTALSARMAVLHARGEMKEGETLTAVSLIGSTFTGRILGTTTVGDRPAILPEISGRGWITGIHQHMLDPSDPWPEGYRLTDTWGAR", "text": "FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Can also catalyze the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4- hydroxy-D-proline (c4DHyp), albeit with 30-fold lower efficiency. Is likely involved in both degradation pathways that convert t3LHyp to L- proline and t4LHyp to alpha-ketoglutarate, which would allow A.tumefaciens to grow on t3LHyp or t4LHyp as a sole carbon source. Displays no proline racemase activity. SIMILARITY: Belongs to the proline racemase family."}
+{"protein": "MMMENGLSMEYGDGYMEQEEEWEREGLLDPAWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAFQGAQQVGNNTALPDERAVMTYVSSYYHCFSGAQKAETAANRICKVLKVNQENERLMEEYERLASDLLEWIRRTMPWLNSRQADNSLAGVQKKLEEYRTYRRKHKPPRVEQKAKLETNFNTLQTKLRLSNRPAYLPTEGKTVSDISNSWKGLELAEKAFEEWLLAETMRLERLEHLAQKFKHKADAHEDWTRGKEEMLQSQDFRQCKLNELKALKKKHEAFESDLAAHQDRVEQIAAIAQELNTLEYHDCVSVNARCQRICDQWDRLGALTQRRRTALDEAERILEKIDILHLEFAKRAAPFNNWLDGTREDLVDMFIVHTMEEIQGLIQAHDQFKATLGEADKEFNLIVNLVREVESIVKQHQIPGGLENPYTTLTANDMTRKWSDVRQLVPQRDQTLANELRKQQNNEMLRRQFAEKANIVGPWIERQMDAVTAIGMGLQGSLEDQLHRLKEYEQAVYAYKPNIEELEKIHQAVQESMIFENRYTNYTMETLRVGWEQLLTSINRNINEVENQILTRDSKGISQEQLNEFRSSFNHFDKNRTGRLSPEEFKSCLVSLGYSIGKDRQGDLDFQRILAVVDPNNTGYVHFDAFLDFMTRESTDTDTAEQVIDSFRILAADKPYILPDELRRELPPDQAEYCIQRMPPYKGPNGVPGALDYMSFSTALYGETDL", "text": "FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line Note=Colocalizes with Smn at the Z-line of indirect flight muscles. SIMILARITY: Belongs to the alpha-actinin family."}
+{"protein": "MGRPLFYDIIEKPATSCIVTLCSVIWFVIQKKSIGYSQVGLSYETAIEGHYWRMITSALSHISVLHLVFNMSALWSLGVVEQLGHVGLGTAYYLHYTLVLVVFSGVLVIGIYHLLIARFKIDYFRRVTAVGYSCVVFGWMTILSVKQPSSKLNLFGLLSLPISFAPFESLIFTSIIVPQASFLGHLSGILVGYAISWGLIGGMNNYWALTMLGWIVVVFVFSLKKSGAYDFSFLEIESLTDASLPSVRFIGNGRTLQASAVPLSGVEVV", "text": "FUNCTION: Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase S54 family."}
+{"protein": "MHCVLARILLWFLIVDLSVIRALVLPPLKDYDPLEPLMKRDMAMGQRNRFKVDGQLPPILNSTDVTDDQRSLHTPGEIPSYVINHCPLVHLYSEEKYWPSDIAEYVQNFQIKDKNGNSISTHENLTLHDLKAEYHVDLFGNKTETHIPSSEVFLTSLDDFDKDPKWLLGHLPEYGTGYNSKAPAILIVVDKGNGWVDAFWFFFYPFNHGPFIMGHGPWGNHVGDWEHSLVRFYKGIPKYLWMSAHSSGTGYRYEAVEKFKKLRKRKQQDSDDGGDTILERPLIFSARGTHANYASAGQHAHDIPFFFMPLSDFTDRGPLWDPSLNFYSYTFDGKTVTPSSEREESLGLDWLHFQGGWGDQQLPARDPRQKWCVAQWKYIGGPRGPLFKKLDRLNLCGGVKKWNFWNGGCPARRLIKKAEGLDSESTDLMGDNCGVLLYRIRPKWLRGILRFLMWRGILCSLMEFFTN", "text": "FUNCTION: Involved in vacuolar protein sorting. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the VPS62 family."}
+{"protein": "MSPEEWTYLVVLLISIPIGFLFKKAGPGLKRWGAAAVGLGLTLFTCGPHTLHSLVTILGTWALIQAQPCSCHALALAWTFSYLLFFRALSLLGLPTPTPFTNAVQLLLTLKLVSLASEVQDLHLAQRKEMASGFSKGPTLGLLPDVPSLMETLSYSYCYVGIMTGPFFRYRTYLDWLEQPFPGAVPSLRPLLRRAWPAPLFGLLFLLSSHLFPLEAVREDAFYARPLPARLFYMIPVFFAFRMRFYVAWIAAECGCIAAGFGAYPVAAKARAGGGPTLQCPPPSSPEKAASLEYDYETIRNIDCYSTDFCVRVRDGMRYWNMTVQWWLAQYIYKSAPARSYVLRSAWTMLLSAYWHGLHPGYYLSFLTIPLCLAAEGRLESALRGRLSPGGQKAWDWVHWFLKMRAYDYMCMGFVLLSLADTLRYWASIYFCIHFLALAALGLGLALGGGSPSRRKAASQPTSLAPEKLREE", "text": "FUNCTION: Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA to a lysophosphatidylinositol (1- acylglycerophosphatidylinositol or LPI) leading to the production of a phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle (PubMed:18772128, PubMed:18094042). Prefers arachidonoyl-CoA as the acyl donor, thus contributing to the regulation of free levels arachidonic acid in cell (PubMed:18772128, PubMed:18094042). In liver, participates in the regulation of triglyceride metabolism through the phosphatidylinositol acyl-chain remodeling regulation (PubMed:32253259). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Localized in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. SIMILARITY: Belongs to the membrane-bound acyltransferase family."}
+{"protein": "MVVVTVARSNADVNEKKDERYWNYECYTITTGSIEKYQIYQRMGRGKYSEVFEGRKDREKIVIKALKPVRKAKICREVLILRNLSHKNIIKLMDVVVDPESQIYSLIFEYIEHEDYAKIFEKLCYKDIVEYSRQILSALSYCHSMGIIHRDIKPQNMVINQARRELKIIDWGLAEFYHPKKEYSVRVASRYYKGPELLVDYPYYDYSLDIWSFGCVLAELVFKKRPFFHGESNSDQLVKIARILGYTHLKKYVRKYKMAPLNPKYEGVGERVLLSSFTPPGKTGLYTNAIDLLEKILIYDHQDRPTADECLRHPLFESR", "text": "FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily."}
+{"protein": "MKSQVIAAVLLIAFCLCVVVTARMELQDVEDMENGFQKRRSCIDTIPKSRCTAFQCKHSMKYRLSFCRKTCGTC", "text": "FUNCTION: Inhibits voltage-gated potassium channels (Kv) with higher potency for Kv1.1/KCNA1 and Kv1.3/KCNA3. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin family. Type 1a subfamily."}
+{"protein": "MSSYLEYVSCAAGGGSGGVGGDVLGFAPKFCRADARPVALQPAFPLGSGDGAFVSCLPLATARPTPSPPAGPAQSPVPQPAAPRYAPCTLEGAYERGAAPASAAEYGFLGSGPAFDFPGALGRAADEGGAHVHYATSAVFSGGGSFLLSGQVDFAAFGEPGPFPACLKEPADGHPGPFQTVSPAPGACPKPASPTSSLPAAHSTFEWMKVKRNAPKKSKLSEYGATSPPSAIRTNFSTKQLTELEKEFHFNKYLTRARRIEIANCLQLNDTQVKIWFQNRRMKQKKREREGLLATAASVASIKLPRSETSPIKSGRNLGSPSQAQEPS", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family. Labial subfamily."}
+{"protein": "EGDRGASKNWKLSIRCGGYTLKVLTENKFLPEPPSTRKKRILESHNNTLVDPCEEHKKKNPDASVKFSEFLKKRSEMWKTIFAKEKGKFEDMAKADKAHYEREMKTYIPPKGEKKKKFKDPNAPKRPPLAFFLFCSEYRPKIKGEHPGLSIDDVVKKLAGMWNNTAASDKQFYEKKAAKLKEKYKKDIAACRAKGKPNSATKRVVKAEKSKKKKE", "text": "FUNCTION: Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. May also play a role in infection by viruses through mechanisms that may involve chromatin and/or transcriptional regulation (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, PML body Nucleus, nuclear body Cytoplasm Note=Accumulates in the cytoplasm upon FAS activation."}
+{"protein": "MMWRPSVLLLLLLLRHGAQGKPSPDAGPHGQGRVHQAAPLSDAPHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIVIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVGSQATNYGEDLTRHHDEL", "text": "FUNCTION: Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum (PubMed:16433634, PubMed:28939891). Required for the proper biosynthesis and transport of pulmonary surfactant-associated protein A/SP-A, pulmonary surfactant- associated protein D/SP-D and the lipid transporter ABCA3 (By similarity). By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis (By similarity). Has an anti-fibrotic activity by negatively regulating the secretion of type I and type III collagens (PubMed:28939891). This calcium-binding protein also transiently associates with immature PCSK6 and regulates its secretion (PubMed:16433634). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the CREC family."}
+{"protein": "MTNLMDHTQQIVPFIRSLLMPTTGPASIPDDTLEKHTLRSETSTYNLTVGDTGSGLIVFFPGFPGSVVGAHYTLQSSGSYQFDQMLLTAQNLPVSYNYCRLVSRSLTVRSSTLPGGVYALNGTINAVTFQGSLSELTDYSYNGLMSATANINDKIGNVLVGEGVTVLSLPTSYDLSYVRLGDPIPAAGLDPKLMATCDSSDRPRVYTVTAADEYQFSSQLIPSGVKTTLFTANIDALTSLSVGGELIFSQVTIHSIEVDVTIYFIGFDGTEVTVKAVATDFGLTTGTNNLVPFNLGGPTSEITQPITSMKLEVVTYKRGGTAGDPISWTVSGTLAVTVHGGNYPGALRPVTLVAYERVAAGSVVTVAGVSNFELIPNPELAKNLVTEYGRFDPGAMNYTKLILSERDRLGIKTVWPTREYTDFREYFMEVADLNSPLKIAGAFGFKDIIRAIRKIAVPVVSTLFPPAAPLAHANREGVDYLLGDEAQAASGTARGASGKARAASGRIRQLTLAADKGYEVVANMFQVPQNPIVDGILASPGILRGAHNLDCVSKEGATLFPVVITTLEDELTPKALNSKMFAVIEGAREDLQPPSQRGSFIRTLSGHRVYGYAPDGVLPLETGRDYTVVPIDDVWDDSIMLSQDPIPPIVGNSGNLAIAYMDVFRPKVPIHVAMTGALNASEIESVSFRSTKLATAHRLGMKLAGPGDYDINTGPNWATFIKRFPHNPRGWDRLPYLNLPYLPPTAGRQFHLALAASEFKETPELEDAVRAMDAAANADPLFRSALQVFMWLEENGIVTDMANFALSDPNAHRMKNFLANAPQAGSKSQRAKYGTAGYGVEARGPTPEEAQRAKDARISKKMETMGIYFATPEWVALNGHRGPSPGQLKYWQNTREIPEPNEDYPDYVHAEKSRLASEEQILRAATSIYGAPGQAEPPQAFIDEVARVYETNHGRVPNQEQMKDLLLTAMEMKHRNPRRAPPKPKPKPNAPSQRPPGRLGRWIRTVSDEDLE", "text": "FUNCTION: Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1 (By similarity). FUNCTION: Structural peptide 2 is a small peptide derived from pVP2 C- terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity). FUNCTION: Capsid protein VP3 plays a key role in virion assembly by providing a scaffold for the capsid made of VP2. May self-assemble to form a T=4-like icosahedral inner-capsid composed of at least 180 trimers. Plays a role in genomic RNA packaging by recruiting VP1 into the capsid and interacting with the dsRNA genome segments to form a ribonucleoprotein complex. Additionally, the interaction of the VP3 C- terminal tail with VP1 removes the inherent structural blockade of the polymerase active site. Thus, VP3 can also function as a transcriptional activator (By similarity). FUNCTION: Structural peptide 3 is a small peptide derived from pVP2 C- terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity). FUNCTION: Structural peptide 1 is a small peptide derived from pre-VP2 C-terminus. It destabilizes and perforates cell membranes, suggesting a role during entry (By similarity). FUNCTION: The precursor of VP2 plays an important role in capsid assembly. First, pre-VP2 and VP2 oligomers assemble to form a procapsid. Then, the pre-VP2 intermediates may be processed into VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the mature virion. The final capsid is composed of pentamers and hexamers but VP2 has a natural tendency to assemble into all-pentameric structures. Therefore pre-VP2 may be required to allow formation of the hexameric structures (By similarity). FUNCTION: Protease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation. FUNCTION: Structural peptide 4 is a small peptide derived from pVP2 C- terminus. It is essential for the virus viability (By similarity). SUBCELLULAR LOCATION: [Structural peptide 4]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Structural peptide 2]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Structural peptide 3]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Structural peptide 1]: Virion Host cytoplasm."}
+{"protein": "MNHSERFVFIAEWFDPNASLFRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYEDLHLEDLFIGNKVNIFSRQLVLLDYGDQYTARQLGSKKEKTLALIKPDAVSKAGEIIEIINKAGFTLTKLKMMTLSRKEATDFHIDHQSRPFLNELIQFITSGPIIAMEILRDDAVCEWKRLLGPANSGLARTDAPESIRALFGTDGIKNAAHGPDSFACAAREMELFFPSSGVCGPANTAKFTNCTTCCIVKPHAVSEGLLGKILMTIRDAGFEISAMQMFNMDRINVEEFYEVYKGVVSEYNEMVTEMYSGPCVAMEIQQTNPTMTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLPEDGLLEVQYFFKILDN", "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 (PubMed:34715025). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SIMILARITY: Belongs to the NDK family."}
+{"protein": "MGLTLTQKILSAKVGREVKPGELIEVDVDMVLGNDVTAPVAIKEFEKIGIDRVFDNTKIALVPDHFVPNKDIKSAEQVNIMRKFAKKHGIVNFFEVGQMGIEHALLPEKGLVLPGDVVIGADSHTCTYGALTCFSTGVGSTDMAAAMATGKAWFKVPEAIKFVLKGNLQKWVSGKDVILYIIGKIGVDGALYKSMEFTGNIKALSMDDRFTIANMAIEAGAKNGIFDFDEITEAYVKGRAKREYKVFERDVDAEYSEVYEISLDEIRPQVAFPHLPENTRNIDEVGKVKIDQVVIGSCTNGRISDMEIAYKILKGKKVHPDVRLLIFPATQEIYLECVKRGYIEEFIKAGAAVSTPTCGPCLGGHMGILAKGERALATTNRNFVGRMGHPESEVYLSSPAVAAASAIAGYIVSPEEV", "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 2 subfamily."}
+{"protein": "QGDKRDICRLPPEQGPCKGRIPRYFYNPASRMCESFIYGGCKGNKNNFKTKAECVRACRPPERPGVCPKTSGPGICLHGCDSDSDCKEGQKCCFDGCGYICLTVAPSGSP", "text": "FUNCTION: The first domain inhibits trypsin; the second one inhibitis subtilisin."}
+{"protein": "MNPAISVALLLSVLQVSRGQKVTSLTACLVNQNLRLDCRHENNTKDNSIQHEFSLTREKRKHVLSGTLGIPEHTYRSRVTLSNQPYIKVLTLANFTTKDEGDYFCELQVSGANPMSSNKSISVYRDKLVKCGGISLLVQNTSWMLLLLLSLSLLQALDFISL", "text": "FUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor."}
+{"protein": "MFNRVQKEINQIINRGFDRTLRLAVTGLSRSGKTAFITSLINQLLSINQHSSQNLPLFEAARNGSILAVKRVSQQDLSVPRFDYESNLNDLSQNPPQWFQSTRGVSETRLAIRFQRQSGLLRHLKERGTLYLDIFDYPGEWLLDLPLLNLDFQQWSQEQIKVTTGVRAELAQNWLSMLQNLDLSAVANEDVLAKIAKSYTDYLHQCKAQGMQFIQPGRFVLPSDLEGAPALQFFPLIHLSGEHWQTLKKTAKSNSYFAVLTKRYNYYRNKIVKGFYENYFSTFDRQVILADCLTPLNHSQQAFLDMQMGLNQLFNNFHYGSRNFLHRLFSPQIDRLMFVATKADHITRDQIPNLVSLMRQIVQEGGRHVEFEGIDTEYTAIAAVRTTKQVIVNQQGKEIKAIQGVRSIDKQLITLYPGTVPSKLPKTEFWQKQPHFDFDSFEPQPLEQGESIPHLRMDAVLQFLLSDRFE", "text": "SIMILARITY: To E.coli YcjX."}
+{"protein": "MFTGIIEETGTIESMKKAGHAMALTIKCSKILEDVHLGDSIAVNGICLTVTDFTKNQFTVDVMPETVKATSLNDLTKGSKVNLERAMAANGRFGGHFVSGHVDGTAEITRIEEKSNAVYYDLKMDPSLTKTLVLKGSITVDGVSLTIFGLTEDTVTISLIPHTISETIFSEKTIGSKVNIECDMIGKYMYRFLHKANENKTQQTITKAFLSENGF", "text": "FUNCTION: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8- ribityllumazine, resulting in the formation of riboflavin and 5-amino- 6-(D-ribitylamino)uracil."}
+{"protein": "MGIPESQLDTWSHQGSIAQSASTYSIIKNALESANTKYHGKNFKVFLQGSYGNDTNIYAESDVDVVICLDDVYYSDLTQLSPEDKDAYDRAFVPATYSYTQFKQDVLEALTERFGSDVKVGDKAIVVAANGSRRKADVIASMQFRRYWKFKGHYDSQYDEGICFFNGAGERIANYPKQHSENLTLKHQASNKWLKPMVRVLKNLRSKLIADGKLKSGLAPSYYLEGLLYNVPNEKFGTSYADCFVNAMNWIQTEADKDKLVCANEQYYLLWEGTHTSWEKADAEAFIDAAIKMWNEW", "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 II-A(UA) CBASS system (PubMed:32839535). FUNCTION: Cyclic dinucleotide synthase that catalyzes the synthesis of 3',3'-cyclic UMP-AMP (cUMP-AMP) from UTP and ATP, a second messenger for cell signal transduction. Controls the activity of cUAMP-activated phospholipase CapE, a patatin-like lipase that is a direct cUMP-AMP receptor encoded in the cdnE operon. SIMILARITY: Belongs to the CD-NTase family. E01 subfamily."}
+{"protein": "MKESNSRREFLSQSGKMVTAAALFGTSVPLAHAAVAGTLNCEANNTMKITDPHYYLDNVLLETGFDYENGVAVQTRTARQTVEIQDGKIVALRENKLHPDATLPHYDAGGKLMLPTTRDMHIHLDKTFYGGPWRSLNRPAGTTIQDMIKLEQKMLPELQPYTQERAEKLIDLLQSKGTTIARSHCNIEPVSGLKNLQNLQAVLARRQAGFECEIVAFPQHGLLLSKSEPLMREAMQAGAHYVGGLDPTSVDGAMEKSLDTMFQIALDYDKGVDIHLHETTPAGVAAINYMVETVEKTPQLKGKLTISHAFALATLNEQQVDELANRMVVQQISIASTVPIGTLHMPLKQLHDKGVKVMTGTDSVIDHWSPYGLGDMLEKANLYAQLYIRPNEQNLSRSLFLATGDVLPLNEKGERVWPKAQDDASFVLVDASCSAEAVARISPRTATFHKGQLVWGSVAG", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily."}
+{"protein": "MNFRRMLCAAIVLTIVLSIMLPSTVFALEDKSSKLPDYKNDLLYERTFDEGLCFPWHTCEDSGGKCDFAVVDVPGEPGNKAFRLTVIDKGQNKWSVQMRHRGITLEQGHTYTVRFTIWSDKSCRVYAKIGQMGEPYTEYWNNNWNPFNLTPGQKLTVEQNFTMNYPTDDTCEFTFHLGGELAAGTPYYVYLDDVSLYDPRFVKPVEYVLPQPDVRVNQVGYLPFAKKYATVVSSSTSPLKWQLLNSANQVVLEGNTIPKGLDKDSQDYVHWIDFSNFKTEGKGYYFKLPTVNSDTNYSHPFDISADIYSKMKFDALAFFYHKRSGIPIEMPYAGGEQWTRPAGHIGIEPNKGDTNVPTWPQDDEYAGRPQKYYTKDVTGGWYDAGDHGKYVVNGGIAVWTLMNMYERAKIRGIANQGAYKDGGMNIPERNNGYPDILDEARWEIEFFKKMQVTEKEDPSIAGMVHHKIHDFRWTALGMLPHEDPQPRYLRPVSTAATLNFAATLAQSARLWKDYDPTFAADCLEKAEIAWQAALKHPDIYAEYTPGSGGPGGGPYNDDYVGDEFYWAACELYVTTGKDEYKNYLMNSPHYLEMPAKMGENGGANGEDNGLWGCFTWGTTQGLGTITLALVENGLPATDIQKARNNIAKAADRWLENIEEQGYRLPIKQAEDERGGYPWGSNSFILNQMIVMGYAYDFTGNSKYLDGMQDGMSYLLGRNGLDQSYVTGYGERPLQNPHDRFWTPQTSKKFPAPPPGIIAGGPNSRFEDPTITAAVKKDTPPQKCYIDHTDSWSTNEITVNWNAPFAWVTAYLDEIDLITPPGGVDPEEPEVIYGDCNGDGKVNSTDAVALKRYILRSGISINTDNADVNADGRVNSTDLAILKRYILKEIDVLPHK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family."}
+{"protein": "MDFNMKKLASDAGIFFTRAVQFTEEKFGQAEKTELDAHFENLLARADSTKNWTERILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGELLAQYMAEAASELGPNTPYGKTLMKVSEAEKRLGAAERDFIHTASLSFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACKARLKKAKAAEAKATCEGDTVPDFQETRPRNYILSASASALWNDEVDKAEQELRAAQTEFDRQAEVTRLLLEGISSAHVNHLRCLHEFVKSQTTYYAQCYRHMLDLQKQLGSSQGAIFPGTFVGTTEPASPPLSSTSPTTTAATMPVVPTGAGLAPPEEAALCLEEVAPPASGTRKARVLYDYEAADSSELALLADELITVYSLPGMDPDWLIGERGNKKGKVPVTYLELLS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endophilin family."}
+{"protein": "MGSLFGRVAALRALLCGPRFQCLLVRPSSGGPPWPQERTLVAVKPDGVQRRLVGTVIQRFERRGFKLVGMKMLQAPESILAEHYRDLQRKPFYPALISYMSSGPVVAMVWEGPNVVHISRAMIGHTDSTEAAPGTIRGDFSVHISRNVIHASDSVDGAQREIELWFQSSELLNWADGGHHSSCYPA", "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. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis. Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity. Acts as mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration. Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria. In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space; Peripheral membrane protein. Mitochondrion matrix Note=Predominantly localized in the mitochondrion intermembrane space. Colocalizes with OPA1 in mitochondria (By similarity). SIMILARITY: Belongs to the NDK family."}
+{"protein": "MIEFPVVLVINCGSSSVKFSVLDAASCEALITGIADGVNTENAFISVNGGEPAPLARKDYEGALAAIALELEARDLMGSVALIGHRIAHGGSVFSESTPITDEVIDQIREISPLAPLHNYANLSGVEAAKHLFPGVQQVAVFDTSFHQTLAPQAYLYGLPYRYFEELGVRRYGFHGTSHRYVAQQAYSLLDIPQQDSGLVIAHLGNGASICAVRNGESVDTSMGMTPLEGLVMGTRCGDVDFGAMAWIAQQTGQTLDDLERVVNKESGLLGISGLSSDLRTLEKAWHDGHERARLAIETFVHRIARHIAGHAASLHRLDGVVFTGGIGENSKLIRQLVTDRLKVFGITLDPLKNALPGSAGERIITTDDSDVPCAVIPTNEEKMIALDAIRLGKVHPAAAYA", "text": "FUNCTION: Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. SIMILARITY: Belongs to the acetokinase family. TdcD subfamily."}
+{"protein": "MLNQIVVAGAIVRGCTVLVAQRVRPPELAGRWELPGGKVAAGETERAALARELAEELGLEVADLAVGDRVGDDIALNGTTTLRAYRVHLLGGEPRARDHRALCWVTAAELHDVDWVPADRGWIADLARTLNGSAADVHRRC", "text": "FUNCTION: May be 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. MutT specifically degrades 8-oxo- dGTP to the monophosphate (By similarity). FUNCTION: May be 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. MutT specifically degrades 8-oxo- dGTP to the monophosphate (By similarity). In vitro has 8-oxo-dGTPase activity. SIMILARITY: Belongs to the Nudix hydrolase family."}
+{"protein": "MPEPGPRMNGFSLGELCWLFCCPPCPSRIAAKLAFLPPEPTYTVLAPEQRGAGASAPAPAQATAAAAAAQPAPQQPEEGAGAGPGACSLHLSERADWQYSQRELDAVEVFFSRTARDNRLGCMFVRCAPSSRYTLLFSHGNAVDLGQMCSFYIGLGSRINCNIFSYDYSGYGVSSGKPSEKNLYADIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYECAAVILHSPLMSGLRVAFPDTRKTYCFDAFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDIELYAQYLERLKQFISHELPNS", "text": "FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards NRAS and DLG4/PSD95. 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": "MAATAAEVAASGSGEAREEAEAPGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMGNFQNFKPRSNREEIKFHEFVEKLQAIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFRNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN", "text": "FUNCTION: Hydroxylates HIF-1 alpha at 'Asn-799' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation (By similarity). Positively regulates ASB4 activity, promoting vascular differentiation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, perinuclear region."}
+{"protein": "MPPRELSEAESSPLRSPTPPPGRGSASPELGIKCVLVGDGAVGKSSLIVSYTCNGYPARYRPTALDTFSVQVLVDGAPVRIELWDTAGQEDLDRLRSLCYPDTDVFLACFSVVQPSSFQNITEKWLPEIRTHNPQAPVLLVGTQADLRDDVNVLIQLDQGGREGPVPQPQAQGLAEKIRACCYLECSALTQKNLKEVFDSAILSAIEHKARLEKKLNAKGVRTLSRCRWKKFFCFV", "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": "MKISRIAQRLDEAAVSGKATPQLTGDDAVTVREAAEIQRLLIAHRIERGARQVGLKMGFTSRAKMAQMGVSDLIWGRLTSDMWVEEGGEIDLAHYVHPRVEPEICYLLGKRLEGNVTPLEALAAVEAVAPAMEIIDSRYRDFKFSLPDVIADNASSSGFVVGAWHKPETDVSNLGMVMSFDGRAVELGTSAAILGSPIRALVAAARLAAQQGEALEAGSLILAGAATAAVALRPGISVRCEVQNLGSLSFSTTGER", "text": "FUNCTION: Involved in the modified meta-cleavage pathway for the 2- aminophenol catabolism. SIMILARITY: Belongs to the hydratase/decarboxylase family."}
+{"protein": "MRIMIKGGVWKNTEDEILKAAVMKYGKNQWARISSLLVRKSAKQCKARWYEWLDPSIKKTEWTREEDEKLLHLAKLLPTQWRTIAPIVGRTPSQCLERYEKLLDAACTKDENYDAADDPRKLRPGEIDPNPEAKPARPDPVDMDEDEKEMLSEARARLANTRGKKAKRKAREKQLEEARRLASLQKRRELKAAGIDGRHRKRKRKGIDYNAEIPFEKRAPAGFYDTADEDRPADQVKFPTTIEELEGKRRADVEAHLRKQDVARNKIAQRQDAPAAILQANKLNDPEVVRKRSKLMLPPPQISDHELEEIAKMGYASDLLAENEELTEGSAATRALLANYSQTPRQGMTPMRTPQRTPAGKGDAIMMEAENLARLRDSQTPLLGGENPELHPSDFTGVTPRKKEIQTPNPMLTPSMTPGGAGLTPRIGLTPSRDGSSFSMTPKGTPFRDELHINEDMDMHESAKLERQRREEARRSLRSGLTGLPQPKNEYQIVAQPPPEESEEPEEKIEEDMSDRIAREKAEEEARQQALLKKRSKVLQRDLPRPPAASLAVIRNSLLSADGDKSSVVPPTPIEVADKMVREELLQLLEHDNAKYPLDDKAEKKKGAKNRTNRSASQVLAIDDFDENELQEADKMIKEEGKFLCVSMGHENKTLDDFVEAHNTCVNDLMYFPTRSAYELSSVAGNADKVAAFQEEMENVRKKMEEDEKKAEHMKAKYKTYTKGHERRAETVWTQIEATLKQAEIGGTEVECFKALKRQEEMAASFRKKNLQEEVIKQKETESKLQTRYGNMLAMVEKAEEIMVGFRAQALKKQEDVEDSHKLKEAKLATGEEEDIAIAMEASA", "text": "FUNCTION: Component of the MAC complex that probably regulates defense responses through transcriptional control and thereby is essential for plant innate immunity. Possesses a sequence specific DNA sequence 'CTCAGCG' binding activity. Involved in mRNA splicing and cell cycle control. May also play a role in the response to DNA damage. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CEF1 family."}
+{"protein": "MQKTKLRLIFMIIYKEIAKLNKTFPLLNEEKILLGTDGSVTNILEILFEGECRVETINQKIVANTNYREVILKVNNIPLVYAVSKTPFKNIEEENLREEIKRDLLSADIPIGKIIRKHNLETRREIKYIGIAEIDDYLKSLLKTNYSRLPKRTYNIIYKNKVLMEITEIFAVRGKLVKNTYSID", "text": "SIMILARITY: Belongs to the chorismate pyruvate-lyase type 2 family."}
+{"protein": "MGMTPRRKRRGGAVQITRPTGRPRTPTTQTTKRPRWVVGGTTILTFVALLYLVELIDQLSGSRLDVNGIRPLKTDGLWGVIFAPLLHANWHHLMANTIPLLVLGFLMTLAGLSRFVWATAIIWILGGLGTWLIGNVGSSCGPTDHIGASGLIFGWLAFLLVFGLFVRKGWDIVIGLVVLFVYGGILLGAMPVLGQCGGVSWQGHLSGAVAGVVAAYLLSAPERKARALKRAGARSGHPKL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.leprae ML1171."}
+{"protein": "MAAGGGGSYDPLAPAGVPCAFSPDSQAYFALASSDGQLRVWETANNRLHQEYVPSAHLSGTCTCLAWAPARLQAKESHQRKKRKSEVTGTKDQADLLALGTAVGSILLYSTVRGELHSKLTSGGHENRVNCIQWHQDNDCLYSCSDDKYIVEWSTQTCKVKCKWKGDNSSVSSLCISPDGKMLLSAGRTIKLWVLETKEVYRHFTGHATPVSSLRFTTIRPNESQPSDGITGLYFLSGAVHDRLLNVWQVRSENKEKSAVMSFTVTDEPVYVDLTLSENKEEPVKLAVVCRDGQVHLFEHILNGHCKKPLTSNCTIQIATPGKGKKVTPKPIPILAASFCLDKMSLLLVYGNWFQPTIERVALNSKDTHICLERDISNCWAPTVETAITKVKTPVMNSEAKVLVPGIPGHHAPIKLPPAQPKEAENKRKLGSTEATIEERLGAMDLDRKGRKDDLQTNSFAVLLTQGLESNDFEILNKVLQTKNVNLIKRTVLRIPLRVVIPLLQELTKRLQGHPNSAALMIQWLKCVLTIHASYLSTLPDLVEQLGTLYQLMESRVKTFQKLSNLHGKLILLVTQVTASEKSKKMTSPGQKAKLVYEEESSEEESDDEVPEKDSDDNWDEDEDKDSEKDEGVDEDNEEEDEDMEDKEENEEDREVSSEKELNGDSDLDPENESEEE", "text": "FUNCTION: Ribosome biogenesis factor that coordinates hyperactive transcription and ribogenesis. 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. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I (By similarity). Essential for stem cell pluripotency and embryonic development (PubMed:31128943). In the nucleoplasm, recruited by promoter- associated/nascent transcripts and transcription to active promoters where it facilitates releases of elongation factor P-TEFb and paused RNA polymerase II to allow transcription elongation and maintain high- level expression of its targets genes (PubMed:31128943). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleolus fibrillar center Nucleus, nucleoplasm. SIMILARITY: Belongs to the UTP5 family."}
+{"protein": "MARLLQASCLLSLLLAGFLPQSRGQDKSKMDCHGGVSGTIYEYGALTIDGEEYTPFKQYIGKYVLFVNVASYUGLTGQYIELNALQEELAPFGLDLLGFPCNQFGKQEPGENSEILPSLKYVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTSELLGTSDRLFWEPMKVHDIRWNFEKFLVGPDGIPVMRWHHRTTISNVKMDILSYMRRQAALGVKRK", "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: Secreted. SIMILARITY: Belongs to the glutathione peroxidase family."}
+{"protein": "MKCLLLALGLSLMCGNQATDIPQTMQDLDLQEVAGRWHSVAMVASDISLLDSESVPLRVYVEELRPTPEGNLEIILREGANHACVERNIVAQKTEDPAVFTVNYQGERKISVLDTDYAHYMFFCVGPPLPSAEHGMVCQYLARTQKVDEEVMEKFSRALQPLPGRVQIVQDPSGGQERCGF", "text": "FUNCTION: Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MIKTKIMGILNVTPDSFSDGGQYHSVDQAVKRAKEMIDEGVDIIDVGGVSTRPGHKEVSHKEVSLKEEMNRVLPVVESIVKYDVQISVDTFRSEVAEACLKLGVSMINDQWAGLFDSNMFNVVSQYGAEIVLMHNGDGHRDKPVVEEMLVSLLAQANKAELAGIPHNKIWLDPGIGFAKTREEENEVMARLDELVATEYPVLLATSRKRYIKEMMNQDSSPSDRDEATAATTAYGIMKGVRGVRVHNVLLNTRLAQSMDFLKENEYERHHLS", "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": "MDGPAIITQVTNPKEDEARSPVAGEKASQRNISLKKQRGRSILSSFFCCFRDYNVEAPPANSPSVLPPLVEENGGLQKGDQRQVIPVPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSFKPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLFECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWFDDMTDTELLDLIPFFEGLSREDDVYSMLHRLCSR", "text": "FUNCTION: 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. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MARKVVVVDDEKPIADILEFNLKKEGYDVYCAYDGNDAVDLIYEEEPDIVLLDIMLPGRDGMEVCREVRKKFEMPIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRELIARVKANLRRHYSQPAQEVSGTTNEITIKDIVIYPDAYSIKKRGEDIELTHREFELFHYLSKHMGQVMTREHLLQTVWGYDYFGDVRTVDVTIRRLREKIEDDPSHPEYIVTRRGVGYFLQQHD", "text": "FUNCTION: Member of the two-component regulatory system WalK/WalR. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MIKIYNRKTKAYDVEQVAGLKYINWSYASPIGKSFLELFIKKKMFSKLYGNFCDSSLSKKKIKAFIDEFNIDMSLCNKNIDEFENFNDFFARTLTPEARPIDYSENILISPGDGRLSAFENIDLDKVVQIKGYTYSLKELIDDPKVAEEFEGGTCLILRLCPTDYHRFHFVDSGTCSESKKISGFYYSVNPIALNNVSELFCKNKREWSIFNSDNFGEILHVEVGATCVGTILQTYSPEKRVKKGEEKGYFKFGGSTTILFFKKDTIKIDSDIVEQTKLGFETKVNMGETIGHK", "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 II sub-subfamily."}
+{"protein": "METVATIQTPTKLMNKENAEMILEKIVNHIAMYISDESIYSENNPEYIDFRNRYGDYRSLIIKSDHEFVKLCKDHAEKSSPETQQMIIKHIYEQYLIPVSEVLLKPIMSMGDIFTYNGCKDNEWMLEQLSTLNFNNLYTWNSCSIGNVTRLFYTFFSYLMKDKLNI", "text": "SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the orthopoxvirus OPG069 family."}
+{"protein": "MSRSETLFNNAQKHIPGGVNSPVRAFKSVGGTPLFFKHAEGAYVLDEDDKRYVDYVGSWGPMILGHSHPDVLDAVRRQLDHGLSYGAPTALEVEMADLVCSMVPSMEMVRMVSSGTEATMSAIRLARGYTGRDSIIKFEGCYHGHSDSLLVKAGSGALTFGVPNSPGVPAAFAKHTLTLPFNDIEAVRKTLGEVGKEVACIIVEPVAGNMNCVPPAPGFLEGLREACDEHGVVLIFDEVMTGFRVALGGAQAYYGVTPDLSTFGKIIGGGMPVGAFGGKREIMQQISPLGPVYQAGTLSGNPLAMAAGLTTLRLISRPGFHDELTAYTTRMLDGLQQRADAAGIPFVTTQAGGMFGLYFSGADAIVTFEDVMASDVERFKRFFHLMLDGGVYLAPSAFEAGFTSIAHGDKELEITLNAAEKAFAALK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
+{"protein": "MATVIPGDLSEVRDTQKAPSGKRKRGESKPRKNFPCQLCDKAFNSVEKLKVHSFSHTGERPYKCTHQDCTKAFVSKYKLQRHMATHSPEKTHKCNYCEKMFHRKDHLKNHLHTHDPNKETFKCEECGKSYNTKLGFKRHLALHAATSGDLTCKVCLQTFESTGVLLEHLKSHAGKSSGGVKEKKHQCEHCERRFYTRKDVRRHMVVHTGRKDFLCQYCAQRFGRKDHLTRHMKKSHNQELLKVKTEPVDFLDPFTCNMSVPIKDELLPVMSLPSSELLSKPFTNTLQLNLYNTPFQSMQSSGSTHQMITTLPLGMTCPIDMDTVHPSHHLAFKCPFSSTSYAISIPEKEQPLKGEIESYLMELQGGAPSSSQDSQASSSKLGLEPQSGSPDDGAGDLSLSKSSISISDPLNTPALDFSQLFNFIPLNGPPYNPLSVGSLGMSYSQDEAHSSVSQLPTQTQDLQDPANTVGLGSLHSLSAAFTSSLSSSTTLPRFHQAFQ", "text": "FUNCTION: Transcription factor whose activation results in up- regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation: when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Cooperates with CBFB-MYH11 (By similarity). SUBCELLULAR LOCATION: Nucleus. Note=Strong nucleolar localization when sumoylation is inhibited. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MAHPHLLAERISRLSSALEKGLYERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQRARAFEYLMTRFSTPEEVFGPLSIQALKDEGRYERLTTGYLPEAEIVFLDEIWKAGPAILNTLLTAINERHFRNGAFEEKIPMRLLVAASNELPEADSSLEALYDRMLIRLWLDKVQDKANFRSMLISQQDESDNPVPASLQVSDEEYQQWQKDIGAISLPDPVFELIFTLRQQLDNLPNAPYVSDRRWKKAIRLLQASAFFSGRDAVAPIDLILLKDCLWYDAQSLNLMQQQLEILMTGHAWQQQAMLTRLGGIVQRRLQLQQQQSDKTAFTVIKEGGMFSRRPHYTLPPEASASTLTLLLQKPLKLHDMEVIHITFDRSALELWLTKGGEIRGKLNGIGFAQTLNMEVDNAQHLVVRDISLQGTRLALPGTAEDSMPAEIKQQLETLENDWRQQHTRFSEQQHCLFIHSDWLGRIEASLQDVGEQIRQAKQC", "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": "MEMPGRRSNYTLLSQFSDDQVSVSVTGAPPPHYDSLSSENRSNHNSGNTGKAKAERGGFDWDPSGGGGGDHRLNNQPNRVGNNMYASSLGLQRQSSGSSFGESSLSGDYYMPTLSAAANEIESVGFPQDDGFRLGFGGGGGDLRIQMAADSAGGSSSGKSWAQQTEESYQLQLALALRLSSEATCADDPNFLDPVPDESALRTSPSSAETVSHRFWVNGCLSYYDKVPDGFYMMNGLDPYIWTLCIDLHESGRIPSIESLRAVDSGVDSSLEAIIVDRRSDPAFKELHNRVHDISCSCITTKEVVDQLAKLICNRMGGPVIMGEDELVPMWKECIDGLKEIFKVVVPIGSLSVGLCRHRALLFKVLADIIDLPCRIAKGCKYCNRDDAASCLVRFGLDREYLVDLVGKPGHLWEPDSLLNGPSSISISSPLRFPRPKPVEPAVDFRLLAKQYFSDSQSLNLVFDPASDDMGFSMFHRQYDNPGGENDALAENGGGSLPPSANMPPQNMMRASNQIEAAPMNAPPISQPVPNRANRELGLDGDDMDIPWCDLNIKEKIGAGSFGTVHRAEWHGSDVAVKILMEQDFHAERVNEFLREVAIMKRLRHPNIVLFMGAVTQPPNLSIVTEYLSRGSLYRLLHKSGAREQLDERRRLSMAYDVAKGMNYLHNRNPPIVHRDLKSPNLLVDKKYTVKVCDFGLSRLKASTFLSSKSAAGTPEWMAPEVLRDEPSNEKSDVYSFGVILWELATLQQPWGNLNPAQVVAAVGFKCKRLEIPRNLNPQVAAIIEGCWTNEPWKRPSFATIMDLLRPLIKSAVPPPNRSDL", "text": "FUNCTION: Acts as a negative regulator in the ethylene response pathway (PubMed:8431946). Phosphorylates the cytosolic C-terminal domain of EIN2, preventing the signaling in the absence of ethylene (PubMed:23132950). Interacts with C24:1-ceramide upon hypoxic conditions (e.g. submergences) to in turn regulate EIN2 endoplasmic reticulum (ER)-to-nucleus translocation and EIN3 stabilization (PubMed:25822663). SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily."}
+{"protein": "MGGFDYLQKGGTGFTLQVKKPQIRRVVQTRPAAPSPSANKATPRTVPSGPQKKTPETASRSVTGERGFSPSKRRLTPLRNRKRPTPEQRLSSDDDDDGSDTDTSLELRKRARTGESAEPDYGRRLRSLKAFSGDETRSLPIVHASEITSVQKPGKFKPAFENMNQTSEIFLQYPSATPKERYEAVVPRDDDEFKPLDDIVQVIETVTQAYIPEDELDEFNNESTGIKRRLRRALARGSEREFRESVKDYNVAIERLRRSGSIAKKLDATYRLSLPHVERILTQIYSRTVSPRVDSLRQYENGTDNVYGELLPRFISTIFKETGLKSNHVFVDLGSGVGNVVLQAALEIGCESWGCEMMQNACDLAELQQAEFKARCRLWGIAPGKTHLVRGDFLKEQSIIDVLKRADVVLINNQAFTPQLNNELINHFLDMKEGCQIVSLKSFVPVGHKIQSRNLNSPINLLTVKQRQYWSNSVSWTDVGGSYFIATKDSSRLKAFSESLA", "text": "FUNCTION: Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family."}
+{"protein": "METQRASLCLGRWSLWLLLLGLVVPSASAQALSYREAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDPGTPKPVSFTVKETVCPRPTWRPPELCDFKENGRVKQCVGTVTLNPSNDPLDINCDEIQSVGRFRRLRKKTRKRLKKIGKVLKWIPPIVGSIPLGCG", "text": "FUNCTION: Exerts antimicrobial activity against both Gram-positive and negative bacteria. Its activity appears to be mediated by its ability to damage bacterial membranes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cathelicidin family."}
+{"protein": "MNISNQLSLEQEFELVLYKQKIEPLNLEQSRNLLAETLRTMLLKDNIIKYVIKNSHFSQ", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf18/nblA family."}
+{"protein": "MNLQHHFLIAMPALQDPIFRRSVVYICEHNTNGAMGIIVNKPLENLKIEGILEKLKITPEPRDESIRLDKPVMLGGPLAEDRGFILHTPPSNFASSIRISDNTVMTTSRDVLETLGTDKQPSDVLVALGYASWEKGQLEQEILDNAWLTAPADLNILFKTPIADRWREAAKLIGVDILTMPGVAGHA", "text": "SIMILARITY: Belongs to the UPF0301 (AlgH) family. SIMILARITY: Belongs to the UPF0301 (AlgH) family."}
+{"protein": "MLKALFGDPNTRKIKKLQPIVAEINLLEEDIQHLSDEQLKEKTVEFREMLDKANNDEELEDILEEILPDAFAVVREAAKRVLGMRHFDVQLMGGMVLHQGQIAEMKTGEGKTLVATLPAYLNGLTSRGVHIVTVNDYLARRDAEWMGQVHRFLGLTVGLIQSGMNPEERKKNYACDVTYTTNSELGFDYLRDNMATAMAEVVQRPPNYCIIDEVDSILIDEARTPLIISGQVERPTEKYIKAAEIAKQLEKQESEEDPKDYEVDEKARNVLMTDQGFEKAEQLLGVGDLYDQENPWAHYIFNAIKAKELFTKDVNYIVKNKEVVIVDEFTGRVLAGRRWSDGLHQAIEAKEGVPIQRETQTLATITYQNFFLLYNKLSGMTGTAKTEETELEKVYNLQVTIVPTNRPSQRYDFPDVVYKTEPAKWKAVAAEVEEMHKMGRPILVGTTSVEKSEVISALLQQSNIPHNILNARPENVERESEIVAQAGRKGAVTIATNMAGRGTDIILGGNSDYMARLKIREYLMPQIVMPEDDNLMAGGMGSNNRRPQGFGQDSKKKKWQPSADIFPTDLSPETQNMLKEAVKFAVDQYGQQSLSELEAEEKIAIASENAPTDDPVIEKLREVYKLIRKQYDAFTDKEHDEVVDKGGLHVIATERHESRRIDNQLRGRAGRQGDPGSTKFFLSLEDNLLRIFGGDRVAGLMNAFRVEEDMPIESKMLTRSLEGAQKKVETFYYDTRKQVFEYDEVMNNQRRAIYAERRRVLEGLDLKEQVLQYAEKTMDEIVDAYVNPELPPEEWDVENLVSKVKEFVYLLEDITAKDMEDMTVAEMKIFLHEEVRKAYDIKEDQVDKVRPGLMREAERFFILQQIDTLWREHLQSMDALRESIGLRGYGQKDPLIEYKQEGYEMFLEMMIDIRRNVVYSLFQFQPQGQPQAV", "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": "MPPSSLAEYLAKKYLTADPATDRPKKKRKKTKTVDTAGDGLIIADDDPPDLRTSATNFDNEDDEGPSLVTSVRSAEFRRAKKSNWRTVGGPATGSSNANDERDAADAILASAAAESAARRGEGEGGDDEAPAVVDEADADDGGELRMESGARAGLQTAEQTAAMVAAQERRKKAEAARHRERPAEAQETIYRDASGRIINVALKRAEARRAEQEKREKEEAAKEALMGDVQRAEREARRQQIQEARAMPLARTIEDDALNEELKAQQRWNDPAAGFLTKTKGPGVSVTGKPLYKGAFQPNRYGIRPGHRWDGVDRGNGFEKEWFAARNKKGRLEALDYQWQMDE", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CWC26 family."}
+{"protein": "MKEPKSNIRKLIDIGGLIGR", "text": "FUNCTION: Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI. Also positively regulates tra gene expression (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TraY family."}
+{"protein": "MCETYSRWLLRVSVAQICQALGWDSVQVSACDLLTDVLQRYLQGLGRGCHRYCELYGRTDPILDDVGDAFKLMGVNLHELEDYIHNIEPVTFAHQIPSFPVSKNNVLQFPQPGSKDAEERKEYIPDYMPPIVSSQEEEEEEQVPTDGGTSAEAMQVPLEEEGDMEEDEAINDENYLSKRPLESPDAEEFPPMKRPKLSVSKGDALDGALEPREPLSSINTQKVPPMLSPVHVQDSTDLAPPSPEPPMLAPIAKSQVPTPKTLESKPPAPKTKSKTSSPGQKTKSPKTTPSPVVAGSPIRSPKTGSKEKKSPGRAKSPKSPKSPKAPVHVPPPPVKPETPSRTPLAALSDKIGKENIQVKQGQTPPEPVTKPNIENQTKKLPVVDKTIDDSIDAVIARACAEREPDPFEFSSGSESEGEIFTSPKRLSVSETTATTPKPSVSTNCSNKAGATPVPPSGGTSSSDISWTMDDSIDEVIRKANMGTPSNPPANFTYFSSPSASPPTPEPLLKVYEEKTKLASSVEVKKKLKKELKTKMKKKEKQKEKDKEKSKEKNKEKEKNKEKDKDKEGNKEAKFQWKELLKDDEHDPYKFKLKDFEDADTKVKLKDGNTKKEKEKHKDKKKEKEKGKKDKDKKDKEKVKDKSKEDKIKPPSAPLVLPPKEMSLPLFSTPTAMRLPSMLPSLSPMLPEKLFEDKEKPKEKKKDKKEKKKKKEREKDKEKEKKDKEKERKEREKKEKEKEKHKHEKIKVEPVVPAPSPVIPRLTLRVGAGQDKIVISKVVPAPEAKPATPVSRPKTPPPVPSPVPAPVHVTPPPAPVPAPPQPTVSPALLPPASPAVSAAGGSKAPVRSVVTETVSTYVIRDEWGNQIWFCPGCNKPDDGSPMIGCDDCDDWYHWPCVGITAAPPEEMQWFCSKCANKKKDKKHKKRKHRAH", "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. The TFIID complex structure can be divided into 3 modules TFIID- A, TFIID-B, and TFIID-C. TAF3 forms the TFIID-A module together with TAF5 and TBP. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The TAF3-TBPL2 complex replaces TFIID at specific promoters at an early stage in the differentiation process. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF3 family."}
+{"protein": "MAPPQQARVLRCCCCSLFQAHQVKKSLKWTCKACGKKQSFLQAYGEGSGADCRRHVQKLNLLQGQISEMSLRSLGESISANEEENVGPWQAARASPQETLQPSKNRWLKYLERDSKELGLKGGGVCFNSQPSSETEKPDPPFSTGLPRKRKWNQSTVQPLCGPHVQDSRNCEVTLKSLKARPLHPTWGARSSPDCSTWDLPCISEELPPSFTQDRAGLAGKGRESSREDLDTMELVPRGEPPCPAQQVRTMSKWEQCLGNSSHLDTEPLTPLQRGLRPIQAAQAEQGAPRAQTPREGGLCRLPGARQSPQTTHTPMPGPKWLCGRIPEQSQGTGPWAEGVPLVKGMQARSSLMRLCDLFKTGEDFDDDL", "text": "FUNCTION: Plays a role in the cellular response to DNA damage and the maintenance of genome stability through its association with the MRN damage-sensing complex. Promotes chromatin loading and activity of the MRN complex to facilitate subsequent ATM-mediated DNA damage response signaling and DNA repair. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Note=Recruited to sites of DNA damage. Phosphorylation on Ser-115 induces its nuclear localization and promotes genome stability. SIMILARITY: Belongs to the MRNIP family."}
+{"protein": "MSFRINTNIAALTSHAVGVQNNRDLSSSLEKLSSGLRINKAADDSSGMAIADSLRSQSANLGQAIRNANDAIGMVQTADKAMDEQIKILDTIKTKAVQAAQDGQTLESRRALQSDIQRLLEELDNIANTTSFNGQQMLSGSFSNKEFQIGAYSNTTVKASIGSTSSDKIGHVRMETSSFSGEGMLASAAAQNLTEVGLNFKQVNGVNDYKIETVRISTSAGTGIGALSEIINRFSNTLGVRASYNVMATGGTPVQSGTVRELTINGVEIGTVNDVHKNDADGRLTNAINSVKDRTGVEASLDIQGRINLHSIDGRAISVHAASASGQVFGGGNFAGISGTQHAVIGRLTLTRTDARDIIVSGVNFSHVGFHSAQGVAEYTVNLRAVRGIFDANVASAAGANANGAQAETNSQGIGAGVTSLKGAMIVMDMADSARTQLDKIRSDMGSVQMELVTTINNISVTQVNVKAAESQIRDVDFAEESANFSKYNILAQSGSFAMAQANAVQQNVLRLLQ", "text": "FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Important for motility and virulence. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the bacterial flagellin family."}
+{"protein": "MWRLMTAKGGNDPYLYSTNNFIGRQTWEFDPDYGTPAERAEVEEARLHFWNNRYQVKPSSDVLWRMQFLKEKNFKQIIPQVKVEDGEEITYEAATTTLRRAVHYFSALQADDGHWPAENAGPLFFLPPLVMCLYITGHLNTVFPAEHRIEILRYIYCHQNDDGGWGLHIEGHSTMFCTALSYICMRILGEGRDGGENNACARARKWILDHGSVTAIPSWGKTWLSILGLFDWSGSNPMPPEFWILPPFLPMHPAKMWCYCRMVYMPMSYLYGKRFVGPITPLILQLREELYAQAYDEINWRKVRHNCAKEDLYYPHPLIQDLMWDSLYIFTEPFLTRWPFNKLREKALQTTMKHIHYEDENSRYITIGCVEKVLCMLACWVEDPNGDYFKQHLARIPDYIWVAEDGMKMQSFGSQEWDTGFAIQALLASDLIDEIRPTLMKGHDFIKKSQVKENPSGDFKSMHRHISKGSWTFSDQDHGWQVSDCTAEALKCCLLFSRMPTEIVGDKMEDNQLFDAVNMLLSLQSKNGGLAAWEPAGSSEWLELLNPTEFFEDIVIEHEYVECTSSAIQAMVMFKKLYPGHRKKEIEVSITNAVQYLEDIQMPDGSWYGNWGVCFTYGTWFAMGGLTAAGKTYNNCQTLHKAVDFLIKSQRSDGGWGESYLSCPNKEYTPLEGNRSNLVHTSWAMMGLIHSRQAERDPTPLHRAAKLLINSQMESGDFPQQEITGVFMKNCMLHYAASRNIYPLWALAEYRKNVRLPSKSV", "text": "FUNCTION: Component of the oleanane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway (PubMed:29378087). Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. SIMILARITY: Belongs to the terpene cyclase/mutase family."}
+{"protein": "MPVLFSSRSLILSIIVPLLISIALYKLDTFDPAIVPSDAFTSSATSLPPLINDEFLTGAEFIGVGLLNIPEDIAYHKESNLIYTGCVDGWVKRVKVADSVNDSVVEDWVNTGGRPLGIAFGIHGEVIVADVHKGLLNISGDGKKTELLTDEADGVKFKLTDAVTVADNGVLYFTDASYKYTLNQLSLDMLEGKPFGRLLSFDPTTRVTKVLLKDLYFANGITISPDQTHLIFCETPMKRCSKYYISEERVEVFTQSLPGYPDNIRYDGDGHYWIALPSGVTTLWNISLKYPFLRKLTAMVAKYGVDLMFMENAGVLQVDLDGNPIAYYHDPKLSHIATCDKIGKYLYCGSLSQSHILRLDLLKYPAQNKKL", "text": "SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the strictosidine synthase family."}
+{"protein": "MITLKQALSLSQDELETLKNEIDAKVRASDLNAYIKAPSLNGASAKGVPILIKDNISVKGWEITCSSKILEGYVAPYHASAIENLHQNGMAGFGLSNMDEFAMGSTTESSCYGITKNPRDKNIVPGGSSGGSAAAVAGGLTVAALGSDTGGSIRQPASYCGCVGLKPTYGRVSRYGVIAYRSSFDQIRPITQNVEDASILFDAISGYDSKDSTSANLKPTHTFINLIRDKRFKIAILRDHINDASNEVQLAYENTIKALKEMGHEVVEKKMLDSHYQISIYYIISMAEASSNLARFDGVRYGRRAQNVKDLKELYLKSRSEGFGDEVKRRIMLGNFVLSSGYYDAYYLKAQQMRLMIKEQYNKIFEEVDLIFTPVAPTTAYLFNYHASPLEMYLSDIYTIGANLSGLPALSLPVAKDPLGLPIGMQFIAKAFDEQSLLDVSYALEQELDLKLD", "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) (By similarity). SIMILARITY: Belongs to the amidase family. GatA subfamily."}
+{"protein": "MEQAVHGESKRGQVTGTHLTNDISKAKKCTVIGGSGFLGQHMVEQLLERGYTVNVFDIHQGFDNPRVQFFIGDLCNQQDLYPALKGVSTVFHCASPPPYSNNKELFYRVNFIGTKTVIETCREAGVQKLILTSSASVVFEGVDIKNGTEDLPYAMKPIDYYTETKILQERAVLDANDPKKNFLTAAIRPHGIFGPRDPQLVPILIDAARKGKMKFMIGNGENLVDFTFVENVVHGHILAAEHLSQDAALGGKAFHITNDEPIPFWTFLSRILTGLNYEAPKYHIPYWMAYYLAFLLSLLVMVVSPLIQIQPTFTPIRVALAGTFHYYSCEKAKKLFGYRPLVTMDEAVERTVQSFHHLRKDK", "text": "FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidative decarboxylation of the C4 methyl groups of 4-alpha-carboxysterols in post-squalene cholesterol biosynthesis (PubMed:10369263, PubMed:14567972). Plays a role in the regulation of the endocytic trafficking of EGFR (PubMed:23125191). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Lipid droplet Note=Trafficking through the Golgi is necessary for ER membrane localization. SIMILARITY: Belongs to the 3-beta-HSD family."}
+{"protein": "MEKYERIRVVGRGAFGIVHLCLRKADQKLVIIKQIPVEQMTKEERQAAQNECQVLKLLNHPNVIEYYENFLEDKALMIAMEYAPGGTLAEFIQKRCNSLLEEETILHFFVQILLALHHVHTHLILHRDLKTQNILLDKHRMVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLVLSLLSLEPAQRPPLSHIMAQPLCIRALLNLHTDVGSVRMRRAEKSVAPSNTGSRTTSVRCRGIPRGPVRPAIPPPLSSVYAWGGGLGTPLRLPMLNTEVVQVAAGRTQKAGVTRSGRLILWEAPPLGAGGGSLLPGAVEQPQPQFISRFLEGQSGVTIKHVACGDFFTACLTDRGIIMTFGSGSNGCLGHGSLTDISQPTIVEALLGYEMVQVACGASHVLALSTERELFAWGRGDSGRLGLGTRESHSCPQQVPMPPGQEAQRVVCGIDSSMILTVPGQALACGSNRFNKLGLDHLSLGEEPVPHQQVEEALSFTLLGSAPLDQEPLLSIDLGTAHSAAVTASGDCYTFGSNQHGQLGTNTRRGSRAPCKVQGLEGIKMAMVACGDAFTVAIGAESEVYSWGKGARGRLGRRDEDAGLPRPVQLDETHPYTVTSVSCCHGNTLLAVRSVTDEPVPP", "text": "FUNCTION: Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia (By similarity). Plays a role in organogenesis and is involved in the regulation of the Hippo signaling pathway. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cell projection, cilium Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Predominantly cytoplasmic. Localizes to the proximal region of the primary cilium and is not observed in dividing cells. SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily."}
+{"protein": "MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASEEVSRRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMKNRPMILIELFLMFPNSPPANPSIFSWDPLHVQGLRPRMSFSSQVATLWKGCRVPQTPPLAQQRLGSGSFQRHYTSRADSDANSKCLSPGSWASAAPSGPQLTSEQLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHRA", "text": "FUNCTION: Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). MOCS1A catalyzes the cyclization of GTP to (8S)- 3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and MOCS1B catalyzes the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'- triphosphate to cPMP. SIMILARITY: In the C-terminal section; belongs to the MoaC family. SIMILARITY: In the N-terminal section; belongs to the radical SAM superfamily. MoaA family."}
+{"protein": "MGAIISRWKTKPSTVELLESLDKDIKDLEEFRAKNQRLLKLWVGRLLFYSSALYLLTCLCVYYLYFPQQWGARLITALPLLAFPALVLLLRKMLIFLFSKRTERNNDKLEDLKTQKRKILEEVMETETYKNAKLILERFDPESKKKAEAEATPVRPHMTPRPGQELRQRHIAMATPGPVLGPMSPGTTPLRTAPGGPPEKGLAGSASTPAGASQAETPQQMMRRSMNPYSPGPGSGMRPPGPPLARPILPRERGAVDRVIEYLVGDGPQNRYALICQQCFSHNGMALKEEFEFVAFRCAYCYFMNPARKTRPQAPRLPEFSFERRLRSESPETQSSAATETPEDSDAPEDDMERTTSADPQNPAADEAPVLQESETEESQPQDVPHAEAEALEEQKKEDESN", "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": "MSAQSLPAATPPTLKPPRIIRPRPPSRHRAPHSPGPLHNGSSPKALPQISNDASASVCTSIFWEPPTASLKPPALLPPSVSRTSLDSQTSPDSPSSTPSPSPVSRRSISPEPAPCSPVPPPKPSGSSRTPLPSGPTPLQDGSASAPGTVRRLAGKFEWGAEGKAQSSDSLERCSQGSTEVNGEKETPEAALSGNGSQENGTPDAALACPPCCPCVCHVAKPGLELRWVPVGSSEDILRIPCRASPLRASRSRINPPVISHPPVVLTSYRSTAERKLLPPLKPPKPTKVRQDISTSEELPQPDLKLPSEDGIQTATKAWEGDRPEGAPLNAPPVALEGREEEGLDGLKGLQWELPLQDEPLYQTYRAAVLSEELWGVGEDGGPSPANPGEAPTFSRLPGPRNTLWQELPAVRGSGLLESLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHITDLCDVVHAHAVGPFFVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRFHKVKALPLVSWSRRLELQGELTELGCRRGGVLFTSRPRFTPLCLLLFSDLLLITQPKSGQRLQVLDYAHRSLVQAQQVPDPSGPPTFRLSLLSNHQGRPTHRLLQAASLSDMQRWLGAFPTPGPLPCSPDTIYEDCECSQELCSEPSTPSKTEGQSLESKAPRKHLHKNPEGWLKGLPGAFPAQLVCEVTGEHERRKHLRQHQKLLEAVGPSSGTPDTPQP", "text": "FUNCTION: Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse- promoting activity of EPHB2. SUBCELLULAR LOCATION: Cell projection, dendrite Note=Expressed exclusively in dendrites of the developing hippocampus."}
+{"protein": "MDEFDRRLLNRLQHGLPLEPHPYALLAAELDCREEDILRRLDDLLDDGTLTRFGPLFDIEPLGGAFTLAAMSVPEARFEEIAALLAGWPQVAHNYRREHALNMWLVVACDSPAEVAETLARLERESGLAVLDLPKEATYHVGLHFPL", "text": "FUNCTION: Involved in heme d1 biosynthesis (PubMed:8982003). Catalyzes the decarboxylation of siroheme into didecarboxysiroheme (By similarity). SIMILARITY: Belongs to the Ahb/Nir family."}
+{"protein": "MKLLSVAAVALLAAQAAGASIKHRLNGFTILEHPDPAKRDLLQDIVTWDDKSLFINGERIMLFSGEVHPFRLPVPSLWLDIFHKIRALGFNCVSFYIDWALLEGKPGDYRAEGIFALEPFFDAAKEAGIYLIARPGSYINAEVSGGGFPGWLQRVNGTLRSSDEPFLKATDNYIANAAAAVAKAQITNGGPVILYQPENEYSGGCCGVKYPDADYMQYVMDQARKADIVVPFISNDASPSGHNAPGSGTGAVDIYGHDSYPLGFDCANPSVWPEGKLPDNFRTLHLEQSPSTPYSLLEFQAGAFDPWGGPGFEKCYALVNHEFSRVFYRNDLSFGVSTFNLYMTFGGTNWGNLGHPGGYTSYDYGSPITETRNVTREKYSDIKLLANFVKASPSYLTATPRNLTTGVYTDTSDLAVTPLIGDSPGSFFVVRHTDYSSQESTSYKLKLPTSAGNLTIPQLEGTLSLNGRDSKIHVVDYNVSGTNIIYSTAEVFTWKKFDGNKVLVLYGGPKEHHELAIASKSNVTIIEGSDSGIVSTRKGSSVIIGWDVSSTRRIVQVGDLRVFLLDRNSAYNYWVPELPTEGTSPGFSTSKTTASSIIVKAGYLLRGAHLDGADLHLTADFNATTPIEVIGAPTGAKNLFVNGEKASHTVDKNGIWSSEVKYAAPEIKLPGLKDLDWKYLDTLPEIKSSYDDSAWVSADLPKTKNTHRPLDTPTSLYSSDYGFHTGYLIYRGHFVANGKESEFFIRTQGGSAFGSSVWLNETYLGSWTGADYAMDGNSTYKLSQLESGKNYVITVVIDNLGLDENWTVGEETMKNPRGILSYKLSGQDASAITWKLTGNLGGEDYQDKVRGPLNEGGLYAERQGFHQPQPPSESWESGSPLEGLSKPGIGFYTAQFDLDLPKGWDVPLYFNFGNNTQAARAQLYVNGYQYGKFTGNVGPQTSFPVPEGILNYRGTNYVALSLWALESDGAKLGSFELSYTTPVLTGYGNVESPEQPKYEQRKGAY", "text": "FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
+{"protein": "MLATAGSLIATIWAALHLRTLLVAALTFLLLADYFKTRRPKNYPPGPWGLPFVGNIFQLDFGQPHLSIQPFVKKYGNIFSLNLGDITSVVITGLPLIKETFTHIEQNILNRPLSVMQERITNKNGLIFSSGQTWKEQRRFALMTLRNFGLGKKSLEQRMQEEAHYLVEAIREEKGKPFNPHFSINNAVSNIICSVTFGERFEYHDSRFQEMLRLLDEVMYLETTMISQLYNIFPWIMKYIPGSHQTVFRNWEKLKLFVSSMIDDHRKDWNPEEPRDFIDAFLKEMSKYPEKTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEVQEKVQAEIDRVIGQKRAASLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAMDTTLNGFHLPKGTMVLTNLTALHRDPKEWATPDVFNPEHFLENGQFKKRESFLPFSMGKRACLGEQLARSELFIFFTSLMQKFTFKPPTNEKLSLKFRNGLTLSPVTHRICAVPRE", "text": "FUNCTION: A cytochrome P450 monooxygenase that may play a major role in intestinal retinoid metabolism. Catalyzes the oxidative transformation of all-trans retinal and 9-cis-retinal to the corresponding active forms all-trans and 9-cis retinoic acids (PubMed:9606960). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates arachidonic acid predominantly at the omega-1 position (PubMed:9143331). 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-- hemoprotein reductase) (PubMed:9143331, PubMed:9606960). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Microsome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MAPEQWEATSQVSLTFEDVAVLFTRDEWKKLVPSQRSLYREVMLENYSNLASLGFPFTKPKVISLLQQGEDPWKVEEEGPGGFSLGLKCSQRTTKSTQTQDSSFRELIMRKSKRKEPWNMKSENLSIHEGKLEEKWDVNASTIERSYKSNELSPKSHREKRSSECEKQISYLSNPLGITPDKRYKCSMCEKTFINTSSLRKHEKNHSGEKLFKCKECSKAFSQSSALIQHQITHTGEKPYVCKECGKAFTLSTSLYKHLRTHTVEKSYRCKECGKSFGRRSGLFIHQKVHAGENPYKYNPGRKASTSLSGCQRIHSRKKTYLCNECGNTFKSSSSLRYHQRIHTGEKPFKCSECGRAFSQSASLIQHERIHTGEKPYRCSECGKGFTSISRLNRHRIIHTGEKFYNCNECGKALSSHSTLIIHERIHTGEKPCKCKVCGKAFRQSSALIQHQRMHTGERPYKCNECGKTFRCNSSLSNHQRTHTGEKPYRCQECGMSFGQSSALIQHRRIHTGEKPFKCNTCGKTFRQSSSRIAHQRIHTGEKPYECNTCGKLFNHRSSLTNHYKIHVDEDP", "text": "FUNCTION: It may play a role in renal development and may also be involved in the repair of the kidney after ischemia-reperfusion or folic acid administration. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MSDDGEQPGPGDGAARDELSGMDLVRRTLAEARAAARARGQDPGRGFAAGPAPRRVAGRRRSWSGPGPDTRDPQPLGKLTRDLAKKRGWSGHVAEGTVLGQWSRVVGAQIADHATPTALNEGVLSVTAESTAWATQLRIMQSQLLAKIAAAVGNGVVTSLKITGPASPSWRKGPRHIAGRGPRDTYG", "text": "SIMILARITY: Belongs to the UPF0232 family."}
+{"protein": "MASLSETLRSHWPIALFGVILFVAGGTELYWNEGRAVHNMMALDEAHADIYSVRFTEEEQEVGLEGRIVHLSGPILVGEPLTEPDYNIQLLAVKLRRRVQMYQWVEEAVEHNYGDSVGTTHSDSRTYYYTREWRDKIVDSRNFYNRHGHTNPSHFPIESHVQVADAVFIGRYELGAEVKEKFNNYQELTSDIRPEDSGVKLHLGIYYHTNDVFNPEVGDLRLLFSFAGMEGEVFSVVGKLSGNKLVPYITSRGVPVLLVYPGGLSVQEVFRLEARAQVLHTWWWRFVGWLLIFFGVTCNTKILRLLFVRVPLLVALAPDPQFPVTGNLLIAFSLALTIAAVAWILHRPVIGACLLLAGASPYVWFTRNLVDYHRLD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM43 family."}
+{"protein": "MNWAPATCWALLLAAAFLCDSGAAKGGRGGARGSARGGVRGGARGASRVRVRPAQRYGAPGSSLRVAAAGAAAGAAAGAAAGLAAGSGWRRAAGPGERGLEDEEDGVPGGNGTGPGIYSYRAWTSGAGPTRGPRLCLVLGGALGALGLLRP", "text": "FUNCTION: Prion-like protein that has PrP(C)-like neuroprotective activity. May act as a modulator for the biological actions of normal and abnormal PrP (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the SPRN family."}
+{"protein": "MARRPDEEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFCLESKSTIGVEFATRTLQVEGRTVKAQIWDTAGQERYRAITSAYYRGALGALLVYDVTKPTTFENVSRWLKELRDHADSNIVIMLIGNKTDLKHLRAVATEDAQSYAEKEGLSFIETSALEALNVEKAFQTILSEVYRIISKKSISSDQTTANANIKEGQTIDVAATSESNAKKPCCSSS", "text": "FUNCTION: Intracellular vesicle trafficking and protein transport. SUBCELLULAR LOCATION: Endosome membrane Golgi apparatus, trans-Golgi network membrane; Lipid-anchor Note=During cytokinesis located to the growing margins of the cell plate. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MKYSVRILDIATRSGILLNYLDARNIGVLDGDRVQLINPKNSLAVTAVVTTTSTLEGQGTAGVYRGTNRRLNLTEGEEIEIREADRPASLDFIKKKMDGGRLTKEETLTIIKDVVNDEISAAELTAFITASYINPLDMEEVEHLTRAMVETGERIKFASRPIVDKHSIGGVPGNKISLLVVPIIAASGLKIPKTSSRAITGAGGTADLMEVLANVEFSAREVQEMTEKVGGTIVWGGATNIAPADDRIILQEYPFKIDARGQMLASVMAKKYAVGANLVVIDIPVGSHTKVPTVQEGRKLAREFIELGERLGMKVECALTYGDIPVGYSIGPNLEVREALRVLEGATEPNSFIQKSVSLAGIALEMSGKAARGTGAQMAQDILSSGKALEKFRQIIEIQGGDPKVKSEDILPGEHQFVVNAPASGYIVEMNNVSLITLARLAGAPHDRGAGILLHAKKGTLIKAGEPLFTIYAEREWRLQKAVEEGRHLVPVLVEGMLLDRVPSQSEV", "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": "MSTNLEEKQRRFSKLQKTLGVVFPAAILLSTGYTVWVFIALICVDSNIKIRNGYRNLGGGIVLIIFFFITSGLAYFSYFRVLFSSPSFCGNTLYTYYGFDNPIFLCGPNGAPRMCGTCKCWLPDRSHHSRVSMRCIRKFDHYCSFVGKDVCFSNQKFFYQFLFYGFSAACMVLISTAIMISRTYHYRSLPGTWIFVLVFSAFGVLFLGVMLVRHTGYLLLNINSHEAKNWKTRIYSFSVFFPEHMDSRVLVQSDPGDLPWDRGYSENWRAVMGDHWYNWILPLRRSPGDGEHFLYSPSFVSKMQSKALSMNS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA5 subfamily."}
+{"protein": "MEAVAKFDFTASGEDELSFHTGDVLKILSNQEEWFKAELGSQEGYVPKNFIDIQFPKWFHEGLSRHQAENLLMGKEVGFFIIRASQSSPGDFSISVRHEDDVQHFKVMRDNKGNYFLWTEKFPSLNKLVDYYRTNSISRQKQIFLRDRTREDQGHRGNSLDRRSQGGPHLSGAVGEEIRPSMNRKLSDHPPTLPLQQHQHQPQPPQYAPAPQQLQQPPQQRYLQHHHFHQERRGGSLDINDGHCGTGLGSEMNAALMHRRHTDPVQLQAAGRVRWARALYDFEALEDDELGFHSGEVVEVLDSSNPSWWTGRLHNKLGLFPANYVAPMTR", "text": "FUNCTION: Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc. SUBCELLULAR LOCATION: Nucleus Cytoplasm Endosome. SIMILARITY: Belongs to the GRB2/sem-5/DRK family."}
+{"protein": "MLNLFAAFKKDRIWDFDGGIHPPEMKTQSSGVPLRTAPLPDKFIIPLQQHLGPEGELCVKVGDTVLKGQPLTVGRGRTVPVHAPTSGTISAITPHITAHPSGLAELCVIIQPDGEDRWCERAPVADYRQLTASELIQRIHQAGIAGLGGAGFPTASKLQGGMNGVETLILNAAECEPYITADDRLMQEHADQVIEGTQILRHLLQPKVTLIGIEDNKPEAIAALKLALRGQPGIALRVIPTKYPSGGAKQLTKILIGKEVPHGKHSSAIGVLMQNVGTAFAIKRAIVDGEPLIERVVTLTGEALSLPGNLWARIGTPVQHLLKFAGFQPQAQQMVVMGGPLMGFTLPALHVPIVKISNCILAPSVSEMAPQEQEQSCIRCGLCVDACPAGLLPQQLYWFSRGEEHEKARNHNLFDCIECGACAFVCPSNIPLVQYYRQEKAEIKAIDLEAARTAEAKARYEAKLARLEREKLAREERHKKAAVKLTDGDQDAVQAALARVRSKNAVPATGTISGDAPDNSEMNAAREARKAQARERRAQQETPVAPVTASASEDEDPRKAAVAAALARVKAKKAAPQATAVETPAESPAVVTEEDPRKAAVAAALARVKAKKAAQQATAVETPAESPAVVTEEDPRKAAVAAALARVKAKKAAQQATAVETPAESPAVVTEEDPRKAAVAAAIARAKAKRAAQSLTTADTDKE", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily."}
+{"protein": "MSSCGVLVVAGTHGNEVNAPWLLQQWQANPDLIDAAGLAVQKVIGNPEALRRRCRYVDRDLNRCFLPEQLEQGASGLEFQRAGELLRLHGPSGEQPCAVAIDLHSTTAAMGNSLVVYGRRPADLALAALVQGALGLPIYLHEADAQQTGFLVESWPCGLVIEVGPVPQGLLNAGVVEQTRLGLESCLRALYQVRQELARLPDALVVHRHLGSRDLPKAENGEPQALVHPELQGRDWQNIASTQAMFRAADGTDRCEAWVGGEIPVFVNEAAYAEKSIAFSLTRREVWPVEPNWLLALKQLLAAA", "text": "SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily."}
+{"protein": "MKTNIINTWHSFVNIPNVVVPAIEKEIRRMENGACSSFSDNDNGSLSEESENEDSLFRSNSYRRRGPSQREHYLPGTMALFNVNNSSNKDQDPKEKKKKKKEKKSKADDKKESKKDPEKKKKKEKEKEKKKEEKPKEKKEEEKKEVVVIDPSGNMYYNWLFCITLPVMYNWTMIIARACFDELQSDYLEYWLIFDYVSDVVYLADMFVRTRTGYLEQGLLVKDELKLIEKYKANLQFKLDVLSVIPTDLLYFKFGWNYPEIRLNRLLRISRMFEFFQRTETRTNYPNIFRISNLVMYIVIIIHWNACVYYSISKAIGFGNDTWVYPDVNDPEFGRLARKYVYSLYWSTLTLTTIGETPPPVLDSEYVFVVVDFLIGVLIFATIVGNIGSMISNMNAARAEFQSRVDAIKQYMNFRNVSKDMEKRVIKWFDYLWTNKKTVDEREVLRYLPDKLRAEIAINVHLDTLKKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGITQFVVLSDGSYFGEISILNIKGSKAGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKTMLEEKGRQILMKDGLLDINIANLGSDPKDLEEKVTRMEGSVDLLQTRFARILAEYESMQQKLKQRLTKVEKFLKPLIETEFSALEEPGGESEPTESLQG", "text": "FUNCTION: Subunit of the rod cyclic GMP-gated cation channel, which is involved in the final stage of the phototransduction pathway. When light hits rod photoreceptors, cGMP concentrations decrease causing rapid closure of CNGA1/CNGB1 channels and, therefore, hyperpolarization of the membrane potential. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGA1 subfamily."}
+{"protein": "MFIINWFYDALAMLGLVNKHAKMLFLGLDNAGKTTLLHMLKNDRLAVMQPTLHPTSEELAIGNVRFTTFDLGGHQQARRLWRDYFPEVNGIVYLVDCCDFERLSESKAELDALLAMEELARVPFLILGNKIDAPGAISEDELKAALGLYQTTGKGVSKPVPGIRPIEVFMCSVVLRQGYGEGFKWLAQYV", "text": "FUNCTION: Small GTPase 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. Sar1 controls the coat assembly in a stepwise manner. Activated sar1-GTP binds to membranes first and recruits the SEC23/24 complex. These sec23/24-sar1 prebudding intermediates are then collected by the sec13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to sar1-GDP triggers coat release and recycles COPII subunits (By similarity). SUBCELLULAR LOCATION: 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 small GTPase superfamily. SAR1 family."}
+{"protein": "MSAQSLLHSVFSCSSPASSSAASAKGFSKRKLRQTRSLDPALIGGCGSDEAGAEGSARGATAGRLYSPSLPAESLGPRLASSSRGPPPRATRLPPPGPLCSSFSTPSTPQEKSPSGSFHFDYEVPLGRGGLKKSMAWDLPSVLAGPASSRSASSILCSSGGGPNGIFASPRRWLQQRKFQSPPDSRGHPYVVWKSEGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLSCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQRDEQKDASDFVASLLPFGNKRQNKELSSSNSSLSSTSETPNESTSPNTPEPAPRARRRGAMSVDSITDLDDNQSRLLEALQLSLPAEAQSKKEKARDKKLSLNPIYRQVPRLVDSCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVSLEEEHSVHDVAALLKEFLRDMPDPLLTRELYTAFINTLLLEPEEQLGTLQLLIYLLPPCNCDTLHRLLQFLSIVARHADDNISKDGQEVTGNKMTSLNLATIFGPNLLHKQKSSDKEFSVQSSARAEESTAIIAVVQKMIENYEALFMVPPDLQNEVLISLLETDPDVVDYLLRRKASQSSSPDMLQSEVSFSVGGRHSSTDSNKASSGDISPYDNNSPVLSERSLLAMQEDAAPGGSEKLYRVPGQFMLVGHLSSSKSRESSPGPRLGKDLSEEPFDIWGTWHSTLKSGSKDPGMTGSSGDIFESSSLRAGPCSLSQGNLSPNWPRWQGSPAELDSDTQGARRTQAAAPATEGRAHPAVSRACSTPHVQVAGKAERPTARSEQYLTLSGAHDLSESELDVAGLQSRATPQCQRPHGSGRDDKRPPPPYPGPGKPAAAAAWIQGPPEGVETPTDQGGQAAEREQQVTQKKLSSANSLPAGEQDSPRLGDAGWLDWQRERWQIWELLSTDNPDALPETLV", "text": "FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MSVASAVLRVETWLLATWHVKVPPMWLEACVNWIQEENNNATLSQAQINKQVLEQWLLTDLRDLEHPLLPDDILELPKGELNGFYALQINSLVDVSQPAYSQIQKLRGKNTTNDLVSAETQSTPKPWEVRPSRMLMLQLTDGVTHIQGMEYQSIPALHSGLPPGTKILVRGCILFRLGVLLLKPENVKVLGGEVDGLSEENAQEKVLARLIGELDPTVPVIPNNSIHNVPKVSGGLDAVLGPSDEELLASLDESEESAANNDVAMERSCFSTGTSSNTTPTNPSGFEPGCNISSRPKEKPPNQPTHFTDGEFDDFSLEEALLLEETVQKEQMETKASQPLTLKENTGKCMEIFSHKPSSLNHTALIHKQGNSNFDEKTSEQMIHEDKFFDCASTRNHHKRFSAHDFTNDSKISEVDDAAQQTLSSSNVHCLRNKILNRKLDLSEKSSQISKENGHPFQACSSRSFENNTYLSIGMDLHSPPFIYLSVLMARKPKEVTTVTVKAFIVTLTGNLSSSGGFWGVTAKVSDGTAYLDVDFIDEILTSMIGYSVPEMKQLRKDPLKYKTFLEGLQKCQRDLIDLCCLMTISYDPSSCKGVVLELQDVGMEHVENLKKRLNK", "text": "FUNCTION: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A- mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Forms foci in response to DNA damage. SIMILARITY: Belongs to the RMI1 family."}
+{"protein": "MEQQNKRGLKRKALLGGVLGLGGLAMAGCEVAPPGGVLGDFLRMGWPDGITPEAVAMGNFWSWVWVAAWIIGIIMWGLFLTAIFAWGAKRAEKRGEGEFPKQLQYNVPLELVLTIVPIIIVMVLFFFTVQTQDKVTALDKNPEVTVDVTAYQWNWKFGYSEIDGSLAPGGQDYQGSDPERQAAAEASKKDPSGDNPIHGNSKSDVSYLEFNRIETLGTTDEIPVMVLPVNTPIEFNLASADVAHSFWVPEFLFKRDAYAHPEANKSQRVFQIEEITEEGAFVGRCAEMCGTYHAMMNFELRVVDRDSFAEYISFRDSNPDATNAQALEHIGQAPYATSTSPFVSDRTATRDGENTQSNA", "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) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
+{"protein": "MPTKAGTKSTANKKTTKGSSKSGSSRGHTGKTHASSSMHSGMLYKDMVNIARSRGIPIYQNGSRLTKSELEKKIKRSK", "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": "MSYPAFDSKTFLEAHIEKTMAFYFPTCIDPEGGFFQFFKDDGSVYDPNTRHLVSSTRFIFNFAQAYLHTNIAEYKHAAVHGIQYLRQRHQSQSGGYVWLLDGGTNLDETNHCYGLAFVILAYSNALQIGLSEAEVWIEVTYDLLETHFWENKHGLYLDEISSDWKTVSPYRGQNANMHMCEALMSAFDATQNPKYLDRAKLLAKNICQKQASLSNSNEVWEHYTNDWQIDWDYNKNDPKHLFRPWGFQPGHQTEWAKLLLMLDKRSPENWYLPKAKYLFDLAYKKAWDTKKGGLHYGYAPDGTVCDPDKYFWVQAESFAAAWLLYKATKDETYYKQYLTLWEFSWNHMIDHTFGAWYRILDENNAQYDNNKSPAGKTDYHTMGACYEVLKTLTL", "text": "FUNCTION: Catalyzes the reversible isomerization of D-mannose to D- fructose. Can also isomerize D-lyxose, with lower efficiency. In longer reaction with a higher concentration of enzyme, it can isomerize 4-OH D-mannose derivatives (D-talose and 4-O-monosaccharyl-D-mannose). Cannot use D-glucose. SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family."}
+{"protein": "MQSSLPQFTFKWPKGPEAIILTGTFDDWKGTLPMVKDPSGAFEITLPVTFDSPSSKFYFKFIVDGQWLPSKDYKVNIDEGVENNFITEEDVIKQRENGSSTLVPESAGLAVSKNAPLIEPEAEKRAKKLRKFKIKRVIKTNKQTGERSIFSQEVVELPDSEDETQQVNKTGKNADGLSGTTTIIENNVGVNEEKAIKPYEENHPKVNLVKSEGYVTDGLGKTQSSESRLYELSAEDLEKEEEEEDEDKGGGKDTSTSADAEASEDQNKEPLSKSAKFEKPEEKVPVSSITSHAKETSVKPTGKVATETQTYETKQGAPTAAAKKIEAKKATRPSKPKGTKETPNKGVQKNPAKNGGFFKKLAQLLK", "text": "FUNCTION: Involved in G-protein mediated signal transduction and in the regulation of polarized cell growth in pheromone-induced cells. FUNCTION: Involved in G-protein mediated signal transduction and in the regulation of polarized cell growth in pheromone-induced cells. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CRP1/MDG1 family."}
+{"protein": "MIMGQLMNMRELFNKKKLHALVFSMWCVNLHASSLSDGIAIEPFEINAKSNRFVEFKVYNNTDEDYIVTQKVVSEENSIKKAKIPFVVNPPIRLLRKRSDAAMGIIYLNEGEVFDKKRKYYLSVSFIPKKKDSDDLGFNIIFTQQIAVKLSALN", "text": "FUNCTION: Could be required for the biogenesis of a putative fimbria. SIMILARITY: Belongs to the periplasmic pilus chaperone family."}
+{"protein": "MAAINVIFISGAIALFALTGSCSESTNPFTNKPYATQNPYSPPQTNQPTKRPYQPGPAPTPAPYIPQKTNPPTKRPLNPTPSPTAKPPSENSESENSEGPVLIEEDHFTVDANFKCGIPPVEPDLKKGKIVGGAEAVPNSWPYAAAFGTYDISGGKLEVSQMCGSTIITPRHALTAAHCFMMDPDIDQTYYIFMGLHDETTYKGVRPNKIVGVRYHPKTNVFTDDPWLVYDFAILTLRKKVIANFAWNYACLPQPKKIPPEGTICWSVGWGVTQNTGGDNVLKQVAIDLVSEKRCKEEYRSTITSKSTICGGTTPGQDTCQGDSGGPLFCKEDGKWYLQGIVSYGPSVCGSGPMAAYAAVAYNLEWLCCYMPNLPSCEDIECDESGEN", "text": "FUNCTION: Trypsin-like protease with a narrow substrate specificity. Preferentially hydrolyzes substrates with Pro in the P2 position and Val in the P3 position. Plays a role in fertilization. SUBCELLULAR LOCATION: Secreted Note=Localized on the sperm head. Released into the surrounding seawater in response to the sperm reaction, a large proportion remains associated with the sperm cell surface. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MADLVDHSPHHATKAAKLASASNVILIDNYDSFTWNIYQYLVLEGATVTVYRNDEVTVEDLVAKKPTQLVISPGPGHPDTDAGISNAVIKHFSGKVPIFGVCMGQQCMITSFGGKVDVTGEILHGKTSELKHDSKGVYQGLPTSLEVTRYHSLAGTHSTIPDCLEVTSRVELGDASGKNIIMGVRHKEFAVEGVQFHPESILTQYGRKMFRNFLELTAGTWDNKQGAAVAAPADKKLSILDKIYAHRKNAVDEQKKIPALRPEALQAAYDLNIAPPQLSFPDRLRQSDYPLSLMAEIKRASPSKGIISANVCAPAQAREYAKAGASVISVLTEPEWFKGTIDDLRAVRQSLEGLPNRPAVLRKEFVFEEYQILEARLAGADTVLLIVKMLDIELLTRLYHYSRSLGMEPLVEVNTPEEMKIAVDLGSEVIGVNNRDLTSFEVDLGTTSRLMDQVPESTIVCALSGISGPQDVEAYKKEGVKAILVGEALMRAPDTSAFVAQLLGGSNQNFAGASPSSPLVKICGTRTEEGALAAIQAGADLIGIIMVQGRSRLVPDDVALGISRVVKSTPRPADTLQQPSSATSLEWFDHSTNILRHPSRALLVGVFMNQPLSYVVSQQQKLGLDVVQLHGSEPLEWSSLIPVPVIRKFAPGDIGIARRAYHTLPLLDSGAGGSGELLEESGVKKVLDSDEGLRVILAGGLNPDNVAGTVKKLGQSGQKVVGLDVSSGVETNGAQDLEKIRAFVKSAKSIRQ", "text": "FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities."}
+{"protein": "MTAELLVNVTPSETRVAYIDGGILQEIHIEREARRGIVGNIYKGRVSRVLPGMQAAFVDIGLDKAAFLHASDIMPHTECVAGDEQKQFTVRDISELVRQGQDLMVQVVKDPLGTKGARLTTDITLPSRYLVFMPGASHVGVSQRIESESERERLKKVVAEYCDEQGGFIIRTAAEGVCEEDLASDAAYLKRVWTKVMERKKRPQTRYQMYGELALAQRVLRDFADAQLDRIRVDSRLTYESLLEFTAEYIPEMTSKLEHYSGHQPIFDLYDVENEIQRALERKVELKSGGYLIIDQTEAMTTVDINTGAFVGHRNLDDTIFNTNIEATQAIARQLRLRNLGGIIIIDFIDMNNEDHRRRVLHSLEQALSKDRVKTSINGFSPLGLVEMTRKRTRESVEHVLCNECPTCHGRGTVKTVETVCYEIMREIVRVHHAYDSDRFLVYASPAVAEALKGEESHALAEVEIFVGKQVKVQVEPLYNQEQFDVVMM", "text": "FUNCTION: Acts in the processing of the 5'-end of precursors of 16S rRNA. Confers adaptive resistance to aminoglycoside antibiotics through modulation of 16S rRNA processing (PubMed:24489121). An endoribonuclease, it prefers 5'-monophosphorylated substrates and cleaves single-stranded sites rich in A and U residues; also contributes to 23S rRNA processing, tRNA processing and mRNA turnover (By similarity). Involved in decay of speF mRNA, has a preference for adenine nucleotides (PubMed:30742606). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily."}
+{"protein": "MSLLTEVETYVLSIVPSGPLKAEIAQRLEDVFAGKNTDLEALMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQRRRFVQNALNGNGDPNNMDRAVKLYRKLKREITFHGAKEIALSYSAGALASCMGLIYNRMGAVTTEVAFGLVCATCEQIADSQHRSHRQMVATTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAEAMEVASQARQMVQAMRAIGTHPSSSAGLKDDLLENLQAYQKRMGVQMQRFK", "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. 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. 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. SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein; Cytoplasmic side Host nucleus. SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family."}
+{"protein": "MNKSGIILIGTILFSSMAIADDLTAPIYTTGPKPVAIGKVTFTQTPYGVLITPDLTNLPEGPHGFHLHKTADCGNHGMHAEGHYDPQNTNSHQGPYGNGHLGDLPVLYVTSNGKAMIPTLAPRLKLSDMHNLAVMIHANGDTYSDNPPQGGGGDRIACGVIK", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
+{"protein": "MLLRSRFLKVIHVRKQLSACSRFAIQTQTRCKSTDASEDEVKHFQELAPTWWDTDGSQRILHKMNLTRLDFVQRTVRNQVKIQNPEIFVPGFNYKEFLPEYVCDNIQREMQESIETNLDKRPEVSVLDVGCGGGILSESLARLKWVKNVQGIDLTRDCIMVAKEHAKKDPMLEGKINYECKALEDVTGQFDIITCMEMLEHVDMPSEILRHCWSRLNPEKGILFLSTINRDLISWFTTIFMGENVLKIVPKGTHHLSKYINSKEILAWFNDNYSGQFRLLDLKGTMYLPYQGWVEHDCSDVGNYFMAIQRLN", "text": "FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. Catalyzes the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate (DHHB) to 3-methoxy-4-hydroxy-5- hexaprenylbenzoate (HMHB) and the methylation of 2-hexaprenyl-3-methyl- 5-hydroxy-6-methoxy-1,4-benzoquinol (3-demethylubiquinol-6) to ubiquinol-6. 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": "MNKRRWIAVGVACGLLLLSIIVALIPGKDKEEASNTTLTGINKIFYGSNEITEETLEEGASNKKIVKLSVNGVIADTGESNLFSREQYNHQNFLTQLKKIQEDKAVKGVLLEVNSPGGGIYESAEIAKEMAKIKKLDIPIYTAFKNTAASGGYYISAGSDKIFATEETTTGSIGVIISGLNYSGLLEKLGVTDATYKSGALKDMMSPQHKPSEEENKVIQEFVMSAYDRFVNVVAKGRNMDTNAVKELADGRIYDGNQAVENGLVDQIGYSEDALDSLKKEKKLTDATVIEYKNDTTGFASSWLGNKIAEWQGLKATTSDRVISVFEKLGFSDTPKPMYYYGGL", "text": "FUNCTION: Digestion of the cleaved signal peptides. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S49 family."}
+{"protein": "MEKILMLNDDQIWIFKKHTNNIQLLIEVALYLKSNKSSVSKKDKDAMYDIFSESELYNPRESLRDKPLDTINHKLDGLSYFMFGYSDRINDENKFIFSPLGNLFLKYLHDKDKLSKIFSCMLISMQFPHPYSKPSECFLLYPFRLIFKLLLDKRLQGRLYHYEVYKIIIHTISIDEAKYEFLVKSILNSRKKSWNEKLNELSEIQHKVVKSVYEWQYYIVPLLGSLHIFKINNGDIEQKLYHPQKDGSKSPPTARKANNGYVEINDNLTNFIDKLLNKYSFLDTPILLSDSQRKSNDVTKEIYSFYPELLLAEIGETISFESHILNIPKLITEYSKNPDNSTSGKFEKILEEAFNLFIDVEAQWLAGAGRTDIECMYLPINEKFSIEAKSTKNKLSMINSGRLKRHRTLISANYTIVITPRYVPSVRYDIEAQDIVLITADTLAEYLYNNIISNNRDISYADIQAIIVANLGKDISTQISNLTLSKFG", "text": "FUNCTION: An S subtype restriction enzyme that recognizes the double- stranded sequences 5'-GACGC-3' and 5'-GCGTC-3' and cleaves respectively 10 bases after G-1 and 10 bases before G'-1."}
+{"protein": "MTNSSNNSNKCENKNYYEILKVSIDADIEEIKKSYRKLALLYHPDKLNKEENIEENINNFSNCLVNNNNNNNNSNTKDFNDIQIAWETLKDDLLRKQYDSLLLEQKRQKYSVSDEIDLDDMEFIEENSEYVYPCRCGDHYIITEDQLSEGSDVVCCSGCSLSIKVIYQME", "text": "FUNCTION: Stimulates the ATPase activity of several Hsp70-type chaperones. Plays a role in the diphthamide biosynthesis, a post- translational modification of histidine which occurs in translation elongation factor 2 (By similarity). SIMILARITY: Belongs to the DPH4 family."}
+{"protein": "MVTWVLNYLLVAFLFAISYNIDAASAGITRHYQFDIQLKNITRLCKTKTIVTVNGKFPGPRVTAREGDNLQIKVVNHVSNNISIHWHGIRQLRSGWADGPSYVTQCPIRMGQSYVYNFTVTGQRGTLWWHAHIQWMRATVYGPLIILPKLHQPYPFPKPYKQVPILFGEWFNADPQAVVQQALQTGAGPNASDAHTFNGLPGPLYNCSTKDTYKLMVKPGKTYLLRLINAALNDELFFTIANHTLTVVEADACYVKPFQTNIVLLGPGQTTNVLLKTKPIYPNATFYMLARPYFTGQGTIDNTTVAGILQYQHHTKSSKNLSIIKPSLPPINSTSYAANFTKMFRSLASSTFPANVPKVVDKQYFFAIGLGTNPCPKNQTCQGPTNTTKFAASINNVSFILPNKTSLLQSYFVGKSKNVFMTDFPTAPIIPFNYTGTPPNNTMVSRGTKVVVLKYKTTVELVLQGTSILGIEAHPIHLHGFNFYVVGQGFGNFNPARDPKHYNLVDPVERNTINIPSGGWVAIRFLADNPGVWLMHCHIEIHLSWGLTMAWVVLDGDLPNQKLLPPPSDFPKC", "text": "FUNCTION: Lignin degradation and detoxification of lignin-derived products (By similarity). Required for root elongation in dehydration conditions. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "MAPPNKNPNGYYVESFPAPGLRQIVRHITGLNKQGESVFLHSDHGDHHRFMVQNQAISNLLYSTQETPVDLNNNIDIQKAKEKEPPFHYKSGSIVRMIDFGPGVESPLHRAMTIDYGIIVEGVFELILDSGEKRIMRQGDVSVQRATAHKWVNVTGNGTLPGRVMWVLLDCKEVVDAKGEKVEGYLGSLQEHYEGR", "text": "FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sordarial, a salicylic aldehyde structurally related to the phytotoxin pyriculol (PubMed:19277664, PubMed:28485098, PubMed:30908040). The most interesting aspect of this pathway is formation of an aromatic product from the highly reducing polyketide synthase srdA (PubMed:30908040). SrdA synthesizes a reduced polyketide chain from one molecule of acetyl-CoA and five molecules of malonyl-CoA (PubMed:30908040). The polyketide chain is then reductively released as an aldehyde (PubMed:30908040). The oxidoreductases srdC, srdD and srdE then oxidize one of the hydroxy groups to facilitate the intramolecular aldol condensation, followed by dehydration to yield a salicylic aldehyde (PubMed:30908040). This aldehyde can undergo facile reduction by endogenous reductases to yield the alcohol 1-hydroxy-2- hydroxymethyl-3-pent-1,3-dienylbenzene (PubMed:30908040). The flavin- dependent srdI counteract against the propensity of the aldehydes to be reduced under physiological conditions and is responsible for reoxidizing 1-hydroxy-2-hydroxymethyl-3-pent-1,3-dienylbenzene back to the salicylic aldehyde (PubMed:30908040). This salicylic aldehyde is then selectively epoxidized by the cupin-domain-containing oxidoreductase srdB to yield the epoxide, which can be hydrolyzed stereoselectively by the hydrolase srdG to give the final product sordarial (PubMed:30908040). SIMILARITY: Belongs to the virC family."}
+{"protein": "MKRQKRDRLDRAFAKGFQAGVGGRSKEMCPYSNLDSRSQWLGGWREGVDGRITGLFTK", "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": "MPNDSVLSLFFFVTLFTCLLSATSHDDHIFLPSQLHDDDSVSCTATDPSLNYKPVIGILTHPGDGASGRLSNATGVSYIAASYVKFVESGGARVIPLIYNESPENLNKKLDLVNGVLFTGGWAVSGPYLDTLGNIFKKALERNDAGDHFPVIAFNLGGNLVIRIVSEQTDILEPFTASSLPSSLVLWNEANAKGSLFQRFPSDLLTQLKTDCLVLHNHRYAISPRKLQYNTKLSDFFEILATSGDRDGKTFVSTARGRKYPVTVNLWQPEKNAFEWATSLKAPHTEDAIRVTQSTANFFISEARKSTNTPDAQKVRDSLIYNYKPTFGGTAGKGYDQVYLFE", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. Secreted, cell wall. Note=Extracellular or cell-wall bound. SIMILARITY: Belongs to the peptidase C26 family."}
+{"protein": "MSSPGTESAGKSLQYRVDHLLSAVENELQAGSEKGDPTERELRVGLEESELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVAADNHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQRMITSHCFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERSDHKEMMEEPGDSQQPGYSQWGWLLPGTSTLCPPANPHPQFGGALSLPSTHSCDRYPTLRSHRSSPYPSPYAHRNNSPTYSDNSPACLSMLQSHDNWSSLGMPAHPSMLPVSHNASPPTSSSQYPSLWSVSNGAVTPGSQAAAVSNGLGAQFFRGSPAHYTPLTHPVSAPSSSGSPLYEGAAAATDIVDSQYDAAAQGRLIASWTPVSPPSM", "text": "FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence and activates gene transcription when bound to such a site. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MEMVFYPNDLLRVKTKQIENIDDKIRDYAKKMIELMDISGGVGLAAPQVGLDLALFVVRENKMARPLVFINPSIIETSYEFSSYKEGCLSIPGVYYDLMRPKAVVINFHDENGKSFTIENSDFLARIIQHEMDHLNGVLFIDYYEEKLKNKLLKPYMRERGLKAK", "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": "MEPGPGGRGAARGQRPPNAAQPREQERKLEQEKLSGVVKSVHRRLRKKYREVGDFDKIWREHCEDAETLCEYAVAMKNLADNHWAKTCEGEGRIEWCCSVCREYFQNGGKRKALEKDEKRAVLATKTTPALNVHESSKLEGPLTNLSFTSPDFITELLQASGKIRLLDVGSCFNPFLKFEEFLTVGIDIVPAVESVYKCDFLNLQLQQPLQLAQDAIDAFLKQLRNPIDALPGELFHVVVFSLLLSYFPSPYQRWICCKKAHELLVLNGLLLIITPDSSHQNRHAMMMKSWKIAIESLGFKRFKYSKFSHMHLMAFRKTSLKTTSDLVSRNYPGMLYIPQDFNSVEEEEYSNTSCYVRSDLEDEQLAYGFTELPEAPYDSDSGESQASSIPFYELEDPILLLS", "text": "FUNCTION: S-adenosyl-L-methionine-binding protein that acts as an inhibitor of mTORC1 signaling via interaction with the GATOR1 and KICSTOR complexes. Acts as a sensor of S-adenosyl-L-methionine to signal methionine sufficiency to mTORC1: in presence of methionine, binds S-adenosyl-L-methionine, leading to disrupt interaction with the GATOR1 and KICSTOR complexes and promote mTORC1 signaling. Upon methionine starvation, S-adenosyl-L-methionine levels are reduced, thereby promoting the association with GATOR1 and KICSTOR, leading to inhibit mTORC1 signaling. Probably also acts as a S-adenosyl-L- methionine-dependent methyltransferase. SIMILARITY: Belongs to the BMT2 family."}
+{"protein": "MPLPLGDPLALAVSPQLGYIRITAMPRWLQLPGMSALGILYSLTRVFGLMATANWSPRGIKRVRQSLYLRIHGCVMLIFVGCFSPFAFWCIFQRMAFLRQNRILLMIGFNRYVLLLVCAFMTLWIHCFKQAEIIGCLNRLLKCRRRLRRLMHTRKLKDSMDCLATKGHLLEVVVLLSSYLLSMAQPIQILKDDPEVRRNFMYACSLVFVSVCQAILQLSLGMYTMAILFLGHLVRHSNLLLAKILADAEHIFESSQKAGFWPNRQELYKGQQKWLALELWRLLHVHHQLLKLHRSICSLCAVQAVCFLGFVPLECTIHLFFTYFMKYSKFILRKYGRSFPLNYFAIAFLVGLFTNLLLVILPTYYSERRFNCTREIIKGGGLAFPSRITVKQLRHTMHFYGLYLKNVEHVFAVSACGLFKLNNAILFCIVGAILEYLMILIQFDKVLNK", "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. Gr77a subfamily."}
+{"protein": "MENLTLVSCSASSPKLLIGCNFTSSLKNPTGFSRRTPNIVLRCSKISASAQSQSPSSRPENTGEIVVVKQRSKAFASIFSSSRDQQTTSVASPSVPVPPPSSSTIGSPLFWIGVGVGLSALFSYVTSNLKKYAMQTAMKTMMNQMNTQNSQFNNSGFPSGSPFPFPFPPQTSPASSPFQSQSQSSGATVDVTATKVETPPSTKPKPTPAKDIEVDKPSVVLEASKEKKEEKNYAFEDISPEETTKESPFSNYAEVSETNSPKETRLFEDVLQNGAGPANGATASEVFQSLGGGKGGPGLSVEALEKMMEDPTVQKMVYPYLPEEMRNPETFKWMLKNPQYRQQLQDMLNNMSGSGEWDKRMTDTLKNFDLNSPEVKQQFNQIGLTPEEVISKIMENPDVAMAFQNPRVQAALMECSENPMNIMKYQNDKEVMDVFNKISQLFPGMTG", "text": "FUNCTION: Involved in protein precursor import into chloroplasts. Part of the motor complex consisting of a co-chaperone (TIC40) and a chaperone (HSP93) associated with the import channel (TIC110). Causes the release of bound transit peptides from TIC110 and stimulates ATP hydrolysis by HSP93. Involved in reinsertion of proteins from the chloroplast stroma into the inner membrane. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Single-pass membrane protein."}
+{"protein": "MTNEEPLPKKVRLNESDFKVLPREELLQRWKQFEAYVQALENKYTDLNSNDVTGLRESEEKLKQQQQDSARRENILVMRLATKEQEMQECTTQIQHLKQVQQPSVAQLRATMVDPAINLFFIKMKAELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKDSRQQLSQFQQQIQTSGNRTPSSESKDEGETSGKDCGRILNGPSNGGSSHQRTHSSVGLYREGSSTEEDFSASPINEGKLPNHSEERTSRGGSSYMNQLSTGYESVDSPTGSENSLTHQSNDTDSNHDSQEEKPVSGKGNRTVSSRHLQNGLDSSVNVQGSVL", "text": "FUNCTION: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, nucleoplasm. SIMILARITY: Belongs to the fl(2)d family."}
+{"protein": "MQKVVLATGNVGKVRELASLLSDFGLDIVAQTDLGVDSAEETGLTFIENAILKARHAAKVTALPAIADDSGLAVDVLGGAPGIYSARYSGEDATDQKNLQKLLETMKDVPDDQRQARFHCVLVYLRHAEDPTPLVCHGSWPGVITREPAGTGGFGYDPIFFVPSEGKTAAELTREEKSAISHRGQALKLLLDALRNG", "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 (PubMed:12297000, PubMed:17976651). Can also efficiently hydrolyze 2'- deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) (PubMed:17090528). 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 (PubMed:12297000, PubMed:12730170, PubMed:17090528). To a much lesser extent, is also able to hydrolyze GTP, dGTP and dUTP, but shows very low activity toward the canonical nucleotides dATP, dCTP and dTTP and toward 8-oxo-dGTP, purine deoxyribose triphosphate, 2-aminopurine deoxyribose triphosphate and 2,6-diaminopurine deoxyribose triphosphate (PubMed:12297000, PubMed:17090528). SIMILARITY: Belongs to the HAM1 NTPase family."}
+{"protein": "MKVSAALLCLLLIAAALTTQVLTQPDAIISPVTCCYTLTNKKISIQRLASYKRVTSSKCPKEAVIFKTVLNKEICADPKQKWVQDSMAHLDKKSQTQTAKP", "text": "FUNCTION: Acts as a ligand for C-C chemokine receptor CCR2 (By similarity). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (By similarity). Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinophils (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity). May play a significant role in monocyte trafficking into the reperfused myocardium (PubMed:9024159). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
+{"protein": "MLDRDVGPTPMYPPSYMEPGIGRHTPYGNQTDYRIFELNKRLQNWTEQDCDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELFYVLKHPKESFHNNFVSLDCDQCTMVTQNGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHREVVPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQAPNKRRKRKMSGGSTMSSGGGNNNNSNSKKKSPASSFALSSQDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNSSPTMGTNSPWNSKAPSSQQGKNDNPSSQSSQ", "text": "FUNCTION: Binds to the LIM domain of a wide variety of LIM domain- containing transcription factors. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the LDB family."}
+{"protein": "MSSRSELLLDRFAEKIGVGSISFNENRLCSFAIDEIYYISLSDASDEYMMIYGVCGKFPTDNPNFALEILNANLWFAENGGPYLCYESGAQSLLLALRFPLDDATPEKLENEIEVVVKSMENLYLVLHNQGITLENEHMKIEEISSSDNKHYYAGR", "text": "FUNCTION: Chaperone for the type III secretion of Tir. Probably stabilizes the protein, prevents inappropriate protein- proteininteractions and aids in secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CesT/SycH chaperone family."}
+{"protein": "MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPQRADDARQLFALSCAAEEQGMLPEDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITQSSLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF", "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. 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 (By similarity). SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily."}
+{"protein": "MRVLFAVFSLIMACQAYDAVLFSNSREIGGTPAAKLVESATAEEPVVFIVNPDFTLGQFSVKANAYTSEPSADYLAKSVKNSNFHESQYFSHQIEATQAQWLSSADQYSAGSPIYIIYGEEWTSMEQLAEQLISKIDNSVGIITSTDAVAHEKSSRVKRVATDEFNSDSENSAAAEANGGFPFPLVIPPYNQTFYSVKPTNGHSCLFYLEGLTVVVEQKKEKVLYYANAYIPGSNFTWAYSETDVTCPNGTIGDFIFKIHLTLENDITGMQGTSKKAFTMKKGDKIDFDLTFTGDLFGYWALNKASASNLAISGYDPYKSASVDGSKVVNGSATQYTKLNSVAGWSLACGQSQAVFFPTNEQSVRIGVALMNTQIQLFNYQNPEKWVESAHFTLQTEDCTGTFSSGSWMGIVSALVLIAGLMFGYVMLQSVQTMDRFDDPKQRQIVINVRE", "text": "FUNCTION: Accessory subunit of the proton-transporting vacuolar (V)- ATPase protein pump, which is required for luminal acidification of secretory vesicles (By similarity). In the germline, required for the trafficking of the receptor RME-2 to the oocyte cell membrane where it regulates the uptake of yolk proteins (PubMed:22768351). Also, plays an essential role in osmoregulation in the embryo, probably by regulating the proper formation of the eggshell (PubMed:22768351). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family."}
+{"protein": "MDPNTVSSFQVDCFLWHVRKRVADQELGDAPFLDRLRRDQKSLRGRGSTLGLDIETATRAGKQIVERILKEESDEALKMTMASVPASRYLTDMTLEEMSRDWSMLIPKQKVAGPLCIRMDQAIMDKNIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTAEDVKNAVGVLIGGLEWNDNTVRVSETLQRFAWRSSNENGRPPLTPKQKREMAGTIRSEV", "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 (PubMed:33766561). Stress granule formation is thus inhibited, which allows protein synthesis and viral replication (PubMed:33766561). 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. SIMILARITY: Belongs to the influenza A viruses NS1 family."}
+{"protein": "MDEHEEAVIFGICLVDFHHKRGPEIEYWYGLPEGTQSAELWPNLPFQALPDGSHSFEETFTYFTLLYDERRQRSPPNGATDLSDDSINDNTTLFAISCSRQIKSDELVTKDKDVTRSTVQKAIVVISRQPIFGQIKDKLSIVTNAFFLQHDFGDRKIIQSLYENLKSIYTPASLVRNAENRLYIGLCLRKILHDFKRNALVLLKAIMLEKKIIVYGNDVEALCNLQFGLISLIPDLMSNLQDSGSPQLFQDISKLNVVDSFKSSNRESVLRFLGFPLPIFEKGGLFSPYTPLQQMNDIRSERTLFFMIGSSNTLLAEQKEELCHIFVNTDNSTVDILDKTLNPVLQLSSHDKKWIESISGIVSDTWNENDDETPKNSQFEGSEDFIRWQFEDYLTGLLSSVKLSDYLDLHKENDQALKTIPEDMLNSNPVHLFNLNWVQSWKETQNFLIFNSRTDDRLFDLFPPKHIYNGADTLSLLQQRFLATFHNLKRSSSNSSSNKNGHQSEEDIKDQESIESKKSVSQISVNPGKNTDKPAANLWNSWKEYFNKPKNTANEDVTESTEDLKNRSKTSNAIQKAMMGLGLHYKPDAETDQQSEEVGNSEDNEDDDTDEDSEDDDDDGGDDDDSEDDDDDDDGEGDENGDDGEGDENGDDGEGDENGDKEDSQDFSNGFTDVTNINTDHDKENEQNFEGNAENFNEDETVADKDIEGGPESNKNSDSKTDIYENDRNVEDSSKTRNTVKKSNEEGGANDAAIGNCVQDEEKL", "text": "FUNCTION: Functions in the late secretory pathway. Required for the generation of secretory vesicles as well as for actin polarization and polarized growth. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AVL9 family."}
+{"protein": "MDFGIGFLSNNVMLPILDFFYGIVPSYGLAIVALTLVVRFAVYPLSAGSIRNMRRMKVVQPIMQKRMQEIQQKYKDNPAEQQKAMAEVYREFGNPLAGCFPLLLQLPILFALFATLRGSPFADVNYQINLQIVPPDQPVLAQPFATKPQNIYVDEGVHFPIQAVVPSGTRIPVGQMVDLQFQTKEGKPFSELVAAYPNSHLQPKWQIIRGQERATIDREGHLQALQPGEVTVQGTIPGIAADKGFLFISALGHVGVIDQGELFITLPDGARQFNWGAIHWDILVMILGFGVSLYVNQLLSGQGSSNNPQQQTVNQLTPIIFSGMFLFFPLPAGVLLYMLIANIFQTVQTFILQREPLPENLQKLVEEQERAEAIKNRAPLPFEGKGAKGAKATKAKGNPSS", "text": "FUNCTION: Probably also aids protein insertion, folding and/or assembly of membrane complexes destined for the thylakoid. 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 (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily."}
+{"protein": "MGLKDELTTFCHDVFNGNWETTEGKNVPDEDSRLTLKNTAITIDGTVLYADLDGSTAMVDGYKNWFAAEIYKTYLYCCARIIAAEGGVVTAYDGDRVMALFIGERKNTRAARAAMKIKWAVDEIIMPKKDARYTSNKFALKHVTGIDTCSLFVAKTGARGANDLVWVGRAANYAAKLTSLPSTYTYITESVYKMLADEAKTSNGKSMWEKVTWNTFNNSTIYRSNWRWRID", "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 signal activates the adjacent effector, leading to bacterial cell death and abortive phage infection. A clade B Pycsar system. FUNCTION: The pyrimidine cyclase gene of a two-gene Pycsar system, generates cyclic UMP (cUMP) from UTP probably in response to bacteriophage infection (Probable). Expression of this and adjacent effector XpPycTIR (AC P0DV29) confers resistance to bacteriophage T7. When cells expressing the Pycsar system are infected phage T7 at low multiplicity of infection (0.2 MOI) the culture survives, at 2.0 MOI bacteria enter growth arrest. The same cells enter growth arrest after exposure to 2.5 mM cUMP but not cCMP; the effector protein responds only to the cUMP produced by its cognate NTP cyclase (PubMed:34644530). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Pyrimidine cyclase subfamily."}
+{"protein": "MLSESLTKTKLTDPLILDLLQNIRKHRSMLEDLKSIKIDPNLTNIISNEIGRELYIENEFHKAKGFRKLHIEVAEFSKNLRILHCVFFPDPKFDIPIFGMDLVKINDIVSAAIVDLSPASQNQALKYEKLLSGVDKSSFTSLREIPKWGRIFSNNVFFASLRNKSEKNDFCSVVDQYLSILIKLSKKAKPEFNEEIIQERIDFQKNYCAQQMKNEKTSMVLLKYFDEKWVNNYIKTVLFDF", "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": "MTDKERAKLAKAYGKLAQKIQKSYPDINVVYGRDAKNKLHALYQDPETGNIFSLEKRKQLPADYPLFELDSDEPISFAPKIIPLTAFDGNNNEVIVQYDQVNNTFYDQDGNVLDVSGYRDGENIPLVDYLNYGGSTASADTTTSEPLSGEGYPDIDAGLPVVDPDATPEQQADQLFGLDPLPQAPDEYQDTTAPPAYDQTFDQATYDQQAYDQNYDPNAYYDQQAYDQSFDQQAYDQAYDANAYNTQNYDQAHDPNAYYDSQAYSDPDQASAVAPIEVAPLQPEPVAPVVEPTAVPIVESAPIVEVTPTVEPTPTPVVETAPVVEAPKVVEPTPTPVVEATPAPKVEPKVVEQPQPTPVTVEVDSPKVEIPKVVTAKVALQVAQPTPVPAVPKVAPQPTPAPVVVQPTAVVQPVVKAEPKVVTPTPAPQVVVTPQVATPKVTPKVVQTTPAVPPVVVQPEVVVQPIIRPTQPEPEWKPSPASVVEPQPCQSACVNNESGAITIHTTNRSLLLEKLASLGHLHDASTRTPLPHERYQLAPPSEYVATKYNEPLFNLPAIRNSWARFTRPTVESTPIASRFTGVTPMAVNYRNPASLNFDSLNSFGAYRSPSSFYPLRRPLELSSLRRNRSSFFNTHRFDLGSNYTSFTPRYRSPLRGGLSQRFPLRSSWSKEF", "text": "FUNCTION: Component of the cytoskeleton-like structure which stabilizes the shape of the wall-less mycoplasma. This cytoskeleton-like network of accessory proteins containing HMW proteins 1 to 5 allows the proper anchoring of cytadhesin proteins in the mycoplasmal membrane at the attachment organelle. Essential for successful surface parasitism. SUBCELLULAR LOCATION: Cell projection, attachment organelle membrane. Note=Localizes specifically to the attachment membrane."}
+{"protein": "MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGGSRESRGGWDSRDDFNSGYRDDFLGGRGGSRPGDRRAGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE", "text": "FUNCTION: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region."}
+{"protein": "MVEPFLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKSTITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEKV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
+{"protein": "MAADLGPWNDTINGTWDGDELGYRCRFNEDFKYVLLPVSYGVVCVPGLCLNAVALYIFLCRLKTWNASTTYMFHLAVSDALYAASLPLLVYYYARGDHWPFSTVLCKLVRFLFYTNLYCSILFLTCISVHRCLGVLRPLRSLRWGRARYARRVAGAVWVLVLACQAPVLYFVTTSARGGRVTCHDTSAPELFSRFVAYSSVMLGLLFAVPFAVILVCYVLMARRLLKPAYGTSGGLPRAKRKSVRTIAVVLAVFALCFLPFHVTRTLYYSFRSLDLSCHTLNAINMAYKVTRPLASANSCLDPVLYFLAGQRLVRFARDAKPPTGPSPATPARRRLGLRRSDRTDMQRIEDVLGSSEDSRRTESTPAGSENTKDIRL", "text": "FUNCTION: Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. The affinity range is UTP = ATP > ATP-gamma-S >> 2-methylthio-ATP = ADP. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MHGSLLKLALLSFSLGSSAAVLPRDTGRTSAPSGCSTVGTSGDYSTIGDALTALGSSTADACIYIAAGTYEEQLVINYAGHLTLYGETTDTQTYKQNTVTITHTISSPEAGSLDNSATVNIKSDLVSVYNINIANGYGSGAQAVALVANADQLGFYACQFTGYQDTLYAKAGHQYYINSRIEGAVDYIFGDASAWFENCDIVSNGAGYITAMSRETTSDTAWYAIDHCNIKAASGVDLTGDVYLGRPWRVLARVIYQYSVLPDIINAKGWHSMADGATPLYYEFNNTGAGSDTSDREYLSTIDAPVTKETVLGDDYKNWVDLSY", "text": "FUNCTION: Involved in maceration and soft-rotting of plant tissue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pectinesterase family."}
+{"protein": "MNLFRFLGDLSHLLAIILLLLKIWKSRSCAGISGKSQVLFAVVFTARYLDLFTNYISLYNTCMKVVYIACSFTTVWMIYSKFKATYDGNHDTFRVEFLVIPTAILAFLVNHDFTPLEILWTFSIYLESVAILPQLFMVSKTGEAETITSHYLFALGVYRTLYLFNWIWRYHFEGFFDLIAIVAGLVQTVLYCDFFYLYITKVLKGKKLSLPA", "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": "MDSHTLIQALIYLGSAALIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDAESILHFAEIGVVLMLFIIGLELDPQRLWKLRAAVFGGGALQMVICGGLLGLFCMLLGLHWQVAELIGMTLALSSTAIAMQAMNERNLMVTQMGRSAFAVLLFQDIAAIPLVAMIPLLATSSASTTMGAFALSALKVAGALVLVVLLGRYVTRPALRFVARSGLREVFSAVALFLVFGFGLLLEEVGLSMAMGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIGVGMSIDFGTLLENPLRIVILLLGFLIIKIAMLWLIARPLQVPNKQRRWFAVLLGQGSEFAFVVFGTAQMANVLEPEWAKSLTLAVALSMAATPILLVILNRLEQSSTEEAREADEIDEEQPRVIIAGFGRFGQITGRLLLSSGVKMVVLDHDPDHIETLRKFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTNLQLTEMVKEHFPHLQIIARARDVDHYIRLRQAGVEKPERETFEGALKTGRLALESLGLGPYEARERADVFRRFNIQMVEEMAMVENDTKARAAVYKRTSAMLSEIITEDREHLSLIQRHGWQGTEEGKHTGNMADEPETKPSS", "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. KefC subfamily."}
+{"protein": "MVTLTFLLSAAYLLSGRVSAAPSSAGSKSCDTVDLGYQCSPATSHLWGQYSPFFSLEDELSVSSKLPKDCRITLVQVLSRHGARYPTSSKSKKYKKLVTAIQANATDFKGKFAFLKTYNYTLGADDLTPFGEQQLVNSGIKFYQRYKALARSVVPFIRASGSDRVIASGEKFIEGFQQAKLADPGATNRAAPAISVIIPESETFNNTLDHGVCTKFEASQLGDEVAANFTALFAPDIRARAEKHLPGVTLTDEDVVSLMDMCSFDTVARTSDASQLSPFCQLFTHNEWKKYNYLQSLGKYYGYGAGNPLGPAQGIGFTNELIARLTRSPVQDHTSTNSTLVSNPATFPLNATMYVDFSHDNSMVSIFFALGLYNGTEPLSRTSVESAKELDGYSASWVVPFGARAYFETMQCKSEKEPLVRALINDRVVPLHGCDVDKLGRCKLNDFVKGLSWARSGGNWGECFS", "text": "FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from phytate. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the histidine acid phosphatase family."}
+{"protein": "MAVSFTNVSSEAGLKKLDEYLLTRSYISGYQASNDDLAVYSAFSTAPSSSYTNVARWFTHIDALLRLSGVTADGQGVKVESTAVPSASTPDVADAKAPAADDDDDDDVDLFGEETEEEKKAAEERAAAVKASGKKKESGKSSVLLDVKPWDDETDMTKLEEAVRNVKMEGLLWGASKLVPVGYGIKKLQIMMTIVDDLVSVDSLIEDYFYTEPANEYIQSCDIVAFNKI", "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": "MAVCIAVIAKENYPLYIRSVPVQNELKFHYTVHTSLDVVEEKISAVGKAMADQRELYLGLLYPTEDYKVYGYVTNSKVKFVIVVDSSNTSLRDNEIRSMFRKLHNSFTDVMCNPFYNPGDTIQSKAFDSMVSAMMVQAS", "text": "FUNCTION: May play 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": "MDLTITTLEGKDAGKVKLNEEIFGLDPRDDILQRVVRWQLARRQQGSHKAQGRGDVSRTGSKMYKQKGTGRARHHSARAPQFRGGGQAHGPVVRNHDHDLPKKVRALGLRHALSAKAKASDLIIIDDLASADAKTKQLVSQFAKLGLENALLIGGAEIDANFQRAASNIPNIDVLPVQGINVYDILRRGKLVLSKAAVEALEERFK", "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). SIMILARITY: Belongs to the universal ribosomal protein uL4 family. SIMILARITY: Belongs to the universal ribosomal protein uL4 family."}
+{"protein": "MVPPVQVSPLIKLGRYSALFLGVAYGATRYNYLKPRAEEERRIAAEEKKKQDELKRIARELAEDDSILK", "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": "MAAWGERLAGVRGVLLDISGVLYDGGEGGGAAIAGSVEAVARLKRSRLKVRFCTNESQKSRADLVGLLRRLGFDVSEGEVTAPAPAACLILKQRGLRPHLLVHDGVRSEFDQIDTSNPNCVVIADAGEGFSYQNMNKAFQVLMELENPVLFSLGKGRYYKETSGLMLDVGPYMKALEYACGIEAEVVGKPSPEFFKSALQEMGVEAHEAIMIGDDIVGDVGGAQRYGMRALQVRTGKFRPSDEHHPEVKADGYVDNLAEAVDLLLQHADK", "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. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HAD-like hydrolase superfamily."}
+{"protein": "MSGFRGLVPELENSLWSSPTTSCMSKMCWWLLWGILHTCPTQASVLLAQQSPQQLTSPGYPEPYLKGQESHTDIEAPEGFAVRLTFQDFDLEPSPDCEGDSVTISTGGTDATRLCGRQGSPLGNPPGHREFVSSGRSLRLTFQAHSSSKSKITHLHKGFLALYQAVAVNQPNGDTEAVTTPGAPKIQNHCQDPYYKADQTGTLSCPSSWKWKDRQDGGEVPECVPVCGRPVVPLAENPNTFGSSRAKLGNFPWQAFTSIYGRGGGALLGDRWILTAAHTIYPKDSIYLRRNQNVEVFLGHTDIDELLKLGNHPVRRVVVHPDYRQHESHNFNGDIALLELEQRVPLGPNLLPVCLPDNETLYHSGLWGYVSGFGVEMGWLTTKLKYSKLPVAPREACEAWLHQRQRTEVFSDNMFCVGEEMQVNSVCQGDSGSVYVVWDDLALRWVATGIVSWGIGCGKGYGFYTKVLSYMDWIKRVIEGKD", "text": "FUNCTION: Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "SDAAETVGEIGSSIGRSMGGTSGIIYTIFFKAAHSVLKASSHSGVTSKQWAEALAASIAAVSKYGGASAGYRTLLDALIPAS", "text": "SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family."}
+{"protein": "MRRRRGIVGIEAAIVLIAFVIVAAALAFVALNMGLFTTQKSKEVMQRGLEEATSALEVDGSVIARAIDADTTTGSYNIVVDALAVPLKISPGREGIDLDPSKLTVRLLLPNGFYENVYCGYASGSAGEDFEAVLSNAPTGCEPYTTSPGPFVATDAYVYVINGDGDSVLELGEKGLLIIRLDSDTTATIDVDYLEPYDKIMIELRAVSGASLTLERVIPPTLPPLDSTSDATTGTTTYAVAPVDLG", "text": "FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella. SUBCELLULAR LOCATION: Archaeal flagellum. SIMILARITY: Belongs to the archaeal flagellin family."}
+{"protein": "MNIFCHALFLLLLGVVSCQNNNRNVKPGGKPAKKPNNPAIEATQHGPEADPNSGLAGAGDSSKETNPGGRGSSQQSASVNKPADDMKLHFLKNTAVTCNDGTAAGFYLKEFKGSKRWLIFLEGGWCCYSKETCDSRYKTIPRLMGSTDWPQTRRGSGLLSAQVDENPHWYNANIVFVPYCSSDVWSGNKAASKPKQGKETEYAFMGSQIIREVIKDLVPKGLKQAKVVMLAGTSAGGTGVLLNIDKVSSLLEQQGAEAQVRGLVDSGWFLESKQQKVPDCPDSASCTPADAIKKGLRLWNGVVPEKCKQQYKRGEDWHCFFGHKLYSYISAPLFVVQWLFDEEQLRVENIYMGSQSLSEQQWTYMQNLGKELKNSLKDVTAVFAPSCLSHTLITKSNWTDFQIKGTSLSRALQCWDRSFQEANKNSKTALKGCPFHLIDNCQWPQCNPTCPALIDQATQQEMTLLQVLASMGLDLQKLGLDVRGDISAGMVSNGG", "text": "FUNCTION: Carboxylesterase that mediates deacylation of target proteins (By similarity). Acts as a regulator of growth cone migration. Does not act as an inhibitor of Wnt signaling (PubMed:23365253). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pectinacetylesterase family. Notum subfamily."}
+{"protein": "MGTVTTSDGTNIFYKDWGPRDGLPVVFHHGWPLSADDWDNQMLFFLSHGYRVIAHDRRGHGRSDQPSTGHDMDTYAADVAALTEALDLRGAVHIGHSTGGGEVARYVARAEPGRVAKAVLVSAVPPVMVKSDTNPDGLPLEVFDEFRAALAANRAQFYIDVPSGPFYGFNREGATVSQGLIDHWWLQGMMGAANAHYECIAAFSETDFTDDLKRIDVPVLVAHGTDDQVVPYADAAPKSAELLANATLKSYEGLPHGMLSTHPEVLNPDLLAFVKS", "text": "SIMILARITY: Belongs to the AB hydrolase superfamily. Bacterial non-heme haloperoxidase / perhydrolase family."}
+{"protein": "MAMASLARRKAYFLTRNLSNSPTDALRFSFSLSRGFASSGSDENDVVIIGGGPGGYVAAIKASQLGLKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHSFANHGIKVSSVEVDLPAMLAQKDNAVKNLTRGIEGLFKKNKVTYVKGYGKFISPNEVSVETIDGGNTIVKGKHIIVATGSDVKSLPGITIDEKKIVSSTGALSLSEVPKKLIVIGAGYIGLEMGSVWGRLGSEVTVVEFAGDIVPSMDGEIRKQFQRSLEKQKMKFMLKTKVVSVDSSSDGVKLTVEPAEGGEQSILEADVVLVSAGRTPFTSGLDLEKIGVETDKAGRILVNDRFLSNVPGVYAIGDVIPGPMLAHKAEEDGVACVEFIAGKHGHVDYDKVPGVVYTHPEVASVGKTEEQLKKEGVSYRVGKFPFMANSRAKAIDNAEGLVKILADKETDKILGVHIMAPNAGELIHEAVLAINYDASSEDIARVCHAHPTMSEALKEAAMATYDKPIHI", "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": "MVKDEFFLDHPGRKHRSRNTEKKKKPRRRERRMKQLVCIKSPWNRFKGIMLQLRLLLEVTINPNDNKLKPDSQGEKSRDGDSISKKGSRYVPSFLPPPLASKGKGPENKRDEERSKEMEKGKTRNIDHFVEELKREQEIRERRNQDRENSRDHNSDNTSSSRFDELPDYFDPSGRLGSLDDGDPQTTNLYVVNLSSKVDENFLLRTFGRFGPIASVKIMWPRTEEEKRRERHCGFVAFMNRADGEAAKEKMQGIIVYEYELKIGWGKVVFLPSQALPAPPPGHMAIRSKEGCNLIFSVTSGPPMNSVPNQNSELVLTPNVPDITVISPEDEHLKQIIDTMALNVLDGGCAFEQAIMERGRGNPLFNFLFELGSKEHTYYVWRLYSFAQGDTLQRWRTEPYIMIAGSGRWIPPPLPATRSPEHGKESRGTYAAGKSRCTEAEQTLTDSQRDEFEDMLRALTLERSQIREAMGFALDNAEAAGEVVEVLTESLTLKETSIPTKVARLMLVSDIIHNSSARVKNASAYRTKFEATLPDIMESFNDLYHSVHGRITAEALRERVLKVLQVWADWFLFSDAYINGLRATFLRSRNFGVTSFHSICGDAPDIEKKGLIGNMNDADKINQDAALAMGEGAARQELMNRPISELERRCRHNGLSLLGGREMMVARLVCLKDAEKQRGYEVVDENAKYRQGHSTWEEVNIEPKRMKTSYDKVETEEPVDLASTIPIPQPELKAFVKKEKIDLILPTSRWAREDDETDDEQKKSYSSGSDNAGGITFKTDEEDLKADPSVRVQPENEIDVEQRQKLRHIEIALIEYRESLEEQGMKNSEEIERKVAIHRKRLEADGLSGNQRVLPEKREKREDSRDSSRKRNRSESQNRSQSPPQKSLTRERVRDHDLDKDRHRDRDRQQHDLDKDRKRRAKSSSRERDDHDRSRERDRDWRRRGMR", "text": "FUNCTION: Probable SR-like splicing factor."}
+{"protein": "MARLGLLALLCTLAALSASLLAAELKSKSCSEVRRLYVSKGFNKNDAPLYEINGDHLKICPQDYTCCSQEMEEKYSLQSKDDFKTVVSEQCNHLQAIFASRYKKFDEFFKELLENAEKSLNDMFVKTYGHLYMQNSELFKDLFVELKRYYVAGNVNLEEMLNDFWARLLERMFRLVNSQYHFTDEYLECVSKYTEQLKPFGDVPRKLKLQVTRAFVAARTFAQGLAVARDVVSKVSVVNPTAQCTHALLKMIYCSHCRGLVTVKPCYNYCSNIMRGCLANQGDLDFEWNNFIDAMLMVAERLEGPFNIESVMDPIDVKISDAIMNMQDNSVQVSQKVFQGCGPPKPLPAGRISRSISESAFSARFRPYHPEQRPTTAAGTSLDRLVTDVKEKLKQAKKFWSSLPSTVCNDERMAAGNENEDDCWNGKGKSRYLFAVTGNGLANQGNNPEVQVDTSKPDILILRQIMALRVMTSKMKNAYNGNDVDFFDISDESSGEGSGSGCEYQQCPSEFEYNATDHSGKSANEKADSAGGAHAEAKPYLLAALCILFLAVQGEWR", "text": "FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May be involved in the development of kidney tubules and of the central nervous system. SUBCELLULAR LOCATION: [Secreted glypican-4]: Secreted, extracellular space. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. SIMILARITY: Belongs to the glypican family."}
+{"protein": "MAAGAVFLALSAQLLQARLMKEESPVVSWWLEPEDGTAL", "text": "FUNCTION: Unknown. Candidate gene encoding tumor antigens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the BAGE family."}
+{"protein": "MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPFNPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQSPSSILSTLDVELPPVCCDIDI", "text": "FUNCTION: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of TP53. The negative regulation of TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the securin family."}
+{"protein": "MSKKLKDLPVSSTFTSNLPPDPLVPTVQAMKKADDRILHVPRFVEGGGLFTYLTPSLKANSQLLAYSPSSVKSLGLEESETQTEAFQQLVVGSNVDVNKCCPWAQCYGGYQFGDWAGQLGDGRVVSLCELTNPETGKRFEIQVKGAGRTPYSRFADGKAVLRSSIREYLCCEALYALGIPTTQALAISNLEGVVAQRETVEPCAVVCRMAPSWIRIGTFDLQGINNQIESLRKLADYCLNFVLKDGFHGGDTGNRYEKLLRDVAYRNAKTVAKWQAYGFMNGVLNTDNTSILGLSIDYGPFGFLDVYNPSFTPNHDDVFLRYSYRNQPDIIIWNLSKLASALVELIGACDKVDDLQYMEQLHNSTDLLKKAFAYTSEVFEKIVEEYKNIVQNDFYDLMFKRVGLPSDSSNKILITDLLQILEDYELDMPNCFSFLSRNSPSSMENEEYAAKLMQACICLNPNNERVRNESVKAFTNWVGRYSEATKTQEDSSRLASMKKVNPHFTLRNWVLEEVIKEAYIGKFELFKKVCKMAACPFEDTWGFSKEEEDYLCYNTTPSKSQIQCSCSS", "text": "FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Tyr residues of target mitochondrial proteins (AMPylation). Involved in redox homeostasis by regulating the cellular response to oxidative stress. Regulates protein S-glutathionylation levels possibly by AMPylation of deglutathionylation enzymes such as glutaredoxins. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the SELO family."}
+{"protein": "IVSYPDDAGEHAHKMG", "text": "FUNCTION: Has no antimicrobial activity. Does not inhibit the formation of NO by neuronal nitric oxide synthase. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MNSLLMITACLALVGTVWAKEGYLVNSYTGCKYECFKLGDNDYCLRECKQQYGKGAGGYCYAFGCWCTHLYEQAVVWPLKNKTCNGK", "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. This toxin affects the activation mechanism of sodium channels of squid axon. It also competes with Cn2 in rat brain synaptosomes. Is lethal to mice. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
+{"protein": "MKSMLVVTISIWLILAPTSTWAVNTIIYNVGSTTISKYATFLNDLRNEAKDPSLKCYGIPMLPNTNTNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFETNKCRYHIFNDISGTERQDVETTLCPNANSRVSKNINFDSRYPTLESKAGVKSRSQVQLGIQILDSNIGKISGVMSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFNPNPKVLNLQETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVGGSCQTTYNQNAMFPQLIMSTYYNYMVNLGDLFEGF", "text": "FUNCTION: Possesses antiviral potency. Inhibits viral infection of plants (tobacco mosaic virus) (PubMed:10403789). Inhibits protein synthesis (PubMed:2930487, PubMed:6091760, PubMed:2248976, PubMed:10403789, PubMed:10595542). Releases both adenine and guanine from Escherichia coli rRNA in vitro. Activity on guanine is 20 times slower than that on adenine (PubMed:10595542). SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily."}
+{"protein": "MTARGKIVWVSGPAVKADGMSEAKMYETVTVGEARLIGEVIRLTGDVAFIQVYESTSGLKPGEPVEGTGNPLSVLLGPGIIGQIYDGIQRPLKELSKKSGSFIGRGITTSPVDMTKKYHFVPSVSVGDDVIPGTVIGTVKETDLIDHSIMVPPDHAGGKIKSIVSEGEYDLETEMAGIEKDGKTIPLKMYHRWPVRQPRSYHTKYDPTVPLITGQRVIDTFFPIAKGGTGSIPGGFGTGKTVTLHQIAKWADSQVVVYIGCGERGNEMTEVLVEFPHLKDPRTDKPLMDRTVLVANTSNMPVAAREASIYTGVTIAEYYRDMGKDVVLVADSTSRWAEALREMSGRLEEMPAEEGYPSYLASRLAEFYERAGRVRALGSPERNGSVTLVGAVSPSGGDFTEPVTTHTMRFIKTFWALDAKLAYSRHYPSINWMNSYSGYLADIAKWWGENVSKDWLDTRSEAYGILQREDTLKEIVRLLGPEALPDEEKLILEVARMMKIGLLQQNSFDDVDTYCSPEKQYKLLKMQVDFYKRGQQALKEGAELADIRAMPVISGLLKAKMDIKDDEMPKLDELAGAMDEQYKGITGVKVAS", "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": "MSHRDTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAATLSVRRNIHHDNCKIIAIDNSPAMIERCRRHIDAYKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGALVLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHNAGFEHSELWFQCFNFGSLVALKAEDAA", "text": "FUNCTION: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). 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. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family."}
+{"protein": "MDLIGFGYAALVTFGSILGYKRRGGVPSLIAGLFVGFLAGYGAYRVSLDKRDVKLSLFTAFFLATIMGVRFKRSKKIMPAGLVAGLSLLMILRLVLLLL", "text": "FUNCTION: Inhibits apoptosis via negative regulation of the mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein Endoplasmic reticulum membrane. SIMILARITY: Belongs to the TMEM14 family."}
+{"protein": "MESLFIFAFGMMLSSASALSCIPCVPEECEDPGPCEYGKVLDPCQCCLICRKGPGEICGGPWNLQGVCAEGFACITLSGNPVMNLNGGGQEVGRCRKKY", "text": "FUNCTION: Has a role in the innate immune system. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MGTTTTHKFDRPLRLPPLPCPFPSEVNPYVEQVDKETLEWLIDSEMLDDAETVERYRQAKYGWLSARTYPYAEHHTLRLVSDWCVWLFAFDDAFCESDRRAAEIARALPQLYAVLEDLDVGSEVDDVFAKSLLEIKGRIAAYGDDEQLDRWRNVTKDYLFAQVWEAANREDEVVPSLEDYIFMRRRTGAMLTVFALIDVASGRSLSADEWRHPGMRAITESANDVVVWDNDLISYAKESNSGNSRNNLVNVLAEHRHYSRQEAMEEIGEMRNQAIADMVAVRPSLEALGSDAVLAYVRGLEFWISGSVDYSLTSSRYTDAWRTARQPSIR", "text": "FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpenol 4-epi-cubebol via a 1,10- cyclization, which requires the abstraction of the pyrophosphate from FPP to yield a (E,E)-germacradienyl cation (PubMed:27666571, PubMed:27829890). The only accepted substrate is (2E,6E)-farnesyl diphosphate (FPP) (PubMed:27829890). SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MAEAPAGRALFEIYDEGFDSPSWGGVETALWHLSRSLREAGTEAEFYRSSEGADLDALAARVERDRVDAVFPLVESDLFEGAAWRRLPALHARTVRVWHDVSRLSADLSAPPPCPVHARVPALPGAPVAEGCPARGAHPEGPMREVFLGEWPWTRCFPRRSVIPWAADHVPAKDLCDPSGPVVLQLGKIDTVDAERCLRRLTGAGVALRVVFATWSRRGREARELVRAHQGAGRRVEVLDAYDIRTDWERVFGGASLFLLPSVFHETYNFAAAEAVQLGVPVAALGEGGNLPRFASLTAPTPDALVDRLLAGGGAVAPRPRPAAGWRDVAARYAEVIREHPAAGAGPAVPAGAGEGRGGREEEHGG", "text": "FUNCTION: Glycosyltransferase involved in the biosynthesis of neomycin by mediating glycosylation of ribostamycin with UDP-GlcNAc as a sugar donor to generate 2'''-acetyl-6'''-hydroxyneomycin C. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
+{"protein": "MAYVPAPGYQPTYNPTLPYYQPIPGGLNVGMSVYIQGVASEHMKRFFVNFVVGQDPGSDVAFHFNPRFDGWDKVVFNTLQGGKWGSEERKRSMPFKKGAAFELVFIVLAEHYKVVVNGNPFYEYGHRLPLQMVTHLQVDGDLQLQSINFIGGQPLRPQGPPMMPPYPGPGHCHQQLNSLPTMEGPPTFNPPVPYFGRLQGGLTARRTIIIKGYVPPTGKSFAINFKVGSSGDIALHINPRMGNGTVVRNSLLNGSWGSEEKKITHNPFGPGQFFDLSIRCGLDRFKVYANGQHLFDFAHRLSAFQRVDTLEIQGDVTLSYVQI", "text": "FUNCTION: Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions."}
+{"protein": "MPAIQPPLYLTFLLLILLYLIITLYVWTILTITYKTTVRYAALYQRSFSRWGFDQSL", "text": "FUNCTION: Plays a role in the inhibition of the host NF-kappa-B pathway. This inhibition occurs at the receptor level, by preventing the signaling of TNFR1 as well as IL-1R and TLR3. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Host cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the rubulavirus small hydrophobic protein family."}
+{"protein": "MDSSTVLFIGAVAVAFIFLKWMVSPIPPQNEFTIDHLSQDQSTGSTTSSNAHQNRDTHSISTQSHRNSRRAVSESMIEVVQSIAPMLTVEQIRYDLETTGNVEATVNRFMELGDLPFPPGYVRPQQPPTPSEEPKKQEVIGKRSVNLLEKYNIDAKNPKSDHNSLLHQRRQEMILGARKRLAAQLSNEL", "text": "FUNCTION: Component of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum membrane where it functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme UBC7 to 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 to 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) (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CUE1 family."}
+{"protein": "MGFYEGDDNDANTKAFNDKYIKDQKFATAPFWNLFPKLRDIDEYDNPLLPLPFNFNFRDLGDSALAMASGIPTVKQFDKCEELKGQSAWTTQGIWKCLVPSKAIPPLPQLDFLLPLEEIKSDKSHSHGLFFNDFNLFLKWRSHMNRLQKQRIKTRSTAVEPLARTPEDLMLNWDDLHLGNDAEYASADGSKKIVGRAQSISTTKDSNDAKPSTVKTEKIYFDDGTVDITTTTTSKGSSPQVKHKVVSVDEDN", "text": "SUBCELLULAR LOCATION: Mitochondrion membrane; Peripheral membrane protein; Intermembrane side."}
+{"protein": "MDMRTSFLCVTYVILLTGSACGLQITSTGQTSIEKASGESVKLDCQFTLASDDSGPLDIEWSLQPSDNQKEEKVVIVYSGDRAFEHYYDPLKGRVHFNSPDPKNGDASMNIMGLKATDTGTYQCKIKKVPGIASRKYLLTVMVRPSKPKCSAEGQTYVGKNMVLKCSSVEGTQPMEYIWERTSGNKLLPPLAILDKVTGTMTLKNATGDASGTYRCQAKNRVGTEECVVEVTITQPPNTAGIIAGVIICILLLLILLALILFCCCRARHKKKYEKEIAYEIREDVPPPKSRVSTARSFTSVGSQRSSLGSMSPSNLHEYSKPQYDKIPSEEYDRPPSHAPIPPPSRMAGPNLSRMGAIPVMIPAQNKDGSIV", "text": "FUNCTION: May function as a homophilic cell adhesion molecule and be essential for tight junction integrity. May also be involved in transepithelial migration of leukocytes through adhesive interactions with jaml. The interaction between both receptors may also mediate the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Basolateral cell membrane; Single-pass type I membrane protein Cell junction, tight junction Cell junction, adherens junction."}
+{"protein": "MSEQCQLRPHSDTLVRKLVEMNDEEIIKQRLLIDGDGTGEDRRIVVLLKQFLKWASDSLDSNPIMYDRLMAQFAQCKLTALKNVQTLQMIAGERDNYTQLVEHHEESIVLAKAEIESSKKELITAKQIRKNKMEYDLLASLIQDQPDRSETQRHIETIRREIDDLVQKKLKMERKFQKRRNDFTLLMYTIHELEQQLDQDSSSSASSSSSDCDARSEPDLDDNGIMEVSDEDDDLNNSTPTKFDGARGEPKYHSVSTEDSKAMSVEEDTVLELSIDKDEHDVDVAVAN", "text": "FUNCTION: The THO complex is required for cell proliferation and for proper export of heat-shock mRNAs under heat stress. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus speckle. SIMILARITY: Belongs to the THOC7 family."}
+{"protein": "MSFVIAAPEAIAAAATDLASIGSTIGAANAAAAANTTAVLAAGADQVSVAIAAAFGAHGQAYQALSAQAATFHIQFVQALTAGAGSYAAAEAASAASITSPLLDAINAPFLAALGRPLIGNGADGAPGTGAAGGAGGLLFGNGGAGGSGAPGGAGGLLFGNGGAGGPGASGGALG", "text": "SUBCELLULAR LOCATION: Secreted, cell wall Cell surface. SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily."}
+{"protein": "MAISLKVLAPNQNVYEGDAEEVILPSTTGQIGVLPGHISLVTAIDIGVLRLRMNSKWKSIALMGGFAEIESDEVIVLVNSAEIGSEINIQNAEDALKKAKSAISKFPENEKSSEKIKALNEVSKAEARIQASKN", "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": "MSKKITKKDEVEENILNLINKANRPYNYQMIEAAFPSMGKTQIVKTLKSLGEQGKLTFKEYNKAIIYWRIQDTGPKLDEQGYEIPQESIHDLNRKLDGINRQLEVEQDTLKSLISQSKQLNNQLSDEQIQKEVNQLSTENKELESKLLTFQTKEIMSDKDKQRLDDTIKKARSEWVKRKALFRDILDQVLERSNKKKKDLQEDIGWETDEDLKIQMIPDYSKPLSQQTLSSTNDESPFKKQKK", "text": "FUNCTION: Required for proper homologous pairing and efficient cross- over and intragenic recombination during meiosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HOP2 family."}
+{"protein": "MDVLGAAALALFLVPLLIVAEQGRTWGWGSPAALALFALGAAGLAVFIPVELRRGDEAILPLGLFRRGSIALCSAVNFTIGVGIFGTVTTLPLFLQMVQGRTPTQAGLVVIPFMLGTIASQMVSGKLIASSGRFKKLAIVGLGSMAGALLAMATTGATTPMWGIVLIVLWLGVGIGLSQTVITSPMQNSAPKSQLGVANGASACAGQIGGSTGIAVLFSVMFAVALGRLADLLHTPRYERLLTDPAITGDPANHRFLDMAESGQGAGINLDDTSLLNGIDARLMQPVTDSFAHGFHIMFLPGGVVLLAGFVMTWFLRELQEETAPEEERPAESGAGAKNGPLPASDA", "text": "FUNCTION: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal- tetracycline/H(+) antiporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
+{"protein": "MDDDLTEYAPDIPDNVLELIFSYLKLQDLRNCALVCKSWHRFLSDENNEVWRAQCMQKLSPDAFKTDLLSVVPTYKAKLRAFFHAWNPYDCSRHVYIKPNGFTLHRNPVAQSTDGSRGKIGFQHGRHAWEVRWEGPLGTVAVVGIATKDAAIQCHGYYALLGADDQSWGWNLVDNLLLHNGDAHGIYPLLNNAPKYKVGERIRVILDCDDNTLSFEKNYEFLGVAFTDLPDKVFYPTVAAVYGNTEISMVYLGPPLDG", "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": "MIPAVADPTTLDGGGARRPLLPETDPRGRAAAGAEQKRPPATPTVLTAVVSAVLLLVLVAVTVLASQHVDGQAGGVPAGEDAVVVEVAASRGVAEGVSEKSTAPLLGSGALQDFSWTNAMLAWQRTAFHFQPPKNWMNDPNGPLYHKGWYHLFYQWNPDSAVWGNITWGHAVSRDLLHWLHLPLAMVPDHPYDANGVWSGSATRLPDGRIVMLYTGSTAESSAQVQNLAEPADASDPLLREWVKSDANPVLVPPPGIGPTDFRDPTTACRTPAGNDTAWRVAIGSKDRDHAGLALVYRTEDFVRYDPAPALMHAVPGTGMWECVDFYPVAAGSGAAAGSGDGLETSAAPGPGVKHVLKASLDDDKHDYYAIGTYDPATDTWTPDSAEDDVGIGLRYDYGKYYASKTFYDPVLRRRVLWGWVGETDSERADILKGWASVQSIPRTVLLDTKTGSNLLQWPVVEVENLRMSGKSFDGVALDRGSVVPLDVGKATQLDIEAVFEVDASDAAGVTEADVTFNCSTSAGAAGRGLLGPFGLLVLADDDLSEQTAVYFYLLKGTDGSLQTFFCQDELRASKANDLVKRVYGSLVPVLDGENLSVRILVDHSIVESFAQGGRTCITSRVYPTRAIYDSARVFLFNNATHAHVKAKSVKIWQLNSAYIRPYPATTTSL", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein Vacuole lumen Note=May be released into the lumen of the vacuole from the tonoplast through a proteolytic processing. SIMILARITY: Belongs to the glycosyl hydrolase 32 family."}
+{"protein": "MSEYWYPILGGILLGLSTVMLLLLNGRIAGISGIVGRLLQGGNPAQDIPFVVGLVLGPLVFSVIFDRFPSVTVAATWPTIIVAGLLVGLGTRMSAGCTSGHGIAGIARHSPRSIVATAIFLISGMATATFMGVYQ", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0394 family."}
+{"protein": "MALRSPKSSRGLSQDPTTRRIWFGIATAHDFESHDGMTEERLYQNIFASHLGQLAIIFLWTSGNLFHVAWQGNSEARIKDPLHVRPIAHAIWDPHFGQPAVEAFARGGGLGPVNIAYPGVYQRWYTIGMRTDQDLYTGAFSLLIVSTLFLVAGWLHLEPKWAPSISWFKNAESRLNHHLSGLFGVSSLARAGHLVHVAIPESRGGHVRWGNLLSASPHPQGLGPLSAGQWGVYARDVDSSSHLFNTSQGAGTAIPTFTGGFHPQTQSPWLTDIAHHHLAIAVVFIIAGHTYRTNFGIGHSIGGALEAHIPPGGRLGRGHQGLYDTINNSLHFQLGLALASLGVVTSLVAQHMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFLTRDYSPERGRGNVLARVLEHKEAIISHLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPVFAQWIQSAHGKASYGFDVLLSSPNDPAFNAGRSIWLPGRLDAIDNNSNSLFLTIGPGDFPVHHAIASGLHTTTLILSKGALDARGSKLMPDKKEFGYGFPCDGPGRGGTCDISAWDAFYPAVFWMLNTIGWVTLHWHWKHITLWQGNVAQLDESSTYLMGWSRDYSWLNSSQLINGYNPFGTNSLSVWAWMFSFGHLVWATGFMFLIPRRGYWQELIETLARAHERTPLANLVRWGDKPVALSIVQARLVGLAHFSVGYIFTYAAFPIPSTAGKFG", "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": "MGSRETPSSCSKTLETLDLETSDSSSPDADSPLEEQWLKSSPALKEDSVDVVLEDCKEPLSPSSPPTGREMIRYEVKVNRRSIEDICLCCGTLQVYTRHPLFEGGLCAPCKDKFLESLFLYDDDGHQSYCTICCSGGTLFICESPDCTRCYCFECVDILVGPGTSERINAMACWVCFLCLPFSRSGLLQRRKRWRHQLKAFHDQEGAGPMEIYKTVSAWKRQPVRVLSLFRNIDKVLKSLGFLESGSGSGGGTLKYVEDVTNVVRRDVEKWGPFDLVYGSTQPLGSSCDRCPGWYMFQFHRILQYALPRQESQRPFFWIFMDNLLLTEDDQETTTRFLQTEAVTLQDVRGRDYQNAMRVWSNIPGLKSKHAPLTPKEEEYLQAQVRSRSKLDAPKVDLLVKNCLLPLREYFKYFSQNSLPL", "text": "FUNCTION: Catalytically inactive regulatory factor of DNA methyltransferases that can either promote or inhibit DNA methylation depending on the context (PubMed:11719692, PubMed:15318244, PubMed:15671018, PubMed:24074865). Essential for the function of DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic domain (PubMed:15671018). Acts by accelerating the binding of DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases (PubMed:15671018). Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by recruitment or activation of DNMT3 (By similarity). Plays a key role in embryonic stem cells and germ cells (PubMed:11719692, PubMed:15318244, PubMed:24074865). In germ cells, required for the methylation of imprinted loci together with DNMT3A (PubMed:11719692). In male germ cells, specifically required to methylate retrotransposons, preventing their mobilization (PubMed:15318244). Plays a key role in embryonic stem cells (ESCs) by acting both as an positive and negative regulator of DNA methylation (PubMed:24074865). While it promotes DNA methylation of housekeeping genes together with DNMT3A and DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter of bivalent genes (PubMed:24074865). Interacts with the EZH2 component of the PRC2/EED- EZH2 complex, preventing interaction of DNMT3A and DNMT3B with the PRC2/EED-EZH2 complex, leading to maintain low methylation levels at the promoters of bivalent genes (PubMed:24074865). Promotes differentiation of ESCs into primordial germ cells by inhibiting DNA methylation at the promoter of RHOX5, thereby activating its expression (PubMed:24074865). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MVQNKTTGSCPKPTEVAPGGPSWCKTSNGHIKRPMNAFMVWSQIERRKLMSLCPNMHNADISRSLGQRWKLLQDTDKIPYVREAERLRLKHMADYPNYKYRPRRRSRTQESKTRARLPRSTATCQSVPSPCLSQMDTGSSMQWGETCPAWGGDQVGQSVETQIRESSARSPEVPTHTKTVPSSPQSAEEHEGLEGGSLVIPVDKEVPPHSGSHFEFPDHCTPEVMEMISGSGLLESVPDLVFSY", "text": "FUNCTION: Transcription factor that binds to the sequence 5'-AACAAT-3' (PubMed:12890561). Acts as a transcriptional activator (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLSSSFERNLHQPLLFIDKDTKVVIQGIGNQGQFHSRLMRQYGTKVVGAVHPKKAGSIIAGLPIFKNMKEVVKRTDANASLIFVPAPGAAAACIEAAQAGMGLVVCITEHIPQHDMIKVKKVMKETGCQLIGPNCPGLIQPGTHTKLGIIPTNIFNNGKIGIVSRSGTLTYEAAYATTLAGLGQSTVVGIGGDPFAGQLHTDVVKRFAADPQTEGIILIGEIGGTSEEDAAEWIAKTKLTQEKPVVAFIAGATAPPGKRMGHAGAIVSGGKGTAEGKYKALEAAGVRIARHPGNMGKFIFEEMKRMGKI", "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: Hydrogenosome lumen. SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family."}
+{"protein": "MRFRIRKCPSCGRYTLKETCPVCGTKTKIAHPPRFSPEDPYGEYRRRLKREQLGIVKR", "text": "FUNCTION: Involved in ribosome biogenesis; more specifically in 18S rRNA pseudouridylation and in cleavage of pre-rRNA. SIMILARITY: Belongs to the NOP10 family."}
+{"protein": "MKAQKGFTLIELMIVVAIIGILAAIAIPQYQNYVARSEGASALASVNPLKTTVEEALSRGWSVKSGTGTEDATKKEVPLGVAADANKLGTIALKPDPADGTADITLTFTMGGAGPKNKGKIITLTRTAADGLWKCTSDQDEQFIPKGCSR", "text": "SUBCELLULAR LOCATION: Fimbrium. Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the N-Me-Phe pilin family."}
+{"protein": "MPRLFSYLLGVWLLLSQLPREIPGQSTNDFIKACGRELVRLWVEICGSVSWGRTALSLEEPQLETGPPAETMPSSITKDAEILKMMLEFVPNLPQELKATLSERQPSLRELQQSASKDSNLNFEEFKKIILNRQNEAEDKSLLELKNLGLDKHSRKKRLFRMTLSEKCCQVGCIRKDIARLC", "text": "FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
+{"protein": "MTTSTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRAKCVQYLDRAEKLKDYLRSKEKHGKKPVKENQSEGKGSDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNLTDANIHELARKTEGYSGADISIIVRDSLMQPVRKVQSATHFKKVCGPSRTNPSMMIDDLLTPCSPGDPGAMEMTWMDVPGDKLLEPVVCMSDMLRSLATTRPTVNADDLLKVKKFSEDFGQES", "text": "FUNCTION: (Microbial infection) In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. 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. It is required for proper accomplishment of various processes including the regulation of endosome size, primary cilium organization, mitotic spindle organization, chromosome segregation, and nuclear envelope sealing and spindle disassembly during anaphase (PubMed:33186545). Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission (PubMed:24814515). VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). Critical for normal erythroblast cytokinesis and correct erythropoiesis (PubMed:33186543). SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein Midbody Cytoplasm, cytoskeleton, spindle Note=Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells, interaction with ZFYVE19/ANCHR mediates retention at midbody (PubMed:24814515). Localized in two distinct rings on either side of the Flemming body. SIMILARITY: Belongs to the AAA ATPase family."}
+{"protein": "MADTDDEHASPQNPDNRIELERQAADEAHKAKILAHPPEGPGGDPLHPPVTPRPGATRVVRDRKGGRRVVEVPSTGHSWDGIEEYDNPLPRWWLWTFYATIVWGVLYLIAYPAIPLVNGATQGLLGQNYRSDVAAEIQRFNEANAPIQAKLVETPLEEIAADPELANYTANAGAAIFRTWCAQCHGSGAGGATGYPSLLDNDWLWGGTLEEIHTTVMHGIRDPKDADTRYSEMPRFGIDGLLENAQISQVVNHVLELGGLPHDAALAAEGVEVFADNCSSCHAEDGTGDRAQGAPDLTDAVWLYGSDPATITRIVRDGPFGVMPAWTGRLSEADIVAVAAYVHSLGGGE", "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. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CcoP / FixP family."}
+{"protein": "MRQDMPKPSEAARCCSGLARRALTIIFALLILGLMTWAYAAGVPLASDRYGLLAFGLYGAFLSAHLVAQSLFAYLEHRRVAAAARRSLAKGPLDAATARSVALTISAYQEDPAYLRQCLTSARALLYPHTRLRVLMVVDGNRAEDLYMVDMFREVFADEDPATYVWDGNYHQPWEPAEATGAVGEGAYREVEAEDPGRLAVEALVRTRRCVCVAQRWGGKREVMYTAFKALGDSVDYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWYNQKFLGTHCTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWMTYEAVVSGLFPFFVAATVLRLFYAGRPWALLWVLLCVQGVALAKAAFAAWLRGCVRMVLLSLYAPLYMCGLLPAKFLALVTMNQSGWGTSGRKKLAANYVPVLPLALWALLLLGGLARSVAQEARADWSGPSRAAEAYHLAAGAGAYVAYWVVMLTIYWVGVRRLCRRRSGGYRVQV", "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 the isozymes catalyzing that reaction. Also able to catalyze the synthesis of chito- oligosaccharide depending on the substrate. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NodC/HAS family."}
+{"protein": "MPFFLKELSLTISLHPSYFGPRMQDYLKAKLLADVEGTCSGQYGYIICVLDSNTIDIDKGRVVPGQGFAEFEVKYRAVLWRPFRGEVVDAIVTTVNKMGFFANIGPLNVFVSSHLVPPDMKFDPTANPPNYSGEDQVIEKGSNVRLKIVGTRTDATEIFAIATMKEDYLGVL", "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. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family."}
+{"protein": "MNRLGHKSVVYHGDLRLGELDVNHVSSSHEFRFPNDEIRIHHLSPAGERCPPLAILQTIASFAVRCKLESSAPVKSQELMHLHAVCFHELKTAVVMLGDEEIHLVAMPSKEKKFPCFWCFSVPSGLYDSCLRMLNTRCLSIVFDLDETLIVANTMKSFEDRIEALKSWISREMDPVRINGMSAELKRYMDDRMLLKQYIDNDYAFDNGVLLKAQPEEVRPTSDGQEKVCRPVIRLPEKNTVLTRIKPEIRDTSVLVKLRPAWEELRSYLTAKTRKRFEVYVCTMAERDYALEMWRLLDPEAHLISLKELRDRIVCVKPDAKKSLLSVFNGGICHPKMAMVIDDRMKVWEDKDQPRVHVVSAYLPYYAPQAETALVVPHLCVARNVACNVRGYFFKEFDESLMSSISLVYYEDDVENLPPSPDVSNYVVIEDPGFASNGNINAPPINEGMCGGEVERRLNQAAAADHSTLPATSNAEQKPETPKPQIAVIPNNASTATAAALLPSHKPSLLGAPRRDGFTFSDGGRPLMMRPGVDIRNQNFNQPPILAKIPMQPPSSSMHSPGGWLVDDENRPSFPGRPSGLYPSQFPHGTPGSAPVGPFAHPSHLRSEEVAMDDDLKRQNPSRQTTEGGISQNHLVSNGREHHTDGGKSNGGQSHLFVSALQEIGRRCGSKVEFRTVISTNKELQFSVEVLFTGEKIGIGMAKTKKDAHQQAAENALRSLAEKYVAHVAPLARETEKGPENDNGFLWESSEDVSNKGLEEEAPKENISEL", "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 CPL1, required for male gametes fertility. Multifunctional regulator that modulates plant growth, stress, and phytohormones responses. Positive transcription regulator of genes involved in high salinity resistance and auxin mediated signaling pathway. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MSTKLILSFSLCLMVLSCSAQLLPWRKGQRSRPHRGHQQFHHQCDVQRLTASEPSRRVRSEAGVTEIWDNDTPEFRCAGFVAVRVVIQPGGLLLPSYSNAPYITFVEQGRGVQGVVVPGCPETFQSESEFEYPQSQRDQRSRQSESEESSRGDQRTRQSESEEFSRGDQRTRQSESEEFSRGDQRTRQSESEEFSRGDQRTRQSESEEFSRGDQHQKIFRIRDGDVIPSPAGVVQWTHNDGDNDLISITLYDANSFQNQLDGNVRNFFLAGQSKQSREDRRSQRQTREEGSDRQSRESDDDEALLEANILTGFQDEILQEIFRNVDQETISKLRGDNDQRGFIVQARDLKLRVPEEYEEELQRERGDRKRGGSGRSNGLEQAFCNLKFKQNVNRPSRADVFNPRAGRINTVNSNNLPILEFIQLSAQHVVLYKNAILGPRWNLNAHSALYVTRGEGRVQVVGDEGRSVFDDNVQRGQILVVPQGFAVVLKAGREGLEWVELKNDDNAITSPIAGKTSVLRAIPVEVLANSYDISTKEAFRLKNGRQEVEVFLPFQSRDEKERERF", "text": "FUNCTION: Seed storage protein. SIMILARITY: Belongs to the 11S seed storage protein (globulins) family."}
+{"protein": "MDRAALLGLSRLCALWAAVLALFPCGAQGNWMWLGIASFGVPEKLGCANLPLNSRQKELCKRKPYLLPSIREGARLGIQECRSQFRHERWNCLVAAASAPGTSPLFGYELSSGTKETAFIYAVMAAGLVHSVTRSCSAGNMTECSCDTTLQNGGSSSEGWHWGGCSDDVQYGMWFSRKFLDFPIKNTTAKESKVLLAMNLHNNEAGRQAVAKLMSLDCRCHGVSGSCAVKTCWKTMSSFEKIGHLLKDKYENSVQISDKIKRKMHRREKDQRKIPIRKDDLLYVNKSPNYCVEDKKLGIPGTQGRECNRTSEGADGCNLLCCGRGYNTHVVRHVERCECKFIWCCYVRCRRCESMTDVHTCK", "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 (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MNIFDRKINFDALFKFSHITPSTQQHLKKVYASFALCMFVAAAGAYIHVVTHFIQAGLLSALGSLGLMIWLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALDLCIAINPSILPTAFMGTAMIFTCFTLSALYARRRSYLFLGGILMSAMSLMLLSSLGNLFFGSVWLFQANLYMGLVVMCGFVLFDTQLIIEKAENGDKDYIWHCVDLFLDFVTLFRKLMMILAMNEKDKKKKK", "text": "FUNCTION: Suppressor of apoptosis. Modulates unfolded protein response signaling. Modulates ER calcium homeostasis by acting as a calcium-leak channel. Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BI1 family."}
+{"protein": "MKMAVLVRTDLDMGKGKIAAQVAHAAVSLVLEIVQKRSKAEWKEWLEMWINQGQPKIVLKVKNLDELLEKYNKALQSGLPATIIQDAGKTQIEPGTITCAGIGPGPEEMIDNITGDLKLL", "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": "MPAHMIPQVARAVVQSTYSGSLSAIDDNLEPTDDIDQAAYITTGRYVVCALCLATVSDSPTQLSRWVFHHCSDDRRPLIRSMLLASSRHAHALRESREVDMRRISRLVHQADEEDELDAPRQARRIGYVDLHSCDLQNPTPELATRQLCNDPTRTHSTHPHLARSHPYMLPTAALDIDPPEPVTMFATMSRTDGVPMLFNMTHRNVEVLASPAARASLMYALLKLANAKLTPKQRSIMYGPSANDMVAACTKACAATTFRHVGRYAARVVIEE", "text": "FUNCTION: Interacts with VP4 to form the outer icosahedral capsid with an incomplete T=13 symmetry, about 80 nm in diameter, and consisting of 200 VP4-VP7 trimers. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the aquareoviridae outer capsid VP7 protein family."}
+{"protein": "MSPMAIEPAGDPEHGAFDRNDNADAVVRSINETHVTYKRLGKTGLRVSVPILGCMSLGDKHWVPWALEEDKALPLLKGAFDLGLNCWDTANVYSNGKSEEIIGKAIKTYQLPRHKLVLLSKCGGYVGEAPNVKGDRYENAISRSKDYVNQGGLSRSAIFEQVEASLRRLDTTYLDVLQIHRFDPNTPIEETMKALHDLVSIGKVRYLGACSMYTYQFAQMQFVAEKNGWTKFVSMQNHYSLLYREEERDMIRFCNETGVGLIPWAPLASGMLTRPATQKVPEGDRAIINRVQEVAEKRGWRMSYVALSWINKRVSAPVIDFDRIDRIEEALATKDKELTAEEEKYVEELYKAKDVEGIPSQR", "text": "FUNCTION: Aldo-keto reductase; part of the gene cluster that mediates the biosynthesis of an emodin derivative that may be involved in black Sigatoka disease of banana (PubMed:27388157, PubMed:30735556). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase PKS8-1 (Probable). The atrochrysone carboxyl ACP thioesterase MYCFIDRAFT_190111 then breaks the thioester bond and releases the atrochrysone carboxylic acid from PKS8-1 (Probable). The decarboxylase MYCFIDRAFT_34057 then catalyzes the concerted decarboxylation-elimination required to convert atochrysone carboxylic acid into emodin anthrone, which is further oxidized to emodin by the anthrone oxygenase MYCFIDRAFT_34418 (Probable). The functions of the other tailoring enzymes as well as the final product of the cluster have still to be identified (Probable). SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MAPPPFRPENAIKRADELISVGEKQAALQSLHDFITARRIRWATPSTVEPVVFKFLEIGVELKKGKLLKDGLHQYKKLIQGSTEGLVSVGAVARKFIDLVESKIASEQTRADELQKQEIDDDLEGGVTPENLLISVYESDQSVAGFNDEAITSWLRFTWESYRAVLDLLRNNALLEITYSGVVKKTMHFCLKYQRKNEFKRLAEMLRQHLDAANYQQSKSGNNLVDLSDADTLQRYLDQRFQQVDVSVKLELWHEAYRSIEDVFHLMKISKRAPKPSTLANYYENLVKVFFVSGDPLLHTTAWKKFYKLYSTNPRATEEEFKTYSSTIFLSAISTQLDEIPSIGYDPHLRMYRLLNLDAKPTRKEMLQSIIEDESIYGKVDEELKELYDIIEVNFDVDTVKQQLENLLVKLSSKTYFSQYIAPLRDVIMRRVFVAASQKFTTVSQSELYKLATLPAPLDLSAWDIEKSLLQAAVEDYVSITIDHESAKVTFAKDPFDIFASTASKEVSEEENTEPEVQEEKEETDEALGPQETEDGEEKEEESDPVIIRNSYIHNKLLELSNVLHDVDSFNNASYMEKVRIARETLIKKNKDDLEKISKIVDERVKRSQEQKQKHMEHAALHAEQDAEVRQQRILEEKAAIEAKLEEEAHRRLIEKKKREFEAIKEREITKMITEVNAKGHVYIDPNEAKSLDLDTIKQVIIAEVSKNKSELESRMEYAMKKLDHTERALRKVELPLLQKEVDKLQETDTANYEAMKKKIVDAAKAEYEARMADRKNLVMVYDDYLKFKEHVSGTKESELAAIRNQKKAELEAAKKARIEEVRKRRYEEAIARRKEEIANAERQKRAQELAEATRKQREIEEAAAKKSTPYSFRAGNREPPSTPSTLPKATVSPDKAKLDMIAQKQREMEEAIEQRLAGRTAGGSSPATPATPATPATPTPSSGPKKMTMAEKLRAKRLAKGGR", "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 A family."}
+{"protein": "QAARPRF", "text": "FUNCTION: An 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. May have a hormonal role in females. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
+{"protein": "DKYIALGEWAGCFGIKEKDIDKDLVI", "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": "MSKPPDLLLRLLRGAPRQRVCTLFIIGFKFTFFVSIMIYWHVVGEPKEKGQLYNLPAEIPCPTLTPPTPPSHGPTPGNIFFLETSDRTNPNFLFMCSVESAARTHPESHVLVLMKGLPGGNASLPRHLGISLLSCFPNVQMLPLDLRELFQDTPLADWYAAVQGRWEPYLLPVLSDASRIALMWKFGGIYLDTDFIVLKNLRNLTNVLGTQSRYVLNGAFLAFERRHEFMALCMRDFVDHYNGWIWGHQGPQLLTRVFKKWCSIRSLAESRSCRGVTTLPPEAFYPIPWQDWKKYFEDINPEELPRLLSATYAVHVWNKKSQGTRFEATSRALLAQLHARYCPTTHEAMKMYL", "text": "FUNCTION: Catalyzes the transfer of galactose from UDP-alpha-D- galactose to lactosylceramide/beta-D-galactosyl-(1->4)-beta-D-glucosyl- (1<->1)-ceramide(d18:1(4E)) to produce globotriaosylceramide/globoside Gb3Cer (d18:1(4E)). Also able to transfer galactose to galactosylceramide/beta-D-Gal-(1<->1')-Cer. Globoside Gb3Cer is a glycosphingolipid of the globo serie, one of the major types of neutral root structures of glycosphingolipids, that constitute a significant portion of mammalian cell membranes. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 32 family."}
+{"protein": "MRTLPLNGSRNSSRLPTLLLAAGLAMTPWAPALAAGMEGMDHGSHSMPMGASSDAPAQSRTPIPPVTDADRAAVYTSHSGHQVHDSAINSYFVADKLEWQDANDGSALAWDLSGWIGGDIDRLLLRSEGERTNGKTEEAEVQALWGHAVSSSWDVVAGARQDFKPGAPQTWAAFGLQGQAISDLDVEATAFIGDAGQTAARLEADYDLLLTNDLILQPTGELNFYGKNDPQRGNGSGLSTSEFGLRLRYEITPQFAPYVGVTWNRSYGKTADYAREDDEDVAQARLVVGLRLWF", "text": "FUNCTION: Exact function not known. Could be involved in copper resistance (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein."}
+{"protein": "MCDVLTIRDLSKSFARNRVLNGVNFRMGKGAVVGLMGENGAGKSTLMKCLFGMYAKDTGQILVDGSPVDFQSPKEALENGVAMVHQELNQCLDRTVMDNLFLGRYPARFGIVDEKRMFDDSLTLFASLKMDVNPRAVMRSMSVSQRQMVEIAKAMSYNAKIIVLDEPTSSLTEREIVRLFAIIRDLSKKGVAFIYISHKMDEIFQICSEVIVLRDGVLTLSQSIGEVEMSDLITAMVGRTLDKRFPDADNTVGDDYLEIRGLSTRYAPQLRDISLSVKRGEIFGLYGLVGAGRSELLEAIFGLRTIADGEISLAGKKIRLKSSRDAMKLNFAFVPEERKLNGMFAKGSIEYNTTIANLPAYKRYGLLSKKKLQEAAEREIKAMRVKCVSPSELISALSGGNQQKVIIGKWLERDPDVLLLDEPTRGIDVGAKYEIYQLIIRMAREGKTIIVVSSEMPEILGITNRIAVMSNYRLAGIVDTKSTDQEALLRLSARYL", "text": "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. SIMILARITY: Belongs to the ABC transporter superfamily. Galactose/methyl galactoside importer (TC 3.A.1.2.3) family."}
+{"protein": "MNSAPFSTLLPPPKKESSPTVASAHQSPENQGDEPVAGIVFDSLQPDGIPNVSFQDFIPIRQRDFNMEIPLPSKQDIEQTFQRTKAYFDKLLNNKPATNSRPSTDARSGKGNYIEYKTTDALTNKSTSRIIKIVDHVADPLQPSQIKRKKVVAPPTDEPVAPILHSATEKLTKEQREQWRIPSAVSNWKNPNGYAIDLEKRIAIDGRYNREGTAIPAVNEKLLELTNALEEAESKAREEVRNRAEARKQEAEQQVRLKEDKLRELAQRSREERQRKRRQPIDHEEYDESAIIRQTERNEKRDQMKNDMRLSKLSTADRLRVLAHAQGRDVSEKIILGAAKPSEVPDVHYDSRLLTKGAGTAVPGAPEQVYDGPLFAQNAMDRLYKPARFTGPENDALDILSKMTSEQRFEDQDPGTSVDQQQTSPGMQKSDAKQDSEHDLKRT", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNW family."}
+{"protein": "MSSAPDLALTARLVQLLQTGNIFTTILSIFGIALSAVAAWGIATCVYNLYFHPLASYPGPFLWRASSLPWKIALLKGTMHHDLMRFHETYGPELRLKPDELSYANAQAWKDIHAHVPGRPEFLKDPIRLPLAPNGVMSILVSDTKNHARFRSLFGHAFSDKGLRTQQKTINTYADQFMEVLKEVADNGKSVEMVNYYNMAVFDTIGALAFGESFNSMRDRKIHPWVDAIHKNLKSVAISHVMRSMGIEPLTPYILPKELRGARANNYSYAIAKINNRMQKTGEQGDFWDRVIVKSGAEGEMNDGSGMSKGEMLNNAAVMVVGGSETSASALCGATYLLAQSPDKMKKAVGEIRGKFKSSDEITLHSVTNMEYLTAVIDETLRMYPSVPGQPPRVVPKGGATVCGKFVPEETRVGVSHIGTYFASYNFTRSHEFIPERHIDKSLFPDDNYAAYQPWSVGVRNCIGKNLAYAELRLILAKTLWHYDITLDREKTGDFLDQKIWSIWAKRELWMKISLAENAK", "text": "FUNCTION: Versicolorin B desaturase; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non- enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MVSLLDFNGNMSQVTGETTLLYKEIARNVEKTKKIKIIDFGIGQPDLPTFKRIRDAAKEALDQGFTFYTSAFGIDELREKIAQYLNTRYGTDVKKEEVIVTPGAKPALFLVFILYINPSDEVILPDPSFYSYAEVVKLLGGKPIYANLKWSREEGFSIDVDDLQSKISKRTKMIVFNNPHNPTGTLFSPNDVKKIVDISRDNKIILLSDEIYDNFVYEGKMRSTLEDSDWRDFLIYVNGFSKTFSMTGWRLGYIVAKREIIQKMGILAANVYTAPTSFVQKAAVKAFDTFDEVNQMVSLFKKRRDVMYDELTKVKGVEVSKPNGAFYMFPNVSKILKTSGFDVKSLAIKLIEEKGVVTIPGEVFPLNIGKEFLRLSFAVNEEVIKEGIQKIREFAEQMMNSR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MFRQNLITSAILLMAPLAFSAQSLAESLTVEQRLELLEKALRETQSELKKYKDEEKKKYTPATVNRSVSTNDQGYAANPFPTSSAAKPDAVLVKNEEKNASETGSIYSSMTLKDFSKFVKDEIGFSYNGYYRSGWGTASHGSPKSWAIGSLGRFGNEYSGWFDLQLKQRVYNENGKRVDAVVMIDGNVGQQYSTGWFGDNAGGENFMQFSDMYVTTKGFLPFAPEADFWVGKHGAPKIEIQMLDWKTQRTDAAAGVGLENWKVGPGKIDIALVREDVDDYDRSLQNKQQINTHTIDLRYKDIPLWDKATLMVSGRYVTANESASEKDNQDNNGYYDWKDTWMFGTSLTQKFDKGGFNEFSFLVANNSIARNFGRYAGASPFTTFNGRYYGDHTGGTAVRLTSQGEAYIGDHFIVANAIVYSFGNNIYSYETGAHSDFESIRAVVRPAYIWDQYNQTGVELGYFTQQNKDANSNKFNESGYKTTLFHTFKVNTSMLTSRLEIRFYATYIKALENELDGFTFEDNKDAQFAVGAQAEIWW", "text": "FUNCTION: May be a sugar porin with a broad carbohydrate specificity. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family."}
+{"protein": "MKTIAVNSFKGGTAKTSTTLHLGAALAQYHKARVLLIDFDAQANLTAGLGLDPDCYDSLAVVLQGEKQISEVIRSIDSSGLDLIPADTWLERVEVSGSLAADRYSHERLKTILSTIEHQYDYVIIDTPPSLCWLTESALIAAQHALICATPEFYSVKGLERLATFIQGISSRHPLNILGVTLSFWNYRGKNNAAFTELIQKTFPGKLLNTRIRRDITISEAAIHGKPVFSTAPSARASEDYLKLTEELLFLLRDI", "text": "SIMILARITY: Belongs to the ParA family."}
+{"protein": "MGVPKQRWTPEEEAALKAGVAKHGPGKWRTILRDSDFSALLRLRSNVDLKDKWRNLSVTAGGYGSREKARMALKKGRRVVPKLTAEPMDVDEKDMDNAHDTVIDVEPLAMAFEPLPFLESPDKSVARLDDLIVEAIRKLNEPSGSNKAVISGYIEDQYWPPADFQYLLSTKLKSLVNSGKLIKVNQKYRIAPSSSLGGISTKVSSSEGMNTENNNVKRLTKPQVVAELEKMKGMTREEAAAFAAKAVAEAEVAMAEAEEAARVAEAAENDAEAAKAFLDAVILSMRNRNAASMILRAC", "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": "MGARVLVATTPGDGHVNPMVPVAQEMVSRGHEVRWYTGKAFRSTVERTGARHEPMRDAHDFGGMPREEAFPQHAGLTGITGMIAGFRDIFIEPAADQMTDLLALLEDFPADVLVTDETFFGAGFVSERTGIPVAWIATSIYVFSSRDTAPLGLGLPPSSSRLGRLRNTVLKQLTDRVVMRDLRRHADVVRDRVGLPRIRKGAFENIMRTPDLYLLGTVPSFEYPRGDMPPEVRFVGPFVSPAPPDFTPPAWWGELDSGRPVVHVTQGTVANDAERLLLPAIRALAAEDVLVVATTGAPLELEPMPANVRVERFIPHHALLPHVDAMVTNGGYGGVNTALAHGVPLVVAAATEEKHEVAARVSWSGAGVHLKKRRLSERDIRRAVRAVLDEPRFRVHAARLRDEYAARDAVVDAVDLIEGLV", "text": "FUNCTION: Catalyzes the penultimate step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid that inhibits topoisomerase 1. Has a wide substrate range, including staurosporine aglycone, EJG- III-108A, J-104303, 6-N-methyl-arcyriaflavin and indolo-[2,3-a]- carbazole. SIMILARITY: Belongs to the glycosyltransferase 28 family."}
+{"protein": "MEDGVYEPPDLTPEERMELENIRRRKQELLVEIQRLREELSEAMSEVEGLEANEGSKTLQRNRKMAMGRKKFNMDPKKGIQFLVENELLQNTPEEIARFLYKGEGLNKTAIGDYLGEREELNLAVLHAFVDLHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCLCNPGVFQSTDTCYVLSFAVIMLNTSLHNPNVRDKPGLERFVAMNRGINEGGDLPEELLRNLYDSIRNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVDDPRKPNCFELYIPNNKGQLIKACKTEADGRVVEGNHMVYRISAPTQEEKDEWIKSIQAAVSVDPFYEMLAARKKRISVKKKQEQP", "text": "FUNCTION: Acts as a guanine-nucleotide exchange factor (GEF). Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Activates ARF factors through replacement of GDP with GTP (By similarity). The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane (PubMed:17398095). Involved in neurite growth (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cytoplasm Cell projection Cell projection, growth cone Cell junction, tight junction Cell junction, adherens junction Note=Both isoform 1 and isoform 2 are recruited to the cell membrane through its association with ARL4A, ARL4C and ARL4D. They require also interaction with phosphoinositides for targeting to plasma membrane (PubMed:17398095). In differentiating neuroblastoma cells, colocalizes with CCDC120 in both neurite shaft and growth cone areas."}
+{"protein": "MRSLCCAPLLLLLLLPPLLLTPRAGDAAVITGACDKDSQCGGGMCCAVSIWVKSIRICTPMGKLGDSCHPLTRKNNFGNGRQERRKRKRSKRKKEVPFFGRRMHHTCPCLPGLACLRTSFNRFICLAQK", "text": "FUNCTION: May function as an output molecule from the suprachiasmatic nucleus (SCN) that transmits behavioral circadian rhythm. May also function locally within the SCN to synchronize output. Potently contracts gastrointestinal (GI) smooth muscle. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AVIT (prokineticin) family."}
+{"protein": "MDSKSLAKSKRAHTLHHSKKSHSVHKPKVPGVSEKNPEKLQGNQTKSPVQSRRVSALPSNWDRYDDELDAAEDSSISLHSDVIVPKSKGADYLHLISEAQAESNSKIENNLDCLSSLDDLLHDEFSRVVGSMISARGEGILSWMEDDNFVVEEDGSGSYQEPGFLSLNLNVLAKTLENVDLHERLYIDPDLLPLPELNTSQTKVSRNEEPSHSHIAQNDPIVVPGESSVREAESLDQVKDILILTDESEKSSAIEADLDLLLNSFSEAHTQPNPVASASGKSSAFETELDSLLKSHSSTEQFNKPGNPSDQKIHMTGFNDVLDDLLESTPVSIIPQSNQTSSKVLDDFDSWLDTI", "text": "FUNCTION: Together with RST1, acts as cofactor of the cytoplasmic exosome and connects the cytosolic RNA exosome to the SKI complex (PubMed:31455787). Acts as post-transcriptional gene silencing (PTGS) suppressor (PubMed:31455787, PubMed:31941670). CER16/RIPR can, like RST1 suppress the production of small interfering RNAs (siRNAs) from the CER3 locus, which is involved in cuticule membrane and wax production, and in the typhine and sporopollenin biosynthesis of pollen (PubMed:31455787, PubMed:31941670). SUBCELLULAR LOCATION: Cytoplasm, cytosol Endoplasmic reticulum."}
+{"protein": "MRILLLSHSFNSLTQRLHVELRERGHEVSVELDIHADVTRESVALHRPDLVIAPFLKRAIPDDVWRSVRCLVVHPGPPGDRGPAALDWAVLEGVAEWGVTVLQADGEFDAGPIWSFRSFPMRCAAKSSIYRNELTSCAVAAVLEAVAAIEAGQAAPQPMQAGDPRIRVRGPCRQADRTIDWQHDSTMTVLRKINSADGMPGLVDSLFFQEVRLFDAHEAHDISGVPGTVIAQCEGALARATVDGAVWIGHVKRLAPKSLKLPAAKVFAAEAAYLPHRPGCGYAPIRYREHGEVGELAFSFYNGAMATGDCEALLGAYRAALERPTRVLLLTGGPDYWSNGIHLAEIEAAESAADESWRNINAIDDLARAIIETTDRLVVSVIRGNAGAGGVFLSLAADEVWASDQIILNPHYKDMGNLYGSEYWTYLLPRRAGAANATRITQCRLPMGVAEARRLAIVDRVLSGEALADASLVQSGAAMASDAGFAARLAAKQQRRAADEAEKPLQSYRDEELRRMKLNFYGFDPSYHVARYNFIHKVPKSRTPLTIAGHRIRRAPGRPVGMAVSS", "text": "FUNCTION: Involved in the post-translational processing of the hydrogenase large subunit."}
+{"protein": "MTDKQLDTKLVNAGRSKKYTLGSVNSVIQRASSLVFDTVEAKKHATRNLANGELFYGRRGTLTHFSLQEAMCELEGGAGCALFPCGAAAVANTILAFVEQGDHILMTNTAYEPSQDFCSKILGKLGVTTSWFDPLIGADITQHIQPNTKVVFLESPGSITMEVHDIPSIVSAVRRVAPEAVIMIDNTWAAGVLFKALEFDIDISIQAGTKYLIGHSDAMVGTAVANARCWEQLRENAYLMGQMLDADTAYMTSRGLRTLGVRLRQHQESSLKIAAWLANHPQVARVNHPALPGSKGHAFWKRDFTGSSGLFSFVLNKKLTEAELSAYLDNFSLFSMAYSWGGYESLIIANQPEQIAAIRPAGGVDFTGTLVRVHIGLESVDDLIADLAAGFARIV", "text": "FUNCTION: Catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
+{"protein": "MDVHTNNWRYFHHGCDVMAHLVIPEDLIEGLYAEDRPKIFSCTLKVIDYQTNLVSEPVIVWARSIDHRHTVGTLTSGIALSIPLLLTNDTWHPFNIILLRFAETANHNACYVRFFYQTIFSGLIKAGAPPVEEVNHPPVELPPREDPLVNILQGRSGRQFPATEESTNDHTASQKLVIGEAASAYLNHRALERSPSLRGALAGEIFSSSGASNLSGSVPPANRQARRTALVNLVGTKDFTKDMLRLLPLTHCLSGKRFWLCMYNPEGYKNLVSCLNHLSEDELKKINPLSIIQQDTSFLTLKMNQFVDSLLEECRAANFRMQQVLGVAIRSDASNALEYVQEQFYEACFTLRCATNENSGWVKAAVATQSRKQGVWLDVISLWDQGVGSWGVSLKLPNPLPGLHTLACIQQLSCQLEGKHKYLLESVCAKDDQIAVLHSHTLNAWLLLPGGFAIKGKFTHSEKDLLHISSRYGV", "text": "FUNCTION: Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae CVC1 protein family."}
+{"protein": "MTNFKDIIKKIEYKFSKHQLPDIKVGDLIRLGISIQESGKQRVQPFEGTVIALHKAGLNTTITVRKILQGIGVERVFPIHASCLTSIQVLRRSQVSRAKLYYLRNRTGKATRLKEKFEKLPPIWVNKLP", "text": "SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family."}
+{"protein": "MELCRVLLLIFSAAGPALCYEHETRLVDDLFREYSKVVRPVENHRDAVVVTVGLQLIQLINVDEVNQIVTTNVRLKQQWTDINLKWNPDDYGGVKQIRIPSDDIWRPDLVLYNNADGDFAIVKYTKVLLEHTGKITWTPPAIFKSYCEIIVTYFPFDQQNCSMKLGTWTYDGTMVVINPESDRPDLSNFMESGEWVMKDYRGWKHWVYYACCPDTPYLDITYHFLMQRLPLYFIVNVIIPCLLFSFLTGFVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHTMPPWVRKIFIDTIPNIMFFSTMKRPSRDKPDKKIFAEDIDISEISGKQGPVPVNFYSPLTKNPDVKNAIEGIKYIAETMKSDQESSNAADEWKFVAMVLDHLLLVIFMLVCIIGTLAVFAGRLIELNQQG", "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": "MNFWNFLEILLFIGIVAAGLIVAVMIKTAEDTTLFDRTQLPEDNPQKLNYYVQPPPNGDEKVPFPTVFEPAKVYTTFVVPAYNEEKRIPKMLDETVEYLKSREAKDKSFTWEIVVVNDGSKDKTKEVVLNYAKDYPNIFLLNQPVNMGKGAAIQAGCLHARGELVLMVDADGATKINEFEALETEIKKLMKNNNQAIVVGSRAQNEKANRTPIRKFLGLGMHVLIVLSGVRGIHDTQCGFKLFSREACKMLFMNQHVQRWCFDPELLVIGRRLGMKISEIPVEWNEIEGSKMKISGMIKMAIDLIDIAIFHRVGAWTIRDRRINK", "text": "FUNCTION: Dolichyl-phosphate beta-glucosyltransferase involved in the glycosylation of glycoproteins through the synthesis of dolichyl beta- D-glucosyl phosphate which serves as a sugar donor for transfer of three glucose residues to the Man-9-GlcNAc-2-PP-dolichol precursor to N-glycans. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
+{"protein": "MPRYTVHVRGEWLAVPCQDAQLTVGWLGREAVRRYIKNKPDNGGFASVDDARFLVRRCKGLGLLDNEDPLDVALEDNEFVEVVIEGDAMSPDFIPSQPEGVYLYSKYREPEKYIALDGDSLTTEDLVSLGKGHYKIKLTPTAEKRVQKSREVIDRIVEEKTVVYGITTGFGKFARTVIPVSKLEELQFNLVRSHSSGVGKPLSPERCRMLLALRINVLAKGYSGISLGTLKQVIEVFNASCLPYVPEKGTVGASGDLAPLSHLALGLIGEGKMWSPKSGWADAKYVLAAHGLKPIVLKPKEGLALINGTQMITSLGCEAVERASAIARQADIVAALTLEVLKGTTKAFDTDIHAVRPHRGQVEVAFRFRSLLDSDHHPSEIAESHRFCDRVQDAYTLRCCPQVHGVVNDTIAFVKNIITTEINSATDNPMVFASRGETISGGNFHGEYPAKALDYLAIGVHELASISERRIERLCNPSLSELPAFLVAEGGLNSGFMIAHCTAAALVSENKALCHPSSVDSLSTSAATEDHVSMGGWAARKALRVIEHVEQVLAIELLAACQGIEFLRPLKTTTPLEKVYDLVRSVVRPWIKDRFMAPDIEAAHRLLVEQKVWEVAAPYIEKYRMEHIPESRPVSPTAFSLEFLHKKSTKIPESEDL", "text": "SIMILARITY: Belongs to the PAL/histidase family."}
+{"protein": "MITKQQVLEFLKDYDLDNITIATICSHSSLQIFDGARKEGFRTLGICVGKPPKFYDAFPRAKPDEYLVLEDYEDLINRAEELRKKNTIIIPHSSLIYYLGRENFTGMAVPTFGNRTSIEWESDRDKESRWFLGAGIQMPKKIDDPHDIKGPVMVEYEGAKGGKGFFVAKNYKEFSELVDHTQKYTIHEYINGTRYDLHYFYSPIRNDGYTLSKGSLELLSMDRRVESNADEIFRLGSPRELIESGICPTYVLTGNVPLVARESILSRIFSLGEQVVEESLALFGGITGAFCIEAVITDSLDIKVFELSSRIVSGTNLYISGSPYSDLMQKRLSTGRRIALEIKEAAKSNQLDKILS", "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": "MIRLIRWNNVQSLVFKRCLFVPSNSLTNKRKRRIPPSKPRSSNRKDGDIEPYRMTDQNQTPNTGSIARLPAEVKKELKDLRSFTKVIAQHLKPEQENDSLTSAEKPDTSQLPPIDIEEATDDIFGEISGTKKLSANAVPPPPPPPGLDIPDEIKERLGLLSELLVPAKTSNNKLPEKQVENNWKLLLSQLDQAGGLSGLSKRSVSKFFSKIPPKNLKNLIPMIENMYNKAEMSIPHPIYYMFVRSLTLGDKISDSQMQLINKYFQEISKQTDLKIDHYETMILAYVKNNHMEKIDGILAQMKKKNIEISKMIYTSIVRGYIFYQKDHQRALDTFDSMKFLSQKTQPDEKVYTDVIVSCVMHREIERALDLYYELKDKGMNVNQNLLSTLAKGCSRSKQFKTQAWNFLFQVYDHGWVPNLQTYEHMLYIAARDGDVELTRVLFYKMLQTNSVTIRAFRYLILSYSKYVPPHKRKEKHLILLNHKGQLFRQNILQDVDFSKPVHGFPFLPSSHIPDSKFVLAESSAIWAHTVMNNPSFLRQQTLVASYVSIALELGDFTEFKDRFDSASYLNTDGIPKVREIEIIEPRQDEPTEKATTTEEQNASSETDNNSLIRSPILNQLQQNINDNQFKAPRDSYLYNLAIKAAGKFKNYGFAQEILHERGQFRKSNSFKLLSPKQQNQDDFQFAGYLVECWTNMNLLEDAYAVVLSSVDRFPWSWRELGVLNNAAMKLGSLELAEAVRKVAQVTQVKHHGKIKRQDFKTYVMKRGY", "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": "MSKFSLKLGSKTLKKNISKKTKKKNSLQKANLFDWDDAETASLSHKPQSKIKIQSIDKFDLDEESSSKKKLVIKLSENADTKKNDAPLVEYVTEKEYNEVPVEEFGDALLRGMGWESDSEQDSKGDKTQSRNKDVSNVSQIHPDGLGIGAKLNKAINVEEASFMPVVKIDKITGTKVDDDKKNKS", "text": "FUNCTION: Involved in pre-mRNA splicing; specifically in the final stages of spliceosome maturation. Promotes the first step of splicing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SPP2 family."}
+{"protein": "DDTPSSRCGSGGWGPCLPIVDLLCIVHVTVGCSGGFGCCRIG", "text": "FUNCTION: Induces the nucleation and stabilization of vaterite, one of the crystalline polymorphs of calcium carbonate. Exhibits strong antimicrobial activity against Pseudomonas aeruginosa and Proteus vulgaris. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
+{"protein": "MSSEELACKLQRRLRLEVRAETDQGDPQPAPCDAPAGHPEPEPPARAPTASADSELNLKLSRRLDIHQGTARPGRSKVFNPYTEFPEFSRRLLKDLEKMFKTYDAGRDGFIDLMELKLMMEKLGAPQTHLGLKSMIKEVDEDFDGKLSFREFLLIFHKAAAGELQEDSGLLALAKFSEIDVALEGVRGAKNFFEAKAQALSCSSKFEAELKAEQEERKREEEARRLRQAAFRELKAAFSA", "text": "FUNCTION: Acts as a calcium sensor for mitochondrial flash (mitoflash) activation, an event characterized by stochastic bursts of superoxide production (By similarity). May play a role in neuronal differentiation (PubMed:16336229). SUBCELLULAR LOCATION: Mitochondrion inner membrane."}
+{"protein": "MKPSIVAKLEALHERHEEVQALLGDAQTIADQERFRALSREYAQLSDVSRCFTDWQQVQEDIETAQMMLDDPEMREMAQDELREAKEKSEQLEQQLQVLLLPKDPDDERNAFLEVRAGTGGDEAALFAGDLFRMYSRYAEARRWRVEIMSASEGEHGGYKEIIAKISGDGVYGRLKFESGGHRVQRVPATESQGRIHTSACTVAVMPELPDAELPDINPADLRIDTFRSSGAGGQHVNTTDSAIRITHLPTGIVVECQDERSQHKNKAKALSVLGARIHAAEMAKRQQAEASTRRNLLGSGDRSDRNRTYNFPQGRVTDHRINLTLYRLDEVMEGKLDMLIEPIIQEHQADQLAALSEQE", "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. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family."}
+{"protein": "MQFTTILSIGITVFGLLNTGAFAAPQPVPEAYAVSDPEAHPDDFAGMDANQLQKRGFGCNGPWDEDDMQCHNHCKSIKGYKGGYCAKGGFVCKCY", "text": "FUNCTION: Antimicrobial peptide that potently acts against several species of Gram-positive bacteria (PubMed:16222292, PubMed:19472324). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20508130). It does not disrupt cell membranes (PubMed:20508130). Is especially active against numerous clinical isolates of S.pneumoniae, including all 90 different serotypes and isolates resistant to clinically used antibiotics (PubMed:16222292). In vitro, shows considerable selectivity for bacteria over mammalian cells (PubMed:16222292). The peptide synthesized in D-amino acids does not show antibacterial activity (PubMed:19472324). In vitro, acts on voltage-gated potassium channels by moderately inhibiting mammalian Kv1.3/KCNA3 (IC(50)=2.8 uM), and moderately inhibiting others potassium channels (PubMed:25568977). SUBCELLULAR LOCATION: Secreted Host cell membrane. SIMILARITY: Belongs to the invertebrate defensin family. Type 2 subfamily."}
+{"protein": "MVADKSKKSKIEEKGEEENLEQIDAELVLSIEKLQEIQDDLEKINEKASDEVLEVEQKYNVIRKPVYDKRNEVIQSIPGFWMTAFLSHPALGDLLTEEDQKIFKYLNSLEVEDAKDVKSGYSITFHFTSNPFFEDAKLTKTFTFLEEGTTKITATPIKWKEGKGLPNGVNHDDKKGNKRALPEESFFTWFTDAQHKEDAGDEIHDEVADIIKEDLWSNPLTYFNNDADEEDFDGDDDGDEEGEEDDDDEEEEDGEE", "text": "FUNCTION: Acts as histone H2A/H2B chaperone in nucleosome assembly, playing a critical role for the correct expression of genes involved in root proliferation and patterning. Required with NRP2 for the maintenance of cell proliferation and differentiation in postembryonic root growth. Involved in both intramolecular and intermolecular somatic homologous recombination. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
+{"protein": "MDVVARLASQRAVVIFSKSTCCMSHAIKRLFYEQGVSPAIVEIDQDMYGKDIEWALARLGCSPTVPAVFVGGKFVGTANTVMTLHLNGSLKILLKEAGALWL", "text": "FUNCTION: May only reduce GSH-thiol disulfides, but not protein disulfides. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily."}
+{"protein": "MDFISKTIGLRLGYNKTHKLIWSLSKNNPIFIQTNHFLEYIIKNDPFFCGLILIDFQLMQYIVVHKNQLGNFSPLKNNLPNSINLFLKLKIATEIQSNFNSVFILEERLHFLFFKYLNKMKNLKMLNNLKIKVKIKFLNNPILEPQWIFYKLHQDLYKGINIRRALAKISSNVIKKGAEGVKIQIKGRINGVDKATVIVEEKGKMPLQNLSSEINYYSRALKTVYGLLGVKIWVFKGFLLK", "text": "SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
+{"protein": "MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCAASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF", "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. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrF/TusC family. SIMILARITY: Belongs to the DsrF/TusC family."}
+{"protein": "MADVSQRTQQAVDTAMAGAAEMSRYGRRLLNMLWDPEPTNDRSLNRPVWCLGCSYTNEPTTVDRPDQDASSTVRATLPTTPSTTTLPYPLKAVPTTPPESSSSSFSSSLAYDELLEDAGWPIAFLDDFESRVWMTYRSEFEPISKSNDPRASAALSFAMRLRTLADQGGFSSDTGWGCMIRSGQSLLANTLVICQLGRDWRRGKAARQEREILARFADDPRAPYSLHNFVRHGAVACGKFPGEWFGPSATARCIQALANSNESSLRVYSTGDLPDVYEDSFMAVAKPDGETFHPTLILVGTRLGIDKINQVYWEALTATLQMPQSVGIAGGRPSASHYFIGAQRSGDAYEPGSYLFYLDPHCTRPALPFHEDVDQYTSDDINTCHTRRLRRLHVRDMDPSMLIGFLIKDEDDWDMWKDSVKYVQGKTIINVADHDPARGMPAEREAAIDEVETLKGEFV", "text": "FUNCTION: Cysteine protease that plays a key role in cytoplasm to vacuole transport (Cvt) and autophagy by mediating both proteolytic activation and delipidation of ATG8. 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. The protease activity is required for proteolytic activation of ATG8: cleaves the C- terminal amino acid of ATG8 to reveal a C-terminal glycine. ATG8 ubiquitin-like activity requires the exposure of the glycine at the C- terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. In addition to the protease activity, also catalyzes deconjugation of PE-conjugated forms of ATG8 during macroautophagy: ATG8 delipidation is required to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS. SUBCELLULAR LOCATION: Cytoplasm Nucleus Preautophagosomal structure. SIMILARITY: Belongs to the peptidase C54 family."}
+{"protein": "MTSKTTASLLAICVACAASAIAGTALCADRRNAPAQAGAGAAAAVSGDAHEQPAAEAPAEEEEETPAVAATDGKLVLPNGQDITPDHMENGRWYTAEDIPTYKIAEEGAVDWATFSGYRRYSAECHVCHGPDGEGSTYAPALRKSVLTMGYYDFLEIAASGKQEVNTAANLVMPAFGTNKNVWCYIDDIYAYLLARGTGDLPRGRPAKREDKSDEFVAQEDSCMSG", "text": "SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MDVPAFRERLLRLAPKDPLVLAVSGGGDSVALALLVKEAGRQAVVAHLDHGLRPESPLDQAFVRALAERLGFPFFTERVEVARIAQARGENLEAVAREVRYAFLHRVAREVGARAILTAHTLDDQAETVLLQLLQGTARATGIREREGIVVRPLLAHTREELRAYLRARGEAWREDPTNQDPALDRNFLRLFVFPLLEERFPAAKRALARFAEARAEEEGVLERQAEARLLPDPRFFVPAFRAAPLLEAPLAVRRRALRRLLEKLGLRPEARLVLLLEEALRGRPQTLPGGVLARRKGGTLFLLPPRPRLPLPPGFRRPAPGDYLERPSGRKRLVDFLAEKGVPRELKPLWPVRAEGNRVVEVLGLYPPPPEEAHMAEALAEAASAFREGEVPVGAVLVLPGRVLRAHNRVEGLRDPTAHAEMLLLREAGPEARGGRLYVTLEPCLMCHHALAQAGVEVVYGAENLKEGALTRFGLPTRARGGVRERECAKLLRDFFARLREGCRSG", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family."}
+{"protein": "MGIMGTFLLLAAEANAVHSELAEGAAEGGFGLNLDIFETNLINLAILVGILFYFGRKVLSNILNERQSNIATAIQEAEGRLKEAKTALSQAQEQLKQSQAEAERIRQSAVENAQKAKEALLAKAVQDVERLKQTAAADLNTETERAIAQLRQRVATLALQKVESQLKGGIADDAQQSLIDRSIAQLGGNV", "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": "MPRRRRASRPVRRRRRPRVSRRRRRGGRRRR", "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": "MRRWFSKLGSTSLASTSRVTAFSSSESAAVEQLADSSIPPPITPFIIAKPDIHWNVDFASDPCSWESCFDAHWEAAEKLLENEEEISYEKVITVFQHLNCTVQLLMMEANAQPESAIGSILDRHFTHQIMERVVDWAIAAPHFLTPTCQVNMIGLYEVIVGESHTQNHCLLVHKPMLLPLLKLLDWCRKSAEKRNFTPSNTDRHFVLLLNQICTKLAEDTTLLHFFFDFDDDCDEQFLVFSLLIPYLYDSGEVGQLARDALLLILSVSRRLKRVATFIAVKSNFCPVVATGLSGCFSQLSRSFGSMLYVSDSWHKINADDIDSYSSLLDFHSSLIFCNAVIQVAHGYVVSQVIRYVYHGFLLPVVLPSLLQGGQDELISSTAYYHLCLDSVTETVLVQTIVKLLLNESCESNKTVLDVIVERISAGNRLSQVSLSLVRTLIDLRCEDIMFDLVFKYLLPCTFLQPNQTLHLKNQMYVRTAAQTLLTFVPECTYKSSALCSQETLHIYLSECRNYVQETTDACCEKWVWSYDGRSPFFMPKINSDEESATNSNGAFVRHSSVRSSMASARNGLNRYFVSRNAHITADSLRQHTPPPELGEQESSSRSSFPYDIADSSLVLDDEGDELIIPALTPTSLMMMTSSSDYFQFAYGELSETDTEAINPSVVSMSGAPAQSISDKASLASTSANCDTDIEMARSFVLRGWGQIEDTDTFMALMDRVPASKIKHSLEENMALIDSRIQYLEELKAEAKLQDLESDGFKSDTNNDNDDEDPAPLGKPIECFGNQGVGPFLESIMRSLENMLDNSLYVTLQTTSVLAALASYPQPLIAHYLFDQRMLLQPNVKNLFKVMDSLKTQIDAYASSLDGFDVLLERGIKFLRSRAERYEKVVESSRRLRSSESFSRNGNMEGRSSSRGLFNRFRSSNNKRLYPSNDSSHPHEFRIYTHKAIESRDVTLDHARAKQFVFAAIILSQFCQELAATVLQHSTVVPRPKVSPAKDYLRREVNSAGKDANCCAD", "text": "SIMILARITY: Belongs to the FHIP family."}
+{"protein": "MALPHDSNETSYLLPPNNEDWDRQAIPDFVYGQKDLMAEGIQWPRNAPGVLEALPQSPFDAALCSAWKQRVELGLFRYRLRELQTQILPGVVGFVAQLNVERGVQRRRPQTIKSVRQAFDPEQFNFNKIQPGEVLYRLHREPDLPGTLLQEDILVVINVSPLEWGHVLLVPEPARGLPQRLLPGALRAGIEAVLLSLHPGFRVGFNSLGGLASVNHLHLHGYYLAHRLPVEQAPSEPLDPGGHLHLLQGLPAPGFLFYTRGPGLDLESLICRVCRATDYLTDHEIAHNLFVTRGAPPGKTSPSSALTGVRVILWARKSCFGIKDGEAFNVALCELAGHLPVKTSQDFSSLTEAAAVALIQDCRLPPSQAEEVQAALVALMSQKEQ", "text": "FUNCTION: Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GDPGP1 family."}
+{"protein": "MTQEKKAEDLERGTDATSAVPRLWSTHCDGEVLLRLSKHGPGHETPMTIPELFQESAERFSAYPALASKNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVENDQQLQKILLIPPDKMETVKAIVQYKLPLMESMANLYSWNDFMELGNDIPNIQLDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDALRGTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLGLKVNTKRMLGKRDIPMNYRMAKALVFAKVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQNKEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETLVKEKIPIISHAMLVGDKAKFLCMLLTLKCETDRKSGEPLNKLSVEAKSFCQMLGSQATTVSDILKSRDQVVYTAIQYGIDIVNQQAMSDSHRIRKWIILEKDFSIQGGELGPTSKLKRSVITQKYKAQIDSMYLS", "text": "FUNCTION: Catalyzes the conversion of fatty acids such as long chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids. Has increased ability to activate oleic and linoleic acid. May play a role in spermatogenesis. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. Bubblegum subfamily."}
+{"protein": "MKISFLLLLAIVICSIGWTEAQFTNVSCSASSQCWPVCKKLFGTYRGKCMNSKCRCYS", "text": "FUNCTION: Potent blocker of both large-conductance calcium-activated potassium channels (KCa1.1/KCNMA1) and voltage-gated potassium channels (Kv1.3/KCNA3 and ERG1/Kv11.1/KCNH2). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 01 subfamily."}
+{"protein": "MAGRRAMRPSGSSMRGVVARLAAARSPAVSFLVAAAAGAALVGGVYFWLVVSSFRLPDSRAVGCLPDGEGSWAIGMYYGKSPLELRPIELEGRSNGNSSAWPVANPVLTCATPTEGGYPSNFVADPFLYVQGDTLFLFFETKTVSTMQGDIGVARSLDQGATWEFLGIALDEAWHLSYPFVFKYENEIYMMPEGNKKKELRLYRATKFPLEWTLEKVLIDKPLIDSSLVQYDGLWWLFASDFTRHGIEKNAELEIRYSNSPLGPWSEHKQNPIYRSDKSLGARNGGRLFIFEGSLYRPGQDCSGTYGRKVKLYKIEKLTKEEYKEVPVNLGIEEAKKGRNAWNGMRYHHIDAQQLASGGWVAVMDGDRVPSGDSTRRSLFGYMGFLVAVALVTFVGFVKGAISCYIPPSFWVPLTRRSELSRILPVHRFNLKIRRYSTSIGRNISATKARLSEKTWSNTLFFCVIALIGIVNVCIAVHFLLGGNGAEEAYTHQGQHSQFTMVTMTYEARLWNLKLFVEHYSRCESVREIVVVWNKGNHPTSDAFDSTVPVRIRVEEINSLNNRFRGDPLIKTRAVLELDDDIMMTCSDVEKGFKVWREHPERMVGFYPRMIDGDPLQYRNERYARGKKGYNLILTGAAFMDSEFAFSKYWSQEAKEGRDYVHKNFNCEDLLMNFLYANASSSRTVEYVHPAWAIDTSKLSSVAISRDTQKHYDIRTKCLAKFASIYGPLPQKWLFGMREDGWDK", "text": "FUNCTION: Essential protein. Glycosyltransferase that mediates the glycosylation of glycosylinositol phosphorylceramides (GIPCs), the major sphingolipids in the plasma membrane; acts as a HexN(Ac)-specific GIPC sugar transferase. Responsible for the glycosylation of a subgroup of GIPCs found in seeds and pollen that contain GlcNAc and GlcN (GlcN(Ac)). Maybe involved in the maintenance of cell-cell adhesion. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 64 family."}
+{"protein": "MINGEQTMVEDELPDQGKPMSDESADIDIKDLKVGESIGSGAYGIVYRGTLFNSDVAIKKIQNEKSEKNEFIKYLKREVAVLKNIQHPNIVQFIGVYYEPLASPSLVNRLLNSSSTWIVTEYIGGGNLHERIKDTKKDFPIELRIKLSLDIALAMAYLHSRDIIFRDLKSKNILIDDSSSPIRGKVCDFGFARILNKKQQGNRHLSICGTDSIMAPELILGMEYDESVDIFSFGVVLLEMILRKKVSKVLERGPQSAFEIDQDSARQLIPDDIPVLYSDLALDCIKYQPEERPNFSHIIHVLKQLTSLFPVVHTFDNPLSPTSSPITPRKNSLNSPFTKSMRMNSFDFNLSNIVSSTSVQNNLKSQNLNFTLLNLNQINNQDLNENNNNNISNNINNINNNNNNLNDCNSNLSSSTSTIYNDSQQTIIDEDELDKEEEENRNKVNNLKEKMLLVMGEFDIYINKVGKELLLVSEEDHISQKYDECRKVIEIKKVLGEVIESDMSNSQQSNTPRKNSNVTNSRVALFLKSMERSLNEIYSSSDVLKQRIVKEDDLVESLLLARVVSKIKKIHLSSLDINN", "text": "SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family."}
+{"protein": "MLVIKELKIDGIGGINSLKLNFNEGLNLICGPNGVGKTTILESIGHMFSNGSRSKVKRNVKFDQGSCEISYSTFLDTIHTQSCILRNYEENDSLDWHGGNANLAKEVIVFKAQRSFTYTQLDSLRKDTETSDGKFLDDSMNGIQFFDFKNWFIHRFLFSHVDNELTTVQKENFKLATDCFGILDNSIRFSSVKSDTFDIIISTSNGEIYFEYLSSGFKSCIYIIHGLIKEIEYRFKNDGGIKVQDYEGLILIDELDLHLHPQWQAKMIYLIKHILPKAQIIATTHSPHMVQAAAINELIALGIDEDADVYVRQLPNVQYGFQGWTVEEILEDVMGLDETRSPMYIEAITEFEKSLDEENEEKIFEAYYKLDLMLHPSNPLRKLLKLQVAQFGRVIE", "text": "FUNCTION: Component of antiviral defense system Septu type I, composed of PtuA and PtuB. Expression of Septu type I in B.subtilis (strain BEST7003) confers resistance to phages SBSphiC and SBSphiJ (PubMed:29371424). May be an ATPase (Probable)."}
+{"protein": "MKFALVLLGVCAFYLVNATGDLETELEASELQELQEALDLIAETPLESLEAEELEEARKFKLPKINWGKLASKAKDVYKKGQKLAKNKNVKKALKYGKQLAENLAAGEVHEPGTPVGNNKCWAIGTRCTDDCDCCPEHHCHCPAKSWTFGLIPCSCQVTESDKVNKCPPAE", "text": "FUNCTION: Has antimicrobial, insecticidal, cytolytic and cytotoxic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the spiderine family. Cationic/spiderine subfamily."}
+{"protein": "MSDQKDQMIDITVDFSGGLEILFSNQKHHALSVPAQDAQGKPANVGFLINYLCQTLMTDPRADLFVLGGELRPGILCLINDCDWELEEEDAYVLQPGDNILFISTLHGG", "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 the MOCS3 homolog nit-1/uba4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as ahp1. 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": "MATCSRQFTSSSSMKGSCGIGGGSSRMSSVLAGGSCRAPSTYGGMSRFSSAGAYAVGSGYGGGFSSSSFGGGFGGGIGGGIGGGLGGGIGGGFGGGIGGGFGGGIGSGFGGGLGDGLLVGSEKVTMQNLNDRLATYLDKVRALEEANSDLEVKIRDWYQRQRPTEIKDYSPYFKTIEDLKSKILAATVDNANVLLQIDNARLAADDFRTKFETEQSLRINVESDINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMASMRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEDWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENNLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLSSAQFSSSSQFSSGSQSSRDVTSTNRQIRTKVMDVHDGKVVSTHEQVLRTKN", "text": "FUNCTION: The nonhelical tail domain is involved in promoting KRT5- KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Expressed in both as a filamentous pattern. SIMILARITY: Belongs to the intermediate filament family."}
+{"protein": "MGRGRVQLKRIENKINRQVTFSKRRAGLLKKAHEISVLCDAEVALVVFSHKGKLFEYSTDSCMEKILERYERYSYAERQLIAPESDVNTNWSMEYNRLKAKIELLERNQRHYLGEDLQAMSSKELQNLEQQLDTALKHIRSRKNQLMHDSINELQRKEKAIQEQNSMLSKQIKEREKILRAQQEQWDQQNHGHNMPPPPPPQQIQHPYMLSHQPSPFLNMGGLYQEEDPMEMRRNDLDLSLEPVYNCNLGCFAA", "text": "FUNCTION: Controls floral meristem identity. Is also required for normal development of sepals and petals. Is required for the transition of an influorescence meristem into a floral meristem. Interacts with LEAFY (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MPRHGVSPGQGLPRSGREQASDRSLGAPCLRLLWLGLALALALPNSPVLWSPAEARPLPTQGHPAKFIRIAPQLQEAFGWWNLTCPTCKGLFTAIDFGLRNQASVAWVGSVAIKLCVLLKIAPPAVCQSAVQLFEDDMVEVWTRSVLSPSEACGLLLGSSCGHWDIFSSWNISLPAVPKPPPQPPKPPAPGSPVSRVLFLTDLHWDHDYLEGTDPNCENPLCCRRDSGPPPASQPGAGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHNIWQQSRQDQLRALTTITALVKKFLGPVPVYPAVGNHESTPVNGFPPPFIKGNQSSHWLYEAMAEAWEPWLPAEALRTLRIGGFYALSPRPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGHCLKSWSWNYYRIVERYENTLAGQFFGHTHVDEFEVFYDEETLSRPLSVAFLAPSATTYIGLNPGYRVYQIDGNYSGSSHVVLDHETYIMNLTEANEPGATPHWYLLYRARETYGLPNALPTAWHDLVYRMRKDTQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSARSDSPALCRHLVPDASLPDVQSLWSMPLLC", "text": "FUNCTION: [Sphingomyelin phosphodiesterase, processed form]: This form is generated following cleavage by CASP7 in the extracellular milieu in response to bacterial infection (By similarity). It shows increased ability to convert sphingomyelin to ceramide and promotes plasma membrane repair. Plasma membrane repair by ceramide counteracts the action of gasdermin-D (GSDMD) perforin (PRF1) pores that are formed in response to bacterial infection (By similarity). FUNCTION: When secreted, modulates cell signaling with its ability to reorganize the plasma membrane by converting sphingomyelin to ceramide. Secreted form is increased in response to stress and inflammatory mediators such as IL1B, IFNG or TNF as well as upon infection with bacteria and viruses. Produces the release of ceramide in the outer leaflet of the plasma membrane playing a central role in host defense. Ceramide reorganizes these rafts into larger signaling platforms that are required to internalize bacteria, induce apoptosis and regulate the cytokine response in infected cells. In wounded cells, the lysosomal form is released extracellularly in the presence of Ca(2+) and promotes endocytosis and plasma membrane repair. FUNCTION: Converts sphingomyelin to ceramide. Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly. However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form. FUNCTION: In the lysosomes, converts sphingomyelin to ceramide. Plays an important role in the export of cholesterol from the intraendolysosomal membranes. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2- diacylglycerolphosphoglycerol. Modulates stress-induced apoptosis through the production of ceramide. SUBCELLULAR LOCATION: Lysosome Lipid droplet Secreted Note=The secreted form is induced in a time- and dose-dependent by IL1B and TNF as well as stress and viral infection. This increase of the secreted form seems to be due to exocytosis of the lysosomal form and is Ca(2+)-dependent. Secretion is dependent of phosphorylation at Ser-504. Secretion is induced by inflammatory mediators such as IL1B, IFNG or TNF as well as infection with bacteria and viruses. SUBCELLULAR LOCATION: [Sphingomyelin phosphodiesterase, processed form]: Secreted, extracellular space Note=This form is generated following cleavage by CASP7. SIMILARITY: Belongs to the acid sphingomyelinase family."}
+{"protein": "MRRCPCRGSLNEAEAGALPAAARMGLEAPRGGRRRQPGQQRPGPGAGAPAGRPEGGGPWARTEGSSLHSEPERAGLGPAPGTESPQAEFWTDGQTEPAAAGLGVETERPKQKTEPDRSSLRTHLEWSWSELETTCLWTETGTDGLWTDPHRSDLQFQPEEASPWTQPGVHGPWTELETHGSQTQPERVKSWADNLWTHQNSSSLQTHPEGACPSKEPSADGSWKELYTDGSRTQQDIEGPWTEPYTDGSQKKQDTEAARKQPGTGGFQIQQDTDGSWTQPSTDGSQTAPGTDCLLGEPEDGPLEEPEPGELLTHLYSHLKCSPLCPVPRLIITPETPEPEAQPVGPPSRVEGGSGGFSSASSFDESEDDVVAGGGGASDPEDRSGSKPWKKLKTVLKYSPFVVSFRKHYPWVQLSGHAGNFQAGEDGRILKRFCQCEQRSLEQLMKDPLRPFVPAYYGMVLQDGQTFNQMEDLLADFEGPSIMDCKMGSRTYLEEELVKARERPRPRKDMYEKMVAVDPGAPTPEEHAQGAVTKPRYMQWRETMSSTSTLGFRIEGIKKADGTCNTNFKKTQALEQVTKVLEDFVDGDHVILQKYVACLEELREALEISPFFKTHEVVGSSLLFVHDHTGLAKVWMIDFGKTVALPDHQTLSHRLPWAEGNREDGYLWGLDNMICLLQGLAQS", "text": "FUNCTION: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5- trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis (PubMed:11085927, PubMed:12747803). Can phosphorylate inositol 2,4,5- triphosphate to inositol 2,4,5,6-tetraphosphate (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles actively between nucleus and cytoplasm with both nuclear import and nuclear export activity. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family."}
+{"protein": "MDAPSTTPHDAVFKQFLMHAETARDFLEIHLPVELRELCDLNTLHLESGSFIEESLKGHSTDVLYSVQMQGNPGYLHVVIEHQSKPDKKMAFRMMRYSIAAMHRHLEADHDKLPLVVPILFYQGEATPYPLSMCWFDMFYSPELARRVYNSPFPLVDITITPDDEIMQHRRIAILELLQKHIRQRDLMLLLEQLVTLIDEGYTSGSQLVAMQNYMLQRGHTEQADLFYGVLRDRETGGESMMTLAQWFEEKGIEKGIQQGRQEVSQEFAQRLLSKGMSREDVAEMANLPLAEIDKVINLI", "text": "FUNCTION: A low activity DNA endonuclease yielding 3'-hydroxyl ends (Probable). Upon expression enhances RecA-independent DNA recombination 2.9-fold, concomitantly reducing viability by 59% and inducing DNA damage as measured by induction of the SOS repair response. SIMILARITY: Belongs to the Rpn/YhgA-like nuclease family."}
+{"protein": "MSVNINYLLLIPEILVLSLGILLFVLALITPRNLQKGIGYLTTIGLLGIFLYMPIAWKHTGMAIEGMYQVDKVAIFFKALSLLAGVFVTAIAPRYMEKIGYYSEFFVFAVFAVLGMMILVSATDFLTLYLGLELMTITFIILAAYRRDSAIGAEAGIKYLILAGVSSAILLYGLSLFYGLTRTLNIVDIAAIVTNNGISPAFVLAMVFVLAGFAFKISAVPFHMWAPDVYQGAPTPVTAFLATGSKAASFAIFFRFFYLAFPGIREHWVGLLATLAALTMVVGNLVAIPQTNLKRMLAYSSIAQAGYILVGFLATDFTGFKAIMFYLSVYLIATIGAFTVVTVYENVTGKEEIRDFAGLSQRSPIMAAVLVVSLLSMAGIPPLAGFAGKFYLFYPIIKNWGWLALLALIMSMVSVYYYLRVVLVVYRDEPEDQTPITLPNSIYFTLLITMAVTIVLGVYPTPLAKIAQQAAMIFMK", "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": "GYLGGYAAPAVAVAPAPALAVAHAPAVVVATSYARISQVTNSVPIAVAAPAVPKAAVPVAAPVVAAAPVIAAHAPLALGHGFGYGGYH", "text": "FUNCTION: Component of the cuticle of migratory locust which contains more than 100 different structural proteins."}
+{"protein": "MNVFFMFSLLFLAALGSCADDRNPLEECFRETDYEEFLEIARNGLKATSNPKHVVIVGAGMSGLSAAYVLSGAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFSQENDNAWYFIKNIRKRVGEVKKDPGVLKYPVKPSEEGKSAGQLYEESLGKVVEELKRTNCSYILNKYDTYSTKEYLLKEGNLSPGAVDMIGDLMNEDSGYYVSFPESLRHDDIFAYEKRFDEIVGGMDKLPTSMYRAIEEKVHLNAQVIKIQKNAEKVTVVYQTPAKEMASVTADYVIVCTTSRATRRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDEGIHGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHQLPREEIQTFCYPSMIQKWSLDKYAMGGITTFTPYQFQHFSEPLTASVDRIYFAGEHTAEAHGWIDSTIKSGLRAARDVNRASEQ", "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:11341935). Shows activity on L-Leu (PubMed:11341935). Exhibits diverse biological activities, such as apoptosis, and inhibition of agonist- and shear stress-induced platelet aggregation (SIPA). 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 induce hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
+{"protein": "MAATTPAQDVGVEIYLGPVWPAPSNSTPLALNLSLALREDAPGNLTGDLSEHQQYVIALFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAAADLILVADSLIEVFNLDEQYYDIAVLCTFMSLFLQINMYSSVFFLTWMSFDRYLALAKAMRCGLFRTKHHARLSCGLIWMASVSATLVPFTAVHLRHTEEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRALIRAHRHRGLRPRRQKALRMIFAVVLVFFICWLPENVFISVHLLQWAQPGDTPCKQSFRHAYPLTGHIVNLAAFSNSCLSPLIYSFLGETFRDKLRLYVAQKTSLPALNRFCHATLKAVIPDSTEQSDVKFSSAV", "text": "FUNCTION: G-protein coupled estrogen receptor that binds to 17-beta- estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells. SUBCELLULAR LOCATION: Nucleus Cytoplasm, perinuclear region Cytoplasm Cytoplasm, cytoskeleton Cytoplasmic vesicle membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein Early endosome Recycling endosome Golgi apparatus, trans-Golgi network Golgi apparatus membrane; Multi-pass membrane protein. Cell projection, dendrite. Cell projection, dendritic spine membrane; Multi-pass membrane protein. Cell projection, axon Postsynaptic density Mitochondrion membrane; Multi-pass membrane protein. Note=Endocytosed in an agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer- associated fibroblasts (CAF) (By similarity). Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MENRCLPKKVPGFCSFRYGLAILLHFCNIVIMAQRVCLNLTMVAMVNKTEPPHLSNKSVAEMLDNVKNPVHSWSLDIQGLVLSSVFLGMVVIQVPVGYLSGAYPMEKIIGSSLFLSSVLSLLIPPAAQVGAALVIVCRVLQGIAQGAVSTGQHGIWVKWAPPLERGRLTSMTLSGFVMGPFIALLVSGFICDLLGWPMVFYIFGIVGCVLSLFWFILLFDDPNNHPYMSSSEKDYITSSLMQQVHSGRQSLPIKAMLKSLPLWAIILNSFAFIWSNNLLVTYTPTFISTTLHVNVRENGLLSSLPYLLAYICGIVAGQMSDFLLSRKIFSVVAVRKLFTTLGIFCPVIFVVCLLYLSYNFYSTVIFLTLANSTLSFSFCGQLINALDIAPRYYGFLKAVTALIGIFGGLISSTLAGLILNQDPEYAWHKNFFLMAGINVTCLAFYLLFAKGDIQDWAKETKTTRL", "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": "MEKYEKLEKVGEGTYGKVYKALEKSTGQVVALKKTRLEMDEEGVPPTALREVSLLQMLSQSLYVVRLLSVEHVDCAKNGKPLLYLVFEYLDTDLKKFIDSHRKGPNPRPLPPQQIQSFLFQLCKGVSHCHAHGVLHRDLKPQNLLLDKDKGVLKIADLGLARAFTVPLKSYTHEIVTLSYRAPEVLLGSSHYSTAVDMSSVGCIFAEMVRRQALFPGDSEFQQLLHIFRLLGTPSDEQWPGVSSLRDWHVYPQWEPQNSAPAVPSLGPDGLDLLTKTLKYDPADRISAKAALDHPYFDTLDKSQF", "text": "FUNCTION: Plays a key role in the control of the eukaryotic cell cycle. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "GWRDWLKKGKEWIKAKGPGIVKAALKAAVQ", "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": "MVDHLANTEINSQRIAAVESCFGASGQPLALPGRVLLGEGVLTKECRKKAKPRIFFLFNDILVYGSIVLNKRKYRSQHIIPLEEVTLELLPETLQAKNRWMIKTAKKSFVVSAASATERQEWISHIEECVRRQLRATGRPPSTEHAAPWIPDKATDICMRCTQTRFSALTRRHHCRKCGFVVCAECSRQRFLLPRLSPKPVRVCSLCYRELAAQQRQEEAEEQGAGSPGQPAHLARPICGASSGDDDDSDEDKEGSRDGDWPSSVEFYASGVAWSAFHS", "text": "FUNCTION: May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8. SUBCELLULAR LOCATION: Nucleus Cytoplasm, perinuclear region Lysosome Note=Translocates to lysosome during apoptosis."}
+{"protein": "MKSMDKISTGIAYGTSAGSAGYWFLQWLDQVSPSQWAAIGVLGSLVLGFLTYLTNLYFKIREDRRKAARGE", "text": "FUNCTION: [Isoform Antiholin]: Counteracts the aggregation of the holin molecules and thus of pore formation. FUNCTION: [Isoform Holin]: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of nanometer-scale pores (pinholes) causing host cell membrane depolarization and endolysin refolding and release into the periplasmic space (PubMed:19861547, PubMed:17827300, PubMed:23671069). Once the pinholin has permeabilized the host cell membrane, the SAR- endolysin is released into the periplasm and breaks down the peptidoglycan layer (PubMed:19861547, PubMed:17827300). Determines the precise timing of host cell lysis (PubMed:23671069). Participates with the SAR-endolysin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles from the host cell (Probable) (PubMed:17827300). SUBCELLULAR LOCATION: Host cell inner membrane; Multi-pass membrane protein Note=Classified as a class II holin."}
+{"protein": "MAWNQPGNNGQDRDPWGSSKPGGNSEGNGNKGGRDQGPPDLDDIFRKLSKKLGGLGGGKGTGSGGGSSSQGPRPQLGGRVVTIAAAAIVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTNPEKYLYSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSDTQRELEETIRPYDMGITLLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVARFAKLLPEYKAAPEITRERLYIETMEKVLGNTRKVLVNDKGGNLMVLPLDQMLKGGNAPAAKSDNGASNLLRLPPASSSTTSGASNTSSTSQGDIMDQRRANAQRNDYQRQGE", "text": "FUNCTION: HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. FUNCTION: HflC and HflK govern the stability of phage lambda cII protein and have been proposed to encode or regulate a cII-specific protease. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the band 7/mec-2 family. HflK subfamily."}
+{"protein": "MAQYTVDSFIVELGFSEKVVKGLQRVEKMSMQAAQRIERNINKAFDVKPNKSSQEALNRIVKNAQSASGRINKALNSSFNLDSQGVKSLKKLETQAKKTAKGINKSLKDAMKVDGKITIKTGRGRGGQSIPPVGGGAPRGQRVDVAQRQMERMFNNNFYSGLTRRLETIGGQGNQMAASFRGSLQNIYNRYKGTGKVGEYEMEVKKLIDVTKRWVIAENARLKSVKESAWLQDRANASLRQLVGGFVSAYALLELSQKTIEAGVKRQSAQLASTAIFGADTQQARMFAASFAHQIGQNYTDTMKQYSNFAAGAQPTLGFQGTQEFYKNAAMFARIRGATDEDLKGIMVAFQQMASKGKIQAEELRGQLGDRLAGAVQLFADAIGKTPQELDKLMKDGKLLAQDVLPKVSERMAELVKQAGGMNAVSKQTATSMGQAKAMWDNTLVALFNNSSEGISQLSNSVAMFLQGSMGSTQALGLVIGNLLKGAGNLLDFVTDFMYRTSALYYYARAWYKDLDNSQQKLIKSAGEFLGTVVTIGGAVAVVSKSVKLLSGLVGGGIFGKILQRLGVSAAGTAAAGEAAAAAGGVTATRMALGTVGSALMLRGSTDPNAAKNYSEVTLPKPFENAVANITNPKRPMFFDENGQLQFAQYTQDVEGNRKLIDNGLSNWEIIMEKLSTSIDNFANKFNQTPMMMTPSGLPMQTKQTLNVTFNLDGKQIATKMVDITDKNQEDILLSSSYPEEE", "text": "FUNCTION: Serves as a base for tail tube protein polymerization and acts as a template for tail length determination. SIMILARITY: Belongs to the Mulikevirus tape measure protein family."}
+{"protein": "MADGVDHIDIYADVEEEFNQESDYPVHDQIDLYDDVISPSANNGDAPEDRDYLDSLPAPGGNEGSKGAPANVVYTYNGKRIALYIGNLTWWTTDEDLTDAIRSIGINDVLEIKFFENRANGQSKGFALVCVGSDSSSRKLMDLLSKRELHGQNPIVTPCNKQSLSQFEMQSRKSTQSGQMSGEGKAGPPGSGSRGGGFPPGKGQRRFPGPPGQGDRFPGPVGPGGPPPHFPGMQGPPRLPSGPPGPLGPPGPPPPGQGLPPPLGGPPNRGDRPPPPVLFPGQFGQPPMGPMPPGPPPPGYGPPPGPPPPQQGPPPPGPFPPRPPGPLGPPLGLAPPPHMQGPPPGGPPPAPHVNPAFFPPPGNNMPSSDGRGPPPGDPYGRPPPYDRDFPGGRDMDASRTPLSEAEFEEIMNRNRAISSSAISRAVSDASAADYGSAIETLVTAISLIKQSKVSADDRCKVLISSLQDCLHGIESKSYGSVAGRRERSRERDHSRSREKSRRHKSRSRDRHEDYYRERSRERDRHRERDRDRERDREREREYRHR", "text": "FUNCTION: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA- 3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. Plays a role in mRNA export. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Nucleus speckle Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the RRM CPSF6/7 family."}
+{"protein": "MAAVRVLVASRLAAASAFTSLSPGGRTPSQRAALHLSVPRPAARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPSEGESRNVLTESARIARGKITDLANLSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIGLCCIAPVLAAKVLRGVEVTVGHEQEEGGKWPYAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCETALHYIHDGIGAMVRKVLELTGK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GATD3 family."}
+{"protein": "MWTARLSSIAVLTQVVGTWADTITLNWEITWVNAAPDGFHRPVIGVNGKWPCPPIHATVGDTVVINMKNSLGNQTTGLHFHGINQLDTNYMDGASMVNSCPVVPGSSMTYSFTADEPGTYWYHSHNMAQYPDGLRGPLIIHDDNDPFDGEFDNEVILTISDWYHQQTLTLVQNMLVSSNDQWRPPLPDGMIVNEGGNTDIELDIGTTTRVRILNFGALTAFMLRFGSRDMDVIMTDASYVQRETIHQLRIAPGQRYDVLVSATKKDKGKNIPYLISMDLNRDFTVSGTWTFNQTGYLITDAKAPCTAKEVVQQWRPFDEALFTPLDEMPLLGPLDRTWTLNFALCKDMNNIPRMCFNDQTYVMQKTPTLYTAATVGNANTDPSVYGAVLPFIIEYGDVLEIVINNLDPAIHPFHLHGHQFQVVERPESGSGSFDGSSTANPVPPRRDVISINGGSYARLRITADNPGVFLFHCHIEWHVEMGLTATLIEAPEMLDGYDIPQAMIDSCKAQGYPVAGNAAGDTINVWDDSGYLTDPPSTYSGSQWPVPKGGNSQKSRPRRKPSGQSSQTRQISNMSGEFQHRITW", "text": "FUNCTION: Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment forming a dark layer in the conidial wall that protects the conidia from UV radiations (PubMed:28517364). The first step of the pathway is the production of the pentaketide 1,3,6,8- tetrahydroxynaphthalene (1,3,6,8-THN or T4HN) by the polyketide synthase PfmaE though condensation of acetyl-CoA with malonyl-CoA. T4HN is not stable and easily oxidizes into the stable form flaviolin (PubMed:28517364). T4HN is also substrate of the hydroxynaphthalene reductase PfmaG to yield scytalone (PubMed:28517364). The scytalone dehydratase PfmaJ then reduces scytalone to 1,3,8-THN (PubMed:31116900). 1,3,8-THN is then substrate of the hydroxynaphthalene reductase PfmaI to yield vermelone (Probable). Vermelone is further converted by the multicopper oxidase PfmaD to 1,8- DHN (Probable). Finally the laccase PFICI_06862 transforms 1,8-DHN to DHN-melanin (Probable). The roles of the 5-oxoprolinase PfmaA and the proline iminopeptidase PfmaB within the cluster have not been elucidated yet (Probable). SUBCELLULAR LOCATION: Secreted Cell surface. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "MNTAGRLLLLCLALGLVFESLGIPVADDVEAVRDTDPDEKDPSVHNSLKAVYGDCGGERCRFGCCKTDDGEEKCQHFGCP", "text": "FUNCTION: Probable toxin with unknown function (Probable). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin H superfamily."}
+{"protein": "MSVADKPFVRTSILAAEPPPPGERGAVAWIRRNLLATPKDVILTILALALIAWAVPHLVNWLFIQAVWSGPDRTFCATTLQGGIQPDGWSGACWAFISAKYDQFIFGRYPLGERWRPAIVGILFILLLVPMLIPSAPRKGLNAILLFAVLPVIAFWLLHGGFGLEVVETPLWGGLMVTLVLSFVGIAVSLPVGILLALGRRSRMPVIRMLCVTFIEVIRGVPLITVLFMASVMLPLFLPTGWNVDKLLRALIGVSIFTSAYMAEVIRGGLQAIPKGQFEGADSLGLGYWQKTRLIIMPQAIKLVIPSIVNTFIGTFKDTSLVTIIGMFDLLGIVKLNFSDANWASAVTPITGLIFAGFIFWLFCFGMSRYSGFMERHLDTGHKR", "text": "FUNCTION: Part of a binding-protein-dependent transport system for L- amino acids, affects the uptake as well as efflux of these amino acids. 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": "MSSAILLGVGIAATAAAGKIGVDAFRKYRNLNGGVKAFLKGGFESKMSRAEAIQILSLNNRTLTRQKIKEAHRRLMLANHPDRGGSPYVASKVNEAKSLLDADRSIRKFSSWALPVSKQRSMPSVLEAVKWLEYSSIPKA", "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": "MGQADISRPVNPDGVEEIGQPTADLGMVMDCVEAGDITPPTKRKSKFSGFGKIFKPWKWRKKKSDKFKETSEVLERKISMRKPREELVKRGLLLEDSEQGGEDPGKLSHATLKNGHTTLIGSTRSSSPVQVEEESERIASLRKPVPEEEPKKRLGSSGSQPHSEAEFVPESIPKQPLLPPKRHLSSSHEANEGQAKDATSSGSLARPSSSASTTAITTAPAATMAATNPAKTVHSSGPPSQAPRTLPAAPASTHTTATLSLTHTGPAKQPPIPPPKPTHRNSNPVIAELSQAINSGTLLSKPSPPLPPKRGIPSALVPTSESAAATTATKAPSDQREKSACSVGSEPLLTPSSSPLPAHIPPEPPQSPPFPAKTFQVVPEIEFPPSLDLPQEIPQQESQKREVPKRMLDHSFGEPQVPPRLPPVPLHIRIQQALTSPLPVTPPLEGSHRAHSLLFENSDNFSEDSSTLGRTRSLPITIEMLKVPDDEEEEEQSHIFAFDEDVASTSVIPKLPQCLQEEEEGKESDSDSEGPIQYRDEEDEDESHHSALANKVKRKDTLAMKLNHKPSEPEMNMNSWPRKSKEEWNEIRHQIGNTLIRRLSQRPTPEELEQRNILQPKNEADRQAEKREIKRRLTRKLSQRPTVAELLARKILRFNEYVEVTDAHDYDRRADKPWTKLTPADKAAIRKELNEFKSSEMEVHEDSKHFTRYHRP", "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": "MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAILINIGPETYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKAVVTPRRAAVAIAGCWILSLVVGLTPMFGWNNLREVQRAWAANGSVGEPVIKCEFEKVISMEYMVYFNFFVWVLPPLLLMVLIYLEVFYLIRRQLSKKASASSGDPHKYYGKELKIAKSLALILFLFALSWLPLHILNCVTLFCPSCQKPSILVYTAIFLTHGNSAMNPIVYAFRIHKFRVTFLKIWNDHFRCRPAPAGDGDEDLPEEKPND", "text": "FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "IEFFA", "text": "FUNCTION: Shows neither neuropeptide activity nor antibiotic activity. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MTSGSLQFTVLRAVNPATDAQRESMLREPGFGKYHTDHMVSIDYAEGRGWHNARVIPYGPIELDPSAIVLHYAQEVFEGLKAYRWADGSIVSFRADANAARLRSSARRLAIPELPDAVFIESLRQLIAVDKAWVPGAGGEEALYLRPFIFATEPGLGVRPATQYRYLLIASPAGAYFKGGIAPVSVWVSTEYVRACPGGTGAAKFGGNYAASLLAQAEAAENGCDQVVWLDAVERRYIEEMGGMNIFFVLGSGGSARLVTPELSGSLLPGITRDSLLQLAIDAGFAVEERRIDIDEWQKKAAAGEITEVFACGTAAVITPVARVRHGASEFRIADGQPGEVTMALRDTLTGIQRGTFADTHGWMARLG", "text": "FUNCTION: Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val. FUNCTION: Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MASGKATGKTDAPAPIIKLGGPKPPKVGSSGNASWFQSIKAKKLNSPQPKFEGSGVPDNENIKTSQQHGYWRRQARFKPGKGGRKPVPDAWYFYYTGTGPAADLNWGDTQDGIVWVAAKGADVKSRSNQGTRDPDKFDQYPLRFSDGGPDSNFRWDFIPLHRGRSGRSTAASSAASSRAPSRDGSRGRRSGSEDDLIARAAKIIQDQQKKGSRITKAKADEMAHRRYCKRTVPPGYKVDQVFGPRTKGKEGNFGDDKMNEEGIKDGRVTAMLNLVPSSHACLFGSRVTPKLQPDGLHLRFEFTTVVPRDDPQFDNYVTICDQCVDGIGTRPKDNEPRPKSRPSSRPATRGNSPAPRQQRPKKEKKPKKQDDEVDKALTSDEERNNAQLEFDDEPKVINWGDSALGENHL", "text": "FUNCTION: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. SUBCELLULAR LOCATION: Virion Host endoplasmic reticulum-Golgi intermediate compartment Host Golgi apparatus Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. SIMILARITY: Belongs to the gammacoronavirus nucleocapsid protein family."}
+{"protein": "MASPSRRLQTKPVITCFKSVLLIYTFIFWITGVILLAVGIWGKVSLENYFSLLNEKATNVPFVLIATGTVIILLGTFGCFATCRASAWMLKLYAMFLTLVFLVELVAAIVGFVFRHEIKNSFKNNYEKALKQYNSTGDYRSHAVDKIQNTLHCCGVTDYRDWTDTNYYSEKGFPKSCCKLEDCTPQRDADKVNNEGCFIKVMTIIESEMGVVAGISFGVACFQLIGIFLAYCLSRAITNNQYEIV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MTVLSEQDKIRLLADIVKIQTENDHEIEVCEYLKDLLSQYDIDSKIVKVNDSRANLVAEIGSGAPVLAISGHMDVVDAGDHDDWTFPPFELTDKDGKLFGRGTTDMKGGLMAMVIAMIELKQSNALKQGTIRLLATTGEETEQYGAQLLADEGYLDDVSGLIIGEPTSNIAYYAHKGSMSCVVTAKGKAAHSSMPHLGTNAVDILVDFVNEMKQEYKNIKEHDKVHELDAVPMIEKHLHRKIGEEESHIYSGFVMLNSVFNGGKQVNSVPHKATAKYNVRTVPEYDSTFVKDLFEKVIRHVGEDYLTVDIPSSHDPVASDRDNPLIQNITRIAPNYVHEDIVVSALIGTTDASSFLGTNENNVDFAVFGPGESIMAHRVDEFIRKDMYLSYIDVYKDVFKAYLEK", "text": "SIMILARITY: Belongs to the peptidase M20A family."}
+{"protein": "MQREEKQLEACLDALISQVSDIKNSLVGFIHKLENEYDRLTWPSVLDSFALLSGQLNTLNKVLKNEKTPLLRNQVIIPLLLSPDRDEEIMRLTEGRVPVFSHEVVPDHLRTKPDPDVEELEKQLSAEAARITSEAAQKQVQSMNKMCSNLLDKISKEERESELGSLRQNKQTFNPTDTNALVAAVAFGKGLSNRRPPGQGGPMAPGQTGASSMLPNATGMQVPMSLPPNQQQQHMAGVSMSQGSQPGKMPSSIKTNIKSASMHPYQR", "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. May play a role as a target recruitment subunit in E3 ubiquitin-protein ligase complexes and thus in ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 8 family."}
+{"protein": "MLRAPKCSRCRNHGYLVPVKGHTGKCRWKQCICDKCYLITERQKIMAAQKVLRTQAAEEQVATVGTQGPQLPPRAPAAAATALSSSICPLPRAVPGGVGPGPTATCFLERPPQAPSPGPSTFQLGPSGRPGPSTFQPGPGAPGGLRDRSSAWLPQLMPQAPRPELCYPDQHLPVRPVPVPGPVRPVPRLPFADYGHPLRFKSDHVVGAGNPEREPFKQCPACVPVSPYQSFPLSEGQDSSSALGVPQQRGFRHVSCSPYHRSGLVSEPARDLQPTYCSPPPPPPPPPPPPLPAPPPQPQQPHFLPPGYLSALHFLPPPPPPPSPPSFSLTYDTDKENTNDQDAEAPTEPSQDSPQEQSN", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DMRT family."}
+{"protein": "MSRPRIGAAAAITQLEGWAIAPNHKDAIVKTFRFDDFNQAFGFMTRVALMADKLDHHPEWFNVYNRVEVLLTTHDADGVTDLDLTLAKFMDSAA", "text": "SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family. SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family."}
+{"protein": "MSLSKKRKLESGDSGGAGAGGEGAEEENGGEQEAAPPRPRRTKSERDQLYYECYSDVSVHEEMIADQVRTEAYRLGILKNWAALRGKTVLDVGAGTGILSIFCAQAGARRVYAVEASAIWQQAREVVRLNGLEDRVHVLPGPVETVELPERVDAIVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFVAPISDQMLEWRLGFWSQVKQHYGVDMSCMESFATRCLMGHSEIVVQDLSGEDVLARPQRFAQLELARAGLEQELEAGVGGRFRCSCYGSAPLHGFAVWFQVTFPGGDSEKPLVLSTSPFHPATHWKQALLYLNEPVPVEQDTDISGEITLLPSPDNPRRLRILLRYKVGDHEEKTKDFAMED", "text": "FUNCTION: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA (PubMed:22904064, PubMed:26070566). Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates (By similarity). Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a (By similarity). H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3) (By similarity). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53 (PubMed:22904064). Repression of TP53 blocks cellular senescence (PubMed:22904064). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively) (By similarity). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity (By similarity). Methylates HMGA1 (By similarity). Regulates alternative splicing events (By similarity). Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1 (By similarity). Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator (PubMed:24570487). Methylates GPS2, protecting GPS2 from ubiquitination and degradation (PubMed:26070566). Methylates SIRT7, inhibiting SIRT7 histone deacetylase activity and promoting mitochondria biogenesis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT6 subfamily."}
+{"protein": "MGTNGGVIAEQSMEIETNENPDKVEEPVVRRKRVTRRRHRRIHSKNNCLTPPNSDDDPQMSTPDDPVIHSPPSIGAAPGMNGYHGSGVKLEESSGACGSPDDGLLDSSEESRRRQKTCRVCGDHATGYNFNVITCESCKAFFRRNALRPKEFKCPYSEDCEINSVSRRFCQKCRLRKCFTVGMKKEWILNEEQLRRRKNSRLNNTGTCNKRSQPGNQQSPQGPNQQPHLSPHHPGVAIYPPQPQRPLTINPMDNQMMHHMQANRPNAMPQLISPPGAQPYPLTSPVGSSASDSPPNRSLTMMHNGEKSPDGYDPNIMAHRAPPPSFNNRPKMDSGQVVLSTEEYKQLLSRIPGAQVPGLMNEEEPINKRAAYNCNGHPMPAETTPPYSAPMSDMSLSRHNSTSSGTEKNHMTHSTVSAIPGNSAQNHFDIASFGMGIVTATGGGDAAEEMYKRMNMFYENCIQSALDSPENQEPKPQEAMIPKEEYMTPTHGFQYQSDPYQVPPAERNINYQLNAAELKALDAVREAFYGMDDPMEQGRQMQSFLKANKTPADIMNIMDVTMRRFVKVAKGVPAFREVSQEGKFSLLKGGMIEMLTVRGVTRYDASTNSFKTPTIKGQNVSVNVDDMFAKLNANAQAQKAKCLEFFGFFDEEIKKNELAVYLVMLAVLFSVRSDPPMNENDVRIVTERHNHFMSLLNRYLESLFGEQARRIFERIPKALGLLNEIARNAGMLFMGTVRSGEAEELPGEFFKIK", "text": "FUNCTION: Nuclear receptor which binds directly to response elements in target gene promoters (PubMed:9477318, PubMed:10859169, PubMed:15314028, PubMed:15489294, PubMed:15383841, PubMed:15611047, PubMed:16626392, PubMed:19828440, PubMed:21814518). Activity is modulated by binding of steroid hormone ligands that include dafachronic acids (PubMed:16529801). Regulates expression of genes involved in postembryonic development and the dauer diapause, in response to environmental cues (PubMed:9477318, PubMed:10859169, PubMed:15489294, PubMed:15383841, PubMed:16626392, PubMed:19828440, PubMed:21814518). Inhibits the expression of let-7 family members when bound to corepressor din-1s which is an isoform of din-1 (PubMed:19828440). Plays a role in controlling the timing of seam cell development during the larval stages (PubMed:21471153). Has a role in the immune response to bacterial infection, via regulation of let-7 miRNAs (PubMed:23990780). Controls expression of genes that promote the aerobic catabolism of fatty acids for reproductive growth (PubMed:25774872). May be involved in thermotolerance (PubMed:24957743). SUBCELLULAR LOCATION: Nucleus Note=Diffuse expression during mitosis (PubMed:10859169). Increased nuclear accumulation upon infection by E.coli (PubMed:23990780). SIMILARITY: Belongs to the nuclear hormone receptor family."}
+{"protein": "MAGSPFTTALLSAWTLSTVAVGYPNGPWYQTPLGPDVVRDPTRYPGAIEKTVDYVVVGGGASGLTVAARLSEDPSVTVAIVEAGSFYQEVSNASVVPGYAADYLTGHIPPELDWGFNTEPQAGADGRVKHYTNAKTLGGNSAFNLMAYMTTSVGAMQKWAEEVDDDSWTYANVTRYFQKSLNFTGIDPHKRRANSTPELNPADVGYGGPLDVTYPNYAQPFSSWVKKAFDQVGMRPVGGFMSGELFGSSWVLDTINHTDGQRASSAKTFLEPILHRRENLFLYNRTLAERVLFDADRTATGVQASRGKTVFNLTATKEVVLTAGGLMTPQLLQVSGVGNAALLQELRIPVVLDAPQVGQQMEDHISFGVAHRVDVETNSALKYAGPRQHAVEEFNEAQAGILSSPGPDFGGFADIPSELRNFSASTHADLAGLPKDWPEGFFISFPVDVGFPQDGYNYAMIVCTLMTPMSRGHISIRSPSMHDRPVIDPRWLTSTSDVEIAVAAVRRIRQYLQMPVLERNVLVGGEVAPGPEVQTFAEIHDYLKKNFNSMSHPACTCRMGKKGDPDAVVDPKGRVFGVKNLRIADASVFRFLPPGLPLGVVYMVAEKIADDIKHDQKHGAGEEGLRTEF", "text": "FUNCTION: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of pyranoviolin A, a pyranonigrin analog with a C-3 methoxy group (PubMed:33117309). Initially, the PKS portion of pyvA synthesizes C-10 carbon chain from 5 molecules of malonyl-CoA, which is then condensed with the thiolation (T) domain-bound glycine activated by the adenylation (A) domain (PubMed:33117309). The subsequent chain release by Dieckmann condensation (DKC) could be catalyzed by the TE domain present at the C-terminus of pyvA and/or the alpha/beta hydrolase pyvD, installing the tetramic acid moiety (Probable). The FAD-dependent monooxygenase pyvC next epoxidizes one of the olefins of the polyketide part, and the epoxide ring-opening induces the dihydro- gamma-pyrone ring formation (Probable). The cytochrome P450 monooxygeanse pyvB would be responsible for the 2 consecutive reactions, in which the dihydro-gamma-pyrone is oxidized to gamma- pyrone and C-7 is hydroxylated to yield pyranonigrin F (Probable). Finally, the O-methyltransferase pyvH methylates the C-3 hydroxy group to complete the biosynthesis (Probable). SIMILARITY: Belongs to the GMC oxidoreductase family."}
+{"protein": "MEQTQKLKLNLQHFASNNVKPQVFNPDNVMMHEKKDGTLMNEFTTPILQEVMENSKIMQLGKYEPMEGTEKKFTFWADKPGAYWVGEGQKIETSKATWVNATMRAFKLGVILPVTKEFLNYTYSQFFEEMKPMIAEAFYKKFDEAGILNQGNNPFGKSIAQSIEKTNKVIKGDFTQDNIIDLEALLEDDELEANAFISKTQNRSLLRKIVDPETKERIYDRNSDSLDGLPVVNLKSSNLKRGELITGDFDKLIYGIPQLIEYKIDETAQLSTVKNEDGTPVNLFEQDMVAITCNYACSIAYR", "text": "FUNCTION: Assembles to form an icosahedral capsid. SUBCELLULAR LOCATION: Virion. Note=Forms the icosahedral capsid shell. SIMILARITY: Belongs to the HK97 phage major capsid protein family."}
+{"protein": "MSAVQPVNPKPFLNSLTGKFVVCKLKWGMEYKGVLVAVDSYMNLQLAHAEEYIDGNSQGNLGEILIRCNNVLYVGGVDGENETSA", "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 (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol. SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily."}
+{"protein": "MEFREQVLNLLAEVAENDIVKENPDVEIFEEGIIDSFQTVGLLLEIQNKLDIEVSIMDFDRDEWATPNKIVEALEELR", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DltC family."}
+{"protein": "MQRYNSTYVVKRDGRKEDVHFDKITSRIQKLSYGLNMDFVDPVAVAIKVISGLYKGVTTVELDNLAAETAASMTTQHPEYALLAARIAVSNLHKKTNKVFSEVMKTLHEFHHPHTGKHAPMISDETWAIIEKNADKLNSAIVYDRDYSYTYFGFKTLERSYLLKINKEIVERPQQMLMRVSIGIHGDDITSAIETYNLMSERYMTHASPTLFNSGTCRPQMSSCFLLTMSEDSILGIYDTLKQCALISKSAGGIGLNVHKIRATGSVIAGTNGTSNGLIPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHADIFEFVSLRKNTGPEEERARDLFLALWIPDLFMKRVEKDQEWSLMCPCECPGLDDCWGEEFEALYAKYEAEGRVRKTVKARKLWEHIVSNQIETGLPYITYKDAANRKSNQQNLGTIKCSNLCTEIIEYSAPDEIAVCNLASIALNRYVTPEKKFDFVKLAEVTKVITRNLNKIIDVNYYPVEEARNSNMRHRPIGLGVQGLADCFMLMRYPFTSAEARDLNKRIFETIYYAALEASCELAELNGPYSTYEGSPVSKGQLQFDMWGVTPTDQCDWATLRKKIAKHGIRNSLLMAPMPTASTAQILGNNESIEPYTSNIYSRRVLSGDFQIVNPHMLKDLVERGLWTDEMKNRLIANNGSIQNIDGIPSDIKELYRTVWEISQKDIIEMAADRGAYIDQSQSLNIHMAKPSYAGITSMHFYGWKKGLKTGMYYLRTKPAVNAVQFTVDKNALKTNQQAETPATVAESQDEGCLMCSG", "text": "FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large chain family."}
+{"protein": "MAEQMQISRRTILAGAALAGALAPVLATTSAWGQGAVRKATAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVIDDAGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAATGALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGAIMVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAYEDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYVNHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSGT", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "MGDFNSNEDNNNPFNNVLYNPYIVDLYDTTNNNNNNNNNNNIISGFNCDSSIFTQQISNTNNELTIPLTQSIQNLLPPVQQQTQLFISPNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNDINTSIDINLNQLVYSTPSQQITNSVQPIYQCATQSTTSNIDTNINTINDNNNNNNNNNNNNNNSVNNNLLSMCQDPTLILQIQQLLLQQQLLQQAQQQSVPLNIQVPTTTTPINQQHQALLVPQQKQFYGNVSDNSSPETNFSYASPSSPSSTQSQSSPYEQQPLSPNPTISLSSSISVTATTTTRPNATEKTKESSLKSKSKSNEKDKEREDEEEDDDDRPKKRKKFDKNVYKGVDLGDELLEITSEEFQAYKNNFFANASDKKTVSALNYQFRKIKNRESARRSRERKATHVDELEAKIAEIEKERDNYKKENERLRMELDQYKLQEKQKSAGSIFDYISIGSPTTQNFSKNFGIILFLFLFGSFILTNTTPNFFNTNNGVINPNLVYNANSNNNNNNNNNVNRFSVNGVHSTQQYFQSQRNPLSNLDEDSLESLTASQGVFSTHFVPEQPSILLNRESIRNWATLPQNSVASLSFEKDNALKTIENANLDKSKHNVISNLNQLQQQQPSSDELMIDQKEEKNCNNNNENNNNNDNNKNSDDEKGKEIEEIKRKSTTTTISPTRYVNNSTISLLVNPTSVIGDIPDDLMKNSNVTTFGENSSFKFNFLIDTQNFPNGSNDISKAFFDNENQQMTVTSVIIAIQKSPKTPSQQPSTK", "text": "FUNCTION: Probable transcriptional regulator. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
+{"protein": "MTKQKLLLNGTFSLILIVACEAQQLPRSHAASSSGPLCEKEAESWGNLLSSERLDAWICSLIGSFMVGLSGIFPLLVIPFETGAALRSEAGSRRLKQLLSFAIGGLLGNVFLHLLPEAWAYTCSAAAGEGQSFQQQKLLGLWVIIGFLTFLALEKIFLEKEEEECPGVGCDYKAPLGKIPNGSGYPPSKVAGKSQRAEKNSTQCNGSSLQSCRTDNRIKISGYLNLLANTIDNFTHGLAVAASFLVSRKVGFLTTMAILLHEIPHEVGDFAILLRAGFDRWSAAKMQLSTALGGIVGACFAICAQSPKGAGETVAWILPFTSGGFLYIALVNVVPDLLEEKNPWNSLQQILLLCTGITVMVLLAHN", "text": "FUNCTION: Functions as a zinc transporter transporting Zn(2+) from the Golgi apparatus to the cytosol and thus influences the zinc level at least in areas of the cytosol. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane Endoplasmic reticulum membrane. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
+{"protein": "MEQFDQLVLNSISAKALKSYLTTKIAEAIDELAAKKNSPKKKAQTKKPENRIPLDLINKNFVSKFGLKGYKDGVLNSLICSLVENNYFENGKLKRGKHDELVLLDIEKEILARIDENSSLNIDVLDVKVLANRLRTNADRFEFKGHTYYLEQNKTEDIINQLIKNSAISMDMKNTIKDTFYMISDELLDVFKNRLFKCPQVKDNIISRARLYEYFIKATKPDDSKIYVILKDDNIAKILNIETIVIDHFIYTKHSLLVSSISNQIDKYSKKFNDQFYSSISEYIKDNEKINLSKVIEYLTISTVKIENTVE", "text": "FUNCTION: Late DNA-binding protein which binds to the hairpin form of the viral telomeric sequence. Required for the production of mature virions (MV) (By similarity). SUBCELLULAR LOCATION: Virion Note=Present in the virus core. SIMILARITY: Belongs to the chordopoxvirinae I1 family."}
+{"protein": "MNKAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI", "text": "FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. SIMILARITY: Belongs to the Nth/MutY family."}
+{"protein": "GILDSFKGVAKGVAKDLAGKLLDKLKCKITGC", "text": "FUNCTION: Antibacterial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli. Weak activity against C.albicans. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Ranatuerin subfamily."}
+{"protein": "MKTQWGEVWTHLLLLLLGFLHVSWAQSSCTGPPGIPGIPGVPGVPGSDGQPGTPGIKGEKGLPGLAGDLGEFGEKGDPGIPGTPGKVGPKGPVGPKGTPGPSGPRGPKGDSGDYGATQKVAFSALRTINSPLRPNQVIRFEKVITNANENYEPRNGKFTCKVPGLYYFTYHASSRGNLCVNLVRGRDRDSMQKVVTFCDYAQNTFQVTTGGVVLKLEQEEVVHLQATDKNSLLGIEGANSIFTGFLLFPDMDA", "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": "MDKDRVELLIKSVIRTDGYLNYANTKSTILLTLASGVLATASLNLSKLLPLSLDKLSTSSFVSFSFFLVIGVLINILSVVRTLKAISPYLKNSDKENIFSFVDIVHYNSSSDTYSEKIKKLDYSHLGEQLTSLNYNLSVGLLDKYKNQRRAIILLKISMASFFLSIVVPWFFYCFDISLTEKGPIVIMLLFIISLVVFIVFLLTLIIYLLYLGKDKK", "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 E Pycsar system. FUNCTION: The effector component of a two-gene Pycsar system. Expression of this and adjacent cytidylate cyclase Ec303145PycC (AC P0DV26) confers resistance to bacteriophage P1, T5, lambda-vir and phi27 (PubMed:34644530). Probably only responds to cCMP (produced by its cognate NTP cyclase), acts by impairing membrane integrity (Probable). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MDQMTVEEKILEHQELEDGSSSFRWLVSSTVIAIGGATVALYISGKIDWKIPAIEAGLALTAGGTITCGYLWFKKRVKTVRKLILQMNKTRSALRKRRQIFFSISMCMPRHRHPSILRACRLTVSAIECLTEETKSLNNGTTWQDLYTDEIREIISRSTVDSQLLKIEEIQEGDNDKMDFEQVFETLISIFKLHASEYSRVVILNFLNSPVFESKKVSKFFETLGRLQELMYNLESVERLALKTETKLSRNERKMDGKMKNKSLLELGWKQQTALALEAILERLESESVTQSEVESALHKTFLVVKAEPAFPQPVKKIDVEVKNQDQKNPEVIVIEKGTGERTDIDMVFEGTPLSEADKLSASKSAVARDVLLDGSEGRCHEASLFGELKMVLEPRRTDFAKRERTALAKFYGVDEHQLEQKEDEETFEAIASGDGEDPDPYDWRKDAEMSAGIHHDANNDDFLKSLKLRRVDDDIIE", "text": "FUNCTION: In the first mitotic division in embryos, required for mitotic spindle alignment and asymmetric cell division (PubMed:9649522, PubMed:17947426). Required for motor-driven chromosome movement and homolog searching within the nucleus, and subsequently ensures homologous chromosome pairing during the prophase stage of meiosis (PubMed:23671424). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion outer membrane; Multi-pass membrane protein Note=Localizes to mitochondria throughout interphase and mitosis (PubMed:17947426, PubMed:23671424). Localizes to mitochondria in the pachytene and transition zone regions of the germ cells (PubMed:23671424)."}
+{"protein": "MVKVYIENYGCARNRADGEIMAALLYLSGHEIVESPEESEIVVVNSCAVKDPTERKIARRIRELLDNGKKVIVTGCLPHVNPDVIDERVSAILGVKSIDRIVQAVEYAMRGEKLISVPDWKKRNLDKLDFPRLSPRNVYFILPIAEGCLNACTYCATRLARGVLKSYSPEKIIGWVKWAIKQGYKEIWLSAEDTGCYGFDIGTNLAKLIDEITAIEGEFRIRVGMMNPNHVLKFLDELIDAYKDEKVYKFLHLPVQSGDNEILRKMGRMYTVEEFEEIVKAFRREFPELNLHTDIIVGFPGESEEAFQRSVELIKRIRPDKVNVSRYSPRPGTIAAKWKQLPGWVVKERSRLLHRIRLQISYEINRKYIGKKVKVLIHGEGKKGNVDAVTMNYKHIILPEGRKGEFREARVKNAASTYLLGEIIT", "text": "FUNCTION: Catalyzes the methylthiolation of N6- threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1 subfamily."}
+{"protein": "MSVNDQITHIGKTLSTTASAFLNYQKSNSNTQDVLTNNGPYKNLLSNTVNNASSTSYFYKRTEHGRFVKNASNTFEDIYSKTRRGDVFRNKFTDNKTCFRMLTYISDDLLNEIPTKEGLKSDADGKLLTEGGENENLRKNASKKETSLFQGFKSYLPIAELAIENTERLNYDTNGTSGTVGAKDVMSKTNERDEIHTELPNFQDSFLIPPGVETKKISSSYSPSALKSFSQTLVNSLEFLNIQKNSTLSEIRDIEVEVENLRQKKEKLLGKIANIEQNQLLLEDNLKQIDDRLDFLEEYGLEVIEANSDENAEDDGMSERKALKNDAIRNEGVTTESISSEASNLPPRRRQQLRDDNSLNRLGAFYSKSKKRHRKSFPTFQQLYEPGTKIGSIMSTHDDFLTCLDFDAPFGTLCTAGYLDHTVKIWDLSKQNKIGELAGHLATINCMQINRDYGTLVTGGRDAALKLWNLNLAQQLYQETQNLTSPTNHIDSPCVHTFEAHTDEVTALSLDPSFLVSGSQDRTIRQWDLRSGKCLQTIDLSFANVLTTSTNVDLSKSTLLTQRNERPSIGALQSFDAALATGTKDGVVRLWDLRSGKVIRTLKGHTDAITSLKFDSACLVTGSYDRTVRIWDLRTGLLNKFHAYSAPVLSLDLFQENAAVVVADEPSVQIYDSEKDESWSCVEQGNETSVSTVKYKENYMVEGRENGDVNIWAV", "text": "FUNCTION: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 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. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Note=Uniformly distributed on the cytoplasmic face of the mitochondrial outer membrane. This localization is dependent on FIS1. Reorganizes to punctate structures on mitochondria, corresponding to mitochondrial constriction sites, at a late step in mitochondrial division. This relocalization is dependent on DNM1. SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family."}
+{"protein": "MAAAIASGLIRQKRQAREQHWDRPSASRRRSSPSKNRGLCNGNLVDIFSKVRIFGLKKRRLRRQDPQLKGIVTRLYCRQGYYLQMHPDGALDGTKDDSTNSTLFNLIPVGLRVVAIQGVKTGLYIAMNGEGYLYPSELFTPECKFKESVFENYYVIYSSMLYRQQESGRAWFLGLNKEGQVMKGNRVKKTKPAAHFLPKPLEVAMYREPSLHDVGETVPKAGVTPSKSTSASAIMNGGKPVNKCKTT", "text": "FUNCTION: Probably involved in nervous system development and function. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the heparin-binding growth factors family."}
+{"protein": "MSPVEKPVEVEKPKVPKRRFVGKKPQNITIKDGEQPLTKTINPARHIGRVMNQIPDDILNDKELNEAIKLLPSNYNFEIHKTIWNIRKTNCKRVALQMPEGLLIYSLIISDILEQFCQVETIVMGDVSYGACCIDDYTARSLDCDFIVHYAHSCLVPIDITSIKVLYVFVTINIDETHLINTIKLNFERGTQIAIFGTIQFNPTIHSVKAKLENDTEKPMYLIPPQTRPLSKGEVLGCTSARLDKEHIKAMIYIGDGRFHLESSMIHNPEIPAYRYDPYSRKFTREYYDHKQMIDVRKDAISTTKYATKVGLILGALGRQGNPITLDKLEKSLSEKGIQVVKIILSEILPQKLAMFDDVDAFVQVACPRLSIDWGYAFNKPLLTPYEAMVMLEKDTMGDEKVYPMDYYSKDGYGRGSIPDHSHLTT", "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": "MLKVRSALSLIQSQKATLSLATQKRWQTNVATAEAREDSEWLQAKPFEQIPRLNMWALSMKMSMPGGKYKNMELMEMFEAMRQDYGDIFFMPGIMGNPPFLSTHNPQDFEVVFRNEGVWPNRPGNYTLLYHREEYRKDFYQGVMGVIPTQGKPWGDFRTVVNPVLMQPKNVRLYYKKMSQVNQEFVQRILELRDPDTLEAPDDFIDTINRWTLESVSVVALDKQLGLLKNSNKESEALKLFHYLDEFFIVSIDLEMKPSPWRYIKTPKLKRLMRALDGIQEVTLAYVDEAIERLDKEAKEGVVRPENEQSVLEKLLKVDRKVATVMAMDMLMAGVDTTSSTFTALLLCLAKNPEKQARLREEVMKVLPNKNSEFTEASMKNVPYLRACIKESQRLHPLIVGNARVLARDAVLSGYRVPAGTYVNIVPLNALTRDEYFPQASEFLPERWLRSPKDSESKCPANELKSTNPFVFLPFGFGPRMCVGKRIVEMELELGTARLIRNFNVEFNYPTENAFRSALINLPNIPLKFKFIDLPN", "text": "FUNCTION: Has a role in resistance to insecticide lufenuron, but no other insecticides. SUBCELLULAR LOCATION: Mitochondrion membrane. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MHMNKPLQAWRTPLLTLIFVLPLTATGAVKLTLDGMNSTLDNGLLKVRFGADGSAKEVWKGGTNLISRLSGAARDPDKNRSFYLDYYSGGVNEFVPERLEVIKQTPDQVHLAYIDDQNGKLRLEYHLIMTRDVSGLYSYVVAANTGSAPVTVSELRNVYRFDATRLDTLFNSIRRGTPLLYDELEQLPKVQDETWRLPDGSVYSKYDFAGYQRESRYWGVMGNGYGAWMVPASGEYYSGDALKQELLVHQDAIILNYLTGSHFGTPDMVAQPGFEKLYGPWLLYINQGNDRELVADVSRRAEHERASWPYRWLDDARYPRQRATVSGRLRTEAPHATVVLNSSAENFDIQTTGYLFSARTNRDGRFSLSNVPPGEYRLSAYADGGTQIGLLAQQTVRVEGKKTRLGQIDARQPAPLAWAIGQADRRADEFRFGDKPRQYRWQTEVPADLTFEIGKSRERKDWYYAQTQPGSWHILFNTRTPEQPYTLNIAIAAASNNGMTTPASSPQLAVKLNGQLLTTLKYDNDKSIYRGAMQSGRYHEAHIPLPAGALQQGGNRITLELLGGMVMYDAITLTETPQ", "text": "FUNCTION: Degrades the rhamnogalacturonan I (RG-I) backbone of pectin. Is required for the full virulence of E.chrysanthemi strain 3937 as it is involved in rotting of plant tissue. SUBCELLULAR LOCATION: Secreted. Note=Via the type II out secretion pathway. SIMILARITY: Belongs to the polysaccharide lyase 4 family."}
+{"protein": "MIEMLFVKVPNEIDRHVFNFLSSNVSKEKQQAFVRYVNVKDAYRSLLGELLIRKYLIQVLNIPNENILFRKNEYGKPFVDFDIHFNISHSDEWVVCAISNHPVGIDIERISEIDIKIAEQFFHENEYIWLQSKAQNSQVSSFFELWTIKESYIKAIGKGMYIPINSFWIDKNQTQTVIYKQNKKEPVTIYEPELFEGYKCSCCSLFSSVTNLSITKLQVQELCNLFLDSTFSENNNF", "text": "FUNCTION: Activates the five peptidyl carrier protein (PCP) domains of gramicidin synthase GrsAB, by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue. Required for gramicidin S production. SIMILARITY: Belongs to the P-Pant transferase superfamily. Gsp/Sfp/HetI/AcpT family."}
+{"protein": "MAKRDGMKLRDELTFDTSRAVKAVSWGEAIDRFQSWYDDQRGTQIVVENELGETVGFDMPNRFTPEYREMLYAKAQSLERGLRERWGSLLHTGMVTLTASSTDDEGRLRPPLEHFEDLLESWEAVRRALARVLEGREWEYLAILEPHESGYVHIHLGVFVRGPVVAEQFEPVLDAHLRNCPTAGEDAHQVFDENGDEDAVRVRRSSHPSRSGGVENLGAYLAAYMAGEYGSEPSEMPENVRAFYATMWASGRQWFRPSNGAQELMQPEEDDEGDSIEEWEMVGIAPEGDLGDIIEVDPSEPRSDPYRRLRTPPPGG", "text": "FUNCTION: Possibly necessary for replication."}
+{"protein": "GWPAYPGRNGIRSSVCQKKLGCGWRKLASLPVCKAFCLARKRFWQKCGKNGSSGKGSKICKSVIAHTFEKAGKGLIKLTDMAVATIIKYAGKK", "text": "FUNCTION: Cytolysin that shows hemolytic activity (on bovine erythrocytes, HC(50)=5.75 mg/ml) (By similarity). This hemolytic activity is completely inhibited by small unilamelar vesicles composed of PC/PG, PC/PI and PC/PS in 1:1 molar ratios (with at least 100 mg/ml concentration) (By similarity). The recombinant protein does not show hemolytic activity, suggesting that it is not properly folded or that it requires a free N-terminal end for its activity (Probable). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the worm cytolysin family."}
+{"protein": "MATAVWAAARLLRGSAALCARPKFGSPAHRRFSSGATYPNIPLSSPLPGVPKPIFATVDGQEKFETKVTTLDNGLRVASQNKFGQFCTLGILINSGSRYEAKYLSGIAHFLEKLAFSSTARFDSKDEILLTLEKHGGICDCQTSRDTTMYAVSADSKGLDTVVGLLADVVLHPRLTDEEIEMTRMAVQFELEDLNMRPDPEPLLTEMIHEAAFRENTVGLHRFCPVENIGKIDREVLHSYLKNYYTPDRMVLAGVGVEHEHLVECARKYLLGVQPAWGAPGAVWMLTAQWHSTRGGSSRWRETCQMSALRPPRFQSSHIYGGARELLLLEEDFIPFAVLNMMMGGGGSFSAGGPGKGMFSRLYLNVLNRHHWMYNATSYHHSYEDTGLLCIHASADPRQVREMVEIITKEFILMGRTVDLVELERAKTQLMSMLMMNLESRPVIFEDVGRQVLATHSRKLPHELCTLIRNVKPEDIKRVASKMLRGKPAVAALGDLTDLPTYEHIQAALSSRDGRLPRTYRLFR", "text": "FUNCTION: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. SUBCELLULAR LOCATION: Mitochondrion matrix Mitochondrion inner membrane. SIMILARITY: Belongs to the peptidase M16 family."}
+{"protein": "MATVDVLTSEVVVPAGETPAGAVWLSNLDLAARRGYTPTVFFYRHNGEPGFFAADAMRDSLARALVAFYPVAGRLGLDGDGRVQVDCTGEGVVFATARSGHYALDDLMGEFVPCDEMRDLFVPAAPAAASCCPRGGALLLVQVTYLRCGGVVLGMALHHSIADGRSAAHFVETWASIARGAPAADAPVPPCFDHRLLAARPARAVLYDHPEYKPEPAPPARAATASTYASAIITLTKQQVGALRAACAGASTFRAVVALVWQCACRARALPPEAETRLHSMIDTRQRLSPPLPPGYFGNAVIRTSTAATAGEVVSSPVGHAARRARAATSQGEDYARSVVDYLEGVDAMNLPRSGVSRADLRAISWLGMSLADADFGWGSPAFMGPAIMYYSGFVYVMNAPGKDGAVALALSLEPESMPEFRKVFADEVARLA", "text": "FUNCTION: Hydroxycinnamoyl transferase that catalyzes in vitro the transfer of an acyl from p-coumaryol-CoA to glycerol or shikimate, to produce 2-O-p-coumaroyl glyceride or coumaroyl shikimate, respectively. Quercetin, glutarate, or malate do not serve as acyl acceptors in vitro. Can use feruloyl-CoA and caffeoyl-CoA as acyl donors. SIMILARITY: Belongs to the plant acyltransferase family."}
+{"protein": "MALAVLRVLEPFPTETPPLAVLLPPGGPWPAAELGLVLALRPAGESPAGPALLVAALEGPDAGTEEQGPGPPQLLVSRALLRLLALGSGAWVRARAVRRPPALGWALLGTSLGPGLGPRVGPLLVRRGETLPVPGPRVLETRPALQGLLGPGTRLAVTELRGRARLCPESGDSSRPPPPPVVSSFAVSGTVRRLQGVLGGTGDSLGVSRSCLRGLGLFQGEWVWVAQARESSNTSQPHLARVQVLEPRWDLSDRLGPGSGPLGEPLADGLALVPATLAFNLGCDPLEMGELRIQRYLEGSIAPEDKGSCSLLPGPPFARELHIEIVSSPHYSTNGNYDGVLYRHFQIPRVVQEGDVLCVPTIGQVEILEGSPEKLPRWREMFFKVKKTVGEAPDGPASAYLADTTHTSLYMVGSTLSPVPWLPSEESTLWSSLSPPGLEALVSELCAVLKPRLQPGGALLTGTSSVLLRGPPGCGKTTVVAAACSHLGLHLLKVPCSSLCAESSGAVETKLQAIFSRARRCRPAVLLLTAVDLLGRDRDGLGEDARVMAVLRHLLLNEDPLNSCPPLMVVATTSRAQDLPADVQTAFPHELEVPALSEGQRLSILRALTAHLPLGQEVNLAQLARRCAGFVVGDLYALLTHSSRAACTRIKNSGLAGGLTEEDEGELCAAGFPLLAEDFGQALEQLQTAHSQAVGAPKIPSVSWHDVGGLQEVKKEILETIQLPLEHPELLSLGLRRSGLLLHGPPGTGKTLLAKAVATECSLTFLSVKGPELINMYVGQSEENVREVFARARAAAPCIIFFDELDSLAPSRGRSGDSGGVMDRVVSQLLAELDGLHSTQDVFVIGATNRPDLLDPALLRPGRFDKLVFVGANEDRASQLRVLSAITRKFKLEPSVSLVNVLDCCPPQLTGADLYSLCSDAMTAALKRRVHDLEEGLEPGSSALMLTMEDLLQAAARLQPSVSEQELLRYKRIQRKFAAC", "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:16314507, PubMed:16854980, PubMed:21362118, PubMed:29884772). Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2- PEX10-PEX12 retrotranslocation channel (PubMed:29884772). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (PubMed:29884772). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome membrane Cell projection, cilium, photoreceptor outer segment Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes (PubMed:12717447, PubMed:16854980). Localized at the base of the outer segment of photoreceptor cells (PubMed:26593283). SIMILARITY: Belongs to the AAA ATPase family."}
+{"protein": "MKPVSCVGLLVLLVGVLVTVKGSILFQSPKVLIVSLIRNKEHTLPYFFSYLEDQEYPKDRISLWFRSDHNEDRSIDIIKAWLKRVTKKYHSVDFGYRSDAAKRYDEKSSTHWSEDRFADVIRLKQEALDKGRKMWADFVLFLDADVLLTNPNTIAKLVSLNLPIVAPMLLSDGLYSNFWCGMTADYYYHRTDEYKEILNYEKTGEFPVPMVHSAVMVNINVQQSLNLSFDKRRLPPGHYTGPVDDIIIFAMSANYSSIPMYISNSASYGYILVPLEQGDPLEKDLEQLTNTKVYIINEHGAINLKEDLKHFVPKVPKDKMGVSHIYMINLERRPERRNKMFNNFDELGLDVEFFPAVDGRQLSDDKLRDIGVKFLPGYADPYHKRPMTMGEIGCFLSHYYIWEKMVAMNQEEVLVLEDDIRFEPYFKRRVAQVLDDARRIGGWDLIYFGRKRLQEDDEKWVVGSETLVVAGYSYWTLGYLISLQGAKKLLEEKPLEKLVPVDEYIPIMFNNHPNESWVNHFKNRNLVAWSAAPLLLYPTHYTGDDGYISDTEDSARIDNFNKVLNDTSDSSAEKKGDKEQLSSKTLMDSTISRDEHELSVANRKSEL", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the glycosyltransferase 25 family."}
+{"protein": "MGKYMRKAKVVVSGEVVAAAVMELAAAPLGVRTRARSLALQKRQGGEYLELRSRRLEKLPPPPPPPPRRRATAAAATADATAAESAEAEVSFGGENVLELEAMERNTRETTPCSLIRDPDTISTPGSTTRRSHSSSHCKVQTPVRHNIIPASAELEAFFAAEEQRQRQAFIDKYNFDPVNDCPLPGRFEWVKLD", "text": "SIMILARITY: Belongs to the CDI family. ICK/KRP subfamily."}
+{"protein": "MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASALAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTAEQAKVSLGLDEDVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLAFLLAVKYIFFEQAETESTLSLKNPITSPVVTSKKAQDNCCRREPLLVRRNQKLSSVEEDPGANQERKVEVIKPLVVEAETTSRATFVLGASVASPPSALGTQEPGIELPIEPRPNEECLQILENAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSTKLAEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDGKEYQVPMATTEGCLVASTNRGCRAISLGGGASSRVLADGMTRGPVVRLPRACDSAEVKTWLETPEGFAVIKEAFDSTSRFARLQKLHVTMAGRNLYIRFQSRTGDAMGMNMISKGTEKALLKLQEFFPDMQILAVSGNYCTDKKPAAINWIEGRGKTVVCEAVIPAKVVREVLKTTTEAMVDVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVRSHMVHNRSKINLQDLQGTCTKKAA", "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": "MAVPVPLGRFGSFCLRLLRLLALLELLVHPVLGRVHHLALKDDVRHKVHLNTFGFFKDGYMVVNVSSLSVNEPEGATDKDAEIGFSLDRTKNDGFSSYLDEDVNYCILKKKSMSSVTLVILDISGSIVKVRSPPEAGKQLPEIVFSKDEKILSQSQEPAVSSNPKDSEARRTLDGFKAGRSTVDSKAITERSFSIHKNDGVVSFQFFFNISTDDQEGLYSLYFHKCSGNNVKPGEQASFSLNIAITEKNPNSYLSAGEIPLPKLYVSMALFFFLSGTIWIHILRKRRNDVFKIHWLMAALPFTKSLSLVFHAIDYHYISSQGFPIEGWAVVYYITHLLKGALLFITIALIGTGWAFIKHILSDKDKKIFMIVIPLQVLANVAYIIIESTEEGTTEYGLWKDSLFLVDLLCCGAILFPVVWSIRHLQEASATDGKAAINLAKLRLFRHYYVLIVCYIYFTRIIAFLLKFAVPFQWKWLYQLLDETATLVFFVLTGYKFRPASDNPYLQLSQEDDDLEMESVVTTSGVMENMKKVKKVSNGAVEPQGSWEGTA", "text": "FUNCTION: Has been proposed to act as a receptor for neuronostatin, a peptide derived from the somatostatin/SST precursor (By similarity). Involved in blood sugar regulation through the induction of glucagon in response to low glucose (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LU7TM family."}
+{"protein": "MKLLSSWVVAALAAQAAGAAISHKLDGFTIREHADPAKRALLQKYVTWDEHSIFVNGERLMIFSGEVHPYRLPVASLYIDIFEKVKALGFNCVSFYVDWALLEGNPGHYSAEGIFDLQPFFDAAKEAGIYLLARPGPYINAEVSGGGFPGWLQRVDGILRTSDEAYLKATDNYASNIAATIAKAQITNGGPIILYQPENEYSGACCGYNGFPDGSYMQYIEDHARDAGIVVPFISNDAWAAGHNAPGTGAGAVDIYGHDSYPLGFDCANPSTWPSGNLPTYFHTSHEQQSPSTPYSLVEFQGGAFDPWGGVGFAKCAALLNHEFERVFYKNDFSFGVAFLNLYMIFGGTNWGNLGHPGGYTSYDYGSAISESRNITREKYSELKLLGNFAKVSPGYLVANPGDLSTSTYTNTADLTVTPLLGSNSSASSFFVIRHSDYSSQASVEYKLTVPTSAGNLTIPQLGGSLTLSGRDSKIHVTDYDVAGTNILYSTAEVFTWKKFNNEKVLVLYGGPGEHHEFAVSGASSSSVVEGSSSGISSKKVGKALVVAWDVSTARRIVQVGSLKVFLLDRNSAYNYWVPQVPTKGTAPGYSNQETTASSIIVKAGYLVRSAYLDGNDLHIQADFNATTPIEVVGAPSGAKNLVINGKKTQTKVDKNGIWSASVAYTAPKVQLPSLKSLKWKSVDTLPEAKNTYDDSAWTSADHAYTNNSAHSLQTPTSLFASDYGYHTGALLFRGHFTANGKEKTFFVQTKGGTAYGHSIWINETYVGSWAGTSINDNNNATYTLPTLQSGKNYVITVVIDNMGLDEDWTIGSEDMKNPRGIIQYSLSGQEASAISWKLTGNLGGENYRDTVRGPLNEGGLYAERQGFHQPQPPTQKWDSSSPFTGLTKPGIRFYSTSFDLDLPSGYDIPLYFNFGNSTSTPAAYRVQLYVNGYQYGKYVNNIGPQTSFPVPEGILNYHGTNWLALSLWAQEDNGAKLDSFELINTTPVLTSLGEVKSVNQPKYQARKGAY", "text": "FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. Has high in vitro transglycosylation activity with p-nitrophenyl-beta-D- galactopyranoside, methyl-beta-D-galactopyranoside or lactose as a donor and galactose as an acceptor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
+{"protein": "MGPQQDRSAAKPYANGSTAAAAAAGRKENNKVVRYRECQRNHAASIGGHAVDGCREFMASGAEGTAAALLCAACGCHRSFHRREVEAAAAECDCSSDTSSGTGRR", "text": "FUNCTION: Inhibits zinc finger homeodomain (ZHD) transcription factors, by interacting with them to prevent both their nuclear localization and their DNA-binding properties. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MSTEIPSLSASYANSFKIGAAVHTRMLQTEGEFIAKHYNSVTAENQMKFEEVHPREHEYTFEAADEIVDFAVARGIGVRGHTLVWHNQTPAWMFEDASGGTASREMMLSRLKQHIDTVVGRYKDQIYAWDVVNEAIEDKTDLIMRDTKWLRLLGEDYLVQAFNMAHEADPNALLFYNDYNETDPVKREKIYNLVRSLLDQGAPVHGIGMQGHWNIHGPSMDEIRQAIERYASLDVQLHVTELDLSVFRHEDQRTDLTEPTAEMAELQQKRYEDIFGLFREYRSNITSVTFWGVADNYTWLDNFPVRGRKNWPFVFDTELQPKDSFWRIIGQD", "text": "FUNCTION: Plays a role in plant xylan biodegradation, probably via the hydrolysis of short xylooligosaccharides resulting from extracellular xylan hydrolysis, once they have been transported inside cells. Shows similar activity on xylans of different rate of arabinose or methylglucuronic substitution. Also displays high activity on aryl- xylosides. Is active on xylotetraose and xylotriose, but does not hydrolyze xylobiose, indicating that XynB is a xylanase and not a beta- xylosidase. SUBCELLULAR LOCATION: Cytoplasm Note=Is not secreted to the medium but instead remains cell-associated, in the soluble fraction, even in late stationary-phase cultures. SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family. Cytoplasmic xylanase subfamily."}
+{"protein": "MYKEPFQPTYEYALECDKHDELKDFQTEFYKKEGTIYLDGNSLGLLSKRAEKSLLTLLDSWKEYGIDGWTEGEHPWFFLSEKLGELTAPLIGALPEETIVTGSTTTNIHQVIATFYEPKGIRTKILADELTFPSDIYALQSQIRLKGLDPDEHLVRVKSRDGRTLSEDDIIQAMTDDIALILLPSVLYRSGQILDMKRLTAEAHKRGIHIGFDLCHSIGSIPHHFKEWDVDFAIWCNYKYLNAGPGGVAGLYVNKKHFNRPPGLSGWFSSRKDKQFDMEHTLTAADHAGAYQIGTPHVLSTAPLIGSLEIFKDAGIERLREKSLHITRYMLNLIDHELKDFGFTIGNPFEDEKRGGHIYLEHAEAARICKALKANGVIPDFRAPNGVRLAPVALYNTYEEVWQSVMILKKIMKDEEYKQFENKREVVA", "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": "MSPERSQEESPEGDTERTERKPMVKDAFKDISIYFTKEEWAEMGDWEKTRYRNVKMNYNALITVGLRATRPAFMCHRRQAIKLQVDDTEDSDEEWTPRQQVKPPWMAFRGEQSKHQKGMPKASFNNESSLRELSGTPNLLNTSDSEQAQKPVSPPGEASTSGQHSRLKLELRRKETEGKMYSLRERKGHAYKEISEPQDDDYLYCEMCQNFFIDSCAAHGPPTFVKDSAVDKGHPNRSALSLPPGLRIGPSGIPQAGLGVWNEASDLPLGLHFGPYEGRITEDEEAANSGYSWLITKGRNCYEYVDGKDKSSANWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWSGDEYGQELGIRSSIEPAESLGQAVNCWSGMGMSMARNWASSGAASGRKSSWQGENQSQRSIHVPHAVWPFQVKNFSVNMWNAITPLRTSQDHLQENFSNQRIPAQGIRIRSGNILIHAAVMTKPKVKRSKKGPNS", "text": "FUNCTION: Histone methyltransferase that selectively methylates 'Lys-4' of dimethylated histone H3 (H3K4me2) to produce trimethylated 'Lys-4' histone H3 (H3K4me3). May play a role in epigenetic regulation of gene expression by defining an active chromatin state. SUBCELLULAR LOCATION: Nucleus Chromosome."}
+{"protein": "MFSIFKRRSVQAALAASGLVGGAVFYSDFIKRPAPSHFNPQFTPFTKSLAPPPSRETLLKNVEDISKFDVLIIGGGATGTGVAVDASTRGLNVCLLEKTDFASETSSKSTKMAHGGVRYLEKAVFQLSKAQLDLVIEALNERANMLRTAPHLCTVLPIMIPVYKWWQVPYFFVGCKIYDWVAGSKNLRASTIFSKETTVAIAPMLDDSNLKASCVYHDGSFNDTRMNTTLAVTAIDNGATVLNYMEVKKLLKSKDNKLEGVLAIDRETGKEYQIKATSVVNATGPFSDKILEMDADPQGEPPKTAQFPRMVVPSAGVHVVLPEYYCPPNIGILDPSTSDNRVMFFLPWQGKVIAGTTDKPLSSVPTNPTPSEDDIQLILKELQKYLVFPVDREDVLSAWCGIRPLVRDPSTVPPGTDPTTGETQGLVRSHFIFKSDTGLLTISGGKWTTYREMAEETVNELIKDHDFGKALKPCQTKKLILVGGENYYKNYSARLIHEYHIPLRLAKHLSHNYGSRAPLILELYSKTDFNKLPVTLADKEVFAPSSDASSDKSVSYASFDEPFTVAELKYSIKYEYTRTPTDFLARRTRLAFLDARQALQAVAGVTHVMKEEFGWDDATTDKLAQEARDYIGGMGVSSDRFDVKQFEVK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family."}
+{"protein": "MLLFWWWELGDPCAWTGKGRGTLKMSPATTGTFLLTVYTLFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEVSNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEEFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPIKDMKEGVYVMVGADVAFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTQFYIDWCKISLVDKTKQVSTYQEVVRGEGILPDGGEYKPPSDSLKSRDYYTDFLVTLAVPSAVALVLFLILAYIMCCRREGVEKRNMQTPDIQLVHHSSIQKSTKELRDMSKNREIAWPLSTLPVFHPVTGEIIPPMHTDNYDSTNMPLMQTQPNLPHQTQIPQQQTTGKWYP", "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. SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single- pass membrane protein Cytoplasm, cytoskeleton Cell projection, dendrite Golgi apparatus. SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family."}
+{"protein": "MRVNEKYSTLPAEDRSVHIINICAIEDIGYLPSEGTLLNSLSVDPDAECKYGLYFRDGRRKVDYILVYHHKRPSGNRTLVRRVQHSDTPSGARSVKQDHPLPGKGASLDAGSGEPPMDYHEDDKRFRREEYEGNLLEAGLELERDEDTKIHGVGFVKIHAPWNVLCREAEFLKLKMPTKKMYHINETRGLLKKINSVLQKITDPIQPKVAEHRPQTMKRLSYPFSREKQHLFDLSDKDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYAAAYPLHDGDYNGENVEFNDRKLLYEEWARYGVFYKYQPIDLVRKYFGEKIGLYFAWLGVYTQMLIPASIVGIIVFLYGCATMDENIPSMEMCDQRHNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEEAVKDHPRAEYEARVLEKSLKKESRNKEKRRHIPEESTNKWKQRVKTAMAGVKLTDKVKLTWRDRFPAYLTNLVSIIFMIAVTFAIVLGVIIYRISMAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLIFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIPKMKKLIRYLKLKQQSPPDHEECVKRKQRYEVDYNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAVRAKDIGIWYNILRGIGKLAVIINAFVISFTSDFIPRLVYLYMYSKNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSENKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQDKQQLLETWMEKERQKDEPPCNHHNTKACPDSLGSPAPSHAYHGGVL", "text": "FUNCTION: [Isoform 4]: Calcium-activated chloride channel (CaCC). Contributes to calcium-activated chloride secretion in human sweat gland epithelial cells. Shows increased basal chloride permeability and decreased Ca(2+)-induced chloride permeability. FUNCTION: [Isoform 5]: Calcium-activated chloride channel (CaCC). Shows increased sensitivity to intracellular Ca(2+). FUNCTION: Calcium-activated chloride channel (CaCC) (PubMed:20056604, PubMed:22178883, PubMed:21984732, PubMed:22946059, PubMed:32487539). Plays a role in transepithelial anion transport and smooth muscle contraction. Required for the normal functioning of the interstitial cells of Cajal (ICCs) which generate electrical pacemaker activity in gastrointestinal smooth muscles. Acts as a major contributor to basal and stimulated chloride conductance in airway epithelial cells and plays an important role in tracheal cartilage development. Required for CFTR activation by enhancing endoplasmic reticulum Ca(2+) store release and is also required for CFTR membrane expression (PubMed:28963502). Required for basal and ATP-dependent mucus secretion in airways and intestine, probably by controlling exocytosis of mucus-filled granules by providing Ca(2+) to an apical signaling compartment (By similarity). Contributes to airway mucus expression induced by interleukins IL3 and IL8 and by the asthma-associated protein CLCA1 and is required for expression of mucin MUC5AC (PubMed:33026825). However, was shown in another study not to be required for MUC5AC expression (PubMed:31732694). Plays a role in the propagation of Ca(2+) waves in Kolliker's organ in the cochlea and contributes to the refinement of auditory brainstem circuitries prior to hearing onset (By similarity). In vomeronasal sensory neurons, modulates spontaneous firing patterns in the absence of stimuli as well as the firing pattern of pheromone- evoked activity (By similarity). Responsible for calcium-activated chloride channel activity in type I taste cells of the vallate papillae (By similarity). Acts as a heat sensor in nociceptive neurons (By similarity). In dorsal root ganglion neurons, plays a role in mediating non-histaminergic Mas-related G-protein coupled receptor (MRGPR)- dependent itching, acting as a downstream effector of MRGPRs (By similarity). In the developing brain, required for the Ca(2+)-dependent process extension of radial glial cells (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Presynapse Note=In differentiating airway epithelial cells, predominantly intracellular at day 0 but is apically localized by day 30. Expressed in the presynapse of retinal neurons (By similarity). SIMILARITY: Belongs to the anoctamin family."}
+{"protein": "MNIKIILLSIILIIQLLLLNNNGGIVESKINFSKRKQTDRKPNPSPKTYTKEYYDNKYLKSLKNVKQTPNDFLVTDLPGLDNGILTSFSGLLTTNETSDGNLFFWFFPANETVINPMDAPLLVWLNGGPGCSSMDSVFIETGPLRFIGDSDNSDKFYINPWSWHNSANMLYIDQPFGTGLSFVSDNDGLVTNDLEINQNFYQFIQEFFQIFSNYSTLPFFISGESYAGHYIPHMASYILNMNENLSKDSIKINLQGVAIGNGYTHPTTQINSYREFGYYATGIIGQRQYNNYENLNNLCQEQLSQGNYNSDECANVFNTLLDDSGSSNTSQVNMYDYRLNDPTAGNNWPLPGINQEFVYLNRDDVRSAIHATVTPHQWNECNDTVNGLLTNQDESSLYLFPELLSNIRVLIYNGQFDVICNHVGTTEYLNQIEWDYTQEWSDAPRFTWTSVGTDGSLQSGGYGKTAANLTFVLALGGSHMYPMNMPSTSFDMITRFLKNKSFNDLPQSIGIDAPSTPKPVPLTLGAWIGITVGGCAFGFLVGGLIIYIIMKKSSKNGYYKVIQ", "text": "FUNCTION: Probable carboxypeptidase. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase S10 family."}
+{"protein": "MLYLPKKLFLFFFSCIVVIVNYNNSDFVNAANSIGFVNAANSIGLNYGLLGDNLPSPSKVITLYKSIDITKIRIFDPNTEVLNALRGHRDIAVTVGVRDQDLAALSASEEAVKGWFATNIEPYLSDINIAFITVGNEVIPGPIGPQVLPVMQSLTNLVKSRNLPISISTVVAMWNLEQSYPPSAGMFTSQAREQLVPVLKLLSQTNSPILVKIYPYFSYASDPSSIRLDYATFNTEAIVVQDGSLGYSNMFDAIFDAFVWAMEKEGVKDLPMVVSETGWPSAGNGNITTPDIAGTYNRNFVKHIASGKGTPKRPNKGIDGFLFATFNENQKPVGTEQNFGLYNPNDMKPIYNLF", "text": "FUNCTION: May play a role in plant defense against pathogens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 17 family."}
+{"protein": "MTRPASAKRRSLLGILAAGTICAAALPYAAVPARADGQGNTGEAIIHADDHPENWLSYGRTYSEQRYSPLDQINRSNVGDLKLLGYYTLDTNRGQEATPLVVDGIMYATTNWSKMEALDAATGKLLWQYDPKVPGNIADKGCCDTVNRGAGYWNGKVFWGTFDGRLVAADAKTGKKVWAVNTIPADASLGKQRSYTVDGAVRVAKGLVLIGNGGAEFGARGFVSAFDAETGKLKWRFYTVPNNKNEPDHAASDNILMNKAYKTWGPKGAWVRQGGGGTVWDSLVYDPVSDLIYLAVGNGSPWNYKYRSEGIGSNLFLGSIVALKPETGEYVWHFQATPMDQWDYTSVQQIMTLDMPVKGEMRHVIVHAPKNGFFYVLDAKTGEFLSGKNYVYQNWANGLDPLTGRPMYNPDGLYTLNGKFWYGIPGPLGAHNFMAMAYSPKTHLVYIPAHQIPFGYKNQVGGFKPHADSWNVGLDMTKNGLPDTPEARTAYIKDLHGWLLAWDPVKMETVWKIDHKGPWNGGILATGGDLLFQGLANGEFHAYDATNGSDLYKFDAQSGIIAPPMTYSVNGKQYVAVEVGWGGIYPISMGGVGRTSGWTVNHSYIAAFSLDGKAKLPALNNRGFLPVKPPAQYDQKVVDNGYFQYQTYCQTCHGDNGEGAGMLPDLRWAGAIRHQDAFYNVVGRGALTAYGMDRFDTSMTPDEIEAIRQYLIKRANDTYQREVDARKNDKNIPENPTLGINP", "text": "FUNCTION: Dehydrogenase component of the alcohol dehydrogenase multicomponent enzyme system which is involved in the production of acetic acid and in the ethanol oxidase respiratory chain. Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of ethanol to acetaldehyde by transferring electrons to the ubiquinone embedded in the membrane phospholipids. The electrons transfer from ethanol to membranous ubiquinone occurs from pyrroloquinoline quinone (PQQ) to one heme c in subunit I (AdhA), and finally to two heme c in subunit II (AdhB). Besides ubiquinone reduction, ADH also has a ubiquinol (QH2) oxidation reaction which mediates electron transfer from ubiquinol to the non-energy generating bypass oxidase system. The electrons transfer occurs from ubiquinol (QH2) to the additional heme c within subunit II (AdhB). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Periplasmic side. SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family."}
+{"protein": "DPLVFFKXXFXXG", "text": "FUNCTION: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the calreticulin family."}
+{"protein": "SGPWMCYPGQAFQVPALPGCRPLLKLQCNGSQVPEAVLRDCCQQLADISEWPRCGALYSMLDSMYKEHGVSEGQAGTGAFPSCRREVVKLTAASITAVCRLPIVVDASGDGAYVCKDVAAYPDA", "text": "FUNCTION: Alpha-amylase inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha- amylase inhibitor) family."}
+{"protein": "MGLELYMDLLSAPCRAVYIFARKNGIPFDFQFVDLLKGHHHSKEYIEINPLRKLPSLKDGKFILSESVAILFYLCRKYSAPSHWYPPDLHMRARVDEFMAWQHTAIQVPMSKILWIKLIIPMITGEEVPTERLEKTLDEVKRNLQQFEEKFLQDKMFITGDHISLADLVALVEMMQPMGSNHNVFVSSKLAEWRMRVELAIGSGLFWEAHERLVKLPNWDCSTLDPTIKMRICDFLQKFK", "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. Theta family."}
+{"protein": "MAFGGILSEADISAALQNCQAADSFNFKTFFAQSGLSSKSADDVKNVFAILDQDRSGFIEEEELKLFLQNFSASARALTDAETKAFLAAGDSDGDGKIGVEEFQSLVKP", "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": "MSAREGEKRSGVIEEFGFPAEVIQIIGRTGVTGEVTQVRVRILEGRDKGRILTRNVIGPVRIGDILILRETEREARKLSGRR", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS28 family."}
+{"protein": "MQVRIVSLAAQPLFVLRVQGPFAQSLGPGFERLMAWSARHGLRGQWMALYYDNPREVAPDALRADVALTTASVTLPSDGEAYGIRRGALAGGLYALAQVRVTDNDFATPWIALFDQALPACGYRPDGGPCFERYLSDGRGSGEWLLELGVPVRKN", "text": "FUNCTION: Inhibits the supercoiling activity of DNA gyrase. Acts by inhibiting DNA gyrase at an early step, prior to (or at the step of) binding of DNA by the gyrase. It protects cells against toxins that target DNA gyrase, by inhibiting activity of these toxins and reducing the formation of lethal double-strand breaks in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DNA gyrase inhibitor family."}
+{"protein": "MASSKKSKTHKKKKEVKSPIDLPNSKKPTRALSEQPSASETQSVSNKSRKSKFGKRLNFILGAILGICGAFFFAVGDDNAVFDPATLDKFGNMLGSSDLFDDIKGYLSYNVFKDAPFTTDKPSQSPSGNEVQVGLDMYNEGYRSDHPVIMVPGVISSGLESWSFNNCSIPYFRKRLWGSWSMLKAMFLDKQCWLEHLMLDKKTGLDPKGIKLRAAQGFEAADFFITGYWIWSKVIENLAAIGYEPNNMLSASYDWRLSYANLEERDKYFSKLKMFIEYSNIVHKKKVVLISHSMGSQVTYYFFKWVEAEGYGNGGPTWVNDHIEAFINISGSLIGAPKTVAALLSGEMKDTAQLNQFSVYGLEKFFSRSERAMMVRTMGGVSSMLPKGGDVVWGNASWAPDDLNQTNFSNGAIIRYREDIDKDHDEFDIDDALQFLKNVTDDDFKVMLAKNYSHGLAWTEKEVLKNNEMPSKWINPLETSLPYAPDMKIYCVHGVGKPTERGYYYTNNPEGQPVIDSSVNDGTKVENGIVMDDGDGTLPILALGLVCNKVWQTKRFNPANTSITNYEIKHEPAAFDLRGGPRSAEHVDILGHSELNEIILKVSSGHGDSVPNRYISDIQEIINEINLDKPRN", "text": "FUNCTION: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol (DAG), thus forming an sn-1-lysophospholipid. Plays a major role in triacylglycerol formation at log phase (PubMed:12963726, PubMed:26990381). Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains (PubMed:26990381, PubMed:28011631). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
+{"protein": "ATVYNQDGTQVNVGGRVEVAL", "text": "FUNCTION: Structural rigidity of the outer membrane of elementary bodies and porin forming, permitting diffusion of solutes through the intracellular reticulate body membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Gram-negative porin family."}
+{"protein": "MKLTCMMIVAVLFLTAWTLVMADDSNNGLANHFSKSRDEMEDPEASKLEKRACRKKWEYCIVPIIGFIYCCPGLICGPFVCV", "text": "FUNCTION: MuO-conotoxins are gating-modifier toxins that inhibit sodium current by trapping the domain II voltage sensor in the closed position to prevent opening of the sodium channel. This toxin inhibits rNav1.2/SCN2A (IC(50)=532 nM), rNav1.4/SCN4A (IC(50)=438 nM) and rNav1.7/SCN9A (IC(50)=345 nM) (PubMed:10627583). It blocks Nav channels by interacting mainly with the C-terminal part of the pore loop of domain-3 (PubMed:16458302). It does not bind on site 1 (PubMed:8890263). At small concentration, this toxin also acts as a calcium current agonist, whereas at higher doses it blocks fast- inactivating calcium current (PubMed:7727394). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
+{"protein": "MWVFKFLLLPMVSFALSPEEMLDTQWELWKKTHQKQYNSKVDEISRRLIWEKNLKQISAHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLRIPPSRSYSNDTLYTPEWEGRVPDSIDYRKKGYVTPVKNQGQCGSCWAFSSAGALEGQLKKKTGKLLALSPQNLVDCVTENYGCGGGYMTTAFQYVQQNGGIDSEDAYPYVGQDESCMYNATAKAAKCRGYREIPVGNEKALKRAVARVGPISVSIDASLASFQFYSRGVYYDENCDRDNVNHAVLVVGYGTQKGSKHWIIKNSWGESWGNKGYALLARNKNNACGITNMASFPKM", "text": "FUNCTION: Thiol protease involved in osteoclastic bone resorption. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation (By similarity). Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed:12782676). SUBCELLULAR LOCATION: Lysosome Secreted Apical cell membrane; Peripheral membrane protein; Extracellular side Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MASRVQKKDDDESDFLFENLDKGQVIQEKRAFNESPIHPRKCSLVISQFLYLLSRGDSFTKTEATDIFFAATKLFQSKDIPLRRLMYLLLKELSTISQDAIIVISSLTKDMSHKIELYRANAIRILCKITDSSILPQIERYFKQSIVEKDPHVSSAALVSSIHLLKVCPEIVKRWANEVQEAISNKSNMVQYHALALLHRIKQHDRLAVSKLVSNLIKNSLRSPYAQSYLIRCCVEVIEETNTEDRIFREYIESCLRSKNEMVAYEAARSICTFKNVSNKEINSAVGVLQNFLNSTKPTLRFAAVRTLNKLAQTNPTAVIPCNLDMENLITDTNRSIATLAITTLLKVGNESNVERLIKQIANFLGDINDEFKIVVVDAITSLSQKFPKKYKHLIIFLNKILRDEGTLQLKQATLDAILTVVNNIPESKEIALTELCDYIEDCDFPDLSVQILHLIGQEGPLTSSPAQYMRYIYNRVLLDGGIIRAAAVTSIAKFGLLYEPMKEKVVILLQRCLLDEDDEVRDRATLYLKLFKENDVRYLNKVLMDDVPVPLNNLQKSLELYLHQGDFSEPFDIASVSTVVETYQSPLLGDGKSPFSTGASKKGDSVTGTPKSNNASNNNNNNEESSGPESFATKLSQIPQFSTFGKLLKSSEYIELTETETEYVVNCVKHIYREHIVFQFNCTNTLNEQQLSNVSVKMVPSDPKLLKYECSIPIDVLPYGEPQQCYVAIRYIPANGYPLCSFSNALKFKVKEVDPSTGELDEPGYDDQYSLERLEIVPKDFLNRAFVGNFSEEWKKMSEDTQLVQTFSLVGVKSIDEAVKQIIKTLGMAPAEKSEVVTPKSAKHILYLTGKSLNNQLIYVRARMKLDQSQTNTDVELTIKSDDESLNDFVISAFIEK", "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 (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 COPG family."}
+{"protein": "MENVQLENGLERRTTSQSSTSSANPANLASPTEECGCVRLGKCKWFNVAKGWGFLTPNDGGQEVFVHQSVIQMSGFRSLGEQEEVEFECQRTSRGLEATRVSSRHGGSCQGSTYRPRINRRTRRMRCYNCGEFANHIASECALGPQPKRCHRCRGEDHLHADCPHKNVTQSHSNSKSISNNSSSSAAQEKSEEAT", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lin-28 family."}
+{"protein": "MSGFISSTAAQGPPSPAIESYLFGCELSSKTKQYTFEVNEEDDAVHLVCLQTISLGAGAKDEHNVVEVTAPNYQNKEVTVPLANLKLSCQPMVNVGYFEIEAPVTFRLTSGSGPVFISGRHYVVASDDEDLSGSEEEMEDEEEEEDDDDDDDDDDDDDDDDDEEEITPIKPAKKPLKTLSRTF", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the nucleoplasmin family."}
+{"protein": "MGEMEREGAAAKAGAAKTGAAKTGTVAKTGIAAKTGVATAVAAPAAPANVAAAQGAGTKVALGAGKAAAGAKVVGGTIWTGKGLGLGLGLGLGAWGPIILGVVGAGAVYAYMKSRDIESAQSDEEVELRDALA", "text": "FUNCTION: Promotes the formation of magnetite in Fe(2+)-rich conditions, when magnetite is not readily formed (PubMed:27112228). Binds Fe(3+) and Fe(2+) (PubMed:12496282, PubMed:23857056, PubMed:27112228) (Probable). May play a role in nucleation of magnetite crystal formation (Probable) (PubMed:22716969). May help control production of crystals with a specific morphology (Probable) (PubMed:22716969, PubMed:27759096). Greatly improves the formation of magnetosome-like magnetite crystals in vitro (PubMed:12496282). Isolated short protein, probably residues 75-133, binds up to 18 Fe(3+) per monomer and self-assembles into micelles about 21-26 nm in diameter; the C-terminal 21 residues also self-assemble (PubMed:23857056). SUBCELLULAR LOCATION: Magnetosome membrane; Single-pass membrane protein Note=Tightly associated with magnetite crystals (PubMed:12496282). Tagged protein forms straight lines with a punctate pattern extending along most of the cell associated with its inner curvature, in the correct position to be associated with magnetosomes. Under aerobic conditions, when magnetites cannot form, or in the absence of iron, the protein is dispersed in the cell, probably in the inner membrane; as magnetosomes form tagged Mms6 localizes in a line that corresponds to the position of magnetite crystals (PubMed:27481925). Short protein seems to localize specifically to magnetosomes which have magnetite crystals (Probable). SIMILARITY: Belongs to the magnetosome Mms6 family."}
+{"protein": "MLLLLLLPLLWGRERVEGQKSNRKDYSLTMQSSVTVQEGMCVHVRCSFSYPVDSQTDSDPVHGYWFRAGNDISWKAPVATNNPAWAVQEETRDRFHLLGDPQTKNCTLSIRDARMSDAGRYFFRMEKGNIKWNYKYDQLSVNVTALTHRPNILIPGTLESGCFQNLTCSVPWACEQGTPPMISWMGTSVSPLHPSTTRSSVLTLIPQPQHHGTSLTCQVTLPGAGVTTNRTIQLNVSYPPQNLTVTVFQGEGTASTALGNSSSLSVLEGQSLRLVCAVDSNPPARLSWTWRSLTLYPSQPSNPLVLELQVHLGDEGEFTCRAQNSLGSQHVSLNLSLQQEYTGKMRPVSGVLLGAVGGAGATALVFLSFCVIFIVVRSCRKKSARPAADVGDIGMKDANTIRGSASQGNLTESWADDNPRHHGLAAHSSGEEREIQYAPLSFHKGEPQDLSGQEATNNEYSEIKIPK", "text": "FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family."}
+{"protein": "MNSFTSALRPGPLGCSLALLLVVATAFPTSAPVREDSNTKASPDKTLTPPGRTIESIRSILETIKELRKEMCDHDVNCMNRKEALAEVNLHLPRLIEEDGCFPPAVNNETCLLRITSGLMEFRMYLEHLQAKFRSDEENTRVSMVLKNIQHLIKTLRPKVKNLNEEATLKPAVAVSLMENLQQKNQWLKTTTIHFILRGLTNFLEFTLRAVDLMECGCPCLRNFMGSASHGQNTPSCPLDT", "text": "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 (By similarity). 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: 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. 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. Induces, through 'trans-signaling' and synergistically with IL1B and TNF, the production of VEGF. Involved in metabolic controls, is discharged into the bloodstream after muscle contraction increasing lipolysis and improving insulin resistance (By similarity). 'Trans-signaling' in central nervous system also regulates energy and glucose homeostasis. 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 (By similarity). 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 (By similarity). 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": "MDIGVHVLGSVTSNENESLGLKELIGTKQDRSGFIGEDCLQRSLKLARTTTRAEEEENLSSSVAAAYCKTMSFHQGIPLMRSASPLSSDSRRQEQMLSFSDKPDALDFSKYVGLDNSSNNKNSLSPFLHQIPPPSYFRSSGGYGSGGMMMNMSMQGNFTGVKGPFTLTQWAELEQQALIYKYITANVPVPSSLLISIKKSFYPYGSLPPSSFGWGTFHLGFAGGNMDPEPGRCRRTDGKKWRCSRDAVPDQKYCERHINRGRHRSRKPVEVQSGQNQTAAAASKAVTTPQQPVVAGNTNRSNARASSNRSLAIGSQYINPSTESLPNNRGVSIYPSTVNLQPKESPVIHQKHRNNNNPFEFGHISSDSLLNPNTAKTYGSSFLDFSSNQEKHSGNHNHNSWPEELTSDWTQLSMSIPIASSSPSSTHNNNNAQEKTTLSPLRLSRELDLSIQTDETTIEPTVKKVNTWIPISWGNSLGGPLGEVLNSTTNSPTFGSSPTGVLQKSTFCSLSNNSSVSSPIAENNRHNGDYFHYTT", "text": "FUNCTION: Transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues. Component of a network formed by miR396, the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRF family."}
+{"protein": "MSRRLIYVLNINRESTHKIQENEIYTYFSHCNIDHTSTELDFVVKNYDLNRRQPVTGYTALHCYLYNNYFTNDVLKILLNHGVDVTMKTSSGRMPVYILLTRCCNISHDVVIDMIDKDKNHLLHRDYSNLLLEYIKSRYMLLKEEDIDENIVSTLLDKGIDPNFKQDGYTALHYYYLCLAHVYKPGECRKPITIKKAKRIISLFIQHGANLNALDNCGNTPFHLYLSIEMCNNIHMTKMLLTFNPNFEICNNHGLTPILCYITSDYIQHDILVMLIHHYETNVGEMPIDERRIIVFEFIKTYSTRPADSITYLMNRFKNIDIYTRYEGKTLLHVACEYNNTHVIDYLIRINGDINALTDNNKHATQLIIDNKENSPYTINCLLYILRYIVDKNVIRSLVDQLPSLPIFDIKSFEKFISYCILLDDTFYNRHVRNRDSKTYRYAFSKYMSFDKYDGIITKCHKETILLKLSTVLDTTLYAVLRCHNSKKLRRYLTELKKYNNDKSFKIYSNIMNERYLNVYYKDMYVSKVYDKLFPVFTDKNCLLTLLPSEIIYEILYMLTINDLYNISYPPTKV", "text": "SIMILARITY: Belongs to the poxvirinae B18 protein family."}
+{"protein": "MSETYDFLFKFLVIGSAGTGKSCLLHQFIENKFKQDSNHTIGVEFGSRVVNVGGKTVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTDARTLASPNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFLKCARSIPNKIESGELDPERMGSGIQYGDASLRQIRQPRGSAAQTKQQCNC", "text": "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). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MFKFVMVFAVLGLAAAVAPVSRSDDVHAEVKVLSSDVRADGFDTDLVVDNSIQQAASGDIHGNAHGSFSWISPEGEHVDIKYVADENGYQPVGAVLPTPPPIPEAIVRALAWLEAHPQAPEHGAHH", "text": "FUNCTION: Component of the larval cuticle."}
+{"protein": "MASSSSKASDSSSQRPKRPDQGPSGKDAAGLVALHGKLAQLKRQVQSTRLAAIKERVEANRKALQVHTCALFDVAAAAEVASRGAEGGNALSRGAAEGHRRFVGWDSASGPGERELVHVQEENLVAGTLVLSSSGGSGASHRTVVQLVKLPVVDKIPPYTTWIFLDKNQRMADDQSVGRRRIYYDPIVNEALICSESDDDVPEPEEEKHVFTEGEDQLIWKATQDHGLSREVLNVLCQFVDATPSEIEERSEVLFEKYEKQSQSSYKTDLQLFLDKTMDVALDSFDNLFCRRCLVFDCRLHGCSQNLVFPSEKQPYGHELDENKRPCGDQCYLRRREVYQDTCNDDRNACTTYNMDSRSSSLKVSATILSESEDSNRDEDNIKSTSIVETSRSKITNSEYADKSVTPPPGDASETENVSPDMPLRTLGRRKISKHASKSNDHSPDKRQKIYSSPFPFAMSVLNKQSVPEIGETCPDSIESAVDQLPSLDDPNKKISTKDMCAGSTTNTTENTLRDNNNNLFISNKEHSISHWSALERDLYLKGIEIFGKNSCLIARNLLSGLKTCMEVASYMYNNGAAMAKRPLSGKSILGDFAEAEQGYMEQDLVARTRICRRKGRARKLKYTWKSAGHPTVRKRIGDGKQWYTQYNPCGCQQMCGKDCACVENGTCCEKYCGCSKSCKNRFRGCHCAKSQCRSRQCPCFAASRECDPDVCRNCWVSCGDGSLGEPLARGDGYQCGNMKLLLKQQQRILLGKSDVAGWGAFIKNPVNRNDYLGEYTGELISHREADKRGKIYDRANSSFLFDLNEQYVLDAYRKGDKLKFANHSSNPNCYAKVMLVAGDHRVGIYAKDRIEASEELFYDYRYGPDQAPAWARRPEGSKKDEASVSHHRAHKVAR", "text": "FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. 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 (Probable). Involved in the regulation of flowering. Promotes flowering under short day (SD) conditions. Regulates the trimethylation on histone H3 'Lys-27' (H3K27me3) of the flowering regulator LF (PubMed:25400654). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily."}
+{"protein": "MLPPGRNGTAHRARLGLQRQLAQVDAPGGSAAPLGPAQVVTAGLLTLLIVWTLLGNVLVCAAIVRSRHLRAKMTNIFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDIWVAFDIMCSTASILNLCIISVDRYWAISRPFRYERKMTQRVALVMVALAWTLSILISFIPVQLNWHRDKAGSQGREGLLSNETPWEEGWELDGRTENCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSRGACEPDPSLRASIKKETKVFKTLSVIMGVFVCCWLPFFILNCMVPFCSSGDAQGPRTGFPCVSETTFDIFVWFGWANSSLNPIIYAFNADFRKVFAQLLGCSHLCFRTPVQTVNISNELISYNQDTVFHREIAAAYVHMIPNAVSSGDREVGEEEEAEEEGPFDHMSQISPTTPDGDLAAESVWELDCEEEVSLGKISPLTPNCFHKTA", "text": "FUNCTION: Dopamine receptor whose activity 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": "MVSTHIGFPTETVIVFIALSVGAIFIDLFMHRDDKPISLKSAALWSVFWVVVAMAFAGFLYIHHGAEVASLFVTGYALEKVLSVDNLFVMMAIFSWFAVPDRYRHRVLYWGIIGAIVFRGIFVAIGTSLLSLGPYVEVVFAIIVAWTAVMMLKSGDDDDEIEDYSQHLAYRMVKRFFPIWPKLRGHAFLLNQKEVDAELAKPENSDVTIGRGKKAALYATPLFLCVAVVELSDVMFAFDSVPAIIAVSREPLIVYSAMMFAILGLRTLYFVLEALKQYLVHLEKAVIVLLFFIAAKLGLNATDHIWHHGYSIAATTSLYVVLGVLALGILASVMFPGKPESEEKGS", "text": "FUNCTION: Could conceivably alter the intracellular level of tellurium in a manner leading to resistance. Alternatively its presence in the membrane may provide a barrier to entry of the tellurium ions. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TerC family."}
+{"protein": "MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MSDEVTYATLMLQDSARVRGNQDGNNLRKEGHPAQSSLWRGAALSLMTLCLVLVTGLVTLATMFLQVSNDINSDSEKLSQLQKSIHPQQDNLSESLNSSRKSLTEESLQSQISALLERQEQMATKLCKEFLIHASDHKCNPCPKTWQWYGNSCYYFSINEEKSWSDSRKDCIDKNATLVKIDSTEERDLLQSQLSLTFSFFWLGLSWNSSGRNWLWEDGSFPPPTLFSDKELASFNGSRDCAYFERGNIYASRCSAEIPWICEKTASLVKTEDLD", "text": "FUNCTION: Inhibitory receptor postulated to negatively regulate immune and non-immune functions (By similarity). Upon phosphorylation, recruits SH2 domain-containing PTPN6 and PTPN11 phosphatases to its ITIM motif and antagonizes activation signals (By similarity). Although it inhibits KLRK1/NKG2D-mediated signaling, it does not bind known ligands of KLRK1/NKG2D and therefore is not its inhibitory counterpart (By similarity). May limit activation of myeloid cell subsets in response to infection or tissue inflammation (By similarity). May protect target cells against natural killer cell-mediated lysis (By similarity). May negatively regulate cell cycle and differentiation of melanocytes via inactivation of STAT3 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
+{"protein": "MTTTLSSNWKKLSSKLNQGSKVTKQPVKGKNGKTKIKKAELENTLNITPTLQKSTLSPIELALWTKENDINVSDIAVQTEKITLIPQGNDIRKKEPGKYLAMDCEFVGVGPEGTESALARVSIVNFYGHTVFDKFVKPRERVTDWRTWVSGVTPKHMNEAISFQEAQNETSKLLEGRILVGHAIHHDLDALFLSHPKSRIRDTSQYKPFRSISMGKTPSLKKLSSHFLKIDIQGSAHSSVEDARATMLLFRLHRKEFEQSIRTQNRKPEKTS", "text": "FUNCTION: Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the REXO4 family."}
+{"protein": "LDLAKHVIGIASKL", "text": "FUNCTION: Lacks antibacterial activity against Gram-positive or Gram- negative bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
+{"protein": "MEKLTILLLVAAVLMSTQALVERAGENHSKENINFLLKRKRAADRGMWGECKDGLTTCLAPSECCSEDCEGSCTMW", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O2 superfamily."}
+{"protein": "MTAPHKVAFPARCAVNICYDKHLCSQVFPAGIPVEGFFEGMVELFDADLKRKGFDGVALPAGSYELHKINGVRLDINKSLDELGVQDGDTLVLVPRVAGESFEPQYESLSTGLAAMGKWLGRDGGDRMFAPVTSLTAAHTAMAIIAMAVGVVLALTLRTRTITDSPVPAAMAGGIGVLLVIGALVVWWGWRERRDLFSGFGWLAVVLLAVAAACAPPGALGAAHALIGLVVVVLGAITIGVATRKRWQTAVVTAVVTVCGILAAVAAVRMFRPVSMQVLAICVLVGLLVLIRMTPTVALWVARVRPPHFGSITGRDLFARRAGMPVDTVAPVSEADADDEDNELTDITARGTAIAASARLVNAVQVGMCVGVSLVLPAAVWGVLTPRQPWAWLALLVAGLTVGLFITQGRGFAAKYQAVALVCGASAAVCAGVLKYALDTPKGVQTGLLWPAIFVAAFAALGLAVALVVPATRFRPIIRLTVEWLEVLAMIALLPAAAALGGLFAWLRH", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EccD/Snm4 family."}
+{"protein": "MGVYRVCVSTGASIYAGSKNKVELWLVGQHGEVELGSCLRPTRNKEEEFKVNVSKYLGSLLFVRLRKKHFLKEDAWFCNWISVQALGAAEDKYWFPCYRWVVGDGVQSLPVGTGCTTVGDPQGLFQKHREQELEERRKLYQWGSWKEGLILNVAGSKLTDLPVDERFLEDKKIDFEASLAWGLAELALKNSLNILAPWKTLDDFNRIFWCGRSKLARRVRDSWQEDSLFGYQFLNGANPMLLRRSVQLPARLVFPPGMEELQAQLEKELKAGTLFEADFALLDNIKANVILYCQQYLAAPLVMLKLQPDGKLMPMVIQLHLPKIGSSPPPLFLPTDPPMVWLLAKCWVRSSDFQVHELNSHLLRGHLMAEVFTVATMRCLPSIHPVFKLIVPHLRYTLEINVRARNGLVSDFGIFDQIMSTGGGGHVQLLQQAGAFLTYRSFCPPDDLADRGLLGVESSFYAQDALRLWEIISRYVQGIMGLYYKTDEAVRDDLELQSWCREITEIGLQGAQKQGFPTSLQSVAQACHFVTMCIFTCTGQHSSIHLGQLDWFTWVPNAPCTMRLPPPTTKDATLETVMATLPNLHQSSLQMSIVWQLGRDQPIMVPLGQHQEEYFSGPEPRAVLEKFREELAIMDKEIEVRNEKLDIPYEYLRPSIVENSVAI", "text": "FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators (PubMed:9600854, PubMed:9414270, PubMed:15123652, PubMed:17493578, PubMed:18311922). It inserts peroxyl groups at C12 or C15 of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) producing both 12- hydroperoxyeicosatetraenoate/12-HPETE and 15- hydroperoxyeicosatetraenoate/15-HPETE (PubMed:9600854, PubMed:9414270, PubMed:15123652, PubMed:17493578). It may then act on 12-HPETE to produce hepoxilins, which may show pro-inflammatory properties (PubMed:15123652). Can also peroxidize linoleate ((9Z,12Z)- octadecadienoate) to 13-hydroperoxyoctadecadienoate. 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. Can convert epoxy fatty acids to hydroperoxy-epoxides derivatives followed by an intramolecular nucleophilic substitution leading to the formation of monocyclic endoperoxides (By similarity). Plays an important role during the maintenance of self-tolerance by peroxidizing membrane-bound phosphatidylethanolamine which can then signal the sorting process for clearance of apoptotic cells during inflammation and prevent an autoimmune response. In addition to its role in the immune and inflammatory responses, this enzyme may play a role in epithelial wound healing in the cornea through production of lipoxin A4 (LXA(4)) and docosahexaenoic acid-derived neuroprotectin D1 (NPD1; 10R,17S-HDHA), both lipid autacoids exhibit anti-inflammatory and neuroprotective properties. Furthermore, it may regulate actin polymerization which is crucial for several biological processes such as the phagocytosis of apoptotic cells. It is also implicated in the generation of endogenous ligands for peroxisome proliferator activated receptor (PPAR-gamma), hence modulating macrophage development and function. It may also exert a negative effect on skeletal development by regulating bone mass through this pathway. As well as participates in ER stress and downstream inflammation in adipocytes, pancreatic islets, and liver (By similarity). Finally, it is also involved in the cellular response to IL13/interleukin-13 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane; Peripheral membrane protein Lipid droplet Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells. SIMILARITY: Belongs to the lipoxygenase family."}
+{"protein": "MPSTTNTAAANVIEKKPVSFSNILLGACLNLSEVTTLGQPLEVVKTTMAANRNFTFLESVKHVWSRGGILGYYQGLIPWAWIEASTKGAVLLFVSAEAEYRFKSLGLNNFASGILGGVTGGVTQAYLTMGFCTCMKTVEITRHKSASAGGVPQSSWSVFKNIYKKEGIRGINKGVNAVAIRQMTNWGSRFGLSRLVEDGIRKITGKTNKDDKLNPFEKIGASALGGGLSAWNQPIEVIRVEMQSKKEDPNRPKNLTVGKTFKYIYQSNGLKGLYRGVTPRIGLGIWQTVFMVGFGDMAKEFVARMTGETPVAKH", "text": "FUNCTION: Mitochondrial antiporter which catalyzes the transport of citrate and oxoglutarate across the membrane. Also shows specificity for oxaloacetate, and to a lesser extent succinate and fumarate. Transports isocitrate, cis-aconitate and L-malate with very low efficiency. Does not show uniporter activity. Helps to maintain normal citrate levels and NADPH/NADP(+) ratios under conditions of oxidative stress. In addition, associates with the mitochondrial nucleoid and binds DNA in vitro, although the relevance of these data in vivo is unclear. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MKKFLFKQKFCESLPKSFSKTLLALSLGLILLGIFAPFPKVPKQPSVPLMFHFTEHYARFIPTILSVAIPLIQRDAVGLFQVANASIATTLLTHTTKRALNHVTINDQRLGERPYGGNFNMPSGHSSMVGLAVAFLMRRYSFKKYFWLLPLVPLTMLARIYLDMHTIGAVLTGLGVGMLCVSLFTSPKKP", "text": "FUNCTION: Removes the 1-phosphate group from tetra- and probably hexaacylated lipid A species, has no requirement for the Kdo moiety of lipid A (PubMed:15489235). Has no 4'-phosphatase activity (PubMed:15489235, PubMed:16740959). Has no activity on phospholipids (phosphatidylglycerol, phosphatidylethanolamine or cardiolipin). This enzyme has to act before EptA can attach phosphoethanolamine to the 1- position of lipid A (PubMed:16740959). Absence of the 1-phosphate group renders the bacteria partially resistant to host-derived cationic antimicrobial peptides (CAMP), allowing it to camouflage itself from the host innate immune response, and plays a role in the long-term colonization of the host's stomach (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Note=Activity depends on msbA function when expressed in E.coli, strongly suggesting this protein acts in the periplasm (MsbA flips the lipopolysaccharide precursor across the inner cell membrane). SIMILARITY: Belongs to the lipid A LpxE 1-phosphatase family."}
+{"protein": "MIDLFDFVVLSSFIILLPLVTDFLNNTFPNAKIGRLAQEVVGMILVFFIVSLIFAGVSLWYTHFLPFYYTKSLLISFDTLNLLDLLKFINTDNNNNSGSSIFNKITFYFHIFFTIQLVVNLYYYYYQTITADNFLPKISKNKQIQLFASETTTTTTTTTDNINEKKNKLCGLCDQVSDGKWSTINKPKSHHCRICKRCIDSMDHHCPFAANCIGINNHHYFILFIGYTVMALIYACYLSFFPYYHCIVNYKNYVSLSFTNDNDNDNNNNNNFKQLAQSCAKFNKYSFIFLCCCLIVTASFGILLFQTYLIITNSKTVQLLSRLKKSKSFLDWFKWLYQNFKQNASINNIYSLFPNFKFYNLIIPYYKRKINKLNK", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
+{"protein": "MAFVASVPVFANASGLKTEAKVCQKPALKNSFFRGEEVTSRSFFASQAVSAKPATTFEVDTTIRAQAVDAKKKGDIPLNLFRPANPYIGKCIYNERIVGEGAPGETKHIIFTHEGKVPYLEGQSIGIIPPGTDKDGKPHKLRLYSIASTRHGDFGDDKTVSLSVKRLEYTDANGNLVKGVCSNYLCDLKPGDEVMITGPVGTTMLMPEDQSATIIMLATGTGIAPFRSFLRRMFEETHADYKFNGLAWLFLGVPTSSTLLYREELEKMQKANPNNFRLDYAISREQTDSKGEKMYIQNRIAEYANEFWNMIQKPNTFVYMCGLRGMEDGIQQCMEDIAKANGTTWDAVVKGLKKEKRWHVETY", "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. SUBCELLULAR LOCATION: Plastid, cyanelle stroma. Plastid, cyanelle thylakoid membrane; Peripheral membrane protein; Stromal side Note=In the vicinity of the photosystem I. SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family."}
+{"protein": "MGAAKNIWALANAEDAANDAEQIPYSSFVVDTSLPLPLMIPRIIELCKDLFKNWGELDDSLFSVERVSGGITNLLLKVSVKEDTNKEVSVTVRLYGPNTEYVINREREILAIKYLSAAGFGAKLLGGFGNGMVQSFINARTLEPSDMREPKIAAQIARELGKFHKVDIPGSKEPQLWVDILKFYEKASTLTFEEPDKQKLFETISFEELHKEIIELREFTGLLNAPVVFAHNDLLSGNFMLNDEEEKLYLIDFEYGSYNYRGFDIGNHFNEYAGYDCDYSLYPSKEEQYHFIKHYLQPDKPDEVSIAEVESVFVETDAYKLASHLYWAIWAIIQARMSPIEFEYLGYFFLRYNEYKKQKPLTFSLVTSHLSASL", "text": "FUNCTION: Involved in phospholipid biosynthesis. Catalyzes the first step in phosphatidylethanolamine biosynthesis (By similarity). SIMILARITY: Belongs to the choline/ethanolamine kinase family."}
+{"protein": "MKFSTVGFLFSTILFKSAFAGWMDTHMKDEHHIDKYTDESFFRLHDLGKKGYWSDQDILSLYGLFENDEVPFVKKNEVLVDVLKKCDPSGNRRITLDEFLAFRKNGGELTDFGFPGHHGDEEEEFEMHHVEKYHPAGLDEPDENWNHPEDIEHFQKHDEIFHGDKKPEERRKHFVKYNNIPDKYRRVSI", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Golgi apparatus lumen."}
+{"protein": "MMLHAQHMPGQPGAPSLVFLHGFSGDCREWQPVGEQFHGCSRLYIDLPGHGGSAAIPVGGFADVIRLLRATLISYNILKFWLVGYSLGGRVAMMAACQGIPGLCGLVVEGGHPGLQNEQARAERRLSDGRWAERFRHEPLTEVFHDWYQQPVFASLTAQQRQALTALRSQNNGETLAAMLEATSLAVQPDLREALNALAFPFYYLCGERDSKFRALAQEVAATCHVIRNAGHNAHRENPAGVVDSLAQILRL", "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": "MLFKKFTWVIPSLFLTIISTSLLISCATKSDNTLIFNISLDHNADTSIEKFFTVFSKKLSGKLNKKINVNFNIVDDSFTKINNIQANKADFAFVNSQAIASNNWFGYTPLIQTLTTAFKEDLELDYYEDGNLQKKAEKTNLLFLSPPYKEWDDIKQKWTGNRYDFLYEPSKLVSFYRSMILITGSASEITAIKKAWNEKNWNQFMKFGIGHGQTNSASRFELPDLLFRKHFAKNYPGLQNAINSDPDKFAVVRGREIGINKNIKIVFDDANSFSWTQNIKGSKRPFYTPIDPNDRLEILTYSDPLLYDIGIVSNNLSRIYQKAIGEIFIELAQSSEDLYGPSIGYNGYKMINDFEKEVVEIIEKTYGK", "text": "FUNCTION: P37 is part of a high-affinity transport system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
+{"protein": "MAHENVWFSHPRNFGKGSRQCRHCSSHSGLIRKYGLDLCRQCFREKAADIGFNKYR", "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 uS14 family."}
+{"protein": "MAENKRVISIENRIPELKKYRKKKLVRHLAILIGIFVILIAITLYFLSPLSKLDKIAVSGNKQLTENEVRKESGLEIGEFVIGISNGKTEDALKKNTLIKDATVSKEGLNDVQINITEFKTIGYQQQDGKYYDVLESGIMLTDQPRQFPIGNDLLFQNFKNGKTLEKMVDQINKLPKDVVSSISEVIYSPTKSDKNHIKLYMNDGNQVSADISTFAEKMQHYPAIVAQLAKGQKGVIDIEVGSYFQSYYQQNAEKKATEEAAKEKKETNE", "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": "MVTHAAGARTFCEEQKKGSTYSVPKSKEKLMEKHSQEARQADRESEKPVDSLHPGAGTAKHPPPAASLEEKPDVKQKSSRKKVVVPQIIITRASNETLVSCSSSGSDQQRTIREPEDWGPYRRHRNPSTADAYNSHLKE", "text": "FUNCTION: Plays an important role in sperm motility and male fertility (By similarity). Required for sperm midpiece flexibility and for the localization of sperm calcineurin to the mitochondria (By similarity). Promotes mitophagy as well as acts as an autophagy mediator in male germline cells (By similarity). Links damaged mitochondria to autophagosomes via its binding to the outer mitochondrial membrane protein VDAC2, as well as to key autophagy machinery component ATG16L1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Cytoplasm Mitochondrion."}
+{"protein": "MQTIDVLIVGGGVIGTSCAYELSQYKLKVALLEKNAFLGCETSQANSGVIHSGIDPNPNKLTAKYNILGRKIWIEDWFKKLIFPRKKIATLIVAFNNEEKLQLNLLKERGIKNSIPVENIQILDQQQTLLQEPFINPNVVASLKVEGSWLIDPLIATKCLALASLQNNVAIYSNKKVTKIEIDSDDDFLVFINNETTPQFKTKKLIDAAGHYADWLAETTQVDNFKQTTRKGQYLVLKNQNNLKINTIIFMVPTIHGKGVVVAEMLDGNILVGPNAVEGIEKNKTRSIDLDSINQIKTIGKKMVPSLQFENSIYSFAGSRAIDIETNDFVIRTAKSNPNFIILGGMKSPGLTSSPAIAKRAVELLNLKLKKKINWNPNYNLSWI", "text": "FUNCTION: Catalyzes the oxidation of glycerol 3-phosphate to dihydroxyacetone phosphate (DHAP), with a reduction of O2 to H2O2. The formation of hydrogen peroxide by this enzyme is crucial for cytotoxic effects on host cells. Does not show any dehydrogenase activity with NAD(+). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Lipid-anchor."}
+{"protein": "MVLYTTPFPNSCLSALHAVSWALIFPCYWLVDRLLASFIPTTYEKRQRADDPCCLQLFCTVLFTPVYLALLVAALPFAFLGFIFWSPLQSARRPYSYSRLEDKNPAGGAALLSEWKGTGAGKSFCFATANVCLLPDSLARLNNVFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSISAASFSSLVSPQGGDGSRAVPGSIKRTASVEYKGDGGRHPSDEAANGPASGEQADGSLEDSCIVRIGGEEGGRPQEADDPAAGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSPSASRESLVKARAGQDSGGSGEPGANSKLLYKTSVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGCCNFKCLNSGLFFASRYPVMDVAYHCYPNGCSFDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPPEDSAVRCEQLDLLQDWLADFRKSTSSTSTANPEELVVFDVICGDLNFDNCSSDDKLEQQHSLFTRYKDPCRLGPGEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSPGAGQKGRKDLLKGNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSAGEEEA", "text": "FUNCTION: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization (PubMed:15051724, PubMed:15764706, PubMed:15929065, PubMed:16025116). Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location (PubMed:21550973). May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor Cell membrane; Lipid- anchor Note=May localize to detergent- resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:15764706). SIMILARITY: Belongs to the neutral sphingomyelinase family."}
+{"protein": "MSTDGNNNKKGSKEGPKSSEISKFDLAKENPKLAEWMDDCIKRMNSLYKDTNINICNVMTGHEIISIIRMVEAIFMEESNLCEAEAPIKVIGDIHAQYQDMNRLFDLIGRVPEEKLMFLGDYVDRGPQGIEVLILLFCLKIRYRDRIYLLRGNHETPSVNKIYGFYVECQYKYGIGLWWDFQSCFNRMPMSGLISKRVLCMHGGLSPELINLDTIRNIPRPCEPLDRGLLIDLLWSDPTNKGEGWFHSIRGISYMFGKGVVEQACKSLEIDLIIRAHQVVQDGYEMMTGRRLITVFSVPNYCAQFTNAAAVVCLNANLQISFQQMIPPPLPEGTKAKAAPAIAIDPNIDAARADKDAIKPFVKE", "text": "SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily."}
+{"protein": "MLRGARSHLPASVAPAAVLAAALLSSFARCSLPGRGDPVASVLSPYFGTKTRYEDANPWLLVDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLKQLQGLLQTRESRDGGSQVAAALAEWPLWYGDWMDGQLVEKGRQDMRQLALRLAALFPDLFSRENYDRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECGPPRINDKLMRFFDHCEKFLTDVERNETALYHVEAFKTGPEMQKVLKKVAATLQVPMNSLNADLIQVAFFTCSFDLAIKGVHSPWCDVFDVDDARVLEYLNDLKQYWKRSYGYTINSRSSCNLFQDIFLHLDKAVEQKQRSQPVSSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNFEEQVNRKFRSGHIVPYASNLIFVLYHCDNAQSPEEQFQIQLLLNEKVLPLAHSQRPVGLYEELKTHYRDILQSCQTSKECSPPKANITSDEL", "text": "FUNCTION: Acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate (By similarity). Acts as a phosphoinositide 5- and phosphoinositide 6- phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). May play a role in bone development (endochondral ossification). May play a role in the transition of chondrocytes from proliferation to hypertrophy (By similarity). Through the regulation of intracellular inositol polyphosphates, may control intracellular cation homeostasis, including that of calcium and iron, hence affecting free cation availability required for neural cell signaling (PubMed:33257696). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Cell membrane Note=Also attached to the plasma membrane in erythrocytes. SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1 subfamily."}
+{"protein": "RGPKNWCKVHPCWTTCGSQMRQSPININTNQTIYKRYPRLKVENVHKRVIATIRNNGHAPYFEVHEKFDDEIVLRNVPERPRRKEYNFAQLHVQLGRDEKEGSEHSIDNKFKPMEAQMVFYDKDYEDVLEAKSKKNGLVVISVMIEVYGRSKEHDDCACDGETCTVRYVRKLSKLMEKYYEKVRRYPLVSINPHFLTFIKLPRKCWYNKCGRTPSPDFIEKKCEKEEPETRPFFVFEGITPLDVIPYDTNRFYTYAGSLTSPPCYETVQWVVFKCPIKVSSKAFRMLQLVQDSHLDPLEKLGVRRPLQTNKNVIVYRNHLK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
+{"protein": "MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNFEFVAMPALAPPEVVMDPALAAQYEQDLQHAQATALPDEDDDL", "text": "FUNCTION: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. SUBCELLULAR LOCATION: Nucleus Nucleus envelope Cytoplasm, cytosol Cytoplasm Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Ran family."}
+{"protein": "MAGCCCLSAEEKESQRISAEIERQLRRDKKDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDRKGFTKLVYQNIFTAMQAMIRAMDTLRIQYMCEQNKENAQIIREVEVDKVTALSRDQVAAIKQLWLDPGIQECYDRRREYQLSDSAKYYLTDIERIAMPSFVPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFESVTSIIFLVALSEYDQVLAECDNENRMEESKALFRTIITYPWFLNSSVILFLNKKDLLEEKIMYSHLISYFPEYTGPKQDVKAARDFILKLYQDQNPDKEKVIYSHFTCATDTENIRFVFAAVKDTILQLNLREFNLV", "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. G(q) subfamily."}
+{"protein": "MAIQFVINLLVSVIWLLVTNSYTLNNFVLGFILGLFLVYLLHRVLPGQFYLVRIYRIIMLIITFLTELIKANFGVLKIILKPRIENKPGFFVYETELERDWQLVLLSNLITLTPGTVVLGISDDRKKIYIHSIDFSTKEEEIQNIKSSLEKVVRKVGEK", "text": "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 E family."}
+{"protein": "MGLDQDKIKKRLSQIEIDINQMNQMIDENLQLVEPAEDEAVEDNVKDTGVVDAVKVAETALFSGNDGADSNPGDSAQVEEHKTAQVHIPTENEANKSTDDPSQLSVTQPFIAKEQITHTAIAIGDSYNSFVANSAGNEKAKDSCTENKEDGTVNIDQNRGEADVEIIENNDDEWEDEKSDVEEGRVDKGTEENSEIESFKSPMPQNNTLGGENKLDAELVLDKFSSANKDLDIQPQTIVVGGDNEYNHESSRLADQTPHDDNSENCPNRSGGSTPLDSQTKIFIPKKNSKEDGTNINHFNSDGDGQKKMANFETRRPTNPFRVISVSSNSNSRNGSRKSSLNKYDSPVSSPITSASELGSIAKLEKRHDYLSMKCIKLQKEIDYLNKMNAQGSLSMEDGKRLHRAVVKLQEYLDKKTKEKYEVGVLLSRHLRKQIDRGENGQFWIGTK", "text": "FUNCTION: Required for normal septin function and cytokinesis. SUBCELLULAR LOCATION: Cytoplasm. Bud. Note=Arrives at the bud site approximately coincident with bud emergence and dissociates from the septin scaffold before cytokinesis."}
+{"protein": "MVKFPALTHYWPLIRFLVPLGITNIAIDFGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSKRDRAKAVLCMVVAGAIAAVFHTLIAYSDLGYYIINKLHHVDESVGSKTRRAFLYLAAFPFMDAMAWTHAGILLKHKYSFLVGCASISDVIAQVVFVAILLHSHLECREPLLIPILSLYMGALVRCTTLCLGYYRNIHDIIPDRSGPELGGDATIRKMLSFWWPLALILATQRISRPIVNLFVSRDLGGSSAATEAVAILTATYPVGHMPYGWLTEIRAVYPAFDKNNPSNKLANTSNTVTSAHIKKFTFVCMALSLTLCFVMFWTPNVSEKILIDIIGVDFAFAELCVIPLRIFSFFPVPVTVRAHLTGWLMTLKKTFVLAPSSVLRIIVLITSLVVLPYLGVHGATLGVGSLLAGFVGESTMVALAACYVYRKQKKKMENESATEGEDSAMTDMPPTEEVTDIVEMREENE", "text": "FUNCTION: Regulates intra- and extracellular levels of inorganic pyrophosphate (PPi), probably functioning as PPi transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ANKH family."}
+{"protein": "MRTLLLTILIFFFTVNPISAKFYTNVSSIPPLQFLNATQNAWETFSKLAGCHIGENINGLSKLKQYFRRFGYITTTGNCTDDFDDVLQSAINTYQKNFNLKVTGKLDSSTLRQIVKPRCGNPDLIDGVSEMNGGKILRTTEKYSFFPGKPRWPKRKRDLTYAFAPQNNLTDEVKRVFSRAFTRWAEVTPLNFTRSESILRADIVIGFFSGEHGDGEPFDGAMGTLAHASSPPTGMLHLDGDEDWLISNGEISRRILPVTTVVDLESVAVHEIGHLLGLGHSSVEDAIMFPAISGGDRKVELAKDDIEGIQHLYGGNPNGDGGGSKPSRESQSTGGDSVRRWRGWMISLSSIATCIFLISV", "text": "FUNCTION: Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (By similarity). Active on Mca-KESAbuNLFVLKDpaR-NH(2) (QF75) and, to some extent, on McaPLGLDpaAR-NH(2) (QF24), myelin basic protein (MBP) and beta-casein (PubMed:24156403). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side. SIMILARITY: Belongs to the peptidase M10A family. Matrix metalloproteinases (MMPs) subfamily."}
+{"protein": "MDSTVPSALELPQRLALNPRESPRSPEEEEPHLLSSLAAVQTLASVIRPCYGPHGRQKFLVTMKGETVCTGCATAILRALELEHPAAWLLREAGQTQAENSGDGTAFVVLLTEALLEQAEQLLKAGLPRPQLREAYATATAEVLATLPSLAIQSLGPLEDPSWALHSVMNTHTLSPMDHLTKLVAHACWAIKELDGSFKPERVGVCALPGGTLEDSCLLPGLAISGKLCGQMATVLSGARVALFACPFGPAHPNAPATARLSSPADLAQFSKGSDQLLEKQVGQLAAAGINVAVVLGEVDEETLTLADKYGIVVIQARSWMEIIYLSEVLDTPLLPRLLPPQRPGKCQRVYRQELGDGLAVVFEWECTGTPALTVVLRGATTQGLRSAEQAVYHGIDAYFQLCQDPRLIPGAGATEMALAKMLSDKGSRLEGPSGPAFLAFAWALKYLPKTLAENAGLAVSDVMAEMSGVHQGGNLLMGVGTEGIINVAQEGVWDTLIVKAQGFRAVAEVVLQLVTVDEIVVAKKSPTHQEIWNPDSKKTKKHPPPVETKKILGLNN", "text": "FUNCTION: Possible molecular chaperone; assists the folding of proteins upon ATP hydrolysis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
+{"protein": "MSEVTRSLLQRWGASFRRGADFDSWGQLVEAIDEYQILARHLQKEAQAQHNNSEFTEEQKKTIGKIATCLELRSAALQSTQSQEEFKLEDLKKLEPILKNILTYNKEFPFDVQPVPLRRILAPGEEENLEFEEDEEEGGAGAGSPDSFPARVPGTLLPRLPSEPGMTLLTIRIEKIGLKDAGQCIDPYITVSVKDLNGIDLTPVQDTPVASRKEDTYVHFNVDIELQKHVEKLTKGAAIFFEFKHYKPKKRFTSTKCFAFMEMDEIKPGPIVIELYKKPTDFKRKKLQLLTKKPLYLHLHQTLHKE", "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": "MTAHANERISDVSPSARGSSSESKYDKLCRVLFFIAITKSSFTPEHILYKHSIFTDKPILADIVTFMYAAFVSIGWFLIWGERAYRTQEMGQPPMYSNINYHLLSFKKRHPKKFTCALWLVFFLAYTVLTVLIWLVQLIFRKGNVFQMLLQLIILDIAIALVNVAIAFTFEIYLSQKAAIEIRDEGLNNLDTA", "text": "FUNCTION: May be required for cell cycle progression. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
+{"protein": "MRPAVLGSPDRAPPEDEGPVMVKLEDSEEEGEAALWDPGPEAARLRFRCFRYEEATGPQEALAQLRELCRQWLRPEVRSKEQMLELLVLEQFLGALPPEIQARVQGQRPGSPEEAAALVDGLRREPGGPRRWVTVQVQGQEVLSEKMEPSSFQPLPETEPPTPEPGPKTPPRTMQESPLGLQVKEESEVTEDSDFLESGPLAATQESVPTLLPEEAQRCGTVLDQIFPHSKTGPEGPSWREHPRALWHEEAGGIFSPGFALQLGSISAGPGSVSPHLHVPWDLGMAGLSGQIQSPSREGGFAHALLLPSDLRSEQDPTDEDPCRGVGPALITTRWRSPRGRSRGRPSTGGGVVRGGRCDVCGKVFSQRSNLLRHQKIHTGERPFVCSECGRSFSRSSHLLRHQLTHTEERPFVCGDCGQGFVRSARLEEHRRVHTGEQPFRCAECGQSFRQRSNLLQHQRIHGDPPGPGAKPPAPPGAPEPPGPFPCSECRESFARRAVLLEHQAVHTGDKSFGCVECGERFGRRSVLLQHRRVHSGERPFACAECGQSFRQRSNLTQHRRIHTGERPFACAECGKAFRQRPTLTQHLRVHTGEKPFACPECGQRFSQRLKLTRHQRTHTGEKPYHCGECGLGFTQVSRLTEHQRIHTGERPFACPECGQSFRQHANLTQHRRIHTGERPYACPECGKAFRQRPTLTQHLRTHRREKPFACQDCGRRFHQSTKLIQHQRVHSAE", "text": "FUNCTION: Binds to target promoter DNA and functions as transcription regulator. Regulates transcription from the PADI1 and CDH2 promoter. May be one regulator of transcriptional events during hemopoietic development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MSLSATQLKALEDSVLNTSGKVLLHDRVRALFTLKSLKNEDAIRIISKGFQDSAALLKHELAYCLGQIRNPLALPVLESVLRNPSEDPMVRHEAAEAMGAISTADSIPILKQYLSDPDRSVRETCEIAIAKIEWDKTEEGAKNDKATRDENRLPLYTSIDPAPATSGLLTGAPRPEEISQTKIDELRDNLLDVNRPLFERYRAMFALRNIGSPAAVDALAAGFSGDSALFKHEIAFVFGQLLSPHSVPCLIEVLQNSPESDMVRHEAAEALGGIATPEVLPPLKEWVARDDAPVVVRESCQVALDLWEYENSGDFQYANGLESPSTPISV", "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": "MAPRPLRRHPPLHHSFHESRRDPVADKHRINFEPVDIEMEVGEDEYILDAAFRQGIHLMHGCREGRCSACKSFVLEGDIQMEDYSTFACNDAEVDEGHVLLCRSTAYSDCTIELLNFDEDELLGGVPIQDVRTRVTRIEPMTKDIVSLRLAPVEPAGYEFKPGQYSDLHIPGTEEHRSFSMATTRSTPGHVEFLIKKYPGGKFAGLLEDGISVGDEIALTGPYGSFTIKEGHVLPMVFIGGGAGMAPLLSLLRHMSETGNTRQVHFYYGARTPQDLFYVDEILELGRGLTDFTFVACLSESMDPPPVGAIAVEDGNVTDVVGRREPDIGRAEVYLCGPPPMVDAALELLEANGTPKDQIFYDKFTSPAFE", "text": "FUNCTION: Reductase component of the propane 2-monooxygenase multicomponent enzyme system which is involved in the degradation of propane via the O2-dependent hydroxylation of propane. Reductase catalyzes the transfer of electrons from NADH or NADPH to monooxygenase (Probable). SIMILARITY: Belongs to the TmoA/XamoA family."}
+{"protein": "MGFTLKSLEFLQGVEPFRIDENHENEGASEEEEVLISAETDAGMSLMLEWKMRLSEDSDQCTTCNCPVDFGDRAVLLEHYQSLFHRTNTLRKARNMTVYTEEDFEGIENSENDLTSSQTTIGLESDDEEFDALLLPANRSFFIKNGSVFSVPRNILHVGERDVSSVTFLRPFDCAIFLWNGGHFAAAMFENDKMTVQKSFHRYVARAKQGGVQSQHDSGGKGAAKSAGAQLRRYNEQKMKEEIQSIMSSWKSRLQKTPLLFIRCAAYHRNIFFEADAGIETRDDRIRTIPFETKRPNIDEISDCWQRLQQVSEHGAESDFRAEMLEVREKRKKLARKVAGKKRKDGGMQMICEWSDDDENEDISKEKKTHHIKVRTIKKPEETVVQWPRLDDEWRQKTYNYVRQDSVEALKEHLASLNEDVTSEANDYLRNAKIPPNRSTFLHVSAANDARKCLKYFLEEVNCDSSTKDGAGLPPYSSSANSDVKSIFIDYRVKNETAGNWARTHIPEPKKKVELTEEQEREQAERKKEKKARQKEKEKLKKEIAKRDVEEMEERQKYVNMSEREKRALAVDRRLAGLPPILRCHQCGVQLPPTPFQYSHYNFCSTSCVAEHRKANPQ", "text": "FUNCTION: Endonuclease that cleaves polypeptidyl-tRNAs downstream of the ribosome-associated quality control (RQC) pathway to release incompletely synthesized polypeptides for degradation (By similarity). The RQC pathway disassembles aberrantly stalled translation complexes to recycle or degrade the constituent parts (By similarity). Dispensable for viability and growth but is required for protection against oxidative stress and for wild-type life span (PubMed:21070972). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Note=translocates from the cytosol to mitochondria upon exposure to hydrogen peroxide. SIMILARITY: Belongs to the ANKZF1/VMS1 family."}
+{"protein": "MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKDPEERPTFEYLQAFLEDYFTSTEPPVPAWREPIGLELLLAPEASLWGTGAWLRAEGPRFGEQPQSRMWHGEVSGAPSLIKTVLGHP", "text": "FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily."}
+{"protein": "MRFLSLAPDRPRRGGPRHLPSGSPAPPPPPPLLLLLLLGGCLGVSGAAKGSRRPNVVLVLADDQDEVLGGMTPLKKTKALIGEMGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPNTFPAILRSMCGYQTFFAGKYLNEYGAPDAGGLGHVPLGWSYWYALEKNSKYYNYTLSINGKARKHGENYSVDYLTDVLANVSLDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQNAFQNVFAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIQFLDNAFRERWQTLLSVDDLVEKLVKRLEFNGELNNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIKPNQTSKMLVANIDLGPTILDIAGYGLNKTQMDGMSFLPILRGASNLTWRSDVLVEYQGEGRNVTDPTCPSLSPGVSQCFPDCVCEDAYNNTYACVRTMSELWNLQYCEFDDQEVFVEVYNLTADPHQLNNIAKSIDPELLGKMNYRLMMLQSCSGPTCRTPRVFDPGYRFDPRLMFSNHGSVRTRRFSKHLL", "text": "SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the sulfatase family."}
+{"protein": "MFRPASRALLRAPAVARGPASRRLISTAPAESKPRSWKNTAVRLGLAAGAIYYYNTSNVFAENPSFSLNNQLKKNSAEEPLPTLDSIKPRIREERESAAPKPNAEQAPAQELPFGEGAVKSPQELEEEAGQEAAFNPETGEINWDCPCLGGMAHGPCGEEFKAAFSCFVYSEEEPKGMDCIEKFKCV", "text": "FUNCTION: Required for the import and folding of small cysteine- containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of 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 (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass type II membrane protein; Intermembrane side."}
+{"protein": "MEDLLDLDEELRYSLATSRAKMGRRAQQESAQAENHLNGKNSSLTLTGETSSAKLPRCRQGGWAGDSVKASKFRRKASEEIEDFRLRPQSLNGSDYGGDIPIIPDLEEVQEEDFVLQVAAPPSIQIKRVMTYRDLDNDLMKYSAIQTLDGEIDLKLLTKVLAPEHEVREDDVGWDWDHLFTEVSSEVLTEWDPLQTEKEDPAGQARHT", "text": "FUNCTION: As a component of IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein- coupled receptors (GPCRs), it is involved in ciliogenesis (PubMed:28400947, PubMed:28973684). Involved in retrograde ciliary transport along microtubules from the ciliary tip to the base (PubMed:21378380). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, cilium Note=Associated with microtubules (PubMed:22361696). Localized at the distal tip of the cilium (PubMed:28973684). SIMILARITY: Belongs to the IFT43 family."}
+{"protein": "RKPCGKNEVWTECTGCELKCGQDEKTPCALMCRPPSCECTPGRGMRRTHDGKCVPVSECPRKMPK", "text": "FUNCTION: Defends the organism against the host's proteinases. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serine protease inhibitor-like (TIL domain- containing) family."}
+{"protein": "MSDINATRLPIWGIGCNPCVGDEVAALLTRGEALC", "text": "FUNCTION: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24050899). SIMILARITY: Belongs to the MSDIN fungal toxin family."}
+{"protein": "MDKKVSFTSSVAHSTPPYLSTSISWGLPTKSNGVTESLSLKVVDARPERLINTKNISFQDQDSSSTLSSAQSSNDVTSSGDDNPSRQISFLAHSDVCKGFEETQRKRFAIKSGSSTAGIADIHSSPSKANFSFHYADPHFGGLMPAAYLPQATIWNPQMTRVPLPFDLIENEPVFVNAKQFHAIMRRRQQRAKLEAQNKLIKARKPYLHESRHVHALKRPRGSGGRFLNTKKLQESTDPKQDMPIQQQHATGNMSRFVLYQLQNSNDCDCSTTSRSDITSASDSVNLFGHSEFLISDCPSQTNPTMYVHGQSNDMHGGRNTHHFSVHI", "text": "FUNCTION: Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NFYA/HAP2 subunit family."}
+{"protein": "MLAPMAGVTNVTFRTLCREFGSTRGNLLRPAPPHLRSPLEQSQVGTISGLYVCEMVTARALVERNAVTIHMTTFAPDESPRSLQLYTVDPATTYTAAKMVADEGLADHIDMNFGCPMPKVTRRGGGAALPYKRRLFGQIVAAAVRATEGTKIPVTVKFRIGIDDEHHTHLDAGRIAEAEGAAAVALHARTAAQRYSGTADWAQIAQLKQQVRTIPVLGNGDIYDASDALAMMAVTGCDGVVIGRGCLGRPWLFAELSAAFTGRPAPAPPTLGEVAEIVRRHGKLLVAHFGEDKGMRDIRKHIAWYLHGFPAGSELRNALALVKTLDELDCLLNRLDGAVPFPDAAIGPRGRQGSPAWVALPDSWLTDPDDCTVPIGADIMESGG", "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": "ACTLECEGKLPSAKAWGTCKELLQLTKLDGVQDGEKYQDNNDSHYIAKKYGGFMKRYGGFMKKMDELYHAEPEEDDAGGEILAKNYGGFMKKEYDSNRDASDLLRELLATSGDPESAIYHDNNSETPGEMNKRYGGFMRGYRRSTDLEDETRGIQKRYGGFMRRVGRPEWWQDYQKRYGGFMTRFTDSFLPSDEDGESYSKENPDMEKRYGGFMRF", "text": "FUNCTION: Enkephalin neuropeptides 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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the opioid neuropeptide precursor family."}
+{"protein": "MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGQ", "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). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ubiquitin family."}
+{"protein": "MADKEKKKKESILDLSKYIDKTIRVKFQGGREASGILKGFDPLLNLVLDGTIEYMRDPDDQYKLTEDTRQLGLVVCRGTSVVLICPQDGMEAIPNPFIQQQDA", "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) (PubMed:28781166). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA (PubMed:10523320). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the snRNP Sm proteins family."}
+{"protein": "MPRAGVAASAFKLRNIWHIHNLHRVRSQQTRLMSDSVEEFSSVFQHAKKVVVLTGAGISAESGIPTFRGEGGLWRDFDATELATPGAFAANPSLVWEFYHYRRTIVAGASPNAGHYAVAALQRRCRRLGKDFILLTQNIDGLHAKAGSTDVVELHGSLWETRCCHCKAVEANRNMPICPALDGKGAPDTVHEANIPSMQLPRCNKCNGLLRPRVIWFGECLERDVLRRTDDALQGCDLLLVVGTSAVVYLFWRNMMEVELHTDFVESLLQDDRLRSRIGLALREKSQYLLVAFRRFKFQGPSSVKLPTALGIGEDELAEMKET", "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": "MYHLIPFAAILGMTYALSLAIYRLFLSPLAKFPGPKLAAVTGWVETYYQLFYGEGGQFIFLYKEWHQKYGPIIRINPWEVHISDSCFFEILYSTNRPLKKLPHLAKVFDNELSGFSTVSPELHRIRRKAVSHLFSKGEVLKRGAQIQSAMDRLSERLKLDFLGHGNRVICMNDMWSVYTADLIAEYAFGRHYGFIDQPNFEADFTKALVHLLEPTHLAQQFPWLTDILKALPTSVLEFLHPHMAAFNKFKAANQVRIAKANFAKDLSKGGTMFSAIFNSDLPDEEKSIERAHQEALAFAAAGAETVAATLSVASFHLLHDPKIRRRLDEELATVVPDSRSSDASMPSLEILWQLPYLTGIINEALRLSYGSYARIPRTSDTPIQYDEWTIPPGVVFSMDIAPAHHDERIFPDSYSFKPERWLDNPQAFDGKPLTRYLFSFSRGTRSCLGMQLALAEMYIGIVSFFSRFDAHLFETDLTDITFVRDRFAPRPRIGSRGVRVNRLTTRKF", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties (PubMed:24845309). The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tailored throughout the backbone (PubMed:24845309). The highly reducing polyketide synthase Bref-PKS is proposed to synthesize the precisely reduced octaketide precursor, which could then be directly offloaded by the thiohydrolase enzyme Bref-TH followed by a cytochrome P450 monooxygenase-mediated formation of the cyclopentane ring and macrocyclization to afford 7-deoxy BFA. Alternatively, the first ring annulation can also occur on the ACP-tethered intermediate before the thiohydrolase release and lactonization (PubMed:24845309). The C7- hydroxylation by another cytochrome P450 monooxygenase is believed to be the final step in the process to obtain the final structure of BFA (PubMed:24845309). In addition to the HRPKS Bref-PKS and the thiohydrolase Bref-TH, the brefeldin A biosynthesis cluster contains 4 cytochrome p450 monooxygenases (called orf3 to orf6), as well a the probable cluster-specific transcription regulator orf8 (PubMed:24845309). SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MGAIHEETANRSPIPDGHQGAGDRAADHRHSARRAGRWPAPGGVCHFAGADQGGGVAGGQSRMGSSRGTAPRGLRASDGGTAGASSVHRQEVGSRRQEETGTQVMKTLVTAIQKGGQGKTFATCHLAFDFLERGLRVAVIDLDTQGNASFTLSAYQSGYLASQLFTGDTDDLRYWFGKREGESLALIAADANLANLDKMELSQAAAALRASVAALGEFFDVCLIDTAPSLGVAMTAAVLTADYMLSPIEMEAYSLQGMKKMVAVISNLRKQNPKLRFLGMVPNKVDARKPRHVNNLATLQQAYPQLILPFSIGARDSIAEALGEQMPVWKIKKTAARKATQEVRALADYVFTKMEIAQ", "text": "FUNCTION: This is one of the proteins encoded by the trfB operon; it is involved in plasmid maintenance and replication. SIMILARITY: Belongs to the ParA family."}
+{"protein": "MGRSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTVIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATAEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLYRSCVNETAIDSRGGQPLLKLLPDVYGWPVATQNWEQTYGTSWSAEKSIAQLNSNYGKKVLINFFVGTDDKNSMNHIIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMIAVAKLIRQEEGLPIDENQISVEMNKVMELEKEIANATTKSEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWSNFTNEIMSTVNINIPNEEDVVVYAPEYLIKLKPILTKYFPRDFQNLFSWRFIMDLVSSLSRTYKDSRNAFRKALYGTTSESATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKKAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWITGAAIVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGIGQAYRAYQNYVKKNGEEKLLPGIDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGSLQNSVEFSEAFQCPKNSYMNPEKKCRVW", "text": "FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:3162886). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (By similarity). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)) (By similarity). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase M13 family."}
+{"protein": "PEEICTLVIAESFPEDAGIFTCSARNDYGSVTSTAQLVVTSANTENCSYDSMGEPNSDHFQHFPPPPPILETGSYELASQKPSEIQQVNTPNLGFNMAALQMQFNSAERETNGVHPSHGVNGLINGKAYGNKSPPTPAALLSPTKEPPPLLAKPKLGFPKKASRTARIASDEEIQGTKDAVIQDLERKLRFKEDLLNNGQPRLTYEERMARRLLGADSANVFNIQEPEETAANQEYKVSSCEQRLISEIEYRLERSPVEESGDEVQEAEVPVENAAAPFFEMKLKHYKIFEGMPVTFTCRVAGSPKPKIYWFKDGKQISPKSDHYTIQRDVDGTCSLHTTASTLDDDGNYTIMAANTQGRVSCTGRLMVQAVNQRGRSPRSPPGHPHARRPRSRSRDSGDENEPIQERFFRPHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVVAAKEAHKAPVFIEKLQNTGVADGYPVRLECRVSGVPPPQIFWKKENESLTHSTDRVSMHQDNHGYICLLIQGATKEDAGWYTVSAKNEAGIVSCTARLDVY", "text": "FUNCTION: Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Plays a role in neurite outgrowth and in the establishment of polarity during neuronal morphogenesis. Participates in the acquisition of the reactive astrocyte morphology. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell junction, focal adhesion Cytoplasm, myofibril, sarcomere, Z line Cell projection, ruffle Cell projection, podosome Cell projection, lamellipodium Cell projection, axon Cell projection, growth cone Note=Localizes to stress fibers (PubMed:16868024, PubMed:11553711, PubMed:16125169, PubMed:22659164). Localizes to Z lines (PubMed:16868024, PubMed:11553711, PubMed:16125169). Preferentially expressed in the excitatory presynaptic terminals (PubMed:11438925). SIMILARITY: Belongs to the myotilin/palladin family."}
+{"protein": "MSRQDVQRLLEEYQLIGELLSSLQAQHATVAELLEELTTALDGVRLLKGEGGERLVHIGAGLFVKGVFEAKEVLAPLGAGYHAFLDLNNAERILQERIEEYSKLKTSLEENIEKLAERAAQIRQALERLGIR", "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 alpha family."}
+{"protein": "MKELDVVDGIQSAGGWIVRNQDLLLGYAVNLVAAVVILIIGSLIARGISTTLIRLLKARGLDVTVVHFLAAMVRYAILAFTIIAALGRLGVQTTSVIAVLGAAGLAVGLALQGSLSNFAAGVLLVLFRPFRAGEVVDLGGVTGTVREVQIFSTTLATADNKVIVVPNGKIIAGNIINFSREPKRRIDIIVGVAYDADIDVVKRVLGDVVAADTRILHDDGVTIRLNEMAASSLNFVVRVWGNNADYWAIYFDLMENFKRALDANNIGIPFPQMDVHLYQAVKARAE", "text": "FUNCTION: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscS (TC 1.A.23) family."}
+{"protein": "MATFKLVISNPKNGIARQVEISGEEAEKLIGKRIGEEISAKELGLNLTEIFGEEIPADTKLKITGGTDKDGFPMRPDVHGPRRVKILVSRGPGFRPKEKGERRKKTVRGNTISPEIVQINMKLVF", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family."}
+{"protein": "MAKSKNHTTHNQSRKWHRNGIKKPRSQRYESLKGVDPKFLRNMRFAKKHNKKGLKKMQANNAKAVSARAEAIKALVKPQAIKPKMPKGPKLKRLAFIAHPKLGKRIRSYMAKGQRLCQPKPKVQTKAGAKAPAKAQASAPAQAPKGAQAPKGAQAPVKAP", "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. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL29 family."}
+{"protein": "MRATWKGVISFGLVSIPVRLYSATQERDVAFHQVRRSDGSRIRYRRVAEADGDEVNYADIAKGYELPDGETVVLTDEDFANLPLSTSRAIDVLEFVPLEQVDPIYFAKSYYVEPDRTGAKPYVLLRDALAASGRVALVKIALRQREQLATLRVRGGVFVLETMVWPDEVRQPDFPFLEEDVAVRPQELSVAASLIHTLAADFDPTRYTDNYREALQAVIDAKVAGREVVASPGGPASEAVGDLMAALRASIAAARAGRPGEAAVAGGAAVAGGAAVADGDAGPAAAGVTDEGPDDKASDDKASDDKASDGRRGGRTSSVKGASSAPGTRSTARKTPSSTRSTAKTNAATKTPPAKTSAAKASAAKTSAAKATSSRTAPKTAPRTPTSKTPPTRRSA", "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": "MRKLTLTLSALALALSLNSVADAKVYMPEKVSDGVTVAQLAEQHAIHWISVEQIEESLKGQPMAVGFDIDDTVLFSSPGFYRGKLEYSPNDYSYLKNPEFWEKMNNEWDKFSMPKKSGMELVQMHLKRGDTVYFITGRSKTKTETVTKYVQEGLRIPADKMNPVIFAGDEEGQNNKVSWMRDHKLKIYYGDADADIAAARELNIRGIRVLRASNSSYQPLPKAGQFGEEVVINSEY", "text": "FUNCTION: Dephosphorylates several organic phosphate monoesters including 5'-AMP, 3'-AMP, pNPP, PDP, 5'-UMP, 3'-UMP, G2P, glucose 6-P and ribose 5-P. No activity toward organic phosphate diesters. 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. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the class B bacterial acid phosphatase family."}
+{"protein": "MSLFTPLSETNVRSHTNTSSVFCRRIKTLVAGLTALGLMLAAVSASAGFYVSGKQLREGNGNNFIMRGVNLPHAWFPDRTNQALADISATGANSVRVVLSNGRLWSRTPESQVASIISQAKARQLITVLEVHDTTGYGEQTAATLSEAVDYWIAIRNALIGQEDYVIINIGNEPFGNGQSASTWLNLHRDAINRLRNAGFTHTLMVDAANWGQDWENIMRNNASSLFNSDPRRNVIFSVHMYEVYPNDTAVNNYMSAFNSMNLPLVVGEFAANHFGSYVDAGSIMARAQQYGFGYLGWSWSGNSSNLSALDVVTNFNAGSLTTWGNLLINNTNGIRNTSRKATIFGGSGSSSSSAGSCGTAPNGYPYCCNASSATGNGWGWENNRSCVVATTSTSCNWYGTSYPICVNTSSGWGWENNRSCIAASTCAAQ", "text": "FUNCTION: Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan. It is able to hydrolyze mannosidic linkages that are flanked by mannose or glucose. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
+{"protein": "MLNGTTLEAAMLFHGISGGHIQGIMEEMERRSKTEARLAKGTQLNGRDAGMPPLSPEKPALCAGCGGKISDRYYLLAVDKQWHLRCLKCCECKLALESELTCFAKDGSIYCKEDYYRRFSVQRCARCHLGISASEMVMRARDSVYHLSCFTCSTCNKTLTTGDHFGMKDSLVYCRAHFETLLQGEYPPQLSYTELAAKSGGLALPYFNGTGTVQKGRPRKRKSPALGVDIVNYNSGCNENEADHLDRDQQPYPPSQKTKRMRTSFKHHQLRTMKSYFAINHNPDAKDLKQLAQKTGLTKRVLQVWFQNARAKFRRNLLRQENGGVDKADGTSLPAPPSADSGALTPPGTATTLTDLTNPTVTVVTTVTSNMDSHESGSPSQTTLTNLF", "text": "FUNCTION: Involved in gonadal development. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "QVRYRQCYFNPISCF", "text": "FUNCTION: Strongly inhibits juvenile hormone biosynthesis. May act as a neurotransmitter or neuromodulator (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the allatostatin family."}
+{"protein": "MKTVLPSVPETVRLSRRGFLVQAGTITCSVAFGSVPAAAGDTAESTPSIAAVSPNVWVRVHADGIVDIVCPAVELGQGAHTALPRFVAEELDADWDRVRVQQAGASDKVYGNPLAWGTQFTAASRTTVGYFDVLRVAGAQARFVLVQTAARRWSVPADQLETQKGVVLHRRSRRSATYGELVASVQVPESFPHFFARNEATQPADDYFGAAPPSVVAQAAGPASGAIALKHRSTYRLIGKDAPRKDIPPKVNGQACYGMDVQVPGMLYAMVETGPVAGMAPERVDDGAARQVPGIHHVLSLPHGVAVVGRDIFAVRAARARLLVNWKANPDKQSYDSGQVLDEFSDLCRNGIERNAVQAWKQGELSSIDAVFARPDVRIESFEMQSDLVYQAPMEPQSAVIQPHADGSAEAWVGTQWPTVEQGFAAGILGIAPDKLTMHLPLVGGGFGRRLEPGALVDAAHIVRAIGKTVKVIWSREDDLKRNPFRQALACRVEAAVLEKDQRILALRHTVAADSWLARLFPQYFNAYQQTDPGNWIGGMVAYDVPLQRIDALTPRRSVDVCYMRGIGVAQVKFAQESLVDQIARRLNADPVDFRLAHLNTSPRGAAVVRTVAEMSDWKRRSADAGGGMALGLAYTPYSNAHVALVSEVHFNRSENTLSVSRVWCAVDVGMVAQPDIVKAQMEGGIIQGLSVALMERVQVAKGVLQHSNFHDYPMLRMSQVPQIHVRLVETDQAMAGVAELGLLQIGPAINNAFARITGQHLRSLPMRPALAQMKRSGPTA", "text": "FUNCTION: Specific towards N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline."}
+{"protein": "MPDETNFTIEDIEPRPDALRGLDTQFLQDNTALVQAYRGLDWSDISSLTQMVDVIEQTVVKYGNPNDSIKLALETILWQILRKYPLLFGFWKRFATIEYQLFGLKKSIAVLATSVKWFPTSLELWCDYLNVLCVNNPNETDFIRNNFEIAKDLIGKQFLSHPFWDKFIEFEVGQKNWHNVQRIYEYIIEVPLHQYARFFTSYKKFLNEKNLKTTRNIDIVLRKTQTTVNEIWQFESKIKQPFFNLGQVLNDDLENWSRYLKFVTDPSKSLDKEFVMSVFDRCLIPCLYHENTWMMYIKWLTKKNISDEVVVDIYQKANTFLPLDFKTLRYDFLRFLKRKYRSNNTLFNNIFNETVSRYLKIWPNDILLMTEYLCMLKRHSFKNSLDQSPKEILEKQTSFTKILETSITNYINNQIDAKVHLQTLINDKNLSIVVVELIKTTWLVLKNNMQTRKYFNLYQKNILIKNSVPFWLTYYKFEKSNVNFTKLNKFIRELGVEIYLPTTVMNDILTDYKTFYLTHSNIVTYESSIIDSNTFDPILYPELKMSNPKYDPVLNTTANVDWHKKTEWKEAGHIGITTERPQISNSIIECNSGTLIQKPISLPNFRNLEKINQVKINDLYTEEFLKEGK", "text": "FUNCTION: Function prior to stable branch point recognition by the U1 snRNP particle to facilitate or stabilize the U1 snRNP/5'-splice site interaction. Has a direct role in the assembly or function of a catalytically active spliceosome. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PRP39 family."}
+{"protein": "MDDLLKVPEIVTNIASYLSTVDYLSFQQVNKRVYAIINGKNDSKYWSLKLTRMGLQQVHSNEEEEITLLDENDNQNSLRIFEIYKSFTAQNSKKIFVKFYRCYNSYARKLYNNNLANFFPTSYSNDPLKQTRILNFIKKYNFSNKNDIETFTRIETNFNILREIFINSVLKESELNYQSNNLAAVARFMKILLISNEESNAIEFFKSKADLPPSLTVLPSNDELFWAEQPREEDSGGSTVIFNSKNLDTFLNQLRDFLNEKIKLADILFKDEFPVILQFIESFIQDILLDILNNILLSYSEFLKENGKDSKANYECVPELYFTFIKKFDTELNDSVNAGANFRKVVRDLLNLYLEPFVVNYMNQTTRVFESLINSQLANYDTQVQDKQREQNAKIYNTLKDQTDASSASNNELPNDLSIITETSKTVPEADSKPSTIHQSVHSTDISNDKLDFLSSFTKIFKFSNNENQRLKQQLQLAYNLNLISNNLQNIKSLISLDLCYKILQETSEKTDQIYKFHTIESLLPLIKLRCQEIFKILITQLNKNHVKPAFEKAILLLQKYNPNEIEQIEIKFNSLSPANTQVEPLVQFTELINIGDIILQMISIFYKNELIPKKIIDKNKDFLNDVIQLKKNFETSIDDFVAEGLNIGINKLMDEISFVFKTLQLPDDYNPPPPSRNSPIRDIKPTKCAIRVVELLSNHCFLLTGATDKGTIDVYQQEIGERFFNEIVKHLKKCFISTEGAIWLICDLNYFYDFIANKLKQKNVVPYFVGLKSIGQLYIISGKDSKELGKLISDLGKFNGIFTQEEIYEFVQRRSDWVRVRKDVEKVMYGLGIRDCCIM", "text": "FUNCTION: Involved in recycling plasma membrane proteins internalized by endocytosis. Required for recycling of the v-SNARE SNC1. SUBCELLULAR LOCATION: Cytoplasm Bud neck Cell tip Note=In unpolarized G1 cells this protein is found in patches in the cytoplasm, while after bud emergence it is concentrated in nascent buds and at the mother-bud neck. Accumulates at the shmoo tips of cells treated with pheromone. Localization depends on an intact actin cytoskeleton and a functional secretory pathway."}
+{"protein": "MSQPIKFAYWVPNVSGGLVVSKIEQRTSWDIDYNRKLAQIAERSGFEYALSQIRFTAGYGADNQHESVTISHALLAATEKLKVIAAILPGPWSPALAAKQLATIDQFTGGRIAVNVVSGWFKGEFRAIGEPWLEHDERYRRSEEFIRALKGIWTQDNFSFHGDFYRFNDYTLKPKPLQRPHPEIFQGGSSRAARDMASRVSDWYFTNGNSVEGIKAQVDDIRAKAAANGHAVKIGVNAFVIARDTEEEARAVLAEIIAKADPEAVNGFGSEVKNAGAASPEGEGNWAKSTFEDLVQYNDGFKTNLIGTPRQIAERIVALKAIGVDLILSGFLHFQEEVEYFGRHVLPLVRELEQERRAAVAVA", "text": "FUNCTION: Involved in the dimethyl sulfide degradation pathway. Catalyzes the oxidation of dimethylsulfone (DMSO2) to yield methanesulfinate, which is oxidized spontaneously to methanesulfonate in the presence of dioxygen and FMNH(2). SIMILARITY: Belongs to the SsuD family."}
+{"protein": "MNEFFPLASAAGMTVGLAVCALIVGLALAMFFAVWESAKWRPVAWAGSALVTILRGLPEILVVLFIYFGSSQLLLTLSDGFTINLGFVQIPVQMDIENFDVSPFLCGVIALSLLYAAYASQTLRGALKAVPVGQWESGQALGLSKSAIFFRLVMPQMWRHALPGLGNQWLVLLKDTALVSLISVNDLMLQTKSIATRTQEPFTWYIVAAAIYLVITLLSQYILKRIDLRATRFERRPS", "text": "FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Probably responsible for the translocation of the substrate across the membrane. FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Probably responsible for the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily."}
+{"protein": "MGICKCKKRSEDFCFNHKKFICDSCVVADHSICYIKSYVSWLTDCEFEDSVCGVCKGKFDVDDNDDSVRLLCYHLYHPECIDVYVAALPQNSSVESYPCPKCPEPILPSNDKQSLLANSIRDRFSVSSWAGDYLKSFKKQNSNSNNNNNDNNNPKSNGITNGINGTHINNATSPEFYTNLDSIKSNGIHHHHHHSNNSNNNNIINPSLLEETPPLSHLNSNPYGLASRKHEHEDTVIQLNSGTNSNISNNIHGNNKIYDDDYDKYNKRPVNPISKIINNIKETKPKYLIMITVAIIVFLILISKMGSNSDSNDNIVGDNNNNNNNININNDNNGGNGAINEETLNDQKIPNNGQ", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ZFPL1 family."}
+{"protein": "MTAQTPIHVYSEIGKLKKVLLHRPGKEIENLMPDYLERLLFDDIPFLEDAQKEHDAFAQALRDEGIEVLYLETLAAESLVTPEIREAFIDEYLSEANIRGRATKKAIRELLMAIEDNQELIEKTMAGVQKSELPEIPASEKGLTDLVESNYPFAIDPMPNLYFTRDPFATIGTGVSLNHMFSETRNRETLYGKYIFTHHPIYGGGKVPMVYDRNETTRIEGGDELVLSKDVLAVGISQRTDAASIEKLLVNIFKQNLGFKKVLAFEFANNRKFMHLDTVFTMVDYDKFTIHPEIEGDLRVYSVTYDNEELHIVEEKGDLAELLAANLGVEKVDLIRCGGDNLVAAGREQWNDGSNTLTIAPGVVVVYNRNTITNAILESKGLKLIKIHGSELVRGRGGPRCMSMPFEREDI", "text": "FUNCTION: Antitumor protein. Has a powerful and dose-dependent inhibitory effect on antigen, superantigen, or mitogen-stimulated human peripheral blood mononuclear cell (PBMC) proliferation. It may inhibit cell proliferation by arresting cell cycle and inducing apoptosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the arginine deiminase family. SIMILARITY: Belongs to the arginine deiminase family."}
+{"protein": "MKKRGKGVGSMWYGIGNTGLPNPAAAFVEIHGDGSANVMFGAADIGQGSGTAMAQIAAEELGLDYEKIHVTWGDTMVTPDGGATSASRQTLITGNAVILACRQAKETLAKTAAEKLDCAPEELSFRDNTVFITADPERSMTYGELMAAMKAAGRMAVGAGSYNPNTTGLAPENMSGIPFEVYSYATTIAEVEVDTETGEVDVLKVVSAHDVGTPINRSMVEGQIEGGVTMGQGFVLMEEIEVNTKNGAIKNPSMSKYIIPSNRDVPEIHSILVESEGGPGPFGAKGVGEPALIPMIPAVVAAIEDALGTRFTHTPIMPKDIVAAVKAQEK", "text": "FUNCTION: Catalyzes the hydroxylation of nicotinate to 6- hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs. SIMILARITY: Belongs to the xanthine dehydrogenase family."}
+{"protein": "MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS", "text": "FUNCTION: Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. Converts oestradiol to oestrone. The physiological substrate is not known. Acts on oestradiol and 5-androstene-3-beta,17-beta-diol (in vitro). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MKLLVLLLCLGLTLVCVHAEEASSMERNFNVEKINGEWYTIMLATDKREKIEEHGSMRVFVEYIHVLENSLALKFHIIINEECSEIFLVADKTEKAGEYSVTYDGSNTFTILKTDYDNYIMIHLINKKDGETFQLMELYGREPDLSSDIKEKFAQLSEEHGIVRENIIDLTNANRCLEARE", "text": "FUNCTION: Male pheromone which stimulates female sexual attraction to male urinary scent and promotes a strong learned attraction to the airborne urinary odor of an individual male (PubMed:20525243, PubMed:31996852). Promotes spatial learning by rapidly conditioning preference for its remembered location among females and competitor males so that animals prefer to spend time in the site even when scent is absent (PubMed:23239735). In addition to promoting a rapid attraction response, also elicits ultrasonic vocalizations and urinary scent marking in females which do not occur immediately after exposure (PubMed:31996852). Stimulates hippocampal neurogenesis and cell proliferation in the subventricular zone in females (PubMed:25972792). Promotes male aggressive behavior (PubMed:18064011). Response to Mup20 is mediated by a neural circuit extending from the accessory olfactory bulb to a subset of nitric oxidase synthase-expressing neurons in the medial amygdala (PubMed:31996852). As well as acting as a pheromone itself, binds most of the male pheromone, 2-sec-butyl-4,5- dihydrothiazole, in urine and is responsible for its slow release from scent marks (PubMed:15934926, PubMed:25279835). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MEDNTPRQRDPISLTSVANGLENMGAELLESLEEGRAPGSDSSPAEVGGGWSKAGPEHLGRRSLQPALRVRRFCREHTQLFRWICTGLLCTAFAAFLLIACLLDFQRALALFVLFCVVLFFLAHSLLKRLLGPKLLRCVKPLRHPCLNLWFKRGLALAAFLGLVLWLVLDTAQRPEQLVSFGGICVFILLLFAGSKHHRAVSWRAVSWGLGLQFALGLFVIRTEPGFIAFQWLGDQIQIFLSYTEAGSSFVFGEALVKDVFAFQVLPIIVFFSCAMSVLYYVGLMQWVILKISWLMQATMGTTATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEIHVVMTGGYATIAGSLLGAYISFGIDAASLIAASVMAAPCALALSKLVYPEVEESKFKREEGVKLTYGDAQNLLEAASSGAAMSVRVVTNIAANLIAFLAVLAFINAALSWLGDMVDVQGLSFQLICSYVLRPVAFLMGVAWEDCPVVAELLGMKLFLNEFVAYQELSGYKQRRLAGAEEWVGSRKQWISVRAEILTTYALCGFANFSSIGIMLGGLTSMVPQRKGDFSQIVLRALCTGACVSLVNACVAGILYVPRGAEVDCVSFLNTTLSSSSFEVYQCCRQFFQSTSLEFSPEALDNCCRFYNHTICV", "text": "FUNCTION: Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum velocity. Therefore, exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit). Involved in renal nucleoside (re)absorption. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT) (TC 2.A.41) family."}
+{"protein": "MKFGKRHYRPQVDQMDCGVASLAMVFGYYGSYYFLAHLRELAKTTMDGTTALGLVKVAEEIGFETRAIKADMTLFDLPDLTFPFVAHVLKEGKLLHYYVVTGQDKDSIHIADPDPGVKLTKLPRERFEEEWTGVTLFMAPSPDYKPHKEQKNGLLSFIPILVKQRGLIANIVLATLLVTVINIVGSYYLQSIIDTYVPDQMRSTLGIISIGLVIVYILQQILSYAQEYLLLVLGQRLSIDVILSYIKHVFHLPMSFFATRRTGEIVSRFTDANSIIDALASTILSIFLDVSTVVIISLVLFSQNTNLFFMTLLALPIYTVIIFAFMKPFEKMNRDTMEANAVLSSSIIEDINGIETIKSLTSESQRYQKIDKEFVDYLKKSFTYSRAESQQKALKKVAHLLLNVGILWMGAVLVMDGKMSLGQLITYNTLLVYFTNPLENIINLQTKLQTAQVANNRLNEVYLVASEFEEKKTVEDLSLMKGDMTFKQVHYKYGYGRDVLSDINLTVPQGSKVAFVGISGSGKTTLAKMMVNFYDPSQGEISLGGVNLNQIDKKALRQYINYLPQQPYVFNGTILENLLLGAKEGTTQEDILRAVELAEIREDIERMPLNYQTELTSDGAGISGGQRQRIALARALLTDAPVLILDEATSSLDILTEKRIVDNLIALDKTLIFIAHRLTIAERTEKVVVLDQGKIVEEGKHADLLAQGGFYAHLVNS", "text": "FUNCTION: Required for induction of competence. Seems to transport the competence-stimulating peptide (CSP) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. HlyB family."}
+{"protein": "MAPPPVNSGDAAAAATGEKSKLSPSGLPIREIPGGYGVPFFSPLRDRLDYFYFQGAEEYFRSRVARHGGATVLRVNMPPGPFISGNPRVVALLDARSFRVLLDDSMVDKADTLDGTYMPSRALFGGHRPLAFLDAADPRHAKIKRVVMSLAAARMHHVAPAFRAAFAAMFDAVEAGLGAAVEFNKLNMRYMLDFTCAALFGGEPPSKVVGDGAVTKAMAWLAFQLHPIASKVVKPWPLEELLLHTFSLPPFLVRRGYADLKAYFADAAAAVLDDAEKSHTGIPRDELLDNLVFVAIFNAFGGFKIFLPHIVKWLARAGPELHAKLATEVRATVPTGEDDGITLAAVERMPLVKSVVWEALRMNPPVEFQYGHARRDMVVESHDAAYEVRKGEMLFGYQPLATRDEKVFDRAGEFVADRFVAGGAAGDRPLLEHVVWSNGPETRAPSEGNKQCPGKDMVVAVGRLMVAELFRRYDTFAADVVEAPVEPVVTFTSLTRASSG", "text": "FUNCTION: Involved in the biosynthesis of jasmonic acid, a growth regulator that is implicated also as a signaling molecule in plant defense. Converts 13-hydroperoxylinolenic acid to 12,13-epoxylinolenic acid (By similarity). SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MENEDGYMTLSFKNRCKSKQKSKDFSLYPQYYCLLLIFGCIVILIFIMTGIDLKFWHKKMDFSQNVNVSSLSGHNYLCPNDWLLNEGKCYWFSTSFKTWKESQRDCTQLQAHLLVIQNLDELEFIQNSLKPGHFGWIGLYVTFQGNLWMWIDEHFLVPELFSVIGPTDDRSCAVITGNWVYSEDCSSTFKGICQRDAILTHNGTSGV", "text": "FUNCTION: C-type lectin-like receptor involved in natural killer cell mediated cytotoxicity and cytokine secretion in keratinocytes via its interaction with CLEC2A. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
+{"protein": "MALLLPEFDPADVRAGRDLIHRLTADAAGIQRGVLREILSRNSGTEYLRRFLGGAAGDDDDVRDAFKRRVPVSGYEDVKPYVDRVASGGEPSSALLCSDPITCLSRSSGTSGGQQKLLPSTAEELDRKVFFYAVQALVRNMSLHTDHGEDDDGGGGEGMYLMFAFHGDRTLSGLPIQSALTTYYHSRQFQECDIGGFDKCTSPLEAILCPYGEQSMYCQLLCGLLHRCRVDRVGASFAAGLVRGIKFLENHWEEMCFNIRSGQLSDWITHTPLRDAVTGQYLQGSNPALADEIASECARKPWDGIVRRLWPRARYIRTIVTGSMSQYIPILEVYGGGLPLVSPIYASTECAAGINLRPLDPPSHVSYALLPNIAYFEFLEVMDENGEKVQGTTRLDDNLGEVKVVDLVDVKVGRCYELIVTTFAGLYRYRVGDLFTVSGFYNATPLFHFSGRHDVILSIDYEKISEEDLLNAIAETDKFHLRPLGYMLVGSTAYADISTLPGHYILFWELTNTCDSNVAIDIDQTAMEKCCLAVEDHFDEMYRKIRHRGSISALEIRILSHGAFDALMDFFVSRGTSASQYKTPTAIRSKEAMMVLEERVVGRFFSQATPSCRSAEFERR", "text": "FUNCTION: May catalyze the synthesis of indole-3-acetic acid (IAA)- amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin. SIMILARITY: Belongs to the IAA-amido conjugating enzyme family."}
+{"protein": "MVLDPEEKIPDDGASGDHGDSASLGAINPAYSNSSLPHSTGDSEEPFTTYFDEKIPIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWVLLLATIVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRIILWLMVELAIIGSDMQEVIGSAIAINLLSAGRVPLYGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLRGMFVPSCSGCHTPQVEQAVGIVGAVIMPHNMYLHSALVKSRQVNRANKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFEKTNEQVVEVCRNSSSPHADLFPNDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVILTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSEFSNGIGWRIAGGILVLLVCSINMYFVVVYVQELGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGLSFLDCGRSYHLGLTARPEIYLLNTVDAVSLVSR", "text": "FUNCTION: Proton-coupled metal ion symporter operating with a proton to metal ion stoichiometry of 1:1 (PubMed:9242408, PubMed:16091957). Selectively transports various divalent metal cations, in decreasing affinity: Cd(2+) > Fe(2+) > Co(2+), Mn(2+) >> Zn(2+), Ni(2+), VO(2+) (PubMed:9242408, PubMed:16091957, PubMed:29317744) (By similarity). Essential for maintenance of iron homeostasis by modulating intestinal absorption of dietary Fe(2+) and TF-associated endosomal Fe(2+) transport in erythroid precursors and other cells (PubMed:9242408) (By similarity). Enables Fe(2+) and Mn(2+) ion entry into mitochondria, and is thus expected to promote mitochondrial heme synthesis, iron-sulfur cluster biogenesis and antioxidant defense (PubMed:29317744). Can mediate uncoupled fluxes of either protons or metal ions. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Mitochondrion outer membrane; Multi-pass membrane protein Extracellular vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP family."}
+{"protein": "MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDKVGSTPNGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRAVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGITFPPAGSQTVSAAAKNGTSSNKNKEDEDIAKAIELSLQEQKQQHTETKSLYPSSEIQLNNKVARKVRALYDFEAVEDNELTFKHGEIIIVLDDSDANWWKGENHRGIGLFPSNFVTTNLNIETEAAAVDKLNVIDDDVEEIKKSEPEPVYIDEDKMDRALQVLQSIDPTDSKPDSQDLLDLEDICQQMGPMIDEKLEEIDRKHSELSELNVKVLEALELYNKLVNEAPVYSVYSKLHPPAHYPPASSGVPMQTYPVQSHGGNYMGQSIHQVTVAQSYSLGPDQIGPLRSLPPNVNSSVTAQPAQTSYLSTGQDTVSNPTYMNQNSNLQSATGTTAYTQQMGMSVDMSSYQNTTSNLPQLAGFPVTVPAHPVAQQHTNYHQQPLL", "text": "FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the STAM family."}
+{"protein": "MKIFVKTLKGTHFEIEVKPEDSVVDVKKNIESVQGADVYPAAKQMLIHQGKVLKDETTIEENKVAENSFIVIMMNKSKPASAAASSASAGTSQAKSIPPSTSQPSISPQTPASVSAPVAPAPTRPPPPAPTPTPAPVAATETVTTPIPEPVPATISSSTPAPDSAPVGSQGDVYGQAASNLAAGSNLESTIQQILDMGGGTWDRETVVLALRAAFNNPERAVEYLYTGIPEQAEVPPVARPPASAGQPANPPAQTQQPAAAPASGPNANPLDLFPQGLPNVGGNPGAGTLDFLRNSQQFQALRAMVQANPQVLQPMLQELGKQNPNLMRLIQDHQADFLRLINEPVEGGGESGNLLGQMAAGMPQPQAIQVTHEEREAIERLEAMGFERALVLEVFFACNKNEELAANYLLDHMHEFEE", "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). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RAD23 family."}
+{"protein": "MTKQSADSNAKSGVTAEICHWASNLATDDIPSDVLERAKYLILDGIACAWVGARVPWSEKYVQATMSFEPPGACRVIGYGQKLGPVAAAMTNSAFIQATELDDYHSEAPLHSASIVLPAVFAASEVLAEQGKTISGIDVILAAIVGFESGPRIGKAIYGSDLLNNGWHCGAVYGAPAGALATGKLLGLTPDSMEDALGIACTQACGLMSAQYGGMVKRVQHGFAARNGLLGGLLAYGGYEAMKGVLERSYGGFLKMFTKGNGREPPYKEEEVVAGLGSFWHTFTIRIKLYACCGLVHGPVEAIEKLQRRYPELLNRANLSNIRHVYVQLSTASNSHCGWIPEERPISSIAGQMSVAYILAVQLVDQQCLLAQFSEFDDNLERPEVWDLARKVTPSHSEEFDQDGNCLSAGRVRIEFNDGSSVTETVEKPLGVKEPMPNERILHKYRTLAGSVTDESRVKEIEDLVLSLDRLTDITPLLELLNCPVKSPLV", "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": "MGFLTLFHMAFLAVSLFVSGALAAFGYTTSGNNFVIDAGSANPLIFSVSKSSCDINSIRYRGTELQYSKQGSHIGSGLGKATVSVSQINGSKSKFIKVTCVTSTLTQYMIVKEADSTIYMATYITAEPAIGELRFIARLLSDKLPYEYPYGEVSTTKGSSSTVEGSDVFVVNGQTRSKFYSSTRFIDEDSHCVYGGSDLTHVCIITPQQESSSGGPFFRDIDSNNAGESTNLYNYMNSGHVQTEDRRMGLHGPYLMTFSRSGIPKLKTVDISWFGELGVTGYVPDSQRGTVIGRATGIPSGFEGVVHWYNAAAQYWVRTAPNGDFTSPKMKPGTYTMVLYQTEFKVATSTVTVSAGKTTTASIASTFNTSHTTLFKIGEYDGQPTGFRNADKFLRMHPSDSRMSSWGPLTYTVGSSSLNDFPMAVFKSVNNPVTIKFNLGSAPSQATTLRIATTLSFAGARPQVVVNGWSAPAPAAPAKIDSRGVTRGAYRGYGEVYDVAVPAGKLISGTNTITISALSGSSGATFLSPNFIFDAVELFY", "text": "FUNCTION: Could be a pectinolytic enzyme that hydrolyzes the alpha-L- rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage by beta-elimination, thereby generating oligosaccharides terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 4 family."}
+{"protein": "MHDFLSIHPEVAAALKAGRPVVALESTLISHGLPAPANLETAQAIEAAVRANGAVPATIAVLDGRIRVGLDAEDMQRLAAPGTAKVSRRDLPLVLAKGADGATTVAATMIAADLAGIAVFATGGIGGVHRGVETTGDISADLEELATTSVAVVCAGAKAILDLPRTLEYLETRGVPVVGFGTDAFPAFYHRDSGLPVDGRCDTPEDAARVLNAKWRLGLAGGIVVAVPIPDEAALDAAQAEAAVQQAVAEAATGGVRGKALTPFLLHRLETLTGGASLTANRALLLNNAAVGARIAVAYARLKQETTLPKKPPPSKRPTY", "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": "MMNHKELVLFAVVCLSLYQAVEPSQDVVKDMSLNFRKGLDACKKELNLPDTINSDFNRFWNDDHVVTNRDTGCAIMCLSSKLELVSDTGLHHGNTLEYAKQHGADDTVAQQIVDLLHSCAQAVPDLEDPCLKVLEWAKCFKAEIHKLNWAPSAEVMAAEMLAEV", "text": "FUNCTION: This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia. SIMILARITY: Belongs to the PBP/GOBP family."}
+{"protein": "MQGNKSTIREYKIVVVGGGGVGKSALTIQFIQSYFVDEYDPTIEDSYRKQVVIDDKVSILDILDTAGQEEYSAMREQYMRTGEGFLLVYSVTSRNSFDELLSYYQQIQRVKDSDYIPVVVVGNKLDLENERQVSYEDGLRLAKQLNAPFLETSAKQAINVDEAFYSLIRLVRDDGGKYNSMNRQLDNTNEIRDSELTSSATADREKKNNGSYVLDNSLTNAGTGSSSKSAVNHNGETTKRTDEKNYVNQNNNNEGNTKYSSNGNGNRSDISRGNQNNALNSRSKQSAEPQKNSSANARKESSGGCCIIC", "text": "FUNCTION: The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MCEEEEVYCPELQDTTQGKSLGKTCMKCKESSAVLLIRAGDAFCKSCFKEYFVHKFRATLGKNRVIYPGEKVLLAFSGGPSSSAMVQQVQEGMSRDAPKKLRFVPGILFIDEGTTCGMSHEERQQNMSEVQNVLQQTGFPFYIVSLEQVFSLPGSILQRGVPEQRANYKQEVDRFMVQQQAQGETGCSDILENLAKLGVNVSESSRESDKMFQSTCRHPPDTHTQKLIQLFASAKTLTAKHQLLHTLRSHLILHIARTCGYSKVMSGESCTRLSVSLLSNISLGRGAFLPLDTGFCDSRYGDVDIIRPMREYSLKEIAFYNRLFHVSSVFIPALNTKVLENSSIQQLSEVFINRLQADFPSTVSTVYRTSEKLNVSKIDANQGTCAKERCLLCLSPLDTQVGEASAFHATQISHYISQKILMKFNDPANSSGKSCCQEGKCCKGPGYGDFCQPRALQAPSFVDMLCYGCRLTVKDLQSLDALPQYVLHEAEHRSRRIEMRKEIEEFLLDKDEENLH", "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": "MVESSDENDQASSFASTEDLKELRFVFWFSVLIPIFFIALIIIKRYHSCTYQKNRLLRSIFCCMSIDDEEELETDMYDLPIVEPSITLPKYSASLQENERLVGIEGEREGIDVVLNFSKAGEGGVNPYPSFDTPNARILQLRQLAKLKKHGPRISYHGIGIGRCNGNRVLPPYPEPALLPEAPNTREASNNTYLYGFSNNFINISRTLNLRYPSASASISDSLPPPYQVLSVPSVTSTHAFSNNANQT", "text": "FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Membrane; Single- pass membrane protein Note=Localizes to the barrier septum and cell tip."}
+{"protein": "MSSSSAHQKASPPIEEEATEHGPFPIEQLQASGIAALDVKKLKDAGLCTVESVAYSPRKDLLQIKGISEAKVDKIIEAASKLVPLGFTSASQLHAQRLEIIQLTTGSRELDQILDGGIETGSITEMYGEFRSGKTQLCHTLCVTCQLPLDQGGGEGKALYIDAEGTFRPQRILQIADRFGLNGADVLENVAYARAYNTDHQSRLLLEAASMMVETRFALMVVDSATALYRTDFSGRGELSARQMHLAKFLRSLQKLADEFGVAVVITNQVVAQVDGAAMFAGPQIKPIGGNIMAHASTTRLFLRKGRGEERICKVISSPCLAEAEARFQISSEGVTDVKD", "text": "FUNCTION: Binds to single and double-stranded DNA and exhibits DNA- dependent ATPase activity. Unwinds duplex DNA (By similarity). Component of the meiotic recombination pathway. Seems to play a role in mediating chromosome homology search, chromosome pairing and synapsis at early stages and probably chromosome crossing-over at later stages in meiosis. Probably is involved in the repair of meiotic double strand breaks (DBSs) and in homologous recombination. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RecA family. RAD51 subfamily."}
+{"protein": "MAGLKSFLASSWLLPVACGASQSIVPSTSATAAYSQFTIPASADVGANLVANIDDPQAVNAQSVCPGYKASDVKHSSQGFTASLELAGDPCNVYGTDVDSLTLTVEYQAKDRLNIQIVPTYFDASNASWYILSEELVPRPKASQNASVPQSDFVVSWSNEPSFNFKVIRKATGDVLFNTKGSTLVYENQFIEFVTLLPEEYNLYGLGERMNQLRLLENANLTLYAADIADPIDDNIYGHHAFYLDTRYYKVGGQNKSHTIVKSSEAEPSQEYVSYSHGVFLRNAHGQEILLRDQKLIWRTLGGSVDLTFYSGPTQAEVTKQYQLSTVGLPAMQQYNTLGFHQCRWGYNNWSEFEDVLANFERFEIPLEYLWADIDYMHGYRNFDNDQHRFSYEEGEKFLNKLHAGGRRWVPIVDGALYIPNPENASDAYETYDRGAKDDVFIKNPDGSLYIGAVWPGYTVYPDWHHPKASDFWANELVTWWNKLHYDGVWYDMAEVSSFCVGSCGTGNLSMNPAHPPFALPGEPGNVVYDYPEGFNITNATEAASASAGAASQSAAASSTTTSAPYLRTTPTPGVRNVDHPPYVINHVQPGHDLSVHAISPNSTHSDGVQEYDVHSLYGHQGINATYHGLLKVWENKRPFIIARSTFSGSGKWAGHWGGDNFSKWGSMFFSISQALQFSLFGIPMFGVDTCGFNGNTDEELCNRWMQLSAFFPFYRNHNVLSAIPQEPYRWASVIDATKAAMNIRYAILPYFYTLFHLAHTTGSTVMRALAWEFPNDPSLAAVGTQFLVGPSVMVIPVLEPQVDTVQGVFPGVGHGEVWYDWYSQTAVDAKPGVNTTISAPLGHIPVFVRGGSILPMQEVALTTRDARKTPWSLLASLSSNGTASGQLYLDDGESVYPEDTLSVDFLASRSTLRASARGTWKEANPLANVTVLGVTEKPSSVTLNGETLSSDSVKYNATSHVLHVGGLQKHTADGAWAKDWVLKW", "text": "FUNCTION: Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch. SIMILARITY: Belongs to the glycosyl hydrolase 31 family."}
+{"protein": "QKPGEAVILEQSIDNDGLGQYTFGFKTSDGLIRQEQGVVKNQGTENEALEVRGTITWLGADGKDYSINFVADENGFQPQYTQ", "text": "FUNCTION: Component of the abdominal endocuticle."}
+{"protein": "MFRSGFIHNTRFNFSKVTTKRLFSSSARPIHSLRIKSLTLGVCGFSAITGLALYNHRLIELDNKKQDISPNISIAVDSSISPFPTALISANQTNLNTDFQLLGYGVRSVTFVNFKVYGIGLYIANDDVNKTKKILSPNYLSTFGTENHSLRELLSDPEFSAQLISKLLEENVRFAVRISPVRNTDFNHLKDGLIKSILAHPESKENKEIVSNGLEELRNVFSGYRGSVPKNHVLWLEILKQGSLSISYENPVKNELTSMGQVKEPIISKLLFLQYLSGKKPLSEPLRKSCNDGFIGL", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM18/AIM46 family."}
+{"protein": "MEKFKAAMLLGSVGDALGYRNVCKENSTVGMKIQEELQRSGGLDHLVLSPGEWPVSDNTIMHIATAEALTTDYWCLDDLYREMVRCYVEIVEKLPERRPDPATIEGCAQLKPNNYLLAWHTPFNEKGSGFGAATKAMCIGLRYWKPERLETLIEVSVECGRMTHNHPTGFLGSLCTALFVSFAAQGKPLVQWGRDMLRAVPLAEEYCKKTIRHTAEYQEHWFYFEAKWQFYLEERKISKDSENKAIFPDNYDAEEREKTYRKWSSEGRGGRRGHDAPMIAYDALLAAGNSWTELCHRAMFHGGESAATGTIAGCLFGLLYGLDLVPKGLHQDLEDKEKLEDLGAALYCLSTEEK", "text": "FUNCTION: Required for myofibril assembly and outgrowth of the cardiac chambers in the developing heart (By similarity). Appears to be catalytically inactive, showing no activity against O-acetyl-ADP-ribose (By similarity). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere. SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family."}
+{"protein": "MEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKLGKERLEAASQQKQQLTAQLSLMALPGEGDGGGHLDSEGEEAPRPIPSIPQDLESREAMSGFMDHLEEKADLSELVEKEELGFFQYYRERCHQKVYHPITKPGGSAKDAAPGGGHHQAGPGQGGDEGEAAGAAGDGVAAGGDYKGHSKFLVTAQNPAHEPSPGAPAPQELGAAHKHGDLCEVSLTDSVEPVQGEAREGSPHDNPTAQPIVQDHQEHPGLGSNCCVPFFCWAWLPRRRR", "text": "SIMILARITY: Belongs to the GOLGA8 family."}
+{"protein": "MASEIHMTGPMCLIESTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTESLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSGLLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS", "text": "FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens. Hydrolyzes GTP to GMP in two consecutive cleavage reactions: GTP is first hydrolyzed to GDP and then to GMP in a processive manner. Following infection, recruited to the pathogen- containing vacuoles or vacuole-escaped bacteria and promotes both autophagy and inflammasome assembly (By similarity). Promotes host defense against bacterial infections by regulating bacteriolytic peptide generation via its interaction with ubiquitin-binding protein SQSTM1, which delivers monoubiquitinated proteins to autolysosomes for the generation of bacteriolytic peptides (By similarity). Also acts as a positive regulator of inflammasome assembly by promoting the release of inflammasome ligands from bacteria. Acts by promoting lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol. Following pathogen release in the cytosol, promotes recruitment of proteins that mediate bacterial cytolysis: 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 (By similarity). Confers protection to several pathogens, including the bacterial pathogens L.monocytogenes and M.bovis BCG as well as the protozoan pathogen T.gondii (By similarity). Exhibits antiviral activity against influenza virus (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm Secreted Note=Localizes to pathogen-containing vacuoles or to the cell surface of bacteria that escaped vacuoles. Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of IFNG induction. Golgi membrane localization requires isoprenylation and the presence of another IFNG- induced factor. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. GB1 subfamily."}
+{"protein": "MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTCPKAAGEMLEADGSERFLCESVFSYQVASTLKQVKHDQQVSRMEKLAGLVEELEADEWRYTPIEQLLGFTPSSGGK", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the APC16 family."}
+{"protein": "MVQLRPRASRAPASAEAMVDEGQLASEEEEAEHGLLLGQPSSGAAAEPLEEDEEGDDEFDDEAPEELTFASAQAEAREEERRVRETVRRDKTLLKEKRKRREELFIEQKKRKLLPDTILEKLTTASQTNIKKSPGKVKEVNLQKKNEDCEKGNDSKKVKVQKVQSVSQNKSYLAVRLKDQDLRDSRQQAAQAFIHNSLYGPGTNRTTVNKFLSLANKRLPVKRAAVQFLNNAWGIQKKQNAKRFKRRWMVRKMKTKK", "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. SUBCELLULAR LOCATION: Nucleus, nucleolus."}
+{"protein": "MSLDAVGSLETKGFPGVLAAADAMVKTGRVTLVGYIRAGSARFTIIIRGDVSEVKTAMDAGIHAVDKAYGAALETWVIIPRPHENVECVLPIAYNENVERFRESTERPLIGSSQNRS", "text": "FUNCTION: A probably essential, minor shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Hexamers form sheets that form the facets of the polyhedral carboxysome. In PCC 7418 there are several CcmK paralogs with presumably functional differences. This subunit can probably make both homohexamers and heterohexamers with CcmK3. Both hexamers can also make dodecamers, formation depends on buffer conditions. SUBCELLULAR LOCATION: Carboxysome Note=This cyanobacterium makes beta-type carboxysomes. SIMILARITY: Belongs to the bacterial microcompartments protein family. CcmK subfamily."}
+{"protein": "MAILKWKRSRWYSSDEISFAGIVTKLPTANNTTTSNSKTCALGTSEGVRRATTSTKRPRTEPEHRNTHHPNKLLRGDSVDSVNCGVISAAACTNQTRAVSCPATTPIIHLKGDANILKCLRYRLSKYKQLYEQVSSTWHWTCTDGKHKNAIVTLTYISTSQRDDFLNTVKIPNTVSVSTGYMTI", "text": "FUNCTION: Plays a role in limiting the replication of viral DNA in keratinocytes. Recruits the host NCoR/SMRT complex to viral replication foci to mediate repression of both viral replication and transcription. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the papillomaviridae E8^E2C protein family."}
+{"protein": "MKKRTFALALSMIIASGVILGACGSSSDDKKSSDDKSSKDFTVAMVTDTGGVDDRSFNQSAWEGLQKFGKANDMEKGTDGYNYLQSASEADYKTNLNTAVRSDYDLIYGIGYKLKDAIEEVSKQKPKNQFAIVDDTIDDRDNVVSIGFKDNDGSYLVGVVAGLTTKTNKVGFVGGVKGTVIDRFEAGFTAGVKAVNPNAQIDVQYANDFAKADKGQQIASSMYSSGVDVIFHAAGGTGNGVFAEAKNLKKKDPSRAVWVIGVDRDQWDEGKVTANDGKDYNVTLTSEIKRVDIAVEDLATRAKAGDFPGGTKIEYGLDKDAVGLSEHQDNISKDVLAKVEEYKQKIVDGDIKVPEKP", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the BMP lipoprotein family."}
+{"protein": "MSHGHSHGGGGCRCAAEREEPPEQRGLAYGLYLRIDLERLQCLNESREGSGRGVFKPWEERTDRSKFVESDADEELLFNIPFTGNVKLKGIIIMGEDDDSHPSEMRLYKNIPQMSFDDTEREPDQTFSLNRDLTGELEYATKISRFSNVYHLSIHISKNFGADTTKVFYIGLRGEWTELRRHEVTICNYEASANPADHRVHQVTPQTHFIS", "text": "FUNCTION: Promotes megakaryocyte differentiation by up-regulating RUNX1 expression (PubMed:25134913). Regulates RUNX1 expression by activating the proximal promoter of the RUNX1 gene and by enhancing the translation activity of an internal ribosome entry site (IRES) element in the RUNX1 gene (PubMed:25134913). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PITHD1 family."}
+{"protein": "LECHNQQSSQTPTTTDCSGGETNCYKKWWSDHRGTIIERGCGCPTVKKGIELNCCTTDRCNN", "text": "FUNCTION: Nicotinic acetylcholine receptor antagonist (PubMed:35418867). Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission (PubMed:35418867). Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site (PubMed:35418867). Induces concentration- dependent inhibition of indirect twitches and abolishes contractile responses of tissues to exogenous acetylcholine and carbachol, in the chick biventer cervicis nerve-muscle preparation at 100-300 nM (in vitro) (PubMed:35418867). Prior incubation of tissues with Indian polyvalent antivenom (1 ml/0.6 mg) prevents the neurotoxic effects at 100 nM (in vitro) (PubMed:35418867). Addition of Indian polyvalent antivenom (1 ml/0.6 mg) at the t90 time point does not reverse the neurotoxic effects (in vitro) (PubMed:35418867). Displays non- competitive antagonism of concentration-response curves to carbachol, with a pA2 of 8.01 (in vitro) (PubMed:35418867). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type I alpha-neurotoxin sub-subfamily."}
+{"protein": "MNNATFNYTNVNPISHIRGSVIITICVSFTVILTVFGYIAKIFTNKKNCTNNVIGLRERIKCSGCEPFCNKRDDISSPRTGVDIPSFILPGLNLSESTPN", "text": "FUNCTION: Putative viral proton channel. May play a role in virus entry (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the influenza viruses type B glycoprotein NB family."}
+{"protein": "MPPAIGGPVGYTPPDGGWGWAVVVGAFISIGFSYAFPKSITVFFKEIEIIFSATTSEVSWISSIMLAVMYAGGPISSILVNKYGSRPVMIAGGCLSGCGLIAASFCNTVQELYFCIGVIGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFLSTLAPLNQAFFGIFGWRGSFLILGGLLLNCCVAGSLMRPIGPQQGKVEKLKSKESLQEAGKSDANTDLIGGSPKGEKLSVFQTVNKFLDLSLFTHRGFLLYLSGNVVMFFGLFTPLVFLSNYGKSKHFSSEKSAFLLSILAFVDMVARPSMGLAANTRWIRPRVQYFFAASVVANGVCHLLAPLSTTYVGFCIYAGVFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVILIIAGLYLFIGMGINYRLVAKEQKAEEKKRDGKEDETSTDVDEKPKKTMKETQSPAPLQNSSGDPAEEESPV", "text": "FUNCTION: Bidirectional proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH. The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (PubMed:9374487, PubMed:9639576, PubMed:10417314, PubMed:19473976, PubMed:8526936, PubMed:10564700, PubMed:11719518, PubMed:17127621). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart. Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 302-Asp is essential for the conformational transition (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Note=Expression at the cell surface requires the ancillary proteins BSG and EMB. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
+{"protein": "DPKDRKKIQFSXPAPPSQLDPRQLEMIRRRRPTPAMLFRLXEHSSPEEEASPHQRAAGEGHHLKSKRPNPCAYTPPSLKAVQRIAESHLQSISNLGENQASEEEDELGELRELGYPREEEEEEEEDDEEEEEEEDSQ", "text": "FUNCTION: Inhibitor of protein-phosphatase 1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family."}
+{"protein": "MGKGTVVGTAVVVCAAAAAAVGVAVVVSRRRRSKREAEEERRRRAAAVIEEVEQRFSTPTALLRGIADAMVEEMERGLRADPHAPLKMLISYVDNLPTGDEHGLFYALDLGGTNFRVIRVQLGGREKRVVSQQYEEVAIPPHLMVGTSMELFDFIAAELESFVKTEGEDFHLPEGRQRELGFTFSFPVHQTSISSGTLIKWTKGFSINGTVGEDVVAELSRAMERQGLDMKVTALVNDTVGTLAGGRYVDNDVAAAVILGTGTNAAYVEHANAIPKWTGLLPRSGNMVINMEWGNFKSERLPRSDYDNALDFESLNPGEQIYEKMISGMYLGEIVRRILLKLAHDASLFGDVVPTKLEQRFILRTPDMSAMHHDTSHDLKHLGAKLKDILGVADTSLEARYITLHVCDLVAERGARLAAAGIYGILKKLGRDRVPSDGSQKQRTVIALDGGLYEHYKKFRTCLEATLADLLGEEAASSVVVKLANDGSGIGAALLAASHSQYASVE", "text": "FUNCTION: Fructose and glucose phosphorylating enzyme (PubMed:16552590). Functions as glucose sensor for plant growth and photosynthesis (PubMed:19010999). SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the hexokinase family."}
+{"protein": "MAVPNELKYSKEHEWVKVEGNVATIGITEYAQSELGDIVFVELPETDDEINEGDTFGSVESVKTVSELYAPISGKVVEVNEELEDSPEFVNESPYEKAWMVKVEISDESQIEALLTAEKYSEMIGE", "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": "MAGSVLENIQSVLQKTWVREFLAEFLSTYVLMVFGLGSVAHMVLGERLGSYLGVNLGFGFGVTMGIHVAGGISGAHMNAAVTFTNCALGRMAWKKFPIYVLGQFLGSFLAAATTYLIFYGAINHYAGGELLVTGPKSTANIFATYLPEHMTLWRGFVDEVFVTGMLQLCIFAITDKLNSPALQGTEPLMIGILVCVLGVSLGMNTGYAINPSRDLPPRFFTFIAGWGKKVFSAGNNWWWVPVVAPLLGAYLGGIVYLGLIHAGIPPQGS", "text": "FUNCTION: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH (PubMed:9252401). The channel is also permeable to urea (PubMed:9252401). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasm, cell cortex Cytoplasmic vesicle membrane; Multi-pass membrane protein Lipid droplet Note=Internalized from the cell membrane in response to catecholamine-induced activation of PKA; detected on intracellular membranes and colocalizes with lipid droplets (By similarity). Colocalizes with PLIN1 in adipocytes, probably on lipid droplets (By similarity). SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
+{"protein": "MEVERVQAIASLSHSNGTIPAEFIRPEKEQPASTTYHGPAPEIPTIDLDDPVQDRLVRSIAEASREWGIFQVTNHGIPSDLICKLQAVGKEFFELPQEEKEVYSRPADAKDVQGYGTKLQKEVEGKKSWVDHLFHRVWPPSSINYRFWPKNPPSYRAVNEEYAKYMREVVDKLFTYLSLGLGVEGGVLKEAAGGDDIEYMLKINYYPPCPRPDLALGVVAHTDLSALTVLVPNEVPGLQVFKDDRWIDAKYIPNALVIHIGDQIEILSNGKYKAVLHRTTVNKDKTRMSWPVFLEPPADTVVGPLPQLVDDENPPKYKAKKFKDYSYCKLNKLPQ", "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": "MYRSSFLREVRKEKYERSDAYDELRGSPEFDSLAQAQGLENLQELNERFASYINRARVLEQRNTILRKQLETFQRMDELVGLDEAFAGQIEFNRQRMRELASDRAKLEREEKDAQRMLDEYHNKYRNEREYQQKLKETLERLNKEADEALLCNLELQIESQFLQDDINATKDRYKKNLMEIQTYVNILQQIIQTTPRVSPITTGISEEKLVAERRIPVLQSQLEEYKSILCQLQAQKYKLQTETTMLEQAIKNTQESYDDEIQLYNEQIENLRKGIEEAERTLEKYTTDCRQLVIYQQSLENELERYKRIIENEDSRLNSAIAGTPVTLFTQIYRPVQPQASRGRDITQAMQEIASVKPRQKALTKKLSRKKEIMSKDITDGLSPEKLYERTVEVFDQDQLEFRHEGSVTCEPGQEELELVEKEAVPEDVPDGAQISKAFDKLCNLVKEKIRVYKRPEAKVDSHPKGRYVLVTGEEGYEEPCFSSIPAGGGITVSTSNGKVTIGGDVEPIPELPEPSEPSEKEKRDICERRDEFETQDKLKEEEKEDLFEWGKIRGKIEQVTKYPDVSEPEAVPSPGLISPAEPGVLQETDHDREDKQGLLFREAGLPGSVSYEKVEVVESIEKFSDDRIQTYEETAMIVETMIEKTSKKKPGDKGS", "text": "FUNCTION: Required for the correct formation of lens intermediate filaments. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Cytoplasm, cytoskeleton Cytoplasm, cell cortex. SIMILARITY: Belongs to the intermediate filament family."}
+{"protein": "MRPLPTGIYTPLPCFFHENEDIDIEALQSHVKFIASAGTIPVVSGSMGEAIHLNREEKKTIIRSARVALDEVNLHDVPIVAGAGGASTRESIELCKDAAEAGADYVMVIPPGYYAGALLADTSSIKKFFVDIAEASPLPVIIYNFPAVSGGIDMDSDLIVQIIQSSANICGVKLTCANVGKLTRIMAQVSRPEFQAAFPRSSATPFRAIDGFIDFLLPSISVGSAGAISGLPNIAPKSCVKLWNLCQDSGSSKQATELQNLIALADGVALKIGIAGMKKLLHRHFGRKVACDMPNGPPCLRCTNKYQECTFEEGPGPRKRARLCEQTETFGTCEQPDGWQDLLTETRPNIGQSEDLEAVSPQGSLLGANQELESTSPRTSHSSLSQDDTASLHSRSSLSSSPGRFPPSQKLVATSDSPSQINSLEFIPDAFSFYIGPTGVTDIHILSHQKYNDQNVSLPKVNGLKYRIMDNPGQKEMATVDFSPPTVFGITDHSLLEKAEPKLDPQLTENGWPRLWAMMDPTAAWHLIKLYSRYIDPYFPILSSHQIPSSSAELNKMPLALLTAICATALPFVMYDDSLYTMLLNPPSSEELYRLCWLCISQELHAPSLATLQACLLLQQRLPTNMYLSDTAFAWTLMATSLAVAQTIGLHRDTGSWTSIPAWEKRLRRRLWWGLYAMEKWVALARGMPSHLGDDDYDVSMLKADDIQDTLSDSPDTQSHIYHLSNLSTILSDIQRSFYSVKAIGKTSNDLQYSLDLARPMRVRLKDWRDNLPSNLRPVSNAVISGEDLDGNGSLYLSYIVTHVALLRALLRPLDRWPAIIKVNKEEPEATYEGAKAVVTGALLCVKEFVEFVERLTGAQWNAFWHSWSRPNFAIAGSFMVHLLQIVTPPNQTDSQSMPELLKYSFEKEHTELQDWIRRWRWATRISANGAAGVKGLTNLGFIKVETLIGNGT", "text": "FUNCTION: Transcriptional regulator; part of the gene cluster that mediates the biosynthesis of communesins, a prominent class of indole alkaloids with great potential as pharmaceuticals. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLNSSGVRTQRRSPRPLSLGGRKIITPTKFAYDHHNPDKVLDFVEMDCLEPKTKNNLTGKLLLVASLLILAIIVISQSSSFTSPSAFSQREEGVTHVLVTGGAGYIGSHAALRLLRDSYRVTIVDNLSRGNLGAVKTLQQLFPQTGRLQFIYADLGDPLAVEKIFSENAFDAVMHFAAVAYVGESTLYPLKYYHNITSNTLGVLEAMARHKVKKLIYSSTCATYGEPEKMPITEDTPQVPINPYGKAKKMAEDMILDFSKNSDMAVMILRYFNVIGSDPGGRLGEAPRPELREQGRISGACFDAARGFIPGLQVKGTDYKTSDGTCIRDYIDVTDLVDAHVKALEKAQPRKVGIYNVGTGKGRSVKEFVEACKKATGVEIKVDFLPRRPGDYAEVYSDPTKILKDLNWTARFTNLQDSLQVAWRWQKIHPHGYNSY", "text": "SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
+{"protein": "MALHMILVMLSLLPLLEAQNPEHVNITIGEPITNETLSWLSDKWFFIGAAVLNPDYRQEIQKMQMVFFNITPNLINDTMELREYHTIDDHCVYNSTHLGIQRENGTLSKYVGGVKIFADLIVLRKHGAFMLAFDLKDEKKRGLSLNAKRPDITPELREVFQKAVKHVGMDESEIIFVDWKKDKCGQQEKKQLELEKETKKDPEEGQA", "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": "MEVMEGPLNLAHQQSRRADRLLAAGKYEEAISCHKKAAAYLSEAMKLTQSEQAHLSLELQRDSHMKQLLLIQERWKRAQREERLKAQQNTDKDAAAHLQTSHKPSAEDAEGQSPLSQKYSPSTEKCLPEIQGIFDRDPDTLLYLLQQKSEPAEPCIGSKAPKDDKTIIEEQATKIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGPIEKELDVDADFVETSELWSLPPHAETATASSTWQKFAANTGKAKDIPIPNLPPLDFPSPELPLMELSEDILKGFMNN", "text": "FUNCTION: May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro). FUNCTION: Involved in starvation-induced autophagy probably by its association with PI3K complex I (PI3KC3-C1). However, effects has been described variably. Involved in the induction of starvation-induced autophagy (PubMed:24785657). Stabilzes PI3KC3-C1 assembly and enhances ATG14-linked lipid kinase activity of PIK3C3 (By similarity). Proposed to negatively regulate basal and starvation-induced autophagy and to inhibit PIK3C3 activity by modulating interactions in PI3KC3-C1 (PubMed:25086043). May be involved in autophagosome biogenesis (PubMed:25086043). May play a role in neural progenitor cell survival during differentiation (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasmic vesicle Cytoplasmic vesicle, autophagosome."}
+{"protein": "MNSTPIEEARSLLNPSNAPTRYAERSVGPFSLAAIWFAMAIQVAIFIAAGQMTSSFQVWQVIVAIAAGCTIAVILLFFTQSAAIRWGINFTVAARMPFGIRGSLIPITLKALLSLFWFGFQTWLGALALDEITRLLTGFTNLPLWIVIFGAIQVVTTFYGITFIRWMNVFASPVLLAMGVYMVYLMLDGADVSLGEVMSMGGENPGMPFSTAIMIFVGGWIAVVVSIHDIVKECKVDPNASREGQTKADARYATAQWLGMVPASIIFGFIGAASMVLVGEWNPVIAITEVVGGVSIPMAILFQVFVLLATWSTNPAANLLSPAYTLCSTFPRVFTFKTGVIVSAVVGLLMMPWQFAGVLNTFLNLLASALGPLAGIMISDYFLVRRRRISLHDLYRTKGIYTYWRGVNWVALAVYAVALAVSFLTPDLMFVTGLIAALLLHIPAMRWVAKTFPLFSEAESRNEDYLRPIGPVAPADESATANTKEQNQR", "text": "FUNCTION: Nucleobase-proton symporter that mediates the sodium- dependent binding and uptake of 5-aryl-substituted hydantoin compounds (PubMed:16621827, PubMed:24952894). 5-indolyl methyl hydantoin and 5- benzyl hydantoin are the preferred substrates, with selectivity for a hydrophobic substituent in position 5 of hydantoin and for the L isomer over the D isomer (PubMed:16621827, PubMed:24952894). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family."}
+{"protein": "MGFGKSSPFLAFSILVLCQAGSLQATPLRSALETLPDPGALSEKEGRLLLAALVKAYVQRKTNELEQEEEQEETEDSSLDSSRAKRCSNLSTCVLSAYWKDLNNYHRYSGMGFGPETPGKKRDIANSLEKDLSSHFGVPTDAN", "text": "FUNCTION: Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calcitonin family."}
+{"protein": "MLRISSSSSMALKFSQILFIVLWLSLFFLLLHHLYSLNFRRLYSLNAVEPSLLKQHYRSYRLVSRKVLSDRFDFTPFHSRDNSRHNHRSGEQYDGDEIDPRYGVEKRRVPSGPNPLHH", "text": "FUNCTION: [CLE12p]: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. SUBCELLULAR LOCATION: [CLE12p]: Secreted, extracellular space. SIMILARITY: Belongs to the CLV3/ESR signal peptide family."}
+{"protein": "MRPRSALRYSLLLLALAASAAIQAQPKTLAVCTEAAPEGFDPARYTSGYTFDASAHPLYNALAAFAPGSATVIPALAESWDVSADGLVYTFRLRQGVKFHSTDYFKPTREFDADDVLFSFQRMLDPQHPAHDLSPSGYPYADAMQLRDIIERIEKIDEHQVRFVLKHPEAPFLADLAMPFGSILSAEYAGQLIARGKGDELNSKPIGTGPFVFTRYRKDAQVRYAANPDYWKGKPAIDHLVLAITLDPNVRVQRLRRNECQIALTPKPEDVAALRQDPQLTVLEEAAMITSHAAINTRHEPFDDPRVRRAIAMGFNKSSYLKIVFGDQARPAIGPYPPMLLGYDDSIRDWPYDPERAKALLKEAGVTPDTPLNLYISTGSGPGGNPARVAQLIQSDLAAIGIRVNIRQFEWGEMVKRTKAGEHDMMLYSWIGDNGDPDNFLTHNLGCASVESGENRARWCDKGFDEAIRKARMSNDESQRVALYKEAQRIFHEQMPWLPLAHPLMFDAQRKNVSGYRMSPMSARDFSRVKLD", "text": "FUNCTION: Binds different tripeptides. Probably recognizes specifically tripeptides composed exclusively of L-amino acids. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family."}
+{"protein": "MSRWKDMNKDELERQFSPSQWSHRMSADDVIKSHVTALKEGTERARGLAQTLLNVPYGEGEGEKLDVYVPTTTSLDVPLVIYLHGGYWQFLSKEESGFMAVPLVHKGVVVVAVGYDIAPKGNMDVMVSQVRRSVVSVIQQYSHISGLYLCGHSAGAHLAAMILSTDWSQYSVTPQIKGAFLVSGIYDLLPILSTYVNEPLKMTEEVALRNSPSQLVPQLKLSSSNCDIVVAVAQNDSPEFRKQSEDYYKALESTEGLKVTLEDVPNTDHFNIIEQLVDGDYHLTQLLLKMMGKS", "text": "FUNCTION: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the kynurenine formamidase family."}
+{"protein": "MNNKKTVTNRKGMIPNRLNKFSIRKYSVGTASILVGTTLIFGLSGHEAKAAEHTNGELNQSKNETTAPSENKTTEKVDSHQLKDNTQTATADQPKVTMSDSATFKETSSNMQSPQNATASQSTTQTSNVTTNDKSSTTYSNETDKSNLTQAKDVSATPKTTTIKPRTLNRMAVNTVAAPQQGTNVNDKVHFSNIDIAIDKGHLNKDTGKTEFWATSSDVLKLKANYTIDDSVKEGDTFTFKYGQYFRPGSVRLPSQTQNLYNAQGNIIAKGIYDSTTNTTTYTFTNYVDQYTNVSGSFEQVAFAKRENATTDKTAYKMEVSLGNDTYSEEIIVDYGNKKAQPLISSTNYINNEDLSRNMTAYVNQPKNTYTKQTFVTNLTGYKFNPNAKNFKIYEVTDQNQFVDSFTPDTSKLKDVTNQFNITYSNDNKTATVDLMNGQTSSNKQYIIQQVAYPDNTSTDNGKIDYTLDTDKTKYSWSNSYSNVNGSSTANGDQKKYNLGDYVWEDTNKDGKQDANEKGIKGVYVILKDSNGKELDRTTTDENGKYQFTGLSNGTYSVEFSTPAGYTPTTANAGTDDAVDSDGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKGVKVTLQNEKGEVIGTTETDENGKYRFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEETSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDTDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDADSDTDSDSDAGKHTPAKPMSTVKDQHKTAKALPETGSENNNSNNGTLFGGLFAALGSLLLFGRRKKQNK", "text": "FUNCTION: Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion. SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. SIMILARITY: Belongs to the serine-aspartate repeat-containing protein (SDr) family."}
+{"protein": "MSEKFAGKTTSTCYPSQPLGNTNKPLELYLFIDPLCPECWGLEPVIKKLTIEYGRFFTLRHILSGTWATWSARKGTKPEAMAKAWEWAANRTGMSCDGSVWLENPISSPFAPSLAIKAAEMQGKRAGLRFLRKLQEQLFLEKQNVADLSVLAECAVKAGLDVDEFLRDMHSPGAAKAFQCDLKITSEMDVDEIPTLVLFNENIEDEGIKISGCYPYDIYVELIAEMLGFHPEPSSPPPLESFLSHFKFVATKEVAVVYNWTIQEAETEMKKLQLKQKVERVPVKHGTFWRYIDDSRP", "text": "FUNCTION: Adapter protein required for efficient degradation of Spx by ClpXP under non-stress conditions (By similarity). Interaction with Spx stabilizes Spx and exposes the C-terminus of Spx for recognition and proteolysis by ClpXP (PubMed:30982633). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SpxH family."}
+{"protein": "MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLESGEVVEGHKKPSSDTPTHRLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDAAQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ", "text": "FUNCTION: Involved in the degradation of L-arabinose. Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5- phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction). SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily."}
+{"protein": "MQTYDNPDVKYEWWAGNARFADLSGQFIGAHVAHAALIVFWAGAFTLFEISYFDPTLPMGEQNLILLPHLATLGLGIEGNGAINTEPYFVIGAIHLISSAVLAAGGLFHVLRGPQDLKTATGPARRFHFDWEDPKQLGLILGHHLLLLGLGAFLLVAKAMYFGGLYDTATQTVRLVTEPTLDPAVIYGYQTHFATVDNLEDIVGGHIYVGVLLVAGGIWHILVPPLQWAKKVLLFSGEAILSYSLGAIALAGFVAAYFCAVNTTAYPVEFYGPVLDVKLSIVPYFADTIELPMNEHTSRAWLANAHFFFAFFFLQGHLWHALRAMGFDFRRVEKVLSDPLDA", "text": "FUNCTION: Functions as an antenna for photosystem I (PSI) under iron- limiting conditions, when phycobilisomes disappear. In the (PSI)3(Isi3)18 complex most of the harvested energy is probably used by PSI; in other PSI-containing supercomplexes a large part of the energy will probably not be used for light harvesting, but rather is dissipated to protect the organism from light damage. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. IsiA/Pcb subfamily."}
+{"protein": "MAVGNINELPENILLELFTHVPARQLLLNCRLVCSLWRDLIDLVTLWKRKCLREGFITEDWDQPVADWKIFYFLRSLHRNLLHNPCAEEGFEFWSLDVNGGDEWKVEDLSRDQRKEFPNDQVKKYFVTSYYTCLKSQVVDLKAEGYWEELMDTTRPDIEVKDWFAARPDCGSKYQLCVQLLSSAHAPLGTFQPDPATIQQKSDAKWREVSHTFSNYPPGVRYIWFQHGGVDTHYWAGWYGPRVTNSSITIGPPLP", "text": "FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex."}
+{"protein": "MTNKLLSIKIADPYAEAFFQLSLSLYIKNNDPDLFYQLIFDIQDFLKLLKETPELDNFLKNPLNSNILKKNILNKIIENKFNLQTINFLNLLIDKKRIDTIQTIGKIFLEKAYEFVCIKFVEVWSTIELSQKQQENLIQKINILLGPIFSEPSVQFYKIQLTLMLDTNLLGGLIIKMGSKIIDLSLRNELQQLGKKLDITI", "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: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase delta chain family."}
+{"protein": "MSSERAQFAAEVAEVERWWKSPRFARVNRPYTAADVVSKRGTIKINYPSDVQGKKLWKLLSEHAKNGTPSHTYGALDPVQVTQMAKYLETVYVSGWQSSSTASSSNEPGPDLADYPSNTVPNKVEHLFMAQLFHDRKQREARSRMSDAELANTPVIDYLRPIVADADTGHGGLTAVMKLTKMFVEKGAAGIHIEDQAPGTKKCGHMAGKVLVPIQEHINRLVAIRLQYDIMGVENLVVARTDSEAATLITSNIDDRDHPFIQGSTNPSLPPLNNVMVEAEAQGKTGDQLQAIEDGWIKAANLQLFPQALAQALANEGASRSTVEKLVARVSRLSWPQAVAVAQKEFGLKQVPYWNWDAPRTREGYYRYQGGTECAIHRANAFAPYADLLWMETKKPILAQAKEFAAGVHAVHPGQWLAYNLSPSFNWEAAGLNAQDMQAYVWELGKLGFVWQFITLAGLHSNAYISDLFAQNFAKTGMKAYVELVQSREREIGCDVLTHQKWSGADYADSLIKTVTGGVSSTAAMGAGVTESQFTSKL", "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": "MPKISIHEALFFELLGERCDDDTLERRLRSAKAELECSSFSVREDKEGGSLSPGGEVCDPVQRTRGQASCVREGAFDARLLKIELNDTNRPDLWSTAGLARLLRVHAGGASRAAQYRAFLSDRCTVRDSYGRCVVVDARLQTIRPFIAGFVARGTGLSEVRLWDLIQTQERLASNFGRRRCTLSLGCYRAQDICWPLAYRAVLLAEVSFTPLGMSMPLSGEQILTQHPKGREYGHLLKDYSFVPLLVDARGEVLSLIPITNSASLGAVVTGDTELFIECSGTDMCAVLVAVNSLACDLSDMGMQIEPVQITYSFDTPWGRSVTTPFYFQEKREVAHEQIDRLLGMPLPVADITEAFARMDCAVQVKQGTYVVEPAAYRNDFLHAVDLIEEVMLGRTLDRFSPQVPCSFTVGRLSDLTLLTRKIKHLLVGFGYQEMIFHYLGSAREFCTRMRCTADDLIEIENPLTESYRFVRRSIIPCLLSAELKSAHALYPHRIFEIGKVAFCSPHGEHGTCTQQSLGFLNASQEASYNEVASLVSGLLYCLKLPYQVEEAQDPRFVLGRQASICVHGSRVGIFGEIHPQVLSNWDIRMPCFAGELDVGALLP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily."}
+{"protein": "MNPESSIFIEDYLKYFQDQVSRENLLQLLTDDEAWNGFVAAAELPRDEADELRKALNKLASHMVMKDKNRHDKDQQHRQWFLKEFPRLKRELEDHIRKLRALAEEVEQVHRGTTIANVVSNSVGTTSGILTLLGLGLAPFTEGISFVLLDTGMGLGAAAAVAGITCSVVELVNKLRARAQARNLDQSGTNVAKVMKEFVGGNTPNVLTLVDNWYQVTQGIGRNIRAIRRARANPQLGAYAPPPHVIGRISAEGGEQVERVVEGPAQAMSRGTMIVGAATGGILLLLDVVSLAYESKHLLEGAKSESAEELKKRAQELEGKLNFLTKIHEMLQPGQDQ", "text": "FUNCTION: May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the apolipoprotein L family."}
+{"protein": "MADQNNPWDTTPAADSAAQSADAWGTPTTAPTDGGGADWLTSTPAPNVEHFNILDPFHKTLIPLDSWVTEGIDWVVTHFRPVFQGVRVPVDYILNGFQQLLLGMPAPVAIIVFALIAWQISGVGMGVATLVSLIAIGAIGAWSQAMVTLALVLTALLFCIVIGLPLGIWLARSPRAAKIIRPLLDAMQTTPAFVYLVPIVMLFGIGNVPGVVVTIIFALPPIIRLTILGINQVPADLIEASRSFGASPRQMLFKVQLPLAMPTIMAGVNQTLMLALSMVVIASMIAVGGLGQMVLRGIGRLDMGLATVGGVGIVILAIILDRLTQAVGRDSRSRGNRRWYTTGPVGLLTRPFIK", "text": "FUNCTION: Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake (PubMed:3305496, PubMed:7898450, PubMed:23249124). Probably responsible for the translocation of the substrate across the membrane (Probable). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily."}
+{"protein": "MQRYDIIRMIGKGGMGEVYLAYDPVCSRKVALKRIREDLSDNELLKKRFLREAKIAADLVHPGVVPVFTICSDSDPVYYTMPYIEGYTLKSLLKSVWQCDSLPKDLAEQTSVATFLSIFHKICSTVEYVHSRGILHRDLKPDNILLGLFSEVVILDWGAALSKEMEEDFLSDIDVRIPGSLFSNMTIPGKIVGTPDYMAPERLRGTPASESTDIYALGVILYQMLTLSFPYRKKKGQKISLRHQISFPEEIAPHREIPPFLSQVVMRALAADPRERYRSVSALKADIEQHLQGSPEWTPKIVLHTQDRECWKFHEPILLSKYFPMLEVSPALWYSLAISKIESFSEVRLEYTLLRKGLEEGFGILLPPSEGVDHGDFYHGYGFWLHIKENILSVSLVKNGLEIQKTSRHIDGNKEKFFIAFEKQNHRLSLIIDNIVWTIHMDYLPARGGRIGVIIQDVADVCGNIVVLESSGSLQVSCLAVPDAFLNEKLYERAITFYRRIVESFPGRKEGYEAQFRIGIALLEKASENSDSEGFIQALEEFSTLHNSVAAPLEYLGKALVYQRLGEYNEEVKSLLLALKRYCQRPEISRVRDHVVYRLHEALYSNHRISLVFMLLALHVAPESINASEEEHFLQNLHGKIQDTLFCNLDISPVDFRSSKMELLLSYWSGFTPFLLGLFQRSWDLKDYRALADIFYTAADLGNKEFIEEYSGILRENIRTTTFSKEIVEILPDQLLCFLSGLEALTLQESIEKVFDGIENLDPVLILYLFDLFAKDALIHGRGEEILKAIALVEKYISPQQRYRYLLPYEVLSYLWMKDANKVYDLLSSYDESSWIDDSSHAFVLYGYWLALAEDSSLAYLHLSGCREDSVFPRALIGVFCSPLGICEEQLSYQERRQLLLQKFIFFHCLGNSEERDKCRTAYDSKERSL", "text": "FUNCTION: Together with the serine/threonine kinase Pkn1, may play a role in the specific interactions with host proteins during intracellular growth. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MLITDIINQASSQLREAGIETPEHDAKLLLAEAAGVELRDVDRALLMGEELGTTGQLAVFRAMLDRRAKREPLQYITGHAPFRYLDLKVGPGVFIPRPETETVVQAGLDWLTKNGMIHPCVVDLCAGSGAIGLSVVSEVPGSQVWAVELSPNTAEWTRRNLSETAKKYPSIASNYHLEIADATSFATLAQLDGTVDIVITNPPYVPQTDIPEQPEVRDWDPELALYGGSMDGTLIPERIIERACRLLKPGGVLVMEHDVTQGDRLVAFARATGFAAASTGQDWTGRDRYLFAVS", "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": "MATCIGEKIEDFRVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRRKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLAAQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPTFLSREAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSKKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDRRRLLIEQPLPNKMTIFPKNKNPSDFSSSGDGISFYTSWGNQEQETSNSGRGRVIQEAEERPHSRYLRRAHSSDRSETSHGQSRVKTYTMERCYSAEMLSKSKRSGVEENERYSPTNNDANIFHFFKEKTSNSSGSFEGPDNNQALSNHLCPGKTPFPFPEQTPQTEMVQQWFGNLQINDPSCEQSKTRGVEPPLVYQKRTLRSITSPLTAYRLKPIRQKTKKAVVSILDSEEVCVELLKDYASQEYVKEVLQISSDGSMITIYYPNDGRGFLLADRPPSPTDNISRYSFDNLPEKYWRKYQYASRFVQLVRSKSPKITYFTRYAKCVLMENSPGADFEVWFYDGAKIHKTEDLIQVIEKTGRSYTLKGESEVNSLKEEVKMYMNHANEGHRICLALESIISEEEKKSGSAPFFPIIVGRRPSSTSSPKALTPPPPVDPNYPMRETPSLNRMIINSAASPKQAPVLNPPVVTNEGLGLMGAASETNSSPRSLKDCLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPSFH", "text": "FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (By similarity). Phosphorylates CEP131 and PCM1 which is essential for proper organization and integrity of centriolar satellites (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Nucleus, nucleolus Cleavage furrow Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Associates with centrioles throughout the cell cycle. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily."}
+{"protein": "MRTIAILAAILLFALLAQAKSLQETADDAATQEQPGEDDQDLAVSFEENGLSTLRASGSQARRTCRCRFGRCFRRESYSGSCNINGRIFSLCCR", "text": "FUNCTION: [Defensin alpha 5]: Exhibits bacteriostatic activity against Gram-positive bacteria S.aureus and L.monocytogenes and Gram-negative bacterium E.coli, antifungal activity against C.neoformans and microbicidial activity against Gram-positive bacteria S.aureus and L.monocytogenes. FUNCTION: [Defensin alpha 4]: Exhibits bacteriostatic activity against Gram-positive bacteria S.aureus and L.monocytogenes and Gram-negative bacterium E.coli, antifungal activity against C.neoformans and microbicidial activity against Gram-positive bacteria S.aureus and L.monocytogenes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MVIPATSRFGFRAEFNTKEFQASCISLANEIDAAIGRNEVPGNIQELALILNNVCRRKCDDYQTRAVVMALMISVKSACQLGWFPERETQELLAIIDLMWNGFSCPENVTSCVNSPVTLISQVIERFYPCVKLGHILVSFEAKPESKMMMKDFHISKKMPHSPKQKVGLFVVRTEDISRSNCIVHPQGVSFLLNGKGIDKRVNISMESGPQLPTNVTALLNLGANLLQAIGCFGGSYLIAIAFMDVIPLPNKPLLKDYVHPEVVGSNSDCDIIEGPSRISLSCPISRTRIKLPVKGHVCKHLQCFDFWNYVNMNTRRPSWRCPHCNQSVCYTDIRVDQKLRKILEEVGRNAADVVISADGTWMVETENDEDVELVPETTHDHGDPNSFINLGPTVKNPARDENEMETSTQVEEHNPCLSEIQGPSNDTHRPASDYTMLNQSHTSTNTLPQLPRTLNAFDGQQFVNLPQVINTRDSPASQALPMTFSPTPSPQDILATNAANFGTSMPAAQSSQFQGSHVTSLGNCEGRTSDLMARWNHIYGRVQTQFPPAPLSHHHYSMQNQSPSPAQQRPVPSYIAHPQTFHVNYGENADQRWMPSSIAHPQTLPVNYGGNTNQRPIPSSIAHPQTLPVNYRGNTDHRSTPYSITHLQTLLNYGGNADQRPMPSSITNLQTLPATYGGYAHQRPMSSSITHPRTSPVNYGGTPDQRPMPSSITHPQTLPVSYGGTTDQILNPGGAMGQFSSREFMNLTPANTENWRPQSRMRGSVAPGTGYDHMIIHPTRPVHPQAQTPPAPLSTSYDGADEIQAFIGHPSYPVSNNETQAGTSSLPVAEGLGYSGSFWSMPPETW", "text": "FUNCTION: E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates. Involved in stress responses (e.g. osmotic, salt and abscisic acid ABA) and sulfur metabolism. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PIAL protein ligase family."}
+{"protein": "MALLSAAPRALRLPRRLPLGAALPALRALATPAAAQKVPVSLIAALRKQHPVPLAQAREALERSGLDLAAALDYLRTSTSASAEKKAAKVSGRDTNEGLIAISLLGGKRVGMIHLACETDFVARNQVFLDTARGVAETTAFLDVPGDHEKPQIASSPYAFDPILDFPTESLLSAPLISLPAADTADGSLSPLPTSEPTTIKQSLLSSLAQTGENLKLLRAVSFAAPFPSTPDVRFVPGGYAHGGITDKEGKVGGIVVLSVTSADPEKPIASIIHGPGGDDLEKAAESLARTVARQVVGFPTKVIDRGDRAVDDEEVLMEQPFMMFNGDSRSVKDVLAEWGKERGVVLRVVGMRRWAVGDEIEIKEKETDA", "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": "NTGELFFGEGSRLTVL", "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": "MLVWLAEHLVKYYSGFNVFSYLTFRAIVSLLTALFISLWMGPRMIARLQKLSFGQVVRNDGPESHFSKRGTPTMGGIMILTSIVISVLLWAYPSNPYVWCVLVVLIGYGIIGFVDDYRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLVGKDTPATQLVVPFFKDVMPQLGLFYILLSYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNMNFANYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLATLKVR", "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. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily."}
+{"protein": "MTSHGAVKIAIFAVIALHSIFECLSKPQILQRTDHSTDSDWDPQMCPETCNPSKNISCSSECLCVTLGGGDETGTCFNMSGVDWLGHAQASDGHNDG", "text": "FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL10 and CXCL11. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MYLYIETLKQRLDAINQLRVDRALAAMGPAFQQVYSLLPTLLHYHHPLMPGYLDGNVPKGICLYTPDETQRHYLNELELYRGMSVQDPPKGELPITGVYTMGSTSSVGQSCSSDLDIWVCHQSWLDSEERQLLQRKCSLLESWAASLGVEVSFFLIDENRFRHNESGSLGGEDCGSTQHILLLDEFYRTAVRLAGKRILWNMVPCDEEEHYDDYVMTLYAQGVLTPNEWLDLGGLSSLSAEEYFGASLWQLYKSIDSPYKAVLKTLLLEAYSWEYPNPRLLAKDIKQRLHDGEIVSFGLDPYCMMLERVTEYLTAIEDFTRLDLVRRCFYLKVCEKLSRERACVGWRRAVLSQLVSEWGWDEARLAMLDNRANWKIDQVREAHNELLDAMMQSYRNLIRFARRNNLSVSASPQDIGVLTRKLYAAFEALPGKVTLVNPQISPDLSEPNLTFIYVPPGRANRSGWYLYNRAPNIESIISHQPLEYNRYLNKLVAWAWFNGLLTSRTRLYIKGNGIVDLPKLQEMVADVSHHFPLRLPAPTPKALYSPCEIRHLAIIVNLEYDPTAAFRNQVVHFDFRKLDVFSFGENQNCLVGSVDLLYRNSWNEVRTLHFNGEQSMIEALKTILGKMHQDAAPPDSVEVFCYSQHLRGLIRTRVQQLVSECIELRLSSTRQETGRFKALRVSGQTWGLFFERLNVSVQKLENAIEFYGAISHNKLHGLSVQVETNHVKLPAVVDGFASEGIIQFFFEETQDENGFNIYILDESNRVEVYHHCEGSKEELVRDVSRFYSSSHDRFTYGSSFINFNLPQFYQIVKVDGREQVIPFRTKSIGNMPPANQDHDTPLLQQYFS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylyl cyclase class-1 family."}
+{"protein": "MKTLNRRDFPGALWPERIIQFGEGNFLRAFIDWQVDLLNEHTDLNAGVVVVRPIASDFPPSLSTQDGLYTTIIRGLNEKGEAVSESRLIRSVNREISVYAQYDEFLKLAHNPDIRFVFSNTTEAGISYHAGDQFDDAPAVSYPAKLTRLLFERFSHFDGAQDKGWVIIPCELIDYNGEALRELVLRYAHEWALPAAFTTWLESANSFCSTLVDRIVTGYPRDEVAQLEESLGYHDAFLDTAEHFYLFVIQGPQWLARELRLDKLPLNVLIVDDIKPYKARKVAILNGAHTALVPVAFLAGLNTVGEAMNDAQICAFVERAIHDEIIPVLDLPRNELESFADAVVSRFRNPYIKHQLLSIALNGMTKFRTRILPQLLAGQAQMGTLPPRLTFALAALIAFYRGERNGEGYPLQDDAHWLARFEQLWTQRGDNTITLRELVDAVLSDCEHWEQDLTAVPGLAAQVTRDLDAILNQGMRHAVAPLC", "text": "SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB subfamily."}
+{"protein": "MFTATEAVPVAKVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQELSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHVDIAPVAPQEIVDQAVLEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQEFHAPVNVDELMSAILSVH", "text": "FUNCTION: Probably part of a binding-protein-dependent transport system YphDEF. Probably responsible for energy coupling to the transport system. SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MTGHAPESTFNADGSRKMIATQQQCEDKNLPLSFRDYCAHLLIPLNDCRVSTYYAPWKCMDEKHAYEGCQYDEYLYRKIKKSEQDEAERIKREVVIEKENPKDRPYEEIKLS", "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 Mitochondrion intermembrane space. SIMILARITY: Belongs to the complex I NDUFB7 subunit family."}
+{"protein": "MSVHATDAKPPGPSPADQLLDGLNPQQRQAVVHEGSPLLIVAGAGSGKTAVLTRRIAYLMAARGVGVGQILAITFTNKAAAEMRERVVGLVGEKARYMWVSTFHSTCVRILRNQAALIEGLNSNFSIYDADDSRRLLQMVGRDLGLDIKRYSPRLLANAISNLKNELIDPHQALAGLTEDSDDLARAVASVYDEYQRRLRAANALDFDDLIGETVAVLQAFPQIAQYYRRRFRHVLVDEYQDTNHAQYVLVRELVGRDSNDGIPPGELCVVGDADQSIYAFRGATIRNIEDFERDYPDTRTILLEQNYRSTQNILSAANSVIARNAGRREKRLWTDAGAGELIVGYVADNEHDEARFVAEEIDALAEGSEITYNDVAVFYRTNNSSRSLEEVLIRAGIPYKVVGGVRFYERKEIRDIVAYLRVLDNPGDAVSLRRILNTPRRGIGDRAEACVAVYAENTGVGFGDALVAAAQGKVPMLNTRAEKAIAGFVEMFDELRGRLDDDLGELVEAVLERTGYRRELEASTDPQELARLDNLNELVSVAHEFSTDRENAAALGPDDEDVPDTGVLADFLERVSLVADADEIPEHGAGVVTLMTLHTAKGLEFPVVFVTGWEDGMFPHMRALDNPTELSEERRLAYVGITRARQRLYVSRAIVRSSWGQPMLNPESRFLREIPQELIDWRRTAPKPSFSAPVSGAGRFGSARPSPTRSGASRRPLLVLQVGDRVTHDKYGLGRVEEVSGVGESAMSLIDFGSSGRVKLMHNHAPVTKL", "text": "FUNCTION: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair (By similarity). FUNCTION: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is required for activity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair, as well as in nitrosative and oxidative stress response and possibly in persistence in the host. Inhibits RecA-mediated DNA strand exchange; this does not require ATPase activity. When combined with UvrA greatly inhibits RecA- mediated DNA strand exchange (By similarity). FUNCTION: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is required for activity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair, as well as in nitrosative and oxidative stress response and possibly in persistence in the host. Inhibits RecA-mediated DNA strand exchange; this does not require ATPase activity. When combined with UvrA greatly inhibits RecA- mediated DNA strand exchange. SIMILARITY: Belongs to the helicase family. UvrD subfamily."}
+{"protein": "MTDIQIAVQEQPFDQNAVYQWLSEQHSIGATVIFVGKVRDLNLGDEVSSLYLEHYPAMTEKALNEIVAQAKVRWDIQRVSVIHRVGLLQTGDEIVLVGVSSAHRGDAYHANEFIMDFLKSKAPFWKKEQTNQGERWIEARESDKEALEKW", "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": "MRKDETSNTSPDISAAQPASALRYQLRPPRRNDGAAIHQLVSECPPLDLNSLYAYLLLCEHHAHTCVVAESPGGRIDGFVSAYLLPTRPDVLFVWQVAVHSRARGHRLGRAMLGHILERQECRHVRHLETTVGPDNQASRRTFAGLAGERGAHVSEQPFFDRQAFGGADHDDEMLLRIGPFTHPPH", "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": "MLTLKIAVYIVVAFFIALFVFGFLSSDPTRNPGRKDFE", "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 PsbI family."}
+{"protein": "MTSRPETKIPDEITSPYPIIGAGTIESGFGRGSAELGIPTANIPVTSELNKLETGIYYGWCRLVPRNQECAAKQRSDGKKVYFNNGTKLADDELETFPMAMSIGWNPFYNNETKTAEVHIIHKFRENFYGADLRYAVMGHIRPELNYTTKEALIADINKDIEITKDALSKPSYEKYRTKI", "text": "FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme. SIMILARITY: Belongs to the flavokinase family."}
+{"protein": "MALSGNCSRYYPRDQGAAVPNSFPEVIELNVGGQVYFTRHSTLISIPHSLLWKMFSPKRDTANDLAKDSKGRFFIDRDGFLFRYILDYLRDRQVVLPDHFPERGRLKREAEYFQLPDLVKLLAPEDVKQSPDEFCHSDFEDASQGSDTRICPPSSLLPHDRKWGFITVGYRGSCTLGREGQADAKFRRVPRILVCGRISLAKEVFGETLNESRDPDRAPERYTSRFYLKFKHLERAFDMLSECGFHMVACNSSVTASFVNQYTEDKIWSSYTEYVFYREPSRWSSSHCDCCCKNGKGDKGESGTSCNDLSTSSCDSQSEASSPQETVICGPVTRQSNIQTLDRPIKKGPVQLIQQSEMRRKSDLLRTLTSGSRESNISSKKKAAKEKLSIEEELEKCIQDFLKIKIPDRFPERKHPWQSELLRKYHL", "text": "FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization. SUBCELLULAR LOCATION: Presynaptic cell membrane Postsynaptic cell membrane Note=Colocalizes with GABRB1."}
+{"protein": "MAMMMRKAAAVPASSRRSVAVNSVSGKRTVSGKAGAPVPEDVLAYAKTLPGVTAPFDNVFDPAGFLATASVKDVRRWRESEITHGRVAMLAALGFIVGEQLQDFPLFFNFDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKTLQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLVLRFEKEVILELEDVERDLGLPLTPLPDNLKAI", "text": "FUNCTION: Required for non-photochemical quenching (NPQ), a mechanism that converts and dissipates the harmful excess absorbed light energy into heat and protect the photosynthetic apparatus from photo-oxidative damage (PubMed:27335457, PubMed:29555769, PubMed:30782831). Is able to sense luminal acidification of the thylakoid membranes, which occurs along with elevated electron flow caused by excess light, and to induce a large, fast, and reversible pH-dependent quenching in LHCII- containing membranes (PubMed:27335457). Mediates excitation energy transfer from light-harvesting complex II (LHCII) to photosystem I (PSI), rather than photosystem II (PSII), at low pH, which mimics the acidified lumen of the thylakoid membranes in high light-exposed chloroplasts (PubMed:29555769, PubMed:30782831). Activates PSI- dependent fluorescence quenching in addition to dissipating excitation energy in LHCII to avoid photooxidative stress under excess light (PubMed:29555769, PubMed:30782831). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family."}
+{"protein": "MARGVAGVLRRAYSSRVTVLFSTRNLHSFRESESRSLCNSDFDVPTNRFCSGNRVRIQFPWNDYRFGCFEIGKVRSFSSTVDNNGENDDIEESVGSESDDYDEEGLINELSDVDEGLLNDSVVAETDEIGSEAARALNDRYHDPVELYRELRGSEVRSKLQHSEWDSLHEIFGFFAQSGWAANQALAIYIGKSFFPTAVSKFRDFFIEKCGIEVVQDLVRVGPTDVAVKFLFPVFVEFCIEEFPDEIKRFKSIVDTADLTKPATWFPFARAMKRKIVYHCGPTNSGKTYNALQRFMEAKNGLYCSPLRLLAMEVFDKVNALGIYCSLLTGQEKKYVPFANHVSCTVEMVSTDELYEVAVLDEIQMMADPSRGHAWTKALLGLKADEIHLCGDPSVLDIVRKMCADTGDELVEEHYERFKPLVVEAKTLLGELKNVKSGDCVVAFSRREIFEVKMAIEKHTNHRCCVIYGALPPETRRQQAKLFNDQENEYDVLVASDAVGMGLNLNIRRVVFYSLNKYNGDKIVPVAASQVKQIAGRAGRRGSRYPDGLTTTLHLEDLNYLIECLQQPFDEVTKVGLFPFFEQIELFAAQVPDMAFSNLLEHFGKHCRLDGSYFLCRHDHVKKVANMLEKVEGLSLEDRFNFCFAPVNIRNPRAMHNLYRFASSYSQNMPVNVAMGIPKSSAKSDAQLLDLESRHQILSMYLWLSNQFEENFPFVEKVEAMATNIAELLGESLSKASWKMESKEEKVKGQMKEDRGYERPASLIKLVKKRKDEKLV", "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. SUBCELLULAR LOCATION: Nucleus Mitochondrion matrix Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the DExH box helicase family."}
+{"protein": "MKKLTTLLLASTLLIAACGNDDSKKDDSKTSKKDDGVKAELKQATKAYDKYTDEQLNEFLKGTEKFVKAIENNDMAQAKALYPKVRMYYERSEPVAEAFGDLDPKIDARLADMKEEKKEKEWSGYHKIEKALYEDKKIDDVTKKDAQQLLKDAKELHAKADTLDITPKLMLQGSVDLLNEVATSKITGEEEIYSHTDLYDFKANVEGAQKIYDLFKPILEKKDKKLSDDIQMNFDKVNQLLDKYKDNNGGYESFEKVSKKDRKAFADAVNALGEPLSKMAVITE", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the EfeM/EfeO family."}
+{"protein": "MLMTMRKHGITLAVFAALATGLTALVNGLTTSTIERQAARQQMQLLDQVVPPDLYNNQLLDECYLVTDPALGSDAPHRLYLARKDGTPVAAAIETTAPDGYAGAIDLLVGADFSGNVLGARVTSHHETPGLGDKIELRLSDWITHFSGKSLRSDNDMSWAVKKEGGMFDQFTGATITPRAVMNAVKRTAGYLKKNLNALEKMPHCGDSSHE", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RnfG family."}
+{"protein": "MKLLLTLLLGSALMCITLADECGLGTHRPVKEVIDNVRTMYYCDCRAGDAERSITVSRCDDNNQKQDDVILTYCGLEQTTGCNTNPYTAAKHDSSGDKPQFYCSCLNYKYEQSHADSRYWTIRCYMGDICD", "text": "FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion channels. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MGAFTEKQEALVNSSWEAFKGNIPQYSVVFYTSILEKAPAAKNLFSFLANGVDPTNPKLTAHAESLFGLVRDSAAQLRANGAVVADAALGSIHSQKALNDSQFLVVKEALLKTLKEAVGDKWTDELSTALELAYDEFAAGIKKAYA", "text": "FUNCTION: Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. SIMILARITY: Belongs to the plant globin family."}
+{"protein": "MEADITNLRNKLKECEDERLKAAHYGLQLLERQTELQSQLDKCHEEMMITAEKYNQEKHALQREVELKSRMLDSLSCECEALKQQQKAQLEQLEVQLHRSHRQEVSDLKNKLENLKVELDEARLGEKQLKQKLDLQGELLAHKSEELRLLSEQRVLSSMSSELLALETELTAAEGVKNALKEEVNELQYKQEQLECLNTSLLHQVDRLKEEKEEREREAVSYYNALEKARVENQDLQVQLGHALQQAADPNSKGNSLFAEVEDRRVAMERQLNLMKDKYQSLKKQNAFTRDQMNKMKLQISTLLRMRGSQTEFEQQERLFAMIEQKNGEIKHLLGEINKLEKFKNLYESMESRPSTSDTACVLEDSTYYSDLLQLKLDKLNKENESTKDELSIQRMKALFESQRALDIERKLFTNERHLQLSESENMKLRAKLDELKLKYEPEERIEVPVLKRRREVLPLNITTPEETEETAAASATEDGVSRLPPHREEESCLNSLKDNTVQWKQPASSCVQPASLSPHKNLHLDTQPKKEKKCVKLVDSPANIEVLHEQSGNTPNSPRLTAESKLPTEVKERIETTSKLGKGACKKSHNIIYVSSKSAPETQCSQQ", "text": "FUNCTION: Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non- processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (By similarity). Plays a role in cell migration (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Chromosome, centromere, kinetochore Nucleus. Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the nucleus in interphase and to the kinetochore in early prometaphase. Relocalizes to the mitotic spindle pole before metaphase and is subsequently lost from the spindle poles after chromosome congression is completed. Removal of this protein from the kinetochore requires the dynein/dynactin complex. SIMILARITY: Belongs to the Spindly family."}
+{"protein": "MNEVTCSITGDNPIHKINNGLGLKWNNLGKFSDFQTNDSAARDARTIDYIFTNCQTGSSIGKIDFRAALPADKSQHSGVSEKEFSRLENQWSKEFSCFPKNKNADVTKPSRNKHEKRSANLHNRYFAQYYSTAYQQNRIYPCRISYNEHSSVSNGWEFQFKSIENQLLNELKIENNVEEKTVGYEYVAEYEETIDFMHMLSSVPQTYQFLKSNIYITERDPYKIGCVLMDNGSNLNEVVMAFEAAISQDPSHINAWLKLGIVNFENESESNGELALRNCLNLDPNNTIALENLAIHHINQQNESESLKLFHKWILSKFSKVFQPSAGENKDSINKIPKKAHLAHILESLLNMGIEKKDQYDIYSVLSILYYSDQKIKQSQKCLEFLLLEKPNNGTIWNRYGAILANTKSYHSAINAYNKCKQLRPNFTRVRYNLAIAYMNKGDYVKASKMLIEVILLRSKGYEHNKAKMQNKFMQNLKNALIASKNFDSLDLINGSHNTESLISTLKAIYNKMD", "text": "FUNCTION: Peroxisomal import receptor that mediates the peroxisomal import of both malate synthases MLS1 and MLS2 in oleate-grown cells (PubMed:27678487, PubMed:27663510). Recognizes the C-terminal peroxisomal targeting signal PTS1 sequence SKL of MLS1 and MLS2, probably via its TPR domains (PubMed:27678487). Interacts with the PTS1-receptor docking protein PEX14 but not with peroxins PEX1, PEX3 through to PEX8, PEX10, PEX11, PEX12, PEX13, PEX15, PEX17, PEX18, PEX19 and PEX21 (PubMed:27678487). SUBCELLULAR LOCATION: Cytoplasm Peroxisome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the peroxisomal targeting signal receptor family."}
+{"protein": "RRTVKSAPQ", "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": "REAAERSKMIDRNLREDGEKASKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYKVVVYSNTIQSIIAIIRAMGRLRIDFGDVARADDARQLFVLASSAEEGVMSPELAGVIQRLWEDSGVQACFSRSREYQLNDSASYYLSDIERIAQGSYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLLLAEDEEMNRMHESMKLFDSICNNKWFIDTSIILFLNKKDLFEEKISRSPLTICYPEYSGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKSNLMECGLY", "text": "FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. Stimulates the activity of receptor-regulated K(+) channels. May play a role in cell division. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome 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": "MTAQVDRYVSFKGIDWVGRSREIFARLQSHIDQANSPFWPYFTRQRKLAHSQGLDDLRVLHNYLPTLRELLENMGDLKTLGMLEELEQICM", "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": "MKGKLLKGVLSLGVGLGALYSGTSAQAEASTNQNDTLKVMTHNVYMLSTNLYPNWGQTERADLIGAADYIKNQDVVILNEVFDNSASDRLLGNLKKEYPNQTAVLGRSSGSEWDKTLGNYSSSTPEDGGVAIVSKWPIAEKIQYVFAKGCGPDNLSNKGFVYTKIKKNDRFVHVIGTHLQAEDSMCGKTSPASVRTNQLKEIQDFIKNKNIPNNEYVLIGGDMNVNKINAENNNDSEYASMFKTLNASVPSYTGHTATWDATTNSIAKYNFPDSPAEYLDYIIASKDHANPSYIENKVLQPKSPQWTVTSWFQKYTYNDYSDDYPVEATISMK", "text": "FUNCTION: Required, with sphingomyelinase, to effect target cell lysis (hemolysis). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neutral sphingomyelinase family."}
+{"protein": "MSTLKKPDLTDTKLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACVVGLAVLDPAFLGDKANPFATPLEILPEWYLYPVFQILRVVPNKLLGIALQTLIPLGLMILPFIENINKFANPFRRPVAMSLFLFGTVLTMYLGIGACLPIDKSLTLGLF", "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. PetD subfamily."}
+{"protein": "MYNYTIYHPVKISGRGLYTGINSTITIYPELPHVGIYFLRTDLTDYPIVPIIPSTLLVLNSKLSTVLGFHDDYSIMLIEHLMSAISLSQLTDLKIILEGPEIPILDGSSIIWLKLLQQAKIYITSLSNCIIFKSSCTFFIQTKDTFIISFPYTSLAINTGIDFKNCLAIKSQWITILDLLINRFELVGIASSRTFGDFNQINILINEGFFQGANLYNALAFQLGNWCNGPLRFICEPAKHKVLDLIGDLRLLGVYNMFFLIGYKTNHFVNSQLVQFFKKLDK", "text": "FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. The target for the lipopolysaccharides produced in the chloroplast could either be the cell envelope of the eukaryote or the plastid membrane. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the LpxC family."}
+{"protein": "MNNLTPENIRQTILATPFLLNRIRTEFPQLAAVLNDPNAFATTWQSINASQLLQIPSSTYSMGMPSFSEDDLFDVEVQRRIEEQIRQNAVTENMQSAIENHPEVFGQVYMLFVNVEINGHKVKAFVDSGAQATILSADCAEKCGLTRLLDTRFQGVAKGVGMAKILGCVHSAPLKIGDLYLPCRFTVIEGRDVDMLLGLDMLRRYQACIDLENNVLRIHGKEIPFLGESEIPKLLANVEPSANAHGLGIEPASKASASSPNPQSGTRLGTKESVAPNNEGSSNPPSLVNPPTDPGLNSKIAQLVSMGFDPLEAAQALDAANGDLDVAASFLL", "text": "FUNCTION: Recognizes and binds polyubiquitin chains (PubMed:11584278, PubMed:16138082). Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Aspartic protease. Appears to act as negative regulator of constitutive exocytosis. May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly. Required for S-phase checkpoint control (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the DDI1 family."}
+{"protein": "MVDINLECVHFIEPKNTRSTEQQQQNVKNAYLEAVRILLVLLENVLSQPNNTKFRTIRLDNKAIKEKLLSLPGCEKLLYAIGFRHTPSSNSYTLPGEVSLQQIQKYYDVLRERRTAWLSGAMPKSPAHPKAACSTPSPLFIKTSVPYRQRITFPRVLRTSNRFLQSLELYSDAVMQYEDELLLATGRSLIPVDDLTSKASEKMMAMQDLIASGECSEKEPCIRDLLLVELTNWFNTQFFEWVNNIQCQVCGSEESKLRRTQTEGDVRVEVNVCCGQESKFYRYNDISQLLVSRKGRCGEYANCFTFLCRCLDYDARLVHSHFDHVWTEVFSETQMRWLHVDPSDNVVDSPLMYQHGWKRGIDYVFAYSRDDAQDVTWRYTNNHQEILKLRKLCDEKELIQTLNAIREKRQQNCSAERKNFLSQRNMFEVIGLTLERKPTENELKGRSSGSLSWRQSRGEHTFTNIFVFSPNEAELKKCQLNLRYSCATDTYERYTKDDGQITLLNTYKTWQSAQFSSKNIYRKVERDWKMAYLARLEDTDCAEIIWKFDLTKTNLKVKSYKLVFETKTFGEGKIDVSVQTNDGKTFIENSSEFQVVAKLMGGKGDVAWQHTQLFRQSLNSREYPFDLQVELH", "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": "MANSSLLRVVLVALLLLGSVTVSAGDGRGTPIAFQAEVSKMLDILVNSLYTNRAVFLRELISNGSDALDKIRVLYLTSPKEPLTKDGEAPTMDLRISFDKEKSELILRDGGVGMTKEELAKHLGSLGTSGTKHFLEKLQEGVGAGGGDQNNLIGQFGVGFYSVFLVGDRVRVASKSDDSDEQYVWESKGDGQYFLYPDPRGNTLGRGTEITIELKPDAEQFLSAETIKKTIHQYSEFINFPIYVQEEVEVASTAATPEPAAEEGSLDEGAVEEDPDKEGDTQGVVKERRWTLVNENRPIWTRPIGNVTEEEYHTFYKAFSGDYRDPLYFNHFKVEGEVDFDSILFVPTTVDPASFSDDNSVPNTNIKLYVRRVFITDEFRDLLPRYLNFVKGIVDSNDLPLNVSREVLQESRILRVIKKKLVRKTLSMFADIAAQDEAIANGKQVESPAPSGHTHLKKPAYTKFWELYGKHLRLGVMLDSNNRNRLTKLFRYKSSRSESEYISLQTYVDRMKKGQKGIYYLSGDSVARIKKSPVLEDAVNHDVEVIFMTDAIDEYVVSQLTDFAGKKLINLAKEGVQLEESDARQRVADRKRKEKYDSFFTHLRALFGYSEVRKVILTKRMTNEAFLVSSGENQITARLASIMRGQSMSLANQQMTAERVLEVNYRHPLVDEMFKRFTVDEDDEVATDIAWVLYDTANLQAEFPVADVAAYSKRINRLLRSSVDLSADDSLLPPDDAEYTVSDTEAEEEEEQPKVDANADEEAEAVGEDDL", "text": "FUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). Required for the synthesis of lipophosphoglycan (LPG), a cell surface glycoconjugate (By similarity). Necessary for the attachment of the galactosyl residue to the mannose within the phosphoglycan repeats of the nascent LPG chain (By similarity). Also required for addition of phosphoglycan to acid phosphatase (By similarity). Not required for normal growth (By similarity). Has ATPase activity (PubMed:29568220). Binds heparin with micromolar affinity which may facilitate infection of host cells (PubMed:29568220). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the heat shock protein 90 family."}
+{"protein": "MGCLGNQLLIAILLLSVYGIYCIQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNDDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDKWGLTKSSTTTASTTTTTTAKSVETRDIVNETSPCVVHDNCTGLEQEPMISCKFNMTGLKRDKKKEYNETWYSADLVCEQGNSTGNESRCYMNHCNTSVIQECCDKDYWDAIRCRYCAPPGYALLRCNDTNYSGFMPNCSKVVVSSCTRMMETQTSTWFRFNGTRAENRTYIYWHGRDNRTIISLNKHYNLTMKCRRPGNKTVLPVTIMSALVFHSQPVNERPKQAWCRFGGNWKEAIKEVKQTIVKHPRYTGTNNTDKINLTAPRGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRSLTTQKPKERHKRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANINWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTNVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASLTVTAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTRVSAIEKYLKDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNETWQEWERKVDFLEANITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLTSWIKYIQYGIYIIVGVILLRIVIYIVQMLARLRQGYRPVFSSPPSYFQXTHTQQDPALPTKEGKKGDGGGSGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPIFQRLSATLRRIREVLRLELTYLQYGWSYFQEAVQAAQRSATETLAGAWGELWEALQRGGRWILAIPRRIRQGLELTLL", "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": "MGVGTLLNGLLVSVVAALLWKYSKLSEHAALLEEELHMTRRSQELSQAHIDYHVALQALQEHGTRMVCTGKMHTDRICRFDYLCYCSEAEEFVFFHSNSSVMLPNLGSRRFQPALLDLSSVEDHNTQYFNFLELPAATLRFLPKPVFVPDVALILNRFNPDNLMHVFHDDLLPAFYTMKQFLDLDEDARLVFMEGWDEGPHFHLYRLLSDKQPLLKEQLRNFGKLMCFTKSYIGLSKMTTWYQYGFVQPQGPKANILVSGNEIRHFAKVLMEKMNVTRAEGGQEDEYIVVFSRSSTRLILNQAELVMALAQEFQMRVVTVSLEEQSFASIVQVIGAASMLVSMHGAQLITALFLPPGAVVVELFPFAVNPDQYTPYRTLAALPGMDLHYISWRNTEEENTITHPDRPWEQGGIAHLEKEEQERIVASKDVPRHLCCRNPEWLFRIYQDTFVDIPSFLEALQAGLKAKPVWKKSKLSGGLHPGRVRDARCQTSVQTSSEAKLTVSWQMPWNLKYLKVREVKYEVWIQEQGENTYMPYILPQQNYTFSDNIKPFTTYLVWVRCIFNKNLLGPFADVLMCRT", "text": "FUNCTION: O-linked mannose beta-1,4-N-acetylglucosaminyltransferase that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D- mannosylprotein. Involved in the biosynthesis of the phosphorylated O- mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N- acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 61 family."}
+{"protein": "MPNLKRLPIPPLQDTLNRYLARVEPLQDERQNRRTRRTVLSAENLDALNTLHERLLEYDARLAESNPESSYIEQFWYDAYLLYDATVVLNVNPYFQLQDDPTIKDTPETAAQGPYGAHTVQVRRAARLTTSILKFIRQIRHGTLRTDTVRGKTPLSMDQYERLFGSSRIPPGPGEPSCHLQTDATSHHVVAMYRGQFYWFDVLDTRNEPIFATPEQLEWNLYSIIMDAESAGSGSAPFGVFTTESRRVWSNIRDYLFHADDCTNWRNLKLIDSALFVVCLDDVAFAADQQDELTRSMLCGTSTINLDPHQHQPPLNVQTGTCLNRWYDKLQLIVTKNGKAGINFEHTGVDGHTVLRLATDIYTDSILSFARGVTKNVVDIFSDDDGKPSSSSLASAAHSANLITIPRKLEWRTDNFLQSSLHFAETRISDLISQYEFVNLDFSNYGASHIKTVFKCSPDAFVQQVFQVAYFALYGRFETVYEPAMTKAFQNGRTEAIRSVTGQSKLFVKSLLDQDASDATKIQLLHDACTAHSQITRECSQGLGQDRHLYALYCLWNQWYKDKLELPPIFRDKSWTTMQNNVLSTSNCGNPCLKSFGFGPVTANGFGIGYIIRDHSVSVVVSSRHRQTARFASLMEKSLLEIDRIFKRQQARAAKPAARTTASANTKSEDMKYLLSGYDYFDVSVSG", "text": "FUNCTION: Involved in the transfer of acetyl-CoA into mitochondria. May also be involved in the metabolism of acetate and of ethanol. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the carnitine/choline acetyltransferase family."}
+{"protein": "MADDVIDWLPYVDTLDQRYLNEVEKTVTAELAAIEQQELHPRIAELFPAVRHHWDEQYGLYKDNVVGLEGSNKRAAEDGVLSELKRRCPGIDISVYNDDSEDPVLLATIAGYRYHQDLVVTQLLPQTLENQWAINNAYLEGAEAAVRRQLQEQEQQIAQLDRHRQELQQREALRFRYLERQWRDRLHGNLERAAGNI", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAGSGGLGGGAGGGQGAGAGQGAALRASRAPMLLVALVLGAYCLCALPGRCPPAARAPAPAPAPSEPSSSVHRPGAPGLPLASGPGRRRFPQALIVGVKKGGTRALLEFLRLHPDVRALGSEPHFFDRCYERGLAWYRSLMPRTLDGQITMEKTPSYFVTREAPRRIHAMSPDTKLIVVVRNPVTRAISDYAQTLSKTPGLPSFRALAFRHGLGPVDTAWSAVRIGLYAQHLDHWLRYFPLSHFLFVSGERLVSDPAGEVGRVQDFLGLKRVVTDKHFYFNATKGFPCLKKAQGGSRPRCLGKSKGRPHPRVPQALVRRLQEFYRPFNRRFYQMTGQDFGWG", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to heparan sulfate. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes Simplex Virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non- anticoagulant heparan sulfate to anticoagulant heparan sulfate. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family."}
+{"protein": "MVRTKNQSSSSSASSSSTKSPIKSSSATGSSGGGVGGRQSTHRSSSASNVAAVVAGGSSAAGGGSSSNRRSPGSSPDGDDDTTTTDDLTPTTCSPRSGHHHTYGGYSSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSSKEQQQSLNHPSELNRDSDGQEQQLSNQPQRFRPIQPLEMAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREQDLQMQRLSLKEKQNEQAPSKPQRTREPMLAGMTNEPMKLRVRSSGYGPKATTGAQPTASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI", "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": "MATVAGDDGGGGGEFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKKDTMIRKEVFVSPSVLREATRIIHESEIMKEDDSNWPEPDRVGRQELEIVMGNEHISFTTSKIGSLVDVQTSKDPEGLRIFYYLVQDLKCFVFSLINLHFKIKPIQS", "text": "FUNCTION: 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). The MAGO-Y14 heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading to EJC disassembly in the cytoplasm (By similarity). EJC core heterodimers play essential roles in plant growth and development, and pollen and seed development (PubMed:25230811, PubMed:24820023). The MAGO-Y14 heterodimer selectively binds to the UDT1 (UNDEVELOPED TAPETUM 1) pre-mRNA transcript and regulates the splicing of UDT1, a key regulator in stamen development (PubMed:24820023). 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 mago nashi family."}
+{"protein": "MEKLTILLHVAAVLMSTQALIQEQRQKAKINLFSKRKPSAERWWGDNGCSLWGSCTVDAECCLGNCGGMYCSLLR", "text": "FUNCTION: Inhibits voltage-gated ion channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O2 superfamily."}
+{"protein": "MVQTNLEVVDDTLHLPRILCLHGGGSNAAIFQAQCRRLIAQLRSEFRFVFAQAPFLSDAEPNVMSVYSQWGPFRRWLRWCPDHPEIRPEDAIRAIDDCLEDVKRQDDAKGATGAWVGLLGFSQGAKMCASLLYRQQIRQELRGRSFAGSDYRFGVLLAGRAPLVSLDPDLDLNSSLPDVSQITDAKYHGPSQDVLRIPTVHVHGMRDPHVDLHRQLFEEFCAPESRRLVEWDGDHRVPLKYNDVSLVAYQIRELATQTGAP", "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, PubMed:29189834). 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, PubMed:29189834). 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). SIMILARITY: Belongs to the LovG family."}
+{"protein": "MSMMCGGISAPLDADEDIQKMCDNVKPHAEEKAGKKYDVFTAKTYTTQIVSGTNYFIKIHVGGDDHVHLRVYKKLPCHGGGLELSGMQHSKSLQDPIAYF", "text": "FUNCTION: Thiol protease inhibitor. Has papain inhibitory activity in vitro. May be involved in immune responses against invading Gram- negative bacteria. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cystatin family."}
+{"protein": "MRGCGVDRTGGYVRLALAAPAVRVADCAYNTQRMIQTVRRAASCGVDILLFPRLSLTGCSCASLFAQDTLLSAVCTHVSALCAGTADCQLLALVSVPCFLRTQVRVCTALVARGRVLALVVQDTLAACGAQKMQVPCEVLYGGAPVPVYDVQTCFESAEGLFSFCVGAMDGSVPATLVLQAYGTPSTAQTPDIFAAHAAAYSAQHQCAYAYVNAGWGESSADAVYGAESGIFECGQCVVQDSLQEMRERGERPAHAVRGLHVSADVDVSLVHFRRRARSGHTTLGASAPCVTLPAGIFAASKAHATLRRPRVPCPFFPPAFQKSQDAVPPLTGAVCLAVSAPSDTQDGFLQRTIDLAAQGVALRLEHMGCRRLVVGVSGGVDSACALLICARALDFLSIARTQLYALTLPGFGTTSGTKGAAQEFARALGCTVQEISISAAVTHHLHDIGHTMQQCDGTYENAQARERTQILLDRANQLDALMIGTGDASEGALGWETFGGDHLSLYAVNASLPKTVVRALISYAGRVPERFVCETDSPYAPRGAAFSRVCAAIVAQPVSPELIPPCDDRIVQCTEEMLGPYELHDFFLYHITVNGFGPRKLFRVAAHAFGXAYSCAQLCAALRVFFTRLFSQQFKRSCVPDGPGLTEVNLSPRVGFYFPSDTSGALWRAELEQLACGE", "text": "FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. SIMILARITY: In the C-terminal section; belongs to the NAD synthetase family."}
+{"protein": "MSELISVVVPIYNTGKYLVECVEHILKQTYQNIEIILVDDGSTDNSGEICDAFMMQDNRVRVLHQENKGGAAQAKNMGISVAKGEYITIVDSDDIVKENMIETLYQQVQEKDADVVIGNYYNYDESDGNFYFYVTGQDFCVEELAIQEIMNRQAGDWKFNSSAFILPTFKLIKKELFNEVHFSNGRRFDDEATMHRFYLLASKIVFINDNLYLYRRRSGSIMRTEFDLSWARDIVEVFSKKISDCVLAGLDVSVLRIRFVNLLKDYKQTLEYHQLTDTEEYKDICFRLKLFFDAEQRNGKS", "text": "FUNCTION: Also catalyzes the fourth step in glycosylation of the serine-rich repeat protein PsrP in this bacteria. Can transfer the sugar from UDP-glucose (and much less well from UDP-galactose) to the terminal sugar moiety of PsrP-GlcNAc-Glc-Gal or of PsrP-GlcNAc-Glc-Glc. FUNCTION: Involved in the polymorphic O-glycosylation of the serine- rich repeat protein PsrP. Catalyzes the third step in glycosylation PsrP in this bacteria. Transfers glucose from UDP-glucose to the terminal glucose moiety of already-glycosylated PsrP (using truncated substrates with PsrP SSR1-GlcNAc-Glc). Has a marked preference for PsrP substrate that has already been modified by GlcNAc and glucose. In vitro has hydrolytic activity against UDP-glucose and to a lesser extent against UDP-galactose. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
+{"protein": "MEFSPLLQRATLIQRYKRFLADVITPDGRELTLHCPNTGAMTGCATRGDTVWYSTSDNTKRKYPHTWELTQSQSGAFICVNTLWANRLTKEAILNESISELSGYSSLKSEVKYGAERSRIDFMLQADSRPDCYIEVKSVTLAENEQGYFPDAVTERGQKHLRELMNVAAEGQRAVIFFAVLHSAITRFSPARHIDEKYAQLLSEAQQRGVEILAYKAEISAEGMALKKSLPVTL", "text": "FUNCTION: Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism. SIMILARITY: Belongs to the SfsA family."}
+{"protein": "MSENGDCENQTSSGFPSIEQMLASSPGKTPISLLQEYGTRVGKTPVYDLLKAEGQAHQPNFTFRVSVGDINCTGQGPSKKAAKHKAAEVALSLLKGGDMFGMMCEENSVMLSVEQPVELREVADVSPPPTNRNHTIEMKPPLSAQQSECNPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFLEIGSGTSKKLAKRNAAAKMLLQIHRVPAEHRESGETEPEEDQFSMGKLDGSRGRGTACTWDSLRNSSGEKILHLRSNPLTILSSGFCSLLQDLSEEQSFQISYLDIDEPSLSGLYQCLVELSTQPTTVCHGSATTRDAARANAAHNALQYLKIMAGGK", "text": "FUNCTION: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of dicer1, ago2 and tarbp2. Within the RLC/miRLC, dicer1 and tarbp2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto ago2. ago2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from dicer1 and tarbp2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by dicer1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TARBP2 family."}
+{"protein": "MRPTATWIWHVSDAWLRRTRDFGVIRLEDFCFQFNYSQPRVGYCRVPLKAWCSNQGKFAAQFTLKSCEKPGHEKFITSFTAYGRTVQQAVSKLVEEAVDFILFRATQLERNV", "text": "SIMILARITY: Belongs to the coronaviruses 12.7 kDa protein family."}
+{"protein": "MPSKTKYNLVDDGHDLRIPLHNEDAFQHGISFEAKYVGSLDVPRPNSRVEIVAAMRRIRYEFKAKNIKKKKVSIMVSVDGVKVILKKKKKKKEWTWDESKMLVMQDPIYRIFYVSHDSQDLKIFSYIARDGASNIFRCNVFKSKKKSQAMRIVRTVGQAFEVCHKLSLQHTQQNADGQEDGESERNSDGSGDPGRQLTGAERVSTATAEETDIDAVEVPLPGNDILEFSRGVTDLDAIGKDGGSHIDTTVSPHPQEPMLAASPRMLLPSSSSSKPPGLGTGTPLSTHHQMQLLQQLLQQQQQQTQVAVAQVHLLKDQLAAEAAARLEAQARVHQLLLQNKDMLQHISLLVKQVQELELKLSGQSTMGSQDSLLEITFRSGALPVLCESTTPKPEDLHSPLLGAGLADFAHPVGSPLGRRDCLVKLECFRFLPAEDNQPMAQGEPLLGGLELIKFRESGIASEYESNTDESEERDSWSQEELPRLLNVLQRQELGDSLDDEIAV", "text": "FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4. In kidney podocytes, plays a role in podosomes and filopodia formation through CDC42 activation (PubMed:33523862). SUBCELLULAR LOCATION: Cell projection, filopodium Cell projection, podosome."}
+{"protein": "MAFSVSSLMALVVISSSPVSSMSCDLPASLDLRKQETLRVLHQMETISPPSCLKHRTDFRFPQEQLDGRQFPEAQATSVLQEMLQQIVSLFHTERSSAAWNTTLLDRLLAGLHQQLEDLNTCLDEQTGEEESALGTVGPTLAVKRYFRRIRLYLTEKKYSDCAWEIVRVDIMRSFSSSANLQGRLGMKDGDLGSP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha/beta interferon family."}
+{"protein": "MASSGSVQQLPLVLLMLLLASAARARLYFRSGQTCYHPIRGDQLALLGRRTYPRPHEYLSPADLPKNWDWRNVNGVNYASVTRNQHIPQYCGSCWAHGSTSAMADRINIKRKGAWPSILLSVQNVIDCGNAGSCEGGNDLPVWEYAHKHGIPDETCNNYQAKDQDCDKFNQCGTCTEFKECHTIQNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATEMMSNYTGGIYAEHQDQAVINHIISVAGWGVSNDGIEYWIVRNSWGEPWGEKGWMRIVTSTYKGGTGDSYNLAIESACTFGDPIV", "text": "FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Capable of producing kinin potentiating peptides (By similarity). SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MTSPVPSEPVSEDTHDSSSGSEVEPSKTSTRAPKRRRLSESSDDSDDSYVAPAPLPTLSRIKKKGAPDAKPAAPAGQDNPVLIRDALEIGLREEASSFAALNVAPWLVGSLTTMAVRKPTAIQKACIPEILKGRDCIGGSRTGSGKTIAFSVPMLQKWAEDPFGIFGVVLTPTRELALQIFEQIKAISAPQSMKPVLITGGTDMRPQAIALAGRPHVVIATPGRLADHIKSSGEDTVCGLKRVRMVVLDEADRLLASGPGSMLPDVETCLSALPPSSERQTLLFTATVTPEVRALKNMPRSANKPPVFVTEISTENQGTIPPTLKQTYLKVPLTHREAFLHVLLSTEGNASKPAIVFCNHTKTADLLERMLRRLSHRVTSLHSLLPQSERNANLARFRASAARILVATDVASRGLDIPTVSLVINYDVPRNPDDYVHRVGRTARAGRRGEAVTLVGQRDVQLVLAIEERVGRQMEEWSEEGVSIEGRLVRTGALKEVGEAKREAMVEIDEGRDVLGRKRNKLKKVR", "text": "FUNCTION: ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX49/DBP8 subfamily."}
+{"protein": "MELLCCEVDPVRRAVPDANLLHDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAINYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQPNEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEDVSSLTGDALVDLLARITNTDVDCLKACQEQIEVVLLNSLQQYRQDQDGSKSEDELDQASTPTDVRDIDL", "text": "FUNCTION: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex 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. SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus membrane Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily."}
+{"protein": "MHPRYSPAPPPQQQQQMGGPLHQQQGGGGGGGGGIRGPSNAQQLPPQIPRSQNYSNGSSSSAAAAPPTSRSAFPGAPLTASAVALKGALPQRPPAMTSPAAAAAGAALAAGAPYRGAASWTPQGYAPAAAAAAAAVAQQAAYRYTAPLPQPAYAAYTPHTATTPATTTYGQRVPTAASPSNTNSSSSSNTGSQSGTLSTSLSNTTNTNTNMGPNGTVQNQNQQGGEQLSKTNLYIRGLQQGTTDKDLVNMCAQYGTIISTKAILDKTTNKCKGYGFVDFEQPAFAECAVKGLQGKGVQAQMAKQQEQDPTNLYIANLPPHFKETDLEAMLSKYGQVVSTRILRDQQMNSKGVGFARMESREKCEQIIQMFNGNTIPGAKDPLLVKFADGGPKKKNLFKTPDPNARAWRDVSAEGIPVAYDPTMQQNGVSVNVGTPIGVPYSRFSAPQVGGYPVAGSQWIPGYMMTQPITQVDDQTSYSPQYMQMAAAPQLGVTSYKPEAVNQVQPRGISMMVSGDTGVPYGTMMPQLATLQIGNSYISPTYPYYAPPPTIIPTMPMTDSEQASTAASPDEAYTQYPHQAAPK", "text": "FUNCTION: Has a role in the perception of gravity."}
+{"protein": "MQSVVCLIGAFIAAAVFRPGSCVGTVIGLYGETIVVPCNDGTKKPDGLIFTKWKYVKDDGSPGDLLVKQAQKDEATVSATDGYKSRVSIAANSSLLIARGSLADQRVFTCMVVSFTNLEEYSVEVKVHKKPSAPVIKNNAKELENGKLTQLGECVVENANPPADLIWKKNNQTLVDDGKTIIITSTITKDKITGLSSTSSRLQYTARKEDVESQFTCTAKHVMGPDQVSEPESFPIHYPTEKVSLQVVSQSPIREGEDVTLKCQADGNPPPTSFNFNIKGKKVTVTDKDVYTLTGVTRADSGIYKCSLLDNDVMESTQFVTVSFLDVSLTPTGKVLKNVGENLIVSLDKNASSEAKVTWTKDNRKLDKLPDFSKLTYSDAGLYVCDVSIEGIKRSLSFELTVEGIPKITSLTKHRSSDGKHKVLTCEAEGSPKPDVQWSVNGTNDEVSYNNGKATYKLTVVPSKNLTVSCLVTNKLGEDTKEISVFSQKNEDGTEQAKVIVGIVVGLLVAAALVGLIYWIYIKKTRQGSWKTGEKEAGTSEESKKLEENNHKPDV", "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": "MSAKIILVFCAQALFVQSALSQCTSRATVAADRGIIGGYGLGAPYGLAYGLEAPLGLGYGLGAPCGLGGPAIDITPTIGGGLPVSSASAIAPVGLAVASENVYEGILAAAGELPFVGTVGVEGVLPTAGAGAVHHSCGNGINAMASRDAAFAPGYAGAYGIGLGAYGLGVPALEVPALGYRAGWRGCGCGL", "text": "FUNCTION: This protein is one of many from the eggshell of the gypsy moth. SIMILARITY: Belongs to the chorion protein family."}
+{"protein": "MSAAAYMDFVAAQCLVSISNRAAVPEHGGAPDAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKYRPIQTPSVCSDSLESPDEDIGSDSDVTTESGSSPSHSPEERQDSGSAPSPLSLLHSGVASKGKHASEKRHKCPYSGCGKVYGKSSHLKAHYRVHTGERPFPCTWPDCLKKFSRSDELTRHYRTHTGEKQFRCPLCEKRFMRSDHLTKHARRHTDFHPSMIKRSKKALASPL", "text": "FUNCTION: Transcription factor that binds to GC box promoter elements. Selectively activates mRNA synthesis from genes containing tandem repeats of GC boxes but represses genes with a single GC box. Acts as an epidermal circadian transcription factor regulating keratinocyte proliferation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family."}
+{"protein": "MEECPICLADDQEGEQFGCLNVCGHKFHLNCIREWHKYSINLKCPICRVESTHLEVGEGQHALSINLKMGFMIKNAIDYVGAETTNERNEDDTGEQDQEIEFLSERLRGTLVMDTIKIIQCSICGDTDVSRLSLYCQDCEAIYHETCLRGLACEVGDRNTWQECTDCRSNALLELRMGAISSQLASYDSRNSMIFAGELRDKHSVKTQQMYEQIRNAKHKIQMHVRRALDRYPLPLLRFKDAYKHVNKQVSRKLYRLSDNKYLPDQYDYDSLARTGVHTELLIYCHDE", "text": "FUNCTION: Required for tolerance to alcohol. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. Accumulates in the nucleus specifically upon alcohol stress. Shuttles between the nucleus and the cytoplasm in a XPO1-dependent manner."}
+{"protein": "MAYHSFLVEPISCHAWNKDRTQIAICPNNHEVHIYEKSGAKWNKVHELKEHNGQVTGIDWAPESNRIVTCGTDRNAYVWTLKGRTWKPTLVILRINRAARCVRWAPNENKFAVGSGSRVISICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRIFSAYIKEVEERPAPTPWGSKMPFGELMFESSSSCGWVHGVCFSAGGSRVAWVSHDSTVCLVDAEKKMAVATLASETLPLLAITFITENSLVAAGHDCFPVLFTYDNAAGTLSFGGRLDVPKQNSQRGLTARERFQNLDKKASSEGGAATGAGLDSLHKNSVSQISVLSGGKAKCSQFCTTGMDGGMSIWDVKSLESALKDLKIR", "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": "MTTLMGSYSWTESLDCSPMDGDLSDGLSPHRSPREKGSETRIRRPMNAFMVWAKDERKRLAVQNPDLHNAELSKMLGKSWKALSPAQKRPYVEEAERLRVQHMQDYPNYKYRPRRKKQIKRICKRVDTGFLLGSLSKDQNSVPDTRGCRTAMEKEENGGYPGAALSDIRHYRETPSNGNKYDQTYPYGLPTPPEMSPLEAIDQDQSFYSTSCSEDCHSHINGAVYPPEYSRSPILCSHLSQVPIPQPGSSMIPPVPTCPPAYYSSSYHSIHNYHAHLGQLSPPPEHPHYDTIDQISQAELLGEMDRNEFDQYLNTSLQDPTEMTIHGHVQVSQASDIQPSETSLISVLADATATYYNSYSVS", "text": "FUNCTION: Transcription factor. Binds to the DNA sequence 5'-AACAAT-3'. Acts downstream of vegt and upstream of nodal signaling to promote endodermal and mesodermal differentiation by promoting vegt-induced expression of both endodermal genes (including endodermin) and mesodermal genes (including snai1/snail and snai2/slug). Induces expression of multiple nodal genes (including nodal, nodal2, nodal4, nodal5 and nodal6) and binds directly to sites within the promoter of the nodal5 gene. The endodermal and mesodermal specification pathways then interact to initiate cardiogenesis. Acts partially redundantly with sox18 during cardiogenesis. Also acts as an antagonist of beta- catenin signaling. Regulates (possibly indirectly) development of the pronephros, the functional larval kidney. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "RKLKTGTASVAVALTVVGAGLASQTEVKANRADDARNEVLRGNLVRAELWYRQIQENDQLKLENKGLKTDLREKEEELQGLKDDVEKLTADAELQRLKNERHEEAELERLKSERHDHDKKEAERKALEDKLADKQEHLNGALRYINEKEAEAKEKEAEQKKLKEEKQISDASRQGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKGLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSKLAALEKLNKELEESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAEKASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTGETT", "text": "FUNCTION: Binds to human plasminogen (and plasmin) via its kringle repeats. Also binds to albumin, immunoglobulin G and fibrinogen. Could provide the bacteria with a mechanism for invasion, as streptococcal- bound plasmin could permit tissue penetration. SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. SIMILARITY: Belongs to the M protein family."}
+{"protein": "MSLLDAHIPQLIASEANFGAKAALMRSTIAQAEQAAMSSQAFHMGEASAAFQAAHARFVEVSAKVNALLDIAQLNIGDAASSYVAQDAAAASTYTGI", "text": "SUBCELLULAR LOCATION: Secreted Note=Secreted via the ESX-3 / type VII secretion system (T7SS). SIMILARITY: Belongs to the WXG100 family. CFP-10 subfamily."}
+{"protein": "EEEDKKEDVGTVVGI", "text": "FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Melanosome Cytoplasm Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epithelial cells; high levels of free iron promotes cell surface localization (By similarity). SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MLRQLKLTLNISRWIFMPWQRQASASSSQVPPFLAPISDDVIVDYEDPDYLPLPEYPVRPNEPLETRKQRLLYQSRKRGMLENDLLLSTFAAKYLKDFSAEQTAIYDQLINGVSNDWDIYYWATEVKPTPEEYNTEIMKLLKEHVKNAERVTRFRQPDLT", "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": "SIYERCELARELINR", "text": "FUNCTION: Lysozymes have primarily a bacteriolytic function. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 22 family."}
+{"protein": "MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI", "text": "FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638). Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense- mediated decay (NMD) pathway (PubMed:23917022). 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). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. FUNCTION: Required for pre-mRNA splicing as component of the spliceosome. Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense-mediated decay (NMD) pathway. 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). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. 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. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Detected in granule-like structures in the dendroplasm (By similarity). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (PubMed:19324961). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Detected in granule-like structures in the dendroplasm (PubMed:16275927). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Detected in granule-like structures in the dendroplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles. SIMILARITY: Belongs to the mago nashi family."}
+{"protein": "MTSGSVFFYILIIGKYFSHGGGQDVKCSLGYFPCGNITKCLPQLLHCNGVDDCGNQADEDNCGDNNGWSLQFDKYFASYYKMTSQYPFEAETPECLVGSVPVQCLCRGLELDCDETNLRAVPSVSSNVTAMSLQWNLIRKLPPDCFKNYHDLQKLYLQNNKITSISIYAFRGLNSLTKLYLSHNRITFLKPGVFEDLHRLEWLIIEDNHLSRISPPTFYGLNSLILLVLMNNVLTRLPDKPLCQHMPRLHWLDLEGNHIHNLRNLTLISCSNLTVLVMGKNKINHLNENTFAPLQKLDELDLGSNKIENLPPLIFKDLKELSQLNLSYNPIQKIQANQFDYLVKLKSLSLEGIEISNIQQRMFRPLMNLSHIYFKKFQYCGYAPHVRSGKPNTDGISSLENLLASIIQRVFVWVVSAVTCFGNVFVICMRPYIRSENKLYAMSIISLCCADCLMGIYLFVIGGFDLKFRGEYNKHAQLWMESTHCQLVGSLAILSTEVSVLLLTFLTLEKYICIVYPFRCVRPGKCRTITVLILIWITGFIVAFIPLSNKEFFKNYYGTNGVCFPLHSEDTESIGAQVYSVAIFLGINLAAFIIIVFSYGSMFYSVHQSAITATEIRNQVKKEMILAKRFFFIVFTDALCWIPIFVVKFLSLLQVEIPGTITSWVVIFILPINSALNPILYTLTTRPFKEMIHRFWYNYRQRKSMDSKGQKTYAPSFIWVEMWPLQEMPPELMKPGLFTYPCEMSLISQSTRLNSYS", "text": "FUNCTION: Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MSLTQQQKDLIFGSLLGDGNLQTGSVGRTWRYRALHKSEHQTYLFHKYEILKPLCGENTLPTESIVFDERTNKEVKRWFFNTLTNPSLKFFADMFYTYDQNTQKWVKDVPVKVQTFLTPQALAYFYIDDGALKWLNKSNAMQICTESFSQGGTIRIQKALKTLYNIDTTLTKKTLQDGRIGYRIAIPEASSGAFREVIKPFLVDCMRYKVSDGNKGHL", "text": "FUNCTION: Probable endonuclease involved in intron homing. Encoded in the group-I intron of the subunit rRNA-encoding gene (rrnL), it generates a staggered cut with 4-nt (CTCG) 3'-OH overhangs 2 bp downstream from the intron insertion site. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the LAGLIDADG endonuclease family."}
+{"protein": "MKKVFGQTVRDLKREVNKKVLKVPGVEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRERAYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERIAEVRQKAAANRDKYRSSAPGGMYKPSGGYGDKYDYGSRDEERSSYGREREYGYRDDDRNSRDGDRHSRDSEDRYGRDGNRDDDYRGRSRSVDNYGSRGRSSEREREDDGHSSSRGSGARADDNSQDGRGGLQRKFSEQNIGAPPSYEEAVSDSRSPVYSERDGGETPQVTAPGAASPPPPQVAAPEAASPPTGTNTANTTATFVNESPSQKVETFDEFDPRSAFSAGPPAYASTDGVTAPPTVTSMSAPTTSNSVEMDLLGSLADVFSSNALAIVPADSIYVETNGQANAGPAPSFSTSQPSTQSFDDPFGDSPFKAFTSTDTDSTPQQNFGASFQPPPPAFTSEVSHPDTAHNFGFGDSFSAVANPDPASQNVQPPSNSPGFPQEQFATSQSGIDILAGILPPSGPPVQSGPSIPTSQFPPSGNNMYEGFHSQPPVSTAPNLPGQTPFGQAVQPYNMVPHSQNMTGAMPFNSGGFMHQPGSQTPYSTPSGPAGQFMAHQGHGMPPSHGPQRTQSGPVTLQGNNNVMGDMFSQATPNSLTSSSSHPDLTPLTGAIEIVPPPQKKFEPKSSVWADTLSRGLVNFNISGSKTNPLADIGVDFEAINRREKRLEKQTNTPATSTINMGKAMGSGTGLGRSGATAMRPPPNPMTGSGMPMGGGMGVGSYGGMNQNQPMGMGMGAGMNQNQPMGMGMGPGMNMNMNMGGYGQGYPMQPQNPGMVPSPNMPGNNYNPMMGQGGYNPQQSYGGGYR", "text": "FUNCTION: May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity). Binds to membranes enriched in phosphatidylinositol 3- phosphate (PtdIns(3)P). Plays an important role in protein trafficking. SUBCELLULAR LOCATION: Golgi apparatus Cytoplasmic vesicle, clathrin-coated vesicle Note=Localizes also to a novel cellular compartment, the 'delta compartment', characterized by colocalization of EPSIN2 and DELTA-ADR. SIMILARITY: Belongs to the epsin family."}
+{"protein": "MTRTSPTLPVIILGAGMVGLTLAQALKKAGIPYEVYERDSAADTEKGRGWALTVHWALNALEECLPAELFNRLEEIQVDPTLDDSRRFCFLDLSTAIPKYVIPPSKRLRVNRRLLGNLLGEGLDINYNKTLSSFHVSPETPDSVTVTFTDGTSTTGCLLVGTDGRNSKTRRLLLGEEAGALNPLPVRSIGTTITMTPEQFAPIREIDPLLFQGSHPETGVYMWFSLVSSPTINGSKDTPNPFYEGQLIQSWLYKSEKDAVPETDADRLALFKNNAQHFQRRLREAIETLPEDSKVLHIKLVDWVPVDWDNRGGRVTLAGDAAHAMTSYRGEAFNHGVADAAMLSRNIIAAWTNPGMTGGIADAPDSPIVSKRAKIAREARDARARAKLSEIAV", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6- (2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:22510154, PubMed:23001671). The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl- CoA units and one methylation step (PubMed:22510154). The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA (PubMed:23001671). The roles of dbaB, C, E and F have still to be determined (Probable). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
+{"protein": "MAVRALKLLTTLLAVVAAASQAEVESEAGWGMVTPDLLFAEGTAAYARGDWPGVVLSMERALRSRAALRALRLRCRTQCAADFPWELDPDWSPSPAQASGAAALRDLSFFGGLLRRAACLRRCLGPPAAHSLSEEMELEFRKRSPYNYLQVAYFKINKLEKAVAAAHTFFVGNPEHMEMQQNLDYYQTMSGVKEADFKDLETQPHMQEFRLGVRLYSEEQPQEAVPHLEAALQEYFVAYEECRALCEGPYDYDGYNYLEYNADLFQAITDHYIQVLNCKQNCVTELASHPSREKPFEDFLPSHYNYLQFAYYNIGNYTQAVECAKTYLLFFPNDEVMNQNLAYYAAMLGEEHTRSIGPRESAKEYRQRSLLEKELLFFAYDVFGIPFVDPDSWTPEEVIPKRLQEKQKSERETAVRISQEIGNLMKEIETLVEEKTKESLDVSRLTREGGPLLYEGISLTMNSKLLNGSQRVVMDGVISDHECQELQRLTNVAATSGDGYRGQTSPHTPNEKFYGVTVFKALKLGQEGKVPLQSAHLYYNVTEKVRRIMESYFRLDTPLYFSYSHLVCRTAIEEVQAERKDDSHPVHVDNCILNAETLVCVKEPPAYTFRDYSAILYLNGDFDGGNFYFTELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKAVTRGQRCAIALWFTLDPRHSERDRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEPAQESLSGSESKPKDEL", "text": "FUNCTION: Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Note=Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG). SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum. SIMILARITY: Belongs to the leprecan family."}
+{"protein": "MSSSGAKDKPELQFPFLQDEETVATLQECKTLFILRGLPGSGKSTLARFIVDKYRDGTKMVSADSYKITPGARGSFSEEYKQLDEDLAACCRRDFRVLVLDDTNHERERLEQLFELADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSAALWKTGQTFLEELGNHKAFKKELRHFVSGDEPREKIELVTYFGKRPPGVLHCTTKFCDYGKAAGAEEYAQQDVVKKSYCKAFTLTISALFVTPKTTGARVELSEQQLALWPNDVDKLSPSDNLPRGSRAHITLGCAGDVEAVQTGIDLLEIVRQEKGGSRGEEVGELSRGKLYSLGSGRWMLSLAKKMEVRAIFTGYYGKGKAVPIRSGRKGGSFQSCTII", "text": "FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'- cyclic substrates (PubMed:6272743). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Melanosome Note=Firmly bound to membrane structures of brain white matter. SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CNPase family."}
+{"protein": "MYEAIFDLEAITPLFMRGADARSPEFSSASVKGVMRWWFRALAGGYFGNNIEALKEVEEKIFGSTRNKSRVFVRAEVEDVKKGNIYRQASSWADKTIIVWSEYVDYFFFSVLDKRRNRKTKKIDIKTRFEYFDVGSKFSISLSSTDERYFRLAEASLWMTINLGGFGFRARRGAGSLKVQMLREMLL", "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), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation- dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'- 3' cyclic phosphate termini (PubMed:19945378). Cmr4 is probably the subunit that cleaves target RNA. Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CRISPR system Cmr1 family."}
+{"protein": "MTPMRITVWRERLQQMRPQRKLLKQTQQRRLLHQLQQRKLL", "text": "FUNCTION: Involved in viral RNA replication."}
+{"protein": "MADFLARDYRSQGEAAHEMLPTFLIGKILRERIVDSIYWKEQCFGLNACSLVDRAVRLEYIGGQYGNQRPTEFICLLYKLLQIAPEKEIIQQYLSIPEFKYLRALAAFYVRLTWDDVEVHQTLEPLLRDYRKLRIRTNSEIRLTYLDEVVDDLLNAEVVCDISLPPLRSRLQLEDLDLLEPLSSSSDEEDDDEEQISKLESNEGAVDRNI", "text": "FUNCTION: Required for pre-mRNA splicing and maintenance of stable U6 small nuclear RNA levels. Implicated in the formation of stable and biologically active snRNP structures. As part of the U4/U6.U5 tri-snRNP particle, dispensible for spliceosome assembly, but required for conformational changes, which result in U4 snRNA release and the subsequent catalytic activation of the spliceosome (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PRP38 family."}
+{"protein": "MDINYERPDPYYLLNKIDKEEKNKNRGKLKIFFGYAAGVGKTYAMLRAAHYMKELGKDIVIGYIEPHARMDTMSLTKGLPQIPVKNIDYKGVILREFDVDKALLRKPEIILVDELAHTNAKSQRNKKRWKDIEELLDAGIDVYTTLNVQHIESLNDIVANITHVSVRETIPDKVFDDADKVELIDIEPDELLKRFTDGKIYRKEQVKRAFNNFFTKNNLYALREIALRRTADRVNFEIEIARLSKGQITVMATSDQILACIGTSPSSARIIRTAARMAESYHSKWIALYVDTGRSLGKADKETLNANFNLVELLGGELVTVHGENVADQIIRYAELRNTTKIVIGKNHKRTGTLLHFYAKDVVDKLMDSNSYIDVYMIPNSSYYRDHKNSILSKISIQHKGSVKDVLKAIIIMAITTDIAELFSYMGFKDVNVIMIFILGVIIVYMATKGQIMGIISSIAAVLVFNYRFTEPKNSFIVYDKSYLVTFPIMMIVAFIIGSLTNKVQKEAQDSNMREKRTQTLYIVSGKLLSAVGTSEVVSIGIKYISRLVNRNVICYLADTSNKLSTPFVYKKDKGAKEEIIMSKDENAAAYWTFLNGKESGCGTSTFYRAKGYYIPIKIKNKVLGVIGVSCPSGPLRPQKKAVVDTVTGQIAIALDREILSKEQEKSKVEIERERLRSNLLRSISHDLRSPLAGIKGAASTILENGELIDEKRKQELINGIYEDTEWLIRLIENLLSMTKFDEGNTKIKKDVELVEEVVSEAVQRSSKYFKNHKIKVSVPEDVIMVSMDGSLIEQVIINLLDNASKFSPKGSTIEIKVYEKKKDVVFEIIDEGQGISEDILPNIFDRFFTNGSKISDSRRGVGLGLAICKSIVEAHGGKIEAVNKGSGGAIFKFNIPKEL", "text": "FUNCTION: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: In the central section; belongs to the universal stress protein A family."}
+{"protein": "GICSEPIVVGPCKAG", "text": "FUNCTION: This recombinant serine protease inhibitor inhibits both trypsin (Ki=2.4 nM) and chymotrypsin (Ki=23 nM) (PubMed:17447883). It may also inhibit the TRPV1 receptor, a receptor of the pain pathway (By similarity). In vivo, shows anti-histamine activity, since it dose- dependently weakens the clinical manifestation of the allergic reaction induced by histamine injection. In vivo, does not show toxicity to mice by intraperitoneal injection (PubMed:17447883). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily."}
+{"protein": "MSEFILEMRGITKQFPGVKALDNVNFKVREGEIHALCGENGAGKSTLMKVLSGVYPYGTYDGEIVFKGEVCKFKNIKQSEQLGIVIIHQELALIPYLSIAENIFLGNERAKKGIINWNETIAQTKKLLQKVGLEESPHTLVGQLGVGKQQLVEIAKALAKDVKLLILDEPTAALNEDDSENLLNLLLELKKQGLSAIIISHKLNEITKVADSITILRDGKTIETLDMKHDEVTEDRIIRGMVGRDLTNRYPARTPKIGEVIFEVKNWTVYHPIYSERKVLDHINLSIRRGEIVGIAGLMGAGRTELAMSIFGRSYGKKISGEIWKNGVKIDVSDVSKAIANGIAYVTEDRKGNGLILMEDIRKNITLSRLGKISNHFVVDENQEIVESERFRDQFKIKTPSVFQKVEALSGGNQQKVVLSKWIFAEPDILILDEPTRGIDVGAKYEIYTIIQQLADAGKGILMISSELPEILGMCDRIYVMSEGRITGEVSREEATQEKLMRLMTKTAIQEGA", "text": "FUNCTION: Part of the binding-protein-dependent transport system for L- arabinose. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MLLRNILHIPETHAHFLMPVLQSSGGHQVSMQNTILWNLFIQSIDKLLLYLMTCPQRALWGVTMVQLIAMIYKDQHVNTLQKLLNLWFEASLSESSEDNESNTSPPKKGSGDSSPMLTSDPTSDSSDNGSNGGGSSGKKEGCDERRQALREGTEATLQEVSRKGHDYQNAMARVTADKPDISEVASDSFEVPCSPQQHLNTEEAMDDIDYEEQVQEYEQEAAAVSSEPLNLSQPANNVNYTTNAVYASTTATETQTTSSLCAMTSLCYEPFKPPAPLPTRRNTLSEMLSDNYTSHSHVSAVKLGQKSSHAGQLQLTKGKCCPQKRECPSSQSELSDCGYATQVENPESISTSSNDDDGPQGKPQHQKPPCNTKPRNKQRTLMSPQDKKELRRKKLVKRSKSSLINMKGLVQHTPTNYDISNLLKEFTVDFLLKGYNYLVEELLKQLLTSAKVLIDTSHFFWLVTFFLKLAAQLELDMEHIDSILTYDVLSYLTYEGVSLCEQLELNAQQEGSDLQPYLRRMHLVVTAIREFLQTIETYNKVSHLSEDDRLRLHQLQLQIGATTDLRCLFVLLLRRFNPRIHSKQYLQDLVVTNHILMLILDSAAKLEGGQTIGLSEHISQFATLEVMHYYGILLEDFDNNGEFVNDCIFTMMHHIGGDLGQIGVLFQPIILKTYSR", "text": "FUNCTION: Required for the production of circadian 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 through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, perinuclear region Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with per is required for nuclear localization. SIMILARITY: Belongs to the timeless family."}
+{"protein": "MVKFLLLALALGVSCAHYQNLEVSPSEVDGKWYSLYIAADNKEKVSEGGPLRAYIKNVECIDECQTLKITFYTKVEGVCQEHTIVGRKGEDGKYITDFSGQNYFHIVEKSDDTMTFHNVNVDDSGKTNVILVVGRGESSSIEQKQRFEKTAEEYDIPKENIEDLVPTDNCDQ", "text": "SUBCELLULAR LOCATION: Secreted Note=Secreted by the lacrimal gland into tears. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MSDPESPLWVATLLRHHKELKQRQGMFQSRHMEFFRFKRFVRALNSDEYRAKSEREPEKYPPVRSEEDARDVFVSLIKAQLVLPCTKLHTAQCREHGLAPSKDYPHLLLSTKATLDADEYYVWTHNPKTLTDYLTVVGVIVGILAFVCYPLWPHSMKRVVYYLSLGLLGLLAVFSALALVRFVIYVLSLAFCSERGGFWIFPNLFEDCGVIASFKPLYGFGETECYGYIKKQKRRKRKLEKKKQ", "text": "FUNCTION: Required for preprotein translocation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SEC62 family."}
+{"protein": "MRSIFIILIFLLFLSSCSEEKAQDKNHEEKQIIEHETQNNETSKATNQEAVNSENTTESIVPANDNNQTDEVSTPASQKQKNPAIKAVKVTFKVDDNDMVLGNKKSNVIVVEYFSPTCPHCAYYHQTIFPELKKKYIDTNKIAYVVREFIATKQDLDAAILARCKGDTNSFTQLHNIILIQQDKWAYSNKYRELLTDIGQLGGISPEEYKQCLNNDKITAILIANTNFVAKAPQFIGTPSFFVNGVQTGNYSIDTISTAVDKALEEQKEKAKNEMSL", "text": "FUNCTION: May be required for disulfide bond formation in some proteins. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily."}
+{"protein": "MKKVEILKTSRPSSAGGAARPSTASPTHGAPKIAIKTRPVADDVAPTAATVIEPSQKAMKESVRFLTDFGEISDAISDLLTSSPNFNVISAIGPQGAGKSTLLSMLAGNNSRQMYREYVFRPVSREANEQSRHQTIQIDIYIVNHQIFLDCQPMYSFSIMEGLPKVRGGRFDDSTAMSDTLRLTAFLLYVSHTVLVVSETHYDKVIIDTLRVAEQIRPYLAIFRPKLAIDRKTNLVFIKTKASSIDLAPTVIREREELLRLSFQDSRWLKVSQEPFKTLIVLEEIRVRREHLFEEGDEPDEAASLNEFDEQIAELREELQKNREDFTVETAAMDEKKWLDMCREVIRDKTLHKTLKEYQRAMTDGVRTHFDNGFHAERDANKFFS", "text": "FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing smg-1 and recruited to stalled ribosomes. SIMILARITY: Belongs to the SMG9 family."}
+{"protein": "MCYNRESNFANQTIDFYCYTEYNGFMTTKGANVMTEVEMKEQVQEVLDKLRPFLLRDGGDCELVDVDEGIVKLRLLGACGSCPSSTITLKAGIERALLEEVPGVVEVEQVF", "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": "MTQINFNASYTSAPTPSRASFDNGYSEFCDKQQPNDYLNYYNNPTPDGADTVVSDSRLQAASNFLASVNSLTDDNDIMECLLKTTDNLGEAVSSAYNAESFELPVAEQPSPSSAYNAESFEHPVGVNQPSATGTKRKLDEYLDDSQSVVGQFNKNKLKPKYKKSTIQSCATLEQTINHNTNICTVASTQEITHYFTNDFAPYLMRFDDNDYNSNRFSDHMSETGYYMFVVKKSEVKPFEIIFAKYVSNVVYEYTNNYYMVDNRVFVVTFDKIRFMISYNLVKETGIEIPHSQDVCNDETAAQNCKKCHFVDVHHTFKAALTSYFNLDMYYAQTTFVTLLQSLGERKCGFLLSKLYEMYQDKNLFTLPIMLSRKESNEIETASNNFFVSPYVSQILKYSESIRKVKFPDNPPNKYVVDNLNLIVNKKSTLTYKYSSVANLLFNNYKYHDNIASNNNAENLKKVKKEDGSMHIVEQYLTQNVDNVKGHNFIVLSFKNEERLTIAKKNEEFYWISGEIKDVDASQVIQKYNRFKHHMFVISKVNRRESTTLHNNLLKLLALILQGLVPLSDAITFAEQKLNCKYKKFEFN", "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": "MKKRRSKKERQELLQQTIETNPFITDEDLAEKFQVSIQTVRLDRMELSIPELRERIKHVATKQHEEDVKSLPLEEVVGEIIDIELDRHAISIFEVKVEHVFKRNQIARGHHLFAQANSLAVAVIDEELALTAKSTIRYIRPVKLGERVVAKARVEDVENGKGRTVVKVRSFVGEELVFTGTFEMYRSSNYSEEGNNL", "text": "FUNCTION: Transcriptional factor involved in regulation of membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism. SIMILARITY: Belongs to the FapR family."}
+{"protein": "MSNKQNIESEVSWVKSKGAFVHPSLEFSVIPDAGSCVLANNDINENTVLLKLPPNILINKRTCSRYSFRDKLTSFQFLSWLISEDVHSNLEISPYYTKALPQGFSFHPVTLTSDHPLWSILPDEVRNSLLERKNVMAFDYEQVKKFVSVDQPTFQWGWLCVNTRCLYYDTGSKNTEDHLTLAPIFEYFNHSPEAQTALINTRGTITIKSTRRIDKGEQIFLCYGPHGNDKLFTEYGFCLSNNPNISIQLDRFIEFDKWQQSFLQDHGYWNDYTCSLHGASFRTLVGVRTLLVSPSEKLNDASYDQTRRVLQYINGFSDGSRDRQDVEDYLKKVLQELLCEAEECKEKVKGISDGSYVFICAEQLWKDRIMCCQYLMEHSFE", "text": "FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that trimethylates 60S ribosomal protein L12 (rpl1201 and rpl1202) at 'Lys-4' and may dimethylate L12 also at 'Lys-40' and 'Lys-41'. Overexpression causes a severe growth defect. Has a role in meiosis. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM2 family."}
+{"protein": "MAGGATAPAGAKPKQPKQKQKKPSSQARKKPSQKQKAMKPVKQELRKVEKQVRVLKARTNGPKVNDTMKTTVTVGTLVGQTQSGLNRQLRVSFNPLLMKSTEGGSTTPLSIRASMYEMWKPLSVEIFATPLSGFSSVVGSVGFMVITLNGLEASADSIDTIKARRHVQMALGRPYRLKLSARELAGPREGWWLVDTSEAPADAYGPAVDLMLAYATENLLGTSSGSTTSYTGTLWQVEMRVTYAFSTYNPKPGLQTLVSQSITGGQTVTIQPSPDDGSLIMTTNSQQVLALLTPRVAGQRKGKSQTIWAIAGSAVDAAATVLGPWGYLLKGGFWLVRLIFGGSSARNTTTRQYQIYPSVESALTDQPIFGNSTGTQSVTVPICHITEVVNPNAESNNLPPPTTGAQPQPQPPAPIEEILLPLAELTGQPGVPPLYTFDGSSYTPPTNWLGSTILLTGIPAHKRVTGNLAKFGVTNLQMSKVAATALEIYDFTDFGVFFGTGSYLSEGGIHTGKTLIYSLMSGQTPNPWLAANQSGTTWYMPSWAGFPQPGQGDYFLQMQDVTDTTTHTTSVNVYFLVAYRQSRRLIAFFNTGGTARPAPTSMLCLYNVDCGRAPQTPYPTFQSTLQSLNQIGVDAKSDPDSDDDISLAGSVIGDEFDSVDHLEREREDLMRRLRDLDLRRFQI", "text": "FUNCTION: Capsid polyprotein VP90: self-assembles to form an icosahedral T=3 capsid. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the astroviridae capsid polyprotein family."}
+{"protein": "MASLEIIKLEWATPIFKVVEHSQDGLYILLQGQISWQNSSQTYDLDEGNMLFLRRGSYAVRCGTKEPCQLLWIPLPGSFLSTFLHRFGSLLSEIRRDNATPKPLLIFNISPILSQSIQNLCAILERSDFPSVLTQLRIEELLLLLAFSSQGALFLSALRHLGNRPEERLQKFMEENYLQGWKLSKFAREFGMGLTTFKELFGTVYGISPRAWISERRILYAHQLLLNGKMSIVDIAMEAGFSSQSYFTQSYRRRFGCTPSQARLTKIATTG", "text": "FUNCTION: Transcriptional activator of the Yersinia virulence regulon."}
+{"protein": "MSLRDCQAWKNAGLPLSTTSNEACKLFDATLTQYVKWTNDKSLGGIEGCLSKLRAADPTFAMGLAISNGLVLVGTGTSVALDKDLALAVKTMVELSQTQTLTPREQLHVSAVEMFAKGNFPRACDLWEQILRDHPTDMLALKFSHDAYFYLGYQEQMRDSVARVYPFWTPDIPLNSYVKGIYSFGLMETNFYDQAQKLAKEALSIEPTDAWSVHTVAHVHEMRAEIKDGLEFMQQSEGHWKDSDMLACHNYWHWALYLIEKGDYEAALTIYDSHILPSLQASGTMLDVVDSCSMLYRLQMEGVPLGQRWQTVLPVTQKHTRDHILLFNDAHFLMASLGARDLQTTRELLTTLQEASKSPGENCQHQLAKDVGLPLCQALLEAENGNPDRVLELLLPIRYRIVQIGGSNAQRDVFNQLLIHAAMTCTSSVHKNVARSLLMERDALKPNSPLTERLIRRAAAVHLMQ", "text": "SIMILARITY: Belongs to the TTC38 family."}
+{"protein": "MVTTTEKTNIGYITQIIGPVLDIEYPSGKMPQIYNALLIRGKNQAGDEVSVTCEVQQLLGDKQVRAVSMSSTDGLVRGMEVIDTGAPISVPVGTITLGRIFNVLGEPVDEKGTVNSETTFPIHRAAPAFTNLETKPSVFETGIKVVDLLTPYRRGGKIGLFGGAGVGKTVIMMELINNIATKHGGVSVFGGVGERTREGNDLYNEMIESNVINKDDPSQSKIALVYGQMNEPPGARMRVGLSALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTDVGELQERITSTNEGSITSIQAVYVPADDLTDPAPATTFAHLDGTTVLSRGLAAKGIYPAVDPLGSTSTMLQPGIVGEAHYKTARAVQATLQRYKELQDIIAILGLDELSEDDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVTLEETIKGFNMILSGELDDLPEQAFYLVGNIEEAIAKAEKIKADSK", "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": "MKSILKKAKHFFHTNETVNGENGGEKTAKESESQQHHQQQQQHDENGANPPDQGVDEASNVSQSQPTTSALQTSTSLQPSSSLHQIPQSQSSLELTTNPTQQLPTTPTKQLPTPPPPQQPHSQQQQQQQQQSQSQLNNNDISISTNTNNTTNNTNNNNNIDSTLTTPVPSSENLATLSTSTTSEQQPNSQPTPNNTNTTTSPPPSSASTSNLSTSTTTTTTTTTTTTAAANENTNTTQEQTVSPNKPPQPPNALSQSTTSSSTSSTSLLSSTFSKFKIKLGSGSTKNKDSSSAPGTPHINNNNNTVSSSNKNRSTLVITPGSVNNNNNNQNNHKNNNTTPDHPPEEQKPVEKEVITIATLADFPEDCQKLIRISGIPEEKLIKNIQILAYVLHFRTGRFFKLVDEPPREPRKKFVSERFNDGEKLLEPVEPALLKKMYKDSDQVGKGGFGTVYFAKSTKEKRLVAIKKMPHVTKRQQQQNFREAAILAKCDHPNIVKLHTCHIDKDSNLWIVMEFMEGGTFEEAAKAWKFNENNLAYVAKELLKGLQYLHENHMVHRDLKSANIMMSVEGKVKLIDFGLCEDVATSTPMHMVGSPFWMAPEMIQQKYHSTPVDIWSFAISLLEMANQRPPMMESAVKAMFTVATDGATGFDDPALWSDCFKDFLSLCLKQDPAERATAEELLKHPFIKKADSRDNMENILKKIFLTNSLMNSGF", "text": "SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
+{"protein": "MLPGLRRLLQGPASACLLLTLLALPSVTPSCPMLCTCYSSPPTVSCQANNFSSVPLSLPPSTQRLFLQNNLIRSLRPGTFGPNLLTLWLFSNNLSTIHPGTFRHLQALEELDLGDNRHLRSLEPDTFQGLERLQSLHLYRCQLSSLPGNIFRGLVSLQYLYLQENSLLHLQDDLFADLANLSHLFLHGNRLRLLTEHVFRGLGSLDRLLLHGNRLQGVHRAAFHGLSRLTILYLFNNSLASLPGEALADLPALEFLRLNANPWACDCRARPLWAWFQRARVSSSDVTCATPPERQGRDLRALRDSDFQACPPPTPTRPGSRARGNSSSNHLYGVAEAGAPPADPSTLYRDLPAEDSRGRQGGDAPTEDDYWGGYGGEDQRGEQTCPGAACQAPADSRGPALSAGLRTPLLCLLPLALHHL", "text": "FUNCTION: Cell surface receptor that plays a functionally redundant role in the inhibition of neurite outgrowth mediated by MAG (By similarity). Plays a functionally redundant role in postnatal brain development (PubMed:27339102). Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum (PubMed:27339102). Does not seem to play a significant role in regulating axon regeneration in the adult central nervous system (PubMed:22406547). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG (PubMed:26335717). 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 Cell projection, dendrite Cell projection, axon Perikaryon Note=Localized to the surface of neurons, including axons. Detected close to synapses, but is excluded from synapses. SIMILARITY: Belongs to the Nogo receptor family."}
+{"protein": "MGSQATTYHMAMYPWFGVGHLTGFFRLANKLAGKGHRISFLIPKNTQSKLESFNLHPHLISFVPIVVPSIPGLPPGAETTSDVPFPSTHLLMEAMDKTQNDIEIILKDLKVDVVFYDFTHWLPSLARKIGIKSVFYSTISPLMHGYALSPERRVVGKQLTEADMMKAPASFPDPSIKLHAHEARGFTARTVMKFGGDITFFDRIFTAVSESDGLAYSTCREIEGQFCDYIETQFQKPVLLAGPALPVPSKSTMEQKWSDWLGKFKEGSVIYCAFGSECTLRKDKFQELLWGLELTGMPFFAALKPPFETESVEAAIPEELKEKIQGRGIVHGEWVQQQLFLQHPSVGCFVSHCGWASLSEALVNDCQIVLLPQVGDQIINARIMSVSLKVGVEVEKGEEDGVFSRESVCKAVKAVMDEKSEIGREVRGNHDKLRGFLMNADLDSKYMDSFNQKLQDLLG", "text": "FUNCTION: Glycosyltransferase that mediates the glucosylation of anthocyanidin 3-O-glucosides to yield anthocyanidin 3-O-sophorosides. 3-O-sophoroside derivatives are required for the color of flowers. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MTLPSGHPKSRLIKKFTALGPYIREGKCEDNRFFFDCLAVCVNVKPAPEVREFWGWWMELEAQESRFTYSYQFGLFDKAGDWKSVPVKDTEVVERLEHTLREFHEKLRELLTTLNLKLEPADDFRDEPVKLTA", "text": "FUNCTION: Binds to the sigma-S subunit of RNA polymerase, activating expression of sigma-S-regulated genes. Stimulates RNA polymerase holoenzyme formation and may bind to several other sigma factors, such as sigma-70 and sigma-32. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Crl family."}
+{"protein": "MNKQDVTIYDVAREAKVSMATVSRVVNGNNNVRKETRDRVMEVIKRLHYQPNAVAQGLASKRTTTVGLIVPDLTNLYFAELSKGIDDIAVLYKYNIIISSVENRLMKEDAVIQGLLNKQVDGVIYMSNKLSEEAAEAFKRTDTPVVLAGTVSDNLEFPSVNIDYKKADTEALNLLLNDGKKKLALIVGDKEASINRNYRIPAFEKFVADNELEGCEIFDNIKDYSDGYNLYPELAKKGINGAIITKDVSSVGLLNSALDRGAKVPEDFEIITASATQIASVVRPALTTIKQPLYDLGAVAMRMLTKLMNDESLEDKHIILPYELIKKQSTLNK", "text": "FUNCTION: Transcriptional regulator of the pepQ gene for prolidase."}
+{"protein": "EAVDFDSQCVPTADPGKCKFYFPMWNVNVFT", "text": "FUNCTION: Serine protease inhibitor. Inhibits trypsin, elastase, plasmin and kallikrein."}
+{"protein": "MATRSPSVVISDDEPGYDLDLFCIPNHYVEDLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKA", "text": "FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5- phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
+{"protein": "MELEKRLKEKLEAPTLDYEKYFSEKALGMKASEIRELLKLVETSDVISLAGGLPAPETFPVEIIGEITKEVLEKHAAQALQYGTTKGFTPLRLALAEWMRERYDIPISKVDIMTTSGSQQALDLIGRVFINPGDIIVVEAPTYLAALQAFKYYEPEFVQIPLDDEGMNVDLLEEKLQELEKEGKKVKIVYTIPTFQNPAGVTMNEKRRKRLLELASQYDFIIVEDNPYGELRYSGEPVKPIKAWDEEGRVIYLGTFSKILAPGFRIGWIAAEPHFIRKLEIAKQSVDLCTNTFSQVIAWKYVEGGYLDKHIPKIIEFYKPRRDAMLKALEEFMPDGVKWTKPEGGMFVWATLPEGIDTKLMLEKAVAKGVAYVPGEAFFAHRDVKNTMRLNFTYVPEEKIREGIKRLAETIKEEMKK", "text": "FUNCTION: Catalyzes the transamination of phenylalanine, tyrosine and tryptophan. Shows virtually no activity towards aspartic acid, alanine, valine or isoleucine. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MAVVAGLRAFGVKWPSWLRRNPWAPLSAGFCSPGSAGPAGSESEPRLTSTRQQDGIRNIVLSNPRRRNALSLAMLKSLRSDILHEAESEDLKVIIISAEGPVFSSGHDLKELTDAQGRDYHAEVFQTCSEVMMLIRNHPVPILAMVNGLATAAGCQLVASCDIAVASDKSSFATPGVNVGLFCSTPAVALGRAVPRKVALEMLFTGEPISAQEALRHGLISKVVPEEQLEAETMRIAKKISSLSRSVVALGKATFYKQLPQDLRTAYFLASQAMVDNLALQDGQEGIEAFIQKRKPIWSH", "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": "MSFVRNISDYFNKIDNLCYNQSWESGDKIAKYLSLNDDHSKEAYLHISEYGSTSRRCRVSEDEIIDEIVCLHLHVLHSVHVAKDLISSQSTQIRIIQLFNKEILQKRKDENWFLPIFYRLCTDLRWLSKGAESCASGDDEGDSNANSFFESAAKAITECYRTCVSDVHAEEGKTKKVAMLNMTNQLFQIYFQINKLNLLKPLIRAIDNCGPLYNKFLMADKVAYNYFLGRKALFDGDLILAEKGLVYAFRNCPTESVSNKRKILVYLIPVKMFLGHMPTASLLHRYRLDEFQEVVAAVKDGHLGRVDNALLTNGEFFIKCGIYLVLEKLRTITYRNLFKKVSQMVGKVQIPLDAFQAALRFVGVTDVDMDELECIIANLIAEKKVKGYLAHQHQKLVISKTNAFPTLSSVSSN", "text": "SIMILARITY: Belongs to the CSN12 family."}
+{"protein": "GGVLKDTIQMIHGPLGCAYDTWHTKRYPTDNGHFNMKYVWSTDMKESHVVFGGEKRLEKSMHEAFDEMPDIKRMIVYTTCPTALIGDDIKAVAKKVMKDRPDVDVFTVECPGFSGVSQSKGHHVLNIGWINEKVETMEKEITSEYTMNFIGDFNIQGDTQLLQTYWDRLGIQVVAHFTGNGTYDDLRCMHQAQLNVVNCARSSGYIANELKKRYGIPRLDIDSWGFNYMAEGIRKICAFFGIEEKGEELIAEEYAKWKPKLDWYK", "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": "MVALIDQLYNVTALRECSSLNVAAWIVFGLGISKMVFLTLNFSKMVLDLFVLPGPDFKKYGKGKGAYAVVTGASDGIGKEYAKQLAKRGFNLILISRTESKLVELKKEIETECKIDVKILAIDVSSDSKENYTLIREVASGLPVTVLINNVGKSHSIPVPFDQTEESELRDIITINNTATLMITQTLLPQLKASVKTLKCRGLILTMGSFGGLLPTPFLATYSGSKAFLQSWSNALAGELSSDSIDVELVLSYLVTSAMSKIRRSSALIPSPKAFVRSTLNSIGKRCGAQERFATSTPYWSHALYHFIIENTVGVYSKIANSINYSFHLSIRKRALKKAERQAKKQ", "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": "MMEAKPKRRIVTENGDTGEDLVLATLIGNGDDVGPLVRHAFEMGRPEPLVHQLKNVARKKEAEIEDLCKTHYEEFIVAVDELRGVLVDAEELKSDLASDNFRLQEVGSALLVKLEELLESYAVKKNVTEAIKMSKICVQALELCVKCNSYISEGQFYHALKTMDLIEKSYLKLIPLKVLKLVIERRIPVIKTHIEKKVCSQFNEWLVHIRSSSKNIGQTAIGLTASARQREEEMLERQRRAEEQNTGGLGELAYTLDVEDSEQDSVLKFDLTPLYRAYHIHTILGVPERFRDYYYENRLLQLQSDLQITYTQPFVESYQTFLAQVAGYFIVEDRVIRTAGDFLLADQVETMWETAISKIVAILENQFARMDSPTHLLLVKDYVTLLGTTLRQYGYEVGPVLDALDKSRDKYHELLLEECRKQIVTAITEDTYQQMVIKKEADYENNVLSFNLQTSDIMPAFTYIAPFSSMVPDVCRIIRSYIKGSVDYLSYGVNTNFFSVLRKYLDKILIDVLNEVILETISNNSIGVSQAMQIAANISFLEKASDYFLRHAAQLCGIPSRSVERPQASLAAKVVLKTSRDAAYLALLNVVNTKLDEFMKLTENVNWTTEEMPQGPHEYINEVVIYLETVMSTAQQILPMDALYKVGVGAIEHISNSIVSTFLSDSIKRFNANAVSAINHDLRVIENFADERYHSSGLNEIYKEGSFRSYLVEARQLINLLSSSQPENFMNPVIRERNYNTLDYKKVATICEKFKDSADGIFGSLANRNTKLTAKKKSMDMLKKRLKEFN", "text": "FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. SUBCELLULAR LOCATION: Cytoplasm, cytosol Note=Localized to globular structures in the perinuclear region. SIMILARITY: Belongs to the SEC15 family."}
+{"protein": "MYVDMNREYLKDINTTEDVKIPEDPLERVIGHEDVMPMIKIAAKQRRHLLLVGPPGIGKSLLAQAISFHLPEPSEEITVVHNPERPERPFVEIKNRKEIEDEILEIERAEGELIDPQSAPDAVAERLGFKCIHCGEYSSAYNSICPRCGGDKFSHIKARRKHIGDLLGMFEMSSGSLSVPQKRVTTTRIIDGVEEVVIYERVGGEEIKVLDQRALEKRRQIVEEKPRNVIVPLDRKTFVQATGASETELLGDVRHDPYGGHPDLGSQPYERVVPGAIHEAHEGVLFIDEIVHIAGLQRFIFSAMQDKTFPIVGRNPQSAGSSVKVDEVPCDFIFVGACNIADLQYILPPLRSRIQGEGYELLLNTTMPDTDENRAKIAQFVAQEIELDGKIPHARAAAVELLIEEARRRARAVDDVDNALTLRLRDLGGVVRMAGDLAVMDGSPYIETRHMEVAIRKAVSVEDQIIRRYKSYEKALEKDLSSSQRMSQHGYSSENIDRSYM", "text": "SIMILARITY: Belongs to the peptidase S16 family."}
+{"protein": "MAKMYGKGKTAIESEELQKRRWQIELEFVQCLSNPNYLNFLAQRGFFKDQSFINYLKYLQYWKEPDYAKYLMYPMCLYFLDLLQYEHFRREIVNSQCCKFIDDQAILQWQHYTRKRIKLIENVTAAQQQQQQLQQQQQQANGMEAATGGESAAPTPNVNGSASTADSQQTSSALQPVQAQPGNPQQQQQINGVASGANIKLELN", "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. Required for activated transcription of the MtnA gene. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 31 family."}
+{"protein": "MARKGKVNTLPQPQGKHQRKGKKQLENKILHSYEEESAGFDSEELEDNDEQGYSFGVNSEDDEEIDSDEAFDEEDEKRFADWSFNASKSGKSNKDHKNLNNTKEISLNEEDDSDDSVNSDKLENEGSVGSSIDENELVDLDTLLDNDQPEKNESNTASTIRPPWIGNNDHATDKENLLESDASSSNDSESELTDSADNMNESDSESEIESSDSDHDDGENSDSKLDNLRNYIVSLNQKRKKDEADAESVLSSDDNDSIEEISIKKVKYDPHETNKESEYNLIGSSEKTIDITDLLDSIPMNEQLKVSLKPLVSESSSISSKKLDAPLAKSIQDRLERQAAYEQTKNDLEKWKPIVADNRKSDQLIFPMNETARPVPSNNGLASSFEPRTESERKMHQALLDAGLENESALKKQEELALNKLSVEEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNRKEKEMALIPKSEEDLENERIKSEEARALERMTQRHKNTSSWTRKMLERASHGEGTREAVNEQIRKGDELMQRIHGKEISEMDGEDVSEFSDSDYDTNEQVSTAFEKIRNEEEPKLKGVLGMKFMRDASNRQKALVQDEMQAFEDELAGVPNEDDTSQKGEDGVPGVLIGNNTGRRSFKPSEEAAKLSLPSRKNPFVSDSAVLKVNKPEMKEGQKKAEARKKKESPLEATEETNPWLQVPDQRTSSAKKLDKNSSKADKKNHKLKMDKVASLQELVEEPKVQPDLIFEEKAFESASEAESDVDVSVPMLKPTKGRLSIKQRELVAKAFAGDDVVAEFEKDKEDWVQEDAPKEEDHSLPGWGSWGGVGVKQRKTKPKVKKIAGLDPSKRKDSKLKHVIINEKRNKKAAKLTADSVPFPFESREQYERSLNLPMGPEWTTRASHHKAVAPRVVTKRGKVINPIKAPN", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: To yeast YML093w."}
+{"protein": "MAAGGAVAAAPECRLLPYALHKWSSFSSTYLPENILVDKPNDQSSRWSSESNYPPQYLILKLERPAIVQNITFGKYEKTHVCNLKKFKVFGGMNEENMTELLSSGLKNDYNKETFTLKHKIDEQMFPCRFIKIVPLLSWGPSFNFSIWYVELSGIDDPDIVQPCLNWYSKYREQEAIRLCLKHFRQHNYTEAFESLQKKTKIALEHPMLTDIHDKLVLKGDFDACEELIEKAVNDGLFNQYISQQEYKPRWSQIIPKSTKGDGEDNRPGMRGGHQMVIDVQTETVYLFGGWDGTQDLADFWAYSVKENQWTCISRDTEKENGPSARSCHKMCIDIQRRQIYTLGRYLDSSVRNSKSLKSDFYRYDIDTNTWMLLSEDTAADGGPKLVFDHQMCMDSEKHMIYTFGGRILTCNGSVDDSRASEPQFSGLFAFNCQCQTWKLLREDSCNAGPEDIQSRIGHCMLFHSKNRCLYVFGGQRSKTYLNDFFSYDVDSDHVDIISDGTKKDSGMVPMTGFTQRATIDPELNEIHVLSGLSKDKEKREENVRNSFWIYDIVRNSWSCVYKNDQAAKDNPTKSLQEEEPCPRFAHQLVYDELHKVHYLFGGNPGKSCSPKMRLDDFWSLKLCRPSKDYLLRHCKYLIRKHRFEEKAQVDPLSALKYLQNDLYITVDHSDPEETKEFQLLASALFKSGSDFTALGFSDVDHTYAQRTQLFDTLVNFFPDSMTPPKGNLVDLITL", "text": "FUNCTION: 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 (PubMed:29911972). Required for internalization of the GABA receptor GABRA1 from the cell membrane via endosomes and subsequent GABRA1 degradation (By similarity). Acts as a mediator of cell spreading and cytoskeletal responses to the extracellular matrix component THBS1 (PubMed:18710924). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytosol Nucleus, nucleoplasm Cell projection, ruffle Cytoplasm, cell cortex Synapse Postsynapse Note=Colocalizes with GABRA1 at synapses and in postsynaptic regions. Colocalizes with actin fibers in the cell cortex."}
+{"protein": "MLILLKKAVKLKIIRPIDFYFSQFIAQKNNIVMLVAACVSYESSRGYISLPIKYFEKHYFFSSSNEVFIKKILTLLEKKINWPVELLKHASIGNGGTSTPLVLHKKKIYLYKMWKSESNIFNYLYTKNKKNKINQKKCSKILENLFPQKNMSFQKIAVALTLINNITFIIGGPGTGKTTTILKIIIALIKSSKKSIKIQLSAPTGKATTHLNEILKNNIFDLYFSEKEKCSLPSTATTIHQLLGIQKISQKSFFNKSNCLDLDVLIIDEISMVDILMMEKILSSISKNTKLIFIGDHNQLGPIESGSILRKICYYANDGYSFKSMISIEKLTQYKLCKKINKKTTNFISDNICVLNKNYRFNKNSGIYTLSNAIFKKKTRIIESLFDNSIKNIFFYETNSSEQYKKMIKNICLNYEDFWEKIYKKATMKEIIESFQNYQVLCILHDGLFGVNIINKKLEENMYKKNIIKYFYIDGEEWYIGKPIMIINNNRALNVSNGNIGITNINKNGILQVSFLKENNTINNIPVKILRNYKTAWAITVHKSQGSEFMNTALILPNFNSHILNKDTLYTGITRSRKILSIFSDKKIFLNTIFKNTNKILF", "text": "FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre- assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD. SIMILARITY: Belongs to the RecD family."}
+{"protein": "MSQTPEARARDNQTRQIQESVNNVEKHFGELCQIFAGYVRKTARLRDKADLLVREVNTYADTETPTVKLGLKNFADELAKLQDYRQAEVERLESRVVEPLKSYGSIIKLKREDLKVTLTARNREAKQMAQLEKTRQRNPSDRQIISQAETELQRATMDASRISQQLEETIDNFEKQKMKDIKKLFTEFVSIEMVFHGKALEVLTAAYQHIQDIDEEEDLEVFRNSLHPPDFQSRLDIVRANSRTGSTSRGPSVISQPPGNRQKNRIEDEDEEEEDDENSTEDEN", "text": "FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling (By similarity). Plays a role in ciliogenesis (By similarity). Plays an important role in the mitochondrial function and is essential for maintaining mitochondrial morphology and inner membrane ultrastructure (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the CIBAR family."}
+{"protein": "MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQFPSSGRFWKLYIEAEIKAKNYDKVEKLFQRCLMKVLHIDLWKCYLSYVRETKGKLPSYKEKMAQAYDFALDKIGMEIMSYQIWVDYINFLKGVEAVGSYAENQRITAVRRVYQRGCVNPMINIEQLWRDYNKYEEGINIHLAKKMIEDRSRDYMNARRVAKEYETVMKGLDRNAPSVPPQNTPQEAQQVDMWKKYIQWEKSNPLRTEDQTLITKRVMFAYEQCLLVLGHHPDIWYEAAQYLEQSSKLLAEKGDMNNAKLFSDEAANIYERAISTLLKKNMLLYFAYADYEESRMKYEKVHSIYNRLLAIEDIDPTLVYIQYMKFARRAEGIKSGRMIFKKAREDTRTRHHVYVTAALMEYYCSKDKSVAFKIFELGLKKYGDIPEYVLAYIDYLSHLNEDNNTRVLFERVLTSGSLPPEKSGEIWARFLAFESNIGDLASILKVEKRRFTAFKEEYEGKETALLVDRYKFMDLYPCSASELKALGYKDVSRAKLAAIIPDPVVAPSIVPVLKDEVDRKPEYPKPDTQQMIPFQPRHLAPPGLHPVPGGVFPVPPAAVVLMKLLPPPICFQGPFVQVDELMEIFRRCKIPNTVEEAVRIITGGAPELAVEGNGPVESNAVLTKAVKRPNEDSDEDEEKGAVVPPVHDIYRARQQKRIR", "text": "FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MDKTTQVNQKTGLLSQPKAVWAVAFACVISFMGIGLVDPILPAIAAQLHASPSEVSLLFTSYLLVTGFMMFFSGAISSRIGAKWTLILGLIFIIVFAGLGGSSSSIAQLVGYRGGWGLGNALFISTALAVIVGVSVGGSAQAIILYEAALGLGISVGPLAGGELGSISWRAPFFGVSVLMFIALIAISFMLPKLPKPAKRVGVFDAMKALKYKGLLTMAVSAFLYNFGFFILLAYSPFVLDLDEHGLGYVFFGWGLLLAITSVFTAPLVHKALGTVRSLVVLFIAFAAILVIMGIWTDHQTLIITCIVVAGAVLGMVNTIMTTAVMGSAPVERSIASSAYSSVRFIGGALAPWIAGMLSEHFTASTPYTVGGIVVFVGMLVLLMGRKHLAGIKAGH", "text": "FUNCTION: Acts to efflux copper or a copper complex. It is possible that YfmO could contribute to copper resistance. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MRFLILFLALSLGEIDAAPPVQSRIVGGFNCEKNSQPWHVAVFRYNKYICGGVLLNPNWVLTAAHCYGNQYNVWLGKNKLFQHESSAQHRLVSKSFPHPDYNMSLMNDHTPHPEDDYSNDLMLLRLSKPADITDAVKPIDLPTEEPKLGSTCLASGWGSITPTKWQIPNDLQCGFIKPLPNENCAKAYIHKVTDVMLCAGEMGGGKDTCAGDSGGPLICDGVLQGITSWGSIPCAKPNAPAIYTKLIKFTSWIKDTMAKNP", "text": "FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. Displays trypsin-like substrate specificity and shows activity towards casein, gelatin, fibronectin and IGFBP3. SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily."}
+{"protein": "MKAIFIILAILMVTQAFKMTSKVKSMNMSRNMSKNTSTLGTKYTYGCPQTNTPTQQDCYDAMYYTFMAMCDLYPDPEHPMFPSYDSCQEESDSADEFYTNQCGCGGYGMAAAHDQVCLLALGVCIPE", "text": "FUNCTION: Mating ciliate pheromones (or gamones) are diffusible extracellular communication signals that distinguish different intraspecific classes of cells commonly referred to as 'mating types'. They prepare the latter for conjugation by changing their cell surface properties. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MNKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNIRVTLIHQDILQFQFPNKQRYKIVGSIPYHLSTQIIKKVVFESHASDIYLIVEEGFYKRTLDIHRTLGLLLHTQVSIQQLLKLPAECFHPKPKVNSVLIKLTRHTTDVPDKYWKLYTYFVSKWVNREYRQLFTKNQFHQAMKHAKVNNLSTITYEQVLSIFNSYLLFNGRK", "text": "FUNCTION: This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family."}
+{"protein": "MTEVLHFPSSPSASHSSSSSSSSPSPSSLSYASRSNATLLISSDHNRRNPVARFDQDVDFHASIEEQDLRRRSSTDGGEEDDGGEDQISLLALLVAIFRRSLISCKSNRRELCSMEIGWPTNVRHVAHVTFDRFNGFLGLPVEFEPEVPRRAPSASATVFGVSTESMQLSYDSRGNCVPTILLLMQNCLYSQGGLQAEGIFRLTAENSEEEAVREQLNRGFIPERIDVHCLAGLIKAWFRELPTSVLDSLSPEQVMQCQTEEENVELVRLLPPTEAALLDWAINLMADVVQYEHLNKMNSRNIAMVFAPNMTQMDDPLTALMYAVQVMNFLKTLIEKTLRERQDSVVEQAHAFPLEPSDESGHQSPSQSLAFNTSEQSEETQSDNIENAENQSSSSEISDELTLENNACEQRETDFGKYRTGRLSDSSQQVVLNLDPPAQWPVGRTKGLTNLSRVGSRVERTEAWR", "text": "FUNCTION: Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state."}
+{"protein": "MKNITFIFFILLASPLYANGDRLYRADSRPPDEIKRSGGLMPRGHNEYFDRGTQMNINLYDHARGTQTGFVRYDDGYVSTSLSLRSAHLAGQSILSGYSTYYIYVIATAPNMFNVNDVLGVYSPHPYEQEVSALGGIPYSQIYGWYRVNFGVIDERLHRNREYRDRYYRNLNIAPAEDGYRLAGFPPDHQAWREEPWIHHAPQGCGNSSRTITGDTCNEETQNLSTIYLREYQSKVKRQIFSDYQSEVDIYNRIRDEL", "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": "MEIRVANKYALGKKLGSGSFGDIYVAKDIVTMEEFAVKLESTRSKHPQLLYESKLYKILGGGIGVPKVYWYGIEGDFTIMVLDLLGPSLEDLFTLCNRKFSLKTVLMTADQMLNRIEYVHSKNFIHRDIKPDNFLIGRGKKVTLIHIIDFGLAKKYRDSRSHTHIPYKEGKNLTGTARYASINTHLGIEQSRRDDIEALGYVLMYFLRGSLPWQGLKAISKKDKYDKIMEKKISTSVEVLCRNTSFEFVTYLNYCRSLRFEDRPDYTYLRRLLKDLFIREGFTYDFLFDWTCVYASEKDKKKMLENKNRFDQIADQEGRVKQN", "text": "FUNCTION: Serine/threonine-protein kinase likely to be involved in many cellular processes. SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, secretory vesicle, microneme Secreted Host cell surface. SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily."}
+{"protein": "MVSWMICRLVVLVFGMLCPAYASYKAVKTKNIREYVRWMMYWIVFALFMAAEIVTDIFISWFPFYYEIKMAFVLWLLSPYTKGASLLYRKFVHPSLSRHEKEIDAYIVQAKERSYETVLSFGKRGLNIAASAAVQAATKSQGALAGRLRSFSMQDLRSISDAPAPAYHDPLYLEDQVSHRRPPIGYRAGGLQDSDTEDECWSDTEAVPRAPARPREKPLIRSQSLRVVKRKPPVREGTSRSLKVRTRKKTVPSDVDS", "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. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DP1 family."}
+{"protein": "MTIFDNYEVWFVIGSQHLYGPETLRQVTQHAEHVVNALNTEAKLPCKLVLKPLGTTPDEITAICRDANYDDRCAGLVVWLHTFSPAKMWINGLTMLNKPLLQFHTQFNAALPWDSIDMDFMNLNQTAHGGREFGFIGARMRQQHAVVTGHWQDKQAHERIGSWMRQAVSKQDTRHLKVCRFGDNMREVAVTDGDKVAAQIKFGFSVNTWAVGDLVQVVNSISDGDVNALVDEYESCYTMTPATQIHGEKRQNVLEAARIELGMKRFLEQGGFHAFTTTFEDLHGLKQLPGLAVQRLMQQGYGFAGEGDWKTAALLRIMKVMSTGLQGGTSFMEDYTYHFEKDNDLVLGSHMLEVCPSIAVEEKPILDVQHLGIGGKDDPARLIFNTQTGPAIVASLIDLGDRYRLLVNCIDTVKTPHSLPKLPVANALWKAQPDLPTASEAWILAGGAHHTVFSHALNLNDMRQFAEMHDIEITVIDNDTRLPAFKDALRWNEVYYGFRR", "text": "FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. SIMILARITY: Belongs to the arabinose isomerase family."}
+{"protein": "MSLSEGQVHRFLDQNPGFADQYFGRKLSPEDVANACEDGCPEGCTSFRELCQVEESAALFELVQDMQENVNMERVVFKILRRLCSILHADRCSLFMYRQRNGVAELATRLFSVQPDSVLEDCLVPPDSEIVFPLDIGVVGHVAQTKKMVNVQDVMECPHFSSFADELTDYVTRNILATPIMNGKDVVAVIMAVNKLDGPCFTSEDEDVFLKYLNFGTLNLKIYHLSYLHNCETRRGQVLLWSANKVFEELTDIERQFHKAFYTVRAYLNCDRYSVGLLDMTKEKEFFDVWPVLMGEAQAYSGPRTPDGREILFYKVIDYILHGKEDIKVIPSPPADHWALASGLPTYVAESGFICNIMNAPADEMFNFQEGPLDDSGWIVKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDEQDEVLMESLTQFLGWSVLNTDTYDKMNKLENRKDIAQDMVLYHVRCDREEIQLILPTRERLGKEPADCEEDELGKILKEVLPGPAKFDIYEFHFSDLECTELELVKCGIQMYYELGVVRKFQIPQEVLVRFLFSVSKGYRRITYHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDIDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKFLLSEETLNIYQNLNRRQHEHVIHLMDIAIIATDLALYFKKRTMFQKIVDESKNYEDRKSWVEYLSLETTRKEIVMAMMMTACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTVLDQQPIPMMDRNKAAELPKLQVGFIDFVCTFVYKEFSRFHEEILPMFDRLQNNRKEWKALADEYEAKVKALEEDQKKETTAKKVGTEICNGGPAPRSSTCRIL", "text": "FUNCTION: Necessary for the formation of a functional phosphodiesterase holoenzyme (By similarity). Involved in retinal circadian rhythm photoentrainment via modulation of UVA and orange light-induced phase- shift of the retina clock (By similarity). May participate in processes of transmission and amplification of the visual signal (By similarity). FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP (By similarity). Necessary for the formation of a functional phosphodiesterase holoenzyme (By similarity). Involved in retinal circadian rhythm photoentrainment via modulation of UVA and orange light-induced phase-shift of the retina clock (By similarity). May participate in processes of transmission and amplification of the visual signal (By similarity). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Cell projection, cilium, photoreceptor outer segment. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family."}
+{"protein": "MRVLRACLSLCVLVVSDSKGSHELHQESGASNCGCLNGGKCVSYKYFSNIQRCSCPKKFQGEHCEIDTSQTCFEGNGHSYRGKANTNTGGRPCLPWNSATVLLNTYHAHRPDALQLGLGKHNYCRNPDNQRRPWCYVQVGLKQLVQECMVPNCSGGESHRPAYDGKNPFSTPEKVEFQCGQKALRPRFKIVGGKSTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVVSATHCFINYQQKEDYIVYLGRQTLHSSTHGEMKFEVEKLILHEDYSADSLAHHNDIALLKIRTDKGQCAQPSRSIQTICLPPVNGDAHFGASCEIVGFGKEDPSDYLYPEQLKMTVVKLVSHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSTQGRLTLTGIVSWGRECAMKDKPGVYTRVSRFLTWIHTHVGGENGLAH", "text": "FUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MAGRSLTSKAEPTAGAVDRAEKAGGQDTSSQKIEDLMEMVQKLQKVGSLEPRVEVLINRINEVQQAKKKANKDLGEARTICEALQKELDSLHGEKVHLKEILSKKQETLRILRLHCQEKESEAHRKHTMLQECKERISALNLQIEEEKNKQRQLRLAFEEQLEDLMGQHKDLWDFHMPERLAKEICALDSSKEQLLKEEKLVKATLEDVKHQLCSLCGAEGPSTLDEGLFLRSQEAAATVQLFQEEHRKAEELLAAAAQRHQQLQQKCQQQQQKRQRLKEELEKHGMQVPAQAQSTQEEEAGPGDVASPKPLKGERPGAAHQAGPDVLIGQEDTLHPDLSPRGFQEIKELF", "text": "FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Requires SYCP1 in order to be incorporated into the central element. May have a role in the synaptonemal complex assembly, stabilization and recombination. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Associates with chromatin. In prophase I stage of meiosis, localizes in the transverse central elements of the central region between lateral elements of the synaptonemal complexes. Found only where the chromosome cores are synapsed. Colocalizes with SYCE2 in the central elements. SIMILARITY: Belongs to the SYCE family."}
+{"protein": "MRLRAVLFDMDGTLLDTAPDFIAICQAMLAERGLPAVDDNLIRGVISGGARAMVATAFAMDPEADGFEALRLEFLERYQRDCAVHSKLFEGMAELLADIEKGNLLWGVVTNKPVRFAEPIMQQLGLAERSALLICPDHVKNSKPDPEPLILACKTLNLDPASVLFVGDDLRDIESGRDAGTRTAAVRYGYIHPEDNPNNWGADVVVDHPLELRKVIDSALCGC", "text": "FUNCTION: Specifically catalyzes the dephosphorylation of N- acetylmuramate 6-phosphate (MurNAc-6P) to MurNac. Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP- MurNAc. Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc. Shows a very low activity on GlcNAc-6P, and neither alpha-1-phosphorylated MurNAc, GlcNAc, or glucose nor glucosamine-6P or glucose-6P can be used as a substrate. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. Phosphatase MupP subfamily."}
+{"protein": "MAYRALMVLRMDPADAEHVAAAFAEHDTTELPLEIGVRRRVLFRFHDLYMHLIEADDDIMERLYQARSHPLFQEVNERVGQYLTPYAQDWEELKDSKAEVFYSWTAPDS", "text": "FUNCTION: Catalyzing the conversion of tetracenomycin F2 to tetracenomycin F1."}
+{"protein": "MVLLSILRILFLCELVLFMEHRAQMAEGGQSSIALLAEAPTLPLIEELLEESPGEQPRKPRLLGHSLRYMLELYRRSADSHGHPRENRTIGATMVRLVKPLTNVARPHRGTWHIQILGFPLRPNRGLYQLVRATVVYRHHLQLTRFNLSCHVEPWVQKNPTNHFPSSEGDSSKPSLMSNAWKEMDITQLVQQRFWNNKGHRILRLRFMCQQQKDSGGLELWHGTSSLDIAFLLLYFNDTHKSIRKAKFLPRGMEEFMERESLLRRTRQADGISAEVTASSSKHSGPENNQCSLHPFQISFRQLGWDHWIIAPPFYTPNYCKGTCLRVLRDGLNSPNHAIIQNLINQLVDQSVPRPSCVPYKYVPISVLMIEANGSILYKEYEGMIAESCTCR", "text": "FUNCTION: May be involved in follicular development. Oocyte-specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
+{"protein": "MPSTPSFVRSAVSKYKFGAHMSGAGGISNSVTNAFNTGCNSFAMFLKSPRKWVSPQYTQEEIDKFKKNCATYNYNPLTDVLPHGQYFINLANPDREKAEKSYESFMDDLNRCEQLGIGLYNLHPGSTLKGDHQLQLKQLASYLNKAIKETKFVKIVLENMAGTGNLVGSSLVDLKEVIGMIEDKSRIGVCIDTCHTFAAGYDISTTETFNNFWKEFNDVIGFKYLSAVHLNDSKAPLGANRDLHERLGQGYLGIDVFRMIAHSEYLQGIPIVLETPYENDEGYGNEIKLMEWLESKSESELLEDKEYKEKNDTLQKLGAKSRKEQLDKFEVKQKKRAGGTKRKKATAEPSDNDILSQMTKKRKTKKE", "text": "FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. APN1 accounts for > 97% of both apurinic/apyrimidinic (AP) endonuclease and DNA 3'-repair diesterase activities. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP endonuclease 2 family."}
+{"protein": "MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHYNGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAINFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGVLRIFPEGKSFVADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALAKD", "text": "FUNCTION: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A (PubMed:24809345). Target proteins are preferentially recognized via a LXXLAP motif (By similarity). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins (By similarity). Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C- terminal, CODD) of HIF1A (By similarity). Also hydroxylates HIF2A (By similarity). Has a preference for the CODD site for both HIF1A and HIF2A (By similarity). Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site (By similarity). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (By similarity). Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy- inducible genes (By similarity). ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia (By similarity). Also hydroxylates PKM in hypoxia, limiting glycolysis (By similarity). Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis (By similarity). In cardiomyocytes, inhibits the anti- apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex (By similarity). In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity (By similarity). Also essential for hypoxic regulation of neutrophilic inflammation (PubMed:21317538). Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (By similarity). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (PubMed:24809345). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Colocalizes with WDR83 in the cytoplasm."}
+{"protein": "MDREAFVQTLTACRLCPRLVAWREEVVGRKRAFRGEPYWARPVPGFGDPEARILLFGLAPGAHGSNRTGRPFTGDASGAFLYPLLHEAGLSSKPESLPGDDLRLYGVYLTAAVRCAPPKNKPTPEELRACARWTEVELGLLPEVRVYVALGRIALEALLAHFGLRKSAHPFRHGAHYPLPGGRHLLASYHVSRQNTQTGRLTREMFLEVLMEAKRLAGL", "text": "FUNCTION: DNA glycosylase with broad substrate specificity. Can remove uracil from double-stranded DNA containing either a U/G, U/A, U/C or U/T base pair (PubMed:12000829, PubMed:17870091, PubMed:24838246). Can also excise hypoxanthine from double-stranded DNA containing G/I, T/I, and A/I base pairs, xanthine from both double-stranded and single stranded DNA, thymine from G/T mismatched DNA, 5'-hydroxymethyluracil and 5'-fluorouracil (PubMed:17870091, PubMed:24838246). SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. Type 5 (UDGb) family."}
+{"protein": "MTTKDHSLATESPTLQQLGEFAVIDRLVRGRRQPATVLLGPGDDAALVSAGDGRTVVSTDMLVQDSHFRLDWSTPQDVGRKAIAQNAADIEAMGARATAFVVGFGAPAETPAAQASALVDGMWEEAGRIGAGIVGGDLVSCRQWVVSVTAIGDLDGRAPVLRSGAKAGSVLAVVGELGRSAAGYALWCNGIEDFAELRRRHLVPQPPYGHGAAAAAVGAQAMIDVSDGLLADLRHIAEASGVRIDLSAAALAADRDALTAAATALGTDPWPWVLSGGEDHALVACFVGPVPAGWRTIGRVLDGPARVLVDGEEWTGYAGWQSFGEPDNQGSLG", "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": "MAFNGTVPSFCMDFTVYKVTISVILIILILVTVAGNVVVCLAVGLNRRLRSLTNCFIVSLAVTDLLLGLLVLPFSAIYQLSCKWSFSKVFCNIYTSLDVMLCTASILNLFMISLDRYCAVTDPLRYPVLITPARVAISLVFIWVISITLSFLSIHLGWNSRNETSKDNDTIVKCKVQVNEVYGLVDGLVTFYLPLLIMCITYFRIFKIAREQARRINHIGSWKAATIREHKATVTLAAVMGAFIICWFPYFTVFVYRGLKGDDAVNEVFEDVVLWLGYANSALNPILYAALNRDFRTAYHQLFCCRLASHNSHETSLRLNNSQLNRSQCQEPRWQEDKPLNLQVWSGTEVTAPQGATNR", "text": "FUNCTION: The H2 subclass of histamine receptors mediates gastric acid secretion. 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": "MSAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATPPGTPGAPPPPATAPGPGGATAAPHLLAASILADLRGGPVVATAASTAGGTSPVSSSSAASSPSSGRAPGAAKSHRCPFHGCAKAYYKSSHLKSHLRTHTGERPFACDWPGCDKKFARSDELARHHRTHTGEKRFPCPLCTKRFTRSDHLTKHARRHPGFRPELLRRPGARSVSPSDSLPCSLAGSPTPSPVPSPAPAGL", "text": "FUNCTION: Transcription factor that binds GC and GT boxes in the D1A, D2 and D3 dopamine receptor promoters and displaces Sp1 and Sp3 from these sequences. It modulates dopaminergic transmission in the brain by repressing or activating transcription from several different promoters depending on cellular context. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family."}
+{"protein": "MAPGKAPAGHFSILYFAAASTFTGKTSEHLPAPVRARHVFTMLEERYPGIGDKVLSSCAVTVNLEYVDIGEEDAEQQIEEGDEVAIIPPVSSG", "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 uba4. 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": "MMCGAPSATQPATAETQHIADQVRSQLEEKENKKFPVFKAVSFKSQVVAGTNYFIKVHVGDEDFVHLRVFQSLPHENKPLTLSNYQTNKAKHDELTYF", "text": "FUNCTION: This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. FUNCTION: This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cystatin family."}
+{"protein": "MEKKAFFQQLDERTDIRYTDSGMKIIRLKFPRAHLRLCNVKIDFGSRDVCLQAESGDTLLPYGTAHFLEHLLFWHNGRNLYTDFFAHGALLNAFTTYTDTNFMFTSLPDRLRQTIPILLDALWNHSFDKKMITQEKAVITSEIQTAHLNHQLYYHYQLISMLSPASPAAVFPAGRIEDIEALDIRDLQKAYNAAYQPQRMTLFLIGGSEDTEALLPPHLRLEKRPNHKAERKIISACPPPALSQKMVLGNEERIEDTWTGLQVGAIPGQNNLLTLKLYWDIASRILFQLDSPFFQEIQQTYRLEIDCLSAEAHMYEDGGFLILHSQGAHSSAYIDVASYYVTQQKQQIETWLQYGKDSLTDAIIYDSDYVRKCFEWAAECDRCDCTFLDMYRIIHDMNSQDFLSLIDALASSKKAVIHVSQKEAIGQ", "text": "FUNCTION: Required for production of the bacteriocin subtilosin. Could catalyze some step in the processing of presubtilosin (By similarity). SIMILARITY: Belongs to the peptidase M16 family."}
+{"protein": "MSALTKIREGLAREDNTHVAGTLAPHEKEIHETPEVVSEVGPDHDKEATAGAINPDDKGNDSDVPSEDVQNGVKEIQAITLTWGKGSLAALLCLIWTLFLISGFRGSFYLVLVPYVTSEWSAHSLMTTIPIVSDAMTAACYIPMAKALDVWGRAEGFLLMSGFATLGLILMAVSQNLATFCAAQVFYSVGWGGMIYAVGVLAADASNLRNRGLAFAFTSSPYMITAFAGSKAAAAFVIDVKNWRWGFGWIALVLPCVTIPLFLVLKVNLRKAFKNGTVTKTTRNRGFFGSIWWAFNEFDVIGIFLFGGGLVVFLLPFNLAGHAPNGWSTGYIIAMIIVGFCTLIFFGVWEYWLAPVPFLQGRFLLDRSVVAACMIDLTYQVSYYTWNYFFTSFLQVVVNLGPAEAGYVNSTFQVVSGVLLFIVGFLIRKTGFYKWTFYFAVPIYIFALGLMIHFRAPNQYVGYIIMCEIFISIGGAVFILVMQLAVLAAVAHQYVAAALATLYVAGGVGGAVGGAISGAIWTNSFIPQLIKRLPESEVANATLIAGSIVNQLAYPVDSPARLAIQESYGFAQIRMLAAGVGIASLFFIWVPMLRNIDVKKLKQTKGLVL", "text": "FUNCTION: Major facilitator transporter involved in extracellular siderophore uptake (PubMed:20507510). Gibberella zeae produces extracellular coprogen-type siderophores as well as the intracellular siderophore ferricrocin (PubMed:17056706). The role of extracellular siderophores is to supply iron to the fungus during plant infection, and the intracellular ferricrocin is required for intracellular iron distribution and storage with a crucial role in ascus and ascospore development (PubMed:17056706, PubMed:17043871, PubMed:17601875). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MSKVTVQDIEAVDDYWGPTFRSILEGNNTKQIGDQLEQRIRSHDKEIERICNLYYQGFIDSIQELLQVRTQAQQLHNEVHSLDTSLRQISASLIQQGNDLVRARQIESNLASAIEALKSCLPALECYMKFTQQAKNKQYYQALRTLETLETEHLTRLKTHNYRFATQMQIQIPIIKENIRRSSASDFREFLENIRKFSPRIGELAITHTKQLQKRDINAIIAEHMQQMNGGEAGGAGAGGDDDGANVSAQDLIDFSPIYRCLHIYMVLGQREYFEKDYRQQRRDQAKLVLQPPPNMHDNLEAYKTYICAIVGFFVVEDHVKNTAGDVVTSSYLEDLWSSSLTKFVNEISMSSSSCTDPNILLRIKNLIMLSINTFKCYGYTVNILWELLHNMRDHYNEVLLQRWVHVFREILDKEQFLPMVVQNTEEYECIIERFPFHSEQLENAPFPKKFPFSRMVPEVYHQAKEFMYACMKFAEELTLSPNEVAAMVRKAANLLLTRSFSGCLSVVFRQPSITLTQLIQIIIDTQYLEKAGPFLDEFVCHMTNTERSVSQTPSAMFHVARQDAEKQVGLRICSKIDEFFELSAYDWLLVEPPGIASAFITDMISYLKSTFDSFAFKLPHIAQAACRRTFEHIAEKIYSIMYDEDVKQISTGALTQINLDLMQCEFFAASEPVPGLKEGELSKYFLRNRQLLDLLILEEWSTYFHDYGKQENRYHLVQPQSIIVILEKIREADKKPIFSLVRKNDKKKLLETVLKQLKHIADRQN", "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 SEC15 family."}
+{"protein": "MTTSQQPPERVVVVGGQDWDQVVAAARQNAAEHAGERIVVNMGPQHPSTHGVLRLILEIEGEIIVEARCGIGYLHTGIEKNLEFRNWTQGVTFVTRMDYLSPFFNETAYCLGVEKLLGITDAIPERASVIRVMMMELNRISSHLVALATGGMELGAMTAMFLGFRERELILSVFETITGLRMNNAYIRPGGVAADLPDEALPQVRDLLTLLPKRLRDMEDLLNENYIWKARTQGIGYLDLTGCMALGITGPVLRSTGLPHDLRKAQPYCGYETYDFDVVTDDQCDSYGRYLIRVKEMHQSIRIVEQCVQRLERSVGAPVMITDKKLAWPADLKVGPDGLGNSPEHIAKIMGHSMEGLIHHFKLVTEGIRVPAGQVYVAVESPRGELGVHMVSDGGTRPYRVHYRDPSFTNLQAVAAMCEGGMVADAITAVASIDPVMGGVDR", "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": "MASATSNNPASSSMSPRRISGNHGSPTASVAQSPRRPSRQVSSPWTQIVRGESEPIAAAAAVAGPSSPQSRAPIEPIASVSVAAPTAAVLTVEAAAGDEKSEASGGQDNAGKKPVWKRPSNGASEVGPVMGASSWPALSETTKAPSNKSSSDSLKSLGDVPSSSSASSSVPVTQGIANASVPAPKQAGRANPNPTPNHSRQRSFKQRNGASGSANGTVSQPSAQGSFTELPSHNPSPRGQNQKNGFASQNHGGTENPSQRDSYRNQNGNHHQSHGGRRNQEHGNQNWTFQRSFNGREGNAQSQRGTPAFVRHPSPTVQPIPQFMAAQPFPSHIPFPTELAQSSYYPRMPYMTPIPHGPQFFYHYQDPPLHMKLHKQIQYYFSDENLITDIYLRGFMNNEGFVPLRVVAGFKKVAELTDNIQQIVEALQNSPHVEVQGDFIRKRDNWQNWVLRRNPTGSGPQSVDRADAVAKRLGNLSVDQSSADPIGGSSSQLQPTEALSDDQQQSSSTAPVSNHNAPDGANR", "text": "FUNCTION: Promotes leaf senescence mediated by abscisic acid (ABA), salicylic acid (SA) and jasmonic acid (MeJA), probably though the induction of expression of senescence-associated genes (SAGs) and defense-related genes. SUBCELLULAR LOCATION: Cytoplasm Note=Present in cytoplasmic foci. SIMILARITY: Belongs to the LARP family."}
+{"protein": "MPPPAEEFAVDDLDEFESRLDSFLNRFHADDLRRILLPDPDGKLHFPLVIDFAELLEFDPEVAHQLYDYPKDVLELFDAAAQRALDKFDAAARRADKRKAGDEPMEKKFVHVRVNTSGSPLECPEASPSIGKVRVKHRGTLLTLKGTVIRSGGVKMIEGERKYQCRKCKCRFTVHPELEAGNRITLPASCKSKSAKGCGGANFQLIEDSITCHDYQEIKIQENIQLLGVGSIPRSMPIILMDDLVDIVKAGDDVVVTGRLSAKWSPDIKDVRSNLDPMLIANFVRRTNELKSDLDIPVEIINKFEEFWAASRATPLKGRNSILKGICPQIYGLFTVKLAVALTLIGGVQHVDASGTKVRGEPHMLLVGDPGTGKSQFLKFAAKLSNRSVITTGLGSTSAGLTVTAVKDGGEWMLEAGALVLADGGLCCIDEFDSMREHDRTTIHEAMEQQTISIAKAGLVTTLNTRTTVFGATNPKGQYDPNESLSVNTTLSGPLLSRFDIVLVLLDTKNKKWDKIVSSHILAENTEEKKGKTSDPEVMWTLSMLRRYIHYVKQHFKPVLTKEAERVISSYYQRQRQSGTRNAARTTVRMLESLIRLAQAHARLMFRNDVTKLDAIAAILCIESSMTTSAIVDTAGNALHSNFTENPDQECILKCDSIAYLSKNIKYLTDEISN", "text": "FUNCTION: Probable DNA helicase that may play a role in DNA repair during meiosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MCM family."}
+{"protein": "MVNAMVERATSEMLIGPDWAMNLEICDMLNSDPAQAKDVVKGIKKRIGSRNPKAQLLALTLLETIVKNCGDMVHMHVAEKGVIHEMVRIVKKKPDFHVKEKILVLIDTWQEAFGGPRARYPQYYAGYQELLRAGAVFPQRSERSAPVFTPPQTQPLTSYPPNLRNAGPGNDVPEPSAEPEFPTLSLSEIQNAKGIMDVLAEMLSALEPGNKEDLKQEVMVDLVEQCRTYKQRVVHLVNSTSDESLLCQGLALNDDLQRVLTNYEAIASGLPGTSSQIEKPKSETGKSLVDVDGPLIDTGDSSNQANGATSSSGNGVLNQLALPAPPVTNGSANSKIDLLSGDDLALVPVGPPQPASPVASDQNALALIDMFSDNTNNPSPATAPSGNPAQNIPLNPQGHQQPNSQAGEAGLQQSNGFAPQVGYSQFEQPSYGQGVSSPWSSQPAQQPVQPSYGAQDSTAFPPPPWEAQLQDYSPSAESGSPFSPGMHPTQTAFTHAQPVNNNNPYPQIPQTGPPVNNNSPYAQMPQTGQAVANISPYPQIPQNGVYMPNQPNQALGSGYQPQQQQQQQMMMAQYYAQQQQLQQQQQQQAYGNQMGGYGYGYNQQQQGSSPYLDQQMYGLSMRDQTSHQVASSSSTTSYLPPMKPKNKPEDKLFGDLVDISKFKPTKPTSGRAGTM", "text": "FUNCTION: Might contribute to the loading of the ESCRT machinery. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TOM1 family."}
+{"protein": "MPHSDELDAGNVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLQRRSREVIELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQAPPIEQKTVVDGEPVLRVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKDAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVPVAEPSRQRPQRVLLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAFMRR", "text": "FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Glutathione importer (TC 3.A.1.5.11) family."}
+{"protein": "MSRRGTAEEKTAKPDPIYWNRLVNMLVNRILKHGKKSLAYQIIYRALKKIQQKTEKNPLYVLRQAIRGVTPDIAVKARRVGGSTHQVPIEIGSTQGKALAVRWLLVASKKRPGQNMAFKLSSELVDAAKGSGDAIRKKEETHKMAEASRAFAHLR", "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": "MTYPQNVGIKAMEIYVPPQCLDQTLFEKHQGVSAGKYTIGLGLQYMNFCTDREDVCSLALTAVSSLLRKFDIDPKSIGRLEVGTESPIDKAKSVKSVLTTLFEPHGNTSLEGIDTIHACYGGTSALFNAVNWVESRSWDGRDAIVVASDIALYKEDASRPTGGAGCVAMLIGPNAVLSLEPSLRGVYMTNTFDFYKPDMKVEFPIVNGHESIACYLGALDECHKDLLRRTEAAKKQLNGDAPKTGKKVLDLFDYMAFHTPNCKLVSKSYGRLKYNDCLNSTNAADWEGIPDELRNLSYKDSLKDKTLERALVAATKTEFKMRVEPCIAAPSLCGNMYTASLYCSLISLISNIDLASAEGKTIGLFSYGSGAASTLFGMRVTGDLTNMVQKIDLMRRLKQRNIQTPEDYEKACALRLKAYGNKSYKPLGDVSSLTPGTYYLKSIDEAYRRTYAIKGQ", "text": "FUNCTION: HMG-CoA synthase; part of the gene cluster that mediates the biosynthesis of 1233A, a natural compound known as an inhibitor of HMG- CoA synthase in the mevalonate pathway and with antibacterial and antifungal activities (PubMed:32139880). This enzyme condenses acetyl- CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase (By similarity). As part of the 1233A biosynthesis cluster, is involved in conferring self-resistance to 1233A (PubMed:32139880). SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase family."}
+{"protein": "MKFYIVFALILACAACVSSQEGTNFYCGRQLSRTLALVCWGAEKRDAGWWVPPQSARALGGGRGKRGPVDECCLKPCSIEEMLTYC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
+{"protein": "MSWLWGSTTNPQFEELAEKACSPLNLPYPQSEDIATALEVADMIRSKAIQPKMAMQSLKKRIASKNGRVQMYAIGLTDTCIKNGGDHFLLEVASKEFVDELSNLIKATTTSPEVKQMLIKYFQQWALAFKSKSELSFFVEVYNELRASGITFPPPPAPVPSHLLTTTTAPAWVDSDACMRCRSAFTFTNRKHHCRNCGLVFDQACSSHSMPLPKYGITEEVRVCDGCWAKAGRNKADAPAPAVPGRTPRSRADLDADLQRAIELSLAESQHSQNRHHSHFTPSEPPLAHGTVEDEDEQMRLAIEASLRDMEARPSAPAGLGEAPEPEYRPLPTFDLSPRENETILTFSNTMDQMAAYGERDLRRFPHAHVLAEQANTVGGRLRRNVEEKSTKQQMLMEMQDKLSQAVNLYGQILDGQQAYAAKRAHEEQARRYQQQQSYYTQQYQPQPQLYGQYPPNGYQAFVPPQQAYQPPQPQPEAQAQHAPSLYPTMPYTTPNFTSPPQERVYPQQSHSSPYSQWSPAPSHVQPGLARQASVVVPPVSSPVPAGVQRQASMTYGAPIPVAEQSQRQQQQYASAPPFASGAAPVDIPSAPPPVNLSTHPNSPQRHSYIPSHPQTQTQTQYESQPQEIPSQQDMQYGASAPPPDSLGSYVSEGTVGSAKSGLEQEHAASQIQPQPQPQASAQTQTQSQSQLQAQPQQNQYAAQTQLPAGMYNAASFPQPLPPTIFPDAPVEAPKGLEKEEKEEALLIEL", "text": "FUNCTION: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the VPS27 family."}
+{"protein": "MVRKPVVSTISKGGYLQGNVNGRLPSLGNKEPPGQEKVQLKRKVTLLRGVSIIIGTIIGAGIFISPKGVLQNTGSVGMSLTIWTVCGVLSLFGALSYAELGTTIKKSGGHYTYILEVFGPLPAFVRVWVELLIIRPAATAVISLAFGRYILEPFFIQCEIPELAIKLITAVGITVVMVLNSMSVSWSARIQIFLTFCKLTAILIIIVPGVMQLIKGQTQNFKDAFSGRDSSITRLPLAFYYGMYAYAGWFYLNFVTEEVENPEKTIPLAICISMAIVTIGYVLTNVAYFTTINAEELLLSNAVAVTFSERLLGNFSLAVPIFVALSCFGSMNGGVFAVSRLFYVASREGHLPEILSMIHVRKHTPLPAVIVLHPLTMIMLFSGDLDSLLNFLSFARWLFIGLAVAGLIYLRYKCPDMHRPFKVPLFIPALFSFTCLFMVALSLYSDPFSTGIGSVITLTGVPAYYLFIIWDKKPRWFRIMSEKITRTLQIILEVVPEEDKL", "text": "FUNCTION: Heterodimer with SLC3A2, that functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (By similarity). Provides L-cystine for the maintenance of the redox balance between extracellular L-cystine and L-cysteine and for the maintenance of the intracellular levels of glutathione that is essential for cells protection from oxidative stress (By similarity). The transport is sodium-independent, electroneutral with a stoichiometry of 1:1, and is drove by the high intracellular concentration of L-glutamate and the intracellular reduction of L- cystine. In addition, mediates the import of L-kynurenine leading to anti-ferroptotic signaling propagation required to maintain L-cystine and glutathione homeostasis. Moreover, mediates N-acetyl-L-cysteine uptake into the placenta leading to subsequently down-regulation of pathways associated with oxidative stress, inflammation and apoptosis. In vitro can also transport L-aspartate (By similarity). May participate in astrocyte and meningeal cell proliferation during development and can provide neuroprotection by promoting glutathione synthesis and delivery from non-neuronal cells such as astrocytes and meningeal cells to immature neurons. Controls the production of pheomelanin pigment directly (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, microvillus membrane; Multi- pass membrane protein Note=Localized to the microvillous membrane of the placental syncytiotrophoblast. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family."}
+{"protein": "MAEAEGESLESWLNKATNPSNRQEDWEYIIGFCDQINKELEGPQIAVRLLAHKIQSPQEWEAVQALTVLEACMKNCGRRLHNEVGKFRFLNELIKVVSPKYLGDRVSEKVKAKVIELLFSWTLALPEEAKIKDAYHMLKRQGIVQSDPPIPMDRTLIPSPPPRPKNPVFDDEEKSKLLAKLLRSKNPDDLQEANQLIKSMVKEDEARIQKVTKRLHTLEEVNNNVKLLHEMLLHYSQEFSSEADKELMKELFDRCENKRRTLFKLASETEDNDNSLGDILQASDNLSRVINSYKTIIEGQIINGEVTTSTVPDSEGNSHCGNQGALIDLAELDTPSSSSPVLAPAPAPPTSGIPILPPPPQTSGPPRSRSSSQAEAPSGPDSTNNALSLLDEELLCLGLSDPAPTAPKESAGNSPWHLFQNEPSSDLDFFSPRLVSAASCPSEGSLLPPPVSTSSLSQAPLPAAFPAPVVPASAVTHSTGSFTFSSGPAPALVPKAEPEGPEYPSSSISHRLDALDQLLEEAKVTSGLVKPVSCFSPGPTASPLLPASTPARPLLPFSTGPGSPLFQSPAFQSQGSPQKGPELSLASVHVPLESIKPSSALPVTAYDKNGFRILFHFAKECPPGRPDVLVVVVSMLNTAPLPVKSIVLQAAVPKSMKVKLQPPSGTELSPFSPIQPPAAITQVMLLANPMKEKVRLRYKLTFALGEQLSTELGEVDQFPPVEQWGNL", "text": "FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell surface. Involved in BACE1 transport and sorting as well as regulation of BACE1 protein levels. Regulates retrograde transport of BACE1 from endosomes to the trans-Golgi network via interaction through the VHS motif and dependent of BACE1 phosphorylation. Modulates BACE1 protein levels independently of the interaction between VHS domain and DXXLL motif through recognition of ubiquitination (By similarity). Key player in a novel DXXLL-mediated endosomal sorting machinery to the recycling pathway that targets NTRK1 to the plasma membrane (PubMed:26446845). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Early endosome membrane; Peripheral membrane protein Recycling endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the GGA protein family."}
+{"protein": "MMMFITVYDINQKQKKRYGLRGCNLNLKATVLPLHKRI", "text": "SIMILARITY: Belongs to the asfivirus C84L family."}
+{"protein": "MEALGPGPPASLFQPPRRPGLGTVGKPIRLLANHFQVQIPKIDVYHYDVDIKPEKRPRRVNREVVDTMVRHFKMQIFGDRQPGYDGKRNMYTAHPLPIGRDRVDMEVTLPGEGKDQTFKVSVQWVSVVSLQLLLEALAGHLNEVPDDSVQALDVITRHLPSMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWNMMLNIDVSATAFYRAQPIIEFMCEVLDIQNINEQTKPLTDSQRVKFTKEIRGLKVEVTHCGQMKRKYRVCNVTRRPASHQTFPLQLENGQAMECTVAQYFKQKYSLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLVKSNSMVGGPDPYLKEFGIVVHNEMTELTGRVLPAPMLQYGGRNKTVATPNQGVWDMRGKQFYAGIEIKVWAVACFAPQKQCREDLLKSFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFKHLKMTYVGLQLIVVILPGKTPVYAEVKRVGDTLLGMATQCVQVKNVVKTSPQTLSNLCLKINAKLGGINNVLVPHQRPSVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDGHPSRYCATVRVQTSRQEISQELLYSQEVIQDLTNMVRELLIQFYKSTRFKPTRIIYYRGGVSEGQMKQVAWPELIAIRKACISLEEDYRPGITYIVVQKRHHTRLFCADKTERVGKSGNVPAGTTVDSTITHPSEFDFYLCSHAGIQGTSRPSHYQVLWDDNCFTADELQLLTYQLCHTYVRCTRSVSIPAPAYYARLVAFRARYHLVDKDHDSAEGSHVSGQSNGRDPQALAKAVQIHHDTQHTMYFA", "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. Also required for RNA-directed transcription and replication of the human hapatitis delta virus (HDV). SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the argonaute family. Ago subfamily."}
+{"protein": "MSGREGGKKKPLKAPKKEQSEMDEDTAAFKAKQKEQQKALEAAKQKATKGGPLLQGGIKKSGKK", "text": "SIMILARITY: Belongs to the TMA7 family."}
+{"protein": "MRKKLNGWLAMAAGAALAALSSVSHAEDRKTVAYLAPSLDISYWQWVGFGVKQKAQELGMDYVEFTSENSPAKQMDNARTAVTKGVDAIVIGPVSSTSTPPLLAYLKSQNIPIAFAGIGPQPGQTDYTSSVTANNYETGKAQGSFVCALAKERGGNKVGMLSLPQDRENAQKYLKGAQEAFAADGCELVQMLETRGLTVNEAVTQANDMLTAHPDIKAIYGMYDEAGTGAAKVLETRGLTGKIGIAVADGSPTTIALLKATAIQGIFFQEAVGQGIDGTLQVFNALTNAPVEKDLALVMPLVTADKIDTAEAKAVIARVFPPSN", "text": "FUNCTION: Probably part of the binding-protein-dependent transport system y4mIJK. This system probably transports a sugar. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 2 family."}
+{"protein": "MQSRKTRALGKGRARVTSCDDTCATATEMVPDAKDRILASVRDYHREQESPTFVAGSTPIRPSGAVLDEDDRVALVEAALELRIAAGGNARRFESEFARFFGLRKAHLVNSGSSANLLALSSLTSPKLGEARLRPGDEVITAAVGFPTTINPAVQNGLVPVFVDVELGTYNATPDRIKAAVTERTRAIMLAHTLGNPFAADEIAEIAKEHELFLVEDNCDAVGSTYRGRLTGTFGDLTTVSFYPAHHITSGEGGCVLTGSLELARIIESLRDWGRDCWCEPGVDNTCRKRFDYHLGTLPPGYDHKYTFSHVGYNLKTTDLQAALALSQLSKISAFGSARRRNWRRLREGLSGLPGLLLPVATPHSDPSWFGFAITISADAGFTRAALVNFLESRNIGTRLLFGGNITRHPAFEQVRYRIADALTNSDIVTDRTFWVGVYPGITDQMIDYVVESIAEFVAKSS", "text": "FUNCTION: Involved in the biosynthesis of forosamine ((4- dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D (PubMed:11358695, PubMed:18345667). Catalyzes C-3 deoxygenation of dTDP-4-keto-2,6- dideoxy-alpha-D-glucose to yield dTDP-4-keto-2,3,6-trideoxy-D-glucose via a combined transamination-deoxygenation reaction (PubMed:18345667). The catalysis is initiated by a transamination step in which pyridoxal 5'-phosphate (PLP) is converted to pyridoxamine 5'-phosphate (PMP) in the presence of L-glutamate (PubMed:18345667). This coenzyme then forms a Schiff base with dTDP-4-keto-2,6-dideoxy-alpha-D-glucose and the resulting adduct undergoes a PMP-mediated beta-dehydration reaction to give a sugar enamine intermediate, which after a 2 electrons reduction and hydrolysis yields dTDP-4-keto-2,3,6-trideoxy-D-glucose as a product (PubMed:18345667). Requires cellular reductase (ferredoxin or flavodoxin reductase) rather than a specific partner reductase (PubMed:18345667). L-glutamate is 20-fold more efficient than L- aspartate as an amino donor (PubMed:18345667). In the absence of an electron source and in the presence of L-glutamate, catalyzes a transamination reaction, converting dTDP-4-keto-2,6-dideoxy-alpha-D- glucose to dTDP-4-amino-2,4,6-trideoxy-D-glucose (PubMed:18345667). SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family."}
+{"protein": "MSLSGRERPAWPGSRLSWLLCCSALLSPAAGYVIVSSVSWAVTNEVDEELDSASTEEALPALLEDSSSIWQQSFPASAHKEDTHLRPRGSARARPAPAARGMFSYRRESGSSEASPGPRVHAGTARSLAHASSWGCLATVSTHEKIQGLPFGSCLAISDGPVHNSTGIPFFYMTAKDPAVADLVKNPTASLVLPESEGEFCRKNIVDPEDPRCARLTLTGRMVTVPPGEVEFAKQAMFSRHPGMRKWPRQYEWFFMKMWVEHIWLQKWYGGVSDIPREEYFKAAPRKA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CREG family."}
+{"protein": "MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSGGGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAAGGGAAGEPLKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATADEPPPKNGRAGAPAGAGGHSNHRHHAHHAHPRASASAPPLPQAPQPPAPSRSAPGGPAASPSALLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPGAAAAAQQLGLGPPFPGPPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTMGRHGGHSFIYLQEALQDSRALTIQLLADAQQGRQAIQLSIEQAQTVAEQVEMKAKVVQSEVKAVTARHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLRQNLNKLESTISAVQQVLEEGRALDILLARDRMLAQVQELKTVRSLLQPQEDDRVMFTPPDQALYLAIKSFGFVSSGAFAPLTKATGDGLKRALQGKVASFTVIGYDHDGEPRLSGGDLMSAVVLGPDGNLFGAEVSDQQNGTYVVSYRPQLEGEHLVSVTLCNQHIENSPFKVVVKSGRSYVGIGLPGLSFGSEGDSDGKLCRPWGVSVDKEGYIIVADRSNNRIQVFKPCGAFHHKFGTLGSRPGQFDRPAGVACDASRRIVVADKDNHRIQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRIQLFGPDGVFLNKYGFEGALWKHFDSPRGVAFNHEGHLVVTDFNNHRLLVIHPDCQSARFLGSEGTGNGQFLRPQGVAVDQEGRIIVADSRNHRVQMFESNGSFLCKFGAQGSGFGQMDRPSGIAITPDGMIVVVDFGNNRILVF", "text": "FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (Probable). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (PubMed:23125361). Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (PubMed:28431233). SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the TRIM/RBCC family."}
+{"protein": "MKRNNKSAIALIALSLLALSSGAAFAGHHWGNNDGMWQQGGSPLTTEQQATAQKIYDDYYTQTSALRQQLISKRYEYNALLTASSPDTAKINAVAKEMESLGQKLDEQRVKRDVAMAQAGIPRGAGVGYGGCGGYGGGYHRGGGHMGMGNW", "text": "FUNCTION: Binds zinc. Could be an important component of the zinc- balancing mechanism (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the ZraP family."}
+{"protein": "MEATGAEATLSQVTAVDGEDNLFQDKESRATAKERGEAAVFGLENIVTANGATSAADLAPPKDVVDEWPEPKQTHTFFFVRICSYEDPSLKAKLEQADKECQKKIQARSHIFEALRTKRSERSNIISELKPLAAENKQYNEVVSGKLKEIEPLQKSLGKFRSENNAMRAQGAGLCSSIEELDQLIKSLNDRISHESISLDEEKRLVKEIKQLNGTRSKVIENAAKRAKMQDTVVERGTIHDQVKQIGVGIDEVKRDRQAVRDKIKVLEDQIHAVDGEIAALQDDLTAATARKDKAFEALNELRKTRDLNNTSFHQYRTISNSVRDLSARGEVEAVQQLCQNEVEKFMAQWCSSKSFREDYEKRILVSLNSRQLSRDGRMRNPDEKPIVLETQVAPPAEQEPAPLKKPAKQAKEAPAPRADVTPKDEIRAKAPAKAAKAKQPLDIDDIPDVHDDEPPKEKTKPKVDEAKLKEMKRQEEIEKNKLALERKKKQAEKQAMKAAARAEKEAEKKLKEKEKKARKRSATAGGAESEEAAESDAKSDEAEAQEEEPAAPVTIKKNARHRSTVTKTKTPLPKAVLKRKKSQAFWSWGAPMAALAAALVALLGALVYYQYYYLPASTSN", "text": "FUNCTION: May regulate plasma membrane ATPase activity. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the plant proton pump-interactor protein family."}
+{"protein": "MTNNDAAVEAPSSSRASSSKQQPKLEITEKVRVLCLHGYRQDGDAFKNKLGSFRKFTSKYAEFVFISAPHIAAPLESAAEPVPEQRSWWANKDDGTFKGTNKGGPAFGFQDSLRLVEEAWKTQGPFQGLLGFSQGACFVGLICGLAKKKLTSIRPEFAVLSSGFVSGSLVHMSAYEEPVSIPTLHIYGSSDEIIPKDMSALLASHFKNVEVLEHGGGHYFPATAQQKQTYINFFQDRLQEYLEHLELQQSSSVSFIESGAEDNDDDGDANDAEVAAATAAAGSDLDDSD", "text": "SIMILARITY: Belongs to the LovG family."}
+{"protein": "ACKDGFPTATCQHAKLVGNCKNSQKYRANCAKTCGPC", "text": "FUNCTION: Inhibits voltage-gated potassium channels (IC(50)=14.42 nM for rKCNA1/Kv1.1, IC(50)=80.4 nM for rKCNA2/Kv1.2, IC(50)=7.76 nM for rKCNA6/Kv1.6, IC(50)=13.12 nM for hKCNA3/Kv1.3, and IC(50)=49.14 nM for insect Shaker IR). Binds the Shaker IR channels in a voltage- independent manner. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin family. Type 1b subfamily."}
+{"protein": "MALAVRLLPRLLLSRPLPGWAARLRTLSSAEVKRPLSGLCYLCRRRLGSGAAPFPRVSWASAALALSARGPQRPLLSPLEVASTLPTFPSCPRRTYSTEEQPQQRQKTKMIILGFSNPINWVRTRIYSFLIWAYFDQEFSITEFSEGAKQAFAHVSKLLSQCKFDLLEELVAKETLHVLKEKVTSLPDNHKNALAADIDEIVYTSTGDISIYYDEKGRKFVNILMCFWYLTSANIPSEAISGARVFQVKLGDQNVETKQLLSASYEFQREFTQGVKPDWTIARIEHPKLLE", "text": "FUNCTION: Promotes sorting of SMDT1/EMRE in mitochondria by ensuring its maturation. Interacts with the transit peptide region of SMDT1/EMRE precursor protein in the mitochondrial matrix, leading to protect it against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB). SUBCELLULAR LOCATION: Mitochondrion matrix."}
+{"protein": "MSGQNIDPAANQVRQKERPRDMTTSKERHSVSKRLQQELRTLLMSGDPGITAFPDGDNLFKWVATLDGPKDTVYESLKYKLTLEFPSDYPYKPPVVKFTTPCWHPNVDQSGNICLDILKENWTASYDVRTILLSLQSLLGEPNNASPLNAQAADMWSNQTEYKKVLHEKYKTAQSDK", "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 is essential for the transition from metaphase to anaphase in mitosis. Involved in both degradation of proteins responsible for maintaining sister chromatid cohesion at the onset of anaphase and of mitotic cyclins A and B at the exit of mitosis. Acts by initiating 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": "MDSIVSSSTILMRSYLTPPVRSCSPATSVSVKPLSSVQVTSVAANRHLLSLSSGARRTRKSSSSVIRCGGIKEIGESEFSSTVLESAQPVLVEFVATWCGPCKLIYPAMEALSQEYGDKLTIVKIDHDANPKLIAEFKVYGLPHFILFKDGKEVPGSRREGAITKAKLKEYIDGLLNSISVA", "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": "MPTCWILNESVSFVVALLWLAINIYLFIDTFCWYAEEESFFYTRVILGSALAWARASAVCLNFNCMLILLPVSRNFVSLVRGTSVCCRGPWRRQLDKNLKFHKLVAYGIAVNSVIHIVAHLFNLERYHLGQAKDAEGLLAALSKLGNAPNESYLNPVRTLYTGTTTQLLMTVSGITGLVISLALILIMTSSTEFIRQSSYELFWYTHHIFIFLFISLAIHGGGRIIRGQTPESLRLHNVTFCRDHFDEWQEAASCPVPQFSGKEPSAWKWTLGPVVLYACEIIIRFWRSHQEVVITKVVSHPSAVLELHMKKRDFKMAPGQYIFIQCPSISPLEWHPFTLTSAPQEDFFSVHIRASGDWTEALLKAFGAEGQAPSELCSMPRLAVDGPFGGSLADVFHYPVSVCIATGIGVTPFASLLKSVWYKCCESQSLPGLSKVYFYWICRDAAAFEWFADLLLSLETQMSEQGKAHLLSYHIYLTGWDEYQAIHIALHWDESLDVITGLKQKTFYGRPNWNEEFKQIAYNHPSSSIGVFFCGPKAMSKTLQKMCRLYSSSDPRGVHFYYNKENF", "text": "FUNCTION: NADPH oxidase which constitutively produces superoxide upon formation of a complex with CYBA/p22phox. Plays a role in the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
+{"protein": "MPALGEILLVPETDKGKSKDYIEVSEDEKITRTRSRSLKKKAIKASNKLTHSLRKRGKRVADQYAPIVIEDVRDEEEEKAVNVFRKALVSLDLLPPRHDDYHTMLRFLKARRFDLEKTVQMWEEMLKWRKENGVDTIIQDFVYDEYEEVQQYYPHGYHGVDREGRPVYIERLGKIDPGKLMKVTTLERFLRYHVQGFEKTFSEKFPACSIAAKRHINSSTTIIDVHGVSWMSFRKLAQDLVMRMQKIDGDNYPETLNQMYIINAGNGFKLVWNTVKGFLDPKTTSKIHVLGNKYRSHLLEIIDPSELPEFLGGNCKCAHEGGCMRFNKGPWNDPEIMKLVRSRDAMYKPKEMGLLENGEVAKLFSLRHVNTDMSSPDGGHVRERESHPEHDKRAQLSNQAEAVGVGRMEQSDSTSPLPNNLAVERSLTTSLQKVASFLARFILQLLGSLCLMFRILGRLVNKQPENQLRPELSVSVSQQQVPPPQVHPCWLRLQNLETMVTVLCDKPSSIPQEKEDILRDSLDRIKSIEQDLQKTKKALFLTASKQIELAECFENLKESSSTGMRSCWPRHCRNFQAET", "text": "FUNCTION: Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SFH family."}
+{"protein": "MDPNCSCATGDSCACASTCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA", "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. This isoform may play a role in regulating the transport, accumulation, and compartmentation of zinc in the hippocampus. SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family."}
+{"protein": "MSGDEMIFDPTMSKKKKKKKKPFMLDEEGDAQTEETQPSETKEVEPEPTEEKDVDADEEDSRKKDASDDLDDLNFFNQKKKKKKTKKIFDIDEAEEAIKDVKIESDAQEPAEPEDDLDIMLGNKKKKKKNVKFPEEDEILEKDEALEDEDSKKDDGISFSSQTAWAGSERDYTYEELLNRVFNIMREKNPDMVAGEKRKFVMKPPQVVRVGTKKTSFVNFTDICKLLHRQPKHLLAFLLAELGTSGSIDGNNQLVIKGRFQQKQIENVLRRYIKEYVTCHTCRSPDTILQKDTRLYFLQCETCHSRCSVASIKTGFQAVTGKRAQLRAKAN", "text": "FUNCTION: Component 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. SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family."}
+{"protein": "MKFDRHRRLRSSKTMRDLVRETHVRKEDLIYPIFVVEQDDIKSEIKSLPGIYQISLNLLHEEIKEAYDLGIRAIMFFGVPNDKDDIGSGAYDHNGVVQEATRISKNLYKDLLIVADTCLCEYTDHGHCGVIDDHTHDVDNDKSLPLLVKTAISQVEAGADIIAPSNMMDGFVAEIREGLDQAGYQNIPIMSYGIKYASSFFGPFRDAADSAPSFGDRKTYQMDPANRLEALRELESDLKEGCDMMIVKPSLSYLDIIRDVKNNTNVPVVAYNVSGEYSMTKAAALNGWIDEEKIVMEQMISMKRAGADLIITYFAKDICRYLDK", "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": "MMNYVKSLGTYNTRNMEKESSKDLVQNEDTPLPVQKISMSLFHEIVFVFIACTAQLMTQAGLGQSIAPNNIIGKSLGTTNPGQLSWFPASYSLTVGTFILIAGRLGDIYGHKKMFVLGYIWFCIWSLISGFSYYAKSVIMFDVCRALTGIAPAFLLPNALALLGRVYPPGKKKNLIFALFGATAPNGFLLGSVFSGIFAQLSWWPWTYWTTAIVCIVFAIIGYFAIPHIEADEVEEKQKFDYLGAFFGVSGLVLINFSWNQGPVVGWQVPYVYILLIIGFLSLVVFVLVEKRVVQPILAPSMMNSEMGCVLICVAAGWACFGIWMYYLWQFLENLRFATPLLVTAQLTPVGISGCAAALTTGYLLKRLKPTKIMVVSMIAFTVGTILIATAPIHQTYWAQTFVSIIVTPWGMDMSFPAATLMLSDFVPKQHQGIAASLVSTVVNYSISIGLGIAGTVETHLNHKGVDLIRGYRSAWYMGTGFGGLGVCVAILTVFASYLKVGQQKSPKFPLIMKNTKAV", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MAVSARPARAPRGSDKVKKDKAAQTSGPRQGSRMGKLLGFEWTDVSSWERLVTLLNRPTDPAGLAVFRFLFGLMMVLDIPQERGLSSLDRRYLDGLEVCRFPLLDALQPLPLDWMYLIYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFVDAHHYWSVDGLLRARKRNAHVPLWNYAVLRGQIFIVYFIAGIKKLDADWVEGYSMEYLSRHWLFSPFKLVLSEEMTSLLVVHWCGLLLDLSAGFLLFFDASRPIGFVFVSYFHCMNSQLFSIGMFPYVMLASSPLFCSPEWPRKLVAHCPKKLQELLPLRTAPQPSTSCMYKRSRARGSQKPGLRHKLSTAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTPWLQPLLMDLSPWRTKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLQEGEKMQLPAGEYHKVYTVSSSPSCYMYIYVNTTEVALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNAPFHERLVRFLLRKLFIFRRSFLMTCISLRNLAFGRPSLEQLAQEVTYANLRPFEPAGEPSPVNTDSSNPNPPEPDSHPVHSEF", "text": "FUNCTION: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
+{"protein": "MINDINNFIESKKLSLNSRKSYHYDLKQFYKIIGGHVNSEKLALYQQSLSEFKLTARKRKLSAVNQFLFFLYNRGTLKEFYRLQETEKITLAQTKSQIMDLSNFYQDTDYPSGRLIALLILSLGLTPAEIANLKKADFDTTFNILSIEKSQMKRILKLPEDLLPFLLESLEEDGDLVFEHNGKPYSRQWFFNQLTDFLNEKNEQQLTAQLLREQFILKQKENGKTMTELSRLLGLKTPITLERYYR", "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": "MESERSKRMGNACIPLKRIAYFLCLLSALLLTEGKKPAKPKCPAVCTCTKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGGFLFTPSLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNLQTLPKDIFKGLDSLTNVDLRGNSFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKINSLSSKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKTFRNYDNITGTSTVVCKPIVIETQLYVIVAQLFGGSHIYKRDSFANKFIKIQDIEILKIRKPNDIETFKIENNWYFVVADSSKAGFTTIYKWNGNGFYSHQSLHAWYRDTDVEYLEIVRTPQTLRTPHLILSSSSQRPVIYQWNKATQLFTNQTDIPNMEDVYAVKHFSVKGDVYICLTRFIGDSKVMKWGGSSFQDIQRMPSRGSMVFQPLQINNYQYAILGSDYSFTQVYNWDAEKAKFVKFQELNVQAPRSFTHVSINKRNFLFASSFKGNTQICKHVIVDLSA", "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."}
+{"protein": "MGELNKSARQIVEAVGGAENIAAATHCVTRLRFALIDESKVDQEMLDQIDVVKGSFSTNGQFQVVIGQGTVNKVYAELVKETGIGESTKDEVKKASEKNMNPLQRAVKTLADIFIPILPAIVTAGLLMGINNILTAEGIFFSTKSIVQVYPQWADLANMINLIAGTAFTFLPALIGWSAVKRFGGNPLLGIVLGVMLVHPDLLNAWGYGAAEQSGEIPVWNLFGLEVQKVGYQGQVLPILLASYMLAKIEVFLTKRTPEGIQLLVVAPITLLLTGFASFIIIGPITFAIGNVLTSGLISVFGSFAALGGLLYGGFYSALVITGMHHTFLAVDLQLIGSKLGGTFLWPMLALSNIAQGSAALAMMFIVKDEKQKGLSLTSGISAYLGITEPAIFGVNLRYRFPFIIAMVSSGLAGMYISSQGVLASSVGVGGVPGIFSIMSQYWGAFAIGMAIVLIVPFAGTYAYARFKHK", "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 trehalose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDALTRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRALEQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF", "text": "FUNCTION: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:7668252, PubMed:9461620, PubMed:18227065, PubMed:9839948, PubMed:9599005). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl- CoA (PubMed:7668252, PubMed:9461620, PubMed:18227065, PubMed:9839948). Among the different mitochondrial acyl-CoA dehydrogenases, very long- chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains (PubMed:21237683, PubMed:9839948). SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
+{"protein": "MKDRTQELRSAKDSDDEEEVVHVDRDHFMDEFFEQVEEIRGCIEKLSEDVEQVKKQHSAILAAPNPDEKTKQELEDLTADIKKTANKVRSKLKAIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMTEYNATQSKYRDRCKDRIQRQLEITGRTTTNEELEDMLESGKLAIFTDDIKMDSQMTKQALNEIETRHNEIIKLETSIRELHDMFVDMAMLVESQGEMIDRIEYNVEHSVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVVLGVVLASSIGGTLGL", "text": "FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones (PubMed:7901002). May mediate Ca(2+)- regulation of exocytosis acrosomal reaction in sperm (By similarity). FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity). FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones (By similarity). May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Note=Colocalizes with Lamin A/C and NuMA in interphasic nuclei, and with NuMA and gamma- tubulin in the pericentrosomal region of the mitotic spindle in dividing cells. SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type IV membrane protein. SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the syntaxin family."}
+{"protein": "MIKSWWAEKSTSEKQIVAALAVLSLGVFCWLGVIKPIDTYIAEHQSHAQKIKKDIKWMQDQASTHGLLGHPALTQPIKNILLEEAKRENLAITLENGPDNTLTIHPVTAPLENVSRWLTTAQVTYGIVIEDLQFTLAGNEEITLRHLSFREQQ", "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 GspL resulting in a stable complex in the inner membrane. Provides thus a link between the energy-providing GspE 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": "MAKPKFIALALVALSFLSIAQSIPFTEKDLASEDSLWNLYEKWRTHHTVARDLDEKNRRFNVFKENVKFIHEFNQKKDAPYKLALNKFGDMTNQEFRSKYAGSKIQHHRSQRGIQKNTGSFMYENVGSLPAASIDWRAKGAVTGVKDQGQCGSCWAFSTIASVEGINQIKTGELVSLSEQELVDCDTSYNEGCNGGLMDYAFEFIQKNGITTEDSYPYAEQDGTCASNLLNSPVVSIDGHQDVPANNENALMQAVANQPISVSIEASGYGFQFYSEGVFTGRCGTELDHGVAIVGYGATRDGTKYWIVKNSWGEEWGESGYIRMQRGISDKRGKCGIAMEASYPIKTSANPKNSSTRDEL", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MIMNSAVSLVILLSLLCEAHTVVLLNPTDSSLPANNFTDTEAALSTPLESADIPKARRKRYISQNDMIAILDYHNQVRGKVFPPAANMEYMVWDENLAKSAEAWAATCIWDHGPSYLLRFLGQNLSVRTGRYRSILQLVKPWYDEVKDYAFPYPQDCNPRCPMRCFGPMCTHYTQMVWATSNRIGCAIHTCQNMNVWGSVWRRAVYLVCNYAPKGNWIGEAPYKVGVPCSSCPPSYGGACTDNLCFPGVTTNYLYWFK", "text": "FUNCTION: Serine protease inhibitor which displays weak inhibitory activity against trypsin (By similarity). May play a role in facial patterning during embryonic development (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
+{"protein": "MSAPNPLLAEINKGADLKHTETQDKSAPKIGSDVHIKKNDHASLLSEVEQGAKLKHAETDDKSAPKINENTTIKPNNHSALLGEIKAKAADS", "text": "FUNCTION: Is able to bind two actin monomers at high concentrations of G-actin. Inhibits actin polymerization by sequestering G-actin and stabilizing actin dimers (By similarity)."}
+{"protein": "METLYRVPFLVLECPNLKLKKPPWLHMPSAMTVYALVVVSYFLITGGIIYDVIVEPPSVGSMTDEHGHQRPVAFLAYRVNGQYIMEGLASSFLFTMGGLGFIILDRSNAPNIPKLNRFLLLFIGFVCVLLSFFMARVFMRMKLPGYLMG", "text": "FUNCTION: Specific component of the STT3A-containing form 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. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1. SUBCELLULAR LOCATION: Endoplasmic reticulum Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OSTC family."}
+{"protein": "MKHVIMLYFIAAATLFSSCAKQDSEHRLITVKNSLDLPRAFETIEISKSDIQLHTGERFEDFSIQDVATKAILTSQFVDEDQDGTADVLLFQPELNPNSEKQFELVKVDGGVEVDSTVYCYSRFVPERTDDYTWENNKVAFRTYGPVAQKMVEDSLPGGTLSSGIDAWLKKVEYSIIDNWYAKNDKDPGYYHIDHGEGLDNFHVGSSRGVGGSAVKVDTSYYISKNFTDYKTITTGPIRTSFILKYADWDANEKTISEEKHISLDYGNNFSRFEIHVDGTDELSVGLTLHDNKGEITQNVDQGWIAYWESEYFDSELGTAIVAPKGVMTASEYYVTSMKDRSNLYAQLNVDNNKVVYYAGFAWKESKQYPTKASWEKYIQEFSEKLNTPLEVSIQ", "text": "FUNCTION: May be involved in ulvan degradation (Probable). 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). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor."}
+{"protein": "MLCVLAGAAYGVFRTEAALSSQWRAEAVSGVPLTVEVTDMPRSDGRRVQFAAKAVDSGGRTFDLLLSDYKRREWAVGSRWRITARVHPVVGELNLRGLNREAWALSNGVGGVGTVGADRVLLHGGSGWGIAVWRSRISRNWRQADADGGLSDGIGLMRALSVGEQSALRPGLWQAFRPLGLTHLVSISGLHVTMVAVLFAWLAKRLLACSPRLPARPRAWVLAAGCAGALFYALLAGFSVPTQRSVLMLAAFAWAWRRGRLSAWATWWQALAAVLLFDPLAVLGVGTWLSFGLVAALIWACAGRLYEGKRQTAVRGQWAASVLSLVLLGYLFASLPLVSPLVNAVSIPWFSWVLTPLALLGSVVPFAPLQQAGAFLAEYTLRFLVWLADVSPEFAVAAAPLPLLVLAVCAALLLLLPRGLGLRPWAVLLLAGFVSYRPEAVPENEAAVTVWDAGQGLSVLVRTANRHLLFDTGTVAAAQTGIVPSLNAAGVRRLDKLVLSHHDSDHDGGFQAVGKIPNGGIYAGQPEFYEGARHCAEQRWQWDGVDFEFLRPSERKNIDDNGKSCVLRVVAGGAALLVTGDLDTKGEESLVGKYGGNLYSQVLVLGHHGSNTSSSGVFLNAVSPEYAVASSGYANAYKHPTEAVQNRVRAHGIKLLRTDLSGALQFGLGRGGVKAQRLRVYKFYWQKKPFE", "text": "FUNCTION: Essential for natural transformation. Could be a transporter involved in DNA uptake. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: To B.subtilis ComEC, H.influenzae REC2, and E.coli YcaI."}
+{"protein": "MSQAIREATHAGSWYLDDTELLTKQLKSFIKNPTPETGKRFVISPHAGYMYSGKVASQGFQQLDFSKIQRVFVFGPSHHIFTRKCLVSRASICSTPLGDLKVDEDLCQKLVASDNSFDSMTLDVDESEHSLEMQFPLLAFHLLKQGCLGKVKIVPIMIGALTSTTMMAAAKFLSQYIKDESNSFVISSDFCHWGRRFGYTLYLNDTNQLEDAVLKYKRRGGPTSPKIYESISNLDHIGMKIIETKSSDDFSEYLKTTQNTICGRYPIELIMKSMECANFSERFKFISYAQSSHVELVTDSSVSYATATA", "text": "SIMILARITY: Belongs to the MEMO1 family."}
+{"protein": "MAYIFALIFAFVVCINTDVIQAEEIQHDTLRNMEYRLSCTPKNSECERMTDICCPGFQCLGCNPYDKNDVNKCKCQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-13 family."}
+{"protein": "MGKGVGRDKYEPAAVSEHGDKKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVIGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVKGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKSSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRDRYAKIVEIPFNSTNKYQLSIHKNPNTSEPRHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDALQNAYLELGGLGERVLGFRHLFLPDEQFPEGFQFDTDDVNFPVENLCFVGFISMIGPPRAAVPDAVGKCRGAGIKVIMVTGDHPITAKAIAKGAGIISEGNETVEDIAARLNIPVRQVNPRDAKACVVHGSDLKDMTSEQLDGILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIVGSDASKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPTHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY", "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. SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein Cell membrane, sarcolemma; Multi-pass membrane protein Cell projection, axon Melanosome. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily."}
+{"protein": "MSFRTQPPAPARLNRCQLFGPGSRPAIFEKMAQSAADVINLDLEDSVAPDDKPQARRNIIEASHNIDWGNKYLSVRINGLDTPFWYRDVVELLEDGSERIDQIMIPKVGCAADVYAVDALVTAIEAAKGRKKRISLEVIIESAAGIAHVEEIAAASPRLQAMSLGAADFAASMGMATTGIGGTQENYYMLHAGVKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDEGFRAQALRSATLGMVGKWAIHPKQVALANEVFTPSDAAVAEAREILAAMEKAKAEGAGATVYKGRLVDIASIRQAEVIVRQAEMAKV", "text": "FUNCTION: Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA. FUNCTION: Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to yield beta-methylmalyl-CoA. SIMILARITY: Belongs to the HpcH/HpaI aldolase family."}
+{"protein": "MAHLQRTFPTEMSKGRASFPKGFLFGTASSSYQYEGAVNEGARGQSVWDHFSNRFPHRISDSSDGNVAVDFYHRYKEDIKRMKDINMDSFRLSIAWPRVLPYGKRDRGVSEEGIKFYNDVIDELLANEITPLVTIFHWDIPQDLEDEYGGFLSEQIIDDFRDYASLCFERFGDRVSLWCTMNEPWVYSVAGYDTGRKAPGRCSKYVNGASVAGMSGYEAYIVSHNMLLAHAEAVEVFRKCDHIKNGQIGIAHNPLWYEPYDPSDPDDVEGCNRAMDFMLGWHQHPTACGDYPETMKKSVGDRLPSFTPEQSKKLIGSCDYVGINYYSSLFVKSIKHVDPTQPTWRTDQGVDWMKTNIDGKQIAKQGGSEWSFTYPTGLRNILKYVKKTYGNPPILITENGYGEVAEQSQSLYMYNPSIDTERLEYIEGHIHAIHQAIHEDGVRVEGYYVWSLLDNFEWNSGYGVRYGLYYIDYKDGLRRYPKMSALWLKEFLRFDQEDDSSTSKKEEKKESYGKQLLHSVQDSQFVHSIKDSGALPAVLGSLFVVSATVGTSLFFKGANN", "text": "FUNCTION: Possesses beta-glucosidase activity toward 4-methyl- umbelliferyl-beta-D-glucoside in vitro. Possesses myrosinase activity toward indol-3-yl-methylglucosinolate (I3M) and 4-methoxy-indol-3-yl- methylglucosinolate (4MO-I3M) in vivo (PubMed:19095900). Component of an inducible preinvasion resistance mechanism that prevents penetration of the nonhost fungal species B.graminis and E.pisi (PubMed:16293760). Involved in indole glucosinolate (IGS) activation during pattern- triggered immunity (PTI). Functions as myrosinase for the breakdown of flg22-triggered IGS. Required for both callose deposition and glucosinolate activation during pathogen-triggered resistance (PubMed:19095898). During fungal attack, required for IGS activation that mediates broad-spectrum antifungal defense (PubMed:19095900). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
+{"protein": "MFTLKKTLLLLFFLGTINLSLCEEERNAEEERRDGDDEMDVEVKKRFITGLIGGLMKALGK", "text": "FUNCTION: Antimicrobial peptide. Active against some Gram-positive and Gram-negative bacterial strains. Active against fungus C.glabrata 090902 but not against C.albicans ATCC 12231. Shows very weak hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily."}
+{"protein": "MINNKPIIGIPIGDPAGVGPEIVVKSLTEAEVYEKCNPILIGDAKVIKQAMGFCNVNLNINSIKKADEGKFTLGTIDLIDLNNIDIDELKIGKVQGIAGKAAFEYIKKSVEMAKEGELDAIATTPINKESLREGNVNYIGHTEILADLTDTEDPLTMFEVRGMRVFFLTRHVSLRKACDLVTKERVLDYIIRCSEALEKLGVKDGKMAVAGLNPHSGEHGLFGDEEMKAVVPAIEEAQKMGYKVEGPIGADSVFHLALKGRYNSVLSLYHDQGHIATKTLDFERTIAVTNGMPILRTSVDHGTAFDIAGTGQASSVSMVEAIILAAKYSPKFKK", "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": "MDLRTGEYITAHQATSGVYTFGITNPLYFTITRHNQNPFNNKYNTLTFQIRFNHNLRKELGIHKCFLNFHIWTTLQSPTGHFLRVFKYQVCKYLNNLGVISLNNVVRAVDYVLFHVFERTIDVTENHEIKFNFY", "text": "FUNCTION: Increases viral DNA accumulation. Enhances infectivity and symptom expression (By similarity). SIMILARITY: Belongs to the geminiviridae replication enhancer protein family."}
+{"protein": "MATTTPPLDRLSPAQAQPAVVVRFKSIGSAPIMKNNVFKATAGHKFQAVIMFLRQQLGMKKEDSLFTYINAAFAPAPDDTVGSLYKSFGTEGHLIVNYSNTQAWG", "text": "FUNCTION: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions 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 ATG12 family."}
+{"protein": "MSSFGYDPYFSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSITSGYSQSSQVFGRSAYSGLQSSSYLMSARSFPAYYTSHVQEEQTEVEETIEATKAEEAKDEPPSEGEAEEEEKEKEEGEEEEGAEEEEAAKDESEDTKEEEEGGEGEEEDTKESEEEEKKEESAGEEQVAKKKD", "text": "FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (PubMed:22723690). SUBCELLULAR LOCATION: Cell projection, axon Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the intermediate filament family."}
+{"protein": "MTDVVSDFDHVYNIIRNNYNLNYYLNCADRSNNVCTIKYLQERKSYFCCAVDESTGRCVLHRCVLIVFGTWLDKKFRKKEFSGGDATCGGGGGDGDQDQDAIDERSNIKGTFMIDGRFLSFPNVMMNNNILMHNFYDKLYSKNCKRMFLYGNVDEEKRINRAIQLVYDDHEDVLFARDVYAKDYVVSENLNETLETYLRSSGKWEPLNFLFDFDKNQTDKMFDRIKMIMRAEINYSIDSLSNKIIYKHAYLTHLLYRPVLKMYQASKIDSAAAVSESNGSLRKLGGNQSGAMYPKDCKKIVDTIVNGKLIHVISKTFSKQKKNFLNHQDNSSNNNIEMCPPMIKYRVGNEVVRIINDNMRQDMLKQEYDFVKFVDSFFHGEMTVAGKKFFLCRDVRLPNVDYESIAKKFKDLIESNLIVRRDEDENGSGGDDDDDEWLMIAFNNRPTTFSCKRKHLVRIVYEFKRKRFPVEIKLSKSILFVNHHEGMICIRKQVRINEKVNISALLTPYEYHNVESIIGQIGARIVDVDHVSALMSKTLQYYYRSHLHIFATIPVPKLIVSVTNLKNAMPVIEYDDVEWNENRDMFIRNLPVGNSVVASPGSVHNNKMINLWTLVRDSRLMTAEDPYIPNVTLPVKLFNNKVNRLKGKMVYASKSKTPLVKFFKSESNNFVDTNEGHVLAMAGVIVSNVKINWTHDGKRYKIETCKNKSFYIFKIYTFLRKIRSQRIELIDAKLSTLNDFVYVKFSIVTSTNNLDGIKICGIHGQKGVMNSSEDLTEWMAEDGTHAQICLSPVSFLSRQSNFDYIERKYVVRGGDHTDPSAVRYPMFRIPYMLFNNTPEILQRIPQTNYTGHEKIEGTRLDQWSINQSFAGNRWAEGLQCVRGGTNLPDSSGEYKVLTSLLHCNNVIVN", "text": "FUNCTION: Required for late and very late gene expression. May be a component of the novel RNA polymerase activity induced by baculovirus infection. SIMILARITY: Belongs to the RNA polymerase beta chain family."}
+{"protein": "SYLMNHFDLPTCDSCRDADDKHKLITKTEAKQEYLLKDCDLEKREPALRFIVKKNPRHSQWGDMKLYLKLQVVKRALEVWGSQDALEDAKEVRQENR", "text": "FUNCTION: Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XPA family."}
+{"protein": "MSRKAPCKYEVRGKCNRGSECKFNHNYWSWPDRYLLLRSNYLLNQLLRNTDRSDGLSLISGAGRDDRTQDFVLGSTNVVQNYIDNNENITKASACYSLYNIIKQLQETDVRQARDNKVDDSKHVALHNLVLSYMEMSKTPASLINNLKKPPKEKLKKLAKLIIELSAGVENDSTAAMQDSANSD", "text": "FUNCTION: Essential for viral replication in vivo (By similarity). Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding (By similarity). SUBCELLULAR LOCATION: Virion Host cytoplasm Host nucleus Note=Localizes in cytoplasmic inclusion bodies substructures called inclusion bodies associated granules (IBAGs). Forms a layer between the matrix and nucleocapsid. SIMILARITY: Belongs to the pneumoviridae M2-1 protein family."}
+{"protein": "MTPQIKTHLLPKQEPSSSENHGSSTSGIVFNVSTSIIGAGIMSMPAAFKVLGIVPAFLIITIIAWLSTISVGFLMKSTLAGESTTYAGVMKESFGKTGSIAVQIATMVATFGCMIIFSIIIGDVLSGNENGGPEHIGVLQEWFGSYWWNTRIFALLFVYGFVLLPLVLRRRVERLAISSAVSFLLAVLFVVISSVLAISALVNGQTKNPRLFPELSNGGSFWQLFTASPVIVTAFTFHFNVHPIGFELKDPLQVIPATKISVILCAAIYFATGLFGYLLFGDATMSDILVNFDQSSGSSIGSLLNDIVRLSYVLHLMLVFPLLNFSLRANLDELLYPKKPSLEKDTKRFIGLTLALLICCFLSAIAVPDIWYFFQFMGSTITVSIAFIFPAAIVLRNIHGVSTSREKIVAAIMLVLAVATSIIAISTNLYSLAAN", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family. Amino acid/auxin permease (AAAP) (TC 2.A.18.6) subfamily."}
+{"protein": "MDAATLTYDTLRFEYEDFPETKEPVWILGRKYSVFTEKEEILLDVTSRLWFTYRKNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWIKGKRQTDNYFSVLNAFIDKKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLATFDTWSSLAVHIAMDNTVVMEEIRRLCQSNFSCAGAAACPAVEADVLYNGYPEEAGVRDKLSLWKPLVLLIPLRLGLTEINEAYIETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEPSDSGCLPDESFHCQHPPCRMSIAELDPSIAVGFFCHTEEDFNDWCHQIKKLSLVRGALPMFELVERQPSHFSNPDVLNLTPDSSDADRLERFFDSEDEDFEILSL", "text": "FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:15140988). Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy. 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. 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. Protease activity is also required to counteract formation of high- molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3. In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy. Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytosol Cytoplasmic vesicle, autophagosome Endoplasmic reticulum Mitochondrion Note=Mainly localizes to the cytoplasm, including cytosol. SIMILARITY: Belongs to the peptidase C54 family."}
+{"protein": "MNDSLKAQCGAEFLGTGLFLFFGIGCLSALKVAGASLGLWEICIIWGLGISLAVYLTAGISGGHLNPAVTIALWLFACFPKQKVLPYIIAQFAGAFGGALLAYVLYSSLFTEFETAHHMVRGSVESLQLASIFSTYPAAALNVWQAALVEVVITSILMGMIMALTDDGNGIPKGPLAPLLIGILVAVIGASTGPLTGFAMNPARDFGPKLFTWLAGWGNMAMSGGREIPYFIVPIVAPVIGACAGAAIYRYFIGKNLPCNRCEL", "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: Probably facilitates diffusion of 1,2-propanediol (1,2-PD) into the cell (Probable). Modeling suggests active transport of 1,2-PD is required at low extracellular concentrations to allow maximal growth and saturation of PduP/PduQ within the bacterial microcompartment (BMC); this protein may be the cellular transporter (Probable). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
+{"protein": "MAQKLNLLNLAVPPVTHRSNFPSTFTFGVATSAYQIEGGWNEGKKGPSIWDKFTHIEGKILDGSNGDVAVDHYHRYKEDVDLIGQLGFGAYRFSISWSRIFPDGLGTEVNEEGIAFYNDLINTLLEKGIQPYVTLYHWDLPSHLQEAIGGWTNRKIVDYFGLYADACFANFGDRVKHWITLNEPLQTSVNGHCIGIFAPGRNEKPLIEPYLVSHHQVLAHATAVSIYRSKYKESQGGQIGLSVDCEWAEPNSEKPEDKVAADRRIDFQLGWFLDPLFFGDYPASMRQKLGDNLPRFTPEEKEFMLQNSWDFLGLNHYTSRLISHVSNKEAESNFYQAQELERIVELENGDLIGERAASDWLYAVPWGIRKTLNYMSKKYNHPPIFITENGMDDEDDGSASIHDMLDDKRRVDYFKSYLANVSQAIEDGVDIKGYFAWSLLDNFEWAQGYTKRFGLVYVDYKNGLTRHPKSSAYWFMKFLKGDEENKGKKE", "text": "FUNCTION: Glucosidase that hydrolyzes scopolin and various beta- glucosides, cellooligosaccharides (mainly cellotriose) and laminarioligosaccharides (PubMed:34965581). Can use p-nitrophenyl-beta- glucosides (pNP beta-Glc) and p-nitrophenyl-beta-D-fucosides (pNP beta- D-Fuc) as substrates, and, to a lower extent, beta-galactosides, beta- mannosides and beta-xylosides (PubMed:34965581). Involved in the secretion of root-derived phenolics upon iron ions (Fe) depletion (PubMed:25138267). Promotes disease resistance toward B.cinerea, H.arabidopsidis and P.syringae pv. tomato DC3000 (PubMed:25138267). Required during rhizobacteria-mediated (e.g. P.fluorescens WCS417r) broad-spectrum induced systemic resistance (ISR) against several pathogens (PubMed:25138267). SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
+{"protein": "MVEKEEAGGGISEEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEHEFVEEKTKVAKVSQGVEDGPDTKRAKLDSSETTMVKKKVVFCPVKEALEVDWSSEKAKAALKRTTSDYFLLQVLLKFRTDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPDLLPEDFVRYCFSEMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKGNGIVECLGPK", "text": "FUNCTION: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. 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). FUNCTION: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. 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. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ubiquitin-activating E1 family."}
+{"protein": "MEIDGNTLVFIIVILFLFFSSPGGDGVSSQYEFNQLQRLKQQFRTEHNTFVNMTYTDSFRNITGLKLSYQDMLNNPLQNATYPLPGKDYDRWFPNQNYMVLPNDVIEAINTEVWNTSNDDASNLFPPNITSTLLGKIDLVSNNKYEKIRMPVPRFYEPATDFSEDIPPEGETYWSEWPSYGELHNVSFQHGEIAIQISHMSNLQDNNNYLRRNFINKKNDRWKLLNLQIDFSDKAEKEKHSIYSKAVYDIQRGRILSISQSSKFHSLFALPHYMSFQNDYNEKIFNDVKELVDEFWNFTDYTDVMTMKDVQDAYNNANFKCEYLIFLQLEPWNQYTRDQIKLIDDELNWPLGRPANLSSLPPINVVSGLLYSPDCGVRLGLHNVKGTRYELKIMSIRKHLLFGIALFAAQIYLLLTQMHHTNTPSMVNKISFYCFSMINLVDGSLATLYFVAASVVPELYLPLVISAFSCFILASIFEIRYLISIYASQVNEQNVGIINLLRGNTGTYDENRPRPAFIPDEGSIGGSLYGRFFFMLIIFTFLILSSTSWPRQLRMVFEYILIFILNSYWIPQIFRNAVKGIPSRRERARSSIGGNRSQNKMPLLWSFVIGTTIIRSLPVVYVFTYSSNVFRHHKDVHFVVFLSLWLLFQISILYSQDVLGSRWFLPKHTIPDGYSYFKPLSNEYISEHGGGTAEHTVDCAICMSDVPIYIEEIPETHKVDQHSYMVTPCNHVFHTSCLENWMNYKLQCPVCRSPLPPL", "text": "FUNCTION: Catalytic component of the DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control (PubMed:25078903, PubMed:29355480). Mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12 and other proteins containing exposed hydrophilic residues within their transmembrane domains, leading to their sorting into internal vesicles in late endosomes (PubMed:11788821). Targets also the unpalmitoylated endosomal SNARE TLG1 to the MVB pathway (PubMed:15973437). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein."}
+{"protein": "MLFSWPYPEAPIEGYWGKPTSLIDWCEENYVVSPYIAEWSNTITNSIFLMTAFYSTYSAWRNKLETRYILIGMGFSLVGIGSWLFHMTLQYRYQLLDELPMLYATIIPSWSIFAETQEILIKDEKKRKESSFRIQMVISFIMCGIVTILTWIYVVVQKPAIFQVLYGILTLLVVVLSGWLTYYHVHDSFAKKNLFITMVMGMIPFVIGFICWQLDIHLCSFWIYIRRTYLALPLGVLLELHAWWHLLTGTGVYIFVVYLQYLRILTHGNPNDFLFIWRWGFFPELVRKGLPIGTSYSLEYLGPIVNTQVDDETKKNN", "text": "FUNCTION: Acyl-CoA-independent ceramide synthase that catalyzes the conversion of dihydroceramide and also phytoceramide to dihydrosphingosine or phytosphingosine. Prefers dihydroceramide. Very low reverse hydrolysis activity, catalyzing synthesis of dihydroceramide from fatty acid and dihydrosphingosine. Is not responsible for the breakdown of unsaturated ceramide. May play a role in heat stress response. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the alkaline ceramidase family."}
+{"protein": "MMPATLAGLALAVTVATMFAQRVDSTTIHHVSGLKGKPLLFGPSLRRTLPAGGTFKWVLVLSDPCAPKPTEICVSVGHCFYDLVSSDNDSECANKDRRVLTLALLTKSKTGELRVIGPMAASSALVGDAGELEQLRRRVSAGMGLTDDGDISFAAADKVNEGLYGVRVMGSGDSYTFFNVTVATETAGDDRDLATVRHVDIAHNIVPSEDRDHVFVSMPRMHVAWPHGTTVLHPKMIIAAASWRPEYNFTYEWYAVPYDGYCATMRLFEACLYHPSAPACLDPAGHRGCVVGTMTHDDLVGRVLMARCRGSDLRTCEPHVIHIKQKPMVSLGRAVPELRVESAAHIPSLYILVVKIDDSVAGWAYTELMAEGSSPRVVIDIHMPRPTSAQGGIAALREIENDDSAPSLGSNEGGGPGNSKRRAAVLGAAVWIALTLLILGGLGAYVAVNKKCLRDKRQWLRGSRKPTLETHAHTYTSLPVGGDLSLEQDAEDEDEDEEELLYERERRRSSSGSKKSSRSPSRRSSRRNSFGPTLSANALSRFDKTVKLAMAEVAGRLLANKTFPSQRY", "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": "MISLAVFPSDFLRSTRSVFLCGDSNLDLTSSVEQCRSRTRDLRTPRRKRDRIPCLNAVGDKFLQVESFSRDEAFSTWNSHCRPLCVVSFVPSQSSVVFSDLSLQAALSRPASACLLCLRVSRVSTFLFRFSAMAKLSSAPRVLVLSAEDSVVSAADASKKDTVLTVLHPDTIIENAADAPSVLYDGVLILDAGKSRENATGNSQGKSAEFAAARSALQAFAQAVCRLVAAGGFVFLAGGSGEREEVHRLVKRLLIYEGLVSAQDSEVAAFVADHLPRVDSSLMWTGRKPTWAAGVADALSGNRGALPNGTAQTDGDDFIDESTLIDPTESYQPLGKDRSSCASRPKACPNCTCGRKEAEEAAEKEERRRKLETGEIRSSCGNCYLGDAFRCAGCPYRGMPAFKPGEKVSLEATSVEAPGGGMQKQVATVMSNKVQITDLGDDM", "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": "AMTDLLVSILVMPISIPYTITQTWSFGQLLCDIWLSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAAAMIAIVWAISICISIPPLFWRQARAHEEISDCLVNTSQISYTIYSTCGAFYIPSLLLIILYGRIYRAARNRILNPPSLYGKRFTTAHLITGSAGSSLCSLNPSLHEGHSHSAGSPLFFNHVKIKLADSVLERKRISAARERKATKTLGIILGAFIICWLPFFVASLVLPICRDSCWIHPALFDFFTWLGYLNSLINPIIYTVFNEEFRQAFQKVV", "text": "FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. 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 inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MAYFNQHQSMISKRYLTFFSKSKKKKPFSTGQLIGLILGPLLFLLTLLFFHPQDLPWKGVYVLAITLWIATWWITEAIPIAATSLLPIVLLPLGHILTPEQVSSEYGNDIIFLFLGGFILAIAMERWNLHTRVALTIINLIGASTSKILLGFMVATGFLSMFVSNTAAVMIMIPIGLAIIKEAHDLQEANTNQTSIQKFEKSLVLAIGYAGTIGGLGTLIGTPPLIILKGQYMQHFGHEISFAKWMIVGIPTVIVLLGITWLYLRYVAFRHDLKYLPGGQTLIKQKLDELGKMKYEEKVVQTIFVLASLLWITREFLLKKWEVTSSVADGTIAIFISILLFIIPAKNTEKHRRIIDWEVAKELPWGVLILFGGGLALAKGISESGLAKWLGEQLKSLNGVSPILIVIVITIFVLFLTEVTSNTATATMILPILATLSVAVGVHPLLLMAPAAMAANCAYMLPVGTPPNAIIFGSGKISIKQMASVGFWVNLISAIIIILVVYYIMPIVLGIDINQPLPLK", "text": "FUNCTION: Mediates the transport of the dicarboxylates fumarate, malate, and succinate across the cytoplasmic membrane via a Na(+)- electrochemical gradient. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. NADC subfamily."}
+{"protein": "AADIFAKFKTSMEVK", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit family."}
+{"protein": "MATQEEKQKALAAALGQIEKQFGKGSIMKLGDTKTLDVESISTGSLGLDVALGIGGLPMGRIVEIFGPESSGKTTLTLSVIAQAQKAGKTCAFIDAEHALDPIYAAKLGVDVKELFVSQPDNGEQALEICDALVRSGAIDVIIVDSVAALTPKAEIEGDMGDSHMGLQARLMSQALRKLTGQIKNANCLVVFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRTGSVKDGENIIGNETRVKVVKNKLAAPFRQVDFQILYGEGISKAGELLELGVKHKLVEKSGAWYSYNGEKIGQGKANSMKWLNENIEKSDELEARLRAELVANPEQALMADIEQSENNTESESDFE", "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. 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. Plays a central role in DNA metabolism, participating in general homologous recombination, recombinational (postreplication) DNA repair, and prophage induction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecA family."}
+{"protein": "MITAEKKKKNKFLPNFEKQSIYSLRYDEMQQWLIDHGQQKFRAKQIFEWLYQKRVNTIDEMTNLSKELRQILKDHFAMTTLTTVVKQESKDGTIKFLFELQDGYTIETVLMRHEYGNSVCVTTQVGCRIGCTFCASTLGGLKRNLEAGEIVSQVLTVQKALDETNERVSQIVIMGIGEPFENYDEMMDFLRIVNDDNSLNIGARHITVSTSGIIPRIYDFAEEDIQINFAVSLHGAKDEIRSRLMPINRAYNVDKLMEAIRYYQEKTNRRVTFEYGLFGGVNDQLEHARDLAHLIKDLNCHVNLIPVNHVPERNYVKTPKDDIFKFEKELKRLGINATIRREQGSDIDAACGQLRAKERQVETR", "text": "FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. Confers resistance to some classes of antibiotics. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family."}
+{"protein": "MFPTGIFLMSVLISQMQGRGIVGVEGQELVHPKKLSLLQKRDLERIHDSDTPEEYEEELLYEIKLGRKTLTLHLLKAREFLALNYSETYYNIKREMVTRHPQILDHCFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDEGDHLVFKYNVKAPYATNYSCEGLNFTKKSTLIDAKIIEEHKVEDYHKEKFIELFVVADEFVYRRNSKPQNKLRKRIWGMVNFVNMIYKALNIRVTLTGMEIWSAGDEIEIVSNLESTLLHFSTWQETVLKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHDDFPCTCPLGKCVMGAGSIPAIKFSKCSQTQYQQFLKNQKPACILNNPLPEEFNDYPFCGNKKVDEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGVICRPAKNECDISEVCTGYSPECPKDESQANGFPCKNGEGYCFMGLCPTRDDQCAELFSGGAEESHSLCYRMNQKGNRFGYCKNKDNTFVPCEEKDLKCGKIYCTGGRRSAHLGEDKTYNLKNVKQNISIKCKTMFLYHNSRDMGLVNSGTKCGEGMVCSNGECIEMEKAYNSTICSSLCDENDVDDNEPDCQCEEGPIITEWGEALNLTSVSIMVVVLVMVIIGVGLVILLIRYQKCIKMKQVQSSSREIRGIENKVYFPDEHQTRSEPIFTDIYPLHNTAESLERVPSTFSSPHYITLKSVSKDPRGIADPKQNDNMNLNLDSQSDCTRLG", "text": "FUNCTION: Required for normal male fertility via maintenance of epithelial cell morphology in the caput epididymis and subsequently correct epididymis lumen structure required for sperm development (By similarity). Plays a role in sperm motility, flagella morphology and tyrosine phosphorylation during sperm capacitance (By similarity). Plays a role in normal expression levels of HSPA5, ITM2B and ADAM2 in sperm both prior to and post-capacitation (By similarity). This is a non catalytic metalloprotease-like protein (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MNPFHSSCWNTSAELSNKSWNKEFAYQTASVVDTVILPSMIGIICSTGLVGNILIVFTIIRSRKKTVPDIYICNLAVADLVHIIGMPFLIHQWARGGEWVFGGPLCTIITSLDTCNQFACSAIMTVMSVDRYFALVQPFRLTSWRTRYKTIRINLGLWAASFVLALPVWIYSKVIKFKDGVESCAFDLTSPDDVLWYTLYLTITTFFFPLPLILVCYILILCYTWEMYQQNKDARCCNPSVPKQRVMKLTKMVLVLVAVFILSAAPYHVIQLVNLQMEQPTLAFYVGYYLSICLSYASSSINPFLYILLSGNFQKRLPQIQRRVTDKEIKNMGNTLKSHF", "text": "FUNCTION: Receptor for melanin-concentrating hormone, coupled to G proteins that activate phosphoinositide hydrolysis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MEDDMWCVSSSGSSRSYRSETAAKYQSGPYQDLEEFEEVDDDIAVEYPCPFCASDYDLVELCHHIDEEHRHEANNGICPVCSKRVKMHMVDHITSHHRDVLKSEQKEMSYREDPYLSDKYLQPHLDELPPSMNHHQHPSKHVSDQFLSFINNSALPNQTKLVLPDSSVEDKNPIKDSSAAKEGTSSCPLSDSDKLEKAKKCEFVQGLLSSAMFDDECDSSE", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the Di19 family."}
+{"protein": "METLVAGSIFMVLVSGVLAIIIYMLPWFIALMRGSKSTVGIFFASLLFNWSIIGWFITFIWSIAGETKKSAQPNQVIIIREKE", "text": "FUNCTION: Inhibits of the DNA ejection of T4 into the host cytoplasm. By this means, T4 excludes superinfection by the phages of the same family. SUBCELLULAR LOCATION: Host cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MLDLEVVPERSLGNEQWEFTLGMPLAQAVAILQKHCRIIKNVQVLYSEQSPLSHDLILNLTQDGIKLMFDAFNQRLKVIEVCDLTKVKLKYCGVHFNSQAIAPTIEQIDQSFGATHPGVYNSAEQLFHLNFRGLSFSFQLDSWTEAPKYEPNFAHGLASLQIPHGATVKRMYIYSGNSLQDTKAPMMPLSCFLGNVYAESVDVLRDGTGPAGLRLRLLAAGCGPGLLADAKMRVFERSVYFGDSCQDVLSMLGSPHKVFYKSEDKMKIHSPSPHKQVPSKCNDYFFNYFTLGVDILFDANTHKVKKFVLHTNYPGHYNFNIYHRCEFKIPLAIKKENADGQTETCTTYSKWDNIQELLGHPVEKPVVLHRSSSPNNTNPFGSTFCFGLQRMIFEVMQNNHIASVTLYGPPRPGSHLRTAELP", "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": "MFNYERPKHFIQSQNPCGSRLQPPGPETSSFSSQTKQSSIIIQPRQCTEQRFSASSTLSSHITMSSSAFPASPKQHAGSNPGQRVTTTYNQSPASFLSSILPSQPDYNSSKIPSAMDSNYQQSSAGQPINAKPSQTANAKPIPRTPDHEIQGSKEALIQDLERKLKCKDTLLHNGNQRLTYEEKMARRLLGPQNAAAVFQAQDDSGAQDSQQHNSEHARLQVPTSQVRSRSTSRGDVNDQDAIQEKFYPPRFIQVPENMSIDEGRFCRMDFKVSGLPAPDVSWYLNGRTVQSDDLHKMIVSEKGLHSLIFEVVRASDAGAYACVAKNRAGEATFTVQLDVLAKEHKRAPMFIYKPQSKKVLEGDSVKLECQISAIPPPKLFWKRNNEMVQFNTDRISLYQDNTGRVTLLIKDVNKKDAGWYTVSAVNEAGVTTCNTRLDVTARPNQTLPAPKQLRVRPTFSKYLALNGKGLNVKQAFNPEGEFQRLAAQSGLYESEEL", "text": "FUNCTION: Component of a complex of multiple actin cross-linking proteins. Involved in the control of myofibril assembly and stability at the Z lines in muscle cells. SUBCELLULAR LOCATION: Cell membrane, sarcolemma Cytoplasm, cytoskeleton Cytoplasm, myofibril, sarcomere, Z line Note=Sarcomeric, also localized to the sarcolemma (PubMed:10369880). Colocalizes with MYOZ1 at the Z-lines in skeletal muscle (PubMed:16076904). SIMILARITY: Belongs to the myotilin/palladin family."}
+{"protein": "MSDIKNITKLQIEDKGKKYSLYSLKKLSQELGKDVTRLPYSIRVLLENQLRNIDGYKVKEDDMHKVLDWDAKASSRPEIPHMPARVVMQDFTGVPAVVDLAAMRKAIKDAGGDADKINPLVDTAMVIDHSVQVDFYGTKTALAQNVAKEFERNGERYSLLKWAQKAFDDFIVVPPGMGIIHQVNLEYLAKDALVKNINGEDVIYPDTLVGTDSHTTMINGVGAVGWGVGGIEAEAVMLGQPYYMVLPDVVGVKFTGKLKTGVTATDLVLKVTEVLRKHGVVGKFVEYYGEGLESLSLPDRATIANMTPEYGATIGFFPVDEVTLDFFNNTNRSELVDAAREMYKEQLLFRENPAEEPEYSNIVEIDLSEVESNLAGPKRPQDRVAFHDMKKAFAEALVHEQGLHGFGLTDEQLQKSAEVKGLNERITHGSVAIAAITSCTNTSNPSLLLGAGLLAKKANEKGLKVKPFVKTSLAPGSQVVTQYLEKANLLPELENLGFNLVGYGCTTCIGNSGPLDEPVVEAINEADLIVASVSSGNRNFEGRINPHIKANYLASPIHVVAYALAGTVDFDPVEDAIGKDAEGNDVYLADIWPTTEEIAAIQSHVINSDMFKKAYATVLDGTEEWQKLKAPEGKLYEFDSSSTYIQCPNFFEKFAEGNDDLDIKGARTLLMLGDSVTTDHISPAGAIPEEYPAGQYLKSHGVEKKDFNSYGSRRGNHEVMMRGTFANIRIRNLLLDNVEGGFTKYHLDGSQQYVFDAAMKYKEKGIPLVILAGKEYGTGSSRDWAAKGTFLLGVKAVIAESYERIHRSNLVGMGVLPLEYVNGQNAKTLGLDGTEMFNIKNLNNIKPRQIVIVEAVHPKTAHTTTFEALARLDADVDVDYLKNGGILQTVLKDIMGDKKESKSTQSTTSKGCGSADTSSETSCPFAKIANFFKKLFK", "text": "FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis- aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein. SIMILARITY: Belongs to the aconitase/IPM isomerase family."}
+{"protein": "MNTPVSVNEKKDFVKWFLNNYQLKQRECVWILNYLMSHDQLMHKVHFVEHAKYCPRGLVMSANCVKDTPFHFFKQNVMTTDAEKSFHDIRLNRDEDIYIQLNFKSSFQNANYVAVLEENPYLPKHIEVNEKDRLLAERFLEESVFSFRRERLLKQIDEALDKQDKEAFHRLTAELKML", "text": "SIMILARITY: Belongs to the UPF0302 family."}
+{"protein": "MSTEYGIALGMIETRGLVPAIEAADAMTKAAEVRLVSREFVGGGYVTVLVRGETGAVNAAVRAGADACERVGDGLVAAHIIARPHKEVEPVLTMEKK", "text": "FUNCTION: One of shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The shell probably limits the diffusion of CO(2) into and out of the carboxysome. SUBCELLULAR LOCATION: Carboxysome Note=This bacterium makes alpha-type carboxysomes. SIMILARITY: Belongs to the bacterial microcompartments protein family. CsoS1 subfamily."}
+{"protein": "MGKGNEDSDLHCSSIQCSTDQPPFQQISFTEKGSDEKKPFKEKGKTAFSHSSEKHIQRQGSEPNPNKENSEETKLKAGNSTAGSEPESSSYRENCRKRKMSSKDSCQDTAGNCPEKECSLSLNKKSRSSTAVHNSEIQETCDAHHRGHSRACTGHSKRHRSRALGVQTPSIRKSLVTSVRAMSEAVYQDLAQVWAQQIHSPLTCEQLTLLTRLRGPLCAQVQTLYSMATQAAYVFPAESWLVPATLPGPGESALDREAHPFPGQEITETVSGSDEAKL", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FRG2 family."}
+{"protein": "MATTSTTTKLSVLCCSFISSPLVDSPPSLAFFSPIPRFLTVRIATSFRSSSRFPATKIRKSSLAAVMFPENSVLSDVCAFGVTSIVAFSCLGFWGEIGKRGIFDQKLIRKLVHINIGLVFMLCWPLFSSGIQGALFASLVPGLNIVRMLLLGLGVYHDEGTIKSMSRHGDRRELLKGPLYYVLSITSACIYYWKSSPIAIAVICNLCAGDGMADIVGRRFGTEKLPYNKNKSFAGSIGMATAGFLASVAYMYYFASFGYIEDSGGMILRFLVISIASALVESLPISTDIDDNLTISLTSALAGFLLF", "text": "FUNCTION: Kinase involved in negative regulation of abscisic acid (ABA) signaling. Substrate preference is farnesol > geraniol > geranylgeraniol, but has no activity with farnesyl phosphate. Can use CTP > ATP > GTP = UTP as phosphoryl donor. SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the polyprenol kinase family."}
+{"protein": "MAYYQEPSVETSIIKFKDQDFTTLRDHCLSMGRTFKDETFPAADSSIGQKLLQEKRLSNVIWKRPQDLPGGPPHFILDDISRFDIQQGGAADCWFLAALGSLTQNPQYRQKILMVQSFSHQYAGIFRFRFWQCGQWVEVVIDDRLPVQGDKCLFVRPRHQNQEFWPCLLEKAYAKLLGSYSDLHYGFLEDALVDLTGGVITNIHLHSSPVDLVKAVKTATKAGSLITCATPSGPTDTAQAMENGLVSLHAYTVTGAEQIQYRRGWEEIISLWNPWGWGEAEWRGRWSDGSQEWEETCDPRKSQLHKKREDGEFWMSCQDFQQKFIAMFICSEIPITLDHGNTLHEGWSQIMFRKQVILGNTAGGPRNDAQFNFSVQEPMEGTNVVVCVTVAVTPSNLKAEDAKFPLDFQVILAGSQRFREKFPPVFFSSFRNTVQSSNNKFRRNFTMTYHLSPGNYVVVAQTRRKSAEFLLRIFLKMPDSDRHLSSHFNLRMKGSPSEHGSQQSIFNRYAQQRLDIDATQLQGLLNQELLTGPPGDMFSLDECRSLVALMELKVNGRLDQEEFARLWKRLVHYQHVFQKVQTSPGVLLSSDLWKAIENTDFLRGIFISRELLHLVTLRYSDSVGRVSFPSLVCFLMRLEAMAKTFRNLSKDGKGLYLTEMEWMSLVMYN", "text": "FUNCTION: Probable non-lysosomal thiol-protease. SIMILARITY: Belongs to the peptidase C2 family."}
+{"protein": "MAWTKYQLFLAGLMLVTGSINTLSAKWADNFMAEGCGGSKEHSFQHPFLQAVGMFLGEFSCLAAFYLLRCRAAGQSDSSVDPQQPFNPLLFLPPALCDMTGTSLMYVALNMTSASSFQMLRGAVIIFTGLFSVAFLGRRLVLSQWLGILATIAGLVVVGLADLLSKHDSQHKLSEVITGDLLIIMAQIIVAIQMVLEEKFVYKHNVHPLRAVGTEGLFGFVILSLLLVPMYYIPAGSFSGNPRGTLEDALDAFCQVGQQPLIAVALLGNISSIAFFNFAGISVTKELSATTRMVLDSLRTVVIWALSLALGWEAFHALQILGFLILLIGTALYNGLHRPLLGRLSRGRPLAEESEQERLLGGTRTPINDAS", "text": "FUNCTION: Involved in the maintenance of mitochondrial membrane potential in pancreatic ductal adenocarcinoma (PDAC) cells. Promotes pancreatic ductal adenocarcinoma (PDAC) cell growth. May play a role as a nucleotide-sugar transporter. SUBCELLULAR LOCATION: Mitochondrion. Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC35F solute transporter family."}
+{"protein": "MARNRQACDCCCIRRVKCDRKKPCKCCLQHNLQCTYLRPLKKRGPKPVKVRNLKKVDDVQVFSKSSSGGIMKVPKALIDQCLRLYNDKLYVIWPLLCYDDLYELLEKRYDETCVYWFLVSLSAATLSDLQTEIESEGGVTFTGIQLSSFCMSSRQEFDDFNGSDIFKIMTYYCLNRCYAQMSNSRTSYRLSCEAVGLIKLAGFHREETLKLLPFDEQQLGRKVYYLLLLTERYFSVYTHCATSLDTTIAPPQPENVTDPRLSLDSFLEMIRVFTVPGKCFFDALATDSANVTCTEDSLKKIWRELHTVPLEIEPWSYGYVDISFSRHWIRTLAWKLVLQISGMRISFLSNSKNTHIPVEIARDMLEDTFLIPKNLYAVHGPGISVKALEIADALVDVVNQYDQNAESEAWNFLFDISKFVFSLKHCDSTLVDKFTTKCQCALITLPLSNPLESTDGSKEDVDALP", "text": "FUNCTION: Transcription factor that regulates respiratory growth and plays a critical role in stress adaptation during non-fermentative growth (PubMed:11353088, PubMed:20975739, PubMed:25673751). Binds to promoters of genes involved in non-fermentative metabolism, including processes such as gluconeogenesis (PCK1, FBP1 and MDH2), glyoxylate shunt (MLS1 and ICL1) and the tricarboxylic acid cycle (ACO1) (PubMed:25673751). Plays a role in maintaining mitochondrial morphology and function (PubMed:25673751). Also plays a role in tolerance to pH and osmotic stress, especially during the oxidative metabolism (PubMed:25673751). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MAL13 family."}
+{"protein": "MGQKNHFDVIVIGSGPGGEGAAMGLTKGGKNVAIIEKESSVGGGCTHWGTIPSKALRHAVSRIIEFNSNPLFCKNNSSIHATFSTILSHAKSVIDKQTRLRQGFYDRNQCTLIFGAAHFIDAHTVAVKKADGSIDTYSADKFVIATGSRPYHPKDVDFGHPRIYDSDSILNLEHDPRHIIIYGAGVIGCEYASIFRGLDVKTDLINTRDRLLSFLDNEVSDALSYHFWNSGVVIRNDETYDKVEGTSDGVIVHLKSGKKMRADCLLYANGRTGNTDKLNLESVGLQADSRGQLVVNANYQTQVEHIYAVGDVIGYPSLASAAYDQGRFVAQAIIHGQAAHLLTEDIPTGIYTIPEISSVGRTEQELTAAKVPYEVGRASFKHLARAQIAGKDIGSLKILFHRETKEILGIHCFGERAAEIIHIGQAIMEQKGEANTIEYFVNTTFNYPTMAEAFRVAALNGLNRLF", "text": "FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MASILLTRSRTPLLKTSRSLKNEFRKGKLSEGACFNCTALRLATNSPGVLGGIVWPHASSVQYLDNSSVLQRRLSRSPRLYCAILVPDPALPVHSRSTYHRTLAWPQNAPVRWVHTTGRLLDDSKVERSLRTLKDRNKKLEEGGPVYSPTVDAEPVRRTIRQRVIDEVKHYYHGFRLLWIDTTIAVRMLWRVLNGHILSRRERRQFLRTCADVFRLLPFLVFIIVPFMEFLLPVALKLFPNMLPSTFETQSKKEERLKKELRVKLEMAKFLQDTIEEIALRNKASKGNVTEEFSTFFQKIRDSGEIPSNEQIIRFSKLFEDELTLDNLTRPQLVALCKLLELQSIGTNNFLRFQLIMKLRAIRADDKLIAEEGVDSLTANELQAACRVRGMRALGVTEERLREQLKQWLELHLNQHIPTSLLLLSRAMFLPDTLSPADQLKTTLQNLPEIMAKEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEAEVLEVEGERRVDAEHALSSVDVAIHSETLRDTAPVLEGIKGEEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTGQEKAVEESKASQRLSKRVNRMIGRMDKIITELEKDKMVLDGQMDSETTPPIGENLISINELITVMKQIQNIPEHKLLSIADALDENKDGKIDIDDVIKVVELIDKEDIDISTNQVAEIMVMLQKEEKLMEKEKAKEKVEKEQAAKIQN", "text": "FUNCTION: Plays an important role in maintenance of mitochondrial morphology and in mediating either calcium or potassium/proton antiport (By similarity). Mediates proton-dependent calcium efflux from mitochondrion (By similarity). Functions also as an electroneutral mitochondrial proton/potassium exchanger (By similarity). Required for the maintenance of the tubular shape and cristae organization (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the LETM1 family."}
+{"protein": "MIKKVVAYAAIAASVMGASAAAAPQAMAIGDDSGPVSANGNGASQYFGNSMTTGNMSPQMALIQGSFNKPCIAVSDIPVSVIGLVPIQDLNVLGDDMNQQCAENSTQAKRDGALAHLLEDVSILSSNGEGGKG", "text": "FUNCTION: Forms part of the rodlet layer on the spore surface; despite their high similarity both RdlA and RdlB are required for rodlet formation (PubMed:12067338, PubMed:15228525). Plays a role in cell adhesion to polystyrene plates (PubMed:12067338). Forms amyloid-like fibrils in vitro composed of stacked beta-sheets (PubMed:28211492). SUBCELLULAR LOCATION: Secreted, cell wall Spore wall Note=Found on the surface of aerial hyphae and probably on the surface of the spore wall (PubMed:12067338). Rodlins probably contribute to the semi- transparent sheath-like structure which encapsulates spores, probably outside the chaplin layer (Probable). SIMILARITY: Belongs to the rodlin family."}
+{"protein": "MWTLVGWTILVAGLVAGIRCPDDQVCPVACCPDSGGASYSCCDPGVDLRTTALSGYLGRPCQSPANCPIGHSCVLTAAGTAACCPFSQAMACGDGHHCCPYGFHCSTDGGTCIQRPDIHLLGAVQCPGGEFECPDSSTCCHMLDGSWGCCPMPQASCCEDRVHCCPHGASCDLVHIRCVTALGSHPLTTKLPAQRTNYTGAEGTPVVSPGLLPAALPTSVICPDSRSQCPDDTTCCLLASGEYGCCPMPNAICCSDHLHCCPQDTVCDLRQSRCLSQNKAKTLLTKLPSWTVWDVECDQEVSCPEGQTCCRLQSGKWGCCPFPKAVCCEDHVHCCPEGFRCHTEKDTCEQGLLQVPWAQKTPAQPSRPSQPSPPGPPGPPSPPGPLRSEISCDEVVSCAPGNICCRLASGEWGCCPSSEGYLCMAGERCQVGDRLAPEKMAAHLMSLSQTTDVGCDQHASCPVGQTCCPKLGGGWACCQLPHAVCCEDGQHCCPAGYTCNVKARSCEKAADGAHLAAPLAVGSTGGVMDVACGDRHFCHDEQTCCRDSRGGWACCPFHQGVCCKDQRHCCPAGFHCESQGTRCVHKKSLLHWDSLPRPAAPRPRL", "text": "FUNCTION: [Granulin-3]: Inhibits epithelial cell proliferation and induces epithelial cells to secrete IL-8. FUNCTION: Secreted protein that acts as a key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation (By similarity). Regulates protein trafficking to lysosomes and, also the activity of lysosomal enzymes (By similarity). Facilitates also the acidification of lysosomes, causing degradation of mature CTSD by CTSB (By similarity). In addition, functions as wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structures (By similarity). Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases (By similarity). Moreover, modulates inflammation in neurons by preserving neurons survival, axonal outgrowth and neuronal integrity (By similarity). FUNCTION: [Granulin-7]: Stabilizes CTSD through interaction with CTSD leading to maintain its aspartic-type peptidase activity. SUBCELLULAR LOCATION: Secreted Lysosome Note=Endocytosed by SORT1 and delivred to lysosomes. Targeted to lysosome by PSAP via M6PR and LRP1, in both biosynthetic and endocytic pathways (By similarity). Co-localized with GBA1 in the intracellular trafficking compartments until to lysosome (By similarity). SIMILARITY: Belongs to the granulin family."}
+{"protein": "MIIAIDAGHGGQDPGAIGKNKFQEKNITLSIAKKLTKLLNHTNFFKAVMIRRGNYFLSVFKRTQIAEKYHANLLISIHANSSKNRKISGVSIWVLPKNVHNTRIQKHKLNKKTKNIHKKINTKTSKFKNFYEIEYDLAKIIIQELRKVSTLNQKKPKYAKFGILKFSQFPSILVETGFISNPIEEQHLNKKFYQNLISKSISIALKKYFLKRIKQYN", "text": "FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell division. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family."}
+{"protein": "MEEGGRDKTPVQSQQPSATAPSGADEKSSGKERRDAGEKDKEQELSEEDKQLQDELEMLVERLGEKDTSLYRPALEELRRQIRSSTTSMTSVPKPLKFLRPHYGKLKEIYENMAPGENKCFAADIISVLAMTMSGERECLKYRLVGSQEELASWGHEYVRHLAGEVAKEWQELDDAEKAQREPLLTLVKEIVPYNMAHNAEHEACDLLMEIEQVDMLEKDIDENAYSKVCLYLTSCVNYVPEPENSALLRCALGVFRKFSRFPEALRLALMLNDMELVEDIFTSCKDVVVQKQMAFMLGRHGVFLELSEDVEEYEDLTEIMSNVQLNSNFLALARELDIMEPKVPDDIYKTHLENNRFGGSGSQVDSARMNLASSFVNGFVNAAFGQDKLLTDDGNKWLYKNKDHGMLSAAASLGMILLWDVDGGLTQIDKYLYSSEDYIKSGALLACGIVNSGVRNECDPALALLSDYVLHNSNTMRLGSIFGLGLAYAGSNREDVLTLLLPVMGDSKSSMEVAGVTALACGMIAVGSCNGDVTSTILQTIMEKSETELKDTYARWLPLGLGLNHLGKGEAIEAILAALEVVSEPFRSFANTLVDVCAYAGSGNVLKVQQLLHICSEHFDSKEKEEDKDKKEKKDKDKKEAPADMGAHQGVAVLGIALIAMGEEIGAEMALRTFGHLLRYGEPTLRRAVPLALALISVSNPRLNILDTLSKFSHDADPEVSYNSIFAMGMVGSGTNNARLAAMLRQLAQYHAKDPNNLFMVRLAQGLTHLGKGTLTLCPYHSDRQLMSQVAVAGLLTVLVSFLDVRNIILGKSHYVLYGLVAAMQPRMLVTFDEELRPLPVSVRVGQAVDVVGQAGKPKTITGFQTHTTPVLLAHGERAELATEEFLPVTPILEGFVILRKNPNYNL", "text": "FUNCTION: Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1. FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. 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. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. SIMILARITY: Belongs to the proteasome subunit S2 family."}
+{"protein": "MSSVNQIYDLFPNKHNIQFTDSHSQEHDTSSSLAKNDTDGTISIPGSIDTGILKSIIEEQGWNDAELYRSSIQNQRFFLTDKYTKKKHLTMEDMLSPEEEQIYQEPIQDFQTYNKRVQREYELRERMEEFFRQNTKNDLHILNEDSLNQQYSPLGPADYVLPLDRYSRMKHIASNFFRKKLGIPRKLKRRSHYNPNAEGHTKGNSSILSSTTDVIDNASYRNIAIDENVDITHKEHAIDEINEQGASGSESVVEGGSLLHDIEKVFNRSRATRKYHIQRKLKVRHIQMLSIGACFSVGLFLTSGKAFSIAGPFGTLLGFGLTGSIILATMLSFTELSTLIPVSSGFSGLASRFVEDAFGFALGWTYWISCMLALPAQVSSSTFYLSYYNNVNISKGVTAGFITLFSAFSIVVNLLDVSIMGEIVYVAGISKVIIAILMVFTMIILNAGHGNDIHEGVGFRYWDSSKSVRNLTYGLYRPTFDLADAGEGSKKGISGPKGRFLATASVMLISTFAFSGVEMTFLASGEAINPRKTIPSATKRTFSIVLISYVFLIFSVGINIYSGDPRLLSYFPGISEKRYEAIIKGTGMDWRLRTNCRGGIDYRQISVGTGYSSPWVVALQNFGLCTFASAFNAILIFFTATAGISSLFSCSRTLYAMSVQRKAPPVFEICSKRGVPYVSVIFSSLFSVIAYIAVDQTAIENFDVLANVSSASTSIIWMGLNLSFLRFYYALKQRKDIISRNDSSYPYKSPFQPYLAIYGLVGCSLFVIFMGYPNFIHHFWSTKAFFSAYGGLMFFFISYTAYKVLGTSKIQRLDQLDMDSGRREMDRTDWTEHSQYLGTYRERAKKLVTWLI", "text": "FUNCTION: Amino acid sensor component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2. Amino-acid permease homolog that seems to interact directly with the extracellular signaling molecules, but has no amino acid transporter activity. May recruit casein kinases YCK1 and YCK2 to hyperphosphorylate and activate downstream component PTR3 in response to amino acid stimulus. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily."}
+{"protein": "MNKSDGNESFALDSLPENIRYPFGKRELEILEKQLDRIVLIYQVDTTYHSALKDIKDQKIISLLVEPSFYGRHHPTSILVVATCNGTYIFDIKALGLIFLELAKILEADQPRKVIHYSHRIADHLLHRQRISLGGIFDTFVAVCLSSNTRIPYTLPEAISLVFGLPMEKVTGGCESQRNFTARPLTHSQMRYLAKLVQLQHIMHDHLNYSHIFCAEVYRISLEFSHSYYGLRSCDVAINMAPASSFGFQLLDSFCKKADKELEQI", "text": "FUNCTION: RNA-binding protein. Inactive exonuclease. SIMILARITY: Belongs to the EXD1 family."}
+{"protein": "MFQPAPKRCFTIESLVAKDSPLPASRSEDPIRPAALSYANSSPINPFLNGFHSAAAAAAAGRGVYSNPDLVFAEAVSHPPNPAVPVHPVPPPHALAAHPLPSSHSPHPLFASQQRDPSTFYPWLIHRYRYLGHRFQGNDTSPESFLLHNALARKPKRIRTAFSPSQLLRLEHAFEKNHYVVGAERKQLAHSLSLTETQVKVWFQNRRTKFKRQKLEEEGSDSQQKKKGTHHINRWRIATKQASPEEIDVTSDD", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EMX homeobox family."}
+{"protein": "MANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEEIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQNKSSSSALTGVLSAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLEVSGLWSLPGLSYNVSIGFGSMFFLKYLCLWLIAVH", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CCDC149 family."}
+{"protein": "MAAGETQLYAKVSNKLKSRSSPSLLEPLLAMGFPVHTALKALAATGRKTAEEALAWLHDHCNDPSLDDPIPQEYALFLCPTGPLLEKLQEFWRESKRQCAKNRAHEVFPHVTLCDFFTCEDQKVECLYEALKRAGDRLLGSFPTAVPLALHSSISYLGFFVSGSPADVIREFAMTFATEASLLAGTSVSRFWIFSQVPGHGPNLRLSNLTRASFVSHYILQKYCSVKPCTKQLHLTLAHKFYPHHQRTLEQLARAIPLGHSCQWTAALYSRDMRFVHYQTLRALFQYKPQNVDELTLSPGDYIFVDPTQQDEASEGWVIGISQRTGCRGFLPENYTDRASESDTWVKHRMYTFSLATDLNSRKDGEASSRCSGEFLPQTARSLSSLQALQATVARKSVLVVRHGERVDQIFGKAWLQQCSTPDGKYYRPDLNFPCSLPRRSRGIKDFENDPPLSSCGIFQSRIAGDALLDSGIRISSVFASPALRCVQTAKLILEELKLEKKIKIRVEPGIFEWTKWEAGKTTPTLMSLEELKEANFNIDTDYRPAFPLSALMPAESYQEYMDRCTASMVQIVNTCPQDTGVILIVSHGSTLDSCTRPLLGLPPRECGDFAQLVRKIPSLGMCFCEENKEEGKWELVNPPVKTLTHGANAAFNWRNWISGN", "text": "FUNCTION: Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors, EGFR and PDGFRB, on the cell surface. Exhibits negligigle protein tyrosine phosphatase activity at neutral pH. May act as a dominant-negative regulator of UBASH3B- dependent dephosphorylation. May inhibit dynamin-dependent endocytic pathways by functionally sequestering dynamin via its SH3 domain. SUBCELLULAR LOCATION: Cytoplasm. Nucleus."}
+{"protein": "MEQMKITNLTDEQISFQLILHSGNARSCIIQSLRAYKEGKKDEADALIAKAEQDLSAAHDIHFQMIQKESGGEATAFSLLLMHAEDHLMSTLSMKELVKEMLDLFKTKNI", "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 GmuABC PTS system is involved in the transport of oligo- glucomannans such as cellobiose or mannobiose. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MKKGSKLILILLVTFFACLLIFPTLKWYFLMSVEDKKISSYSQEALRDYSKKKALNDLVKLKELYNKDPNSSIPASLSYLIPIAKNNYRSSMKIPPNIFTAKTLREGFLTDSDMGEVSLEIYRYYENIKKGKSRIIHLGLDLSGGMSVTISLDYSSVEKKLGRSLTFAEREDAIYRIMQILKDRVBRFGLTEPKIVREAGGNKIFLDIPGEKDESRVSTLLSGKGNLTFYVVDDESTSLLHRKILEAGSLFSIPEIQASMNLPDSKQIFPWYVKDSYGVDDESSVRYYVVDASPENSFDGAHIKDAGVSNDPRTGRDTVAFSLDVDGSEKFFKFTQKNVGKSLAVVMEGKIKSVAGIGYAITGGNVSIQGDSFDKKEAQDLALVFKTAAFPVDIKIDDLRIIGPTLGARTIDLGIKASALALCLVFLFICVYYGLSGVVAGFSLVIYNVFLILAILSAFNFTLTLTSIAGLILTMGMAVDINIVIYERIKEEIREGRRFENAFEAGFKKAFLSIMDANITTFIAVLFLTLLGTGVIQGFAWSLSVGIVASLFSSLIFSRFILEFIISVRKSKFISISWSSKYAKSN", "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 inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily."}
+{"protein": "MASRVLSAYVSRLPAAFAPLPRVRMLAVARPLSTALCSAGTQTRLGPLQPALVLAQVPGRVTQLCRQYSDMPPLTLEGIQDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE", "text": "FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain. Accessory protein, of the core iron-sulfur cluster (ISC) assembly complex, that regulates, in association with LYRM4, the stability and the cysteine desulfurase activity of NFS1 and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (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). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acyl carrier protein (ACP) family."}
+{"protein": "MEKPPSIEETPSSEPMEEEEDDDLELFGGYDSFRSYNSSVGSESSSYLEESSEAENEDREAGELPTSPLHLLSPGTPRSLDGSGSEPAVCEMCGIVGTREAFFSKTKRFCSVSCSRSYSSNSKKASILARLQGKPPTKKAKVLHKAAWSAKIGAFLHSQGTGQLADGTPTGQDALVLGFDWGKFLKDHSYKAAPVSCFKHVPLYDQWEDVMKGMKVEVLNSDAVLPSRVYWIASVIQTAGYRVLLRYEGFENDASHDFWCNLGTVDVHPIGWCAINSKILVPPRTIHAKFTDWKGYLMKRLVGSRTLPVDFHIKMVESMKYPFRQGMRLEVVDKSQVSRTRMAVVDTVIGGRLRLLYEDGDSDDDFWCHMWSPLIHPVGWSRRVGHGIKMSERRSDMAHHPTFRKIYCDAVPYLFKKVRAVYTEGGWFEEGMKLEAIDPLNLGNICVATVCKVLLDGYLMVCVDGGPSTDGSDWFCYHASSHAIFPATFCQKNDIELTPPKGYEAQTFNWENYLEKTKSKAAPSRLFNMDCPNHGFKVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEYDQWVDCESPDIYPVGWCELTGYQLQPPVAAEPATPLKAKEATKKKKKQFGKKRKRIPPTKTRPLRQGSKKPLLEDDPQGARKISSEPVRGDIIAVRVKEEHLDVPSPNKASSPELPVSVENIKQETDD", "text": "FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27' (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLEFSSQDCVFMQRALDLAAKGQYTTTPNPSVGCVLVKNGEIVGEGFHFKAGQPHAERVALAQAGENAKGATAYVTLEPCAHYGRTPPCALGLIEAGVVKVIAAMQDPNPQVAGKGLKMLSDAGIESTVNLLNDQAEKINKGFLKRMRQGMPFVQLKLAMSLDGRTAMASGESKWITGPDARSDVQKMRAKSSALLSTSTTVIADDPSLNVRWDEFPENLKTEYKKEWLRQPVRVILDSQHRIQPTHKLFLTHSPVWLVSSEPRDLTGFPDFCEQIIFPKENLLKELMRELGKRQINTLWVEAGANLSGSLIDAKLVDELIIYIAPKLLGDNARGLCQLPNLTKLADAPLWQLNELEQIGDDIKLTYTPKGV", "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": "MSASSSGGSPRFPSCGKNGVTSLTQKKVLRTPCGAPSVTVTKSHKRGMKGDTVNVRRSVRVKTKVPWMPPGKSSARHVGCKWENPPHCLEITPPSSEKLVSVMRLSDLSTEDDDSGHCKMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANVFGDAPYTSSYLTSSPIRSRSPPA", "text": "FUNCTION: Seems to be a major component of sperm tail outer dense fibers (ODF). ODFs are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail. May have a modulating influence on sperm motility. Functions as a general scaffold protein that is specifically localized at the distal/subdistal appendages of mother centrioles. Component of the centrosome matrix required for the localization of PLK1 and NIN to the centrosomes. Required for the formation and/or maintenance of normal CETN1 assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, spindle pole Cell projection, cilium, flagellum Note=Localized at the microtubule organizing centers in interphase and spindle poles in mitosis. Localized at the distal/subdistal appendages of mother centrioles. SIMILARITY: Belongs to the ODF2 family."}
+{"protein": "MIKSTVVYRDDGLPLCSSVDDDISDLSLNEQKKRIKMVVSRMTPQSANEATLESKDSEIHYIRQQGVIYFVICEAGYPRNLAFSYLNDVAVEFQHSYSNELSKPTIRPYAFASFDTFLQRTKKAYSDKKVQDNLDQLNQELVGVKQIMSKNIEDLLYRGDSLEKMDDMSNSLKISSKKYRKSAQKINFDLLISQYAPIVMVAFFFVFLFWWVFLR", "text": "FUNCTION: Required for transport from the ER to the Golgi complex. SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein Endoplasmic reticulum membrane; Single-pass type IV membrane protein Golgi apparatus membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the synaptobrevin family."}
+{"protein": "MNSKIFAVLLLLAFLSCVLSDQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNICKYPTDRPGGKRAAGGKSCKTGYVY", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom protein 11 family. 01 (wap-1) subfamily."}
+{"protein": "KSIFERDNRRDWLVIPDAVAAYVYETVNKMFPKVGQFLADAAQIPVIVGTRNFLIRETSKLSILAEQMMEKVKTLWNTKVLGYY", "text": "FUNCTION: Protein component of the very low density lipoprotein (VLDL) of egg-laying females. Potent lipoprotein lipase inhibitor, preventing the loss of triglycerides from VLDL on their way from the liver to the growing oocytes. SIMILARITY: Belongs to the apovitellenin family."}
+{"protein": "DTHKSEIAHR", "text": "FUNCTION: Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (By similarity). Its main function is the regulation of the colloidal osmotic pressure of blood (By similarity). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ALB/AFP/VDB family."}
+{"protein": "MSLISAVPLASSCVSKSLISSVREHKALRRAIATLQMSRPGKSVAASTRMSSATAGCDDGVKRRIGDYHSNLWDDNFIQSLSSPYGASSYGDHADRLIGEVKEIFNSFSIADGELTSPVSDLLQQLWMVDNVERLGIDRHFQTEIKVALDNVYRYWSEKGIGCGRDSASTDLNTTALGFRIFRLHGYTVSSDAFEHFKDQMGQFTASANDTELQTRSVFNLFRASLIAFPEEKVLEEAEKFAAAYLKAALQTLPVSGLSREIKYVFDYRWHSNLPRLEARSYIDILADNTISGTPDANTKKLLELAKLEFNIFHSLQQKELQCLWRWWKEWGCPELTFIRHRYVEFYTLVSGIDMVPEHATFRLSFVKTCHLITILDDMYDTFGTIDELRLFTAAVKRWDPSATECLPEYMKGVYMVLYETVNEMAKEAQKSQGRDTLGYVRQALEDYIGSYLKEAEWIATGYVPTFQEYFENGKLSSGHRIATLQPILTLSIPFPHHILQEIDFPSKFNDYACSILRLRGDTRCYKADSARGEEASCTSCYMKENLGSTQEDALNHINGMIEDLIKKLNWEFLRPDNNAPISSKKHAFNISRGLHHFYNYRDGYSVASNETKDLVIKTVLEPVLM", "text": "FUNCTION: Monoterpene 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:23679205). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (+)-3-carene and, to a lower extent, to terpinolene (PubMed:23679205). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
+{"protein": "MVHCAGCKRPILDRFLLNVLDRAWHVKCVQCCECKCNLTEKCFSREGKLYCKNDFFRCFGTKCAGCAQGISPSDLVRRARSKVFHLNCFTCMMCNKQLSTGEELYIIDENKFVCKEDYLNNSNTAKENSLHSATTGSDPSLSPDSQDPSQDDAKDSESANVSDKETGSNENDDQNLGAKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLVDRLEPGELLPNGPFSFYGDYQSEYYGPGANYEFFPQGPPSSQAQTPVELPFGAAGGPPGTPLGALEHPLPGHHPPGEAQRFPDMLAHPAGDSPSPEPTLPGSLHSMSAEVFGPSPPFSSISVNGGANYGNHLSHPPEMNEAAVW", "text": "FUNCTION: Transcriptional factor that defines subclasses of motoneurons that segregate into columns in the spinal cord and select distinct axon pathways. Acts in conjunction with ISL-2. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MADLWDDIYNDTKLLEELAPIAIDAALLQGVLMRTKESPNSSDVVSFAPFALLPSPVPKALFEQAKCVQEDFNTLVDRISQDTSFLEQVLSSTIKVDDFIRRLFAIHKQVQQEDCTQEVFLGINRSDYMFDCRDDGTPALKQIEINTIAASFGGLASRTPAVHQHVLKFLRKSEESSSILTNDAVEGIGWGIAHAWALYGSVDATVMFLVENEQRNILDQRFIEAELCKRNVRVIRRRLADVFERGTLDEERHLFIDGYEVAVAYFRTGYVPQDYTEQDWEARLMLERSRAVKCPDVPTQLVGTKKVQQELSRPQILEKFLPDKPEAVARIRETFTGLYSLDIGEEGDEAVRVALANPDQFVLKPQREGGGNNLYGEELKEKLQECKDSEERTSYILMDKINPKPLKNCLLRAGGRVQISECISELGMFGVYVRHRDQMIYYDQVGHLLRTKAIEHSDGGVAAGVAVLDNPYLV", "text": "FUNCTION: Catalyzes the production of glutathione from gamma- glutamylcysteine and glycine in an ATP-dependent manner. Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells and is required for numerous processes including the protection of cells against oxidative damage, amino acid transport, the detoxification of foreign compounds, the maintenance of protein sulfhydryl groups in a reduced state and acts as a cofactor for a number of enzymes. Participates in ophthalmate biosynthesis in hepatocytes (By similarity). SIMILARITY: Belongs to the eukaryotic GSH synthase family."}
+{"protein": "LNPFRWMINKYREWKNKKN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 06 subfamily."}
+{"protein": "MDSSLSQKFTLAYASLLGVGGLMGYLKRGSKISLVAGGGSAALFYYVYTELPGNPVLASSIGIVGSAALTGMMGSRYLRTRKVVPAGLVSVVSLVMTGAYLHGLIRSS", "text": "FUNCTION: May be involved in free fatty acids export. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM14 family."}
+{"protein": "MLVTSSRKPSARTRTLCKLLSRFIAGRCMTRGKMGMQELLEFAEGGPLIVIGEYHGNPGELSFYDEAGELLFSLRFTDWYSKELDSYWFSGIEPKLAGQGEIAEAFKVFFHFQRVENDKIDQLPPSSTLIVVGENDIDFMGSGKSLFKLNLRGFKKY", "text": "FUNCTION: Probably involved in the biogenesis of the ribosome."}
+{"protein": "MSLQVKDIKKSFGNGQSETPVLKGINFNVNEGEFVILNGASGSGKTTLLTILGGLLSQSSGDILYNNQPLFTRDRKASELRLNEIGFIFQSSHLVPYLKVKAQLTTIGKEAGMTMQEANQRAETLLKQIGLNHRLTAFPHMLSGGEKQRVAIVRALMNHPKIILADEPTASLDAERATEVIEMIKNQIKSKKMIGIMITHDKRLFEYADKVIELDDGVITNA", "text": "FUNCTION: Part of the ABC transporter complex hrt involved in hemin import. Responsible for energy coupling to the transport system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. HrtA family."}
+{"protein": "MGQPAKVLQLFKTLHRTRQQVFKNDKRALEAARVKINEEFKKHKNETSPEKIKEMLKIGSDVELLLRTSVIQGIHTDHDTLQLVPRKDLLTENVPYCDAPTQKL", "text": "FUNCTION: Assembly factor required for Rieske Fe-S protein UQCRFS1 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 (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I LYR family."}
+{"protein": "MADLSSPDGDPTIRTLLRHVLDTADSHTPRRRQSTQTNPQRRRSQTPYSKRQGSQRKTSTRKHSHGTGSVGRLARVQGHGHLEEQTPRTLLQNILLTAPESSTVMPNPVVKPAQVPEVARPSRRGSSRGSLELQLPELDPPSTLAPGLKAPGKRKQKLRLSVFQQEVNQQLPLPQEQRGAADGSSLASSFNLSFVPSVQPQTVDRPGLARRRPVRRPVNIGAFLQNLENKSLTSALPGDSHRTPVAALPTDVVFEDTQPFSQPLAGCSLSVHHSLPNPSQTEVEDAERVVGPRTPSTGTRPQSQMSRAGFGASPLPFSEPQPQSPELREAVGSKEAEEPKDLEGSSGDEETSGMPASRELSSSAQDLLLAEEPHQLFEPPPSPGVAAVSSESVPAKLPSRTRTAQPRHHQDPYKAGLSHYVKLFSFHTKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRRQGLVTDQVSLHVLVERYLPLEYRQQLIPCAFRGNSVFPAQ", "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": "MFGTVNNYLSGVLHAAQDLDGESLATYLSLRDVHVQNHNLYIAQPEKLVDRFLKPPLDEVVSAHLKVLYHLAQEPPGYMEAYTQQSAACGAVVRLLQQLKDENWCLPLMYRVCLDLRYLAQACEKHCQGFTPGHVLEKAADCIMACFRVCAADGRASEEDTKRLGMMNLVNQLFKIYFRINKLHLCKPLIRAIDNCIFKDSFPLPEQITYKYFVGRRAMFDSNYQAAVQYLSYAFSNCPDRFASNKRLILIYLVPVKMLLGYLPSKSLLQRYDLLLFLDLAMAMKAGNVNRFDEIVRDQELVLIRSGIYLLVEKLKFLVYRNLFKKVFVIRKSHQLDMGDFLSALHFVGLTDVSLDETHCIVANLIYDGKIKGYISHAHNKLVVSKQNPFPSVSL", "text": "FUNCTION: Required for the export of nuclear mRNAs and involved in mRNA trafficking in the cytoplasm (PubMed:27016737, PubMed:28554770, PubMed:33602059). Component of the nuclear pore complex (NPC)- associated TREX-2/AMEX complex (anchoring and mRNA export complex) which functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), thereby enabling the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:27016737, PubMed:28554770, PubMed:33602059). Within the complex, specifically promotes the association of factors involved in regulating nuclear mRNA export, such as Moe, sbr/NXF1 and the ORC complex, to the mRNPs particles (PubMed:27016737, PubMed:28554770, PubMed:33602059). In the cytoplasm, functions independently of its role in the TREX-2/AMEX complex, to promote cytoplasmic mRNA trafficking together with nudC (PubMed:33602059). Associates with translationally active polysomes (PubMed:18086857). SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus membrane Cytoplasm, cytoskeleton Note=Shuttles in and out of the nucleus by a emb/Crm1-dependent mechanism (PubMed:18086857). The ubiquitinated forms are localized to the cytoplasm, the nonubiquitinated forms are localized to the nucleus, and both forms are associated with the nuclear membrane (PubMed:33602059). Associated with cytoplasmic microtubules (PubMed:33602059). Associates with mRNA in the nucleus and cytoplasm (PubMed:33602059). SIMILARITY: Belongs to the CSN12 family."}
+{"protein": "MGKIEATSKEEKLRVQKEAEARRRAYRDLKKEARQMQKEVKFDTDDNSELPKKRFYRQRAHSNPFSDHRLEYPRSPDTMDWSKFYPQYYDSESKKMTSEVEIADIGCGYGGLLINLAPEFPDKLLLGMEIRVQVTQYVEDRIIALRNQYRNELQNNYQNISVLRGNAMKFLPNFFHKAQLSKMFFCFPDPHFKQRKHKARIITNTLLAEYAYVLKEGGIIYTITDVEDLHNWMVKHLEEHPMFERLSKEWEKQDKCVSIMWNSTEEGKKVTRNKGSKWVACFKRLPTPDDCE", "text": "FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family."}
+{"protein": "MSNVTVCARFRPRSSKEMRDPSRDGVCARPIDAETFVFQDDKEDEFTFSLDRVFYEDSTQAAVYEFLALPIMRDAVNGINGTIITYGQTGAGKTYSMEGPGIQDCDEHNKGLLPRVVHGMFEQISSSNDIARYTVKLSMVEIYMEKVRDLLDLSKANIQIKENKTQGILLSGVTEVPVSDSVEALQHLCTGLANRAVGETQMNMSSSRSHCAYLFTIQQDSVKDKRVKTGKLILVDLAGSEKADKTGAEGRVLEEAKTINKSLSALGNVINALTSGPSSKGNHIPYRDSKLTRILQDALGGNSRMALLCCCSPSTLNASETLSTLRFGMRAKHIKASPRASEVKSAKAQEEPSSVTKDEKCGRILEKMKERMSNEDIKMLEDVFIQEGIIFSLDSMAEVETVYEDIVSKTIQSLQQAVDELQQKVKKLEAENIGIQEQALRNHEPGSVGKMSRFISSWYASFFTS", "text": "FUNCTION: Kinesin-like motor protein that promotes synapsis and is required for proper crossover distribution in meiosis (PubMed:25330379). Plays a role in the nuclear division cycles during megagametogenesis (PubMed:24667993). SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-1 subfamily."}
+{"protein": "MGSFSITLGFFLVLAFWLPGHIGANPVYSAVSNTDLMDFKNLLDHLEEKMPVEDEVMPPQALSEQTEEAGAALSSLPEVPPWTGEVNPPLRDGSALGRSPWDPSDRSALLKSKLRALLAGPRSLRRSSCFGGRIDRIGAQSGLGCNSFRYRR", "text": "FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis. Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides. Possibly functions in protein excretion in urine by maintaining the integrity of the proximal tubules and enhancing protein excretion by decreasing proximal tubular protein reabsorption. FUNCTION: [Auriculin-A]: May have a role in cardio-renal homeostasis through regulation of regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, vasodilates intestinal smooth muscle but not smooth muscle strips. FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (PubMed:8760210, PubMed:22437503, PubMed:12890708). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (PubMed:12890708). Regulates vasodilation, natriuresis, diuresis and aldosterone synthesis and is therefore essential for regulating blood pressure, controlling the extracellular fluid volume and maintaining the fluid-electrolyte balance (PubMed:8760210, PubMed:22437503). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (By similarity). Plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus, and thus prevents pregnancy-induced hypertension (PubMed:22437503). In adipose tissue, acts in various cGMP- and PKG- dependent pathways to regulate lipid metabolism and energy homeostasis (By similarity). This includes up-regulating lipid metabolism and mitochondrial oxygen utilization by activating the AMP-activated protein kinase (AMPK), and increasing energy expenditure by acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose tissue (By similarity). Binds the clearance receptor NPR3 which removes the hormone from circulation (By similarity). FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+- ATPase. May have a role in potassium excretion but not sodium excretion (natriuresis). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption. FUNCTION: [Auriculin-B]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. FUNCTION: [Atriopeptin-2]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal and vascular smooth muscle strips. FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio- renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (By similarity). However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report, in vivo it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis (By similarity). Appears to bind to specific receptors that are distinct from the receptors bound by atrial natriuretic peptide and vessel dilator. Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (By similarity). FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis. Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance. Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney. FUNCTION: [Atriopeptin-1]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal smooth muscle but not vascular smooth muscle strips. FUNCTION: [Auriculin-D]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted Note=Detected in blood. SUBCELLULAR LOCATION: [Vessel dilator]: Secreted Note=Detected in blood. SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted Note=Detected in blood. SUBCELLULAR LOCATION: [Urodilatin]: Secreted Note=Detected in urine. Not detected in blood. Increased electrolytes, osmolality and intracellular cAMP levels increase peptide secretion/excretion. SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted Note=Detected in blood. Slight increase in secretion in response to the vasopressin AVP. SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted Perikaryon Cell projection Note=Detected in blood. Detected in urine in one study. However, in another study, was not detected in urine. Detected in cytoplasmic bodies and neuronal processes of pyramidal neurons (layers II-VI) (By similarity). Increased secretion in response to the vasopressin AVP (By similarity). Likely to be secreted in response to an increase in atrial pressure or atrial stretch. In kidney cells, secretion increases in response to activated guanylyl cyclases and increased intracellular cAMP levels. Plasma levels increase 15 minutes after a high-salt meal, and decrease back to normal plasma levels 1 hr later (By similarity). SIMILARITY: Belongs to the natriuretic peptide family."}
+{"protein": "MEAAQAFENLANLEQEFGKAEIEILKKQNELFQPLFEQRRDILKTINNFWVVVLEAAGDEISQYITPEDSVLLEKLENIYVERFNEKEPRDVRISLTFQPNEYLQDDNLTLVKEVRIKEEKAKDDEGLEKKITKYTSQPVDIHWKPGKSLFRKNKKLPPNFFDYFQWTGEEEDDDFDGATLTIFLAEDLFPNAVKYFTEAMTEEASDEDESVDLEEDEEEEDEEDEEGDEEKQEPPSKKSKKSN", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
+{"protein": "MKSFKNKNTLRRKKAFPVFTKILLVSFLVWVLKCSNNCNNGNGSGDSFDFRNKRTLAQKQHEHHHHHHHHHHHQHQAPHQAPHQAHHHHHHGEVNHQAPQVHQQVHGQDQAHHHHHHHHHHLHPQQPQGTVANPPSNEPVVKTQVFREARPGGGFKAYEEKYESKHYKLKENVVDGKKDCDEKYEAANYAFSEECPYTVNDYSQENGPNIFALRKRFPLGMNDEDEEGKEALAIKDKLPGGLDEYQNQLYGICNETCTTCGPAAIDYVPADAPNGYAYGGSAHDGSHGNLRGHDNKGSEGYGYEAPYNPGFNGAPGSNGMQNYVHPWSGYSAPYGVPHGAAHGSRYSSFSSVNKYGKHGDEKHHSSKKHEGNDGEGEKKKKSKKHKDHDGEKKKSKKHKDNEDAESVKSKKHKSHDCEKKKSKKHKDNEDAESVKSKKVLKKREKSIMEKNHAAKKLTKKIKIKKKTNNSKSDGSKAHEKKENETKNTAGENKKVDSTSADNKSTNAATPGAKDKTQGGKTDKTGASTNAATNKGQCAAEGATKGATKEASTSKEATKEASTSKEATKEASTSKEATKEASTSKGATKEASTTEGATKGASTTAGSTTGATTGANAVQSKDETADKNAANNGEQVMSRGQAQLQEAGKKKKKRGCCG", "text": "FUNCTION: KAHRP might mimick human histidine-rich glycoproteins to anchor host thrombospondin or a parasite analog in a binding complex with the endothelial cell receptor. SUBCELLULAR LOCATION: Secreted. Note=Cytoplasmic side of the membrane of infected erythrocytes."}
+{"protein": "MTKLSRRVLEMEESVTLATSARAKTLKAQGRDVLELSLGQPDFVTPKNIQEAAMKSIRDGRASFYTIASGLPELKDAISQYFEKFYGYSVERKQIVVGTGAKFILYALFAAVINPKDEVIIPTPFWVSYADQIKMNDGVPVFIRTSEENHFKATVEQLEAARTNKTKMIVLNSPSNPTGMIYSKKELEAIGNWAVKHDILILSDDIYGRLVYNGARFTPISTISQPICQQTIVINGVSKTYSMTGWRVGYAVGDPEIIGAMSKIVSQTTSNLTTAAQYAAIEALIGNQDTVEVMRQAFEERLNTIYPLLAKVPGFHVVKPEGAFYFFPNVKKAMEMKGYTDVTEFTTALLEETGVALVTGAGFGAPENVRLSYATDMVTLKEAINRIQAFMEK", "text": "FUNCTION: Catalyzes the transamination reaction between L-asparagine and 2-oxoglutarate to produce L-glutamate and 2-oxosuccinamate (PubMed:22569339). Is not active with pyruvate as amine acceptor (PubMed:22569339). May also use other amino acids as substrates. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MVSEKCVAAFFLLQLCWAGCGFCSKVLVWPCDMSHWLNLKTILEELGARGHEVTVLKYPSIIIDQSKRIPLHFENIPLLYEIETAENRLNEIANLAVNVIPNLSLWEAAKTLQDFFLQVTGDFESICRSVLYNQKFMDKLRDAQYDVVVIDPVVPCGELVAEVLQIPFVYTLRFSMGYYMEKHCGQLPIPLSYVPVVMSELTDNMTFTERVKNMMFSLLFEYWLQQYDFAFWDQFYSETLGRPTTFCKTVGKADIWLIRTYWDVEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFVQSSGEHGVVVFSLGSMVKNLTEEKANLIASVLAQIPQKVLWRYSGKKPATLGSNTRLFNWIPQNDLLGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMLGDQPHNIAHMEAKGAALKVSISTMTSTDLLSAVRAVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLSWFQYHSLDVIGFLLLCVVTLTFIITKFCLFVCQKLYMKESKKMGNRKKKN", "text": "FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MGNDERKRPTKKMKYGGKDDQKMKNIQNVEDYYDDADEDSRDGEGEEKRRDFTDLELKPDHGNRPLWACADGKIFLETFSPLYKQAYDFLIAIAEPVCRPESMHEYNLTPHSLYAAVSVGLETETIISVLNKLSKTKLPGEIIDFIHASTANYGKVKLVLKKNRYFIESPFPEVLKRLLSDDVINRARFTSEPYYGGDGFTIGKTSGELEAGPGELLNEAELAAAAEEKETHSFEIDPALVENVKQRCLPNALNYPMLEEYDFRNDNVNPDLDMELKPHAQPRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVSAAARIKKSCLCLATNAVSVDQWAYQFKLWSTIKDDQICRFTSDSKERFRGNAGVVVTTYNMIAFGGKRSEEAEKIIEEMRNREWGLLLMDEVHVVPAHMFRKVISITKSHCKLGLTATLVREDEKITDLNFLIGPKLYEANWLDLVKGGFIANVQCAEVWCPMTKEFFAEYLKKENSKKKQALYVMNPNKFRACEFLIRFHEQQRGDKIIVFADNLFALTEYAMKLRKPMIYGATSHIERTKILEAFKTSKTVNTVFLSKVGDNSIDIPEANVIIQISSHAGSRRQEAQRLGRILRAKGKLEDRMAGGKEEYNAFFYSLVSTDTQEMYYSTKRQQFLIDQGYSFKVITSLPPPDAGSSLGYHSQEEQLSLLGKVLNAGDDMVGLEQLEEDTDGKALKTRRSMGSMSAMSGANGRVYMEYNSGRQKSGNQSKKPKDPTKRHNIFKKRYV", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily."}
+{"protein": "MEHTPHIAMVPTPGMGHLIPLVEFAKRLVLRHNFGVTFIIPTDGPLPKAQKSFLDALPAGVNYVLLPPVSFDDLPADVRIETRICLTITRSLPFVRDAVKTLLATTKLAALVVDLFGTDAFDVAIEFKVSPYIFYPTTAMCLSLFFHLPKLDQMVSCEYRDVPEPLQIPGCIPIHGKDFLDPAQDRKNDAYKCLLHQAKRYRLAEGIMVNTFNDLEPGPLKALQEEDQGKPPVYPIGPLIRADSSSKVDDCECLKWLDDQPRGSVLFISFGSGGAVSHNQFIELALGLEMSEQRFLWVVRSPNDKIANATYFSIQNQNDALAYLPEGFLERTKGRCLLVPSWAPQTEILSHGSTGGFLTHCGWNSILESVVNGVPLIAWPLYAEQKMNAVMLTEGLKVALRPKAGENGLIGRVEIANAVKGLMEGEEGKKFRSTMKDLKDAASRALSDDGSSTKALAELACKWENKISST", "text": "FUNCTION: Broad spectrum multifunctional glucosyltransferase. In addition to hydroquinone it accepts at least 45 natural and synthetic phenols as well as two cinnamyl alcohols as substrates. Hydroquinone was however the best substrate. In contrast to this broad acceptor substrate specificity, only pyrimidine nucleotide activated glucose is tolerated as a donor substrate. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "METCRCPLSYLISFLLFLSHSETACRPLGKRPCRMQAFRIWDVNQKTFYLRNNQLVAGYLQGSNTKLEEKLDVVPVEPHAVFLGIHGGKLCLACVKSGDETRLQLEAVNITDLSKNKDQDKRFTFILSDSGPTTSFESAACPGWFLCTALEADRPVSLTNRPEEAMMVTKFYFQKE", "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": "RALATQLPVIPRSQVTFLAPVTRPEK", "text": "FUNCTION: May have hydrolase activity. SIMILARITY: Belongs to the FAH family."}
+{"protein": "MAGARGLLHLWLSCLCVSLAQGQRLRQPFPELRVAVPADRAAGGGPESPLQPLDQVSEHMLRLYDRYSGGRTEEARTPGNSERGSPSLRPQPLREGNTVRSFRAGAAGMLENKELHIFNLTSLTKSENILSATLYFYIRELINISLSCPVSQECSHHAQRKHIQIDLSAWILKSSGNQSQLLGHLSVDGGKPHRDFVSWLSKDITQLLRKAKENEEFLIGFNITTKGHQLPKKMTPSPEPYILVYANDAAISEPESVVSSLQGHRNFPTGAVPKLDSQSRSAPSIERRRRKRSTGVLLPLQNNELPGAEYQYKEDEVWEERKPYKTLQTQPPDKSKNKKKQRKGPQQKSQTLQFDEQTLKKARRKQWIEPRNCARRYLKVDFADIGWSEWIISPKSFDAYYCSGACQFPMPKSLKPSNHATIQSIVRAVGVVPGIPEPCCVPEKMSSLSILFFDENKNVVLKVYPNMTVESCACR", "text": "FUNCTION: Induces cartilage and bone formation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
+{"protein": "MASGQESRKELDRKAREGETVVPGGTGGKSVEAQEHLAEGRSRGGQTRREQLGQQGYSEMGKKGGLSTTDESGGERAAREGVTIDESKFTK", "text": "FUNCTION: LEA proteins are late embryonic proteins abundant in higher plant seed embryos. They may play an essential role in seed survival and in controlling water exchanges during seed desiccation and imbibition. SIMILARITY: Belongs to the small hydrophilic plant seed protein family."}
+{"protein": "MEFSEWYSDILEKAEIYDVRYPIKGCGVYLPYGFKIRRYTFEIIRNLLDESGHDEALFPMLIPEDLLAKEAEHIKGFEDEVYWVTHGGKTQLDVKLALRPTSETPIYYMMKLWVKVHTDLPIKIYQIVNTFRYETKHTRPLIRLREIMTFKEAHTAHSTKEEAENQVKEAISIYKKFFDTLGIPYLISKRPEWDKFPGAEYTMAFDTIFPDGRTMQIATVHNLGQNFSKTFEIIFETPTGDKDYAYQTCYGISDRVIASIIAIHGDEKGLILPPIVAPIQVVIVPLIFKGKEDIVMEKAKEIYEKLKGKFRVHIDDRDIRPGRKFNDWEIKGVPLRIEVGPKDIENKKITLFRRDTMEKFQVDETQLMEVVEKTLNNIMENIKNRAWEKFENFITILEDINPDEIKNILSEKRGVILVPFKEEIYNEELEEKVEATILGETEYKGNKYIAIAKTY", "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 non-cognate amino acids such as cysteine and alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily."}
+{"protein": "MDKLSGSARLIIVSDLDHTMVDHHDEENLSLLRFGALWESVYCQDSLLVFSTGRSPTLYKELRKEKPMLTPDITIMSVGTEITYGEAMVPDDGWEEYLNNKWDRNVVVEETAKFSELKLQPETEQRPHKVSFFVDKKSAQEVIKSLSGNMEKCGLDVKIIYSGGQDLDILPQGAGKGQALAYLLKKLSSCGKPPNNTLVCGDSGNDAELFSIPGVHGVMVSNAQEELLQWYAENAKGNPKIIHATERCAAGIIEAIGHFKLGPSVSPRDVGFPYVKEDHIKPTDAVVKFYVLYEKWRRAEVPKSDSVVQYFKNITHANGVIIQPSGLECSLHASVDALSSCYGEKQGKKYRTWVDRLFVSQSGSDSWLVRFDLWEAEGDARLCCLTSLALNVKPETPAGFLITHVHKTWLKGYSSADEQSSKL", "text": "FUNCTION: Catalyzes the final step of sucrose synthesis. SIMILARITY: Belongs to the sucrose phosphatase family."}
+{"protein": "MDNNLEIKDLEKIAKKVRYNIVKMVGLAKSGHPGGSLSATDIIVALYFKLMNYSPDNPYKKDRDRFVLSKGHAAPALYAVLSELGIIEEEELWKLRRLEGKLQGHPSMDTPGVEICTGSLGQGFSAAVGMALGCRLDKLNNYVYVLLGDGECQEGIVWEAAMAAAHYKLDNLIAFIDRNKLQIDGCTEDVMSLGDIKAKFEAFGWDVFEIDGHNFEEIINTVEKAKSMKNGKPKMIIAYTVKGKGVSFMENNVAFHGKAPNEEQLKQALEELSE", "text": "SIMILARITY: Belongs to the transketolase family."}
+{"protein": "MSSCVEKSRGRNPYAAVQVDPDSDYITPGTLDLEQLFWSGPTAQYAHVNQVWPRIYLGDEKTALERPALKDLGITHVLNAAVGKWNNVLTGADYYTGMNIRYLGVEADDKPTFNISQYFSQAAEFIHEALIHPVLVHCVMGRSRSATLVLAYLMIKEHLSVVDAVEHVRQRRCILPNHGFLKQLRALDIALQEEKLRLKRKDE", "text": "FUNCTION: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (By similarity). Involved in the modulation of AMPK and MAPK1/2 signaling pathways (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
+{"protein": "MRKTKSKTITGYKLLDCEYGLVDVIQLRATIDSESIEPIADMKTREISDEKFYGKKSFVTKIETLDGREVPDSFFEDFVCTTHVFGIEREEFRPQTKIKNVFMYFYNKDVSDREDVLTYDPFKRKIYSSVEDLQVLETQNIDIVWKKHKKLTFKYACLFGDYKNAHNKLQGFDVCNQKINHIINKNQEKDKWIFRRVKQNCYDEYYKQLSDLTVYEKELTDILNVRIKLGDYLRSNKEKSID", "text": "SIMILARITY: Belongs to the mimivirus L74/L77/R857 family."}
+{"protein": "MVPVENTEGPSLLNQKGTAVETEGSGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLALSCHEQEMVVSSLVIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEGAASKVLGRLRALSDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVISTIPATLLVDHVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTHICRSHNSINQSLDESVIYGPGNLSTNNNTLRDHFKGISSHSRSSLMPLRNDVDKRGETTSASLLNAGLSHTEYQIVTDPGDVPAFLKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTIMSLASLLFVVMFIPETKGCSLEQISMELAKVNYVKNNICFMSHHQEELVPKQPQKRKPQEQLLECNKLCGRGQSRQLSPET", "text": "FUNCTION: Insulin-independent facilitative glucose transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endomembrane system; Multi-pass membrane protein Cytoplasm, perinuclear region Note=Localizes primarily perinuclear region in the absence of insulin. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily."}
+{"protein": "MKKLLVVLLPTLLAGCSYYDAMVERMNTDTLEYRCDEKPLTVSLNKQREQVSFVLDDKMLHLNQGRAASGTRYTDGIYAFWSKGDEATVYHRDNIVLNHCQLQNPKR", "text": "FUNCTION: Specifically inhibits C-type lysozymes. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Note=Anchored to the periplasmic side. SIMILARITY: Belongs to the MliC family. Type 1 subfamily."}
+{"protein": "MSPLLLLLLCLLLGNLEPEEAKLIRVPLQRIHLGHRILNPLNGWEQLAELSRTSTSGGNPSFVPLSKFMNTQYFGTIGLGTPPQNFTVVFDTGSSNLWVPSTRCHFFSLACWFHHRFNPKASSSFRPNGTKFAIQYGTGRLSGILSQDNLTIGGIHDAFVTFGEALWEPSLIFALAHFDGILGLGFPTLAVGGVQPPLDAMVEQGLLEKPVFSFYLNRDSEGSDGGELVLGGSDPAHYVPPLTFIPVTIPAYWQVHMESVKVGTGLSLCAQGCSAILDTGTSLITGPSEEIRALNKAIGGYPFLNGQYFIQCSKTPTLPPVSFHLGGVWFNLTGQDYVIKILQSDVGLCLLGFQALDIPKPAGPLWILGDVFLGPYVAVFDRGDKNVGPRVGLARAQSRSTDRAERRTTQAQFFKRRPG", "text": "FUNCTION: May be involved in processing of pneumocyte surfactant precursors. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MDLSAKDEFSAEKRNPDNYDSVNNPSGDWRVDSYPSENLISAGPASCSPSQMMDSFGQTLWYDPTSVQAVGYAGFNGGNASSSSFRGSIDRSLEMGWNLPNLLPPKGNGLFLPNASSFLPPSMAQFPADSGFIERAARFSLFSGGNFSDMVNQPLGNSEAIGLFLQGGGTMQGQCQSNELNVGEPHNDVSVAVKESTVRSSEQAKPNVPGSGNVSEDTQSSGGNGQKGRETSSNTKKRKRNGQKNSEAAQSHRSQQSEEEPDNNGDEKRNDEQSPNSPGKKSNSGKQQGKQSSDPPKDGYIHVRARRGQATNSHSLAERVRREKISERMKFLQDLVPGCNKVTGKAVMLDEIINYVQSLQRQVEFLSMKLATVNPQMDFNLEGLLAKDALQLRAGSSSTTPFPPNMSMAYPPLPHGFMQQTLSSIGRTITSPLSPMNGGFKRQETNGWEGDLQNVIHINYGAGDVTPDPQAAATASLPAANMKVEP", "text": "FUNCTION: Transcriptional activator involved in cell elongation. Regulates the expression of a subset of genes involved in cell expansion by binding to the G-box motif. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "LKDAQSRITK", "text": "FUNCTION: Involved in the high-affinity maltose membrane transport system. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
+{"protein": "MHYKKSIIGIAVTATAIIAGCQVTHQIVKSQGTAQGKHGEVQVETTFKDGHIVAIDVLKQKENKVLAGAVFKDVKQAIIDNNSIEVDGIAGATVTSKALKEAVGKSIEAAGVTLVATASAKKSEALTPAEYTYDVVIIGSGGAGFSAGLEAIAAGRSAVIIEKMPIIGGNSLISGAEMNVAGSWVQKNMGITDSKELFISDTLKGGDFKGDPEMVKTMVDNAVGAAEWLRDYVKVEFYPDQLFQFGGHSVKRALIPKGHTGAEVISKFSIKADEVGLPIHTNTKAEKLIQDQTGRIVGVEAAHNGKTITYHAKRGVVIATGGFSSNMEMRKKYNPELDERYGSTGHAGGTGDGIVMAEKIHAAAKNMGYIQSYPICSPTSGAIALIADSRFFGAVLINQKGERFVEELERRDVISHAILAQPGRYTYVLWNQDIENVAHTVEMHQGELKEFTKDGLMYKVDTLEEAAKVFNIPEDKLLSTIKDVNHYAATGKDEAFNHRSGLVDLSKGPYWILKATPSVHHTMGGLVVDTRTRVLDEQGKVIPGLFAAGEVTGLTHGTNRLGGNAYTDIIVYGRIAGQEAAK", "text": "FUNCTION: Catalyzes the two-electron reduction of urocanate to dihydrourocanate (also named imidazole propionate or deamino- histidine). The physiological electron donor is unknown; it might be the membrane-bound tetraheme cytochrome c (CymA). Enables anaerobic growth with urocanate as a sole terminal electron acceptor, and thus can provide the cells with a niche where no other bacteria can compete and survive. Is unable to reduce cinnamate and other unsaturated organic acids such as acrylic, crotonic, fumaric and orotic acids. Has no fumarate reductase or succinate dehydrogenase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Periplasmic side Note=Is associated, but not too tight, with the membrane. SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily."}
+{"protein": "MYPPEFSYVRAESLQEALKFLEGNDNTRPLAGGQSLIPMLKLRVLSPDYILDINRLNELNYVKTSLNGVSIGALTRYHDILSNDIVKSKVPLMHHATRTIGDMQVRNMGTIGGAISNADPASDMPVVLTALNATIILSSASGSRSVKALDFFKGPFTTDTNKGELVTQIEVPVLDGYKTVYKKVVRRAGDYALASVALAIKLKGNEIEDIKLAYGGVHDKPFRAMEVEKNVIGKKLNDDLVKDIASKVSSQINPPSDHRGSSWYRREVVKVLTMKAFKEVA", "text": "FUNCTION: Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme shows a broad substrate range (glyceraldehyde-3-phosphate, formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MELKAMYLYAAVLAVLLCSSVNFIQSPTDVLGPVALLEPTPSSARDFGAVVSDAPFAVMRPESPDDIALLLGALSSTAPSPRATVAAVGAGHSLHGQAQARDGIVVETRALPRDVHVVSARAHGGDDDATVRAYADVGAGALWVEVLEECLKLGLAPPSWTDYLYLTVGGTLSNGGISGQTFKHGPQISNVLQLEVVTGKGEVVTCSPTEIPELFFAVLGGLGQFGIITRARIPLQLAPPKVRWVRAFYDSFETFTGDQELLVSMPEQVDYVEGFMVLNEQSLHSSSVAFPAQLNFSPDFGSKGRKKVYYCIEFAVHDFQQDSSRADHVVKLVSAKLSYLRPHVYSVEVSYFDFLNRVRMEEESLRSRGLWDVPHPWLNVFVPKHGITQFKGLLMDTVSADDFEGPILVYPLLTDKWDGNTSAVVPAAPDGVMYIFGVLRSTDPARCGRACVDSIMARHRRVADEACRDGGGGGRGIGAKQYLARQPSPARWRDHFGAGWGRFAARKARFDPLHVLGPGQGIFPRTDSAGSM", "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": "MKVKIKCWNGVATWLWVANDENCGICRMAFNGCCPDCKVPGDDCPLVWGQCSHCFHMHCILKWLHAQQVQQHCPMCRQEWKFKE", "text": "FUNCTION: Together with the cullin protein ANAPC2, constitutes the catalytic 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. May recruit the E2 ubiquitin-conjugating enzymes to the complex. FUNCTION: Together with the cullin protein ANAPC2, constitutes the catalytic 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. May recruit the E2 ubiquitin-conjugating enzymes to the complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the RING-box family."}
+{"protein": "MNTEASQDQTVTETPGVRLRQARESLGLTQQTVAERLCLKVSTIRDIEEDNAQANLASTFHRGYIRSYAKLVHLPEDELLPILEKQAPVRAAKVAPMQSFSLGKKHKKRDGWLMSFTWLIVLVVLGLTGAWWWQNHQAQQAEIANMVDQSSAQLSQNGGQPVPLTDDNSDAIAPTDAPAPVANGQPVPLTNHSTSAVTNSATTSSATTSSVPTTSSVPKTTLVPKTTLVPKTNSTEPVDTANTNTTMHQEGAASAAVSPSQVPQLGMPTDQPPLPTADAGVSGSASSVGALVMNFTADCWLQVVDATGKTLFSGIQKGGAVLNLAGKAPYKLTIGAPGALTISYQGNPVDLSKFIKANRVARLTVGVE", "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": "MRIRKNITKFIKRAYIDMGELKQVKGYTKTRLNIISNKVFLLKQELYPLKKQKKVGKLKKKRVTTYTRKKLKRILSLLFRIGGKIYRRKIKKKKINLKKKEEHFTNNLILYRLFRKFYINLKLKQFKRLYKKYKGNEKIIIQQLEKRIDMILLRSGFVRSIYEARQLINHKHILVNGNIARIPSYTLNVGDIISIKEGSHKQNLIHRLKKILLPKVVPEHKKNLIHRFVSKGMDKYKYNYKQKYQPNDKAKYQQNYKYQAKRRRESKKKRRIRATGPKYLEISHALLLISLIEEPKLTAIKYPFTLQPENNIKFISLLNKYKRIR", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS4 family."}
+{"protein": "MLRLSLSPTYSLGFHLLAMMTLLISHVDHITAETEMVEEGNETGECTGSYYCKKGVILPIWEPQDPSFGDKIARATVYFVAMVYMFLGVSIIADRFMSSIEVITSQEKEITIKKPNGETTKTTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFTAGDLGPSTIVGSAAFNMFIIIALCVYVVPDGETRKIKHLRVFFVTAAWSIFAYTWLYIILSVISPGVVEVWEGLLTFFFFPICVVFAWVADRRLLFYKYVYKRYRAGKQRGMIIEHEGDRPSSKTEIEMDGKVVNSHVENFLDGALVLEVDERDQDDEEARREMARILKELKQKHPEKEIEQLIELANYQVLSQQQKSRAFYRIQATRLMTGAGNILKRHAADQARKAVSMHEVNTEVAENDPVSKIFFEQGTYQCLENCGTVALTIIRRGGDLTNTVFVDFRTEDGTANAGSDYEFTEGTVVFKPGETQKEIRVGIIDDDIFEEDENFLVHLSNVKVSSEASEDGILEANHISTLACLGSPSTATVTIFDDDHAGIFTFEEPVTHVSESIGIMEVKVLRTSGARGNVIVPYKTIEGTARGGGEDFEDTCGELEFQNDEIVKTISVKVIDDEEYEKNKTFFLEIGEPRLVEMSEKKALLLNELGGFTITGKHLYGQPVLRKVHARDHPIPSTVITIADEYDDKQPLTSKEEEERRIAELGRPILGEHTKLEVIIEESYEFKSTVDKLIKKTNLALVVGTNSWREQFIEAITVSAGEDDDDDECGEEKLPSCFDYVMHFLTVFWKVLFAFVPPTEYWNGWACFIVSILMIGLLTAFIGDLASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAATQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIYHAANGEQFKVSPGTLAFSVTLFTIFAFINVGVLLYRRRPEIGGELGGPRTAKLLTSCLFVLLWLLYIFFSSLEAYCHIKGF", "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:7986817). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. 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. SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. 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": "MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC", "text": "FUNCTION: Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9 (PubMed:11029580, PubMed:1371271). Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway (PubMed:2383557). Acts also intracellularly (PubMed:22265821). For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha- synuclein/SNCA cleavage (PubMed:21330369). In addition, plays a role in immune response and possesses antiviral activity against various viruses such as vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1 (PubMed:35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed:35940311). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Nucleus Cytoplasm. SIMILARITY: Belongs to the peptidase M10A family."}
+{"protein": "MPLPNQIATSNVETKNFASLKRSDEPIAIAQASRTPAKIYFDFQATTPVDPRVLDAMLPYFTKKYGNPHSRTHSFGWESEKAVETARKQVADLIGAHEKEIIFTSGATESNNLAIKGAVDWKAQDGNPVHVITTQVEHKCVLDSMRFLEEKGARVTYMKVNKDGVIDLEELKRSISDDTVLVSIMGVNNEIGTVQPLEEIGKICKERNVLFHCDAAQMFGKLKIDVNKMNIDLLSISGHKIYGPKGVGALYVRRRPRVRLVPLFSGGGQERGLRSGTLPTPLIVGLGKAAAVCQEEMQRDLSWIESLSKKLYTCLKENIPNVIKNGSLQTNPLRWFPGCLNLSFPHVEGEGLLMALKNIALSSGSACTSASLEPSYVLRALGNDDELAHSSIRFGIGRFTTPCEIKEVAKQTTSAVKKLRDMSPLYEMEQEGIDLKTIKWT", "text": "FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe- S) clusters in mitosomes. SUBCELLULAR LOCATION: Mitosome. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily."}
+{"protein": "MNGGGRRRYSSEQLMFDVPANAGGGAGKWGQRGGVRRGDGEIFVSVEPTTPARLRGGEAAAAAAGESPGQRQQLSPGLLDLHAFDTELISDFQVPGIGMYDGAQKFGYGNGGFDDSDPTFAPNKQMSKSTVFAESNFLKAFPEKEKAAPVAKIKVVVRKRPLNKKEISKKEEDIIDIEQQSNSLTVHETKLKVDLTEYVEKHEFVFDAVLDEDVSNDEVYRETVEPVVPAIFNRTKATCFAYGQTGSGKTYTMRPLPLKASQDILRLMHHTYRNQGYQLFVSFFEIYGGKLFDLLNERSKLCMREDGKQKVCIVGLQEYRVSDVETIKELIEKGNATRSTGTTGANEESSRSHAILQLAIKKRVDGNDSKPPRLAGKLSFIDLAGSERGADTTDNDKQTRIEGAEINKSLLALKECIRALDNDQTHIPFRGSKLTEVLRDSFIGDSRTVMISCISPSSGSCEHTLNTLRYADRVKSLSKGSNTKKDLSLAAAPLRESSPSLLASAVPSFSSAEVMNDITERSNFGWTKQQYVKEHQAPTFVDRMQKVKEDTEFSLSNGGYFKEQRTKGSVPVGIAEVPDTVYQQGRQPTRKARDLTSDNNMRNSIAYPIIRRVVPDEDEHLNELLQEEEDLVSAHRKQVEETLDMIKEEMNLLVEADQPGNQLDDYITRLSGILSQKAAGIVDLQARLAQFQRRLNENNVLLYAQCP", "text": "SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-13 subfamily."}
+{"protein": "MWNSGFESFSSSSYGAAGGYTQSPGGFGSPTPSQAEKKSRARAQHIVPCTISQLLSATLTDEVFKIGDVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSGENTVVPPETYVKVAGHLRSFQNKKSLVAFKIIPLEDMNEFTAHILEVVNSHLMLSKANSQASVGRPSMSNPGMGEPGNFSGNNFMPANGLTVVQNQVLNLIKACPRPEGLNFQDLRSQLQHMPVASIKQAVDFLCNEGHIYSTVDDDHFKSTDAE", "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 Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner. SIMILARITY: Belongs to the replication factor A protein 2 family."}
+{"protein": "MAATRNLSLLAQSSQPWAGIYGSHGSPRPISSWLRRQSIAKTSYICMCTPLSMSQLIATPLITDIESLLKYLRQPQVLPHEIDDSTKRRELLERTRRELQTTLEPLQAMKMIDTLQRLGLAYHFEDDINSLLTGFSNGQPDEDLLTASLRFRLLRHNGHRINPNIFQKFMDKQGKFIDSLKEDTRGLFSLYEASYLGANGEDILLQALEFTKAHLKESLPSLAPPLAKKVSQALELPRHRRMARLEARRYIEEYGGENGHSPDLLELAKLDYNKVQSLHQLELSEISRWWKQLGLVDKLTFARDRPLECFLWTVGILPEPKYSSCRIELAKTIAILLVIDDIFDTHGTLDELILFTNAIRRWDLEAMEDLPEYMRICYMALYNTTNEICYKILKQNGWSVLPYLKATWIDMIEGFMLEASWLNTGYVPNMEEYVENGVTTAGAYMALVHLFFLIGQGVTEENVKLLVKPYPKLFSYSGRILRLWDDLGTAKEEQERGDLASSIDLFMRENNITSDEEGRKCILKIIDNLWKELNGELVSRHALPLAIIKAAFNMARASQVVYQHEEDSYFSSVDNYVQALFFTPFN", "text": "FUNCTION: Monoterpene synthase involved in the biosynthesis of volatile organic compounds (PubMed:25956881). Mediates the conversion of (2E)- geranyl diphosphate (GPP) into the acyclic monoterpene, geraniol (PubMed:25956881). Does not use (2E,6E)-farnesyl diphosphate (FPP) as substrate (PubMed:25956881). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsg subfamily."}
+{"protein": "MDRNQKMDHVIGGKFKLGRKLGSGSFGELYLGINIQTGEEVAVKLEPVKTRHPQLQYESKIYMFLQGGTGVPHLKWFGVEGEYSCMVIDLLGPSLEDLFNYCKRIFSLKSVLMLADQLICRVEYMHSRGFLHRDIKPDNFLMGLGRRANQVYIIDYGLAKKYKDLQTQKHIPYRENKNLTGTARYASVNTHLGIEQSRRDDLESLGYVLMYFLRGSLPWQGLKAGTKKQKYDKISEKKMLTSVETLCKSYPSEFTSYFHYCRSLRFEDKPDYSYLRRLFRDLFIREGYQLDYVFDWTISKYPQIGSSSRPRPTPRPALDPPGPPAERAEKPTVGQDLRGRFTGAIEAFTRRNVSSQGALGDRSRHRSSDDIPSSAKEVHESRNGSTSKRGVISSTRPGSSAEPSENHSSRLFSSGSRHATTQRVPQSYESAAAARPGHEDAIRNFELLTIGSGKKRK", "text": "FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate casein, phosvitin, myosin light chains and poly(Glu,Tyr) in vitro. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily."}
+{"protein": "MAAADVEYRCFVGGLAWATNNETLEQAFANFGQVIDSKVITDRETGRSRGFGFVTFSSEQSMLDAIENMNGKELDGRNITVNQAQSRGGGGGGGGYGGGGGGYGGREGGGYGGGGGGYGGRREGGGGYGGGGYGGGGGGYGGREGGGGYGGGGGYGGNRGDSGGNWRN", "text": "FUNCTION: Possibly has a role in RNA transcription or processing during stress."}
+{"protein": "MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGDDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIAHQMGIESLMTRLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGIKSHIL", "text": "FUNCTION: Part of the ABC transporter complex ThiBPQ involved in thiamine import (PubMed:9535878). Responsible for energy coupling to the transport system (Probable). Is also involved in thiamine pyrophosphate (TPP) transport (PubMed:9535878). 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": "MSLYQRYLSKSLIFIFSLFFLILFFLESSIGFKYFFNFTNYFFIGLKTEEISGNWRDFKLKKINFNIFGTSIKAESVHIITDPISLFKVSTILKKIKTKNLVISFNKKIKKVALKNNFLKEKKIKNTIFFKHSLILRKIYSDKILLKTQKKNIFLFGVFSGLQLSNDTCTFLPTKINSIYIDSSMRNVKNIDNKKSNFFIKKDIFYRNKIDNALSFFSIFKNFFIPININLINLKCNQLKFFNRTFLDIYKIKMSAQLKKNILKIKKIQIYSKYFKTKSKGKIFFRSDFSIFFIVKNEMSINIINNKAMNLLFKDTIDHKLNFKSNNLIKFNIHGEISLDDLNYPIHINLHLNRLFLPISKNLILSSKNFNFSLKGKINNYFLSLKNIINISGMPSFFISISAIGNIQNVVIKKIHFFPFFKEIKTKKFIKIKKEIDYNKYITQLAGKMRILSDFNKQSSNIFLPYFHVYGDFMRKKISVLGSLYYRKLNGITIPRINFLLGKNKGHISGSISKKVNLRSSIYANNLNYFSPNLKGIIKATLNIYSFCSLPSFSSVILGQKINWKNILYFNNIKITTNGNLKKSFPNKFFADFKNIRFSKFHINSLHIKSDWNNINQKFSLSLKDKKLSITFILNGHLNRKVGIWKGVLKKIDVKTSWGQWISRNNPLIFYHIKNSINFKNIKKIKNKNAFYSAINNIQTSLFKLIRQSPVKFQTDLFFNTQFQWKLRENITNLKLFLKGSNINLEKKIKEKIMFEKISAVNLYINFKKNNFITKWIIKKSKNSLKVNKISGFLNIYDFFHEKKIEGKVFLSDFSCSFLNFFENFFTKIQGKFSGNINFLGTIYQPQISADINFQDFYIKSDKIFKYMLLFFCSFPNKIENIKINQEIIMKKGNALFKLNSVVKNNISHIKWNILFHSNKLAIVLFPKIKLNFSSQLNLYYFLSKYDLIGYLKFSFFSFKINEKNFLF", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: To E.coli YtfN."}
+{"protein": "MAAAAGGGAAPFVWKTYRMVEDPGTDGVIGWGKGNNSFVVADPFVFSQTLLPAHFKHNNFSSFVRQLNTYGFRKVDPDRWEFAHASFLRGQTHLLRNIVRRGSAAAGGGGGGGGGKRRDASADGGGGGGDEDMTMVATEVVRLKQEQRTIDDRVAAMWRRVQETERRPKQMLAFLLKVVGDRDKLHRLVGGGGNGNGAATAAAADNGFADAARAGCGEKRARLLLDGDNTGAFGPDAVDFAGFYTGADMFPDVAVDAAAAAAGGSAGCSFAFGVDSGY", "text": "FUNCTION: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HSF family. Class C subfamily."}
+{"protein": "MDGKSKMQAEKHLTGTLVLSVFTAVLGFFQYGYSLGVINAPQKVIEAHYGRMLGAIPMVRHATNTSRDNATITVTIPGTEAWGSSEGTLAPSAGFEDPTVSPHILTMYWSLSVSMFAVGGMVSSFTVGWIGDRLGRVKAMLVVNVLSIAGNLLMGLAKMGPSHILIIAGRAITGLYCGLSSGLVPMYVSEVSPTALRGALGTLHQLAIVTGILISQVLGLDFLLGNDELWPLLLGLSGVAALLQFFLLLLCPESPRYLYIKLGKVEEAKKSLKRLRGNCDPMKEIAEMEKEKQEAASEKRVSIGQLFSSSKYRQAVIVALMVQISQQFSGINAIFYYSTNIFQRAGVGQPVYATIGVGVVNTVFTVISVFLVEKAGRRSLFLAGLMGMLISAVAMTVGLVLLSQFAWMSYVSMVAIFLFVIFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFCNWACNFIVGMCFQYIADLCGPYVFVVFAVLLLVFFLFAYLKVPETKGKSFEEIAAAFRRKKLPAKSMTELEDLRGGEEA", "text": "FUNCTION: Facilitative hexose transporter that mediates the transport of glucose, fructose and galactose. Likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily."}
+{"protein": "MSGVSEEDPEGLAPQGLPALGGACLATMDKKLNVLTEKVDRLLHFQEDVTEKLQCVCQGMDHLEQDLHRLEASRELSLAGSGSTPPTTAQAAWPEVLELVRAVRQEGAQHGARLEALFKMVVAVDRAITLVGSTFQNSKVADFIMQGTVPGRKGSLADGPEENKEQAEVAGVKPNHVLTTGGVQADASRTLWEESQKEDIPVRTVEGLPLIINTSLKGADLTQAGASLRQGVEVLGPGQVPLPTEAESRLPETASENTGATLELSVAIDRISEVLTSLKMSQGGGQETSSSKPDCWLSEEAMRLSSGPLPQPLGPLTPDSDIHSGDALPRIPINMQEMATPGELLETQSGSPIGSAEAPGLGTVLEDQIPKGARPFPPLPKRSSNNGGMSAEEEIGSGAEPMRGPSLATRDWRDETVGTTDLQQGIDPGAVSPEPGKDHAAQGPGRTEAGRLSSAAEAAIVVLDDSAAPPAPFEHRVVSIKDTLISAGYTVSQHEVLGGGRFGQVHRCTERSTGLALAAKIIKVKNVKDREDVKNEVNIMNQLSHVNLIQLYDAFESKSSFTLIMEYVDGGELFDRITDEKYHLTELDVVLFTRQICEGVHYLHQHYILHLDLKPENILCVSQTGHQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYEFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNFIVNCSWDFDADTFKGLSEEAKDFVSRLLVKEKSCRMSATQCLKHEWLSHLPAKASGSNVRLRSQQLLQKYMAQSKWKKHFHVVTAVNRLRKFPTCP", "text": "FUNCTION: Kinase that phosphorylates MYL2 in vitro (PubMed:18202317, PubMed:17885681). Has been proposed to be calmodulin-dependent (PubMed:17885681), although MYL2 phosphorylation has also been observed in the presence or absence of calmodulin (PubMed:18202317). Promotes sarcomere formation in cardiomyocytes and increases cardiomyocyte contractility (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
+{"protein": "MKTQTLLFTFSLVLLMVATQTEALLGGLLQSLLGKRGLLDNLLGKRGLLFGKRALTNQDLFDLAYDPSLSAADMDALEMLLENY", "text": "FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Forms an alpha-helical membrane channel in the prey. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family."}
+{"protein": "MAEQESLEFGKADFVLMDTVSMPEFMANLRLRFEKGRIYTFIGEVVVSVNPYKALNIYGRDTIEQYKGRELYERPPHLFAIADAAYKAMKRRSKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIVQQPGERSFHSFYQLLQGGSEQMLRSLHLQKSLSSYNYIHVGAQLKSSINDAAEFKVVADAMKVIGFKPEETQTVYKILAAILHLGNLKFMVDGDTPLIENGKVVSIIAELLSTKTDMVEKALLYRTVATGRDIIDKQHTEQEASYGRDAFAKAIYERLFCWIVTRINDIIEVKNYDTTIHGKNTVIGVLDIYGFEIFDNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIIAILDDACMNVGKVTDEMFLEALNSKLGKHGHFSSRKLCASDKILEFDRDFRIRHYAGDVVYSVIGFIDKNKDTLFQDFKRLLYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIEHCGFQDDVAYGKTKIFIRTPRTLFTLEELRAQMLIRIVLFLQKVWRGTLARMRYKRTKAALTIIRYYRHYKVKSYIQEVARRFHGVKTMKDHGKHVKWPTPPKVLRRFEEALQAIFNRWRASQLIKSLPASDLPQVRAKVAAMEMLKGQRADLGLQRAWEGNYLASKPDTPQTSGTFVPVANELKRKDKYMNVLFSCHVRKVNRFSKVEDRAIFVTDRHLYKMDPTKQYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGELVGVLVNHFKSEKRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPEPDFTKNRSGFILSVPGN", "text": "FUNCTION: Unconventional myosin that functions as actin-based motor protein with ATPase activity (By similarity). Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (PubMed:11208135). Required for normal planar cell polarity in ciliated tracheal cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement in the trachea. Required for normal, polarized cilia organization in brain ependymal epithelial cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm Perikaryon Cell projection, dendrite Early endosome Cytoplasm, cell cortex Note=Colocalizes with the actin cytoskeleton in the cell cortex close to the apical cell membrane (PubMed:11208135). Colocalizes with cytoplasmic puncta that are reminiscent of transport vesicles (By similarity). SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family."}
+{"protein": "MATKNKPNLSVQDVKLLNVNELTPLTPNVISRQATINIGTIGHVAHGKSTVVKAISGVLTVRFTSEFKRNITIKLGYANAKIYKCDNPQCERPGCYKSARSNTEDNPQCERPGCGGRMTLLRHVSFVDCPGHDVLMATMLNGAAVMDAALLLIAGNESCPQPQTSEHIAAIEIMNLKNIIILQNKIDLVKEAAAQEQYGQILKFIQGTIAENAPIIPISAQMKYNIDVICEYIVKKIPIPVRDFTSDPRMIVIRSFDVNKPGSRVDEIKGGVAGGSILKGVLKIGDEIEVRPGVISKELDGKIKCSPIFCRIISLFAEENELQYAVPGGLIGVGTKIDPTLCRADRLVGQVLGSVGKLPEIFVALEVNFFLLRRLLGVKSDGDKQSKVKKLSKEDTLMVNIGSTSTGCRVVAVKHDLAKLQLLTPVCSQEGEKIALSRRVDKNWRLIGWGEIKKGTVLTN", "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": "MQLLCYFVILFVGIAPWSSLANDDGCNEVVCGSVVSKCLITQSCQCKLNDCHCCKDCLNCLGELYIECCGCLDMCPKHKDVLPSLTPRSEIGDIEGVPELFDTLTAEDDEGWSTIRFSMRAGFKQRVQGGASGDAGNGNGNGNAGSAGVTLCTVIYVNSCIRANKCRQQCESMGASSYRWFHDGCCECVGENCLNYGINESRCRGCPEDQDQLLTADTVPAEAEQDLERFFGNEEIEDEWGYGEEDEFS", "text": "FUNCTION: Involved in dorsal-ventral patterning. Required for specification of a narrow strip of dorsal midline cells that will give rise to the amnioserosa, but not for specification of dorsal ectoderm cells. Inhibits BMP signaling; enhances the binding of sog to dpp, thus enhancing the antagonistic activity of sog. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the twisted gastrulation protein family."}
+{"protein": "MTNPVSTIDMTVTQITRVAKDINSYELRPEPGVILPEFTAGAHIGVSLPNGIQRSYSLVNPQGERDRYVITVNLDRNSRGGSRYLHEQLRVGQRLSIVPPANNFALVETAPHSVLFAGGIGITPIWSMIQRLRELGSTWELHYACRGKDFVAYRQELEQAAAEAGARFHLHLDEEADGKFLDLAGPVAQAGQDSIFYCCGPEAMLQAYKAATADLPSERVRFEHFGAALTGEPADDVFTVVLARRSGQEFTVEPGMTILETLLQNGISRNYSCTQGVCGTCETKVLEGEPDHRDWVLSDEKKASNSTMLICCSLSKSPRLVLDI", "text": "FUNCTION: Involved in the degradation of the xenobiocide pentachlorophenol (PCP) (PubMed:19325743, PubMed:23676275). Catalyzes the reduction of tetrachlorobenzoquinone (TCBQ) to yield tetrachlorohydroquinone (TCHQ) (PubMed:19325743, PubMed:23676275). Also able to reduce 2,6-dichloroindophenol (DCIP) (PubMed:23676275). SIMILARITY: Belongs to the PDR/VanB family."}
+{"protein": "MKTISFNFNQFHQNEEQLKLQRDARISSNSVLELTKVVNGVPTWNSTGRALYAKPVQVWDSTTGNVASFETRFSFSIRQPFPRPHPADGLVFFIAPPNTQTGEGGGYFGIYNPLSPYPFVAVEFDTFRNTWDPQIPHIGIDVNSVISTKTVPFTLDNGGIANVVIKYDASTKILHVVLVFPSLGTIYTIADIVDLKQVLPESVNVGFSAATGDPSGKQRNATETHDILSWSFSASLPGTNEF", "text": "FUNCTION: Lectin. SIMILARITY: Belongs to the leguminous lectin family."}
+{"protein": "MRNTILFGVSMILLANLCFGIMSAFVKITADYFSPMENVFYRSITMTLLLLLIYPFKPYRLKSYKQGGFKKLAFRVVVGGLAMLAFFYNIEKISLATATAFSQCAPIYTVLLSPLLLKEKLKRSTLISACIGIVGVVLISDPSVENVGPVEIFMGILSGIFVSLAYITLRDLREYYDKQAVILAFAFGMSLLGLVGMFIDIPFLSTGIHVPRKEDILWISLIGISGTLGQYFLTYAYMNAPAGIIAPIEYTRIVWGLLFGLYLGDTFLDLKSSLGVALILCSGLLIALPALLKELKKI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EamA transporter family."}
+{"protein": "MALLEICCYSMECALTAQQNGADRVELCAAPKEGGLTPSLGVLKSVRQRVTIPVHPIIRPRGGDFCYSDGEFAAILEDVRTVRELGFPGLVTGVLDVDGNVDMSRMEKIMAAAGPLAVTFHRAFDMCANPLNTLNNLAELGITRVLTSGQKSDALQGLSKIMELIAHRDAPIIMAGAGVRAENLHHFLAAGVLEVHSSAGAWQASPMRYRNQGLSMSSDAHADEYSRYVVDGAAVAEMKGIIERHQAK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CutC family."}
+{"protein": "MITASTSVFGGLILAFIFSLLYKNKKTRIPAEIDRVRTGGFLAHIRAFGCRLGTRVDDIRNGYNKFNKNGKPFVIQDSTFIPQVVIPPQYLGWLKEQPEKALSAETVRLEQLGLRYLVPSSDPEMVHLLTDVVCRYLTRNFQRVQERLYEELHMSTDEIMGLEATEWRQICLHEAMETILRRMISCVLIGLPWCRDEECLKSWTGFLHCMAIAGTILGAVTPWFLRPLLGLLLKPPVGYMRRRSLRYLTPIFTERWKKIEKHEKSSLTTRELPDDFVTWCIQEVRNGAAEVTMLDLLSADPTIGYWEKLVEEATTAFRTDEDWIHAGTVSKLAYTDSAIRESLRRNPFSIRNVTREVIGKDGLTLPSGTRLPQGTWITTALANIHHDARFYSNPTEYQPFRFVARDAFHTEGKEGSEKVLQPSEAILTSTIDERLLTFGYGRRACPGRWFASHILKMLIAYITINYDIQPLTGPPKKVKFADFTVPSPSIKIIVRRKNLAYLRQRER", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NA). Nodulisporic acid A (NAA) and its chemically modified derivatives are of particular significance because of their highly potent insecticidal activity against blood-feeding arthropods and lack of observable adverse effects on mammals, in particular the tremogenicity associated with the paspaline-derived IDTs is not observed (PubMed:29283570). The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (PubMed:29283570). Condensation of indole-3- glycerol phosphate with GGPP by the prenyl transferase nodC then forms 3-geranylgeranylindole (3-GGI) (PubMed:29283570). Epoxidation by the FAD-dependent monooxygenase nodM leads to a single-epoxidized-GGI that is substrate of the terpene cyclase nodB for cyclization to yield emindole SB (PubMed:29283570). The terminal methyl carbon, C28, of emindole SB is then oxidized by the cytochrome P450 monooxygenase nodW to produce nodulisporic acid F (NAF), the pentacyclic core of NAA (PubMed:29283570). NAF is converted to nodulisporic acid E (NAE) via prenylation. This step is probably performed by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). Several oxidation steps performed by the FAD-linked oxidoreductase nodO and one of the cytochrome P450 monooxygenase nodR, nodX or nodZ further convert NAE to nodulisporic acid D (NAD) (Probable). NAD is substrate of cytochrome P450 monooxygenase nodJ to produce the precursor of nodulisporic acid C (NAC), converted to NAC by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). The FAD- dependent monooxygenase nodY2 then oxidizes NAC to nodulisporic acid B (NAB) (Probable). Finally NAB is converted to NAA by one of the cytochrome P450 monooxygenases nodR, nodX or nodZ (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MSTTSRPGLWALITAAVFALCGAILTVGGAWVAAIGGPLYYVILGLALLATAFLSFRRNPAALYLFAVVVFGTVIWELTVVGLDIWALIPRSDIVIILGIWLLLPFVSRQIGGTRTTVLPLAGAVGVAVLALFASLFTDPHDISGDLPTQIANASPADPDNVPASEWHAYGRTQAGDRWSPLNQINASNVSNLKVAWHIHTKDMMNSNDPGEATNEATPIEFNNTLYMCSLHQKLFAVDGATGNVKWVYDPKLQINPGFQHLTCRGVSFHETPANATDSDGNPAPTDCAKRIILPVNDGRLVEVDADTGKTCSGFGNNGEIDLRVPNQPYTTPGQYEPTSPPVITDKLIIANSAITDNGSVKQASGATQAFDVYTGKRVWVFDASNPDPNQLPDDSHPVFHPNSPNSWIVSSYDRNLNLVYIPMGVGTPDQWGGDRTKDSERFAPGIVALNADTGKLAWFYQTVHHDLWDMDVPSQPSLVDVTQKDGTLVPAIYAPTKTGDIFVLDRRTGKEIVPAPETPVPQGAAPGDHTSPTQPMSQLTLRPKNPLNDSDIWGGTIFDQMFCSIYFHTLRYEGPFTPPSLKGSLIFPGDLGMFEWGGLAVDPQRQVAFANPISLPFVSQLVPRGPGNPLWPEKDAKGTGGETGLQHNYGIPYAVNLHPFLDPVLLPFGIKMPCRTPPWGYVAGIDLKTNKVVWQHRNGTLRDSMYGSSLPIPLPPIKIGVPSLGGPLSTAGNLGFLTASMDYYIRAYNLTTGKVLWQDRLPAGAQATPITYAINGKQYIVTYAGGHNSFPTRMGDDIIAYALPDQK", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein; Periplasmic side. SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family."}
+{"protein": "MKAQDLREKSVEELNSELLNLLKEQFNLRMQAATGQLQQTHTLKAVRRDIARVKTVLTEKAGA", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL29 family. SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
+{"protein": "MASLRIAPLALFFFLAASVMFTVEKTEAGIPCGESCVFIPCITAAIGCSCKSKVCYRNHVIAAEAKTMDDHHLLCQSHEDCITKGTGNFCAPFPDQDIKYGWCFRAESEGFLLKDHLKMSITN", "text": "FUNCTION: Probably participates in a plant defense mechanism (Probable). Active against Gram-negative bacteria E.coli ATCC 700926 (MIC=1.0 uM), K.pneumoniae ATTC 13883 (MIC=5.5 uM) and P.aeruginosa ATCC 39018 (MIC=7.5 uM) (PubMed:21596752). Has hemolytic and cytotoxic activity (PubMed:21596752). SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily."}
+{"protein": "MAYIQLEPLNEGFLSRISDVLLCGWTCQHCCQRCYESSCCQSSEDEVEILGPFPAQTPPWLMASRSNDKDGDSVHTASDVPLTPRTNSPDGRRSSSDTSKSTYSLTRRISSLDSRRPSSPLIDIKPIEFGVLSAKKEPIQPSVLRRTYTPDDYFRKFEPRLYSLDSNLDDVDSLTDEEIMSKYQLGMLHFSTQYDLLHNHLTVRVIEARDLPPPISHDGSRQDMAHSNPYVKICLLPDQKNSKQTGVKRKTQKPVFEERYTFEIPFLEAQRRTLLLTVVDFDKFSRHCVIGKVAVPLCEVDLVKGGHWWKALIPSSQNEVELGELLLSLNYLPSAGRLNVDIIRAKQLLQTDVSQGSDPFVKIQLVHGLKLVKTKKTSFLRGTIDPFYNESFSFKVPQEELENASLVFTVFGHNMKSSNDFIGRIVIGQYSSGPSESNHWRRMLNTHRTAVEQWHSLRSRAECDRVSPASLEVT", "text": "FUNCTION: Plays a role in dendrite formation by melanocytes. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the synaptotagmin family."}
+{"protein": "MDIFLAILPAIFWGSIVLFNVKLGGGPYSQTLGTTFGALIFSIVVYIFMKPVLTPTVIGVGIVSGLFWALGQANQLKSIDLMGVSRTMPISTGLQLVATTLFGVIVFHEWSTTISVVLGVLALVCIIIGVILTSLQSEEEKNAEQAGNFKRGIIILLISTVGYLVYVVVIRLFNVDGWSALLPQAVGMVLGGILLTFKHHPFNKYAIRNIIPGLIWAAGNMFLFISQPRVGVATSFSLSQMGIIISTLGGILILGERKTKRQLTGIVVGIVFIIAAGIMLGIAKS", "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": "MGKKSKATKKRLAKLDNQNSRVPAWVMLKTDREVQRNHKRRHWRRNDTDE", "text": "FUNCTION: Binds to the 23S rRNA. Forms part of the polypeptide exit tunnel. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family."}
+{"protein": "MSTSRLQQQFIRLWQRYNGQSTETTLQALAEVLNCSRRHVRSLLGKMQHAGWLDWQAEAGRGKRSQLIFLRSGLALQQQRAEELLEQDHIDQLVQLVGDKKAVRQMLLSQLGRSFRQGKHILRVLYYRPLENLLPGTALRRSETHMVRQIFNGLTRINEENGELEPDLSHHWQAITPLHWRFYLRPAIHFHHGRELEMSDVISSLTRLIPQPLFSHIAEVRSPTPYVIDVYLHSPDHWLPWLLGSVHAMILPQEWETQPDFHRQPIGTGPYSVIRNHHSQLKIQAFDNYFGFRALIDEVNIWVLPELSEELVYSGVQLQADDTGKNELESRLEEGCYFLLFDQRSPQACTPEIRRWLCELITPIALLSHAAPFYQRYWSPAYGMLPRWHHNRLTTQEPKPEGLNELTLTFYSEHSEFDAISQTLTQLLAAQGVTLKIQVLDYTRWYQGDAQSDIWLGSANFYLPLEFSLFATLYEMPLLQHCLSEELHQDIESWRNNTLLMADWSQRLVSQHQFHPLFHHWLELYGQHSMRGVRMNTLGWFDFKSAWFTPPEA", "text": "FUNCTION: Activates the small RNA gene sgrS under glucose-phosphate stress conditions as well as yfdZ. Represses its own transcription under both stress and non-stress conditions. Might act as a sensor of the intracellular accumulation of phosphoglucose by binding these molecules in its C-terminal solute-binding domain."}
+{"protein": "MDEKTIKKSILSSSNDEKIIYKSRIKKFQKNHKFYIILLVFIAILQFISIAFFTRGFLLSRHVLDNISSQNETSKLPPRFNKAVILVIDALRFDFAIPVNESHSNYNLNYHNNILSLYDSFASDKDASSLLLKFIADPPTTTLQRLKGLTTGSLPTFIDAGSNFDGTVIEEDNFLKQLHLANKTVKFAGDDTWMALFHPFLSNDSFPLESLNVWDLDTVDNGVMDYFHDHLQQDKEWDVMIGHMLGIDHVGHKYGPDHFTMREKQIQVDQFIDWILKSIDDDTLLVILGDHGMDHTGNHGGDSIDELESTLFLYSKKPDMWRLKETSNYNIDNLGHDYRSVRQIDLVSSLALLMGQPIPFNNLGWPIDEIARNDREWSQFVNSAISQLQLYKDTMQIHHGNDEILEPLAKNISNTPPTSDPEKFVKLGHKYQKVFLQTCEELWAKFDYYSIATGITLLATSLVLLISITKLIPSIVVNQMVPEFVPGIIIMVLVTNLCFHGIFYVYQQPSFVDQFWGTLLATAIGIIIGCYITIFDRYNFIWIAMRLGETLADYWSRIAVMFMIIHALLFTSNSFTIWEDRIVAFLLSTFGMLTLYEFVFLPKRQSTTALLTATISEKEGTTSGVNPSTANSNYLPLTRFARLLGGYHSAVLIIFTRLASMITICREEQGEYCIPTFNNQNNSSWWVLGLCFLMIFILPACITGYYNLTSSYQAAAPIWINVFLKGILGLNFVYWSLTSLENNSAVIAIPFLRDVTIFKFTLARIIAGFSLIASNVGWLMGPLCIKLNIHNTDVKSHEATILGYTNIYGSEFFLLVINVLISILLFNKPLAQLSYFLMCNQLLSILEIIDLLKLKENIIGPIALGLLSYQHFFTTGHQATIPSVQWDIGFMLSEKVTFPFTQIAIILNTFGPHILVSLSVALLTLWSQPPDVLKPQTLLGRIVSNCGILLTYNTILCLSSFIWVTHFRRHLMVWKIFCPRFIFASLSLIVTQLVVTFGTIAFASGRLIKHINDIFWK", "text": "FUNCTION: Involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond. Involved in cell wall biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily."}
+{"protein": "MWFLVFSIWIASGQLLPHISNVIEKELDQLEITELSREYINNKFPITQSSCVKNALGEFLEICMRKGFEFVDADLRVITAVRLSVCEFESSGLTNYPSECHEKRLGGIDTISCVNALESSPQWWTTYSGNYQNLPHICMENSLPFEKEQILELFLNITDMYSEFQRNIENYWKSFSSDLEINGKENIDMIQNLFNSLVNDLIQNHKMKDEELITEFDKMKAEFDIRFFNFTESFDNLNDEVNEDLSLIKSHLIETFRQVDSEYMAQLQKNKNSTDKAFNELESMSTYILDHQKTSMELIDSFFSDLIDLTRDKNLVISDELMQTQEETIHLIFQYNKLVHESVIPLLTDDLLPVVRGVSNSIVENLDNMNVELTSHLENVSQTIEVKFKALEKETDRSLLKAKEVESNLRNLNNLVSTSLKGLQTIVRLLTFLLKRQVVLVGILQIFLRKYISMNLYLYAIAVVVTALAGSKVGSWGSLLMKSFVTR", "text": "FUNCTION: Required for nuclear membrane fusion during karyogamy. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus membrane; Single-pass membrane protein. SIMILARITY: Belongs to the KAR5 family."}
+{"protein": "MSQNTLKVHDLNEDAEFDENGVEAFDEKALSEEEPSDNDLAEEELLSQGATQRVLDATQLYLGEIGYSPLLTAEEEVYFARRALRGDVASRRRMIESNLRLVVKIARRYGNRGLALLDLIEEGNLGLIRAVEKFDPERGFRFSTYATWWIRQTIERAIMNQTRTIRLPIHIVKELNVYLRTARELSHKLDHEPSAEEIAEQLDKPVDDVSRMLRLNERITSVDTPLGGDSEKALLDILADEKENGPEDTTQDDDMKQSIVKWLFELNAKQREVLARRFGLLGYEAATLEDVGREIGLTRERVRQIQVEGLRRLREILQTQGLNIEALFRE", "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 master transcriptional regulator of the stationary phase and the general stress response, including response to organic acid stress. 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 master transcriptional regulator of the stationary phase and the general stress response. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. RpoS subfamily."}
+{"protein": "MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHKIYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNECMKDDFFIKIETWHKPDLGTLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKELANSPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTMEDIRRMEDETQKELETLRNQGQVRGTSAASDE", "text": "FUNCTION: Catalyzes the transfer of phosphatidylinositol, phosphatidylcholine and sphingomyelin between membranes (By similarity). Required for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum; phosphatidylinositol and phosphatidylcholine transfer activity is essential for this function (By similarity). SUBCELLULAR LOCATION: Golgi apparatus Golgi apparatus membrane Endoplasmic reticulum membrane. SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer class I subfamily."}
+{"protein": "MNKIAVIGKVFVDIKGTSFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVEMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQSIYALDGVDAVAIDLDLSVTVLERLIHLCRKMELPLFGVCGHLSVIERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDRRTATSGHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIASTENGLVPEMLDALQ", "text": "FUNCTION: Catalyzes the phosphorylation of guanosine and inosine to GMP and IMP, respectively (PubMed:9357959, PubMed:11129609). Can also use deoxyguanosine (PubMed:9357959). Shows a strong preference for guanosine (PubMed:9357959). dATP, GTP and dGTP can serve as phosphate donors (PubMed:9357959). SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
+{"protein": "MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVDTAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNKKDLHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEKIDGAASQGKSSCSVM", "text": "FUNCTION: Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity. SUBCELLULAR LOCATION: Endomembrane system; Lipid-anchor; Cytoplasmic side Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side Cytoplasm, cytosol Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rheb family."}
+{"protein": "MQTSMFLTLTGLVLLFVVCYASESEEKEFPKELLSSIFAADSDFKEEERGCFGYKCDYYKGCCSGYVCSPTWKWCVRPGPGRR", "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": "MRKGLTLVEVLVTLVIMGIAFAALLTSQLANLRASAQARFATDAKAAAVQVLERRSAEVLKSEIVPALSPYKDAPLDPDNPSGNWRSFYFVDYYFSCPTRVAPSPKQRGGSVANLRPGLTCSGTETIFGIPVAWDIRGENGILGEGVVTVVVTATHPRGPKVTLGRRVTCYDVYPSPTQDQPAPCPPPGGGRP", "text": "FUNCTION: Plays an essential role in natural DNA transformation but is not required for pilus biogenesis. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein Cell outer membrane; Single-pass membrane protein Periplasm Note=The single N-terminal transmembrane is initially involved in the correct localization to the inner membrane. Once the leader sequence cleaved, this region plays a role in multimerization and protein-protein interactions in the periplasm and the outer membrane."}
+{"protein": "MDAAAIISLFILGSVLVTCSILLSSFSSRLGIPILVIFLAIGMLAGIDGIGGIPFDNYPFAYMVSNLALAVILLDGGMRTQASSFRVALGPALSLATVGVLITSGLTGMMAAWLFHLDIMEGLLIGAIVGSTDAAAVFSLLGGKGLNERVGSTLEIESGSNDPMAVFLTITLIEMIQQHETGLSWMFAWHILQQFGLGIIIGLAGGYLLQQMINRISLPAGLYPLLALSGGILIFALTTALDGSGILAVYLCGFLLGNRPIRNRHAILQNFDGLAWLAQIGMFLVLGLLVTPSDLLPIAIPALLLSAWMIFFARPLSVFAGLLPFRGFNLRERIFISWVGLRGAVPIILAVFPMMAGLDNARLFFNVAFFVVLVSLLFQGTSLGWAAKKAKVVVPPVGLPVSRVGLDIHPENPWEQFVYQLSADKWCVGASLRDLHMPTETRIAALFRDNALLHPTGSTRLREGDILCVIGRETDLPALGKLFSQSPPVALDQRFFGDFILEASAKFADVALIYGLDEGLEYRDKQQTLGEIVQQLLGAAPVVGDQVEFAGMIWTVAEKEDNAVRKVGVRPTEDEPE", "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": "MNEPEGLRFRRLNRPQIITDELQEPQYKGTSTYSGKVFRVILVTLGGCLILPLLVVFFLLESPIHPELLSLSEPPLMSGCYEPNFKLREAQRLFEDQLVGPESIANFGDLIYTGTADGKIVKIEGKSITVIARLGKPPCDGSREQEPSCGRPLGIRVGPNGTLFVADAYLGLFKVNPVTGEVTNLVSAGQMVGGRRLSFVNDLDVTQDGRKVYFTDSSSRWQRRDYLHLIMEATADGRVLEYDTETKEVTVLMENLRFANGIQLFPDEESVLVAETTMARIRRVHVSGLNKGGMDTFVDNLPGFPDNIRRSSSGGYWVAMSAVRPNPGFSMLDFLSQKPWIKKLIFKLFSQDVLMKFVPRYSLVIELQESGACMRSFHDPHGMVAAYVSEAHEHDGHLYLGSFRSPYLCKLDLSKV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the strictosidine synthase family."}
+{"protein": "MLQLNQVIHPDTRNKRFKFEPFLLKEYNFGLDPDRPVCQFYNPSNPNNSCPNGSLCPHKHVSSMYSNKIVCKHWLRGLCKKNDHCEFLHEYNLRKMPECLFYSKNGFCTQTPECLYLHVDPQSKIPPCSSYEKGFCPDGPKCANRHIRKIMCPLWLTGFCPKGAECDYTHPRFEAIIDRLRIKPDEDAVEEKEKVANGSDKEDQNMADATSNGNTEEKDESGP", "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": "MASFLKKTMPFKTTIEGTVNGHYFKCTGKGEGNPFEGTQEMKIEVIEGGPLPFAFHILSTSCMYGSKTFIKYVSGIPDYFKQSFPEGFTWERTTTYEDGGFLTAHQDTSLDGDCLVYKVKILGNNFPADGPVMQNKAGRWEPATEIVYEVDGVLRGQSLMALKCPGGRHLTCHLHTTYRSKKPASALKMPGFHFEDHRIEIMEEVEKGKCYKQYEAAVGRYCDAAPSKLGHN", "text": "FUNCTION: Pigment protein that is intensely purple in color. SIMILARITY: Belongs to the GFP family."}
+{"protein": "MNSNKKEFLYSAFETEINKKASVSLFDRFGGKSCIFLHQLDHTKKSLIKHENLKRQKSIEGMLQAVDTSIQEKRKELSLLKAFNRHKLTAAEDLQDKILELKEDIHFEIESLNNGQPSSQEEENSSETSIPDTIMQWRIEALPRVPSATF", "text": "SIMILARITY: Belongs to the herpesviridae UL96 family."}
+{"protein": "MSQASRALKAYRNALRATSVAFKNDVATLDAARNEIRTHMKSQEDPKGTNRSIDERLKLLDEVTVFLRHNIVQGRKVDEGKYRLNIHKDTELGDNDDIKKKKDGLSNGGFTGCCGGSGAKTT", "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": "MKSIKGLGKLLLASSILFSSSAFAKTIIKLGHYNSDIHPSHIALQEYFKKTIENETNHKYEIRLYPNNQLGGEDQIVNGLRNGTIEAGITGLLLQNVDPIFGVWEWPYLFKDNQEAKKVLESPIANKIGQKMEKYGIKLLAYGMNGFRVISSNKKLEKFDDFKGLRLRVPLNSLFVDWAKAMNINPQSMPLSEVFTALEQKVIDGQENPYMLIKDSGLYEVQKYIIQSNHIFSPGLLQISLKTWNKIPKEDQIIFEKAAKLYQEKEWELAIKTELEVKDYLAKHGNEIIVPSEAFKNDMVNASKVLYDSFYKKYDWAKDVVQKINEAK", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 7 family."}
+{"protein": "MPTHSRSRDRYGGRDSDREARYDYDYARRRYATDDDDDYDDDELEHDLTERRYRRDGYRPPRESRARGYYERDAEGAADEELLGNERDPGPRASRSYGDDYDARRREHSRAREAPRRSERHRDRDREGRSRRRAYEDDGRHRTRDGRRDRGRESDGEARRSRRREAGRETAARKHRSSDSTNSASHLLSADALAKLGAQYEKEERRKREIAKDAAKAERKRQKKLAVVGEETRALRDPPGESHRDRTKARVASGAYLEEGRSPEMRVRHRGGGGPAMEARWRKEGSWGGTMDDSGGGRPFWKRKRWIGLGALIIILVIVIPVAVVVSKKHDNKSDPADSQGTSPGKSNLDGLSHDSIPAYAQGTYLDPWTWYDTTDFNVTFTNETVGGLSIMGLNSTWDDSARPNDNVPPLNEPFPYGSQPIRGVNLGGWLSIEPFIVPSLFDSYSSVSGIIDEWTLSKRLGSSAASTLEKHYATFITEQDFADIRDAGLDHVRIQYSYWAVATYDDDPYVAKISWRYLLRAIEYCRKYGLRVNLDPHGIPGSQNGWNHSGREGVIGWLNGTDGELNRNRSLAVHDSVSKFFAQDRYKNIVTIYGLVNEPLMLSLSIEDVLDWTTEATKLVQKNGITAYVALHDGFLNLSKWKSMLKNRPDKMLLDTHQYTIFNTGQIGLNHTAKVNLICNDWYNMIKEINSTSTGWGPTICGEWSQADTDCAKYLNNVGRGTRWEGTFSLTDSTQYCPTADTGPPCSCANANADVSKYSADYKKFLQTYAEAQMSAFETGQGWFYWTWRTESAAQWSYRTAWKNGFMPAKAYAPSFRCGDAVPDFGDLPEYY", "text": "FUNCTION: Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
+{"protein": "MSKKLTTAAGCPVAHNQNVQTAGKRGPQLLQDVWFLEKLAHFDREVIPERRMHAKGSGAYGTFTVTHDITKYTKAKLFSEIGKQTELFARFTTVAGERGAADAERDIRGFALKFYTEEGNWDLVGNNTPVFFLRDPLKFPDLNHAVKRDPRTNMRSAKNNWDFWTSLPEALHQVTIVMSDRGIPATYRHMHGFGSHTFSFINSDNERFWVKFHFKSQQGIKNLSDAEAAQVIGQDRESHQRDLLESIDNQDFPKWTLKVQIMPEADAATVPYNPFDLTKVWPHKDYPLIEVGEFELNRNPQNFFAEVEQSAFNPANVVPGISFSPDKMLQGRLFAYGDAQRYRLGVNHQHIPVNAPRCPVHSYHRDGAMRVDGNFGSTLGYEPNNEGQWAEQPDFAEPALNLDGAAAHWDHREDEDYFSQPGDLFRLMTAEQQAILFDNTARNLNGVPKEIQLRHLRHCYKADPAYGEGIGKLLDIDVSEFN", "text": "FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. Could protect cells in nodules which have a high potential to produce hydrogen peroxide because of the strong reducing conditions required for nitrogen fixation and the action of several proteins. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the catalase family."}
+{"protein": "IWYLFRDNLLPRNTKFIGYARTKQTLAEVKEKCKKYIKVRTGEEDKLEEFWAANDYLSGSYDKRVDYEFLNQVISKYEKGPIANRIFYLAVPPTVFEDATLNIRNACTSIKGFTRVIIEKPFGRDDKSSDILSKDLAGLFKEEQIYRIDHYLG", "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": "MNRLPNIAKPPQKSNQRKEKAPPEVPALIADKDRGTYYEKGRFLGKGGFAHCYELTNRATREVVAGKVVPKSMLVKQYQRDKVDNERILIHRELGHINIVKLFNFFEDNLNVYITLELCARRSLMELHKRRKAVTEPEARYFTHQIVDGVLYLHDLNIIHRDMKLGNLFLNDDLVVKIGDFGLATTVNGDERKKTLCGTPNYIAPEVLNKAGHSFEVDIWAVGCILYILLFGQPPFESKSLEETYSRIRHNNYTIPSIATQPAASLIRKMLDPEPTRRPTAKQVQRDGFFKSGFMPTRLPVSCLTMVPKFGGHETSMMEENVAPRGVDARSQRPLNGRAGLSALPQHIVSNNADRERAQQQAAEATFREPEDAYLSQLFHQVAVLLEQRIPGLEEEEAALDGYQSPECLPVFWISKWVDYSDKYGIGYQLCDNSVGVLFNDNSRIMLDQAGNELTYIEKSNKEHYFSMHSGEMPGLLNKKVTLLKYFRSYMNDHLVKAGEGSEQRAGDDLARLPTLRVWFRTKSAIVLHLSNGTVQINFFNDHVKMMMCPLMQAVTFIDQNKRMLTYKLNNLQRNGCPEKFLHRLKYAKTMIERLMSDANVVSQNPARQPDMPRSMAAARSASAGSRGPNQAASHLPQSASGSNIHPRR", "text": "FUNCTION: Required for oocyte nuclear envelope breakdown before entry of oocyte into spermatheca (PubMed:10660671). In meiotic cells, required for spindle dynamics and probably for spindle attachment to the chromosomes (PubMed:10660671). Zygotic role in the development of the germline and nerve cord (PubMed:10660671). In mitotic cells, plays a role in spindle organization and centrosome maturation (PubMed:20823068). Involved in asymmetric nuclear localization of cdc- 25.1 during embryogenesis which affects cell division timing (PubMed:18305005, PubMed:18316412, PubMed:20823068). Together with plk- 2, regulates cytoplasm polarity in early embryos (PubMed:18199581, PubMed:18316412, PubMed:18305005). May play a minor role in chromosome pairing and synapsis during oocyte meiosis I (PubMed:22018922). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Midbody Cytoplasm Nucleus Chromosome Chromosome, centromere, kinetochore Note=In mitosis, remains associated with centrosomes entering prophase through to anaphase. During metaphase, embryos show anterior enrichment and located to the chromosomes of the metaphase plate. In meiosis, detected at centrosomes after pronuclear meeting in post-meiotic 1-cell embryos. Associated with chromatin during chromosome segregation of anaphase and in the region between the dividing chromosomes. Cytoplasmic in mature, unfertilized oocytes (PubMed:10660671). Asymmetric cytoplasmic localization is regulated by mex-5 and mex-6 (PubMed:18199581, PubMed:18316412). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily."}
+{"protein": "MSGSSSPKCTPKSLPTSGQKSLHDIKHPLSCSPGAEDDAAAAGENGAVIIDSPSPDLPHTEPSSIADKDLSLPNGTPADTSSPASSSSLLNRLQLDDDLDGETRDLFVTVDDPKKHVCTMETYITYSVSTKTTRTEFDLPEYSVRRRYQDFDWLRNKLEETQPTHFIPPLPEKFVVKGVVDRFSEEFVETRRKALDKFLKRIADHPVLSFNEHFNVFLTAKDLNSHKKQGVTLLSKMGESVRYVTSGYKLRNRPAEFATVTDYLDTFALKLGTIDRIAQRIIKEEVEYLMELREYGPVYSTWSGLEKELNEPLEGVSACVGNCCTALEELTEDMSEDFMPVIREYILYSESMKTVLKKRDQVQAEYEAKSEAAALKREERSTVPTDVEKCQDKVECFNADLKADMDRWQNNKRQDFRQLLMGVADKNIQYYEKCLTAWESIIPLLQDKQEPK", "text": "FUNCTION: May be involved in several stages of intracellular trafficking. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "MGIKFLEVIKPFCAVLPEIQKPERKIQFREKVLWTAITLFIFLVCCQIPLFGIMSSDSADPFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIGVGDTPKDRALFNGAQKLFGMIITIGQAIVYVMTGMYGDPSEMGAGICLLIIIQLFVAGLIVLLLDELLQKGYGLGSGISLFIATNICETIVWKAFSPTTVNTGRGTEFEGAIIALFHLLATRTDKVRALREGFYRQNLPNLMNLIATVFVFAVVIYFQGFRVDLPIKSARYRGQYNTYPIKLFYTSNIPIILQSALVSNLYVISQMLSTRFSGNFLVNLLGTWSDATSGGPARAYPVAGLCYYLSPPESFGSVLDDPVHAGIYIVFMLGSCAFFSKTWIEVSGSSAKDVAKQLKEQQMVMRGHRETSMVHELNRYIPTAAAFGGLCIGGLSVMADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF", "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. May cooperate with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post- translational transport of small presecretory proteins. 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. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecY/SEC61-alpha family."}
+{"protein": "MGFYSLKQLLLLYIIIMALFSDLKLAKSSSPEYTNLIYKGCARQRLSDPSGLYSQALSAMYGLLVTQSTKTRFYKTTTGTTSQTSVTGLFQCRGDLSNNDCYNCVSRLPVLSGKLCGKTIAARVQLSGCYLLYEISGFAQISGMELLFKTCGKNNVAGTGFEQRRDTAFGVMQNGVVQGHGFYATTYESVYVLGQCEGDIGDSDCSGCIKNALQRAQVECGSSISGQIYLHKCFVGYSFYPNGVPKRSSPYPSSGSSGSSSSSSSSGTTGKTVAIIVGGTAGVGFLVICLLFVKNLMKKKYDDY", "text": "FUNCTION: Modulates cell-to-cell trafficking. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell junction, plasmodesma Note=Co- localizes with the Grapevine fanleaf virus (GFLV) 2B-MP at the base of tubules within modified plasmodesmata. SIMILARITY: Belongs to the cysteine-rich repeat secretory protein family. Plasmodesmata-located proteins (PDLD) subfamily."}
+{"protein": "MINFIRSYALYFAWAISCAGTLISIFYSYILNVEPCILCYYQRICLFPLTVILGISAYREDSSIKLYILPQAVLGLGISIYQVFLQEIPGMQLDICGRVSCSTKIFLFSYVTIPMASVVAFGAIVCLLVLTKKYRG", "text": "FUNCTION: Required for disulfide bond formation in some proteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. BdbC subfamily."}
+{"protein": "GWTLNSAGYLLGPHAIDNHRSFHDKHGLA", "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": "MSNRVVCREASHAGSWYTASGPQLNAQLEGWLSQVQSTKRPARAIIAPHAGYTYCGSCAAHAYKQVDPSITRRIFILGPSHHVPLSRCALSSVDIYRTPLYDLRIDQKIYGELWKTGMFERMSLQTDEDEHSIEMHLPYTAKAMESHKDEFTIIPVLVGALSESKEQEFGKLFSKYLAEPSNLFVVSSDFCHWGQRFRYSYYDESQGEIYRSIEHLDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQKNGMNMSFSFFQQASWRRRMGAAAV", "text": "FUNCTION: May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). SIMILARITY: Belongs to the MEMO1 family."}
+{"protein": "MDSQVLPLILLIIVFAASSAHGHFPHRTNQDSDCPEASNGCWCHDSFAQCWKTYEVANIARKKDVIRKLELLSLQLEDVLKYIAQLPNLEAIKLGPEGDDHLFECSCDNVLELSGSVVSVVNANDVHVTGCLEHGWSRDIYTMNAFATRCRRRLILESGGAEMRHRRSAKDDDVNKRASPRKGSSPAGKKVQIMEQDAGKGDAHNEKEVVKDQKPTKELFDFFMGHRRKRRSIDDVIGEMRAERQRRYAQGAGGMQGGYGYPQAGGAQYGGQPVQGYMNQGPPMGQRPAAAGPAGGFGAPQGQPPVGQPIGEAAGGGEFLGEPGVGGESEFAEYSSSIGEGETINAEVMEKIKAVLGATKIDLPVDINDPYDLGLLLRHLRHHSNLLANIGDPEVRNQVLTAMQEEEEEEEQDAANGVRDNVLNNLNEGPGAGAVAGAAMAAGMPPYPGGAQGGMRVGGQPQNPMGGNAYNPMTGYRQQG", "text": "FUNCTION: Species-specific sea urchin sperm protein required for adhesion of sperm to the egg surface during fertilization. Bindin coats the acrosomal process after it is externalized by the acrosome reaction. It binds to sulfated, fucose-containing polysaccharides on the vitelline layer receptor proteoglycans which cover the egg plasma membrane. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the bindin family."}
+{"protein": "MAAAVTAAVSLPYSNSTSLPIRTSIVAPERLVFKKVSLNSVSISGRVGTIRAQITTEAEAPVTKVVKHSKKQDEGIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFTTEGEVPYREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHEDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSIRPKDGIDWIEYKRTLKKAEQWNVEVY", "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. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side Note=In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane. SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family."}
+{"protein": "MKIRLHTLLAVLTAAPLLLAAAGCGSKPPSGSPETGAGAGTVATTPASSPVTLAETGSTLLYPLFNLWGPAFHERYPNVTITAQGTGSGAGIAQAAAGTVNIGASDAYLSEGDMAAHKGLMNIALAISAQQVNYNLPGVSEHLKLNGKVLAAMYQGTIKTWDDPQIAALNPGVNLPGTAVVPLHRSDGSGDTFLFTQYLSKQDPEGWGKSPGFGTTVDFPAVPGALGENGNGGMVTGCAETPGCVAYIGISFLDQASQRGLGEAQLGNSSGNFLLPDAQSIQAAAAGFASKTPANQAISMIDGPAPDGYPIINYEYAIVNNRQKDAATAQTLQAFLHWAITDGNKASFLDQVHFQPLPPAVVKLSDALIATISS", "text": "FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. FUNCTION: Functions in inorganic phosphate uptake, although probably not the main uptake protein under phosphate starvation (PubMed:15731097, PubMed:20933472). Binds phosphate; probably able to bind both H(2)PO(4)(-) and HPO(4)(2-) (PubMed:8294447, PubMed:12842040). Part of the ABC transporter complex PstSACB involved in phosphate import (Probable). FUNCTION: A host TLR2 agonist (toll-like receptor), shown experimentally for human and mouse (PubMed:1906192, PubMed:19362712). Requires both host TLR1 and TLR2 as coreceptors to elicit host response in mouse (TLR6 may also play a role) neither CD14 or CD36 function as accessory receptors (PubMed:19362712). Protein purified from culture filtrate induces host (human) monocytes to produce TNF-alpha, IL-6 and IL-12 p40 (IL12B) via ERK1/2 (MAPK3 and MAPK1) and p38 MAPK pathways; MEK inhibitors U0126 and PD98059 and p38 inhibitor SB203580 block most cytokine production (PubMed:16622205). Host ERK1/2 and p38 MAPK activation is mediated mainly by TLR2, but also partially by TLR4, and unlike the case for lipoprotein LpqH the protein moiety of PstS1 seems to be the antigenic agent (PubMed:16622205). Greater activation of ERK1/2 and p38 MAPK is seen in patients with active pulmonary tuberculosis than in tuberculin-negative patients (PubMed:16622205). Induces apoptosis when incubated with human monocyte-derived macrophages via TLR2 (PubMed:19140873). Protein purified from culture filtrate acts via TLR2 and TLR4 to induce host macrophage (shown for mouse) endoplasmic reticulum stress-mediated apoptosis via MAPK (at least JNK), C-C motif chemokine 2 (MCP-1, Ccl2) and ZC3H12 endoribonucleases (MCPIP, Zc3h12) (PubMed:25544271). Functions as an adhesin, binds to human and mouse macrophages via mannose residues, binds to the mouse macrophage mannose receptor (possibly Mrc1) and mediates bacterial phagocytosis (PubMed:25359607). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Cell surface Secreted, cell wall Secreted Note=A soluble cell wall-associated protein (PubMed:10426995). Also found in culture filtrate in increasing quantities during growth (PubMed:1906192, PubMed:16622205). SIMILARITY: Belongs to the PstS family."}
+{"protein": "MATFGFLSAPLKSTNEVDLVKPLTSYIDNVYNTSDNNRSDVAEAVQELNKLRSKACCQPLDKHQSALDVLTRYYDQLVAIENKIIISATQNPVVFKWKDAFDKGSLFSSRASLSLSDGSFERAAVLFNIGSLMSQIGAAQQFHTDDEIKVSAKLFQQSAGVFARLRDVVLGMVQQEPTPDLMPDTLAALSALMTAQAQEAIYIKGHKDKMKATSMVKISAQVAEFYSEAQKMMSKDIVRGLWDKDWSAIVSGKNLAYQALAQYHQSEVCGEARQIGEQLSRLAESLKLFDTAQKYLPRDITGIWDIYPSVSKAHAAAKKDNDFIYHEKVSDFRTLPTLPKAVLAKPTPMQTPMTPSFRDMFAVLVPVQVHNAMQSYDARKAELVNMETVRMREATQLMNGVLASLNLPAALDDVTSTETLPESLKLKSAKLKQNGGSSEIMRLFSELPTLYQRNEDILTETSRILNEEKESDDTMRKQLGTKWTRMSSEQLTGPLVTEIGKYRGILHTASNADKMVKEKFESHRQGIELLSKNESELRSSIPGQTAHATGETDTVRQLRQFMSQWNEVTTDRELLEKELKNTNCDIANDFLKAMAENQLINEEHISKEKIAQIFGDLKRRVQSSLDTQETLMNQIQAANNTFTGEKTGSSTGAERERILKMLAQASDAYVELKANLEEGTKFYNDLTPILVRLQQKVSDFAFARQTEKEDLMRQLQLSIVSGQAAKAVVDGVNSLVSSYLTGGTNAAQSPANAPPRPPPPRPAAPSVESPIPPPRTQQSMQATPGAPPQYNPYQQQQQPQMQQFQQHPGYYQQPMPYGQPQPMFQPQYQPTFAAPYPTFPGAFPSYQQQWPQQQQQGGFPPNPQFGQQNQQQGGGGGANPFQ", "text": "FUNCTION: Required for lin-12 degradation after it has been internalised in the vulval precursor cells."}
+{"protein": "MHLKASSILALLVIGANAYPASANSAAALVPEPQQPEAPAVAGSTVGAQVDIHHPRLEARYGRDEPQIMCGYCGKRFWNKPDLEKHIKLKPSKGGHKGQPYKEHSWNRPT", "text": "FUNCTION: Secreted effector that translocates into the nuclei of host cells to reprogram the expression of immunity-associated genes by binding to effector binding elements (EBEs) in rice (PubMed:33203871). Binds the 5'-CCACCTCC-3' EBE of promoters from targeted rice genes and probably recruits a yet to be determined host repressor (PubMed:33203871). Causes ambivalent immunity with increased susceptibility to the hemibiotrophic pathogens Magnaporthe oryzae and Xanthomonas oryzae pv. oryzae, but enhances resistance to Cochliobolus miyabeanus, a necrotrophic pathogen (PubMed:33203871). SUBCELLULAR LOCATION: Secreted Host nucleus Note=Secreted via the biotrophic interfacial complex (BIC) and translocated into the nuclei of initially penetrated and surrounding cells."}
+{"protein": "MTTQLEQAWELAKQRFAAVGIDVEEALRQLDRLPVSMHCWQGDDVSGFENPEGSLTGGIQATGNYPGKARNASELRADLEQAMRLIPGPKRLNLHAIYLESDTPVSRDQIKPEHFKNWVEWAKANQLGLDFNPSCFSHPLSADGFTLSHADDSIRQFWIDHCKASRRVSAYFGEQLGTPSVMNIWIPDGMKDITVDRLAPRQRLLAALDEVISEKLNPAHHIDAVESKLFGIGAESYTVGSNEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYVPQLLLHVSRPVRWDSDHVVLLDDETQAIASEIVRHDLFDRVHIGLDFFDASINRIAAWVIGTRNMKKALLRALLEPTAELRKLEAAGDYTARLALLEEQKSLPWQAVWEMYCQRHDTPAGSEWLESVRAYEKEILSRRG", "text": "FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose. FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose (PubMed:14243758, PubMed:2558952, PubMed:8564401, PubMed:1650346). Can also catalyze the isomerization of L-lyxose to L-xylulose (PubMed:1650346). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose isomerase family. SIMILARITY: Belongs to the rhamnose isomerase family."}
+{"protein": "MNQMMTFLQTNGGELLYKTGEHLYISLIAVVLGIIVAVPLGVALTRMKKGAGAVIGFVNIVQTLPSLAILAFFIPLLGVGKVPAIVALFFYSVLPILRNTYTGIKGVNKNLLESGKGIGMTGWEQIRLVEIPLAIPIIMAGIRTSTIYLIGWATLASFIGGGGLGDYIFIGLNLYQPEYIIGGAVPVTILAIIIDYVLAVTERKVTPKGLQGMKEVS", "text": "FUNCTION: Involved in a high affinity multicomponent binding-protein- dependent transport system for glycine betaine, carnitine and choline; 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. CysTW subfamily."}
+{"protein": "MSTKAQNPMRDLKIEKLVLNISVGESGDRLTRASKVLEQLSGQTPVQSKARYTVRTFGIRRNEKIAVHVTVRGPKAEEILERGLKVKEYQLRDRNFSATGNFGFGIDEHIDLGIKYDPSIGIFGMDFYVVMNRPGARVTRRKRCKGTVGNSHKTTKEDTVSWFKQKYDADVLDK", "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 Note=The SYO1-uL5-uL18 complex is transported into the nucleus by KAP104. SIMILARITY: Belongs to the universal ribosomal protein uL5 family."}
+{"protein": "MFKHTLGAAALSLLFNSNAVQASPVPETSPATGHLFKRVAQISPQYPMFTVPLPIPPVKQPRLTVTNPVNGQEIWYYEVEIKPFTHQVYPDLGSADLVGYDGMSPGPTFQVPRGVETVVRFINNAEAPNSVHLHGSFSRAAFDGWAEDITEPGSFKDYYYPNRQSARTLWYHDHAMHITAENAYRGQAGLYMLTDPAEDALNLPSGYGEFDIPMILTSKQYTANGNLVTTNGELNSFWGDVIHVNGQPWPFKNVEPRKYRFRFLDAAVSRSFGLYFADTDAIDTRLPFKVIASDSGLLEHPADTSLLYISMAERYEVVFDFSDYAGKTIELRNLGGSIGGIGTDTDYDNTDKVMRFVVADDTTQPDTSVVPANLRDVPFPSPTTNTPRQFRFGRTGPTWTINGVAFADVQNRLLANVPVGTVERWELINAGNGWTHPIHIHLVDFKVISRTSGNNARTVMPYESGLKDVVWLGRRETVVVEAHYAPFPGVYMFHCHNLIHEDHDMMAAFNATVLPDYGYNATVFVDPMEELWQARPYELGEFQAQSGQFSVQAVTERIQTMAEYRPYAAADE", "text": "FUNCTION: Oxidation of bilirubin and other tetrapyrroles. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "GDDVKSACCDTCLCTKSNPPICRCVDIRETCHSACNSCVCTASIPPQCRFCYK", "text": "FUNCTION: Inhibits trypsin (IC(50)=6.20 nM), neutrophil elastase (ELANE) and, to a lesser extent, alpha-chymotrypsin (IC(50)=3.44 uM). SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor family."}
+{"protein": "MAAAAASTKIVAVVVAVLLAILEMPSCAVARRHHHDHHDKPGHHDGGFPAVMTVNGFEKGEDGGGPAACDGHYHSDGELIVALSTEWFAGGRRCHRRIRITPSEHGRRGGGGGRRAVEATVVDECDSRRGCKDDVVDSSPAVWRALGLDTDSGEVRVTWSDV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kiwellin family."}
+{"protein": "MAYSEKVIDHYENPRNVGSLDKKDSNVGTGMVGAPACGDVMQLQIKVDDNGIIEDAKFKTYGCGSAIASSSLITEWVKGKSLEEAGAIKNSQIAEELELPPVKVHCSILAEDAIKAAIADYKAKQG", "text": "FUNCTION: A scaffold on which IscS assembles Fe-S clusters. Subsequently gives the nascent cluster to other proteins. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (By similarity). SIMILARITY: Belongs to the NifU family."}
+{"protein": "MTTEYLDEERDLPLPRQKKGIDHTQTEPIRGFFGVKDMFAFENVGFTRSSEGKRYLVCGECEQGPVGFVDPVTEMNYVSPERLDVLPDVAAAAVEAGK", "text": "FUNCTION: Guanine-nucleotide-releasing protein that acts on members of the sec4/ypt1/rab subfamily. SIMILARITY: Belongs to the DSS4/MSS4 family."}
+{"protein": "MATEGLAGALATVLGGKGLLVQSCDSEPAGKPLFPVRLRKNVCYVVLAVFLNEQDEVLMIQEAKRECRGTWYLPAGRMEPGETIVEAMQREVKEEAGLLCEPVTLLSVEERGASWIRFVFLARPTGGVLKTSKDADSESLQAGWYPRVSLPTPLRAHDVLHLVELGAKFCQQAMHPLILPQELPCSVVCQRLVTTFTTVQSVWVLVGTVGTPHLPITACGFTPMEQRGGIKVAILRLLQECLTLHSLAVETKGLLGLQHLGRDHVDGVCLNVLVTVAFRNPGIQDEPPKIRGENYFWWKVLEEDLQKLLLYRLQESSVIPLSR", "text": "FUNCTION: Mediates the hydrolysis of oxidized nucleoside diphosphate derivatives. Hydrolyzes 8-oxo-7,8-dihydroguanine (8-oxo-Gua)-containing deoxyribo- and ribonucleoside diphosphates to the monophosphates. Hydrolyzes 8-oxo-dGDP and 8-oxo-GDP with the same efficiencies. Hydrolyzes also 8-OH-dADP and 2-OH-dADP. Exhibited no or minimal hydrolysis activity against 8-oxo-dGTP, 8-oxo-GTP, dGTP, GTP, dGDP and GDP. Probably removes oxidized guanine nucleotides from both the DNA and RNA precursor pools (By similarity). SIMILARITY: Belongs to the Nudix hydrolase family."}
+{"protein": "MTSQYAGELCTLLVEDNFGELFARIFSTLNRYDRLSFSRLKFYSRLSNAQLRHGLAAMIQQHLVYHYTSYDDGITYYEPNMQSAYYLVRSGKILELIEHRLGKYAATVMSTIMFLGHAQVGYLETLPALRPSNSDVNRASEERGGIHETEEYHGEEARQETEEHRETEGRPNGLNSDYTSSERPALLHPTLKALAGHGYILRVRDAQFQSYADNALDAERTIKSRPDIKALKGKKLDEAVTEGTLELLKERLDGDLTRGLMFNGVPRGAKRRHTTGATEASNKKARVDYAAVDEDEDGGEENEWSDDDFGEDTIPMESGITVRINYEKLDVALRNRRFLELAERDSSPVTAEVYESLLRRIEYQTAKCRDTTEIPREGEEGEHYSVPVPLRAVVEDVDLFLDLAGSVGPMEVSQPINRRGKRPLEETTNGAAHDGTNGGQSDGNRTYEVDQHLCLLAQPPYSLTSKRMVSGLITWTVEFRHLARKLRHLELERIIEARYGDVALRVVRVLHDKGKLDEKRLQEISLLPFKDLRQVLASMQTGGFVDLQEVPRDALRQPSKTIFLWFYDPDRVGNSVLEDTYKAMSRCLQRLRFERSRLKEFLEKTERSDVKGNEERYLSEAELTLLGQWRAKEALLLGEVARLDEMVAVIRDY", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RNA polymerase beta chain family."}
+{"protein": "MYTMGLDIGSTASKGVILKNGEDIVASETISSGTGTTGPSRVLEKLYGKTGLAREDIKKVVVTGYGRMNYSDADKQISELSCHARGVNFIIPETRTIIDIGGQDAKVLKLDNNGRLLNFLMNDKCAAGTGRFLDVMAKIIEVDVSELGSISMNSQNEVSISSTCTVFAESEVISHLSENAKIEDIVAGIHTSVAKRVSSLVKRIGVQRNVVMVGGVARNSGIVRAMAREINTEIIVPDIPQLTGALGAALYAFDEAKESQKEVKNI", "text": "FUNCTION: Involved in the reductive branch of L-leucine fermentation. Required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. This protein is extremely sensitive towards oxygen. SIMILARITY: Belongs to the HadI activator family."}
+{"protein": "LYSIASSAIGDFGFGDSKLDFAVSRGIDDIMVDLAAK", "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. SUBCELLULAR LOCATION: Plastid, chloroplast stroma Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side Note=In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane. SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family."}
+{"protein": "MRDRTQCVAVPTQAFNEILDQDGQLTAYAQRLEQLRERGSHRVALLRGELARIRQDQVLGMPEKRVQVAAHRLKISEAQAVARQCKTEETQLVRKAVARVRGLFRDFDCSVRDAMREQRLLLKQVATVQHTSASSDQREHCLAQLRQCKEARHHAYRSLVEKSAALRNGKMTFIERVVRALREYSFNFDATQFFLANGLYIAIAVFFIACIVVAPFSGNGNLLTIPNILTILEQSSVRMFYAVGVAGIILLAGTDLSIGRMVAMGSVVTGIILHPGQNIVTFFGLGPWDFTPVPMAVRVVMSLAVSVALCVSFSLFAGFFSARLKIHPFISTLATQLIIYGVLFFGTSGTPVGSIDPYIKDLFGGRWILGTMQGTLVTFPKLIIPATIAVAIAWFIWNKTILGKNMYAVGGNAEAANVSGISVFGVTMSVFAMAAVFYGFGAFFETFKANASAGTGQGYELDAIASCVVGGISFNGGIGKLEGAVVGVIIFTGLTYCLTFLGIDTNLQFVFKGLIIIAAVALDSVKYLKRR", "text": "FUNCTION: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside 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. AraH/RbsC subfamily."}
+{"protein": "MSENSIRLTQYSHGAGCGCKISPKVLETILHSEQAKFVDPNLLVGNETRDDAAVYDLGNGTSVISTTDFFMPIVDNPFDFGRIAATNAISDIFAMGGKPIMAIAILGWPINKLSPEIAREVTEGGRYACRQAGIALAGGHSIDAPEPIFGLAVTGIVPTERVKKNSTAQAGCKLFLTKPLGIGVLTTAEKKSLLKPEHQGLATEVMCRMNIAGASFANIEGVKAMTDVTGFGLLGHLSEMCQGAGVQARVDYEAIPKLPGVEEYIKLGAVPGGTERNFASYGHLMGEMPREVRDLLCDPQTSGGLLLAVMPEAENEVKATAAEFGIELTAIGELVPARGGRAMVEIR", "text": "FUNCTION: Synthesizes selenophosphate from selenide and ATP. FUNCTION: Synthesizes selenophosphate from selenide and ATP. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I subfamily. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I subfamily."}
+{"protein": "MPSFDFDIPRRSPQEIAKGMVAIPGGTFRMGGEDPDAFPEDGEGPVRTVRLSPFLIDRYAVSNRQFAAFVKATGYVTDAERYGWSFVFHAHVAPGTPVMDAVVPEAPWWVAVPGAYWKAPEGPGSSITDRPNHPVVHVSWNDAVAYATWAGKRLPTEAEWEMAARGGLDQARYPWGNELTPRGRHRCNIWQGTFPVHDTGEDGYTGTAPVNAFAPNGYGLYNVAGNVWEWCADWWSADWHATESPATRIDPRGPETGTARVTKGGSFLCHESYCNRYRVAARTCNTPDSSAAHTGFRCAADPL", "text": "FUNCTION: Oxidase that catalyzes the conversion of cysteine to 3- oxoalanine on target proteins. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3- oxoalanine as a catalytic nucleophile. SIMILARITY: Belongs to the sulfatase-modifying factor family."}
+{"protein": "MKNEKRKTGIEPKVFFPPLIIVGILCWLTVRDLDAANVVINAVFSYVTNVWGWAFEWYMVVMLFGWFWLVFGPYAKKRLGNEPPEFSTASWIFMMFASCTSAAVLFWGSIEIYYYISTPPFGLEPNSTGAKELGLAYSLFHWGPLPWATYSFLSVAFAYFFFVRKMEVIRPSSTLVPLVGEKHAKGLFGTIVDNFYLVALIFAMGTSLGLATPLVTECMQWLFGIPHTLQLDAIIITCWIILHAICVACGLQKGGRIPSDVRSYLSFLMLGWVFIVSGASFIMNYFTDSVGMLLMYLPRMLFYTDPIAKGGFPQGWTVFYWAWWVIYAIQMSIFLARISRGRTVRELCFGMVMGLTASTWILWTVLGSNTLLLMDKNIINIPNLIEQYGVARAIIETWAALPLSTATMWGFFILCFIATVTLVNACSYTLAMSTCREVRDGEEPPLLVRIGWSILVGIIGIVLLALGGLKPIQTAIIAGGCPLFFVNIMVTLSFIKDAKQNWKD", "text": "FUNCTION: Catalyzes the exchange of L-carnitine for gamma- butyrobetaine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family. CaiT subfamily."}
+{"protein": "MTPHSTHVTLDHEGIIQPPAEFKERSKSKPNLADFETYSKMYKESIENPSKFFGEQALEHLSWDRPFDEARYPVSSEQDFADGDIASWFVNGQLNASYNAVDRWAIKNPNKPAIIYEADEENEGRIITYGQLLKDVCKLAQCLTKLGIRKGDSVAVYLPMIPEALVTLLAIVRIGAVHSVVFAGFSSSSLKDRILDASSKIVITTDESKRGGKTIETKKIVDDALKNCPDVTNVLLFKRTGNAHIPFTEGRDLWWHEEMAKYGPYFPPVPVNSEDPLFLLYTSGSTGKPKGIQHSTAGYLLGAAMTSKYTFDVHEDDVLFTAGDVGWITGHTYVVYGPLLCGATTVVFEGTPAHPNYSRYWEIVDKYQVTQFYVAPTALRLLKRAGTKYIENYKLDSLRVLGSVGEPIAAEIWHWYNDNIGRRKCHIVDTYWQTESGSHMLAPLAGITPTKPGSASLPCFGIDAKILDPVSGKELKENDVEGVLCVKSCWPSISRGIYNDYARFIETYLKPYPNHYFSGDGAARDVDGFYWILGRVDDVVNVSGHRLSTAEIEAALILHESVAECAVVGYADELTGQAVAAYVSLKSNVSEDLEVIKKELILTVRKEIGPFATPKTILLVDDLPKTRSGKIMRRILRKVLAGEEDQLGDISTLSNPGVVAQIIDVVKATRK", "text": "SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MARNSRIRITNNDKALYAKLVKNTKAKISRTKKKYGIDLSNEIELPPLESFQTRKEFNEWKRKQESFTNRANQNYQFVKNKYGIVASKAKINEIEKNTKEAQRIVDEQREEIEDKPFISGGKQQGTVGQRMQILSPSQVTGVSRPSDFNFDDVRSYARLRTLEEGMAEKASPDYYDRRMAQMHQNFIEIVEKSFNSYWLTDELVERLKKIPPDDFFELYLIFDEISFEYFDSEGEDVEASEAMLNKIHSYLDRYERGDVNLDLKGF", "text": "FUNCTION: Hydrolyzes host peptidoglycans during virus entry. FUNCTION: Acts as a primer for DNA elongation during viral genomic replication. Acts as the small terminase protein during packaging. Recruits the phage DNA polymerase to the bacterial nucleoid. Primer terminal protein (TP) is covalently linked to the 5'-ends of both strands of the genome through a phosphodiester bond between the beta- hydroxyl group of a serine residue and the 5'-phosphate of the terminal deoxyadenylate (dAMP). To start replication, the DNA polymerase forms a heterodimer with a free TP that recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP. Since the polymerase initiates the replication on the second thymine, the TP-dAMP initiation product slides backwards to recover the template information of the first nucleotide. SUBCELLULAR LOCATION: Virion Note=Associates with the host bacterial nucleoid through its N-terminal region. SIMILARITY: Belongs to the phi29likevirus DNA terminal protein family."}
+{"protein": "METQLLRFPSHTITSSITTNSSRNTTPFLPHKKWSHFVKFQLVNSSSSIKHGIRPLQASATSLGLGNKNRVDETESYTLDGIRHSLIRQEDSIIFSLVERAQYCYNAETYDPDVFAMDGFHGSLVEYIVRETEKLHATVGRYKSPDEHPFFPKVLPEPVLPPMQYPKVLHPIADSININVKIWEMYFENLLPRLVKEGDDGNYGSTAVCDTICVQALSKRIHYGKFVAEAKYRASPEVYNAAIRAQDRNGLMDLLTYPAVEEAIKRRVEIKTRTYGQELHINGPENGGDPVYKIKPSLVAELYGDWIMPLTKEVQVQYLLRRLD", "text": "FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid (FVBPs) biosynthetic pathway (PubMed:19811620). Mediates the conversion of chorismate to prephenate, thus coupling metabolites from the shikimate pathway to the synthesis of FVBPs in the corolla (PubMed:19811620). SUBCELLULAR LOCATION: Plastid, chloroplast stroma."}
+{"protein": "MADESNTGPVAAAEAVAETQAPAGKRKSSSRRQRTAAGQVAESKTTAKPKRYSETERADKLNLIEAEVAQGNSTLKDAIKSAGISEQTYYVWKKSAKPADRKPEESVVAGDDLADLIQLDKENLRLRNLLSDKLRAENAELRKRLGLD", "text": "FUNCTION: Responsible for the repression of SyrM activity. SIMILARITY: Belongs to the SyrB family."}
+{"protein": "MAFANFRRILRLPNFEKKRLREYEHVRRDVDPNQVWEIIGELGDGAFGKVYKAKNRETGILAAAKVIETKNEEELEDYMVEIEILATCNHHFIVKLLGAFYWEGKLWIMIEFCPGGAVDAVMLELDRGLKEPEIKTICRQMLEALAYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSSLSKWSPEFHSFLKTALDKNPETRPSAAQLLEHPFVKKASGNKPLRDLVAEAKAEVLDEIEEQGEAEEEEDSDMLSPKTKGVSQSTHVEIGKDIEREQVGNGIKPHSATSPQKTDSQADNYSQRRNNEVKNCPENGRPDAVNGKPDIIILNPLSSNLEPKRNSTAESYRGEEHSSASSQRQRSAQSAELVPNGSFDSPTRYFTNWSKRDSDSGSNSASESMDISMNLSADLSMNKETGFLSHRENRLHKKTLKRTRRFVVDGVEVSITTSKIIGDDEKKDEEMRFLRRQELRELRLLQKEEHRHQAQLTSKHSFQLEQMSRRFEQEMNSKRKFYDTELETLERHQKQQIVWMEQEHAFRRRDEAKHIKTEQERDHIKFLEQLKLRKKELKAHVEKLPRQQRRETMKVQMDGFAHKKQTEEQQFVNRQKEDLNLAMRVIVLENRKEIYNKEREFLNKKQQLLRDRESVIWELEERHLQERHQLVKQQLKDQYFLQRHELLRKHEKEQEQMQRYNQRMMEQLRLRQQQEKVRLPKNQKAEAKTRMTMFKKSLHISPSGSAAEQRDKIKQFSLQEEKRQKAERLQQQQKHEHQLMEMLAECDCNVRDLLQMQNEKCHLLVEHETQKLKSLDEHHIQLIREWRENIRPRKKAFEDELELKKEAQEMFFRLNEEVAGDPFLSNKPTRFYSFSSPEAS", "text": "FUNCTION: May act as a polo kinase kinase by mediating phosphorylation of plk1/plx1 and subsequent activation of plk1/plx1 during oocyte maturation. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
+{"protein": "GHVPCGKDGRKCGYHADCCNCCLSGICKPSTSWTGCSTSTFLLTR", "text": "FUNCTION: Iota-conotoxins bind to voltage-gated sodium channels (Nav) and act as agonists by shifting the voltage-dependence of activation to more hyperpolarized levels. Produces general excitatory symptoms (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin I1 superfamily."}
+{"protein": "MQPIVWLLGGAIALLVVVIRAAWTYGHRNQDMPSGPPTLPFIGNAHLIPKSYTHIQFTAWARQYGGLYMLKVGNSNMAVVTDRRIVKEVLDSKSSLYSHRPHSFVSHELITQGDHLLVMHYGPKWRTFRRLVHQHLMESMVDSQHLPIVNAEAIQLVRDYMLDPEHHMAHPKRFSNSITNSIVFGIRTADRHGSNMNRLYTLMEQWSEIMETGATPPVDIFPWLKRLPEALFGHYVTRARAIGAQMETLYEDILQRVEKRRSGGVHLDTFMDRVIASQDRNQLPRHQLAFIGGVLMEGGSDTSSSLTLAIVQALTLHPEVQRKAHAEIDAVVGHARSPVWDDLARLPYINMIIKEGHRWRPILPLCFPHALGQDDWVDGKFLPKGTMVVVNTWGMHMDPDHRLNQKYDPAKFVPERFAEHPALAPEYVPGAWENRDHYGYGVSRRICPGIHLAERNMFLAIAKLLWAFEFQPGPEGEPCDSDPVTGYQHGFLYCAKPYSTRPVLRSESIRETVEREFALAQREVFSTFTEG", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aculins (PubMed:26374386). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) acuA via condensation of acetate and malonate units (PubMed:26374386). The 6-methylsalicylic acid decarboxylase acuB then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m- cresol (also known as 3-methylphenol) (Probable). These first reactions occur in the cytosol (By similarity). The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase acuE that probably catalyzes hydroxylation of the aromatic ring (Probable). The aromatic system might then be opened by oxidation through a Baeyer-Villiger type of oxidation, which could be catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed, before the dehydrogenase acuH would reduce the double bond between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results in formation of aculinic acid, which exists as two diastereomers (both R/S configurations at C-1) by non-enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI could be involved in the linking of aculinic acid to an aculene A moiety produced by the aculene biosynthesis cluster and which leads to the production of aculin A (Probable). AcuI may also be involved in the attachment of proline to aculinic acid to form epi-aculins A and B (Probable). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MPRFSCYEVRSEFPELERGIVYLDNAASTLKPRRVVEAMREFSYRSYANVHRGVHRLSMEASKAYEDAHEVVARLVGGSWDEVVFTRNTTEAMQLAALTLAYNGLLRGGEVLVTAADHHSTLLPWVRAARLGGGRARILPLDGRGVPRWDLLEDYITEDTRAVAVGHVSNVTGVVAPVEDIVKAAKKVGALVVLDSAQGVPHLPVDFRRMGVDMAAFSGHKMLGPTGIGVLWARRDLLEELEPPLGGGGTVSRVRLQGGSVEIEWEEPPWKFEAGTPPIIEAVGLAEAANMLMEIGMEHVARHEDELTSHTMKLLEPLYSEGLIRYVGPDKPGERHGIVSITTHLKSPDELGLLLDRRGIAVRTGLHCAHILHDHVDASMGSVWASFYIYNCKEDAERLAEALEEILTTRR", "text": "SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily."}
+{"protein": "MAPALLLVPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDQSILVPLAWDLGLLLLFVGQHSLMATETVKAWMSRYFGVLQRSLYVACTALALQLVMRYWEPVPRGPVLWEAQAEPWATWVPLLCFVLHVISWLLIFSILLVFDYAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLALLLTLYLGLAHGLDQQDLRYLRAQLQRKLHLLSRPQDGEAE", "text": "SUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nurim family."}
+{"protein": "IGKAHGGVSVSGGVGERTREGNXLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYDTAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVRLSETIKGFQMILSGELDXLPEQ", "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 (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
+{"protein": "LECYQMSKVVTCKPEETFCYSDVFMPFRNHIVYTSGCSSYCRDGTGEKCCTTDRCNGARGG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Orphan group XX sub-subfamily."}
+{"protein": "MSFAENVGRFIGNSVNSVGSVIGDGLKGFNSTQSISSAKQANLLNNLPLPSLDNVLNIGMFGGLASGLLSYRAAKKQNKVMQDIANRQMAFQERMSSTAVRRHVEDLKKAGLNPLLALGGSASTPQGAFYSPVNPMESGLNSAISVADKVFDYQRLAHADFQGRLNSAMSVVQLASAVQDYKRNYGKFGEVAYWFDRYAGKLLPAMLFYLFRKHPVGRAVSAANSGYAVAKGAKGVNFKFSNMSSTAVQRHNSRYNVSKGWRR", "text": "FUNCTION: Probably triggers with protein G the injection of the phage DNA into the host upon conformational changes induced by virus-host receptor interaction. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the microviridae H protein family."}
+{"protein": "MSSKTIELNFLGQVLRLNCPEEQHDSLREAAKLLDSRVTEMKDRTGILQVEKALAIVALNLSFELLQEQHKTHKTENVLQNQIEQLTRSLESISASTPTQQASYSID", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Localizes at mid- cell. SIMILARITY: Belongs to the ZapA family. Type 1 subfamily."}
+{"protein": "TITPSLKGFFIGLLSGAVVLGLTFAVLIAISQIDKVQRSL", "text": "FUNCTION: Involved in the binding and/or turnover of quinones at the Q(B) site of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbX family. Type 1 subfamily."}
+{"protein": "MDHIQLVNSQIDINHIHNLLIDESCGASSVFVGTTRDNFDGKKVISLEYESYEKMALKEMSKICSQLRARWPDLKHIAIYHRLGTVPVKEASVVIATSAPHRAAALESVTFAVEQLKSRVPIWKKEIYENDTIGEWKENMECPWPQYSKASLRTFDFSSCKIKQTIENIPDKLVQIRVNDSDLNKRVKCFLKRKRDEINLHNINDFKQQSSQIPCEETTTFSCARTQSFLVKQQQSSGHLKVRRANNCCGPQVRPNYSLQLNKLMTPQSDCDDLIEYKLGNSRLRNIEAYMCVSPDDDNILNRIKNIEDRILLIESTSPEYKHFVQFGTDSEKTCLKKPKKEVYLTDRINEFLTKIKREIEQ", "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": "MIRSSIAPSRQLLSPTTGRQWLQSSRVRGGLVGKKHYSRTRKAPVISKAIPTLDGVVLPVRGNNAFTTSAILANDSHVRSPPSPSSESAIAPEGVPRPPQSHPVQTSPGSSVDGRAQPPPETNTPPPPPPPAPKKGGRFRRFLIYLIFTTGLAYAGGIWLSLTSDNFHDFFTEYVPYGEEAVLYVEEQDFRRRFPNAARQITRRVTGPREEGQNVTIPGKSGLSWKVSEEESEAKEAGSDVSRKGKHMSATEVNKEKTAAVEQVKAKKEAAPAIKKETTPAESKKPALEEARSPALPTASPVQPLSIAIEDEPTVQELMRIVNDLISVVNADESSSRFTSTLSKAKADFEKLGERIIAAKQESYKFAQEEIEKARADMEKSANELIRRIDEVRADDAAQFREEYEAERERLARAYQEKIKIELQRVQEVSEQRLRNELVEQAIELNRKFLSDVRSLVENEREGRLSKLSELTANVGELERLTAEWNSVVDTNLTTQQLQVAVDAVRSALENSDIPRPFINELVAVKELAAGDPVVDAAISSISPVAYQRGIPSSAQIIERFRRLATEVRKASLLPENAGIASHAASYMMSKVMFKKQGSEEGDDVESILTRTETLLEEGRLDDAAREMNSLQGWSKILSKDWLADVRRVLEVNQALELIETEARLRCLQVE", "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": "MSSTQFNKGPSYGLSAEVKNRLLSKYDPQKEAELRSWIEGLTGLSIGPDFQKGLKDGIILCTLMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMNPVDLFEANDLFESGNMTQVQVSLLALAGKAKTKGLQSDVDIGVKYSEKQQRNFDDATMKAGQCVIGLQMGTNKCASQSGMTAYGTRRHLYDPKNHILPPMDHSTISLQMGTNKCASQVGMTAPGTRRHIYDTKLGTDKCDNSSMSLQMGYTQGANQSGQVFGLGRQIYDPKYCPQGPAADGAPAAAGDCPGPGES", "text": "FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. SIMILARITY: Belongs to the calponin family."}
+{"protein": "MEKLSEKDKELIRGSWESLGKNKVPHGVVMFSRLFELDPELLTLFHYTTNCGSTQDCLSSPEFLEHVTKVMLVIDAAVSNLDDLPSLEDFLLNLGRKHQAVGVNTQSFAEVGESLLHMLQCSLGQAYTAPLRQAWLNLYSIVVAAMSQGWAKNGEDKAD", "text": "FUNCTION: Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Capable of penetrating cell membranes (By similarity). SUBCELLULAR LOCATION: Perikaryon Cytoplasm Note=Located in the soma (perikaryon) of most nerve cells in brain. Has ability to penetrate cell membranes and translocate into cells (By similarity). SIMILARITY: Belongs to the globin family."}
+{"protein": "MLKQSGHKHGKLLKILKHNKPKERKFGKGARRCERCGRYDGIIRRYGLYLCKDCFKEVAHELGFFKWGE", "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": "MEYEIVIGLEVHAELATKTKMYCGCTAEFGGQPNTHVCPVCMGLPGALPHINKRAVDYGIKAGLALNCSITHIGRMDRKHIFYPDNSRNYQITQDELPLCTNGYIEIELEDGSKKKIGVERIHIEEDAGKLLHTNAGTLVDFNRCGVPLAEIVSKPDMRSPREAVTYLEELKSILSCVGVSDCKMEEGSLRCDANISVMKKGAKEFGVRTEIKNMNSFKAVEKALNYEYERHIKAIESGEKLTQETRRWDDAKNETAPMRSKEEANDYRYFPEGDLVTLNIDDEWIESIRKTIPELPYQKRERFIKEFGIPKYDASVLTLTMSMADFFEKTAKISGDAKSASNWLMGDISKIMKENYVWIEDLKFTPEQLSELIKLINEGTVSNAIGKKVIIKMFETGKSPKNIIEEEGLIQNSNEDEILNIVKEVLSENEKSIEDYKNGKNRVVGFLIGLVMKKTKGKANPKIVNKLMIDELNKQ", "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 GatB/GatE family. GatB subfamily."}
+{"protein": "MSPSIKKLDCFSPMLCHCKVACTNSTISLMFGCKKYRHQDEDTGSPQEPSSPQFTDDTPGPELVQVAEKSLSQIENVHGFVAHSHISPMKVESLECIFDGPSPVVKEESPPSPSTPLSNPYPQSPVSVQANPPPVVVNTESLDSAPYVNGTEADFEYEEITLERGNSGLGFSIAGGTDNPHIGEDPSIFITKVIPGGAAAQDGRLRVNDVILRVNEVDVRDVTHSKAVEALKEAGSLVRLYVRRRKSASEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKLLAVNSSCLEEVTHEHAVTALKNTPDVVYLKVAKPNSVFMNDSFAPPDITNSYSQHMENHISPPSYLSQPLPPVHSGRFSPTPKTTVGDDDVTREPRKVVLHRGTTGLGFNIVGGEDGEGIFISFILAGGPADLCGELRKGDRLVSVNGIDLRGATHEQAAAALKNAGQTVTIVAQYRPEEYSRFEAKIHDLREQMMNSSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVVNASDDEWWQARQVTAQGEVEEMGVIPSKRRVEKKERARLKTVKFNSKSREKGDNPDDMLSKGQSGQEEYVLSYEPVSQQEVNYSRPVIILGPMKDRVNDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVVSREQMERDIQEHKFIEAGQYNSHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQVAMLYPIGIFIKPKSVENIMEMNKRLTEEQGRKTYDRAMKLEQEFMEHFTAIVQGDTLEEIYDQVKQIIEEQSGPYIWVQSKEKL", "text": "FUNCTION: May play a role in synapse assembly and function. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the MAGUK family."}
+{"protein": "MATTTTSWEELLGSKNWDTILDPLDQSLRELILRCGDFCQATYDAFVNDQNSKYCGASRYGKSSFFDKVMLENASDYEVVNFLYATARVSLPEGLLLQSQSRDSWDRESNWFGYIAVTSDERSKALGRREIYIALRGTSRNYEWVNVLGARPTSADPLLHGPEQDGSGGVVEGTTFDSDSEDEEGCKVMLGWLTIYTSNHPESKFTKLSLRSQLLAKIKELLLKYKDEKPSIVLTGHSLGATEAVLAAYDIAENGSSDDVPVTAIVFGCPQVGNKEFRDEVMSHKNLKILHVRNTIDLLTRYPGGLLGYVDIGINFVIDTKKSPFLSDSRNPGDWHNLQAMLHVVAGWNGKKGEFKLMVKRSIALVNKSCEFLKAECLVPGSWWVEKNKGLIKNEDGEWVLAPVEEEPVPEF", "text": "FUNCTION: Acylhydrolase that catalyzes the hydrolysis of phosphatidylcholine (PC) at the sn-1 position. High activity toward PC, medium activity toward monogalactosyldiacylglycerol (MGDG) and low activity toward triacylglycerol (TAG). Confers sensitivity to UV-B radiation probably by deesterifying membrane phospholipids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
+{"protein": "MVDISLIIGGPQGGGIESAGQIAIKSMVLLGYEVLGSREYHSNIMGAHSYYHLRVQQHRPRSLKLPVDGVLALDAESVFTHFRDVRPGGILVYDPGTKSTRVDAIQPMAGPLKKRLKSLFDSRGMQPVVESAVKLAEEAGARIVGLPLKEMLKTLSERTGAPVARVSRALNTLGLASMLYMLGVPVEYIEKAISLQFAGKEKVINMNVEAVRIAVDYVREAFGEPESRLPPGPRRGQTMMVATGNDLVAMGKIVGGLGVITYYPITPSSDEALYVEKHSYISIDGPLAEKLGYDKIAVAIVQMEDELASINAVLGAAAAGARASTTTSGPGFSLMNEAVSLAVEAEIPVVVTLWMRAGPSTGMPTRTGQQDLLHSIFSGHGDAPKIVLASGDHVEAFYDAIKAFNWAEEFQTPVIHLLDKYLASSMVSLAREDLDPSKVPITRGKLLDNPPADYRRYEVVEDGISPRARLGSATMVITGLEHDEYGYATEDPVMREIMMFKRERKFKVIEERIPDEEKAVLHGDSEASVALVSFGSTKQPILEALEMLRDEGVRARFAQVRLLYPFPGRLVEEMLEGVEKVIMVEQNLLGQLAMLLRAHTSIKPDSSIVKINGRPLYSFEVAGAVKRILETGEERVVVSHGS", "text": "FUNCTION: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as pyruvate, 2-oxobutyrate, glyoxylate and 2-oxoglutarate to form their CoA derivatives."}
+{"protein": "MARFHNPAERPYKLPDLCTTLDTTLQDITIACVYCRRPLQQTEVYEFAFSDLYVVYRDGEPLAACQSCIKFYAKIRELRYYSDSVYATTLENITNTKLYNLLIRCMCCLKPLCPAEKLRHLNSKRRFHKIAGSYTGQCRRCWTTKREDRRLTRRETQV", "text": "FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway. FUNCTION: This protein may be involved in the oncogenic potential of this virus (cervical neoplasia-associated virus). SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the papillomaviridae E6 protein family."}
+{"protein": "HLPQVSSSLHSRAATSVVDLNGNEIQLHDMLSGHYLTTANAPVLESTALFNNNNNFNHDVVNGLNRDPSPTFPTKQAVKKDRHSKIYTSQGPRDRRVRLSIGIARKFFDLQEMLGFDKPSKTLDWLLTKSKTAIKELVQSKSTKSNSSSPCDDCEEVVSVDSENVTDHSKGKSLKANNKCKEAMDSHQAAAKESRAKARARARERTKEKMCIKQLNEAIVLRNHQFEVSGTREAFVHPVFGFHQQNYGNTSHENWDQSNFASQSNQLCAIL", "text": "FUNCTION: Involved in the dorsovental asymmetry of flowers. Retards growth rate and reduces organ number in the dorsal region of flowers (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MVKCTPLLALTVIVSAGSDALSDPTVKRLAKLATINQAPATQSNSDSKRVLRASDVPDEVAAGESRSPKSLWPWEVEDKLAPLKEKLISTSADDLEAGGSANKNALPMIWRWLWQNQIETKKTPIDEISKEVQTAMDLISSQATHEELNKAGVSVSDYVKALRFTLSDIDVVNRGMEYNIHLGNK", "text": "FUNCTION: Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein RPP39 (PubMed:22359513). The allele ATR39-1 is recognized by RPP39, whereas the ATR39-2 allele is not recognized (PubMed:22359513). SUBCELLULAR LOCATION: Secreted Host cell. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MSFRKEDGVSSLCQKALHIITELCFAGQVEWDKCSGIFPADRSGQGGGGTDISVSLLAVVVSFCGLALLVVSLFVFWKLCWPCWKSKLVAPNLSVLPQSISSAPTEVFETEEKKEVEENEKPAPKAIEPAIKISHTSPDIPAEVQTALKEHLIKHARVQRQTTEPTSSSRHNSFRRHLPRQMNVSSVDFSVGTEPILQRGETRTSIGRIKPELYKQKSVDSEGNRKDDVKTCGKLNFALQYDYENELLVVKIIKALDLPAKDFTGTSDPYVKIYLLPDRKKKFQTRVHRKTLNPLFDELFQFPVVYDQLSNRKLHFSIYDFDRFSRHDMIGEVILDNLFEVSDLSREATVWKDIHCATTESIDLGEIMFSLCYLPTAGRMTLTVIKCRNLKAMDITGSSDPYVKVSLMCEGRRLKKRKTTTKKNTLNPVYNEAIIFDIPPENVDQVSLCIAVMDYDRVGHNEVIGVCRTGLDAEGLGRDHWNEMLAYHRKPITHWHPLLELPGRATSFDSQGSCSSPRPPSTP", "text": "FUNCTION: Ca(2+) sensor specifically required for the Ca(2+)-dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb (PubMed:21496647). Exocytosis of IGF1 is required for sensory perception of smell (PubMed:21496647). Not involved in Ca(2+)- dependent synaptic vesicle exocytosis (PubMed:21496647). Acts through Ca(2+) and phospholipid binding to the C2 domain: Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein Note=Localizes to neuronal vesicles containing IGF1 that are not enriched at synapses (PubMed:21496647, PubMed:23345244). Does not colocalize with synaptic vesicles or with the Golgi apparatus (PubMed:21496647, PubMed:23345244). SIMILARITY: Belongs to the synaptotagmin family."}
+{"protein": "METKGRRSAAVLDQQDESEAHPRKRPTRRAPLHRDGNNPDSDAATMEGSDPGSAGRPSSDSLLQEPSQPAKRGGLLDRDAIEHITELWDRLELLQQTLSKMPMADGLKPLKNFSSLQELLSLGGERLLTDLVRENIHVREMMNEVAPLLREDGSCRSLNYHLQPVIGVIYGPTGCGKSQLLRNLLSSQLITPAPETVFFIAPQVDMIPPSELKAWEMQICEGNYAPGPQGTFIPQSGTLRPKFIKMAYDDLTQEHNYDVSDPRNVFARAAAHGPIAIIMDECMENLGGHKGVSKFFHAFPSKLHDKFPKCTGYTVLVVLHNMNPRRDLGGNIANLKIQSKMHIISPRMHPSQLNRFVNTYTKGLPVAISLLLKDIVQHHALRPCYDWVIYNTTPEQEALQWSHLHPRDGLMPMYLNIQSHLYRVLEKIHRVLNDRNRWSRAYRARKIK", "text": "FUNCTION: Component of the packaging machinery which encapsidates the viral DNA into preformed capsids and transcriptional activator of the viral major late promoter (MLP). Binds, along with packaging proteins 2 and 3, to the specific packaging sequence on the left end of viral genomic DNA and displays ATPase activity thereby providing the power stroke of the packaging machinery. The activity of packaging protein IVa2 is stimulated by protein 33K which acts as a terminase. May be the protein that pumps DNA into the capsid powered by ATP hydrolysis. Specifically binds to the 5'-CG-3' nucleotides of the repeats making up the packaging sequence. Component of the DEF-A and DEF-B transcription factors that bind downstream elements of the major late promoter (MLP), and stimulate transcription from the MLP after initiation of viral DNA replication. DEF-A is a heterodimer packaging proteins 1 and 2 and DEF- B is a homodimer of packaging protein 1. SUBCELLULAR LOCATION: Virion Host nucleus, host nucleoplasm Host nucleus, host nucleolus Note=Located at a unique vertex of the capsid. Present in about 6-8 copies per virion. SIMILARITY: Belongs to the adenoviridae packaging protein 1 family."}
+{"protein": "MMVDFSPSRRRMGTQELSLKPQVETPGIKLLAVMFCRYHLIRQLKQVQAASRTRYAHSVPQSRPTLKERLAALHEKQQLSLLPPDAVKRVSENNPAVLIDCDARTLLQLFLAALQTDPQKTTLSELLSQEEGFSVFIHRLLPTYTPSSDLKHLVSKDGTTALLQKLYGFYREQFADAPIGRPSPGRLHDANSFARWFMAESKLRLARTVFAELVGNPTELAKLPRDTETIITLLQLHLGAKHIFWRDPGNSVGRGGQLFTPAHMAVVTAYNSLGEETLLRLLRLLQSDPQWKSVCSPDLDRNIILALAFHNRLDLVHAQAARYYAPAAPGHGLPSTPLLPDGALVGAVVTAFAFKHQLAQGLAIAYQFLDRFTHLPNEHELWKIIFTWLARRHPTGSQGAALYDEAWSKMRTRYAEHGQPTPYDYSIARASYRIVRRDSSLRRVRALLNDYMSPLYQQPAVAPRDRLLLLKCQAHIVGRLVRARRNSAAADFVDQWALDSEARSHLLEHIAARASSRTDADDDDAGDGLYLTGAPLW", "text": "FUNCTION: Required for translation of the mitochondrial OLI1 transcript coding for the mitochondrial ATP synthase subunit 9. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AEP2 family."}
+{"protein": "MAFLKKSLFLVLFLGLVSLSVCEEEKRENEDEEEQEDDEQSEEKRALWKTIIKGAGKMIGSLAKNLLGSQAQPESEQ", "text": "FUNCTION: Has antimicrobial activity. Exhibits a bactericidal activity towards several species of mollicutes, firmicutes and gracilicutes. This peptide is membranotropic and it efficiently depolarizes the plasma membrane. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
+{"protein": "MAKSAAIITFLFAALVLFAAFEAPIMVEAQKLCEKPSGTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPAHKCICYFPC", "text": "FUNCTION: Confers broad-spectrum resistance to pathogens. Has antifungal activity in vitro. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family."}
+{"protein": "MQPALNAFTEQPADTAEATSRAGLEQAFALFNQMSSQLSESYSLLEERVTELKGQLALVSAQRMEELAEKERLANRLQSLLDLLPGGVIVIDAHGVVREANPAALGLLGEPLVGMLWREVIARCFAPREDDGHEISLRDGRRLSIATRSLNGEPGQLILLNDLTDTRRLQEQLARHERLSALGRMVASLAHQIRTPLSAALLYAGHLSEQALPTDQQQRFAGRLKERLHELEHQVRDMLVFARGELPLTDRVAPKALFDSLRAAAEVHVQGLQVRWQCEARGGELLCNRDTLVGTVLNLVENAIQACGPELRLKVHLYARADSLRLSVSDNGPGMDPATLARLGEPFFTTKTTGTGLGLAVVKAVARAHQGQLQLRSRPGRGTCATLILPLIPAAPLSAIQE", "text": "FUNCTION: Member of the two-component regulatory system FleS/FleR that regulates the expression of multiple genes involved in flagellar synthesis, adhesion, swarming, motility and antibiotic resistance (PubMed:30877999, PubMed:7591148). May function as a membrane- associated protein kinase that phosphorylates FleR in response to environmental signals leading to activation of specific gene promoters (Probable)."}
+{"protein": "MDSSPVSARFDIFEIYRRFCAIRSGQQLCNKKPCDGEESQRFNLSKEAITQLLYLVENKFQARNSIFDELFKLMSRLDLMVDFTEFTCFYDFVFFMCRENGQKNITISRAITAWKLVLAGRFRLLNRWCDFIEKNQRHNISEDTWQQVLAFSRCVHENLEGYDSEGAWPVLIDDFVEHMYSILGPNKDTSLFCKCGDTESESCLYQEDEHHKDYRRPHTGLRNIPGLKRKTSKKNDEEEEDEDEEVLETQNSSSLLNFKRIKTSNSPRCSSKSPCSIERSLSQGFASLLSTGDKP", "text": "FUNCTION: May contribute 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; neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity). Regulates responses to the synthetic auxin 2,4-dichlorophenoxyacetic acid (2,4-D) in roots, probably by modulating the SCF(TIR1) ubiquitin E3 ligase complex- mediated proteolysis (PubMed:17905859). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MATRKAGSRLETEIERCRSECQWERIPELVKQLSAKLIANDDMAELLLGESKLEQHLKEKPLRQGASPRGPRPQLTEVRKHLTAALDRGNLKSEFLQESNLVMAKLTYVEGDYKEALNIYARVGLDDLPLTAVPPYRLRMIAEAYATKGLCLEKLPVSSSTSNLHVDREQDVITCYEKAGDIALLYLQEIERVMLTNIQNRSPKPGPAPHDQELGFFLETGLQRAHVLYFKNGNLTRGVGRFRELLRAVETRTTQNLRMTIARQLAEILLRGMCEQSYWSPLEEPPYQSPLDDPLRKGANTKAYTLPRRARVYSGENIFCPQENTEEALLLLLISESMANRDAVLSRIPEHKSDRLISLQSASVVYDLLTIALGRRGQYEMLSECLERAMKFAFEEFHLWYQFALSLMAAGKSARAVKVLKECIRLKPDDATIPLLAAKLCVGSLHWLEEAEKFAKTVVDVGEKTSEFKAKGYLALGLTYSLQATDASLRGMQEGLQRKALLAFQRAHSLSPTDHQAAFYLALQLAISRQIPEALGYVRQALQLQGDDANSLHLLALLLSAQKHYHDALNIIDMALSEYPENFILLFSKVKLESLCRGPDEALLTCKHMLQIWKSCYNLTNPSDSGRGSSLLDRTIADRRQLNTITLPDFSDPETGSVHATSVAASRVEQALSEVASSLQSSAPKQGPLHPWMTLAQIWLHAAEVYIGIGKPAEATACTQEAANLFPMSHNVLYMRGQVAELRGHFDEARRWYEEALSISPTHVKSMQRLALVLHQLGRYSLAEKILRDAVQVNSTAHEVWNGLGEVLQAQGNDAAATECFLTALELEASSPAVPFTVIPRVL", "text": "FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and HYCC1, via direct interactions. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane Note=Localizes to the cytosol and is recruited to the plasma membrane following interaction with EFR3 (EFR3A or EFR3B)."}
+{"protein": "MTTKRKPYVRPMTSTWWKKLPFYRFYMLREGTAVPTVWFSIELIFGLFALKHGAESWMGFVGFLQNPVVVILNLITLAAALLHTKTWFELAPKAANIIVKDEKMGPEPIIKGLWVVTAVVTVVILYVALFW", "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": "MVLDLLKSGVLLAVLASFTFSVMNALVKEASATLPAAEIVFFRSAIGTLLIYLLMRQAGVALSRQGVPMLLVRGVMGALYLVCYFYAIAHIPLADASILAHMSPFFVILFSALFLGERIPRAVYWLLLVVVLGALMIVKPFSYSSYSVYAVVGLLSAVFAAGASVAIRQLSARHHTYEIVFYFLAVATLVAIPLMWSDFVVPATLREWGLLLAIGVVSLLGQVFLTRAFSHESATIVAVTRYIGIVFNAGWGWLFWSEVPDALTIAGGVLIVVACIALSRTKKG", "text": "FUNCTION: Transports the metallophore pseudopaline, which is involved in the acquisition of nickel and zinc, and thus enables bacterial growth inside the host, where metal access is limited. Is probably involved in the export of pseudopaline. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EamA transporter family."}
+{"protein": "MLRSVWNFLKRHKKKCIFLGTVLGGVYILGKYGQKKIREIQEREAAEYIAQARRQYHFESNQRTCNMTVLSMLPTLREALMQQLNSESLTALLKNRPSNKLEIWEDLKIISFTRSTVAVYSTCMLVVLLRVQLNIIGGYIYLDNAAVGKNGTTILAPPDVQQQYLSSIQHLLGDGLTELITVIKQAVQKVLGSVSLKHSLSLLDLEQKLKEIRNLVEQHKSSSWINKDGSKPLLCHYMMPDEETPLAVQACGLSPRDITTIKLLNETRDMLESPDFSTVLNTCLNRGFSRLLDNMAEFFRPTEQDLQHGNSMNSLSSVSLPLAKIIPIVNGQIHSVCSETPSHFVQDLLTMEQVKDFAANVYEAFSTPQQLEK", "text": "FUNCTION: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes. SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peroxin-3 family."}
+{"protein": "MSASRRESEPKEAETSPEAGGAASDRRRSKTSRACDQCREKKTRCDFSDERPICSACQRMGKTCTFERVPMKRGPTKGYTRNSEPPEGFDTSRRGSRKRSSSDVFKGDAGRPRADPVSLPPLAQYLPQSGSQPRLQPLLAPGAQPQQQFWKVPYYEYQHQRRGSIDSLGSDVSNRNGSEQLAYLPSNASSGSQFYPASQAQYASQLPSDVEGANPEDCRGSLSLPAIQKFQQPPSGYYLQYPYSQFSMLPQQQQQQQQQNAQQSYFTSQYVPPAAPPGAEHFKEFDEGFHSRKGSDVSVAVSPSSPVQVTRTQQAGLNSESRDTNTATAVSPKPLPKPSKPQMQTERSSSKSDGNHNGPRKQKRKNSNRNKPGSQSSIESIASSSHASIIYGKIPDKQLIDIYFEFIHPNFPVIPINKETLTDDLLLVNTQPISPVHELNTYILHWFRNSLELLVRVALKKPSGSGQAYSDGAVDILDSQATFINALNECFQRIVDIHPGLRENEKLLSLKTKFIYLATFSILNYILAFVGYDNSFVLGMSVTIYNECKLYRYLMYDELPSNDTEASENEDEAGAGDAHASGTPERGKSAKHDLGHQVLFKRLYVLLVVFDSLQSCAFGVPKLISVPLAELTEETFKFSTGKWCVERDPQRFETIRQSLVLGQVLSWLSISRKSVRRNSLQAAPQDASWKDEKSDSVSSSLFAKFLVQKHEMMEDFLLLAPLENSSHLLTFDLLSKSSTAICGLISSMHRLLALLMKINPTNSVDPNNRPPLRQGDFVHTDTEIQSESSNPPAATAAPDSCDADKFDVYRKLLGLNGGQERHVAQGTISPFVISIVVEIRNVLELVKHLPTSIIGVVVNLLPNGEGENYQKRSHRLVMSLSNAMNELVQITSLISLLKPFKMFDHTLRSNRPSAKVSTKLLRQKFAPESVKTPSSQPPSSSPGPNSDGSNNTSLSQNTVMHAILDAAWDLMDGEELGWL", "text": "FUNCTION: Glucose-responsive transcription factor that regulates expression of several glucose transporter (HXT) genes in response to glucose. In the absence of glucose, it functions as a transcriptional repressor, whereas high concentrations of glucose cause it to function as a transcriptional activator. In cells growing on low levels of glucose, has a neutral role, neither repressing nor activating transcription (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the EDS1/RGT1 family."}
+{"protein": "MAHRKLESVGSGMLDHRVRPGPVPHSQEPESEDMELPLEGYVPEGLELAALRPESPAPEEQECHNHSPDGDSSSDYVNNTSEEEDYDEGLPEEEEGITYYIRYCPEDDSYLEGMDCNGEEYLAHSAHPVDTDECQEAVEEWTDSAGPHPHGHEAEGSQDYPDGQLPIPEDEPSVLEAHDQEEDGHYCASKEGYQDYYPEEANGNTGASPYRLRRGDGDLEDQEEDIDQIVAEIKMSLSMTSITSASEASPEHGPEPGPEDSVEACPPIKASCSPSRHEARPKSLNLLPEAKHPGDPQRGFKPKTRTPEERLKWPHEQVCNGLEQPRKQQRSDLNGPVDNNNIPETKKVASFPSFVAVPGPCEPEDLIDGIIFAANYLGSTQLLSERNPSKNIRMMQAQEAVSRVKRMQKAAKIKKKANSEGDAQTLTEVDLFISTQRIKVLNADTQETMMDHALRTISYIADIGNIVVLMARRRMPRSASQDCIETTPGAQEGKKQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDIINTQEMYNDDLIHFSNSENCKELQLEKHKGEILGVVVVESGWGSILPTVILANMMNGGPAARSGKLSIGDQIMSINGTSLVGLPLATCQGIIKGLKNQTQVKLNIVSCPPVTTVLIKRPDLKYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATAHEKIVQALSNSVGEIHMKTMPAAMFRLLTGQETPLYI", "text": "FUNCTION: Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta."}
+{"protein": "MPPLSLLIKPASSGCNLKCTYCFYHSLSDNRNVKSYGIMRDEVLESMVKRVLNEADGHCSFAFQGGEPILAGLEFFERLMELQRKHNYKNLKIYNSLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEIHNLNRKDCCGLDTFSKVERAAELFKKYKVEFNILCVVTSNTARHVNKIYRYFKEKDFKFLQFINCLDPLYEEKGKYNYSLKPQDYTKFLKNLFDLWYEDFLNGNRVSIRYFDGLLETILLGKSSSCGMNGTCTCQFVVESDGSVYPCDFYVLDKWRLGNIQDMTMKELFETNKNHEFIKSSFKVHEECKKCKWFKLCKGGCRRCRDSKEDSDLELNYYCQSYKEFFEYAFPRLINVANNIK", "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": "MADIQTERAYQKQPTIFQNKKRVLEGETGKEKLPRYYRSVGLGFKTPREAIDGTYIDKKCPFTGNVSIRGRILSGVVTKMKMQRTIVIRRDYLHYIRKYNRFEKRHKNMSVHLSPCFRDVQVGDTVTVGECRPLSKTVRFNVLKVTKAAGTKKQFQKF", "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 uS17 family."}
+{"protein": "MTVGDHLVARMRAAGISVVCGLPTSRLDSLLVRLSRDAGFQIVLARHEGGAGYLADGFARASGKSAAVFVAGPGATNVISAVANASVNQVPMLILTGEVAVGEFGLHSQQDTSDDGLGLGATFRRFCRCSVSIESIANARSKIDSAFRALASIPRGPVHIALPRDLVDERLPAHQLGTAAAGLGGLRTLAPCGPDVADEVIGRLDRSRAPMLVLGNGCRLDGIGEQIVAFCEKAGLPFATTPNGRGIVAETHPLSLGVLGIFGDGRADEYLFDTPCDLLIAVGVSFGGLVTRSFSPRWRGLKADVVHVDPDPSAVGRFVATSLGITTSGRAFVNALNCGRPPRFCRRVGVRPPAPAALPGTPQARGESIHPLELMHELDRELAPNATICADVGTCISWTFRGIPVRRPGRFFATVDFSPMGCGIAGAIGVALARPEEHVICIAGDGAFLMHGTEISTAVAHGIRVTWAVLNDGQMSASAGPVSGRMDPSPVARIGANDLAAMARALGAEGIRVDTRCELRAGVQKALAATGPCVLDIAIDPEINKPDIGLGR", "text": "FUNCTION: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. SIMILARITY: Belongs to the TPP enzyme family."}
+{"protein": "MESLLLARLPEAYVVFSPLVDVFPVIPVFFLLLAFVWQAAVGFR", "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": "MDAPVPLSLSTLLELCTNLLQKSVNKSNGRFTAQLVHCRVIKSGLMFSVYLMNNLMNVYSKTGYALHARKLFDEMPLRTAFSWNTVLSAYSKRGDMDSTCEFFDQLPQRDSVSWTTMIVGYKNIGQYHKAIRVMGDMVKEGIEPTQFTLTNVLASVAATRCMETGKKVHSFIVKLGLRGNVSVSNSLLNMYAKCGDPMMAKFVFDRMVVRDISSWNAMIALHMQVGQMDLAMAQFEQMAERDIVTWNSMISGFNQRGYDLRALDIFSKMLRDSLLSPDRFTLASVLSACANLEKLCIGKQIHSHIVTTGFDISGIVLNALISMYSRCGGVETARRLIEQRGTKDLKIEGFTALLDGYIKLGDMNQAKNIFVSLKDRDVVAWTAMIVGYEQHGSYGEAINLFRSMVGGGQRPNSYTLAAMLSVASSLASLSHGKQIHGSAVKSGEIYSVSVSNALITMYAKAGNITSASRAFDLIRCERDTVSWTSMIIALAQHGHAEEALELFETMLMEGLRPDHITYVGVFSACTHAGLVNQGRQYFDMMKDVDKIIPTLSHYACMVDLFGRAGLLQEAQEFIEKMPIEPDVVTWGSLLSACRVHKNIDLGKVAAERLLLLEPENSGAYSALANLYSACGKWEEAAKIRKSMKDGRVKKEQGFSWIEVKHKVHVFGVEDGTHPEKNEIYMTMKKIWDEIKKMGYVPDTASVLHDLEEEVKEQILRHHSEKLAIAFGLISTPDKTTLRIMKNLRVCNDCHTAIKFISKLVGREIIVRDTTRFHHFKDGFCSCRDYW", "text": "SIMILARITY: Belongs to the PPR family. PCMP-H subfamily."}
+{"protein": "MSDGKKTKTTVNIYGQHFTIIGEESKAHMRHVAGVVDDKMREINEKNPYLDINKLAVLTAVNVVHDYMKLQEKYEILERQLKEKE", "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. In sporulating cells, localizes near the cell poles. SIMILARITY: Belongs to the ZapA family. Type 2 subfamily."}
+{"protein": "MGLLAYLLVILLILNVFFAAVTVFLERRDTSATWAWLLVLTFVPIFGFIIYLIFGRKLSGKKIFDWKGQEKIGIQESTANQIEMIRQKEFPFSDPNVKKHRDLIYLLLVNDGAILTQDNEVELFIDGHEKFDALIADIEKAKDHIHLIYYIFHSDELGNRLMRVLERKAAEGLNVKIIYDAMGSRTTKKSFFRTFEKNGGLVRPFFPSKLPLINFRLNYRNHRKLAIIDGDVGYIGGFNIGDEYLGRSKKFGYWRDTHLRVHGKAVYAMQTRFIMDWNSASSTHKIDYKARYFPTFHGKGHTSMQIVSSGPDSEWQQIKNGYIKMINAAKKTIYLQSPYFIPDASLLEAIKIAALSGVDVRVMIPNKPDHAFVYRATTNYAGELMETGAKIFIYDNGFIHAKTLVVDGEIASVGTANMDFRSFRLNFEVNAFIYEKKMVQKLEDAFLEDILKSYQLTPELYAKRSLWIKFKEAVSRLLSPIL", "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": "MSGLGIMLLTLLLLVFMETSHQDAGEKQATQRDAINVRRRRSLTRRVTEECEENCEEEEKHCCNTNNGPSCAPQCFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O3 superfamily."}
+{"protein": "MDPSMDTWDLSSPLISLWINRFYIYLGFAVSISLWICVQIVIKTQGRNLQEKSVPKAAQDLMTNGYVSLQEKDVFVSGVKIFYGSQTGTAKGFATVLAEAVTSLDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEAAIDFRFGKTYLKGMRYAVFGLGNSAYASHFNKVGKNVDKWLWMLGAHRVMSRGEGDCDVVKSKHGSIEADFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQRGSEEREEGSHEQDELHHRDTEEEEPFESSSEEEFGGKDHQSLNSIVDVEDLGKIMDHVKKEKREKEQREEKSGLFRNMGRNEDGEIRAMITPALREALTKQGYQLIGSHSGVKLCRWTKSMLRGRGGCYKHTFYGIESHRCMETTPSLACANKCVFCWRHHTNPVGTEWRWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPLFKDFWRRFLDSLKALAVKQQRTVYRLTLVKAWNVDELQAYAQLVSLGNPDFIEVKGVTYCGESSASSLTMAHVPWHEEVVQFVCELVDLIPDYEIACEHEHSNCLLIAHKKFKIGGEWWTWIDYNRFQELIQEYEDSSGSKTFSAKDYMARTPHWALFGANERGFDPKDTRHQRKNKSKAISGC", "text": "FUNCTION: Probable 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. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity). SIMILARITY: Belongs to the TYW1 family."}
+{"protein": "MAPKKKLQLPPPPTDEEEYWDSQAEEVLDEEEEDMMEDWESLDEEASEVEEVSDETPSPSVAFPSPAPQKSATGSSMATTSAPQAPPALPVRRPNRRWDTTGTRAGKSKQPPPLAQEQQQRQGYRSWRGHKNAIVACLQDCGGNISFARRFLLYHHGVAFPRNILHYYRHLYSPYCTGGSGSGSNSSGHTEAKATG", "text": "FUNCTION: Component of the packaging machinery which encapsidates the viral DNA into preformed capsids and transcriptional activator of the viral major late promoter (MLP). Binds, along with packaging proteins 1 and 3, to the specific packaging sequence on the left end of viral genomic DNA and plays an active role in packaging of the viral genome into preformed capsids. Specifically binds to the 5'-TTTG-3' nucleotides of the repeats making up the packaging sequence. Forms a transcription factor called DEF-A through cooperative binding with packaging protein 1 (Probable). DEF-A binds to downstream elements of the major late promoter (MLP) and stimulates transcription from the MLP after initiation of viral DNA replication. Simultaneously suppresses early gene expression and is thus likely to participate in the early- late switch in the expression pattern of the late viral proteins. May as well enhance transcription from IVa2 and pIX promoters. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the adenoviridae splicing factor family."}
+{"protein": "MSVRTLPLLFLNLGGEMLYILDQRLRAQNIPGDKARKDEWTEVDRKRVLNDIISTMFNRKFMEELFKPQELYSKKALRTVYERLAHASIMKLNQASMDKLYDLMTMAFKYQVLLCPRPKDVLLVTFNHLDTIKGFIRDSPTILQQVDETLRQLTEIYGGLSAGEFQLIRQTLLIFFQDLHIRVSMFLKDKVQNNNGRFVLPVSGPVPWGTEVPGLIRMFNNKGEEVKRIEFKHGGNYVPAPKEGSFELYGDRVLKLGTNMYSVNQPVETHVSGSSKNLASWTQESIAPNPLAKEELNFLARLMGGMEIKKPSGPEPGFRLNLFTTDEEEEQAALTRPEELSYEVINIQATQDQQRSEELARIMGEFEITEQPRLSTSKGDDLLAMMDEL", "text": "FUNCTION: May be involved in drug clearance in the placenta. SUBCELLULAR LOCATION: Basal cell membrane. Note=Syncytiotrophoblast in placenta."}
+{"protein": "MLPVCVDADQALRCSVLWRPWSLSPTEARGHKTLAGGVRSARPSGGVFHHPVRLFLPRSRMQEYLSRLGSSVLASFPVQATLHFYNDEDSSSEEEEDEEHANTRCRLWRP", "text": "FUNCTION: Probable transcriptional regulator involved in developmental processes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ripply family."}
+{"protein": "MGFLKILRKQRAREREMRILILGLDNAGKTTLMKKFLDEPTDTIEPTLGFDIKTVHFKDFQLNLWDVGGQKSLRSYWKNYFESTDALIWVVDSSDRERLTQCSEELKKLLQEERLSGASLLVLANKSDLPGAIDVNSIAQVLELQSIKTHHWKIFSCCALSGERLVQAMTWLCDDVGSRIFILD", "text": "FUNCTION: GTP-binding protein that functions in embryogenesis, cytokinesis, germline development and microtubulule cytoskeleton dynamics. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Some diffuse cytoplasmic expression is detected but expression is concentrated mainly next to centrosomes and is excluded from the mitotic spindle area. Localizes to the cortical plasma membrane of embryonic blastomeres (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
+{"protein": "SCADAYKSCDSLKCCNNRTCMCSMIGTNCTCRKK", "text": "FUNCTION: Non-toxic to mice and insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family."}
+{"protein": "MAATMAVTTMVTRSKESWSSLQVPAVAFPWKPRGGKTGGLEFPRRAMFASVGLNVCPGVPAGRDPREPDPKVVRAADNCDIAASLAPPFPGSRPPGRRGRGSEEEEAEGRRHEEAAAAGRSEPEEGQGQDRQPAPARLVSGAIAGAVSRTFVAPLETIRTHLMVGSIGVDSMAGVFQWIMQNEGWTGLFRGNAVNVLRVAPSKAIEHFTYDTAKKFLTPKGDEPPKIPIPTPLVAGALAGFASTLCTYPMELIKTRVTIEKDVYDNVAHAFVKILRDEGPSELYRGLTPSLIGVVPYAACNFYAYETLKRLYRRATGRRPGADVGPVATLLIGSAAGAIASSATFPLEVARKQMQVGAVGGRQVYQNVLHAIYCILKKEGAGGLYRGLGPSCIKLMPAAGIAFMCYEACKKILVDKEDEEEEDEAGGGEDDKKKVE", "text": "FUNCTION: Probable adenylate translocator that mediates transport of ADP-glucose into endosperm storage plastids during starch synthesis. Transports cytosolic ADP-glucose to amyloplast stroma by counter- exchange with ADP. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein Plastid, amyloplast inner membrane; Multi-pass membrane protein Mitochondrion inner membrane; Multi-pass membrane protein Note=Dually targeted to mitochondria and plastids. The N-terminal extension acts as plastidic transit peptide. Dual localization of BT1 does not seem to be due to alternative transcription start sites, translation initiation sites or alternative exon splicing (PubMed:21330298). SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MAFASEDIAYHSSNAVYRVPSNRHEADQEALLGKPLDYPAPGLQRPEDRFNGAYIIFFCLGIGGLLPWNFFVTAKEYWAFKLRNCSSPASGKDPEDADILNYFESYLAVASTVPSLLFLVANFLLVNRIRVHVRVLASLSVSLAIFVVMAVLVRVDTSSWTRGFFSIAMACMAIISSSSTIFNSSVYGLTGSFPMRNAQALISGGAMGGTVSAVASLVDLAASSDVRDSALAFFLTAAVFLGLCVGLYLLLPQLEYARYYMRPVVPIHVFSSEDSPPRDAPSTSSVAPASRAVHTPPLGPILKKTAGLGFCAVFLYFITALIFPAISTNIQPMHKGTGSPWTSKFYVPLTVFLLFNFADLCGRQVTAWIQVPGPRSKLLPILAVSRVCLVPLFLLCNYQPRSHLTLVLFQSDIYPILFTCLLGLSNGYLSTLVLMYGPKIVPRELAEATSVVMLFYMSLGLMLGSACAALLEHFI", "text": "FUNCTION: Uniporter that mediates the facilitative transport of nucleoside across lysosomal and mitochondrial membranes. Functions as a non-electrogenic Na(+)-independent transporter. Substrate transport is pH-dependent and enhanced under acidic condition, probably reflecting the location of the transporter in acidic intracellular compartments. Proton is not a cotransporting ion but most likely change the ionization state of the transporter which dictates transport- permissible/impermissible conformation for nucleoside translocation. May direct the nucleoside transport from lysosomes to cytosol or cytosol to mitochondria to facilitate the fundamental function of salvage synthesis of nucleic acids. Involved in the transport of nucleosides (adenosine, guanosine, uridine, thymidine, cytidine and inosine) and deoxynucleosides (deoxyadenosine, deoxycytidine). Also mediates transport of purine nucleobases (adenine, guanine) and pyrimidine nucleobases (uracil). Also able to transport monoamine neurotransmitters dopamine, serotonin, noradrenaline and tyramine. Capable of transporting ATP (By similarity). Mediates nucleoside export from lysosomes in macrophages, which regulates macrophage functions and numbers (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Mitochondrion membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family."}
+{"protein": "MTTPRWRLILNGKSAGNDELRDAVGHWRGQGVQLEVRVTWEDGDAERYVAEAIDHGVDVIVAAGGDGTLSAVAETLAHREELADALPSLALIPMGTANDFATAAGIPTEPKEAFALIGQATPHAIDLLRVDADGTQWWCANLASGGFGTQVTVETDAGLKKMLGGLAYVITGIAKLGRIEPITARLSGPDFAWEGDFIALGIGNGRQAGGGQQLCPQALIDDGLLDVTVLPELEGEVTATLGQMLKSGTQAALEQLATRARLPWLEIASERPLTLNLDGEPVQARQFRIECVPGRVRMHLPAGCPLLGG", "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": "MESNYTGMDGNWALNGTVSVGNGTLISVDEFLHNALPMHLQALFQDGNSQGPLLTMEDLEKAIEFKRASQELVNDNVLAPDGLFVELLRQQEKTLPRLISATSNTQGSFSSWSFAQGLIVGQVSVVLVLIFFIKFFIFSDSSTKTNPNPAKNSSSTNSLSGLSSESRSFISPHFFTSIMNRKGNEQAESNDDENERSRQIDDILEKTYYNVDTHPAESLDWFNVLIGQTIQQLREEAWKKDNIVYSLNAFIERKAQELPSYLDSIKITELDIGHDFPIFSNCRIQYSPNSNGRKLEAKIDIDLNDRLAVGIETRLLLNYPKPLTASLPINVTVSIIRFQACLTVSLTKAEEFVPTSPESVDEDDNDGYFLMFSFAPEYRMEFETQSLIGARSKLENIPKIGSLVEYQIKKWFVERCVEPRFQFIKLPSVWPRSKNTREGKADVDESEPGRETHY", "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 (By similarity). Preferentially binds to glycerophospholipids such as phosphatidylcholoine (PC), phosphatidic acid (PA), phosphatidylglycerol (PG), and phosphatidylserine (PS), but not to phosphatidylethanolamine (PE) (PubMed:29078410). 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 (By similarity). 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": "MVVAYKHEPFTDFSVEANKLAFEEGLKKVESYLGQDYPLIIGGEKITTEDKIVSVNPANKEELVGRVSKASRELAEKAMQVADETFQTWRKSKPEMRADILFRAAAIVRRRKHEFSAILVKEAGKPWNEADADTAEAIDFMEYYGRQMLKLKDGIPVESRPIEYNRFSYIPLGVGVIISPWNFPFAIMAGMTTAALVSGNTVLLKPASTTPVVAAKFMEVLEEAGLPAGVVNFVPGNGSEVGDYLVDHPRTRFISFTGSRDVGIRIYERAAKVNPGQIWLKRVIAEMGGKDTIVVDKEADLELAAKSIVASAFGFSGQKCSACSRAVIHEDVYDHVLNRAVELTKELTVANPAVLGTNMGPVNDQAAFDKVMSYVAIGKEEGRILAGGEGDDSKGWFIQPTIVADVAEDARLMKEEIFGPVVAFCKAKDFDHALAIANNTEYGLTGAVISNNRDHIEKAREDFHVGNLYFNRGCTGAIVGYQPFGGFNMSGTDSKAGGPDYLALHMQAKTTSETL", "text": "SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA subfamily."}
+{"protein": "MAHHDSVLVISSSPDFPSICDLLPKATRQPSLRSGSNAAPVSNDAPAAFTSAANIWQSSRARHLEGAEISNIGPSQSATTAADLATVPAESPIKSGVEGPTLPLGGDKKKPRTAGARKKKGKTETIEPPLALDMAVADGPVAVAPPKKSGRKPRAKKDATLAQTTLPKGKVTKTAAREITKAQKKAETVSRHFTPHTSAPPELVAGPIDDSPSVFEPAMARRMDWTPPRESASVHCLADSSMEKEVSSSALSLQDHVFKNLQDTYGRTMEASGYIGAALPLTSMDVLGKRKLVEMVSCVGHRQEIPQASPTKPKVVKKKPRTITELATAAYRRPEEAERSTLSRQQDTHIPSGNLELPSEQLTAASKSASAKPKAAKKAPKPRATKKKQSPPEPILLSPTSAMRQVSNQDFVFGTASQLATEDDPVLLRALHEAMKVSNQADSDPFATPSPGNSNLAIRRRSGAGLWAAGARYGDGDLLDAEVLDLTRSSPLTLAQFAQNPPPPCPEAVLADKPPVESAYIEIEMSDDTLDLTISPPVGSPKTLPPCPPRPGGQAVRHKDSNLAVSGRPQTPPQEADFDPPPSNQEQHQLLLSQSNTPQQPQPAPPPPPSFELYTDARLAKEVASYGFKVVKKRTAMIALLNRCWESRNKTALGSTAAQAAMSTSAPNQAASPSRPRGRPRKDSLTATTEVVQAPSPAKKGRKKAGVVSGAGSEVPQPEKWPRGRPRKDSAASVSSITAPAATNPRRRSAAISDVDSDEPQVEKRSRGRPKKDATTSPATRATRAKAPPSPKRAKSPCTTQPAPTTPRRRKAPAKQIFEIPDSGSDDPFASSAPSSPDQHSDLFSSPPAVDLSVTEDTEASLIASPTTQDVSLFGYITRAVASAPPTKDPANPSWHEKMLMYDPIILEDLTAWLNAGRLDQVGFDGEVAPGDVKKWCESKSVCCLWRVNLRGKERKRF", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX4 family."}
+{"protein": "MSLRDDLTINERDPLLSSFDQRQEYNTSNNTYKVNNNSNEPSVLTLYNSDELGTSQRSSYQKFVRRSQEFKMQHREFLAEFIGTLILVLLTCGFCAEQTLNIEKSKSWLTSSLGSGLSVLIGICVAGHVSGGHLNPAITIAFWVFSGFPIRKVPMYITAQLLGAFSGAALLYSIVEPAISQFDHGKRQILGELGTAGIFGTYPPLYVGTGSAVASEVVGTAMLLLVVMVTGHPNNLPFRTAQGAMIALGVTTISLCIGYTSGFSLNPARDFGPRLFTAVAGWGIDVFTVHHYYALVPMFAPILGGLAGGFIYTVFID", "text": "FUNCTION: Water channel required to facilitate the transport of water across membranes (PubMed:26959825). Contributes to water uptake of spores during the early stages of spore germination (PubMed:26959825). Aquaporins AQP1 and AQP2 act as extracellular pH sensors and enable the spores to hydrate under favorable conditions and to commence germination (PubMed:26959825). Wounded vegetables and fruit present acidic pH, so the optimal pH range for germination is adapted to the relevant host pH (PubMed:26959825). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
+{"protein": "MGETIADVYAESIDPEIYANNPAYSSLFTPYIHKQTIIADHVSVQCHIDLNGIDAVGSKFGNLNAHAGNFTSLCAPNCLPERLALVAYTVEYAFLHDDETDNAADQEALLLENKMLHQAINQSSMTSVSNRVSAKAQRKSEVQAKIAAEYLRLDPVFGEFFLKAWQTFTASVQDVRSLEFPSLDDYLEFRIVDAAADWTLYNFRWGSGITLTPEEEKIADPMSYVAYAELCLVNDLFSWDKEYDAHVKSNGEVPLVNAVHIVAVTQGLTHCAAKAVVQAEIRAHEERFCYLKEQYKATASPSDSILSWLKLLEHSMAGNWVWSLCVPRYFKVERNPYKDHLEKFGSEAVRVLTPEEHLRDSKQEINGTKEIELQEPKSNNTAESDVLAKYTSGYPTIDEPVLNPYTYINSLPSKNVRQTMIAALNSWYKVPVKSLLIIEGAVNFLHNSSLLLDDIQDGSVLRRGRPVAHQIFGVGQTINTATYLMNEALYLVQMLSPSAVLVYTDEMRNLQLGQGRDLHWSYHTHVPTPAQYISMVDGKTGGLFRLISRLMRSEATVNRDLDISQFATLLGRHFQIRDDYQNLQSDDYTKNKGFCDDLDEGKLSFPIILSMQSPGFSNTALSSVFKGSQKGETLSPEMKQYILEEITARGAFSQTKAVLRKLHIELLRLLMETEQKAGGIENWALRLLIMKLDLGDEKKKEAHKSDSAWKVNQRRAWKGSQKNGRPIDKACFLRAMEEASQK", "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 PrDS converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into deoxyconidiogenol (PubMed:30343633). The C- terminal prenyltransferase (PT) domain of PrDS 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 PrP450 then catalyzes two rounds of oxidation to furnish conidiogenone (PubMed:30343633). 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": "MNQYNVKYLAKILCLKTEIARDPYAVINRNVLLRYTTDIEYNDLVTLITVRHKIDSMKTVFQVFNESSINYTPVDDDYGEPIIITSYLQKGHNKFPVNFLYIDVVISDLFPSFVRLDTTETNIVNSVLQTGDGKKTLRLPKMLETEIVVKILYRPNIPLKIVRFFRNNMVTGVEIADRSVISVAD", "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 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 (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. 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 22 kDa subunit family."}
+{"protein": "SVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTPACISLGSRSQIVTNVRNTIHGFKKIRLPYELQKMPNGSTGVKVRLKVLATTFDPYLGGRVEPPLKSVMDQANLQREDINSIEIVGGATRIPAVKEQVTRFFLKDISTTLNADEAVARNHPAPFSKSIDLPIQSSLYRNAVEEYVYDFRDKFITPEDMNKYGQPIQMKYVEHEERPK", "text": "FUNCTION: Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=May translocate to the nucleus after heat shock. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MEKLPKKRVSKTKSQKLIHSLTTQKNRAFLKKISANEMLLELEKGAFKKNEAYFISDEEDKNYVLVPDNVISLLAENARKAFEARLRAELERDIITQAPIDFEDVREVSLQLLENLRQKDGNLPNINTLNFVKQIKKEHPNLFFNFDNMFKQPPFNENNFENFDNSDEENF", "text": "SIMILARITY: Belongs to the UPF0763 family."}
+{"protein": "MAFLKKSLFLVLFLGLVSLSICEQEKREEENQEEDEENEAASEEKRGLMSSIGKALGGLIVDVLKPKTPAS", "text": "FUNCTION: Amphipathic alpha-helical antimicrobial peptide with moderate activity against Gram-positive bacteria (MIC=100 ug/mL against L.lactis and MIC=50 ug/mL against S.uberis) (PubMed:10951191). Has no activity against Gram-negative bacteria (PubMed:10951191). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Aurein subfamily."}
+{"protein": "MRIVIGSFTAFLLLLLQNSNAEIPGCDFFDTVDISKAPRFSNGSYLYEGLLIPAHLTAEYDYKLLADDSKEKVASHVRGCACHLRPCIRFCCPQYQKMQKSKCYGDMSEDELNKHDPFVNVTLSDGSVVRRHFKEDLIVQSDLAKPGCPRMYFLNHELPGNEFTLFENGSLLRHWDKVELSKREYCVQHLSFKDDSIRIAPHFCPLSSEHSRTWKTVAIVISLICIILTISVYLYVEKLRNLHGKCFICYLASLFLGYFFLVLNVWKYSSGFCVTAGFLGYFSVIAAFFWLSVISLTLWNSFSGNSSWLNRFLPQNRFLSYNLYAWGMALLLTAITYIADQVVKNEKLRPRVGVGKNCWIYTGDMTVMIYFYGPMLLIIVFNITMFVLTAFRIMKVKKEAQNFTQQQKTTNRLNSDKQTYALFLRLFIIMGLSWSLEIISFLLSKNQAWAKAFMVADYFNWSQGTVIFLLFVLRPSTLKLLKERIKGGRDEAGASDEHISLQNTKIDPSVF", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Mth subfamily."}
+{"protein": "MLELRLVQGSLLKKVLEAIRELVNDANFDCSGTGFSLQAMDSSHVALVALLLRAEGFEHYRCDRNLSMGMNLNNMAKMLRCAGNDDIITIKADDGSDTVTFMFESPKQDKIADFEMKLMDIDSEHLGIPDSEYQAIVRMPSSEFMRICKDLSSIGDTVVISVTKEGVKFSTSGEIGSANIVCRQNQTIDKPEEATIIEMQEPVSLTFALRYMNSFTKASSLSEQVTISLSSELPVVVEYKIAEMGYIRFYLAPKIEDDEEMKP", "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": "MDDENGLELSLGLSLGGTSGKSKARDAPLEPKAEPQVEESSSKGVSQTPEAPFVHYYQTNAENQEHSSKQRHSPAAPPFGNFWGQPGSSSVPVADGSNEQKPVSSKRKLLSEEISFQKKPNTAAEQPDAFSKSSDGGVKNAPISISTDDGSTGENEDVAESEAEGSNSWLVAQREDSAKGSVVNRGSDRKRSSDDAAVGFQGKRQPSFSGSESSSGKLPQGNPLSLQASNVVAVPYQVPSQVSAPPSITNASNFTPVCTVQLRPPTNNGLAVTMGSTSQVAFGYPAVQLPTLETSSSWAFGAPPQAMSSFTAKDKVERAGISQADDGKKTQEAGASSSALVEDDKKSDRALPLMGSAIRPGIAPNVKFGGSGSYPDLPWVSTTGTGPNGRTISGVTYKFGRNEVKIVCACHGTHMTPEEFMRHASADAPGQENSATLPAFPVGNQAASAQN", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Ninja family."}
+{"protein": "MKPSLKRRLLLLSRKFAKASIRKLLRQSSFSSHEFLLQAPFPAMSWYRRTKLVFDSLRRNINPKILPRSHVTSRINNPIGSSNPSAKFSSISSREVGLRSWTSLGRNTNRIAYNPFLSQPKRYYYVDRYQVRHFKPRGPGRWFQNPRTVFTVVLVGSVGLITLIVGNTETIPYTKRTHFILLSKPMEKLLGETQFEQIKKTYQGKILPATHPESIRVRLIAKEVIDALQRGLSNERVWSDLGYASTESSLGGGSDKGVKEMEMAMSGEDTMTDMKWSKEDQVLDDQWIQKSRKKDSKAHAATSHLEGISWEVLVVNEPIVNAFCLPAGKIVVFTGLLNHFKSDAEVATVIGHEVGHAVARHVAEGITKNLWFAILQLVLYQFVMPDLVNTMSALFLRLPFSRKMEIEADYIGLLLLASAGYDPRVAPTVYEKLGKLGGDALGDYLSTHPSGKKRSKLLAQANVMEEALMIYREVQAGRTGVEGFL", "text": "FUNCTION: Protease that is part of the quality control system in the inner membrane of mitochondria (By similarity). Metalloendopeptidase that modulates the oxidative phosphorylation (OXPHOS) system and plant growth (PubMed:28936218). Involved in tolerance mechanisms to heat, osmotic and oxidative stresses (PubMed:28936218). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase M48A family."}
+{"protein": "MGHPPLEFSDCYLDSPDFRERLKCYEQELERTNKFIKDVIKDGSALISAMRSYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLNEVENERMMMVQNASDLLIKPLETFRKEQIGFTKERKKKFEKDGERFYSLLDRHLHLSSKKKESQLLEADLQVDKERHNFFESSLDYVYQIQEVQESKKFNIVEPVLAFLHSLFISNSLTVELTQDFLPYKQQLQLSLQNTRNHFSSTREEMEELKKRMKEAPQTCKLPGQPTIEGYLYTQEKWALGISWVKYYCRYEKETRTLTMTPTEQKPGAKQGPVDLTLKYCVRRKTESIDKRFCFDIEANERTGTITLQAPSEANRRLWMEAMDGKEPIYHSPITKQEEMELNEVGFKFVRKCINFIETKGIKTEGLYRTVGSNIQVQKLLNAFFDPKCPGDVDFYNSDWDIKTITSSLKFYLRNLSEPVMTYKLHKELVSAAKSDNLDYRLGAIHSLVYKLPEKNREMLELLIKHLVNVCEHSKENLMTPSNMGVIFGPTLMRAQEDTVAAMMNIKFQNIVVEILIEHFGKIYLGPPEDSQVPPVPPPRVTARRHKPITISKRLLREKAVFYTPSLDDVEDEIHHPTPNGTIASNLDPPKQLQHLKLPMQKSGEMDPGRKSPSRPVSDCQTEPCLEADMGKLVYRLQDGGTKAIPKASNGPVPGSGHTKTSSFHIKRPAPRPIVHHKEGDTDCFSKVRPPGEKQTIIRPPVRPPDPPCRSSTSQKPESKPETVSSNAEEIPSSVVASRTRFFETASRKTGSSQGKLPGDES", "text": "FUNCTION: Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function, in hippocampal neurons. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the regulation of synaptic vesicle endocytosis at pre-synaptic terminals. Required for the localization of NR1D1 to dendrites, can suppress its repressor activity and protect it from proteasomal degradation. SUBCELLULAR LOCATION: Postsynapse Presynapse Cell projection, axon Cell projection, dendritic spine Cell projection, dendrite Cytoplasm."}
+{"protein": "MPETTQDTCASAKDSPFFIKNLLNSDSKPSKPKPILAPTKAGLDGSFSLSQVGEINFPRFELPTQRFALPAYLERASAWWYPYTLSASAHLHRTEAAQKARDSSPTTGTDRDSPELVLKSDPDAKDDEDDNKSGDEIVLEEGDTEDGKKEGGIDDWKKSDDGADKKPCRKKKTRTVFSRSQVFQLESTFDMKRYLSSSERAGLAASLHLTETQVKIWFQNRRNKWKRQLAAELEAANLSHAAAQRIVRVPILYHENSASESTNTAGNVPVSQPLLTFPHPVYYSHPIVTSVPLLRPV", "text": "FUNCTION: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development. Binds to the 5'-CAAGTG-3' core sequence (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HMX homeobox family."}
+{"protein": "MDIWKPEIKYLRYTNGFNVSELEDACFKFNYKFPKVGYCRVPSHAWCRNQGSFCATLTLYGKSKHYDKYFGVITGFTAFANTVEEAVNKLVFLAVDFITWRRQELNVYG", "text": "SIMILARITY: Belongs to the coronaviruses ns12.7 protein family."}
+{"protein": "MAHDEQLWLTPRLQKAAALCNQTPAASDTPLWLGVDLGTCDVVSMVVDGNAQPVAVCLDWADVVRDGIVWDFFGAVTLVRRHLDTLEQQLGCRFTHAATSFPPGTDPRISINVLESAGLEVSHVLDEPTAVADLLALDNAGVVDIGGGTTGIAIVKQGKVTYSADEATGGHHISLTLAGNRRIPLEEAEQYKRSNAQEIWPVVKPVYEKMAEIVARHIEGQGIADLWLAGGSCMQPGVEALFRQRFPELQVHLPQHSLFMTPLAIANSGRAKAEGLYAS", "text": "FUNCTION: May protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition, may function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. FUNCTION: May protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition, may functin in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity (Probable). Overexpression of eutJ and eutS in E.coli leads to multiple BMC-like structures; eutS expression alone leads to 1 BMC-like structure per cell (PubMed:27063436). 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). SIMILARITY: Belongs to the EutJ family."}
+{"protein": "MANKAPSQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKRNEALINDIMEDLDTNQDNQLSFEECMMLMAKLIFACHEKLHENNPRGHGHSHGKGCGK", "text": "FUNCTION: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response (PubMed:15331440, PubMed:17767165, PubMed:18403730, PubMed:19402754, PubMed:22804476, PubMed:34562450). It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism (By similarity). Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions (By similarity). The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH- oxidase (PubMed:15331440). Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX (By similarity). The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities (PubMed:21382888). Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration (By similarity). Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER) (PubMed:17767165, PubMed:18403730, PubMed:19402754). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade (PubMed:17767165, PubMed:18403730, PubMed:19402754, PubMed:22804476). Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth (By similarity). Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3 (By similarity). Can regulate neutrophil number and apoptosis by an anti- apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK (By similarity). Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants (By similarity). The iNOS- S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, NXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x- [DE] motif (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm Cytoplasm, cytoskeleton Cell membrane; Peripheral membrane protein Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation or endothelial adhesion of monocytes, is secreted via a microtubule-mediated, alternative pathway. SIMILARITY: Belongs to the S-100 family."}
+{"protein": "MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEGKKGKTTIKTGASVLNKWQMNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFPPKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNPKTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPTVQGLAALEKEAQTSFLHLGYLPNQLFRTS", "text": "FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double- strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation. Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1. Specifically binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasmic granule Cytoplasm, cytosol Mitochondrion Note=Localized with MBNL1, TIAL1 and YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage bodies. Forms large aggregates called DDX1 bodies. Relocalized into multiple foci (IR-induced foci or IRIF) after IR treatment, a process that depends on the presence of chromosomal DNA and/or RNA-DNA duplexes. Relocalized at sites of DNA double-strand breaks (DSBs) in an ATM-dependent manner after IR treatment. Colocalized with RELA in the nucleus upon TNF-alpha induction. Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low. Colocalizes in the cytosol with DDX21, DHX36 and TICAM1. Colocalizes in the mitochondria with TICAM1 and poly(I:C) RNA ligand. The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) stimulation (By similarity). SIMILARITY: Belongs to the DEAD box helicase family. DDX1 subfamily."}
+{"protein": "MQSSLARPLRPPVLAGRGGRRGLVAVARCHAEAAPPVGTASRAPAGPYTGRDPEVKKPAWLRQRAAQGEKYARLRESIGELKLNTVCVEAQCPNIGECWNGGGGAGGEGDGIATATIMVLGDTCTRGCRFCAVKTSNKPPPPDPLEPLNTALAVASWGVDYVVLTSVDRDDLPDGGSSHFAQTVKALKELKPGILVECLTSDFRGDLEAISSLASSGLDVYAHNIETVRSLQRIVRDPRAGYDQSLAVLKHAKACREGMVTKSSIMLGLGETDEEVKQAMMDLRAIGVDILTLGQYLQPTERHLTVREYVTPEKFQFWKEYGESVGFRYVASGPLVRSSYRAGELFVQNLVRNNKTGSSSS", "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: Plastid, chloroplast. SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase family."}
+{"protein": "MGCRQSRHSRGKRAEKVEETQTELLEALDKEGRILEGRHEEAGQVPQTSNAQEKVSLSDCIQEAKASLQNTCASHVSPQEATQAKMNKVDGSILSRLYRNHIQDYGSPGPFWEQELESLHHVIEMKNERIHELEKQLFLLEMLKEKNLILALKNTTLRQEVEDLQFQAGNRLTMSRQLRKDLLQDLEKESQNGHCCSRRRSH", "text": "FUNCTION: May act as a scaffold to regulate the recruitment and assembly of spindle midzone components. Required for the localization of AURKB and PLK1 to the spindle midzone. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Midbody Note=During early anaphase, localizes along overlapping interpolar microtubules between the separating chromosomes. During late anaphase, localizes to the center of spindle midzone. Concentrated at the midbody during telophase. SIMILARITY: Belongs to the CCDC69 family."}
+{"protein": "MATALYTANDFILISLPQNAQPVTAPGSKTDSWFNETLIGGRAFVSDFKIPEFKIGSLDTLIVESEELSKVDNQIGASIGKIIEILQGLNETSTNAYRTLPINNMPVPEYLENFQWQTRKFKLDKSIKDLITLISNESSQLDADVRATYANYNSAKTNLAAAERKKTGDLSVRSLHDIVKPEDFVLNSEHLTTVLVAVPKSLKSDFEKSYETLSKNVVPASASVIAEDAEYVLFNVHLFKKNVQEFTTAAREKKFIPREFNYSEELIDQLKKEHDSAASLEQSLRVQLVRLAKTAYVDVFINWFHIKALRVYVESVLRYGLPPHFNIKIIAVPPKNLSKCKSELIDAFGFLGGNAFMKDKKGKINKQDTSLHQYASLVDTEYEPFVMYIINL", "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 (PubMed:10781598, PubMed:11777935, PubMed:1730668, PubMed:8416931). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:8416931). 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 (PubMed:15792803). Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section (PubMed:15792803). SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the V-ATPase C subunit family."}
+{"protein": "MGDVSELKMQITPETPGRIPVLNPFESPSDYSNLHEQTLASPSIFKSTKLPTPGKFRWSIDQLAIINPVEIDPEEIHRQASYLRLSRIDKDVEDKRQKAIEEFFTKDVIVPSPWTDHDGKQPSELHPSKCLSSHDDSPDGKKPSLPSQKCNAACQTLLSLPVDFNLEAILGDYFREEDFVAHTPGNLSSSSLRRKLFLDGNGSICDPLPSPSPGSPPCSARGSLEGQFSSSPIQNSVKKYSLGSVTTSPSAISSPTFSPIALQGGKTPLSEPRKLTFHSPEASCATASTGIVNPSIRSPYIDGCSPIKNWSPRRLRGGPQCLSSLVRIPFTLEAHSEDEEADVSCTGAAPLSTNACGEPRVVTAMSVTQSHSGIAEKERAVLDDAESERENDTVDMVDPTDTVAESTWIKEPVDDGNSPMTDSASGIAFSIENSHMCMSPLAESSVLPYESSAIQMNSDYNTQTCVSNITDIVGTERYCKENVTHTNVPVPFEVEMKSQVNNVTPGHTAQRCWMKSPRPSQCSRP", "text": "FUNCTION: Required for the activation of AURKA at the onset of mitosis. SIMILARITY: Belongs to the BORA family."}
+{"protein": "MKLPKEGDFITIQSYKHDGEIHRTWRDTMVLKTTENAIIGVNNHTLVTENDGRRWVTREPAIVYFHKKYWFNIIAMIRENGVSYYCNLASPYVLDNEALKYIDYDLDVKVFADGEKRLLDVDEYERHRKAMKYSDDIDFILKENVKILVDWINNQRGPFSPAYVNIWYKRYLELRSR", "text": "SIMILARITY: Belongs to the UPF0374 family."}
+{"protein": "MSSRFAGGNAYQRDTGRTQLFGPADGSNSLDDNVSSALGSTDKLDYSQSTLASLESQSEEQMGAMGQRIKALKSLSLKMGDEIRGSNQTIDQLGDTFHNTSVKLKRTFGNMMEMARRSGISIKTWLIIFFMVGVLFFWVWIT", "text": "FUNCTION: SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type IV membrane protein Endoplasmic reticulum membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the BET1 family."}
+{"protein": "MSQPKRIHRICKGLARFTIRATLYGSWVLGLFPFTFDSRKRRLNRSKWLLAYGLVLNLTLLVLSMLPSTDDHNSVKVEVFQRNPLVKQVEELVEVISLITTLVTHLRTFSRSSELVEILNELLVLDKNHFSKLMLSECHTFNRYVIEKGLVIILEIGSSLVLYFGIPNSKIVVYEAVCIYIVQLEVLMVVMHFHLAVIYIYRYLWIINGQLLDMASRLRRGDSVDPDRIQLLLWLYSRLLDLNHRLTAIYDIQVTLFMATLFSVNIIVGHVLVICWINITRFSLLVIFLLFPQALIINFWDLWQGIAFCDLAESTGKKTSMILKLFNDMENMDQETERRVTEFTLFCSHRRLKVCHLGLLDINYEMGFRMIITNILYVVFLVQFDYMNLKFKTD", "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. Gr22e subfamily."}
+{"protein": "MRYTGLMGTLLTLVNLLQLAGTLRIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRDKPDTYRYVVSEPLGRKSYKEQYLFVYRPDQVSILDSYQYDDGCEPCGNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPTEAVSEIDALYDVYLDVWQKWGLEDIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAGALLQAAVVPNSAVPFDFQAEYGLSNQLAEAISDHYPVEVTLRKI", "text": "FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:29191910). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA. Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (PubMed:29191910). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (PubMed:29191910). 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 (PubMed:29191910). 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": "MYAMKAMKQYQQVSIEAQVSDANPHRLIQLLMQGGLERLAQARGAMEREQIPEKGILIGKAIGIIGGLREALDSERGGELAGNLDRLYEYMIARLVEANTSNDTSLLDEVSALLLEVKSGWDGISH", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the FliS family."}
+{"protein": "MSTDSDTTPDTEEAREQLIDLAADFYDQFADGEVPTMTIPTRTKSNIVFDEDEQVWVYGDRNSTRSAKTISGAEKILKAVYTIDFLSQQLEEDRSSTLRELYYLSESWDLDEAQFNTQDESNNLIEDLEIVSDVKREDFHMRPEESGAKVMGPLLLREQTNRGDREIHCQDDVGQGGYQIPNNPDTIEFLDNDAKFVLCVETGGMRDRLVENGFDDEYDALVVHLGGQPARATRRLIKRLHDELDLPVTVFTDGDPWSYRIFGSVSYGSIKSAHLSEYLATPEAQFIGIRPEDIVEYELPTDPLSDSDVNALESELEDPRFQTDFWEEQIELQLDINKKAEQQALASRGLDFVTETYLPERLDEMGIL", "text": "FUNCTION: Relaxes both positive and negative superturns and exhibits a strong decatenase activity. SIMILARITY: Belongs to the TOP6A family."}
+{"protein": "METQVKVLVLVGALFINTYTDNYKSVDLTHDSEQAYGFKDKWEAQQVAAKVGGQVVVRTTSFKIV", "text": "SIMILARITY: Belongs to the phi29likevirus GP5.5 family."}
+{"protein": "MKNFILLAVSSILLVDLLPTHFEHNVDLSRAINVNGVSFNNVDTSSLGAQQVRQSASRGRGLGEKPKEGADKEKKKEKGKEKEEEPKKPNENKLKQPNEGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANAGQPQAQGDGANVPRQGRNGGGAPAGGNEGNKQAGKGQGQNNQGANAPNEKVVNDYLHKIRSSVTTEWTPCSVTCGNGVRIRRKAHAGNKKAEDLTMDDLEVEACVMDKCAGIFNVVSNSLGLVILLVLALFN", "text": "FUNCTION: [Circumsporozoite protein C-terminus]: In the vertebrate host, binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes and is required for sporozoite invasion of the host hepatocytes. FUNCTION: Essential sporozoite protein (By similarity). In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands (By similarity). In the vertebrate host, required for sporozoite migration through the host dermis and infection of host hepatocytes (By similarity). Binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Cytoplasm Note=Localizes to the cytoplasm and the cell membrane in oocysts at day 6 post infection and then gradually distributes over the entire cell surface of the sporoblast and the budding sporozoites. SIMILARITY: Belongs to the plasmodium circumsporozoite protein family."}
+{"protein": "SYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEF", "text": "FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. FUNCTION: Precursor protein for pituitary hormones that regulate stress and environmental adaptation. FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the POMC family."}
+{"protein": "MGEQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFSSEHHLSKFAEKFQEFKEAARLAKEKSQEKMELTSTPSQESAGGDLQSPLTPESINGTDDERTPDVTQNSEPRAEPTQNALPFPHSAGDRTQALSHASSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHSHKTELNQTVQELEETLKVKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRSNLKTLLEILDGKIFELTELRDNLAKLLECS", "text": "FUNCTION: Postsynaptic density scaffolding protein. Binds and cross- links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER- associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoform 1 regulates the trafficking and surface expression of GRM5. Differentially regulates the functions of the calcium activated channel ryanodine receptors RYR1 and RYR2. Isoform 1 decreases the activity of RYR2, and increases the activity of RYR1, whereas isoform 5 counteracts the effects by competing for binding sites. Isoform 3 regulates the trafficking and surface expression of GRM5. Isoform 5 acts as a natural dominant negative, in dynamic competition with constitutively expressed isoform 1, isoform 2 and isoform 3 to regulate synaptic metabotropic glutamate function. Isoform 5, may be involved in the structural changes that occur at synapses during long-lasting neuronal plasticity and development (By similarity). Forms a high-order complex with SHANK1, which in turn is necessary for the structural and functional integrity of dendritic spines (By similarity). Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Postsynaptic density Synapse Cell projection, dendritic spine Note=Isoform 1 inhibits surface expression of GRM5 causing it to be retained in the endoplasmic reticulum. The N-terminal of isoform 2 may facilitate trafficking of the complex with GRM5 from the endoplasmic reticulum (ER) to the plasma membrane (PM). SIMILARITY: Belongs to the Homer family."}
+{"protein": "LGPDIVSPPVCGNELLEVGEECDCGTPENCQNE", "text": "FUNCTION: Metalloproteinase moojenin: snake venom metalloproteinase that cleaves both alpha- and beta-chains of fibrinogen, but not the gamma-chain. Shows a coagulant activity on bovine plasma about 3.1 fold lower than crude venom. Renders the blood incoagulable when intraperitoneally administered into mice. Induces necrosis in liver and muscle, but does not cause histological alterations in mouse lungs, kidney or heart. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIb sub-subfamily."}
+{"protein": "MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRTRDMGGYSTTTDFIKSVIGHLQTKGS", "text": "FUNCTION: Plays a structural role to facilitate the assembly and ensure the full activity 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": "MTALNPVLFLLCGVSVSLSLKVVSKRGSVDGCTDWSVDYLKYRVLHGEPVRIKCALFYGYIRANYTQAQSIGLSLMWYRSSGLGHGDFEEPISFDGTRMSKEEDAIWFRPAELQDAGLYSCVLRNSTFCMKVSMTLLVADNDTAGCYNSKLRYTEKGELGKSKDISCPDIQDYVQPGEKPQITWYKECNVQQWRSSVLQTADLLAIQDVREDDIGNYTCELLFGGFLVRRTTYLSVTAPLTEEPPRILFPSENKLLAMDVQLGSMLNLTCRAFFGYSGDISPLVYWMKGEKFIEDMDQSRIRESEIKTVREHLGEQEVSITLTIDSLEEVDLGNYSCYAENGNGRRQANVQIGKRVELMYTVELAGGLGAILLLLALLLSVYKCYRIELLLCYRHHFGGEDTDGDNKEYDAYLSYSKVELDQWGQELQEEERFALEILPDVLEKHYGYKLFIPDRDLIPTSTYIEDVSRCVDMSKRLIIVLTPSYVLRRGWSIFELESRLRNSLVSGDIKVILIECADLRGVINYQEVEELKQSIKCLSVVHWNGPQSNKPGSRFWKQLRYTMPYRRPQQTITNHALDTSEPGPFADLQTVSAISMATATSAALAPAHPELRPSLRSSYRSHSLARQKHSHYRSYDYELPFTAGGTLPPQHTYCNLPLTLLNGQRPVNNKTLRQHSLDEHHGNNAMLPLLPRETSISSVIW", "text": "FUNCTION: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. During presynaptic differentiation may regulate both synaptic vesicle accumulation in axon terminals and subsequent axon terminal remodeling. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cytoplasm Note=May localize to the cell body and growth cones of dendrite-like processes. SIMILARITY: Belongs to the interleukin-1 receptor family."}
+{"protein": "MPSVKETLTLLLSQAFLATGSPVDGETVVKRQCPAIHVFGARETTVSQGYGSSATVVNLVIQAHPGTTSEAIVYPACGGQASCGGISYANSVVNGTNAAAAAINNFHNSCPDTQLVLVGYSQGAQIFDNALCGGGDPGEGITNTAVPLTAGAVSAVKAAIFMGDPRNIHGLPYNVGTCTTQGFDARPAGFVCPSASKIKSYCDAADPYCCTGNDPNVHQGYGQEYGQQALAFINSQLSSGGSQPPGGGPTSTSRPTSTRTGSSPGPTQTHWGQCGGQGWTGPTQCESGTTCQVISQWYSQCL", "text": "FUNCTION: Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family. Acetylxylan esterase subfamily."}
+{"protein": "MAWFSGKVSLGGFPDLTGAVNKFQESVKNIEKNFDNALGFDDKSDSAAEDAASSMWPPAVDTKSLFDPVMSFMGNTSDEKPDTLEDSVRTENPSQIEQKEEEAGSVKLATEQAVSVEANKETNVRREADQADNPEVTETVVLDPKDDEPQSQILLEESSEYSLQTPESSGYKTSLQPNEKLEMTASQDSQPEQPKSEAEESQPEDSEAKEVTVENKDTVHSPVLDGQHKITYMDETTNEQEILGENLEGRTSSKNFEVSPDINHVNRIESPVAHPSLIFESDGSPYESSIPKRSSSDEISERIVDFVSREIDSRLDTSELNESQRSSSATNVSDSADVILELEKTKKEIKMLENALQGAARQAQAKADEIAKLMHENEQLKSVTEDLKRKSNEAEVESLREEYHQRVATLERKVYALTKERDTLRREQNKKSDAAALLKEKDEIINQVMAEGEELSKKQAAQEAQIRKLRAQIREAEEEKKGLITKLQSEENKVESIKRDKTATEKLLQETIEKHQAELTSQKDYYSNALAAAKEAQALAEERTNNEARSELENRLKEAGERESMLVQALEELRQTLSKKEQQAVYREDMFRGEIEDLQRRYQASERRCEELITQVPESTRPLLRQIEAMQETSYRTAEAWAAVERTLNSRLQEAESKAATAEERERSVNERLSQTLSRINVLEAQLSCLRAEQGQLSKSLEKERQRAAENRQEYLAAKEEADTLEGRANQLEVEIRELRRKHKQELQEVLLHNELIQKDLEREKASRLDLERTARINSSAVSEQLPIARQNSAFENGSLPRKLSSASSLGSMEESYFLQASLDSSDKFSEKRSMPEATMSPYYMKSITPSAYEATLRQKEGELASYMTRLASMESIRDSLAEELVKMTAECEKLRGEADRVPGIKAELEALRQRHAAALELMGERDEELEELRADIVDLKEMYREQVNMLVNKIQ", "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 Cytoplasm Note=May be located to the trans-Golgi or trans-Golgi network (TGN)."}
+{"protein": "MAGEHIKVIYFDGRGRAESIRMTLVAAGVDYEDERISFQDWPKIKPTIPGGRLPAVKVTDDHGHVKWMLESLAIARYMAKKHHMMGETDEEYYSVEKLIGQAEDVEHEYHKTLMKPQEEKEKITKEILNGKVPVLLNMICESLKGSTGKLAVGDKVTLADLVLIAVIDHVTDLDKGFLTGKYPEIHKHRENLLASSPRLAKYLSNRPATPF", "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": "MAAAATMAAAARELVLRAGASDVEEEEGPLGGGSGLQEPLQLGELDITSDEFILDEVDVHIQANLEDELVKEALKTGVDLRHYSKQVELELQQIEQKSIRDYIQESENIASLHNQITACDAVLERMEQMLGAFQSDLSSISSEIRTLQEQSGAMNIRLRNRQAVRGKLGELVDGLVVPSALVTAILEAPVTEPRFLEQLQELDAKAAAVREQEAMGTAACADVRGVLDRLRVKAVTKIREFILQKIYSFRKPMTNYQIPQAALLKYRFFYQFLLGNERATAKEIRDEYVETLSKIYLSYYRSYVGRLMKVQYEEVAEKDDLMGVEDTAKKGFFSKPSLRSRNTIFTLGTRGTVISPAELEAPILVPHTAQRGEQRYPFEALFRSQHYALLDNSCREYLFICEFFIVSGPAAHDLFHAVMGRTLSMTLKHLESYLADCYDAIAVFLCIHIVLRFRNIAAKRDVPALDRYWEQVLALLWPRFELILEMNVQSVRSTDPQRLGGLDTRPHYITRRYAEFSSALVSINQTIPNERTLQLLGQLQVEVENFVLRVAAEFSSRKEQLVFLINNYDMMLGVLMERAADDSKEVESFQQLLNARTQEFIEELLSPPFGGLVAFVKEAEALIERGQAERLRGEEARVTQLIRGFGSSWKASVESLSQDVMRSFTNFRNGTSIIQGALTQLIQLYHRFHRVLSQPQLRALPARAELINIHHLMVELKKHKPNF", "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 VPS52 family."}
+{"protein": "MAPTKTIKNKHAANKSGIKGSKDAERSRNDGVLKSKGKPKGKAHTLVTASKGRPNIQELIARKKKKKTYSEKELAIPELNMITPVGVTKPKGKKKGKVFVDDKESMATILAIVQAEKEGQIESKMIKARQMEEIREARRAEAEKKEAERKARLEETKDSLRKKRKRSKQSGGSKGDDDDDSRDVKEFSSAGTKAVKSKKKKSVSFAAPE", "text": "FUNCTION: Required for efficient assembly and nuclear export of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the LOC1 family."}
+{"protein": "MKKQALICALLATVLLPGCSEDGENTPQPTDGRVALEATSGIRMNTRAYDKTWEAGDAIGIYMLNGDATDGNGNRKYTTAQTAENGSFTAAEGQTIYFPVDASQRDFVAYYPYRETLADGNVYTVDVSVQTPQKDIDLMGAAKVEGKDKTDPKVAFVFTHKLVKLDITIKADGTSLTDADLAGTTVSISNQQTAATYNVVTGGDATVTTGTTKEIVLHTDGLKAEGIVLPAASTAGMALTFTVPGLEGQAFHWDVNSAAQSKAFVAGSKYLYTITISKAGVEVSSKVEDWTPGNGGGETGNAE", "text": "FUNCTION: Putative component of the fimbrium tip. Fimbriae are filamentous appendages on the cell surface that mediate cell adhesion and biofilm formation. SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily. Mfa- like family."}
+{"protein": "MKHLPKHVRPRWRYLAVGIEAWPDAGIERSDFQRALWFAAGNLLGDPGSADAGVRVVAYSFRDGRGEALVRARRGTVSRARAAVACVSAVREHPVRVCVRGVSGTMRAARERYLDGLDTPERRSDVAFDGDARDGVCRGENVDVVAGDDGWVGARRRDCGTDGE", "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": "MNKATANERKKLRLLLVASRKHLSRGDLRSLIRFLESEDCGFEIKLQFSDPKEQPELLELHRLVAIPALIKLDPQPKQIFAGTSILEQLKNWLPRWEQEDILISSGLGINLRQKESENGRTRNELLLEDENLVLRQENETLSNQIESQERLLRMVAHELRTPLSAAKLALQSQALGQIDLIKLQEVVKRRLEEIESLSKDLLEVGTTRWEALFNPQEANLANIAAEVILELEKFWLSRGIGINTDIPADLPNVFADQSRMKQVLLNLIENALKFSNDGDTVEITMLHRTNQWVQISVSDKGPGIPEEEQQRIFLDRVRLPQTSNETSGFGIGLSVCRRIVEVHGGKIWVVSQPGEGSCFYFTVPVWDKRNKSLEPLTLTQG", "text": "FUNCTION: Member of the two-component regulatory system SasA/RpaA involved in genome-wide circadian gene expression. One of several clock output pathways. Participates in the Kai clock protein complex, the main circadian regulator in cyanobacteria, via its interaction with KaiC. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. In addition to its output function, recruits fold-shifted KaiB (KaiB(fs)) to KaiC to cooperatively form the KaiB(6):KaiC(6) complex (independent of SasA kinase activity). Required for robustness of the circadian rhythm of gene expression and is involved in clock output, also required for adaptation to light/dark cycles."}
+{"protein": "MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFGMPMLDLDDDDDREESLMMNRLANVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPPERPPPIPPDNRLSRHIHHVESVPSRDPPMPLEAWCPRDVFGTNQLVGCRLLGEGSPKPGITASSNVNGRHSRVGSDPVLMRKHRRHDLPLEGAKVFSNGHLGSEEYDVPPRLSPPPPVTTLLPSIKCTGPLANSLSEKTRDPVEEDDDEYKIPSSHPVSLNSQPSHCHNVKPPVRSCDNGHCMLNGTHGPSSEKKSNIPDLSIYLKGDVFDSASDPVPLPPARPPTRDNPKHGSSLNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFVDLASGQVPLPPARRLPGENVKTNRTSQDYDQLPSCSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Upon EGF stimulation, associates with endocytic vesicles."}
+{"protein": "MAQGSGDQRAVGVADPEESSPNMIVYCKIEDIITKMQDDKTGGVPIRTVKSFLSKIPSVVTGTDIVQWLMKNLSIEDPVEAIHLGSLIAAQGYIFPISDHVLTMKDDGTFYRFQAPYFWPSNCWEPENTDYAIYLCKRTMQNKARLELADYEAENLARLQRAFARKWEFIFMQAEAQVKIDRKKDKTERKILDSQERAFWDVHRPVPGCVNTTEMDIRKCRRLKNPQKVKKSVYGVTEESQAQSPVHVLSQPIRKTTKEDIRKQITFLNAQIDRHCLKMSKVAESLIAYTEQYVEYDPLITPAEPSNPWISDDVALWDIEMSKEPSQQRVKRWGFSFDEILKDQVGRDQFLRFLESEFSSENLRFWLAVQDLKKQPLQDVAKRVEEIWQEFLAPGAPSAINLDSHSYEITSQNVKDGGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLLLAKKKGKSLAGKRLTGLMQSS", "text": "FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP- bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity (PubMed:10521509). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytosol Membrane; Peripheral membrane protein Nucleus Cell membrane Note=Interaction with GNB5 mediates translocation to the nucleus."}
+{"protein": "MDILGEIVNVDEYVEKLELQKNDIGFYKCPFCDYTNADAKVVRKHVKSKHLEEIEKELKKLESQKSKNNGKKQTGQKKQGKGKKQPKRVRETCVSTQERKDYVLFFCHNHKVRLHLANGEVLEGKCCCKDPYTVLVDVGKGDVVIVNKAYIVKYVPLDLEKL", "text": "SIMILARITY: To M.jannaschii MJECS06."}
+{"protein": "MSREVYICDAVRTPIGRFGGSLAAVRADDLAAVPVKALVERNPQVDWSQLDEVYLGCANQAGEDNRNVARMALLLAGLPDSVPGVTLNRLCASGMDAVGTAFRAIASGEAELVIAGGVESMSRAPYVMGKADSAFGRGQKIEDTTIGWRFINPLMKAQYGVDAMPETADNVADDYKVSRADQDAFALRSQQLAGRAQAAGYFAEEIVPVVIKGKKGETVVDADEHLRPDTTLEALAKLKPVNGPDKTVTAGNASGVNDGSVALILASAEAVKKHGLKARAKVLGMASAGVAPRVMGIGPVPAVRKLLERLNLSVADFDVIELNEAFAAQGLAVTRELGIADDDARVNPNGGAIALGHPLGASGARLVLTAVHQLEKSGGQRGLCTMCVGVGQGVALAVERV", "text": "FUNCTION: Catalyzes thiolytic cleavage of beta-ketoadipyl-CoA to succinyl-CoA and acetyl-CoA. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
+{"protein": "MAKKMKLSEITNMFAGMNVEALEGVTIEGDIEIDLGGLGGFDPMLAAALGQESAVLAQHFARIAGMFGYPVSVGAPAAAPAAVSPALAAPKLKDLIPAKFEFSNIEEWTTQVEEVPIGNTSADGGSRGKRILLGGEKALPFFPDAPMPNRNQVTIDVFDMRLGLAKAVKENYDDVMDNPGEWAKKNVEKFNADMITIHLISTDPLIKDTSPKDAAKTVEEVLQAVDVPIAIGGSGNPQKDPLVLAKAAEVAEGERCLLASASLNLDYAAIAEAALKYDHDVLSWTQLDMNAQKELNRKLMKQCNVPRDRIIMDPTTAALGYGLDYAYTNMERIRLAALMGDDELTFPMSSGTTNAWGARESWMVSSPLKEDSDWGPREYRGPIWEIITGLSLAIAGNDLFMMMHPTSVAVLKHMTQTLFGSIEAEPVDIANWIGAEV", "text": "FUNCTION: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. Probably maintains the overall quaternary structure of the ACDS complex (By similarity). SIMILARITY: Belongs to the CdhD family."}
+{"protein": "MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQELARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCVIM", "text": "FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays an important role in the regulation of cell proliferation (PubMed:3110778). 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 (By similarity). FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays an important role in the regulation of cell proliferation (PubMed:6474169, PubMed:1352876). 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 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Endomembrane system Cytoplasm, cytosol. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Endomembrane system Cytoplasm. SUBCELLULAR LOCATION: [Isoform 2B]: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MRHSLTKLLAASGSNSPTRSESPEPAATCSLPSDLTRAAAGEEETAAAGSPGRKQQFGDEGELEAGRGSRGGVAVRAPSPEEMEEEAIASLPGEETEDMDFLSGLELADLLDPRQPDWHLDPGLSSPGPLSSSGGGSDSGGLWRGDDDDEAAAAEMQRFSDLLQRLLNGIGGCSSSSDSGSAEKRRRKSPGGGGGGGSGNDNNQAATKSPRKAAAAAARLNRLKKKEYVMGLESRVRGLAAENQELRAENRELGKRVQALQEESRYLRAVLANETGLARLLSRLSGVGLRLTTSLFRDSPAGDHDYALPVGKQKQDLLEEDDSAGGVCLHVDKDKVSVEFCSACARKASSSLKM", "text": "FUNCTION: Strongly activates transcription when bound to HCFC1. Suppresses the expression of HSV proteins in cells infected with the virus in a HCFC1-dependent manner. Also suppresses the HCFC1-dependent transcriptional activation by CREB3 and reduces the amount of CREB3 in the cell. Able to down-regulate expression of some cellular genes in CREBZF-expressing cells. SUBCELLULAR LOCATION: Nucleus Note=Colocalizes in promyelocytic leukemia protein nuclear bodies (PML- NB) with CREB3 and HCFC1. SIMILARITY: Belongs to the bZIP family. ATF subfamily."}
+{"protein": "MGFGSDLKNSQEAVLKLQDWELRLLETVKKFMALRIKSDKEYAYTLQNLCNQVDKESTVQVNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYVGIHQQIEAEMIKVTKTELEKLKSSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQSQYYDTTLPLLLDSVQKMQEEMIKALKGIFDDYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTADSLQVMLKTLAEELTQTQQMLLHKEAAVLELEKRIEESFETCEKKSDIVLLLGQKQALEELKQSVQQLRCTEAKCAAQKALLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIKSPKSVLGSSTQVCDVISVGERPLAEHDWYHGAIPRIEAQELLKQQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQFVDNLYRFEGTGFSNIPQLIDHHFNTKQVITKKSGVVLLNPIPKDKKWVLNHEDVSLGELLGKGNFGEVYKGTLKDKTPVAIKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVPGGDFLTFLRKRKDELKLKQLVRFSLDVAAGMLYLESKNCIHRDLAARNCLVGENNTLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQNCPEEVFTIMMKCWDYKPENRPKFNDLHKELTVIKKMIT", "text": "FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF- kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according to PubMed:10878010 and PubMed:19159681, but clearly plays a redundant role in STAT3 phosphorylation. According to PubMed:11134346, cells where wild type FER has been replaced by a kinase-dead mutant show no reduction in STAT3 phosphorylation. Phosphorylates TMF1. Isoform 3 lacks kinase activity. SUBCELLULAR LOCATION: [Isoform 4]: Nucleus. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell projection Cell junction Membrane; Peripheral membrane protein; Cytoplasmic side Nucleus. Cytoplasm, cell cortex Note=Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts (By similarity). Not detected in the nucleus, but detected in the nuclear area surrounding the chromosomes after breakdown of the nuclear envelope during mitosis (PubMed:11339827). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily."}
+{"protein": "MIIYREENEIIKKALENLNIPDRVYIFDTTLRDGEQTPGVSLTPEEKIDIAIKLDDLGVDVIEAGFPVSSLGEQEAIKKICSLNLDAEICGLARAVKKDIDVAIDCGVDRIHTFIATSPLHRKYKLKKSKEEIIDIAVDAIEYIKEHGIRVEFSAEDATRTEIDYLIEVYKKAVDAGADIINVPDTVGVMIPRAMYYLINELKKEIKVPISVHCHNDFGLAVANSLAAVEAGAEQVHCTINGLGERGGNAALEEVVMSLMSIYGVKTNIKTQKLYEISQLVSKYTEIKVQPNKAIVGENAFAHESGIHAHGVLAHALTYEPIPPELVGQKRKIILGKHTGTHAIEAKLKELGIEVGKDINKDQFDEIVKRIKALGDKGKRVTDRDVEAIVEDVVGKLAKKDRVVELEQIAVMTGNRVIPTASVALKIEEEIKKSSAIGVGPVDAAVKAIQKAIGEKIKLKEYHINAITGGTDALAEVIVTLEGYGREITTKAASEDIVRASVEAVIDGINKILAKREK", "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). SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family."}
+{"protein": "MVRLFYNPIKYLFYRRSCKKRLRKALKKLNFYHPPKECCQIYRLLENAPGGTYFITENMTNELIMIAKDPVDKKIKSVKLYLTGNYIKINQHYYINIYMYLMRYNQIYKYPLICFSKYSKIL", "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": "MAARAVLDEFTAPAEKAELLEQSRGRIEGLFGVSLAVLGALGAEEPLPARIWLQLCGAQEAVHSAKEYIKGICEPELEERECYPKDMHCIFVGAESLFLKSLIQDTCADLCILDIGLLGIRGSAEAVVMARSHIQQFVKLFENKENLPSSQKESEVKREFKQFVEAHADNYTMDLLILPTSLKKELLTLTQGEENLFETGDDEVIEMRDSQQTEFTQNAATGLNISRDETVLQEEARNKAGTPVSELTKQMDTVLSSSPDVLFDPINGLTPDEEALSNERICQKRRFSDSEERHTKKQFSLENVQEGEILHDAKTLAGNVIADLSDSSADSENLSPDIKETTEEMEYNILVNFFKTMGYSQEIVEKVIKVYGPSTEPLLLLEEIEKENKRFQEDREFSAGTVYPETNKTKNKGVYSSTNELTTDSTPKKTQAHTQQNMVEKFSQLPFKVEAKPCTSNCRINTFRTVPIEQKHEVWGSNQNYICNTDPETDGLSPSVASPSPKEVNFVSRGASSHQPRVPLFPENGLHQQPEPLLPNNMKSACEKRLGCCSSPHSKPNCSTLSPPMPLPQLLPSVTDARSAGPSDHIDSSVTGVQRFRDTLKIPYKLELKNEPGRTDLKHIVIDGSNVAITHGLKKFFSCRGIAIAVEYFWKLGNRNITVFVPQWRTRRDPNVTEQHFLTQLQELGILSLTPARMVFGERIASHDDRFLLHLADKTGGIIVTNDNFREFVNESVSWREIITKRLLQYTFVGDIFMVPDDPLGRSGPRLEEFLQKEVCLRDMQPLLSALPNVGMFDPSFRVPGTQAASTSHQPPTRIQGAPSSHWLPQQPHFPLLPALPSLQQNLPMPAQRSSAETNELREALLKIFPDSEQRLKIDQILVAHPYMKDLNALSAMVLD", "text": "FUNCTION: Potent suppressor of cytokine production that acts as a regulator of innate immune signaling and inflammation. Acts as a key negative regulator of select cytokine and chemokine responses elicited by TRIF-independent Toll-like receptors (TLRs), thereby limiting inflammatory cytokine responses to minor insults. In response to more threatening pathogens, cleaved by CASP8 downstream of TLR3 or TLR4, leading to its inactivation, thereby allowing production of inflammatory cytokines (By similarity). Acts as a restriction factor against some viruses, such as HIV-1: restricts HIV-1 replication by binding to HIV-1 mRNAs and mediating their degradation via its ribonuclease activity (PubMed:31133753). Also acts as an inhibitor of the E3 ubiquitin-protein ligase ITCH: acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Nucleus, nucleolus Nucleus, PML body Note=Primarily localizes to the nucleolus. Also localizes to the PML nuclear bodies, when desumoylated. SIMILARITY: Belongs to the N4BP1 family."}
+{"protein": "MTAASTTATTMLQATQSDVLQEIQSNFLLNSSIWVNIALAGVVILLFVAMGRDIESPRAKLIWVATMLVPLVSISSYAGLASGLTVGFLQMPPGHALAGQEVLSPWGRYLTWTFSTPMILLALGLLADTDIASLFTAITMDIGMCVTGLAAALITSSHLLRWVFYGISCAFFVAVLYVLLVQWPADAEAAGTSEIFGTLKILTVVLWLGYPILWALGSEGVALLSVGVTSWGYSGLDILAKYVFAFLLLRWVAANEGAVSGSGMSIGSGGAAPADD", "text": "FUNCTION: Light-driven chloride pump. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family."}
+{"protein": "MKVEYHTVYLKKRFPLRISRGVFEGSDNLYISLTENGHTGWGEMAPGGTEGAETAAAGQAMLEQFCATGLSASIHDTWQNAHAAGVAPCALAALDMALWDLRAKQAGVPLYALLGLARRAVVSSVTVGINPPDVVRERVPLLLARGARALKIKLGSPEGIEADQAMFAAVFEAAQGSGAVLRVDANGGWSLKDARRMMGWLAEHDVEYIEQPLVRGAEDQLPDLFKDRAMPIFVDESCRMSGDIATFFQSVDGVNLKLMKCGGITEALRIVATARAFGLKTMIGCMGESSVSIAAGASIGALFDYIDLDSHLNLDPDPATGAPFENGITLPADQPGHGGVLSHA", "text": "FUNCTION: Dipeptide epimerase with a preference for hydrophobic substrates. Catalyzes the epimerization of L-Ala-L-Thr, L-Ala-L-Met, L- Ala-L-His, L-Ala-L-Phe, L-Ala-L-Tyr, L-Ala-L-Trp, L-Ile-L-Ala, L-Ile-L- Ser, L-Ile-L-Met, L-Ile-L-His, L-Ile-L-Phe, L-Ile-L-Tyr, L-Ile-L-Trp, L-Phe-L-Met, L-Phe-L-His, L-Phe-L-Phe, L-Phe-L-Tyr, L-Phe-L-Trp, L-Phe- L-Ser, L-Phe-L-Thr and L-Phe-L-Lys (in vitro). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family."}
+{"protein": "MARAPAQARGSRGLNCLARSQQTGIPAQETDDLFSTCYCEETEEDTAHQEAGMTVDCLSIPKKKLAQSQKKINQFINSKMSTKANKELIRCFILSQIVFGKEHWKCAQALANLAYGYLTLRGLPAQAKKHAEKARNTLLTWKRNTTSDKDKKEILETLVRLYYTLGVAWLLQNHGKQAYIHLQKAERNMKELKELNNGNICGIQVSEKDLTIALGRASLAMHRMNLALAYFEKAICDVILDKGHNTSELISLYEEIAQIEQLRKNHKQAIQYLQQAYSICVSSFSEVSPQTAEASALLAKAYAMSGASEYRDAVEIYFIRSISTYQTLGSEDYETLTAIEDFCTWLIENGEKQEAYRLLKSTLNSGNFGDCGKKVAETFYNMGSICFAKGELGEAIELLSKCLMIQSLVYGSEHIKSIETKSLLSLLQRWRLKETLEKNRKEASGGETFQKTVITLLQ", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Midbody Note=Exhibits dynamic subcellular localization during the cell cycle. In prophase cells, detected on split centrosomes. Translocates to the mitotic spindles during metaphase and early anaphase, then to the midbody and cleavage furrow in late anaphase."}
+{"protein": "MTEPGNLQPTFVGFIGTTVDALLLFEACRQNYTHFVDRRPQDRERERLIRSGSVFVFDEVQSGIKRWTDGIAWSPSRVIGNFLVYRQLCKKNSVSDRKRSSKSRSDSDEEEVSAFTVSVPVDVDVASHVNISSPSAPSLSDNLFPGSSFSASSQQNPSSPGSNDIKSEFAAVKNEYVLSPTSPTTSAAFPSSFSSLPLVSSKPTGTPFVPKSPPSSSPSTTNVSNASTSSAPINPRAPQTRRESISSTSSIHYCSSSSLSYLHDTERALVGSLTDSYGFKKSGLIKKTISLMIDGRLHHLISYYTPEDVLNGKLQTPSSFNLFQQLTISKDLLEYKSFRIPPLVEAAESEKISQLSTLEKRTLPSFPYNPFFSSSTAEIDPYHFQGLTLSTSPISGVESSSLSSAISRNQSNLSSFQQQQQFSALQSISNNALNENIEQPPIKMAARHSYPNFLQTLPQYMNDVYNPSGLAFNPVNPNANNSFVNLNLIQFTSPSQALFDYGEGPYVDQKSQYLQPKQPSSNTDSIDQSSYNMSLAASKQFLTSDTQPDVNENYSFISNSIPKNLSTSWNQNMGYHVTNSNSELASQNPLYAQQAVSMESMGNAIQSSAYSAMSTPHGGHYDHYAATAKGKNPLAAENHASGGRLPKVPIPPLSNMRRGSVPIIPSSASLPMRTSGNRFCHYSSLNGNHNRISARTNPYPINNQTMLFTEPLSKERGSLS", "text": "FUNCTION: Promotes the onset of gluconate uptake upon glucose starvation. SIMILARITY: To S.pombe pac2 in the N-terminal region."}
+{"protein": "MIEEEIEVDVDIKTRADKFHKFIRRSQHVPKATHYIKGCDLLEGEWGKVGSILLWKLVFDGEPRVSKDMIEVIDEEKNVIQLRVLEGPLKKEYKSFLKTMKVMSPKHGGPGSVVKWNMKYERIDQNVDHPNRLLQFFVEVTKEIDQYLLSKD", "text": "SIMILARITY: Belongs to the MLP family."}
+{"protein": "MSSIIRKVISTSKAPAAIGAYSQAVLVDRTIYVSGQIGMDPSSGQLVPGGVAEEAKQALKNLGEILKAAGCDFTNVVKTTVLLADINDFGTVNEIYKTYFQGNLPARAAYQVAALPKGSRIEIEAIAVQGPFTTAGL", "text": "FUNCTION: Also promotes endoribonucleolytic cleavage of some transcripts by promoting recruitment of the ribonuclease P/MRP complex (PubMed:10400702). Acts by bridging YTHDF2 and the ribonuclease P/MRP complex (By similarity). RIDA/HRSP12 binds to N6-methyladenosine (m6A)- containing mRNAs containing a 5'-GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such transcripts lead to recruitment of the ribonuclease P/MRP complex and subsequent endoribonucleolytic cleavage (By similarity). FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'- phosphate-dependent dehydratases including L-threonine dehydratase. SUBCELLULAR LOCATION: Cytoplasm Nucleus Peroxisome Mitochondrion Note=Mostly cytoplasmic but, in less differentiated cells occasionally nuclear. SIMILARITY: Belongs to the RutC family."}
+{"protein": "MTKRKLRNNWIIVTTMITFVTIFLFCLIIIFFLKDTLHNSELDDAERSSSDINNLFHSKPVKDISALDLNASLGNFQEIIIYDEHNNKLFETSNDNTVRVEPGYEHRYFDRVIKKRYKGIDYLIIKEPITTQDFKGYSLLIHSLENYDNIVKSLYIIALAFGVIATIITATISYVFSTQITKPLVSLSNKMIEIRRDGFQNKLQLNTNYEEIDNLANTFNEMMSQIEESFNQQRQFVEDASHELRTPLQIIQGHLNLIQRWGKKDPAVLEESLNISIEEMNRIIKLVEELLELTKGDVNDISSEAQTVHINDEIRSRIHSLKQLHPDYQFDTDLTSKNLEIKMKPHQFEQLFLIFIDNAIKYDVKNKKIKVKTRLKNKQKIIEITDHGIGIPEEDQDFIFDRFYRVDKSRSRSQGGNGLGLSIAQKIIQLNGGSIKIKSEINKGTTFKIIF", "text": "FUNCTION: Member of the two-component regulatory system ArlS/ArlR involved in the regulation of adhesion, autolysis, multidrug resistance and virulence. ArlS probably functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to ArlR (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MTFAKIKFSAQIRLETGLHIGGSDAFAAIGAIDSPVIKDPITNIPIIPGSSLKGKMRTLLAKVYNEKVAEKPSDDSDILSRLFGNSKDKRFKMGRLIFRDAFLSNADELDSLGVRSYTEVKFENTIDRITAEANPRQIERAIRNSTFDFELIYEITDENENQVEEDFKVIRDGLKLLELDYLGGSGSRGYGKVAFEKLKATTVFGNYDVKTLNELLTAEV", "text": "FUNCTION: Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity; target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. FUNCTION: This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals. The number of cleavage sites in the target RNA correlates with the number of Csm3 subunits in the Csm effector complex (PubMed:25458845). In the Csm complex target RNA and ssDNA are cleaved simultaneously, although RNase activity (of Csm3) is much faster. RNA cleavage by Csm3 is not required for ssDNase activity as Csm complex with inactive Csm3 still has ssDNase activity; however as the cleaved target RNA products dissociate away ssDNase activity decreases (PubMed:27105119). 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. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. SIMILARITY: Belongs to the CRISPR-associated Csm3 family."}
+{"protein": "MEFDLGEYFRAAFEDKLLVKMPDREDDFLTPATRLLEKRREMVEVEQALSTQKEEFQMKSESLQQRRAELELKEEKLKDSLFKFDKFLKENDSKRKRALHKAAEERQLAAHKEREALRLQAENTQLMQRKGTLLERQEKNSKYQQYLQRVLERTDEFQEVQEMIDRFNTLMATQNKLLKRDLENQELAEREKARLLHYQEETRSQILELNNQIAQLQGELERVRAVAFQWESRWAQIQNTAAENTLRLGRIRMSTLNLFQTISKQMRLKTEISVEDTEAQLEKIQICFEDLSAIYKDLKKAGTTPQTPAVPTTN", "text": "SIMILARITY: Belongs to the CFAP73 family."}
+{"protein": "MLKEYLGISLFLAAGLIIPFLAFAVSRLLQTRKNSLVKGEPYECGMETIGDTWIQFKSNYFLYALVFVAFDVETVFLYPWAVKFQQLGTFAIVEMFIFITILVVGFWYAWKEGALEWK", "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": "MRVPQHYKKPGWQRFFAGMMCGAVISWFFFLFTYGTFQEEQVSLIEKQKEHVKDLNNQISIYQEDLHKLNEDNKRKLLIQSVSVKLLNGDKYKISQPDKTKFEEHVKDDISEVITKDIESVYQTKDLLKRTIENKVYMINEKKYEATVRELIIYTRLTVELEISFAT", "text": "FUNCTION: Involved in sporulation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
+{"protein": "MASGFKKPSAASTGQKRKVAPKPELTEDQKQEVREAFDLFDVDGSGTIDAKELKVAMRALGFEPRKEEMKKMISEVDREGTGKISFNDFLAVMTQKMSEKDTKEEILKAFRLFDDDETGKISFKNLKRVANELGENLTDEELQEMIDEADRDGDGEVNEEEFLRIMKKTSLY", "text": "FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function (PubMed:8175926). Plays a role in sperm cilia formation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium Note=Centrosome of interphase and mitotic cells. In the retinal photoreceptor cells, localizes at the connecting cilium, a thin bridge linking the cell body and the light- sensing outer segment (By similarity). SIMILARITY: Belongs to the centrin family."}
+{"protein": "MKWLVGLLPLCSYAVAQVHKDPTLDHHWNLWKKTYSKQYKEENEEVARRLIWEKNLKFVMLHNLEHSMGMHSYDLGMNHLGDMTGEEVISLMGSLRVPSQWQRNVTYRSNSNQKLPDSVDWREKGCVTEVKYQGSCGACWAFSAVGALEAQLKLKTGKLVSLSAQNLVDCSTEKYGNKGCNGGFMTTAFQYIIDNNGIDSEASYPYKAMNGKCRYDSKKRAATCSKYTELPFGSEDALKEAVANKGPVSVAIDASHYSFFLYRSGVYYEPSCTQNVNHGVLVVGYGNLNGKDYWLVKNSWGLNFGDQGYIRMARNSGNHCGIASYPSYPEI", "text": "FUNCTION: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L. SUBCELLULAR LOCATION: Lysosome Secreted Cytoplasmic vesicle, phagosome. SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MAAPMTPAARPEDYEAALNAALADVPELARLLEIDPYLKPYAVDFQRRYKQFSQILKNIGENEGGIDKFSRGYESFGVHRCADGGLYCKEWAPGAEGVFLTGDFNGWNPFSYPYKKLDYGKWELYIPPKQNKSVLVPHGSKLKVVITSKSGEILYRISPWAKYVVREGDNVNYDWIHWDPEHSYEFKHSRPKKPRSLRIYESHVGISSHEGKVASYKHFTCNVLPRIKGLGYNCIQLMAIMEHAYYASFGYQITSFFAASSRYGTPEELQELVDTAHSMGIIVLLDVVHSHASKNSADGLNMFDGTDSCYFHSGPRGTHDLWDSRLFAYSSWEILRFLLSNIRWWLEEYRFDGFRFDGVTSMLYHHHGVGQGFSGDYSEYFGLQVDEDALTYLMLANHLVHTLCPDSITIAEDVSGMPALCSPISQGGGGFDYRLAMAIPDKWIQLLKEFKDEDWNMGDIVYTLTNRRYLEKCIAYAESHDQALVGDKSLAFWLMDAEMYTNMSVLTPFTPVIDRGIQLHKMIRLITHGLGGEGYLNFMGNEFGHPEWLDFPRKGNNESYHYARRQFHLTDDDLLRYKFLNNFDRDMNRLEERYGWLAAPQAYVSEKHEGNKIIAFERAGLLFIFNFHPSKSYTDYRVGTALPGKFKIVLDSDAAEYGGHQRLDHSTDFFSEAFEHNGRPYSLLVYIPSRVALILQNVDLPN", "text": "FUNCTION: Required for normal glycogen accumulation (PubMed:8463281, PubMed:26199317, PubMed:8613547). The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule (Probable). SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB subfamily."}
+{"protein": "MYTYMEYLQKCFYKSTNWNEDNIFSNITATSQAILEFPIPNGFKIDSSSKTTDYSASSFTLSNNHQINGSLAYLYSSVPLKNTMGTKDVSLQDAIAGFRIIEPMVRLQPKFNNKAPHSKSSLLYGRMYFPGSALEAMIIKRISENTQLLIKCVNNPHLSKNGTMIVYLQNNTAKYSREFIYSTNESLIGLRCLYNLGTPTSSSTVSSFNPRTIPKFDNSVVSIGTELWFATRSMSPGLSGALRYSTRSTSTGKPLTMTLAINPILGHISSTYTVKTSVASTFCSRYDFNVFSYASNLSLGFELYSYANKKRSDFYNHEIYSSSEENKYLKQHPELQKHHRVPIRAYKHHDNRTIINPIHNLDNVYHINPTLLSTTSGSGHTSETVTTAFQNLVNESDFSSVLKFSTSLNDKVVKILWEGRLRDFLVSTGVKLSLNPVTNTPEFNKLGISFSYAL", "text": "FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria. 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 MDM10 family."}
+{"protein": "LSHCVPERKRGRQTYTRYQTLELEKEFHYNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKENARATGTP", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family."}
+{"protein": "MLAKITRSSFYASRAVGRLSGSIPTSPAALASNCRYIQIERKRTKSHEMALYETVEKGAKNSPSYSLYFKNKCGNVISPMHDIPLYANEEKTIYNMVVEVPRWTNAKMEISLKTPMNPIKQDIKKGKLRFVANCFPHKGYIWNYGALPQTWENPDHIEPSTGCKGDNDPIDVIEIGYRVAKRGDVLKVKVLGTIALIDEGETDWKIIAIDVNDPLASKVNDIADVDQYFPGLLRATVEWFKIYKIPDGKPENQFAFNGDAKNADFANTIIAETHKFWQNLVHQSPASGSISTTNITNRNSEHVIPKEEAEKILAEAPDGGQVEEVSDTVDTWHFIHLK", "text": "FUNCTION: Component of NURF (nucleosome remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin (PubMed:9784495). NURF is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis (PubMed:9784495, PubMed:8521501). Inorganic pyrophosphatase (PPase), hydrolyzes inorganic pyrophosphate to inorganic phosphate, essential for driving critical biosynthetic reactions including transcription, replication, and DNA repair (PubMed:9784495). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the PPase family."}
+{"protein": "MAAGTAAALAFLSQESRTRAGGVGGLRVPAPVTMDSFFFGCELSGHTRSFTFKVEEEDDAEHVLALTMLCLTEGAKDECNVVEVVARNHDHQEIAVPVANLKLSCQPMLSLDDFQLQPPVTFRLKSGSGPVRITGRHQIVTMSNDVSEEESEEEEEEEDSDEEEAELCPILPAKKQGGRP", "text": "FUNCTION: Plays a role in the regulation of diverse cellular processes such as ribosome biogenesis, chromatin remodeling or protein chaperoning. Modulates the histone chaperone function and the RNA- binding activity of nucleolar phosphoprotein B23/NPM. Efficiently mediates chromatin remodeling when included in a pentamer containing NPM3 and NPM. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Note=Mainly found in the granular component of the nucleolus. SIMILARITY: Belongs to the nucleoplasmin family."}
+{"protein": "MFIESFRVESPHVRYGAAEIESDYQYDTTELVHESHDGASRWIVRPKSVRYNFRTTTTVPKLGVMLVGWGGNNGSTLTAGVIANREGISWATKDKVQQANYYGSLTQASTIRVGSYNGEEIYAPFKSLLPMVNPDDLVFGGWDISNMNLADAMTRAKVLDIDLQKQLRPYMESMVPLPGIYDPDFIAANQGSRANNVIKGTKKEQMEQIIKDIREFKEKSKVDKVVVLWTANTERYSNVCVGLNDTMENLLASVDKNEAEISPSTLYAIACVMEGIPFINGSPQNTFVPGLIDLAIKNNCLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQTFRSKEISKSNVVDDMVSSNAILYELGEHPDHVVVIKYVPYVGDSKRAMDEYTSEIFMGGKSTIVLHNTCEDSLLAAPIILDLVLLAELSTRIQLKAEGEEKFHSFHPVATILSYLTKAPLVPPGTPVVNALAKQRAMLENIMRACVGLAPENNMILEYK", "text": "FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1- phosphate in a NAD-dependent manner (By similarity). Is a key enzyme in the phytic acid biosynthesis pathway in seeds (PubMed:19021878). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family."}
+{"protein": "MKSDKVLDAKGLACPMPIVRTKKAMNELESGQILEVHATDKGAKNDLTAWSKSGGHDLLEQTDEGDILKFWIQKG", "text": "SIMILARITY: Belongs to the sulfur carrier protein TusA family."}
+{"protein": "MSVKTKKFVNKKYTTAKFKVTPTGKCRNKNNESIKKLIFNNGTKINTGLNLLLTQPNQVNIPPPPKILLDRIREERKRMVSSANSDITVIDIELCWEIDKFLAHHFQNTDSSKNDNYTKSNIKKPINAFIAFRAYYSQLGAGIKQNILSSILSEAWNSPETDQNIWDIFAQQFNFASARCGFVNYIMAQASSAP", "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. Transcriptional activator that induces the transcription of alpha- specific genes (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MATALPHA1 family."}
+{"protein": "MVKETEYYDVLGVSPTATESEIKKAYYIKARQVHPDKNPNDPQAAHNFQVLGEAYQVLSDSGQRQAYDACGKSGISTDAIIDPAAIFAMLFGSELFEGYIGQLAMASMASLDIFTEGDQFDTKKIQEKLRIVQKEREDKLAQILKDRLNEYVINKDEFISNAEAEVARLSNAAYGVDMLNTIGYIYVRQAAKELGKKAIYLGVPFIAEWFRNKGHFIKSQLTAATGAYALFQLQEEMKRQLNTEGNYTEEELEEYLQAHKRVMIDSLWKLNVADIEATLCRVCQLVLQDPEAKREELRTRARGLKALGRIFQRAKTASESDPLENSEPQKLNGNGKNHDEDTSTSPKSSEASHSTSGPQEPQSPYVEEFKLGDEQFNYYFPRPAPPPGAGKYSSSGYD", "text": "FUNCTION: Plays a continuous role in plant development probably in the structural organization of compartments. SIMILARITY: Belongs to the DnaJ family. C/III subfamily."}
+{"protein": "MDDFTSISLLSLAMLVGCYVSGIIPLAVNFSEEKLKLVTVLGAGLLCGTALAVIVPEGVHALYEEALEAKHHEMGEIHKVKDAETGAEASVAHEHDHSNLHAYIGVSLVLGFVFMLLVDQIGSSHMHSADDPEAARAASSKITTTLGLVVHAAADGVALGAAASTSQTSVQLIVFVAIMLHKAPAAFGLVSFLMHAGLERNRIRKHLLVFALAAPLLSMLTYLGLSKSSKEALSEVNATGVAMLFSAGTFLYVATVHVLPEVGGMGHSHKQDLGAAKGLSRLEVCALVLGCLIPLVLSIGHQH", "text": "FUNCTION: Transports zinc ions across cell and organelle membranes into the cytoplasm and regulates intracellular zinc homeostasis. Participates in the zinc ions efflux out of the secretory compartments. Regulates intracellular zinc level, resulting in the enhancement of AKT1 and MAPK3/MAPK1 (Erk1/2) phosphorylation in response to the BCR activation (By similarity). Also functions as membrane androgen receptor that mediates, through a G protein, the non-classical androgen signaling pathway, characterized by the activation of MAPK3/MAPK1 (Erk1/2) and transcription factors CREB1 or ATF1 (By similarity). Moreover, has dual functions as membrane-bound androgen receptor and as an androgen-dependent zinc transporter both of which are mediated through an inhibitory G protein (Gi) that mediates both MAP kinase and zinc signaling leading to the androgen-dependent apoptotic process (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane Cell membrane; Multi-pass membrane protein Cytoplasm, perinuclear region Mitochondrion Nucleus. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
+{"protein": "MKTLNFCLFLVIISSLTVRVFCLNDRFLTVNDNYVICLYINKSFVNCENLCKAYMNAKDGFCRQPHCFCTDVE", "text": "FUNCTION: Putative sodium channel toxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily. Sodium channel inhibitor family."}
+{"protein": "MAAAAVARRVVLVLVLAAASLAAAPRGAAARSLGGREGPGEVDADAAVDLNATNFDAFLKASLEPWAVVEFFAHWCPACRNYKPHYEKVAKLFNGRDAAHPGLILMARVDCASKVNIDLCNRFSVDHYPFLLWGPPTKFASAKWDPKQENNEIKLIDDGRTAERLLKWINNQMKSSFSLEDKKYENENMLPKNASDPEQIVQAIYDVEEATAQALQIILERKTIKPKNRDSLIRFLQILVARHPSKRCRRGSAELLINFDDHWSSNLSLSSQEGSKLLESVAEENHWICGKEVPRGYWLFCRGSKSETRGFSCGLWVLMHSLTVRIGDGESQSTFTSICDFIHNFFICEECRKHFYEMCSSVSAPFRTARELSLWLWSTHNKVNMRLMKEEKDMGTGDPLFPKVTWPPNQLCPSCYRSSKVTDGAVDWNEDAVYQFLVNYYGKKLVSSYKETYMESLQQQEKKIVSEDSSISNAASVPIGAALGVAIASCTFGALACFWRAQQKNRKQRKNWN", "text": "FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins (By similarity). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MNTESVVEFLGNVTLLQRLPSSSLKRISEVVVFKGYDRGDYVVRENQNVDGVYFLLQGQAQVLRSAGEENYQEFPLKRYDFFGHGIFGDVYSADVVAVTELTCLLLMSDHRALLEIKSVSDSDKERCLVEDILYLEPLDLNVYRGFTPPNAPTYGKVYGGQLVGQALAAASKTVETMKIVHNFHCYFLLVGDINIPIIYDVNRLRDGNNFATRSVDARQKGKTIFTLFASFQKKQQGFIHQESTMPHTPAPETLLPREEMLERLVTEPLLPRDYRNQVATEISVPFPIDIRFCEPNRSTKQNKSPPRLKYWFRAKGKLSDDDQALHRCVVAFASDLIFATISLNPHRREGMSVAALSLDHSMWFHRPVRADDWLLFVIVSPTATESRGFATGKMFNRKGELVVSLTQEAVLREAVTIKPSFGAKL", "text": "FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (By similarity). Active with both medium chain and long chain acyl-CoAs as substrates (By similarity). SUBCELLULAR LOCATION: Peroxisome matrix Note=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded. SIMILARITY: Belongs to the C/M/P thioester hydrolase family."}
+{"protein": "TMCYSHTTTSRAILTNCGENSCYRKSRVHP", "text": "FUNCTION: Inhibits acetylcholinesterase (By similarity). Has been described to inhibit both the slowly and the rapidly inactivating phases of potassium efflux (PubMed:1304870). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Acn-esterase inhibitor sub-subfamily."}
+{"protein": "MRPADLLQLVLLLDLPRDLGGMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLLILLTSHYKLNVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACAIMVGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIVFVLTLNIVAFVIVCCCYVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFICMAPISFYALSAILNKPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQVQKVTHDMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL", "text": "FUNCTION: Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin (PubMed:11847099, PubMed:12045258). Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin (PubMed:12045258). The activity of this receptor is mediated by G proteins which activate adenylate cyclase (PubMed:11847099). 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": "MKGDKEVLRHLNGVLKLHLTAINQYFLHARMLKNWGLKDLGKAVYKYSIEEMKQADEVIERILFLEGLPNLQDLGKLGIGEDVAEMLASDLKMEQAEHKALTEAIALCETKQDFVTRDELGEILEDTEEHIDWLETQIDLMAKMGTQNYLQAAMGQIEGD", "text": "FUNCTION: Iron-storage protein. SIMILARITY: Belongs to the bacterioferritin family."}
+{"protein": "MLLWVILLVLAPVSGQFARTPRPIIFLQPPWTTVFQGERVTLTCKGFRFYSPQKTKWYHRYLGKEILRETPDNILEVQESGEYRCQAQGSPLSSPVHLDFSSASLILQAPLSVFEGDSVVLRCRAKAEVTLNNTIYKNDNVLAFLNKRTDFHIPHACLKDNGAYRCTGYKESCCPVSSNTVKIQVQEPFTRPVLRASSFQPISGNPVTLTCETQLSLERSDVPLRFRFFRDDQTLGLGWSLSPNFQITAMWSKDSGFYWCKAATMPYSVISDSPRSWIQVQIPASHPVLTLSPEKALNFEGTKVTLHCETQEDSLRTLYRFYHEGVPLRHKSVRCERGASISFSLTTENSGNYYCTADNGLGAKPSKAVSLSVTVPVSHPVLNLSSPEDLIFEGAKVTLHCEAQRGSLPILYQFHHEGAALERRSANSAGGVAISFSLTAEHSGNYYCTADNGFGPQRSKAVSLSVTVPVSHPVLTLSSAEALTFEGATVTLHCEVQRGSPQILYQFYHEDMPLWSSSTPSVGRVSFSFSLTEGHSGNYYCTADNGFGPQRSEVVSLFVTVPVSRPILTLRVPRAQAVVGDLLELHCEAPRGSPPILYWFYHEDVTLGSSSAPSGGEASFNLSLTAEHSGNYSCEANNGLVAQHSDTISLSVIVPVSRPILTFRAPRAQAVVGDLLELHCEALRGSSPILYWFYHEDVTLGKISAPSGGGASFNLSLTTEHSGIYSCEADNGLEAQRSEMVTLKVAVPVSRPVLTLRAPGTHAAVGDLLELHCEALRGSPLILYRFFHEDVTLGNRSSPSGGASLNLSLTAEHSGNYSCEADNGLGAQRSETVTLYITGLTANRSGPFATGVAGGLLSIAGLAAGALLLYCWLSRKAGRKPASDPARSPSDSDSQEPTYHNVPAWEELQPVYTNANPRGENVVYSEVRIIQEKKKHAVASDPRHLRNKGSPIIYSEVKVASTPVSGSLFLASSAPHR", "text": "FUNCTION: May be involved in B-cell development and differentiation in peripheral lymphoid organs and may be useful markers of B-cell stages. May have an immunoregulatory role in marginal zone B-cells. May play a role in fertilization (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MDMMMMSTRLIHLSRHFPQYGFRCHPSGLISSARMQYNINNGLAHMGKQMPNTSTHTTRIHPASFSSDLASRKYSLIYAFPLIRGLRALSRLKLLQTGITVVLLPTVYYLHLQGQASVLVLNRSIGIALFAGVMLYSISHFVRRVVGMMYLDSTQTILKVSHLSFWGHRRDIYVPVSDVVTLGDSGDSRGESILRLKRYSTSNTMYFSTRLGRVVDRHAFGKVFGSLS", "text": "FUNCTION: May be 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": "MLKMESTQQMAVSIINSSFEAAVVAATSALENMGIEYDYQDIYSRVKNKFDFVMDDSGVKNNLIGKAITIDQALNNKFGSAIRNRNWLADTSRAAKLDEDVNKLRMMLSSKGIDQKMRVLNACFSVKRIPGKSSSIIKCTKLMRDKLERGEVEVDDSFVDEKMEVDTIDWKSRYEQLEQRFESLKSRVNEKYNNWVLKARKMNENMHSLQNVISQQQAHIAELQVYNNKLERDLQNKIGSLTSSIEWYLRSMELDPEIKADIEQQINSIDAINPLHAFDDLESVIRNLISDYDKLFLMFKGLIQRCNYQYSFGCE", "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": "MERYKCRFCFKSFINGRALGGHMRSHMLTLSAERCVITGEAEEEVEERPSQLCDDDDDTESDASSSSGEFDNQKMNRLDDELEFDFAEDDDVESETESSRINPTRRRSKRTRKLGSFDFDFEKLTTSQPSELVAEPEHHSSASDTTTEEDLAFCLIMLSRDKWKQQKKKKQRVEEDETDHDSEDYKSSKSRGRFKCETCGKVFKSYQALGGHRASHKKNKACMTKTEQVETEYVLGVKEKKVHECPICFRVFTSGQALGGHKRSHGSNIGAGRGLSVSQIVQIEEEVSVKQRMIDLNLPAPNEEDETSLVFDEW", "text": "FUNCTION: Probable transcription factor that may be involved in stress responses. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "SLYAPSAMVFSVAQGDDVAAPTVVRATTVSCAPGARGTHPDPKAACAALKSTGGAFDRLLSEPNPDRACPMHYAPVTVSAVGVWEGRRVAWDHTFANSCTMAATLDGNAVF", "text": "FUNCTION: Inhibitor of subtilisin and chymotrypsin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I16 (SSI) family."}
+{"protein": "MKLDELRKKYIDFFKSKGHCEIAGKSLIPDNDSTVLFNTAGMQPLVPYLLGEMHPSGDMLVDVQKCLRTGDIDEVGDLSHLTFFEMLGNWSLGAYFKELSVKYSFEFLTSPNYLNISKDKLYVSVFEGDESIPRDTETANVWESLGIPKDRIFYLSREHNFWGPVGNTGPCGPDTEIFVDTGKEKCSVRCDITCSCGKYFEIWNNVFMQYKRDENGNYEELKRKCVDTGMGIERTITFLQGKSSVYDTDAFKPIIDKIEKISGKIYGQNLEDDRSIRIIADHIKASCFILADNFAVLPSNIGQGYVLRRIIRRAIRYAKKLGMESYVLADLVDSVEEIYKSFYKELTEKKDFIKAELNVEEEKFFKTLRHGEQEFIKLIQQLSSKSIPGDISFKLYDTYGFPYEITEELATEYGFSIDKAGFEEHFKKHQEVSKKGGDKVFKGGLADCTYETTKLHTATHLLHKALQLVLGEHVRQKGSNITAERLRFDFNHPYKMTDDEIKQVEDMVNLQIKNKLSVKRSVMNLDDALAKGAMALFGEKYEDIVSVYEIDGFSIEVCGGPHVKNTGELGTFKIQKEQASSSGVRRIRAILID", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
+{"protein": "MTLVMSPDSSYGRYDAPAPADNRIMSPVHKEREPELHIEFDGTTVLCRVCGDKASGFHYGVHSCEGCKGFFRRSIQQKIQYRPCTKNQQCSILRINRNRCQYCRLKKCIAVGMSRDAVRFGRVPKREKARILAAMQSSTTRAHEQAAAAELDDGPRLLARVVRAHLDTCEFTRDRVAAMRNGARDCPTYSQPTLACPLNPAPELQSEKEFSQRFAHVIRGVIDFAGLIPGFQLLTQDDKFTLLKSGLFDALFVRLICMFDAPLNSIICLNGQLMKRDSIQSGANARFLVDSTFKFAERMNSMNLTDAEIGLFCAIVLITPDRPGLRNVELVERMHSRLKSCLQTVIAQNRSDGPGFLRELMDTLPDLRTLSTLHTEKLVVFRTEHKELLRQQMWVEDEGALWADSGADDSARSPIGSVSSSESSETTGDCGTPLLAATLAGRRRLDSRGSVDEEALGVAHLAHNGLTVTPVRPPPRYRKLDSPTDSGIESGNEKHERIVGPESGCSSPRSSLEEHSDDRRPIAPADDMPVLKRVLQAPPLYDASSLMDEAYKPHKKFRAMRRDTWSEAEARPGRPTPSPQPPHHPHPASPAHPAHSPRPIRAPLSSTHSVLAKSLMEGPRMTPEQLKRTDIIQQYMRRGETGAPTEGCPLRAGGLLTCFRGASPAPQPVIALQVDVAETDAPQPLNLSKKSPSPSPPPPPPRSYMPPMLPA", "text": "FUNCTION: Orphan receptor possibly involved in the regulation of genes in the ecdysteroid cascade. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
+{"protein": "MFRRLLIATVVGILAAFAVAGFRHAMLLLEWLFLNNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLMGWQKFTQQRPHAPTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQCFTPRQEWKLWIACGAAAGMAAAYRAPLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALLYSVQLSVTVLARDYALIISTGVLAGLCGPLLLTLMNACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLFAVLASSGSGAPGGVFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLHRDSIYRQHTAKHS", "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": "MKLKDTKSRPKQSSCGKFQTKGIKVVGKWKEVKIDPNMFADGQMDDLVCFEELTDYQLVSPAKNPSSLFSKEAPKRKAQAVSEEEEEEEGKSSSPKKKIKLKKSKNVATEGTSTQKEFEVKDPELEAQGDDMVCDDPEAGEMTSENLVQTAPKKKKNKGKKGLEPSQSTAAKVPKKAKTWIPEVHDQKADVSAWKDLFVPRPVLRALSFLGFSAPTPIQALTLAPAIRDKLDILGAAETGSGKTLAFAIPMIHAVLQWQKRNAAPPPSNTEAPPGETRTEAGAETRSPGKAEAESDALPDDTVIESEALPSDIAAEARAKTGGTVSDQALLFGDDDAGEGPSSLIREKPVPKQNENEEENLDKEQTGNLKQELDDKSATCKAYPKRPLLGLVLTPTRELAVQVKQHIDAVARFTGIKTAILVGGMSTQKQQRMLNRRPEIVVATPGRLWELIKEKHYHLRNLRQLRCLVVDEADRMVEKGHFAELSQLLEMLNDSQYNPKRQTLVFSATLTLVHQAPARILHKKHTKKMDKTAKLDLLMQKIGMRGKPKVIDLTRNEATVETLTETKIHCETDEKDFYLYYFLMQYPGRSLVFANSISCIKRLSGLLKVLDIMPLTLHACMHQKQRLRNLEQFARLEDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYVHRSGRTARATNEGLSLMLIGPEDVINFKKIYKTLKKDEDIPLFPVQTKYMDVVKERIRLARQIEKSEYRNFQACLHNSWIEQAAAALEIELEEDMYKGGKADQQEERRRQKQMKVLKKELRHLLSQPLFTESQKTKYPTQSGKPPLLVSAPSKSESALSCLSKQKKKKTKKPKEPQPEQPQPSTSAN", "text": "FUNCTION: ATP-dependent RNA helicase. SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily."}
+{"protein": "MGKKSKSQKEAPATESAGSLPFLGGNVSVDPSLASLFEQSAGPVKVPEVPRLGAAPKTKITDVEKDEEESSSAGNDSASEDQFMEDAPESPDAAEEAVQAVPEPPSRKRKRAAGEDLEESYMRRLAKEEQKEQKKRRAERSSSLEEESEDGEKESPQSEDGESEDEGADIPKHEALAGAANDDDELSKSNRTVFLGNVSTKAITSKSAKKELMKHLSSFLSTLPESTGPHKIDSIRFRSTAFASGGKIPKRAAFAKQEIHDDTTPSTNAYAVYSTAQAAKKAPAALNGTVVLDRHLRVDNVAHPAKVDHKRCVFVGNLDFIDNETGTEEGEKKKKNRPPADVEEGLWRTFNAHTKASQSGPAGRGNVESVRVVRDRSTRVGKGFAYVQFYDQNCVEEALLLNDKRFPPLLPRKLRVVRAKKVAKKSVETTGAPKGSDRTLQGRAGKLLGRSSEARLKAAAKKSISQSSLVFEGNRATADGSSRIRVRTKSRGSKAKKDSRSKKRAAAYKAAGGKKAKIGK", "text": "FUNCTION: Involved in pre-25S rRNA processing. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRM RBM34 family."}
+{"protein": "MAFLKARLAALLSVAVSCSAVLYDDAKKLPSTSYDYIVVGGGTAGSVLANRLTEDAKTQVLVLEGGPSGQGVLELEIPFYNLYGPHDPLWNWNISVLPQDTAADRVLVYPAGRVLGGTSMINGMYYSRGPSSDWDRMAAITGDSGWSWDKIYPYFIKSEVLTPSVGGRNTTGELDPSIHGKQGIVATSSPNWSYETDPLIISALNELGGPYSPILDFNNGSPLGVAWFQYTMRNGSREDAATSYFADKFLGRSNLHVLVNATVDRVVQSKSGGPVNGVEYHLSNGTGSTLHATANKEVIVSAGTFGTPHLLLNSGIGDNSTLASYNVTPIAHVPDVGKNLTDYSTVILTWSVNSTTTLYDLITKNETFANDSLAQWTASHTGPFSNGVSNHMFNLRLNETDPEVQQMLKQYGDPSSSDKAPHITLQFVEGGLGSGNSISMENFVVTPLSRGSVTLNTTDPSGPPVVDAGILTSPFDVFVLEQGILAARKFLSASAWDNYIIAPASGLDAGIPVDGSVNTTALESYIRTQATAGWRETGTAKMSPKGARWGVVDPDFRVKNVQGLRVVDASVFPEIPSLHTQIPIYAIAERAADLIKGSH", "text": "FUNCTION: Dehydrogenase; 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:31535864, PubMed:28371074). The role of the dehydrogenase eriK within the pathway has still to be determined (Probable). The first step of the erinacines biosynthesis pathway is catalyzed by the geranylgeranyl diphosphate (GGPP) synthase eriE via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). 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 (Probable). SIMILARITY: Belongs to the GMC oxidoreductase family."}
+{"protein": "ANKRPVWIMAHMVNAVAQIDEFVNLGANSIETD", "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) with high activity (9.5 U/mg) (PubMed:15450925). 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": "MKYLLPSAAAGLLLLAAQPTMAANTGGYATTDGGDVSGAVKKTARSLQEIVDIIEAAKKDSSGKAVKGGAYPLVITYNGNEDALIKAAEANICGQWSKDPRGVEIKEFTKGITILGTNGSSANFGIWMVNSSNVVVRNMRFGYMPGGAKDGDAIRIDNSPNVWIDHNEIFAKNFECAGTPDNDTTFESAVDIKKGATNVTVSYNYIHGVKKVGLSGSSNTDTGRDLTYHHNIYSDVNSRLPLQRGGKVHAYNNLYDGIKSSGFNVRQKGIALIESNWFENALNPVTARNDDSNFGTWELRNNNITSPSDFAKYKITWGKPSTPHINADDWKSTGKFPAVPYSYSPVSAQCVKDKLASYAGVGKNLAVLTAANCK", "text": "FUNCTION: Involved in maceration and soft-rotting of plant tissue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLADES subfamily."}
+{"protein": "MFDFDATLPLMAVQFLILTVILNALLYKPLGQALDNRDEYIRTNLQQAKERLQQATELAQQYEQELASTRRQAQALIEEARVEAQKIATAEIAEAQQAVQAELLKIQAEIDQQKQATLQALEGQVASLSEQLLAKLMA", "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. FUNCTION: The complex from the organism is particularly stable to disruption and remains functional after 6 hrs at 55 degrees Celsius. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
+{"protein": "MDDPSATLLPEHSEDLRLARDAELKKVLKLKLVLDELRRLDVGPNPSDEIKRALKLVSIGSYARLGEMEGAGQEQVLGLPSGSSFPPLNYTDRKTVRTKLSAQLRTTLQPIAELCDRIREEFPDAFGQEADLSCDQKEILRLEEEHRSGLEKLVALLTRKCTLLKETAELKLGPQLANELKLQQAQAQLVQTKAELLRGFFVHEAASRTEHSVKAHKEVEAHLDELLAAKK", "text": "FUNCTION: As part of the augmin complex, plays a role in centrosome- independent generation of spindle microtubules (PubMed:18443220). The complex is required for mitotic spindle assembly through its involvement in localizing gamma-tubulin to spindle microtubules (PubMed:17412918). dgt2 binds to microtubules in vitro (PubMed:19289792). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=Stably associates with the polar regions of some acentrosomal meiotic spindles in contrast to the uniform staining observed over mitotic spindles in syncytial embryos (PubMed:19289792, PubMed:23785300)."}
+{"protein": "MAASSAAFAACLLACALLFQMCVASRKLTALVQDQPITMTYHKGALLSGRIAVNLIWYGNFSAPQRAVITDFVSSLSTPPSPQPQPEPSVASWFKTAQKYYANSKARFPALSLGQHVLDQSYSLGKRLGEKDLVRLAARGSPSRAINVVLTADDVAVDGFCMSRCGTHGASPRSRAGRFAYVWVGNPATQCPGQCAWPYHQPVYGPQAAPLTPPNGDVGVDGMVISLASMIVGTVTNPFGNGFFQGDADAPLEAATACAGVYGKGAYPGYAGSLLVDPASGASYNANGAHGRKYLVPALVDPDTSACSTVG", "text": "FUNCTION: Involved in the control of organ size (PubMed:24486766). Upon auxin signaling, is targeted by the transcription activator SMOS1 to regulate cell expansion during organ size control (PubMed:24486766). May promote cell expansion by modulating microtubule organization (PubMed:24486766). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the EXORDIUM family."}
+{"protein": "MVAPSQFKQLEKVGNGTYATVYKGLNKTTGVYVALKEVKLDSEEGTPSTAIREISLMKELKHDNIVRLFDVIHTENKLTLVFEFMDNDLKKFMDNRNKGNSHKGLEMDLVKYFQWQLLQGVAFCHENRILHRDLKPQNLLINNRGQLKLGDFGLARAFGIPVNTFSSEVVTLWYRAPDVLMGSRNYCTSIDIWSCGCILAEMIMGKPLFPGSNDEEQLKLIFDTMGTPVEQTWPQVTQLAKYNPLLPPHMPRDLKQLLQNNTEEVLDDNVVDLLHGLLQLNPDARLSAKDALNHPWFAEYNHAN", "text": "FUNCTION: When phosphate concentrations are high it phosphorylates the PHO4 transcription factor thus establishing repression. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "MSNVTVSVFTLDKSISEEPVLPSSFIPSSGNVFPKFTSAIPKTAWELWYFDGISKDDRSSIVIGVTRNAEGLKHGGFKVQVFVIWADERTWHRDLFFPESVVSIDESGATEGIWKHATSSSSISFSCAGDLSKASLVFDVPGIVQGDMHLEALPGDTGLDTDATLGPSVYYVRPLGRASVKAQLSLYSSDATAAEQFILGTSANGGMDRVWSPLSWPQVMTESYYLRAQVGPYAMQIMRIFPPKGSENSENQPSTMARLYREGQLICAPQHVVTRDDALITHDSLILSKQNTSDSGDAVTGEYRDKNTGYTVEFVGKGNEEQRWEFQVRHERIIWNTPTSRPGPDATGNTGFVERLYGGTIGESYEGVGTGGQCELS", "text": "FUNCTION: Diels-Alderase; 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). SIMILARITY: Belongs to the Diels-Alderase family."}
+{"protein": "MEKPSGQFLGLSLLLLPLLLPISCNAQQLFIFGDSLYDNGNKPFLATDVPSTFWPYGLSIDFPNGRWSDGRIVPDFIAEFLGIPFPPPVLDRSANFSSGVTFATADATILGTPPQTLTLGDQVKAFAQIKSTWTDAQRQKGIYMFYIGANDYLNYTNANLNATAQQQEAFVSQVIAKLKDQLLAIYGLGGRKFAFQNLAPLGCLPIVKQDFKTGNFCLPLASNLAAQHNQLLSETLENLSETLDGFNYIIYDYFNSSLRRMARPNNYGYFTTNLACCGTGSHDAFGCGFKNVHSNLCSYQRGYMFFDGRHNAEKTNEAVAHLIFSADPSVVFPMNLRELFVHP", "text": "FUNCTION: Has lipolytic activity towards triacylglycerols, vinyl esters and phospholipid. Of the triacylglycerols, the highest activity is towards tributyrin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family."}
+{"protein": "MQDAITSVINSADVQGKYLDGSAMDKLKAYFTTGALRVRAASTISANAAAIVKEAVAKSLLYSDVTRPGGNMYTTRRYAACIRDLDYYLRYATYAMLAGDPSILDERVLNGLKETYNSLGVPVGSTVQAIQAMKEVTAGLVGADAGREMGVYFDYICSGLS", "text": "FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=Forms the core of the phycobilisome. SIMILARITY: Belongs to the phycobiliprotein family."}
+{"protein": "MNNLFALCQRSAVIFSIIFTVVACDKLDSPKPISPQIETQKNTQLESNRVELKRGVYSDLTLQPWQAQSEEQTQLLRDLFEGLTAYDVQGNLVPAVAENWQTEDNKTWIFTLRENAKWSNGEPITASDFVQSWQTLSQSESPLKNYLAFMNLKNAKAVLEKALPVESLGLFAENDRTLRIELDKASPYLPSMLAHVSLLPHYAKSTEIFISNGAYQLQRQAENQHILTTNPYYWAKEKVIFQQVKYQKISVDADLSDFDVVMNPKKVNQNIQDYPQLCTYFYEFNLSDPVLQKSAVRKAIVSMISTNNLVADIAHLYPNNTFLPKSMLGEQESVWEPVVAEQLFSQNQISETRPLKLRIRYDDLSLNQTIAMRLNHQLSQSDLLRVENQGMSWQELQTARTKGDFQLIRSGWCADFNDPAAFLNLFYSKSPDNKNGYKNAEFDRLFESAMTTISEKVRLENYAKLKGIVQQEHLVLPIFQYSTPVYLVPSIMGAQVNSVGVIYSKDLWRKVQSQ", "text": "FUNCTION: Part of a binding-protein-dependent transport system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family."}
+{"protein": "MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR", "text": "FUNCTION: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down- regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate. FUNCTION: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down- regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton, spindle. Golgi apparatus. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity. SUBCELLULAR LOCATION: Cytoplasm. Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, perinuclear region Cell membrane Cytoplasm, cytoskeleton, spindle Golgi apparatus Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily."}
+{"protein": "MTEEACRTRSQKRALERDPTEDDVESKKIKMERGLLASDLNTDGDMRVTPEPGAGPTQGLLRATEATAMAMGRGEGLVGDGPVDMRTSHSDMKSERRPPSPDVIVLSDNEQPSSPRVNGLTTVALKETSTEALMKSSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQKPTGSVGSTVTTPPPLVRGTQNIPAGKPSLQTSSARMPGSVIPPPLVRGGQQASSKLGPQASSQVVMPPLVRGAQQIHSIRQHSSTGPPPLLLAPRASVPSVQIQGQRIIQQGLIRVANVPNTSLLVNIPQPTPASLKGTTATSAQANSTPTSVASVVTSAESPASRQAAAKLALRKQLEKTLLEIPPPKPPAPEMNFLPSAANNEFIYLVGLEEVVQNLLETQGRMSAATVLSREPYMCAQCKTDFTCRWREEKSGAIMCENCMTTNQKKALKVEHTSRLKAAFVKALQQEQEIEQRLLQQGTAPAQAKAEPTAAPHPVLKQVIKPRRKLAFRSGEARDWSNGAVLQASSQLSRGSATTPRGVLHTFSPSPKLQNSASATALVSRTGRHSERTVSAGKGSATSNWKKTPLSTGGTLAFVSPSLAVHKSSSAVDRQREYLLDMIPPRSIPQSATWK", "text": "FUNCTION: Transcriptional repressor (PubMed:12183469, PubMed:16415179). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Enhances MBD2-mediated repression (PubMed:12183469, PubMed:16415179). Efficient repression requires the presence of GATAD2B (PubMed:16415179). SUBCELLULAR LOCATION: Nucleus speckle Nucleus Chromosome Note=Speckled nuclear localization requires both CR1 and CR2 regions (PubMed:16415179). Localizes to sites of DNA damage in a manner partially dependent on ZMYND8 (PubMed:27732854)."}
+{"protein": "MIFSGKFTSHLLNYGFKPNNLRLLSTSTHPTIYFTGIQPTGIPHLGNFFGSIEPWTELQNSVDKNILMMLSVVDQHAISLGPLPANELRQNTHQMTASLIACGVDPNRTLLFRQSDVPQIAQISWILGSLQTTSKLARLPQYKEKKERFKKGDIPVGLLTYPLLQAADVLTFKATTVPVGEDQSQHLNLLGGLAYAFNKTYETEIFPIPKQLTRESHARIRSLREPEKKMSKSSGGPRSRIEITDSRSTIIEKCQKAQSDNAGKVTYDKENRLAVSNLLDLYSAVTKTQTSEIDFSNWTTLDLKMNLAEAVDKRLAPIRQKFEELQNTGEVDKVLTENGEKAREIAEKNLEEIRRTIGFL", "text": "FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
+{"protein": "MTAPWAALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEPGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEVRQCQRWAGRRDGCADSFKPLPFQDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNGTTSDCLVSLVTSVTNVDLLPKESSI", "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": "MEVKARAPGKIILAGEHAVVHGSTAVAAAIDLYTYVTLRFPLPSAENNDRLTLQLKDISLEFSWSLARIKEAIPYDSSTLCRSTPASCSEETLKSIAVLVEEQNLPKEKMWLSSGISTFLWLYTRIIGFNPATVVINSELPYGSGLGSSAALCVALTAALLASSISEKTRGNGWSSLDETNLELLNKWAFEGEKIIHGKPSGIDNTVSAYGNMIKFCSGEITRLQSNMPLRMLITNTRVGRNTKALVSGVSQRAVRHPDAMKSVFNAVDSISKELAAIIQSKDETSVTEKEERIKELMEMNQGLLLSMGVSHSSIEAVILTTVKHKLVSKLTGAGGGGCVLTLLPTGTVVDKVVEELESSGFQCFTALIGGNGAQICY", "text": "FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5- phosphate, a key step in isoprenoid and cholesterol biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase subfamily."}
+{"protein": "MTGSLWLSLALSLAVLAQFKVSAAPNLVCFYDSQGFQRQGLAQFSMTDMELALQFCTHLVYGYAGVNADNYEMQSINKRLDLEQRHLAQVSSLKERYPHIKFLLSVGGDADTNEGNQYIKLLESGQQGHRRFIESARDLVRRYNFDGLDLALQLPRNKPRKVHGDVGSAWKSFKKFFTGDFIVDTDSETHKGQVTALIKDLSAALKQNDLLLSLTVLPNVNSSWYYDAPSIAPSLDFINLGTFDFLTPQRNPEEADFSAPTYEAVGQNRLGHYNLNFQTEHWLLQRVPANKINIGIATYGRTWKMTKDSGDSGMPVVPSTQGPAPAGPQSKKEGLLNWAEICSLMPNPGNTNARGPSAPVKRVLDPTKRYGSYAFRAADENGDHGLWISYDDPDSASSKAMFARVRNLGGVALFDLTQDDFRGQCTNDRFPMLRAIKYRLL", "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 (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": "MITYEEYVKQLKELDVYSTVAFKRVVPYVLIQQQQNEDELLLRLRAPSEKLVGEINNGSNKLVIIDLKISYSHVYQEPQLSIQLWETNGRQENQEEEQVDEIYLWYPNNINETLAIPTNLFTIELDTVPRPRVERTTTDNINNSGSKKLMSSSAWYVVHSCDTSEIVGTPIQNYLQRWASVYIASWWGIVRTPNNC", "text": "FUNCTION: E2-like enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy and nucleophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for proper localization of ATG8 to the preautophagosomal structure (PAS). Likely serves as an ATG5-recognition molecule (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG10 family."}
+{"protein": "MKKQRMLVLFTALLFVFTGCSHSPETKESPKEKAQTQKVSSASASEKKDLPNIRILATGGTIAGADQSKTSTTEYKAGVVGVESLIEAVPEMKDIANVSGEQIVNVGSTNIDNKILLKLAKRINHLLASDDVDGIVVTHGTDTLEETAYFLNLTVKSDKPVVIVGSMRPSTAISADGPSNLYNAVKVAGAPEAKGKGTLVVLNDRIASARYVTKTNTTTTDTFKSEEMGFVGTIADDIYFNNEITRKHTKDTDFSVSNLDELPQVDIIYGYQNDGSYLFDAAVKAGAKGIVFAGSGNGSLSDAAEKGADSAVKKGVTVVRSTRTGNGVVTPNQDYAEKDLLASNSLNPQKARMLLMLALTKTNDPQKIQAYFNEY", "text": "FUNCTION: Catalyzes the conversion of L-asparagine to L-aspartate and ammonium. SIMILARITY: Belongs to the asparaginase 1 family."}
+{"protein": "MTHDLIEKSKKHLWLPFTQMKDYDENPLIIESGTGIKVKDINGKEYYDGFSSVWLNVHGHRKKELDDAIKKQLGKIAHSTLLGMTNVPATQLAETLIDISPKKLTRVFYSDSGAEAMEIALKMAFQYWKNIGKPEKQKFIAMKNGYHGDTIGAVSVGSIELFHHVYGPLMFESYKAPIPYVYRSESGDPDECRDQCLRELAQLLEEHHEEIAALSIESMVQGASGMIVMPEGYLAGVRELCTTYDVLMIVDEVATGFGRTGKMFACEHENVQPDLMAAGKGITGGYLPIAVTFATEDIYKAFYDDYENLKTFFHGHSYTGNQLGCAVALENLALFESENIVEQVAEKSKKLHFLLQDLHALPHVGDIRQLGFMCGAELVRSKETKEPYPADRRIGYKVSLKMRELGMLTRPLGDVIAFLPPLASTAEELSEMVAIMKQAIHEVTSLED", "text": "FUNCTION: Catalyzes the transfer of the alpha-amino group from L-lysine to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). B.subtilis is the only bacterium known to utilize L-lysine as an amino donor in the biosynthesis of DAPA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily."}
+{"protein": "MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLEVCDDYSLDDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGENMGKKDKVQDNHLSPNKWKWTKRTLSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYNKMAKTQSQPILNTKESAAQSKPKEELEMESIPSPVAPLPTRTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLTSLPSKTGGSTAPEVGWRGALGASGGRFVEANPSPDASQHSSFFIESPKSSMKTNNPLKLRALKVNFMEGDPSPLLPVLGMYHDPLRNRGSAAAAVAGLECATLLDKAVLSPESSIYTTASAKTPPRSPEKHTAIAFNFEAGVHQYIDADTDDEGQLLYSVDSSPPKSLPGSTSPKFSTGTRSEKNHFESSPLPTSPKFLRQNCIYSTEALTGKGPSGQEKCKLENHISPDVRVLPGGGAHGSTRDQSI", "text": "FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain (PubMed:23161216). Plays also a role in the regulation of exocytosis independently of its electrical function (By similarity). 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. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:8081723, PubMed:1283219, PubMed:10484328, PubMed:12560340, PubMed:19074135, PubMed:19717558, PubMed:24901643). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes (PubMed:10484328, PubMed:11852086, PubMed:12060745, PubMed:19074135, PubMed:19717558, PubMed:24901643). Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic- treated pulmonary artery smooth muscle cells (By similarity). Channel properties are also modulated by cytoplasmic ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels (By similarity). 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. Major contributor to the slowly inactivating delayed- rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle cells. Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation. Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus (By similarity). Contributes to the regulation of glucose-induced action potential amplitude and duration in pancreatic beta cells, hence limiting calcium influx and insulin secretion (PubMed:23161216). Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells. May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval. Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury. May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions (By similarity). Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits (PubMed:12060745). Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner (By similarity). SUBCELLULAR LOCATION: Cell membrane Perikaryon Cell projection, axon Cell projection, dendrite Membrane; Multi-pass membrane protein. Postsynaptic cell membrane Synapse Synapse, synaptosome Lateral cell membrane Cell membrane, sarcolemma Note=Localizes to high-density somatodendritic clusters and non-clustered sites on the surface of neocortical and hippocampal pyramidal neurons in a cortical actin cytoskeleton-dependent manner (PubMed:24477962). Localizes also to high-density clusters in the axon initial segment (AIS), at ankyrin-G- deficient sites, on the surface of neocortical and hippocampal pyramidal neurons (PubMed:24477962). KCNB1-containing AIS clusters localize either in close apposition to smooth endoplasmic reticulum cisternal organelles or with GABA-A receptor-containing synapses of hippocampal and cortical pyramidal neurons, respectively (PubMed:24477962). Localizes to high-density clusters on the cell surface of atrial and ventricular myocytes and at the lateral plasma membrane in epithelial cells. Localizes both to the axial and transverse tubules (T tubule) and sarcolemma in ventricular myocytes. Associated with lipid raft domains. In cortical neurons, apoptotic injuries induce de novo plasma membrane insertion in a SNARE-dependent manner causing an apoptotic potassium current surge. SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily."}
+{"protein": "MARSALLNVMVQAAMKAGRSLSRDFGEVQNLQVSLKGPGDYVSQADRKAEDIIFAELSKARPGYGFLMEERGAVEGEDSQHRWIVDPLDGTTNFLHGIPLFAVSIALERQGQIVAGVIYNPAMDELYTTERGGGAFMNDRRLRVAGRIKLVDTVIGCGMPHLGRGHHGNFLVELRNVMAEVSGVRRLGSAALDLAYVAAGRMDGFWETGLSAWDIAAGLLLIREAGGFVSDMDGGQDMLDNGSVVAGNEVIQRALLKAVKKPLSAR", "text": "SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
+{"protein": "MAMNKSVGLFSSASLAVDYVDSLLPENPLQEPFKNAWVYMLDNYTKFQIATWGSLIVHETIYFLFSLPGFLFQFIPFMRKYKIQKDKPETFEGQWKCLKGILFNHFFIQLPLICGTYYFTEFFNIPYDWERMPRWYFTLARCLGCAVIEDTWHYFLHRLLHHKRIYKYIHKVHHEFQAPFGIEAEYAHPLETLILGTGFFIGIVLLCDHVILLWAWVTMRLLETIDVHSGYDIPLNPLNYIPFYTGARHHDFHHMNFIGNYASTFTWWDRIFGTDVQYHAYTEKMKKLGKKSE", "text": "FUNCTION: Catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, which can be subsequently metabolized to cholesterol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
+{"protein": "MLKSTTRHVHIFAADIRNDNFIASDTKLTLDVDPDNEFIWNDPALQKVYSEFDRLVAAYTGLALTEYNLRRIGSDLENFIRGLLQQGEIAYNLDSRVLNFSMGRPQVRGPGQIENRPGQ", "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 NdhM subunit family."}
+{"protein": "MPNHIVLYQPEIPANTGNISRTCAGTDTYLHLIRPLGFSTDDKMLKRAGLDYWDNVKLSYYDSLDEFFEKNAGGEFYYITKFGRHVYSDVDYSDPNKNYFFVFGKETTGLPDELLQANEENCLRIPMTDHIRSLNLSNTAAVLAYEALRQQSFGALLQEPNYDRKIFKD", "text": "FUNCTION: Could methylate the ribose at the nucleotide 34 wobble position in tRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily."}
+{"protein": "MKTFLLLLLVLLELGQAPGALHRVPLSRRESLRKKLRAQGQLTELWKSQNLNMDQCSTIQSANEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACQTHPVFHPSLSSTYREVGNSFSIQYGTGSLTGIIGADQVSVEGLTVVGQQFGESVQEPGKTFVHAEFDGILGLGYPSLAAGGVTPVFDNMMAQNLVALPMFSVYMSSNPGGSGSELTFGGYDPSHFSGSLNWVPVTKQAYWQIALDGIQVGDSVMFCSEGCQAIVDTGTSLITGPPGKIKQLQEALGATYVDEGYSVQCANLNMMLDVTFIINGVPYTLNPTAYTLLDFVDGMQVCSTGFEGLEIQPPAGPLWILGDVFIRQFYAVFDRGNNRVGLAPAVP", "text": "FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain (By similarity). SUBCELLULAR LOCATION: Endosome Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MSENNGKQFINGQRVAANAPTIESINATDYQPTGYLFSQATLDEVDQAAQAAYQAFLKYQHTTQQQRADFLDEIAIQIENLGSKLQEVAAQETGLPLVRLQGETGRVTGQLRLFAELLRRGDFYGARIDTALPERKPLPRVDLRQYKIGVGPVAVFGASNFPLAFSTAGGDTVAALAAGCSVVFKAHSGHMATAELVAQAIEKAILNSGIPSGTFNMIFGSRVGANLVEHPLIQAAGFTGSLEGGMALFNLAQNRPQPIPFFAEMSSVNPVIVMPEALNARGEKVAQDTVASFNMGCGQFCTKPGLIIGIKSPAFDQFVTALIDTTRTAVPQIMLNQGTLKSYQQGIDALLNEQGFKCIASGQAPELISQAQPHLFQADQSVLLSGNPKLQHEVFGPMSIVIAVDDEATLLNGLEKLAGQLTATIIADESDLPQAKELLNLLTRKAGRVLFNGFPTGVEVSDAMVHGGPFPATSDSRGTSVGTGAIERFLRPVCYQNTSQVLLPDVLKDGNPLHITRLVNGVLTQN", "text": "FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of alpha- ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate in the D- glutarate degradation pathway. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
+{"protein": "MKEVIAIIRPNTVSKTVKALDVVGFPAVTMAECFGRGKQKGYFSANLPEIVDIQKIIEEGEKEGRFIKYIPKRLISIVVDDADVPLVVGIISKVNRTGSFGDGRIFVLPVEEAIRVRTGETGEIAIGN", "text": "FUNCTION: Could be involved in the regulation of nitrogen fixation. SIMILARITY: Belongs to the P(II) protein family."}
+{"protein": "MNKTAIALLALLASSASLAATPWQKITQPVPGSAQSIGSFSNGCIVGADTLPIQSEHYQVMRTDQRRYFGHPDLVMFIQRLSSQVSNLGMGTVLIGDMGMPAGGRFNGGHASHQTGLDVDIFLQLPKTRWTSAQLLRPQALDLVSRDGKHVVSTLWKPEIFSLIKLAAQDKDVTRIFVNPAIKQQLCLDAGTDRDWLRKVRPWFQHRAHMHVRLRCPADSLECEDQPLPPPGDGCGAELQSWFEPPKPGTTKPEKKTPPPLPPSCQALLDEHVI", "text": "FUNCTION: Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the peptidase M74 family."}
+{"protein": "MKIALYSILLITVCYLSSTDAYLFDPKAVDALLREIRARLQATGKEPHARKIEQETEEIKKEELMQAEDVEGSGSGEEIEGSGEVISTITGVPIMDNEEKKDLKPENFPRPEPIFDKYGNLKSKDKLEALTYSNFKKQAPATLQDHYNLNPTGTLQMLQGLDIHGGSGGYHRALSGGYLPPSTYDPYNVNWHSYGDEGVKMKDKAISVFRRVIAPGR", "text": "FUNCTION: Probably acts downstream of the Wnt signaling pathway. SUBCELLULAR LOCATION: Nucleus Secreted."}
+{"protein": "MQQSPQMIPMVLPSFPPTNNITTEQIQKYLDENKKLIMAILENQNLGKLAECAQYQALLQKNLMYLAAIADAQPQPPAATLTSGAMTPQAMAPNPSSMQPPPSYFMQQHQAVGMAQQIPPGIFPPRGPLQFGSPHQFLDPQQQLHQQAMQGHMGIRPMGLNNNNGLQHQMHHHETALAANNAGPNDASGGGKPDGTNMSQSGADGQGGSAARHGGGDAKTEGK", "text": "FUNCTION: Transcription coactivator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues (By similarity). Component of a network formed by miR396, the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation (By similarity). GIFs are involved in the positive regulation of cell proliferation of lateral organs in a functionally redundant manner. SIMILARITY: Belongs to the SS18 family."}
+{"protein": "MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNSSDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYYYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGFYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSVEEPEDCDSYCKASKGKLKMNMKKYCRKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKCKKA", "text": "FUNCTION: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Involved in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977). It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in colorectal tumorigenesis by regulating apoptosis (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Mainly secreted."}
+{"protein": "MSDGKEELVNRAKLAEQAERYDDMAASMKKVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGSEKKQQMAKEYREKVEKELRDICQDVLNLLDKFLIPKAGAAESKVFYLKMKGDYYRYLAEVASGDDRNSVVEKSQQSYQEAFDIAKDKMQPTHPIRLGLALNFSVFFYEILNAPDKACQLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDAATDDTDANETEGGN", "text": "FUNCTION: Required for extension of lifespan by sir-2.1 (PubMed:16777605). Required to modulate lifespan, in concert with hcf- 1, acting redundantly with 14-3-3-like protein par-5 (PubMed:21909281). Promotes nuclear export of yap-1 (PubMed:23396260). Negatively regulates the transcriptional activity of daf-16 by sequestering it to the cytoplasm (PubMed:21531333). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the 14-3-3 family."}
+{"protein": "MNKQSWLLNLSLLKTHPAFRAVFLARFISIVSLGLLGVAVPVQIQMMTHSTWQVGLSVTLTGGAMFVGLMVGGVLADRYERKKVILLARGTCGIGFIGLCLNALLPEPSLLAIYLLGLWDGFFASLGVTALLAATPALVGRENLMQAGAITMLTVRLGSVNSPMIGGLLLAIGGVAWNYGLAAAGTFITLLPLLSLPALPPPPQPREHPLKSLLAGFRFLLASPLVGGIALLGGLLTMASAVRVLYPALADNWQMSAAQIGFLYAAIPLGAAIGALTSGKLAHSARPGLLMLLSTLGSFLAIGLFGLMPMWILGVVCLALFGWLSAVSSLLQYTMLQTQTPEVMLGRINGLWTAQNVTGDAIGAALLGGLGAMMTPVASASASGFGLLIIGVLLLLVLVELRHFRQTPPQVTASDS", "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": "MTSTNPVVAEVIPAETSTDATETTIATTEAGEAPEKKVRKAYTITKSRESWTEGEHDKFLEALQLFDRDWKKIEDFVGSKTVIQIRSHAQKYFLKVQKNGTLAHVPPPRPKRKAAHPYPQKASKNAQMSLHVSMSFPTQINNLPGYTPWDDDTSALLNIAVSGVIPPEDELDTLCGAEVDVGSNDMISETSPSASGIGSSSRTLSDSKGLRLAKQAPSMHGLPDFAEVYNFIGSVFDPDSKGRMKKLKEMDPINFETVLLLMRNLTVNLSNPDFEPTSEYVDAAEEGHEHLSS", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Actively translocating nucleo-cytoplasmic shuttle protein."}
+{"protein": "MIRSSIKNKITTTKSLSCISLINRQYGTSTKEVRETFLNYFEKNGHKRLPSGSLLPYNDNSLLFTNAGMVQFKNQFTGNEESKYKKVTTSQKCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGGYNHFKRDSIQHAWDLLTKEYGLPKERLAISVLEGDEESAEIWRNQIGLPNDKIMYKGREDNFWSMGDGPGPCGPCSEIFWDHGKEVDGERYLEIWNLVFMQYNKSGKEGDEMPVDKLPIPCVDTGMGLERMASVLQGKFTNYDIDLFQNLINSFKEIVTMDVGRAQFQLQQDPQRVETAYRVIADHLRSISFLISDGVIPFNIGRGYVLRKIIRRALSYGKILGFNGPFLSTLFPLLEREMGDIYPQLIERSNEIRNVILNEEGTFYNAIQRGIPYLEEFVQQNKLNEESLFLLYNTYGLPLEMSQVKAKQNNIEIDMDKVNKLIDETREQSRLTWNTSSSSSDQTTQQTTQLPEKTFLSWKSDNIKPKFIGYNGCVENDNSKVLRSHFDNDSHLVYLSLDETPFYGTSGGQVGDVGELINVSSGKNVYRVINTIKPYEGGLVLVVEWDPSQQLASQVYQDLKQDSLLNCRVDRSIRNQVAVHHSATHLLHAALRNVIGKSVVQAGSLVGSESLRFDFTHGQKLTPNQIEQIEQWVNDAIAKDIALNTDEIPYEQASKNSDTLQLFSEKYSELVRVVSIPGFSKELCGGTHVERSSSIHQFKIISESSVAAGTRRIEAVAGLAATNFFKNHYQLVHQLSNSINSPIVNFQQSFERLVNTNSKQEKEIFDLKLKIAQLSSVNYNGQYKSDNGGEMIPLSLHIIDCEDKKAFTKVTENFAKEFSSSPIQLTISKGGKVLCQLLSSSSSSSSSLSADTVLKQLFKSIGMGKGGGNKLMANASIQPLNNEILNSILNWSNVNNNYNNKKN", "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 tRNA(Ala) via its editing domain. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
+{"protein": "MNSKTPSTDIAALKDLLRYKVTVARHGFLFDDGKIVWSEDGDEAWNRLLVVVGALRSSNRMSQALFMDMSITKGDGYLLFSDLQGTNNLQYRTPKFRQYLFPVDEFLPLPR", "text": "FUNCTION: Plays an essential role for the viral pathogenicity. SIMILARITY: Belongs to the novirhabdovirus NV protein family."}
+{"protein": "MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQNRIKEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHEALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKESALV", "text": "FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily."}
+{"protein": "MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFTVLDTVIMGHKELWEVKQERDRIYALPEMSEEDGYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKSRQATSRARQIDKIKLEEVKASSRQNPFIRFEQDKKLFRNALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEYEFENDLTVFEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYEDYLRSKGIE", "text": "SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. YbiT subfamily. SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. YbiT subfamily."}
+{"protein": "MRGLKDELLKAIWHAFTALDLDRSGKVSKSQLKVLSHNLCTVLKVPHDPVALEEHFRDDDEGPVSNQGYMPYLNKFILEKVQDNFDKIEFNRMCWTLCVKKNLTKSPLLITEDDAFKVWVIFNFLSEDKYPLIIVPEEIEYLLKKLTEAMGGGWQQEQFEHYKINFDDNKDGLSAWELIELIGNGQFSKGMDRQTVSMAINEVFNELILDVLKQGYMMKKGHKRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLIKCFDKTFEISASDKKKKQEWIQAIYSTIHLLKLGSPPPHKEARQRRKELRRKLLAEQEELERQMKELQAANENKQQELESVRKKLEEAASRAADEEKKRLQTQVELQTRFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQTTEAEKQELEQQRVMKEQALQEAMAQLEQLELERKQALEQYEGVKKKLEMATHMTKSWKDKVAHHEGLIRLIEPGSKNPHLITNWGPAAFTQAELEEREKSWKEKKTTE", "text": "FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. It also mediates signaling of membrane ruffling. Regulates the actin cytoskeleton as an effector or adapter protein in response to agonist stimulated phosphatidylinositol (3,4)-bisphosphate production and cell protrusion (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Nucleus Cell projection, lamellipodium Cytoplasm, cytoskeleton Note=Localizes predominantly to the nucleus in activated cells. Only a small amount can be detected in the cytoplasm."}
+{"protein": "MELQEVLRMNGGEGDTSYAKNSAYNQLVLAKVKPVLEQCVRELLRANLPNINKCIKVADLGCASGPNTLLTVRDIVQSIDKVGQEKKNELERPTIQIFLNDLFPNDFNSVFKLLPSFYRKLEKENGRKIGSCLIGAMPGSFYSRLFPEESMHFLHSCYCLQWLSQVPSGLVTESGISTNKGSIYSSKASRLPVQKAYLDQFTKDFTTFLRIHSEELFSHGRMLLTCICKGVELDARNAIDLLEMAINDLVVEGHLEEEKLDSFNLPVYIPSAEEVKCIVEEEGSFEILYLETFKVLYDAGFSIDDEHIKAEYVASSVRAVYEPILASHFGEAIIPDIFHRFAKHAAKVLPLGKGFYNNLIISLAKKPEKSDV", "text": "FUNCTION: Involved in the biosynthesis of caffeine (PubMed:17401201, PubMed:17434991). Specific for xanthosine (PubMed:17434991). Cannot use xanthosine 5'-monophosphate (XMP) as substrate (PubMed:17434991). Directly produces 7-methylxanthine, and therefore the methyl transfer and nucleoside cleavage may be coupled (PubMed:17434991). Catalyzes the 7-N-methylation of xanthosine, but does not have 1-N- or 3-N- methylation activity (PubMed:17434991). SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family."}
+{"protein": "MNILLFGKTGQVGWELQRALAPLGNLIALDVHSTDYCGDFSNPEGVAETVKKIRPDVIVNAAAHTAVDKAESEPNFAQLLNATCVEAIAKAANEVGAWVIHYSTDYVFPGNGDTPWLETDATAPLNVYGETKLAGEKALQEHCAKHLIFRTSWVYAGKGNNFAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRVAANKPEVAGLYHLVAGGTTTWHDYAALVFEEARRAGINLALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNELFTTTAI", "text": "FUNCTION: Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS) (PubMed:8170390). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity). RmlD uses NADH and NADPH nearly equally well (By similarity). SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family."}
+{"protein": "MPFVELDTNLQQQEVPQDLAEKLCSATATILGKPRERVNVTVRTGVSMVVGGSSAPCTQLIISSIGVVGTAEQNKEHSAKFFNFLTEQLGLAQDRILLRFVPLEPWQIGKNGTVMTFL", "text": "FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MIF family."}
+{"protein": "MPADYTSTARALSLPMSPAESLSPAEEDTRPLWSHLASSRRNTASPSVRESTGLRDQVVNQATKMLRRTKKTWRRLTFWQRIGAIGAALLAILLGLSFMIFTGQVFFWLGPVAEKWEQSWLAFFVLWLCVFFVSFPPLVGWSTFGTISGFIYGIWKGWILYATATVLGSTCSFIVSRTILSKFVNRMMERDKRFAALALTLKYDGLKLLCMIRLCPLPYSVCNGAVSTFPTVHPLMYGLATALITPKLLVPAFIGSRIRILSEKNEEMSAASKAVNICSIILTIGIGVFTGWYIYRRTLARAKELEAKERADIRRSLQADHAAHRPHGSFSEDPDVNTAATTLARDEEERIGFNDFDDDNVDLVIDDDSGSEISPNLTKKQFPGPYRDEFTDNDSDVFGDGDGPDSQMFRLHTHVRSG", "text": "FUNCTION: Golgi membrane protein involved in vesicular trafficking and spindle migration. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TVP38/TMEM64 family."}
+{"protein": "MEIRPLLMCFALCVVYATSKPTEKKERIHHDAPLSSREHDDAQGFDYDHDAFLGQKEAKSFDDLSPEESKRRLGVIVEKIDGDSDGFVTEVELRAWIKKAQKKYIYENVDRQWKDFDVNNDGMISWEEYRNVTYGTYLDDPEPDDGYNYQHMMARDERRFKMADQNRDQIANKEEFTAFLHPEEYDHMKDIVVLETMEDIDKNGDGFIDLNEYIGDMYNHEDEMEEPDWVATEREQFSEFRDKNKDGKMDREETMDWILPSDYDHAEAEAKHLVYESDSNKDGKLSKEEILNKYDLFVGSQATDFGEALVRHDEF", "text": "FUNCTION: Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma- carboxylase ggcx. Binds 7 calcium ions with a low affinity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane Golgi apparatus Secreted Melanosome Sarcoplasmic reticulum lumen. SIMILARITY: Belongs to the CREC family."}
+{"protein": "MKTSEELRLAPDSLPSDLVPAPVLQASPADKNTDSEPVPPPCGGDDQLQVATDAVASSVVSQELQQGDSAPLEVEFNISSELSPRIEEQEVPENASLPVEETNRPELESGEAMEGVSEEPAAVDEGDIFWSYSFSQVPQYLSGSWSEFSTRSENFLKGCKWAPDGSCILTNSADNVLRIYNLPPELYSESEQVDYAEMVPVLRMVEGDTIYDYCWYSLMSSTQPDTSYVASSSRENPIHIWDAFTGELRASFRAYNHLDELTAAHSLCFSPDGSQLFCGFNRTVRVFSTSRPGRDCEVRTTFAKKQGQSGIISCLAFSPAQPLYACGSYGRTLGLYAWDDGSPLALLGGHQGGITHLCFHPDGNLFFSGARKDAELLCWDLRQPGHLLWSLSREVTTNQRIYFDLDPSGQFLVSGNTSGVVSVWDISGAFSDCKQLEPVMTFLPQDDCTNGVSLHPTLPLLATASGQRMFPEPTNSGDEGEPELDLPLLSLRHAHPECQLQLWWCGGGPDPSNPDEDQDEKGQGRTEAVGMS", "text": "FUNCTION: RNA chaperone that plays a key role in telomere maintenance and RNA localization to Cajal bodies. Specifically recognizes and binds the Cajal body box (CAB box) present in both small Cajal body RNAs (scaRNAs) and telomerase RNA template component (TERC). Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes. In the telomerase holoenzyme complex, required to stimulate the catalytic activity of the complex. Acts by specifically binding the CAB box of the TERC RNA and controlling the folding of the CR4/CR5 region of the TERC RNA, a critical step for telomerase activity. In addition, also controls telomerase holoenzyme complex localization to Cajal body. During S phase, required for delivery of TERC to telomeres during S phase and for telomerase activity. In addition to its role in telomere maintenance, also required for Cajal body formation, probably by mediating localization of scaRNAs to Cajal bodies. Also plays a role in DNA repair: phosphorylated by ATM in response to DNA damage and relocalizes to sites of DNA double-strand breaks to promote the repair of DNA double-strand breaks. Acts by recruiting the ubiquitin ligase RNF8 to DNA breaks and promote both homologous recombination (HR) and non-homologous end joining (NHEJ). SUBCELLULAR LOCATION: Nucleus, Cajal body Chromosome, telomere Chromosome Note=Released from telomerase RNA template component (TERC) in mitotic cells coincident with delocalization from Cajal bodies. In response to DNA damage, localizes to sites of DNA double-strand breaks following phosphorylation by ATM. SIMILARITY: Belongs to the TCAB1 family."}
+{"protein": "MPSSGPGDTSISSLEREDDRKEGEEQEENRGKEERQEPSATARKVGRPGRKRKHPPVESSDTPKDPAVTTKSQPTAQDSGPSDLLPNGDLEKRSEPQPEEGSPAAGQKGGAPAEGEGTETPPEASRAVENGCCVTKEGRGASAGEGKEQKQTNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAVMNAVEESQASGESQKVEEASPPAVQQPTDPASPTVATTPEPVGADAGDKNATKAADDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPACHDSDESDTGKAVEVQNKQMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTTEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV", "text": "FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity (By similarity). Also has weak auto-methylation activity on Cys-706 in absence of DNA (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Accumulates in the major satellite repeats at pericentric heterochromatin. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family."}
+{"protein": "MTLLHCWLLLVGHLASTAYADFITKDFKSLPPPAYDTNATQALVPYNAALEERNGPSSSTALLQYIDHKPGLMKKLLAGLSIRFAPPTMKVISTPTDMLRIDKIKNNIIKSSQWKRWARSLLEQNSMQNSHVIITKKMMDDLKPTNFFLVLLEASKDKNTKAVAKILEETQFARWCTIEHESISPMEFYDVLQLNLNEPIAYMERLPVLLRYWKYYKSVHSPMSSVATPKDIIDKQTVNRFGPYWKHTGEIAELLRLDFDSDSFFNHPARNVWLDLMKTYLDDTKTAEPLMIKTFQLLGNAAAKNLQNNVYSPIHFAERWIQANLQPIDVVTILGLDIHDSNLATNSAFSFLKVFIEKFLVNHPEADTTVVKIFSRLGSDESEKALALRKSFVSFFLRTPKFTPKTVMSIFDLTISADYVEKNPVWAIWMEYVNVYLVKNKVCPEGPLADTLEFLGSTAAADGVVRKKSIELLYSSWSGKTSQDTRIKQFLTAAARLNQLEL", "text": "FUNCTION: Secreted effector that triggers a robust hypersensitive response (HR) in Lactuca serriola LS102. The response to BLN06 was visible as chlorosis but not as strong necrosis. SUBCELLULAR LOCATION: Secreted Host cell membrane. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MELHILEHRVRVLSVARPGLWLYTHPLIKLLFLPRRSRCKFFSLTETPEDYTLMVDEEGFKELPPSEFLQVAEATWLVLNVSSHSGAAVQAAGVTKIARSVIAPLAEHHVSVLMLSTYQTDFILVREQDLSVVIHTLAQEFDIYREVGGEPVPVTRDDSSNGFPRTQHGPSPTVHPIQSPQNRFCVLTLDPETLPAIATTLIDVLFYSHSTPKEAASSSPEPSSITFFAFSLIEGYISIVMDAETQKKFPSDLLLTSSSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAADISAYYISTFNFDHALVPEDGIGSVIEVLQRRQEGLAS", "text": "FUNCTION: Functions as an intracellular arginine sensor within the amino acid-sensing branch of the TORC1 signaling pathway (PubMed:26972053, PubMed:27487210, PubMed:33594058). As a homodimer or a heterodimer with CASTOR2, binds and inhibits the GATOR subcomplex GATOR2 and thereby mTORC1 (PubMed:26972053, PubMed:27487210, PubMed:33594058). Binding of arginine to CASTOR1 allosterically disrupts the interaction of CASTOR1-containing dimers with GATOR2 which can in turn activate mTORC1 and the TORC1 signaling pathway (PubMed:26972053, PubMed:27487210, PubMed:33594058). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GATS family."}
+{"protein": "MSQSDTIFDYKHIWHPYSSMNNPHPCYTVISAKGVYLKLKNRKYMIDGMSSWWAAIHGYNHPVLNKALKKQIRKMSHVMFGGITHPPAISLCRKLISLTPEKLDCVFLSDSGSVAIEVAIKMLIQYWQALGQKRKLFLTIRNGYHGDTFSAMSVSDPKNSFHQIYHNLLPKHLFADAPVSSFYKNWDNEDILSFKKIIEKNSFKIAGVILEPIVQGVGGMNFYHPMYLKQIKILCNHYSIPVIFDEIATGFGRTGKMFAFEHANVVPDILCLGKSITGGTITLAATLTSRHIADTISKGKVGCFMHGPTYMGNPLACAVANANIKILKTNQWKIQVLNIEKQLFKSLMPLINHPYVTDVRVLGAIGVVECSRSINMISIQKFFVENGVWIRPFKKLIYIVPPYIISPHTLKKLTNVISNALNKTELFI", "text": "FUNCTION: Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily."}
+{"protein": "MSSEAVAQATAATTSPEHGVPTSSATPTPPPSKGGGAGGGGGGEQQQVPFQMIPPGHFFANPFLNPYIPTAGAPAQEGEAQPQMVFSPAQYQEVMHHYFQQMMAASGAQFPIPFPMQFQPALQQPRPSSQASSSHRSEDDNGRQTAGSVVSSNVSPNHREVRPAEDSTETSGVVQNNDELLVPTSTSSDVTIGDVIEKSDSPENSQESAGGEEKSEEKRKLSGDRTDSLIRKQMSEMEKEITRRSQNKNIKTIDDDGLAELIGGSSTRTVADDFSPFVDKSGLSYTAPAPPSTEKSAPKESLNQLRSSFNLPDDSTTVGPVGPSTVPQQSQQFANNSMFMANAGNFVQNAFPIGVTMTPQATFGAAPGFQMMQPHQHNLFMQQPNPTFVNNGTNPFLQTQATLPNFVQNGTAPLVPTVSAQQFTPEQLAAAFAQQQIAQSAAPTPFDSPPPSMPSTSSGPSGALAPPPPPSHPIPRRVSGNGWPEENKENGTSTSTTNGAQSVPAAAGTDDPVWVLRDSYLKKMQREQRTSEEEEMSWQEAATAAQEAAENGGGDDQEEQETDRLLNGGTTGASTKGAERRGSVDKKKNSKETMVHEPAVLIEGVLFRARYLGSTQMLCESRGSKAARMAQAQEAVARVKAPEGDVQPSTEIDLFISTEKIMVLNTDLQRISDTDVRQDILMDHALRTISYIADIGDLVVLMARRMSTSHSDESCSDGDSSGGGVRKTPKVICHVFESDEASFIAQSIGQAFQVAYVEFLRANGIDDPSYLRQIDYQEVLNSQELLGDELEMFAKKETQKEVVVPKKAGEPLGIVVVESGWGSMLPTVVLAHMNPVGPAAHSNKLNIGDQIININGISLVGLPLSAAQTQIKNMKTATAVRMTVVSTPPVVEVRIRRPDTKYQLGFSVQNGVICSLLRGGIAERGGIRVGHRIIEINGTSVVAVAHDRIVNMLATAVGEIHMKTMPTSMFRLLTGQEQPQYI", "text": "FUNCTION: Required specifically for the determination of 3 vulval precursor cell fates P5.p, P6.p and P7.p during late second and early third larval stages; required for basolateral localization of receptor tyrosine kinase let-23. Could have a general but redundant role in development, functioning in diverse cell lineages to control cell fates (PubMed:10359617, PubMed:2159938). Regulates the trafficking of the glr-1 subunit of AMPA-type glutamate receptors (AMPRs) in the ventral nerve cord (PubMed:17671168, PubMed:22252129, PubMed:22213799). This may be partly through interacting with the small GTPase rab-6.2 in its active GTP-bound state (PubMed:22213799). SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral membrane protein Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Cytoplasm Synapse Perikaryon Note=In trans cisternae of Golgi or trans-Golgi network (PubMed:10359617). Localizes to Gogli-associated structures (PubMed:22213799). Partially co-localizes with glr-1 at the synapse (PubMed:17671168). Localizes in endosome-like structures in ventral cord dendrites. During hypoxia, diffused cytoplasmic localization. Localization in the ventral nerve cord is regulated by egl-9 isoform e and cdk-5 (PubMed:22252129). Co-localizes with rab-6.2 in neuronal cell bodies (PubMed:22213799). Co-localizes with rme-8 in puntate structures in neuronal cell bodies and in the intestine (PubMed:22213799)."}
+{"protein": "MDKLKKVLSGQDTEDRSGLSEVVEASSLSWGTRIKGFIACFALGILCSVLGTLLLWVPRKGLGLFAVFYTLGNIMSIGSTVFLMGPLKQLKRMFEPTRLIATILVLLCFALTLCSAFLWNKGLALIFCILQSLALTWYSLSYIPYARDAVKKCFAVCLA", "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": "MDDPNSYDVIIVGTNLRNSILSAALSWANQRVLHIDENSFYGEIDGSLTLRDLEQINEKIKKVDSSQILNDNGSHKSPLKRFEVQFLNKDLIPKNKGSVIQFHPQEIFASSELVKLLSETKIYKYLLLKPARSFRLLTSNEEWIKVPESRADIFNNKNLSLASKRIVMRFMKFVSNIADEQNQNLVKEWESKPFYKFLEEVFQLSGAIEESIIYGLCQSLSKDIPTKDALDTVLKYFHSFGMYGDYSYLLAMYGTGSELCQGFCRSSAVMGGTFMLGQAIDKIDESKIVLKDGSTLSAKKIVSSVDEGKLPHQQIQQRYLLVKGDCQQLFQEDGFFAALDASLIHFSPFSISENFGNSVQAKLYGSGSGDCPEGYCIWYLKTLNDSPCNEVFNLATKKLCSFSGCDDLEIIVQVDETLNQLRHIDYDDTLHSAKSLFYEILGQNNTFLQREGLFDEDDE", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the Rab GDI family."}
+{"protein": "MVFRIASSPYTHNQRQTSRIMLLVLIAALPGIAAQTWFFGWGTLFQIVLAAITALVAEAIVLRLRKQSVASHLQDYSALLTGLLLAVSIPPLAPWWMVVLGTGFAIIIAKQLYGGLGQNPFNPAMIGYVVLLISFPVQMTSWLPPYEIAATTPDMLDTLRMIFTGHTASGGDMTLLRIGIDGISQATPLDTFKTSLRAGHSVEQIMQYPIYSGALAGVGWQWVNLAWLVGGVFLLWQKAIRWHIPVSFLLTLALCAALGWLFSPATLASPQLHLLSGATMLGAFFILTDPVTASTTNRGRLIFGALAGVLVWLIRSFGGYPDGVAFAVLLANITVPLIDYYTRPRVYGHRKG", "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": "MAMATHFTFPFNYVVSEGSHGRRSFVRKLVRAVASGDSVAPAISEESKVKLGGSDLKVTKLGIGVWSWGDNSYWNDFQWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLLGRFIRERKERYPGAEVSVATKFAALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLWGNEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRGRIYTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLASEIKPVVGFPVEYL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule. SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily."}
+{"protein": "MSKKYSEENTSSIPLTDLTSPSTGETSSQQQRQRASQQQPPQQPESNTATGSRWSNFVDSFKPAIENEKLAMRYRDANADVEEDAGGYYNSTDQLTEIQRININSSKSNLKRKLKNRHLQMIAIASSIGSGLLIGTGGALATGGPGGILIAWILSGISILCTIQAMAELAVTFPVSGGFNVLFSRFIDPSVGFSVAWNYVLQYLVLLPLELVAASMTIQYWNTDINPDVWVIIFYVTVTSINFFGVRLYGEVEFILSSLKVIAVVGFIILSIVLAAGGAPNGVHHGTKYWHDPGAFANGFKGVSSTFITAAFSFAGTELTGLTSAEAENPRKALPKACKQVFWRILLFYVVSIILITFLVPYDNPRLLGASDVSASPFVIAIQDGGISGLASVMNSVILISVISVGSSSVYATSRTLVSLAEQNLAPKICGYVDRAGRPLVAILITNVFGLLSFIAASGKEDEVFTWLLSISGLSSIFTWLCICISHIRFRRALHVQGRNTDELTFVSQTGVIGSWFGILLNVLVLVAEFWLAIFPLGEKSNAKSFFETYLGFVILIIFYFGHKLWRNNWILFIRSRDIDIDSGRRETDLEALKRELQEEREVLRNKPFWYRAYHFWC", "text": "FUNCTION: Amino-acid permease that is able to transport phenylalanine (PubMed:21764911, PubMed:28028545). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family."}
+{"protein": "MTFLLSRTFISLTLRPSCSISMANLTTNAKTRLRGVVFDMDGTLTVPVIDFAAMYRAVLGEDAYKRIKAESPSGIDILHHIESWSPDKQQKAYEIIADYEKQGIDKLQIMPGTAELCGFLDSKKIKRGLITRNVQKAIDIFHQRFEVIFSPALGREFRPYKPNPDPLLHICSTWDIQPNEVMMVGDSLKDDIACGKRAGAFTCLLDETGRYGPDDFSVSGLQPDFKVDSLSKIQNLLETNFDLNP", "text": "SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP family."}
+{"protein": "NLYQFKNMIHCTVPSRPWWHFADYGCYCGRGGKGTPVDDLDRCCQVHDNCYEKAGKMGCWPYFTLYKYKCSQGKLTCSGGNSKCGAAVCNCDLVAANCFAGARYIDANYNINFKKRCQ", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that shows several activities. It shows strong anticoagulant activity, probably by binding to coagulation factor Xa (F10) and inhibiting the formation of the prothrombinase complex (PubMed:15922780), shows direct hemolytic action, causes neuromuscular blockade with a gradual contracture and a decreased sensitivity to ACh and KCl, abolishes twitches evoked by indirect stimulation earlier than those by direct stimulation (in the mouse phrenic nerve-diaphragm preparation), and causes myonecrosis when injected intramuscularly (PubMed:3615669). 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": "MSPPQTTLPVTEAGLVPLLQPYGPYVLVRKLAEGGMAEIFLAKLLGADGFERNVVIKRMLPHLTNNPDFVEMFRDEARLAAKLAHPNIVQIQELGFAEGCYYICMEYLAGEDFSTTLRLAGRKRHYVPLPVVLRVLIDAARGLHFAHEFTNEAGQPLNVVHRDISPSNLYLTYQGQVKVLDFGIAKAESRLVNTRTGVVKGKYMYMAPEQARGKEVDRRADIFALGVSLYEALTHVRPFSRENDLAVLNALLQGELKPPRELRPDLPEELEAILLKAMAFKPEDRYPTAEAFADALETFLSEHLSGSGAMPLGAFLKGHFGEERFTERSRIPTLATLTATYGGAAAGAQGQAPGAEPHGTNLYGVLAREGDATSAQRPGMSMRPSSPGVPAHGAASRGSTSPESAPTAGGRRWRTLAVGLAGGLMLAAAGIVGYRQWMTTPASVSLVPATVPVVEAVAPEAAAAQVGAPMEAVAPVGAAAQAGSLTDAVANGAGGDVGETDSAQLSVDAAGVTETDEAGLAGAASDVEAEADEEGADAAPVRSKKASSQKRVTLGIDDVQRVVSRGRARITTCFERYKADLPSSQGEVQVQLTIVSSGKVRAGTRGPLASSGVGRCLEAQAERLRFPPHRDQEVTVVMPFSWRVTQ", "text": "FUNCTION: Essential for growth. Interacts with MglA to control social gliding motility. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family."}
+{"protein": "VDFNVPLKEGVVKDPTRIAGSIPSIKKILETNPRGLVLMSHLGRPDGQRVEKHSLKPVLPKLEELLGTKVTFLNDCVGKDVEEAVKSSRNGEIILLENLRFHIEEEGKAVDAAGNKVKADPKAVKEFRKSLTNLGDLFFNDAFGTAHRAHSSMVGVDHKIRVAGYLLKKELEYFSKALESPTLPFCVVLGGAKVKDKIQLINSMLDNVNEMIIGGGMAFTFLKRLHNLEIGNSLFDEEGYKIVDELLEKAKKKNVKIHLPVDFLCGDSLEANANTAIHDLQSGIPKGWIGLDAGPKTIALNAEVIARANTIVWNGPQGRFEVDKFRNGSSDLLKKVIERTKTGATSIIGGGDTVNLVQQEKASNKVSHVSTGGGAS", "text": "SIMILARITY: Belongs to the phosphoglycerate kinase family."}
+{"protein": "MSARPFSTPFDRERRVRSTLKKVFGFDSFKTPLQESATMAVVKGAEDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRTKLLYITPEMAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVFAALHLKQPVASFKTPCFRANLFYDVQFKELIPDVYGNLRDFCLKALGQKAENGSSSGCGIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKELAKLQEKRGNKPSDKATLLAFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNPAAITKKLDALERSSSWSKTCIGPSQGNGFDPELYEGGRRGYGGFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMSLRKGKEPKIEEFTPPDEDCPLREASSRKIPKLTVKAREHCLRLLEEALISNHQAAGSTHGADLQAKAVELEHETFRNAKMVNLYKASVLKKVAEIHKASKDGQLYDMESGTKSCGAAAEFSEPSDYDIPPTSHVYSLKPKRVGAGFSKGPCSFQTATELLGKSHSQKQAPEAMLEGGQEPPGWVCDLQDEDRSKPHPGYQEKALGSSVNCGDPSPEKKTKGSSQGSAKARASKKQQLLATAARKDSQNITRFLCQRTESPPLPASVPRSEDASPSCGDVPGKCTQEVGAQGHLVAVFQTEGPRERPSTCSLRDQSFPEGQPSPLKETQAEKRPRPQQGNPERRAQKRLRPSTKSSILAEAKDSTLASDRSTENKVAQEPCQLSASGTSLREAADIVVRHLTPFYKEGRFISKDLFKGFARHLSHLLAQQLSPGRSVKEEAQSLIKQFFHNRARCESEADWHSLRGPQR", "text": "FUNCTION: DNA helicase that plays an important role in DNA replication, transcription and repair. Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability. Associates also with POLR1A and enforces the stability of ribosomal DNA arrays. Plays an important role in mitotic chromosome separation after cross-over events and cell cycle progress. Mechanistically, removes RAD51 filaments protecting stalled replication forks at common fragile sites and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination. SUBCELLULAR LOCATION: Nucleus, nucleoplasm Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks. SIMILARITY: Belongs to the helicase family. RecQ subfamily."}
+{"protein": "MAVTAFNTLKLVSSSLDPIPSVSCSSYSFSLIYVGSPYKRCLKQSCSVRAMTSSSSAASSSSSSFGSRMEESIRKTVTENTVVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLGPQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDLELMLAEANGKNGQS", "text": "FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. Can assemble a [2Fe-2S] cluster, but cannot transfer it to an apoferredoxin. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily."}
+{"protein": "MTELRDETPLFHKGEIVLCYEPDKSKARVLYTSKVLNVFERRNEHGLRFYEYKIHFQGWRPSYDRCVRATVLLKDTEENRQLQRELAEAAKLQIRGDYSYKGTPDKPSAKKKRGGKAAHVEEPIVVPMDTGHLEAEHEMAPTPRAAGNRTRDNSGGKRKEKPPSGDGRLKGNRGRQTETFYNNAINDVSVYNHVPQEDRIMMRVSERLRELIEYDRNMIKVLGKQHALPARVPIVTIMENFVKQQAVELAISIKQDSSRARNTQSRNARMEREYDRVMSTVCMLKEVVDGLRIYFEFHVDDHLLYTEEKEYVHNYLTDDNMRNCSLILNKSYEYINPSGDTELIGLDGTPVVEGSGDTNGQIGVINIGGPEYEKQLQKCLLYIVTASGKNTAQAYERTSPYTAAYKLPVEMRGFLNETFKWRLLSAESPPEKSMVFGAPHLVRLMIKMPMFLNASPISNKKLEDLLPHLDAFINYLENHREWFDRENFVNSTALPQEDLQRELLDSLDGIAA", "text": "FUNCTION: The MSL proteins are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). Mle, msl-1 and msl-3 are colocalized on the X chromosome. Each of the MSL proteins requires all the other MSLs for wild-type X-chromosome binding. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Msl-3 is associated with hundreds of discrete sites along the length of the X chromosome in males and not in females, and is also associated with 10-20 autosomal sites in males."}
+{"protein": "MPSDREGLWMLAAFALMTLFLLDNVGVTQAKSFDDVRCKCICPPYRNISGHIYNRNFTQKDCNCLHVVDPMPVPGNDVEAYCLLCECKYEERSTNTIRVTIIIFLSVVGALLLYMLFLLLVDPLIRKPDPLAQTLHNEEDSEDIQPQMSGDPARGNTVLERVEGAQQRWKKQVQEQRKTVFDRHKML", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM9 family."}
+{"protein": "MISTTSLFAPVDQDLRLLTDNLKRLVGARHPILGAAAEHLFEAGGKRVRPAIVLLVSRATLLDQELTARHRRLAEITEMIHTASLVHDDVVDEADLRRNVPTVNSLFDNRVAVLAGDFLFAQSSWYLANLDNLEVVKLLSEVIRDFAEGEILQSINRFDTDTDLETYLEKSYFKTASLIANSAKAAGVLSDAPRDVCDHLYEYGKHLGLAFQIVDDILDFTSPTEVLGKPAGSDLISGNITAPALFAMEKYPLLGKLIEREFAQAGDLEQALELVEQGDGIRRSRELAANQAQLARQHLSVLEMSAPRESLLELVDYVLGRLH", "text": "FUNCTION: Possible role in synthesis of the nonaprenyl side chain of plastoquinone or in synthesis of other prenyl chains such as undekaprenyl pyrophosphate. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MSILRGSLRGVLAPNASVVFRSRLPPQLTSALLCPLRSLSGTPLAEPDGKVTRKMSENGTCNRILTLDSMNPCIQKVEYAVRGPIVIRAVELEKELQQGVKKPFTEVIKANIGDAHAMGQKPVTFLRQVSAICLYPELMNDNKFPEDVKQKAARILQACGGHSIGAYSASQGIEVIRQDVAKYIERRDGGILSDPNNIYLSTGASDSIVTMLKLLVSGQGKSRTGVMIPIPQYPLYSAALAELDAVQVNYYLDEENCWALDINELRRALAEARKHCDPKVLCIINPGNPTGQVQSRKCIEDVIRFAAEENLFLMADEVYQDNVYAKGCAFHSFKKVLFEMGPKYSETLELASFHSTSKGYMGECGFRGGYMEVINMDPAVKQQLTKLVSVRLCPPVPGQVLLDVIVNPPKPGEPSYKQFISEKQAVLNNLAEKARLTEEILNQAPGIRCNPVQGAMYSFPRIHIPEKAIKLAQAEGQAPDMFFCMKLLEETGICVVPGSGFGQREGTHHFRMTILPPTDKLKSLLERLKDFHQKFMDEYS", "text": "FUNCTION: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily."}
+{"protein": "MRSRALLFLLFVLLPMLPAPPAGQPSGRRRGQAGCGGGFWGDRVDSQPFALPYIHPTNPFASDIPAAAGTGARPRQPIRPLGSAWRDQSQRPAASTRRRPAPAGASPLTAVAPAPDTAPVPDADSRGAILRRQYNLSTSPLTSTIATGTNFVLYAAPLSPLLPLQDGTNTHIMATEASNYAQYRVVRATIRYRPLVPNAVGGYAISISFWPQTTTTPTSVDMNSITSTDVRILVQPGIASELVTPSERLHYRNQGWRSVETSGVAEEEATSGLVMLCIHGSPVNSYTNTPYTGALGLLDFALELEFRNLTPGNTNTRVSRYSSSARHKLRRGPDGTAELTTTAATRFMKDLHFTGTNGVGEVGRGIALTLFNLADTLLGGLPTELISSAGGQLFYSRPVVSANGELTVKLYTSVENAQQDKGVAIPHDIDLGESRVVIQDYDNQHEQDRPTPSPAPSRPFSVLRANDVLWLSLTAAEYDQTTYGSSTNPMYVSDTVTFVNVATGAQGVSRSLDWSKVTLDGRPLTTIQQYSKTFYVLPLRGKLSFWEAGTTKAGYPYNYNTTASDQILIENAAGHRVCISTYTTNLGSGPVSVSAVGVLAPHSALAALEDTADYPARAHTFDDFCPECRALGLQGCAFQSTVGELQRLKMKVGKTREY", "text": "FUNCTION: [Isoform Capsid protein]: Forms an icosahedral capsid with a T=1 symmetry and a 34 nm diameter. The capsid is composed of 60 copies linked to each other. Binds to the 5' end of the genomic RNA to mediate genome encapsidation (By similarity). Binds to heparin surface proteoglycans (HSPGs) to mediate viral entry. Additionally, the interactions with host ASGR1 and ASGR2 facilitate viral infection of hepatocytes (By similarity). Inhibits IFN production by blocking host TBK1-induced IRF3 phosphorylation (By similarity). The nuclear form probably modulates host gene expression (By similarity). FUNCTION: [Isoform Secreted protein ORF2]: Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry. SUBCELLULAR LOCATION: [Isoform Capsid protein]: Virion Host cytoplasm Host endoplasmic reticulum Host Golgi apparatus Host cell surface Host nucleus Note=Translation from the internal AUG codon disrupts the signal sequence, producing a cytoplasmic protein that is responsible for virion assembly (By similarity). Shuttles between cytoplasm and nucleus (By similarity). This isoform is found in quasi-enveloped virions (By similarity). SUBCELLULAR LOCATION: [Isoform Secreted protein ORF2]: Secreted Note=Cotranslationally translocated into the ER. SIMILARITY: Belongs to the hepevirus capsid protein family."}
+{"protein": "MTTTEEAPKSPLFEAIDKNDTEAALALLKTKEQAAQRDPSGMSVLAAAAYRGNLTLVEKAIELKCDVNDKTDGTLYTPLMFAALSGKQDVCRLLMDSGARMYLVNGIGKTASELAAFVGHHECVAIINNHITIDVIEDLLRPKVNGKYEGAEEYPDELAVFIHSLCGSHEIHPVKIIFRFSKYPDSLKYKKKILYVIDRVFEKQLRCKESNEIMSLKLWLILFSMRETSKFVESNKEKSPEEASLQYAKLISTWQEGDETRRALDVMLRNAVASFPYKHSLLHDTLQKALQKSQIGERPSAYEYIVQALFGQRIAAVCQFCSVCGHPGAKKRCTQCKLAYCSQECQKFDWPIHKKVCSFLKTRQEVSPTDETAMSLDDIQAQIAKIDV", "text": "FUNCTION: May be involved in the trafficking and dendritic transport of signaling proteins, such as the receptor-type guanylate cyclases gcy-12 and daf-11, to the cilia. In ciliated sensory neurons, required for the calcium flux to the cytoplasm in response to onset and removal of a nitric oxide (NO) stimulus and is thereby required for the behavioral avoidance response to NO-producing organisms like P.aeruginosa (PubMed:30014846). SUBCELLULAR LOCATION: Cell projection, cilium."}
+{"protein": "MAVDMFIKIGDVKGESKDKTHAEEIDVLAWSWGMSQSGSMHMGGGGGAGKVNVQDLSFTKYIDKSTPNLMMACSSGKHYPQAKLTIRKAGGENQVEYLIITLKEVLVSSVSTGGSGGEDRLTENVTLNFAQVQVDYQPQKADGAKDGGPVKYGWNIRQNVQA", "text": "FUNCTION: Required for assembly of the protein secretion apparatus HSI- I. Actively secreted during chronic infection of cystic fibrosis patients. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the hcp1 family."}
+{"protein": "MCQNKINTNNTMTIKSNKKLSYSVKKLLQKIFKQQQRVEEEQNLKNALKANSLESLESMENSRNADLESASICASLESCENEANERLSQSCEIEDYDFEQLPTVPVHFVRTAHGTFFWTAVSDLPADNDLVEPLYCSTSNAIAIPQDRWVQA", "text": "FUNCTION: Part of the Notch signaling pathway. SIMILARITY: Belongs to the M4-like protein family."}
+{"protein": "MAEEQARHVKNGLECIRALKAEPIGSLAIGEAMAAWSEISDNPGQERATYKEEKAGGSGLSKPCLSAIGSTEGGAPRIRGQGSGESDDDTETLGIPSRNLQASSTGLQCHYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSEGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSETPIKKGHRREISLIWDGDRVFIDRWCNPMCSKVTLGTIRARCTCGECPRVCEQCRTDTGVDTRIWYHNLPEIPE", "text": "FUNCTION: Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Blocks the type I interferon signaling pathway by interacting with host TYK2 and thereby inhibiting downstream STAT1 and STAT2 phosphorylation. Moderately affects the type II interferon signaling (By similarity). SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the paramyxoviruses V protein family."}
+{"protein": "MFDYLENEEVALDELKQMLRDRDPNDTRNQFKNNALHAYLFNEHCNNVEVVKLLLDSGTNPLHKNWRQLTPLGEYTNSRHGKVNKDIAMVLLEATGYSNINDFNIFTYMKSKNVDIDLIKVLVEHGFDFSVKCEKHHSVIENYVMTDDPVPEIIDLFIENGCSVIYEDEDDEYGYAYEEYHSQNDDYQPRNCGTVLHLYIISHLYSESDSRSCVNPEVVKCLINHGINPSSIDKNYCTALQYYIKSSHIDIDIVKLLMKGIDNTAYSYIDDLTCCTRGIMADYLNSDYRYNKDVDLDLVKLFLENGKPHGIMCSIVPLWRNDKETISLILKTMNSDVLQHILIEYITFSDIDISLVEYMLEYGAVVNKEAIHGYFKNINIDSYTMKYLLKKEGGDAVNHLDDGEIPIGHLCKSNYGRYNFYTDTYRQGFRDMSYACPILSTINFCLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNIELLNMLLCHKPTLDCVIDSLREISNIVDNAYAIKQCIRYAMIIDDCISSKIPESISKHYNDYIDICNQELNEMKKIIVGGNTMFSLIFTDHGAKIIHRYANNPELRAYYESKQNKIYTWKYMILFPNAIVKHNKIHKNIESVDDNTYISNLPYTIKYKIFEQQ", "text": "FUNCTION: Substrate-specific adapter of SKP1-containing E3 ubiquitin- protein ligases which mediate the ubiquitination and subsequent proteasomal degradation of host target proteins. Prevents activation and subsequent nuclear localization of NF-kappa-B in infected cells, by targeting NF-kappa-B RELA subunit to the SCF E3 ligase complex (By similarity). SIMILARITY: Belongs to the orthopoxvirus OPG023 family."}
+{"protein": "MKTSVVILAMSYITSIFANNSYDFCDGEFAISEKDDKCGFSFNPCTLYKQIQKEYSNCVILRFYLKAISNMLESICDNNKRCLPFSIDSLYRPLYNREQFKHKHHHTLYALFRNCLYLVNPIYFKEYQDALACNQLDVCYFLIRRTVCPKYGVTKYIECLKKRCEDRFDEKELAIFICDSETFVNIKLEIDACRKICPADCTLDICKIYSLDFWERRDLLKAIFDYHYCHVLSSDNTRDEIIKKIEEIYLNGTERDIKFTSFIIYQLFTDLVACKSSDKNIKRILDLICLYEKKDKCPSGVMVMIEFFVKVCSYQC", "text": "SUBCELLULAR LOCATION: Spore, perispore."}
+{"protein": "MPQFQTWEEFSRAAEKLYLADPMKVRVVLKYRHVDGNLCIKVTDDLVCLVYRTDQAQDVKKIEKFHSQLMRLMVAKESRNVTMETE", "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). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP (By similarity). The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SRP9 family."}
+{"protein": "MINCLIVDDDKKLLQYVSSHLERESIQTHTFTSGEASLDFLENKNVDIAIVDIMMSGMDGFELCQTLKDDYHIPVIMLTARDALSDKERAFLSGTDDYVTKPFEVKELLFRIKAVLRRYQINADNELQLGNLILNQSYMEITVGSKTMNLPNKEFQLLFLLASNPKHIFTRDDIIGKIWGFDYEGDDRTVDVHIKRLRQRLSKLKSSVSIQTVRGQGYRVDQNV", "text": "FUNCTION: Member of the two-component regulatory system HssS/HssR involved in intracellular heme homeostasis and tempering of staphylococcal virulence. Phosphorylated HssR binds to a direct repeat sequence within hrtAB promoter and activates the expression of hrtAB, an efflux pump, in response to extracellular heme, hemin, hemoglobin or blood (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MKTLLLTFLVVTIVCLDLGYTLICHQVHGLQTCEPAQKFCQKRTTMFFPNHPVLLMGCTYNCPTERYSVCCSTDKCNK", "text": "FUNCTION: This three-finger toxin binds and inhibits the nicotinic acetylcholine receptor (nAChR). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily."}
+{"protein": "MLPAERKRRIVELVSDSDGRSVESLSDHLGYSKATIRRDLRELEDRGLIERSHGGAVPVTSVGREQTYGQKEVQNLEGKRAIADRAVEELAEGQVVFFDAGTTTMEVARKVPKDGTILGVTNSPRLAIELNEEDNEVKLTGGTLRRRTKALVGPTAESFMERTNFDLLFLGTNALDVESGLTTPNEDEARMKELMVEKAAKVVLVADLSKLGRRSFVQFASLEEIDLFITDGTLDADSREEIESAGVTVVDGVAR", "text": "FUNCTION: Transcriptional repressor of genes encoding both fructose and glucose metabolic enzymes such as phosphofructokinase (PFK) or 2-keto- 3-deoxy-D-gluconate kinase (KDGK) during growth on glycerol. Required for the glycerol-mediated repression of pfkB-specific transcripts, but not needed for the high-levels of the pfkB-specific transcript present when cells are grown on fructose."}
+{"protein": "MKSFLQLVVVVAALLSVSTADFCSQWRLSKAGKYVIYNNLWNKNAAASGSQCTGVDKISGSTIAWHTSYTWTGGAATEVKSYSNAALVFSKKQIKNIKSIPTKMKYSYSHSSGTFVADVSYDLFTSSTASGSNEYEIMIWLAAYGGAGPISSTGKAIATVTIGSNSFKLYKGPNGSTTVYQPPGLPLST", "text": "FUNCTION: Secreted XEG1-like protein that has lost enzyme activity but binds to host soybean apoplastic glucanase inhibitor protein GIP1 more tightly than does XEG1, thus it outcompetes XEG1 for GIP1 binding and frees functional XEG1 to support P.sojae infection (PubMed:28082413). With XEG1, is required to elevate apoplastic sugar during P.sojae infection (PubMed:28082413). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family."}
+{"protein": "MIKIKRKTAPPPVEQDSDSDSSFDEEEPQDLEVQEGPVTDSSDEEAASSSKKTAKQGEASEDLKEEDDDDDEEENDDDDEEEDDDDDDDKKTRIPVLNPLSWMRNKEQRLALYKKMKKEKHKKKMQERRARRKAGVPANPGHTIESLREKDQTEVANLNDSDNEELQKELQLDDFSSYFERSYEPKVLITFADNPVTKTRKFGLELSRIFPNALVKIRNKSSVKKICKSAEREEFTDVVIVNEDRRKPNGLLVIHLPNGPTAHFKLSNVKLTSDIKRDHKEITKHRPEVILNNFTTRLGLTVGRMLGALFHHDPEFRGRRAVTFHNQRDYIFFRHHRYEFTKEGKRVKLRELGPRFTLKLRSLQEGTFDSKTGDYAWIISNKRHAMESRRRFFL", "text": "FUNCTION: May be required for ribosome biogenesis. SUBCELLULAR LOCATION: Nucleus, nucleolus."}
+{"protein": "EQLIELVGPWKTVYIVHFNGET", "text": "FUNCTION: Binds the chemical odorant, 2-isobutyl-3-methoxypyrazine. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MSKHAASSAKRFSLLALGLMFVGGIVFVWAVDFGIKTTNTLEFCTSCHTMQTNFEEYKESLHYKNTSGVQATCADCHVPKELGPKLVTKIVAAKDVYHEVMGTIDTPEKFEARRWYLANLVWKRLEASDSRECRSCHDYADMDLSEQSRSARSRHSAAQDKGQTCIECHKGVAHHEPTEPDDAS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the NapC/NirT/NrfH family."}
+{"protein": "MTPVRMQHSLAGQTYAVPLIQPDLRREEAVQQMADALQYLQKVSGDIFSRISQQVEQSRSQVQAIGEKVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFTGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKDFPVCVSTKPEPEDDAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISKREQLEQQVPENYFYVPDLGQVPEIDVPSYLPDLPGIANDLMYIADLGPGIAPSAPGTIPELPTFHTEVAEPLKVDLQDGVLTPPPPPPPPPPAPEVLASAPPLPPSTAAPVGQGARQDDSSSSASPSVQGAPREVVDPSGGRATLLESIRQAGGIGKAKLRSMKERKLEKKKQKEQEQVRATSQGGHLMSDLFNKLVMRRKGISGKGPGAGEGPGGAFARVSDSIPPLPPPQQPQAEEDEDDWES", "text": "FUNCTION: Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T- cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T- cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). SUBCELLULAR LOCATION: Early endosome membrane Recycling endosome membrane Late endosome Cytoplasmic vesicle, autophagosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localization to the endosome membrane is mediated via its interaction with WASHC2. SIMILARITY: Belongs to the WASH1 family."}
+{"protein": "MLSYISAAFQSPSPDEGVQQRPPRYVGEDTTPTSRREILGWYSYGIAAEVFAVCGVGSFLPLTLEQLARERGTLQTSRLPCVGPSAGNSTNATEHGQCVVPVFGLEINTASFAMYTFSLAVLIQALTLISFSALADYENNRKTLLMVFGFAGALASMLFVFIAPPLFVIGSILVVVGVTCLGSSFVVLNSYLPVLVANDPSLQEGKADDGTEMSSFDRDEGDSEGNPWGKDHTDNDSLDGLQPSDQPQSSLEGGMGTKAPLSSSPELQLSTKISSRGIGLGYCAAVFVQIISIIMLLTLSKTKLAKVSATLPMRFVLLLVGIWWGAFTLVTRNLLKTRPGPRLDTVSTKGTGRWRAWLRLVGFAWKSLWETVKVVSKLREVLIFLVAWFLLSDAMATVSGTAILFARTELKLSTPLIGLLSITATLSGMTGAFLWPQVSRYFRLQPSHTIILCIALFEMIPLYGLLAYIPFIKNWGVFGLQQPWEIFPLAIVHGVVSGGLASYCRSFFGLLIPPGSEAAFYALYAATDKGSSFIGPAIVGGIVDATGQIRSGFFFMAILIVLPIPLVWMVNADKGRREGLAMAETLGKSHGGPAEDAQEAEGLLARE", "text": "FUNCTION: Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Vacuole and punctate structures. SIMILARITY: Belongs to the ATG22 family."}
+{"protein": "MKIQQLIVFLFAVVLIDARTPKRYSELDIVMSTCTTFIGKYGTVCTSTGKRSTNWNCYCKTDAGFGTISDCLVRGFNNNTNIISKFTESCNMTESKFHAKYDKIQAEFKTNGTEYAKMTTKSSSGSKTSASASKSSKSTGSSNASKSSTNAHGSNSSTSSTSSSSSKSGKGNSGTSTTETITTPLLIDYKKFTPYKDAYQMSNNNFNLSINYGSGLLGYWAGILAIAIFANMIKKMFPSLTNYLSGSISNLFRKHLFLPATFRKKKAQEFSIGVYGFFDGLIPTRLETIIVVIFVVLTGLFSALHIHHVKDNPQYATKNAELGHLIADRTGILGTFLIPLLILFGGRNNFLQWLTGWDFATFIMYHRWISRVDVLLIIVHAITFSVSDKATGKYNTRMKRDFMIWGTVSTICGGFILFQAMLFFRRKCYEVFFLIHIVLVVFFVVGGYYHLESQGYGDFMWAAIAVWAFDRVVRLGRIFFFGARKATVSIKGDDTLKIEVPKPKYWKSVAGGHAFIHFLKPTLFLQSHPFTFTTTESNDKIVLYAKIKNGITSNIAKYLSPLPGNTATIRVLVEGPYGEPSSAGRNCKNVVFVAGGNGIPGIYSECVDLAKKSKNQSIKLIWIIRHWKSLSWFTEELEYLKKTNVQSTIYVTQPQDCSGLECFEHDVSFEKKSDEKDSVESSQYSLISNIKQGLSHVEFIEGRPDISTQVEQEVKQADGAIGFVTCGHPAMVDELRFAVTQNLNVSKHRVEYHEQLQTWA", "text": "FUNCTION: Ferric reductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)- salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake (By similarity). Involved in maintenance of cell wall integrity (CWI), mitochondrial function, and interaction between the pathogen and the host. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ferric reductase (FRE) family."}
+{"protein": "MGILIALIPAIAWGSIGLISGRMGGTARQQTLGMTMGALVFGLALWAVEQPTLTSKIWLIGIVSGLFWSIGQGQQFTSMKAVGISRTTPISTGMQLVANALAGVLLFNEWHGNMYWIGSASVIVLIAGAVLTSLTDKTDPNRSASENWGVGIRALILSTIGYAGYTIVVHYGNVNAQAVVMPQAVGMLLGALIWSFKDKPWVVKATYRNIVTGLVWGIGNLFMFMAMAQIGQAVAYSLSQMGIVISTFGSIYLLGEHKTKREMVYVVIGSILVIVGGVALSLMKA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GRP transporter (TC 2.A.7.5) family."}
+{"protein": "MAQGNQQIDNQVLHHLRQKFPEVPEDVVCECVLQNKSDLAACCEYLTKVSPRFLYSEGSQSLTDLRNHMTQLNLGVSQNTHGAVQRDAVGMNGSRTLAPSVSDGPLNVPSALSEFYQPETPSVPTHTPASLSMESTRKPQPPQHLGLYQVGGKGHAPPQAPRFNPITVTLAPNTGRNTPTSLHIHGGPQSGLNSPNSIYIRPYVTQPGSTRQVQCRAQYSPTSQPAQQIYQITHPAAPQSSWSQHQTSHVYMPISSPTNTQAPSIPSAVASQAVSSSPLPSSGSSFSQYNIQNISTGPRKNQIEIKLESPQRGSGSSSLLRSSSAPRSACSSTSSSCPSSCTSLASSSGSSTPISIGGAGLSRSQPTVYISPSPPTAATAPSEDCALVPNTPRSQPKIYFSANTSADDGGGRNPPTVYISANPALQGPAGLRALGSQMSMGPAYIHHHPPKSRPSVGAGGTATSPRVVVTQPNTKYTFKITVSPNKPPSVSPGVVSPTFEPNNMLSLPADHHYAEPEISQPDPMRDKAVEPRRLSMGADDAAYTQALLVHQRARMERLWHELELKKRKLEKLKEEVNEMESDLTRRRLQRSNAFCQIPSIEEMQQLRCKNRLLQIDIDCLTKEIDLLQTRGPDFNPIAIHNFYDNLGFLGPVPPKPLKGPTKAEVSRTDAGVRVLSEPEEDDGVQWSCTACTFLNHPALNRCEECEFPRNF", "text": "FUNCTION: Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains. The RanBP2-type zinc finger (NZF) specifically recognizes Lys- 63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1 and RIPK2: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 (By similarity). Involved in heart development (PubMed:20493459). SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Cytoplasm, cytosol Note=Following IL1 stimulation, translocation occurs from the membrane to cytosol."}
+{"protein": "MKKTTITLFVLTSVFHSGNVFSRQYNFDYGSLSLPPGENASFLSVETLPGNYVVDVYLNNQLKETTELYFKSMTQTLEPCLTKEKLIKYGIAIQELHGLQFDNEQCVLLEHSPLKYTYNAANQSLLLNAPSKILSPIDSEIADENIWDDGINAFLLNYRANYLHSKVGGEDSYFGQIQPGFNFGPWRLRNLSSWQNLSSEKKFESAYIYAERGLKKIKSKLTVGDKYTSADLFDSVPFRGFSLNKDESMIPFSQRTYYPTIRGIAKTNATVEVRQNGYLIYSTSVPPGQFEIGREQIADLGVGVGVLDVSIYEKNGQVQNYTVPYSTPVLSLPDGYSKYSVTIGRYREVNNDYIDPVFFEGTYIYGLPYGFTLFGGVQWVNIYNSYAIGASKDIGEYGALSFDWKTSVSKTDTSNENGHAYGIRYNKNIAQTNTEVSLASHYYYSKNYRTFSEAIHSSEHDEFYDKNKKSTTSMLLSQALGSLGSVNLSYNYDKYWKHEGKKSIIASYGKNLNGVSLSLSYTKSTSKISEENEDLFSFLLSVPLQKLTNHEMYATYQNSSSSKHDMNHDLGITGVAFNSQLTWQARGQIEDKSKNQKATFLNASWRGTYGEIGANYSHNEINRDIGMNVSGGVIAHSSGITFGQSISDTAALVEAKGVSGAKVLGLPGVRTDFRGYTISSYLTPYMNNFISIDPTTLPINTDIRQTDIQVVPTEGAIVKAVYKTSVGTNALIRITRTNGKPLALGTVLSLKNNDGVIQSTSIVGEDGQAYVSGLSGVQKLIASWGNKPSDTCTVFYSLPDKNKGQISFLNGVCK", "text": "FUNCTION: Involved in the export and assembly of the SefA fimbrial subunit. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family."}
+{"protein": "MEGSKTSSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLATAQVKPGETQEEEANPGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMHEDDSEQLRMELRELALEEERLIQELEEVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK", "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. 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. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (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 Note=Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells. SUBCELLULAR LOCATION: [Beclin-1-C 37 kDa]: Mitochondrion. SUBCELLULAR LOCATION: [Beclin-1-C 35 kDa]: Mitochondrion Nucleus Cytoplasm. SIMILARITY: Belongs to the beclin family."}
+{"protein": "MQGNMRLWMSVLTLCLSMLICLGTFAEAYPSKPDNPGEDAPAEDMAKYYSALRHYINLITRQRYGKRSSPETMLSDVWWRENTENIPRSRFEDPPMW", "text": "FUNCTION: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle. SIMILARITY: Belongs to the NPY family."}
+{"protein": "MLYLIGLGLSYESDITVRGLETVKKCKRVYLEAYTSILMAANQESLEKFYGREIILADRELVETGSDDILKDADKEDVAFLVVGDPFGATTHTDLVIRARELGIKVETIHNASVMNAVGACGLQLYQFGQTVSLVFFTDSWKPDSFYGKIMENRKIGLHTLLLLDIKVKEQSIENMARGRLIYEPPRYMDIATAAQQLLEIESIRQEQAYTPNTPCVAISRLGSPTQTFKAGTLQELSEYDSGEPLHSLVMLGRQVHELELEYLYQFVDDKEKFKKFVEQDQEFFKPAPYVPPEDVDSE", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the diphthine synthase family."}
+{"protein": "MATAVAEELLLAEERMLAALAYLQCAVGCAVLARNRETNLAYGRHASPSFRVRVPARAAWVVQELPSLALPLYQYASESAPRLRSAPNCILLAMFLVHYGHRCLIYPFLMRGGKPMPLLACTMAIMFCTFNGYLQSRYLSHWAVYADDWVTDPRFLIGFGLWLAGMLINIHSDHILRNLRKPGDTGYKIPRGGLFEYVTAANYFGEIMEWCGYALASWSVQGAAFAFFTFCFLSGRAKEHHRWYLQKFEEYPKFRKILIPFLF", "text": "FUNCTION: Converts testosterone into 5-alpha-dihydrotestosterone 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": "MEGSTSPKALRVAAISGSLRRGSANTGLIRAAKEICEESIPGMVIDHVDIPDLPLLNTDMEVDDGFPPAVEAFRASVRAADCFLFASPEYNYSISGPLKNALDWGSRPPNCWADRAAAIVSASGGSGGSRSMYHIRQVGVFLDIHFINKPEVFIKAHQPPKKFDSDGNLIDPEIKEELKDMLLSLQAFALRLQGKPANSKHAA", "text": "FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways. SIMILARITY: Belongs to the SsuE family."}
+{"protein": "MPPKFDPNEVKVVYLRCTGGEVGATSALAPKIGPLGLSPKKVGDDIAKATGDWKGLRITVKLTIQNRQAQIEVVPSASALIIKALKEPPRDRKKQKNIKHSGNITFDEIVNIARQMRHRSLARELSGTIKEILGTAQSVGCNVDGRHPHDIIDDINSGAVECPAS", "text": "FUNCTION: Binds directly to 26S ribosomal RNA. SIMILARITY: Belongs to the universal ribosomal protein uL11 family."}
+{"protein": "MEEVDNIIIHTLRQIGCEIPEEIQSLREFTTTVIVQASSKCLHVINEDIDIPSNLPSSMSAKFRVGTMLAAALQDLGYRGEIGYQTFLYSNEKDIRSVFMFLVEHLPKETSLAASEPLGSSVLLNRRVASDLAQRLTLSWTPTFLKKGGVRWKGSKPKTYFREGSASMRRFHACNLKSPQGLTDLTAKISKETKAYYSVIPYVTSQPPCRQDVVPSVLESNSLSVTAVAEWELEWNQSGLSSRLTKEEYLARKRQRLEKKIKDHVLAEMQRVEAGGRAASDLSDIVSSFSDRVSTIESQTQGSRFTRTEKLQFAQDEQKAAAMAGLSESGPPKMDTEEELQKKREQELEALQNKLKDLASSVDEKKSEIKTMNAGLQQTNEQVTATKVQNSEHEESYKVKKRTVDLLPDAENNIAKLQGVVDSSSQRLVNLAQQWETHRTALIDEYRELKVINANKVSETQKKLEEIKSLREKMKEVAEETRGKDDLYKQLVSEYERMSRDVNRSAYTRRILEIVGNIKKQKEEINKILVDTKSVQKEINQLSGKLDRTFTVTDELIFRDAKKDEACRKAYKYLASLHENCKELIQAVEDTGVIMREIRDLEEQIDTESQRNTANNLERITADHKQMKEENATLTKKIKALKSS", "text": "SIMILARITY: Belongs to the CCDC22 family."}
+{"protein": "MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVRLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADAISKSELTKFKIKITSELVSNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCTE", "text": "FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. May play a role in HCV RNA replication. 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 (PubMed:25588830). 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 (PubMed:25588830). SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
+{"protein": "MNDALKTYLKGICWFLLSLVTSSVNDVISKYLGTRLHSFEVAFFRFLFSSIVLLPFVVYYGKSTLKTRHPVIHVLRGLLLFFGMTSWTYGLTIAPVTTATVISFSIPLFTLILAVFILNENIIWQRWVVTVVGFIGLVVMLKPHTKDFNPEILYLILAAISFAMLDIINKKFVVKESMLSMLFYSAIVTAIVSLPVSMEYWITPSSFELTLLFVLGSSGSFILFFLLKAFTMVDATATAPYRYLELVISAIAAYFIFNEFPDKSTAHGAVIIIPATLFIMYSEKKSMSSKHESQ", "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": "MALVRNNSSNGREPVLSPRSLTSPRGLTSPRPLSVQPTPEPVRPLANFPPSIWADRFISFSLDNSQLEAYANALEEPKEAVKSLITDTTIDANTKLKLIYSVHRLGLSYLYPDEIDAELNKLFEKIDLQYYEQVDLYTIAVQFQVFRHHGYKISSDVFKKFKDSTTGTFTDDVTKDVKGMLSLYESAHLRLHGEDILDEALAFTEAHLKKILTTLEGDLARQVNQVLKRPFHTGMPMVEARLYFITHEEDFSSHESVVKLAKVHFNYLQLQQKEELRLVSQWWKDMQFQQSVPYIRDRVPEIYLWILGLYFEPYYSRARIIATKITLFLVVLDDTYDAYATIDEIRSITDAINRWEISAIDQLPEYIKPFYRILLNEYDDLEKEYSKDGRAFSVHASKQAFQEIARGYLEEAEWLHNGYVATFPEYMKNGLITSAYNVISKSALVGMGAIADEEALAWYETHPKILKASELISRLQDDVMTFQFERKRGQSATGVDAYIKEYNVSEEVAIKELMKMIENAWKDINEGCLKPTEVSVALLTPILNLARMIDVVYKFDDGFTFPGKTLKDYITLLFVSPPPSLEN", "text": "FUNCTION: Involved in sesquiterpene lactone biosynthesis. Produces exclusively (+)-germacrene A. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTMHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDTVPLCMSADFPRVGMGSSYNGQDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDPDIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLAPQNVRDDVENDDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEAVTNAVLHEVKREGLPVEQRNEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDVSMPLPFDLTDIVSELRGQLLEAKP", "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": "MSQLVLDLKCLKDKIATNYDIHNNVYGGNGMEPNIIHPSKRFRIVVRLVDFLFCKSDEEFIKGFFCQMIVRNLHCLNSTNGAEEMRLYMSERLFSAHKDDLRLINGQVLDVRIGVWYGIHQSPPIFEIIDFKILSRNDVRDFCEFVKSPLGEKFLNISNS", "text": "FUNCTION: Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere."}
+{"protein": "MESSRSLEHVLSMQGGEDDASYVKNCYGPAARLALSKPMLTTAINSIKLTEGCSSHLKIADLGCAIGDNTFSTVETVVEVLGKKLAVIDGGTEPEMEFEVFFSDLSSNDFNALFRSLDEKVNGSSRKYFAAGVPGSFYKRLFPKGELHVVVTMSALQWLSQVPEKVMEKGSKSWNKGGVWIEGAEKEVVEAYAEQADKDLVEFLKCRKEEIVVGGVLFMLMGGRPSGSVNQIGDPDSSLKHPFTTLMDQAWQDLVDEGLIEEEKRDGFNIPVYFRTTEEIAAAIDRCGGFKIEKTENLIIADHMNGKQEELMKDPDSYGRDRANYAQAGLKPIVQAYLGPDLTHKLFKRYAVRAAADKEILNNCFYHMIAVSAVRV", "text": "FUNCTION: Methylates the carboxyl group of several gibberellins (GAs). Substrate preference is GA9 > GA20 > GA3 > GA4 > GA34 > GA51 > GA1 > GA19 > GA12. No activity with diterpenes abietic acid and ent-kaurenoic acid. SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family. SABATH subfamily."}
+{"protein": "MHALLLLLLLALGSALRSPQPPEARAKLCGHHLVRALVRVCGGPRWSPEATQPVDTRDRELLQWLEQRHLLHALVADADPALDPDPALDPQLPHQASQRQRRSVATNAVHRCCLTGCTQQDLLGLCPH", "text": "FUNCTION: Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
+{"protein": "MAAAGAEAPGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKDMEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFFNDKHNYLSQVKKGKAITLKENHRALKPAVAEYIVKKAKQRIALQRWQDELNRRKTHKGMIFVENTVDLEGPPSDFYYINEYKPAPGISLVNEATFGCSCTDCFFEKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCPNRIVQKGTQYSLCIFRTSNGCGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQLYDNKGITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTINAGEELTFDYQMKGSGDVSSDSIDHSPAKKRARTVCKCGAVTCRGYLN", "text": "FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Associates with centromeric constitutive heterochromatin. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily."}
+{"protein": "MEDSQMDTSSPTESSSEVNFTAEEDKSQETRSAAGVCYCGKERNLNIVELLCATCSRWVHETCVSYQLGKGKLLPFITNYVFVCKNCSASGLESFRKSQATISQMCHCAIANMQQAASRDGRRQIQFSKDKEIIPYIEQYWEAMTTMPRRLTQSWYSTVQRSLVKDVQTLFTYEEHAEHGAMYGLFHQDLRIIKPNYESMSKSGALRLTDDGYTQASLSKNNRQKRKFPGTDSGPTGKKGRPSSDITANVKLPPHGYPLEHPFNKDGYRYILAEPDPHAPFRQEFDESSDWAGKPIPGWLYRILVPHSVLLALHDRAPQLKISEDRLAVTGERGYCMVRATHSVNRGCWYFEVTIEEMPDGAATRLGWGREYGNLQAPLGYDKFGYSWRSRKGTKFTESHGKHYSDAYVEGDTLGFLIELPEEASLDYLPNTFKDRPLVKFKSHLYYEDKDKITETLKNLHILQGSRIEFFKNGQSQGVAFEDIYAGSYFPAISIHKSATVSVNFGPAFKYPEVLVEHKAKGMHDRVEELITEQCLADTLYLTEHDGRLRLDNMGL", "text": "FUNCTION: Transcriptional regulator. Regulates a number of genes involved in wing development including activation of net and bs and repression of rho and kni and controls vein-intervein patterning during wing development. Required for correct expression of a number of homeotic genes including Scr in the first leg imaginal disk and Ubx in the third leg imaginal disk and haltere disks. Required for stabilization of the histone-lysine N-methyltransferase trr and for trimethylation of 'Lys-4' of histone H3. Plays a role in maintenance of transcriptionally active chromatin through down-regulation of histone H1 hyperphosphorylation. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Accumulates on salivary gland polytene chromosomes."}
+{"protein": "MKTKLITRAGYNKLKQELDYLWKEQRPEITQKVSWAASLGDRSENADYTYNKRLLRQIDRRVRFLSKLLPELKIVDYSPQQEGKVFFGAWVEIENEAGEVKKFRIVGPEEIYGDAKDYISIDSPMARALLKKQVDEEFQVHTPTGIKEWFINSIEYEKGEL", "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. GreB releases sequences of up to 9 nucleotides in length. SIMILARITY: Belongs to the GreA/GreB family. GreB subfamily."}
+{"protein": "MSPIENSSSWTLESDLEDLDLDLQDYKPSVPLKKVPNGDIFEASRAGDVDRLRYLVETGVNVNARDRWDSVALYYACLAGHIDSARLLLENGAICSEHTFDGDRCHYASLNLRIRKLLKAFEARPPPLAPLQASLRDTFLGCCHNRDYLQQEEANLDVSDTLSEFGSSNYFPPDVMFYVQGRPIEAHRVILSARSPFFKQKFENEWKDRREVRFSKEKLSYPALCSLIHFFYSDRLEISVDDMEDLVRICKVCKCESLQKIIEKELIHQRYAEYKTHRDLDNSMKRFILQGISLPEEDRLPASLHRILRVSLAKSFVGDVIDSSVGDTRVGDSVESLADVCVRVDKRNFYCHQVILASRSEYFRARLSRVNDFHEGKNGLPGDTLPFLEEHDLSAEAFEKMIEYMYTDGLKEINPNQAEEIFDVASRYLLFPLKRAVADALLPHLETATPAELCQWLVLSDMYGVLKIREYCLDLVACNFEAFVETHEFRAMLLTLPPPSGDSSLRTTVPSAPGAMMTTDQGNLLDDLREKWLEAEALELDMRDESALIFDKRLAMLVEIAEREKSESEAEDYKDTSA", "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": "MKHNFSLRLRVFNLNCWDIPYLSKHRADRMKRLGDFLNLESFDLALLEEVWSEQDFQYLKQKLSLTYPDAHYFRSGIIGSGLCVFSRHPIQEIVQHVYTLNGYPYKFYHGDWFCGKAVGLLVLHLSGLVLNAYVTHLHAEYSRQKDIYFAHRVAQAWELAQFIHHTSKKANVVLLCGDLNMHPKDLGCCLLKEWTGLRDAFVETEDFKGSEDGCTMVPKNCYVSQQDLGPFPFGVRIDYVLYKAVSGFHICCKTLKTTTGCDPHNGTPFSDHEALMATLCVKHSPPQEDPCSAHGSAERSALISALREARTELGRGIAQARWWAALFGYVMILGLSLLVLLCVLAAGEEAREVAIMLWTPSVGLVLGAGAVYLFHKQEAKSLCRAQAEIQHVLTRTTETQDLGSEPHPTHCRQQEADRAEEK", "text": "FUNCTION: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Hydrolyze 1-acyl-2-lyso-sn-glycero-3- phosphocholine (lyso-PC) and 1-O-alkyl-2-lyso-sn-glycero-3- phosphocholine (lyso-platelet-activating factor). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the neutral sphingomyelinase family."}
+{"protein": "MTRLVWFCMQVAYCLHGWDWDIMDRGRSSNSYDSLWGGKARDNPIVSQLPLQYRIRSALTQEQQTAYQVMYRIQEITIKLRTNDLNPPTSRYRSLSPPPVYDSQGKRTNTREHRYRKKLEEERHRLVEIALKMIPHFIAPDDYRRPSKFQDKYYIPINDYPEINFVGLLLGPRGNTLKQLQQQSGCKIVIRGRGSVKEGKAATDLPKGAMNMNEPLHCVISADTEEKIPLGINAVESIIIKAITSPEGQNDLKRGQLRELAVLNGTLREDNRPCPLCGEQGHKKWECSSNPSLSMTVICQRCNQPGHAARDCTSPLNEFGKRTSDGPEFRETKKLQQDAPPPSGPVGSHPSAPGSGSANSGVAPASLHPPGTMAPPGALPPPGSLAAPGTLPPPAALPAPAAPGTLPPPVALPAPATLPQAGVPPAPDASPAVKTAVPIEGPPAPPQTAPPLRQTAATASSAGSSQSAQEEPENARNGVEKAAPGPPAAVLPPPPPPPPPPPPPPSS", "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": "MVSWKGIYFILFLFAGSFFGSIFMLGPILPLMFINLSWYRWISSRLVATWLTLPVALLETMFGVRVVITGDAFVPGERSVIIMNHRTRVDWMFLWNCLMRYSYLRVEKICLKSSLKSVPGFGWAMQVAAFIFIHRKWKDDKSHFEDMIDYFCAIHEPLQLLIFPEGTDLTENNKARSNDFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPYNIPQTEKHLLLGDFPKEIHFHVQRYPADSLPTSKEDLQLWCHRRWEEKEERLRSFYQGEKNFHFTGQSTVPPCKSELRVLVVKLLSIVYWALFCSAMCLLIYLYSPVRWYFIISIVFFVLQERIFGGLEIIELACYRFLHKHPHLNSKKNE", "text": "FUNCTION: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling (PubMed:15152008). Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors (PubMed:15152008). Also exhibits 1-acyl-sn-glycerol-3-phosphate acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol- 3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn- glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Possesses lysophosphatidylinositol acyltransferase (LPIAT) activity (PubMed:20668164). Possesses lysophosphatidylglycerol acyltransferase (LPGAT) activity (By similarity). Required for establishment of the hematopoietic and endothelial lineages (PubMed:17675553). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family."}
+{"protein": "MAGAGSEARFAGLSLVQLNELLEDEGQLTEMVQKMEETQNVQLNKEMTLASNRSLAEGNLLYQPQLDTLKARLTQKYQELQVLFEAYQIKKTKLDRQSSSASLETLLALLQAEGAKIEEDTENMAEKFLDGELPLDSFIDVYQSKRKLAHMRRVKIEKLQEMVLKGQRLPQALAPLPPRLPELAPTAPLPYPAPEASGPPAVAPRRIPPPPPPVPAGRLATPFTAAMSSGQAVPYPGLQCPPLPPRVGLPTQQGFSSQFVSPYPPPLPQRPPPRLPPHQPGFILQ", "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 Note=Recruited to the endosomal membrane in a VPS4A-dependent fashion. SIMILARITY: Belongs to the VPS37 family."}
+{"protein": "MDIRESRSQSPELSQSEDAVGPCPFLISVYHQFQTKNHVLDIFEDVIPSIQVYGWLTMTLYELGVLIADQLLLNNEETRHSEWSLQIRTIFYDKYKDRPIARDLGTVCLHNPKLFQGNKLLKRTGIKCGDKIDVTIKEDKIRIKK", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SAP18 family."}
+{"protein": "MANVQKIGKAVYKGPSVVKEIIYGITLGFAVGGLWKMHHWNNQRRTKEFYDLLEKGEISVVVEDE", "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. SIMILARITY: Belongs to the cytochrome c oxidase subunit 5C family."}
+{"protein": "MKIAVLGGTGDQGLGLALRLALAGEEVIIGSRDAEKAVSAAQKVLEIAERDDLKVKGATNAEAAEEAEVAILTVPLQAQMATLGSVKEAIKGKVLIDATVPIDSCLGGSAVRYIDLWDGSAAERAARFLEDQGTRVAAAFNNISASALLDITGPVDCDCLIASDHRDALDLASELAEKIDGVRAIDCGGLENARVIEKITPLLINLNIKNRIRNAGIRITNLPE", "text": "FUNCTION: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions. SIMILARITY: Belongs to the F420-dependent NADP reductase family."}
+{"protein": "MAIKEETNEFSQGNEGNSHSTNNNNNSNNSNSNNNADVSAPVDDDDDDDGTSQGKTQKERRKIEIKFIQEKSRRHITFSKRKAGIMKKAYELSVLTGTQVLLLVVSETGLVYTFTTPKLQPLVTKSEGKNLIQACLNAPEEGLGDDQENQSDGNTGDSPDQSPAPATNPNVMGAAGHAHHIQQQQQQQQQAQQQAQQQMAPMPSHGLPTHYSNPQGAGNPGVPPQQQGQHQPGIPLQGGYSDQYSYFGNIQNNNIPNQQQYQ", "text": "FUNCTION: Transcription factor that is recruited by AHR1 to the promoters of genes involved in biofilm formation, which include several key adhesion genes. Plays an important role in cell adhesion, hyphal growth and virulence. Implicated in the regulation of opaque-phase- specific gene expression. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MGSFPFHRDLQEIASSQLTKALDPEEFRKQGHMVINFIADYYQNIEKYPVLSRVEPGYLKKCLPVSAPYDPEPISTILRDVQNHIVPGLTHWQSPNFFAYFSSTASTAGFLGEILTTGFNVVGFNWVSSPAATELENIVMDWLGDMLQLPKSFHFSGNGGGVLHGSTCEAIVCTMVAARDQMLRRIGSENLGKLVVYGSDQTHSTLQKATQIVGINTENFRAIKTTKSTGFALSPEMLRLTISSDLEKGLVPLFLCATIGTTATTAIDPLEALCHVAKEYGVWVHVDAAYAGSACICPEFRHFINGVEGANSFSFNPHKWLFTGMDCCCLWVKNPSVLASSLSTNPEFLRNKASDSKQVVDYKDWQIALSRRFRALKLWLVLRSYGVANLRNFIRIHVKMAKTFEGLVRMDKRFEILVPRNFSLVCFRISPSALISSNEDDEIGMVNEVNCKLLEAINASGKAYMTHAVVGGLYVLRCAVGATLTEEKHIVEAWNVVQDHAQAILSTY", "text": "FUNCTION: Bifunctional enzyme that catalyzes the decarboxylation of L- phenylalanine to produce 2-phenylethylamine, which is then oxidized to form 2-phenylacetaldehyde, a constituent of floral scent in petals (PubMed:16766535, PubMed:17928708). 2-phenylacetaldehyde is a precursor of 2-phenylethanol, another constituent of floral scent in petals (PubMed:16766535, PubMed:17928708). SIMILARITY: Belongs to the group II decarboxylase family."}
+{"protein": "MTDYSSKEYFDKLEKFWRAANYLSVGQLYLKDNPLLKRDIKPEDVKVHPIGHWGTIPGQNYIYAHLNRVINKYGVNMFYVEGPGHGGQVMVSNSYLDGSYTEAYPAITQDEEGMKKLFKQFSWPGGVASHAAPVTPGSIHEGGELGYSLSHGVGAILDNPDQIAAVVVGDGEAETGPLAASWQHNRFINPITDGAVLPILDINGYKLSNPSLTSRMSDEELTEFFHGQHWDPYFVEGDDSEAMDPKMAEVMDKAIEKIQEIQKNARENHDETMPYWPVIVFRSPKGWTGPKTWDNKVIEGTFRAHQIPIPVDQKNLEHVDALIDWMKSYKPEELFDENGRVLPEIAEIAPKGEKRMASNPITNGGVNPTDLNLPDYRDYAVDTTKRGQNIKQDMLVWSDYLRDVITKNPTNFRMFGPDETMSNRLYGLFEVTNRQFVAPIKKDWDEALAPEGRILDAQLSEHSAEGWLETYTLTGRHGIFTSYEAFLRVVDSMITQHFKWLRKADELDWRNDYPSLNLVSTSTSFQQDHNGYTHQDPGLLTHLAEKKPEFIREYLPADANSLLAISPLVMNDRNKINLIIASKQPRPQFYSMEEAEVLAKNGLGIIDWASTTNGEEPDVVFAAAGTEPNMESLAAINILHDNFPDLKIRFINVVDLLKLQSPKVNPNGLSDEEFDRYFTKDKPVIFTFHGFEDLIRSIFFDRHNHNLHVHGYREEGDITTPFDMRVLNELDRFHLAQDTINSIPEFAEKGADFSQQMDNTLERHYQYIRDNGDDLPEVTNWTWKDVN", "text": "SIMILARITY: Belongs to the XFP family."}
+{"protein": "MADHMMAMNHGRFPDGTNGLHHHPAHRMGMGQFPSPHHHQQQQPQHAFNALMGEHIHYGAGNMNATSGIRHAMGPGTVNGGHPPSALAPAARFNNSQFMGPPVASQGGSLPASMQLQKLNNQYFNHHPYPHNHYMPDLHPAAGHQMNGTNQHFRDCNPKHSGGSSTPGGSGGSSTPGGSGSSSGGGAGSSNSGGGSGSGNMPASVAHVPAAMLPPNVIDTDFIDEEVLMSLVIEMGLDRIKELPELWLGQNEFDFMTDFVCKQQPSRVSC", "text": "FUNCTION: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates the peroxisome proliferator-activated receptors PPARA transcriptional activity. Enhances estrogen-dependent transactivation mediated by estrogen receptors. Acts also as a transcriptional corepressor; interferes with the binding of the transcription factors HIF1A or STAT2 and the p300/CBP transcriptional coactivator complex. Participates in sex determination and early gonad development by stimulating transcription activation of SRY. Plays a role in controlling left-right patterning during embryogenesis; potentiates transcriptional activation of NODAL-mediated gene transcription in the left lateral plate mesoderm (LPM). Plays an essential role in differentiation of the adrenal cortex from the adrenogonadal primordium (AGP); stimulates WT1-mediated transcription activation thereby up-regulating the nuclear hormone receptor NR5A1 promoter activity. Associates with chromatin to the PITX2 P1 promoter region. SUBCELLULAR LOCATION: Nucleus Note=Colocalizes with EP300 in dot-like structures. SIMILARITY: Belongs to the CITED family."}
+{"protein": "MSVPQIHVEEVGAEEGAGAAAPPDDHLRSLKALTEKLRLETRRPSYLEWQARLEEHTWPFPRPAAEPQASLEEGERGGQEPLLPLREAGQHPPSARSASQGARPLSTGKLEGFQSIDEAIAWLRKELTEMRLQDQQLARQLMRLRGDINKLKIEHTCRLHRRMLNDATYELEERDELADLFCDSPLASSFSLSTPLKLIGVTKMNINSRRFSLC", "text": "SIMILARITY: Belongs to the FAM167 (SEC) family."}
+{"protein": "GLWSKIKDAGKAVLKAAGKAALGAVTDAV", "text": "FUNCTION: Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
+{"protein": "MADTDDIIDYESDDLTEYEDDEEDGESLETSDIDPKSSYKIVESTSTHIEDAHSNLKHIGNHISALKRRYTRRISLFEIAGIIAESYNLLQRGRLPLVSEFSDETMKQNMLHVIIQEIEEGSCPIVIEKNGELLSVNDFDKDGLKFHLDYIIKIWKLQKRY", "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 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. SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 19 kDa subunit family."}
+{"protein": "MVAPGLVLGLVLPLILWADRSAGIGFRFASYINNDMVLQKEPAGAVIWGFGTPGATVTVTLRQGRETIMKKVTSVKAHSDTWMVVLDPMKPGGPFEVMAQQTLEKINFTLRVHDVLFGDVWLCSGQSNMQMTVLQIFNATRELSNTAAYQSVRILSVSPTQAEQELEDLVAVDLQWSKPTSENLGHGYFKYMSAVCWLFGRHLYDTLQYPIGLIASSWGGTPIEAWSSGRSLKACGVPKQGSVPYDSVTGPSKHSVLWNAMIHPLCNMTLKGVVWYQGESNINYNTDLYNCTFPALIEDWRETFHRGSQGQTERFFPFGLVQLSSDLSKKSSDDGFPQIRWHQTADFGYVPNPKMPNTFMAVAMDLCDRDSPFGSIHPRDKQTVAYRLHLGARALAYGEKNLTFEGPLPEKIELLAHKGLLNLTYYQQIQVQKKDNKIFEISCCSDRRCKWLPASMSTVSTQSLTLAIDSCRGTVVALRYAWTTWPCEYKQCPLYHPSSALPAPPFIAFITDQDPGHQSNVAK", "text": "FUNCTION: Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid. SUBCELLULAR LOCATION: Lysosome."}
+{"protein": "MSKLIRRVVTVLALTSMASCFASGGIEAAVAESLITKIVASAETKPAPVPMTAKKVRLVRRNKQPVEQKSRGAFCDKEFYPCEEGRCQPVEAQQESCYGRLYSVKVNDDCNVEICQSVPEYATVGSPYPIEILAIGKKDCVDVVITQQLPCEAEFVSSDPETTPTSDGKLVWKIDRLGAGDKCKITVWVKPLKEGCCFTAATVCACPELRSYTKCGQPAICIKQEGPDCACLRCPVCYKIEVVNTGSAIARNVTVDNPVPDGYSHASGQRVLSFNLGDMRPGDKKVFTVEFCPQRRGQITNVATVTYCGGHKCSANVTTVVNEPCVQVNISGADWSYVCKPVEYSISVSNPGDLVLHDVVIQDTLPSGVTVLEAPGGEICCNKVVWRIKEMCPGETLQFKLVVKAQVPGRFTNQVAVTSESNCGTCTSCAETTTHWKGLAATHMCVLDTNDPICVGENTVYRICVTNRGSAEDTNVSLILKFSKELQPIASSGPTKGTISGNTVVFDALPKLGSKESVEFSVTLKGIAPGDARGEAILSSDTLTSPVSDTENTHVY", "text": "FUNCTION: In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the major outer membrane porin. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan (By similarity). SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MLKIIDAKVIVTCPGRNFVTLKITTSDGVTGVGDATLNGRELAVVSYLRDHMIPCLIGRDAHRIEDVWQFFYRGSYWRGGPVAMTALAAVDMALWDIKAKLAGMPLYQLLGGACREGVMVYGHANGETIEDTIAEARKYQALGYKAIRLQSGVPGLPSTYGVSGDKMFYEPADGNLPTENVWSTSKYLKHAPKLFEAAREALGDDVHLLHDVHHRLTPIEAGRLGKDLEPYRLFWLEDAVPAENQAGFRLIRQHTTTPLAVGEIFSHVWDCKQLIEEQLIDYLRATVLHAGGITNLRKIAAFADLHHVRTGCHGATDLSPITMAAALHFDLSVSNFGLQEYMRHTPETDAVFPHAYSYKDGMLHPGEAPGLGVDIDEALAGQYPYKRAYLPVNRLEDGTMYNW", "text": "FUNCTION: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. GalD subfamily."}
+{"protein": "MGRAGTGTGGEAVAAVVAGPLLLLLLARPPPASAGYSGKSEVGLVSEHFSQAPQRLSFYSWYGSARLFRFRVPPDAVLLRWLLQVSRESGAACTDAEITVHFRSGAPPVINPLGTSFPDDTAVQPSFQVGVPLSTTPRSNASVNVSHPAPGDWFVAAHLPPSSQKIELKGLAPTCAYVFQPELLVTRVVEISIMEPDVPLPQTLLSHPSYLKVFVPDYTRELLLELRDCVSNGSLGCPVRLTVGPVTLPSNFQKVLTCTGAPWPCRLLLPSPPWDRWLQVTAESLVGPLGTVAFSAVAALTACRPRSVTIQPLLQSSQNQSFNASSGLLSPSPDHQDLGRSGRVDRSPFCLTNYPVTREDMDVVSVHFQPLDRVSVRVCSDTPSVMRLRLNTGMDSGGSLTISLRANKTEMRNETVVVACVNAASPFLGFNTSLNCTTAFFQGYPLSLSAWSRRANLIIPYPETDNWYLSLQLMCPENAEDCEQAVVHVETTLYLVPCLNDCGPYGQCLLLRRHSYLYASCSCKAGWRGWSCTDNSTAQTVAQQRAATLLLTLSNLMFLAPIAVSVRRFFLVEASVYAYTMFFSTFYHACDQPGEAVLCILSYDTLQYCDFLGSGAAIWVTILCMARLKTVLKYVLFLLGTLVIAMSLQLDRRGMWNMLGPCLFAFVIMASMWAYRCGHRRQCYPTSWQRWAFYLLPGVSMASVGIAIYTSMMTSDNYYYTHSIWHILLAGSAALLLPPPDQPAEPWACSQKFPCHYQICKNDREELYAVT", "text": "FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchor proteins (GPI-AP). Has phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. Required for the shedding of the GPI-AP TDGF1, but not CFC1, at the cell surface. Shedding of TDGF1 modulates Nodal signaling by allowing soluble TDGF1 to act as a Nodal coreceptor on other cells (PubMed:27881714). Also indirectly involved in the translocation of RAC1 from the cytosol to the plasma membrane by maintaining the steady state amount of CAV1-enriched plasma membrane subdomains, stabilizing RAC1 at the plasma membrane (PubMed:27835684). In contrast to myomaker (TMEM8C), has no fusogenic activity (PubMed:26858401). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM8 family."}
+{"protein": "MRAFSAATVRATTRKSFIPMAPRTPFVTPSFTKNVGSMRRMRFYSDEAKSEESKENNEDLTEEQSEIKKLESQLSAKTKEASELKDRLLRSVADFRNLQQVTKKDIQKAKDFALQKFAKDLLESVDNFGHALNAFKEEDLQKSKEISDLYTGVRMTRDVFENTLRKHGIEKLDPLGEPFDPNKHEATFELPQPDKEPGTVFHVQQLGFTLNDRVIRPAKVGIVKGEEN", "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 SSC1 to substrate proteins and the association of SSC1 with TIM44. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the GrpE family."}
+{"protein": "MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPIDGIRSSFTSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFPIGQEVAYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQRTKY", "text": "FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:21880860). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass membrane protein Cytoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus Cytoplasm. SIMILARITY: Belongs to the H-rev107 family."}
+{"protein": "MKILIAVVFGCLLIILSFSKYFNDQLLDATTKDIKESERPVDKLIGGLLTADFDEGSCLSRYHKYFLYRKPSPYMPSEYLVSELRSYEMLHKRCGPDTKAYKEATEKLSRDEYYASESNGECRYIVWLARDGLGNRLITLASVFLYAILTERIILVDNRKDVSDLLCEPFPGTSWLLPLDFPMLNYTYAYGYNKEYPRCYGTMLENHAINSTSIPPHLYLHNIHDSRDSDKLFFCQKDQSFIDKVPWLIIQTNAYFVPSLWLNPTFQTKLVKLFPQKETVFHHLARYLFHPTNEVWDMVTKYYDAHLSNADERLGIQIRVFGKPSGYFKHVMDQVVACTQREKLLPEFEEESKVNISKPPKLKVVLVASLYPEYSVNLTNMFLARPSSTGEIIEVYQPSAERVQQTDKKSHDQKALAEMYLLSLTDNIVTSGWSTFGYVSYSLGGLKPWLLYQPVNFTTPNPPCVRSKSMEPCYHTPPSHGCEADWGTNSGKILPFVRHCEDMMYGGLKLYDDF", "text": "FUNCTION: May be involved in cell wall biosynthesis. May act as a fucosyltransferase. SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the glycosyltransferase 37 family."}
+{"protein": "MANPPHGGVLKDLIARDAPRRQELYAEAEKLPAIVLSDRQLCDLELILNGGFSPLEGFMNEKDYTGVVAENRLADGNLFSIPITLDVSKETIDEVGVKAGARIALRDSRDDRNLAIITVDDIYKPDKVKEANEVFGDNDEAHPAVKYLHHTAKEFYVGGKVEAIDRLEHYDYVGLRYTPAELRLHFDKLGWQKVVAFQTRNPMHRAHRELTVRAARARQANVLIHPVVGLTKPGDIDHFTRVRVYQALMPRYPNGMAVLALLPLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNSKGVDFYGPYDAQDAVEKYRDELGIEVVPFQQMTYLPDSDEYKPKDEVAKDIKTLDISGTELRKRLRTGQEIPEWFSYPEVVKVLRESHPPRNQQGFTVFLTGYQNSGKDAIARALNVTLNQQGGRSVSLLLGETVRSELSSELGFSREDRDKNIARIAFVAAELTKAGAAAIVAPIAPFQKSRQQARETVEKYGSFFLVHVATPLDHAEKTDRRGVYAKARAGEIKGFTGVDDPYEAPENADLVVDTSKTNVRTAVHQIVLLLESQGLLTQL", "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": "MNVENQDPNIMVIPNNNLGPIDGNNISPAMNDENSNNGSSFLKNLVNTGTNLLFSSSSSIASPPNLGGLSNDSTNNNSNSNNTIDSSKPLSFENDMSDGYEALVRRSEIAIDQCKELLDFFKKRASEEEKYSKNISNMFSKFKVKDDHDTFQKGVSLLNKINDAESTIHRSFSQNITTNLYHPLNEAIKDMEKSRKRLLEDGKKLKNDLKDSIENVKKSNQKYEKLCREMEQAKLELIEEGNDTKSGKVETLEKKLEKTKLASIKAEDEYKEQINETNEFISGVYQNRLSENLREFQQFELTRLEIMKSNIRNYIGFMKDIPQALQCEIDSTKGFVDIIDPEVDLQNYIMNNSNPKKVLLPFIFEAYNDHKPFVDQHNQNSSSSSSTNALNYASPMSASGSITNTITSQSGSTIISNGASQPIEIPSPQPISEQQQIPPQQQQQQQQAQVPPTSINQSSSPPVNPMGRQQSLKENIFGFFNKATTNLKSSTSSLLTKDGNSTTSSNTSTSNSNQLSKSGIGLPIINTNSIFGVELEVLIENDNSKKKGNGVELEVPLILTQFVQALLKLESFKMDGVFVSLPSHFNIQQEKQKLDQTGTLENITDVYLIASLFKNWIGDLPNPLISYAIYQEIIEAPDNAWKIIESGIPILHRRVLHYIIDFLVDFVNCSKMDTHSISLIFTPVLIRSPFNGDSLLNSKKEVAVIENMIIDSLETKRGNYILKRNLPIIPDDENSDDDDDDSGHIDDENNSSTSGENDINTTNINNNNNVNSNNDTNNNNNNSNTTTTNNNNNNDSNNSNSTNNNNNNNNNNTNNDDNESNNSGYGVSSNGNNINSSVGGSVTHHFLYQTTPTNNVTPVLSDFFDTNSSNGSSKANTNTHNLGVRNSSNISFDTISTNQSDSEPVLVEYDNDDFDILSYK", "text": "FUNCTION: Rho GTPase-activating protein involved in the signal transduction pathway (By similarity). Regulator of the contractile vacuole network as well as involved in driving vacuole emptying. SUBCELLULAR LOCATION: Cytoplasm Contractile vacuole Note=Localized to tubules of the contractile network."}
+{"protein": "MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGGQRSSAAQKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIIRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDTSRAYLTATWYYYDSILPSFRELALLFEHIQRARNGGLRPLEVRRAPVPDGAPSRYPPVATCHRPGSASFCPGESSRMGIKDRIRISSSQKRTGPSKQHLAPPPIPTSPSSEQVGEASSPSKVQKSWSFNDRTRFRASLRLKPRCSAEEGPSEEVAEEKSYQCELTVDDVMPAVKTVIRSVRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQARVDQIVGRGPGDRKTREKGDKGPSDTEAVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSASLGTVQVPLFDPDITSDYHSPVDHEDISVSAQTLSISRSVSTNMD", "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": "MPAPSMDCDVSTLVACVVDVEVFTNQEVKEKFEGLFRTYDDCVTFQLFKSFRRVRINFSNPKSAARARIELHETQFRGKKLKLYFAQVQTPETDGDKLHLAPPQPAKQFLISPPASPPVGWQPISDATPVLNYDLLYAVAKLGPGEKYELHAGTESTPSVVVHVCDSDIEEEEDPKTSPKPKIIQTRRPGPPPSVSN", "text": "FUNCTION: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development (By similarity). SIMILARITY: Belongs to the RCAN family."}
+{"protein": "MAAQNEQRPERIKTTPYLEGDVLSSDSGPLLSVFALQEIMQKVRQVQADYMTATREVDFTVPDVQKILDDIKALTVEQVYKIVKVPSISFRHIVMQSRDRVLRVDTYYEEMSQVGDVITEDEPEKFYSTIIKKVRFIRGKGSFILHDIPTRDHRGMEAAEPEVLGVEFKNVPPVLTAEHRAMIQSALDGSIIENGNVATRDVDVFIGACSEPIYRIYNRLQGYIEAVQLQELRNSIGWLERLGQRKRITYSQEVLTDFRRQDTIWVLALQLPVNPQVVWDVPRSSIANLIMNIATCLPTGEYIAPNPRISSITLTQRITTTGPFAILTGSTPTAQQLNDVRKIYLALMFPGQIILDLKIDPGERMDPAVRMVAGVVGHLLFTAGGRFTNLTQNMARQLDIALNDYLLYMYNTRVQVNYGPTGEPLDFQIGRNQYDCNVFRADFATGTGYNGWATIDVEYRDPAPYVHAQRYIRYCGIDSRELINPTTYGIGMTYHCYNEMLRMLVAAGKDSEAAYFRSMLPFHMVRFARINQIINEDLHSVFSLPDDMFNALLPDLVAGAHQNADPVVLDVSWISLWFAFNRSFEPTHRNEMLEIAPLIESVYASELSVMKVDIRHLSLMQRRFPDVLIQARPSHFWKAVLNDSPEAVKAVMNLSHSHNFINIRDMMRWVLLPSLQPSLKLALEEEAWAAANDFEDLMLTDQVYMHRDMLPEPRLDDIERFRQEGFYYTNMLEAPPEIDRVVQYTYEIARLQADMGQFRAALRRIMDDDDWVRSDGVLRTVRVKFFDARPPDDILQGLPFSYDTNEKGGLSYATIKYATETTIFYLIYNVEFSNTPDSLVLINPTYTMTKVFINKRIVERVRVGQILAVLNRRFVAYKGKMRIMDITQSLKMGTKLAAPTV", "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": "MKKTLMLLAMVVALVILPFFINHGGEYGGSDGEAESQIQAIAPHYKPWFQPLYEPASGEIESLLFTLQGSLGAAVIFYILGYCKGKQRRDDRA", "text": "FUNCTION: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiN family."}
+{"protein": "MSRKLVIDPVTRIEGHGKVVVHLDDDNKVVDAKLHVVEFRGFEKFVQGHPFWEAPMFLQRICGICFVSHHLCGAKALDDMVGVGLKSGIHVTPTAEKMRRLGHYAQMLQSHTTAYFYLIVPEMLFGMDAPPAQRNVLGLIEANPDLVKRVVMLRKWGQEVIKAVFGKKMHGINSVPGGVNNNLSIAERDRFLNGEEGLLSVDQVIDYAQDGLRLFYDFHQKHRAQVDSFADVPALSMCLVGDDDNVDYYHGRLRIIDDDKHIVREFDYHDYLDHFSEAVEEWSYMKFPYLKELGREQGSVRVGPLGRMNVTKSLPTPLAQEALERFHAYTKGRTNNMTLHTNWARAIEILHAAEVVKELLHDPDLQKDQLVLTPPPNAWTGEGVGVVEAPRGTLLHHYRADERGNITFANLVVATTQNNQVMNRTVRSVAEDYLGGHGEITEGMMNAIEVGIRAYDPCLSCATHALGQMPLVVSVFDAAGRLIDERAR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family."}
+{"protein": "MFSILQGHAGFSRDLATGIWREIKAEDYTFAKRFSKEHPEGKPASMPFKFDVIEEHDPQSLAEMLPLMRRLTSDPHIVAVRGRCLAPKNNVRRKKGNFNVSNPSNIIAMDVDGILDTGGYDKFNLVGMARHIIKMLNSISEDMFPLDAGFIAHASSSAGLKPGIRMHLMLESNVKVTQGQLKFLFTSINDSSKQKFGFDIADLAYYSSVQLHYFADPLFSDGIVDPFKAESKPRLVYVKGSKVNLPNNLVDYETTRGEFKEEFYSLLDQIKGKKIASDKVEETISELEEADDGVYLRIIPKLYHRALEDGVDFAWLEREIKPALSEYIATKDNSRNIQDYFNNGRKQALKAFVNNSKREIPLNLKGVPLKKLEVDSPPEVPYLKINIVPPKGHITFVKASLGTGKTTAVTKWLDAGVLPGNFLAVTNTRALVSSNAKKFSAGQYDKSVDMLNFKRGAIDRMSTTIHSLHKFKSFIGQIDTIFIDECDAVMNDLLFAPVVKQRRECIQVLRDILMTAKTVILSDGDISAETIEAYGSLIDFDKPVAFYNHHRKMLSKAHAYEFPDESSIWVALQTSLEMGEKSILVSDCGPDELNEKGMALRRNTGALVKEIHSNSTSDVDIRRILDYTTNELIDQQIDCLLCSPSVTSGVDFNYFDNVFVITRTSNQAPNMRFQAIRRDRGAQNIYYFIDKSTSGFSAGSEQYNIDEGWLELAQQLYARRRELESRNYTSTLRYYLLDQGATIDIFSESWGTIEGAGKEYTEERIKAILHSTPDYCAPRHADAYEAKLLLVRYYHLESIKDVTVEHVEQYIKDKPNDRAAFFHKMHEMFWEDIKKCSNVTIKPFIEALKGKKKDFFLKTGQSANPKYARMYLGMMGIGKDMNTENIVDWYRTYCKIECMPIPFKFMTEEERAMAEEVMSELGATNEDA", "text": "FUNCTION: Displays bipolar ssDNA and dsDNA unwinding activities that require the same core catalytic residues for unwinding in either direction, the 3'-5' direction being more robust. SIMILARITY: Belongs to the herpesviridae oribp family."}
+{"protein": "MNVGVAHSEVNPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFFSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETPDQGKARLLTHWEQLDYGVQFTSSRKFFTISPIILYFLASFYTKYDPTHFILNTASLLSVLIPKMPQLHGVRIFGINKY", "text": "FUNCTION: Negative regulator of sphingolipid synthesis. FUNCTION: Negative regulator of sphingolipid synthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ORM family."}
+{"protein": "MLKYKPLLKISKNCEAAILRASKTRLNTIRAYGSTVPKSKSFEQDSRKRTQSWTALRVGAILAATSSVAYLNWHNGQIDNEPKLDMNKQKISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFEPLHAPNVIDKYIAPEKKLGPLQGSMPPELVCPPYAPGETKEDIARKEQLKSLLPPLDNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPLEGEKDVARGCGQGVTKVPQMISTLASCSPEEIIEAAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQREKDMKLKFSNTKAGPKAMKKTNVEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMPILEQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLLDLSTLKARTVGVPNDVLYNEVYEGPTLTEFEDA", "text": "FUNCTION: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate with subsequent transfer of electrons to cytochrome c (PubMed:11914072). Is involved in the utilization of (S)-lactate as a sole source of carbon for growth (PubMed:3004948). Can also use ferricyanide as an electron acceptor in vitro (PubMed:4593578, PubMed:3004948). SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: In the N-terminal section; belongs to the cytochrome b5 family. SIMILARITY: In the C-terminal section; belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family."}
+{"protein": "MSSTNHFTYLVLGAGSGGIASARRAAKHLNAKGNGDRIGIVEVTRPGGTCVNVGCVPKKVMWNTSFIKEMINAAPSYGFDFGGQQVKFNWPTIKKARDEYIKRLNGIYDSNLAKDNIVRINGYGRFSGPKEIQVNGANGEKYTADHILIAAGGRPTVPDVPGKELGITSDGFFELEDLPKSTLVVGAGYIAVELAGVLHSLGSETTMVIRQKQFLRTFDEMLHTTLLKQMTDDGVKFVTEASIKSLERDVDGKRIIATTNAGVKLPPVECVIWAIGRVPNTDDLGIDKAGIQLTEQSGFIKVDEFQNTNVPGVHAVGDICGNFLLTPVAIAAGRRLSERLFNGKSDLKFEYENVATVVFSHPPIGTVGLTEQEAITKYGTENIKCYNTSFINMFYSVQVHKVRTSMKLVCLGKEEKVIGLHIIGDGCDEIIQGFAVAVKMGCTKWDLDNTCAIHPTSAEELVTMV", "text": "FUNCTION: Maintains high levels of reduced glutathione (GSH) in the cytosol by reducing glutathione disulfide (oxidized glutathione or GSSG) (PubMed:16678813). The amount of GSH may affect the determination of cell fate (PubMed:16678813). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MVIRRLYKFCASHVVRNCSSLKCAQNIHGHNYEVEVFIETNRLDNANMALDFGLMQQEMQTFIDSFDHAHHFWDKESPEFQRFIENHCVRYVKCSFNLSAESYALMFLYYLTKILQKSVFSNNEGELKVSSVRVHETKNGYAESFLKDLENPHFKSLVHDHCVSFSQGIQSLWHDKDFFHKIISDEKQCFFHAKPLHQIP", "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": "MRTLWIVAVLLLGVEGSLVQFETLIMKIAGRSGLLWYSAYGCYCGWGGHGLPQDATDRCCFVHDCCYGKATDCNPKTVSYTYSEENGEIVCGGDNPCGTQICECDKAAAICFRDNIPSYSNKYWLFLPKNCRGDPEPC", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that significantly inhibits ADP-induced platelet aggregation in platelet-rich plasma of human, rabbit and guinea pig. 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": "MDLRIGGKYRISRKIGGGSFGEIYLGTNISTNEEVAIKLEPAKAIHPQLLFESKLYKIFQGGIGIPAVKWFGFDGDYNIMVMDLLGPSLEDLFNYCGRKFSLKTVLMLGDQMLRRIEFIHSNNFIHRDIKPDNFLMGIGKRGHVVNLIDFGLAKRYRDPKTHQHIPYREHKNLTGTARYASLNTHQGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAYTKRDKYEKICDKKAQTKIDTLCQGFPSEFATFLNYTRFLKFEDKPDFLYLRKLLREMFVREGYRYDYMFDWVIVRKLREKPPLERPLSNDNKQIQQQIQQQQQAQQQLQQQAQQQQQQTTTTTTTSSSQPSNVKNISTVSNIATTTTDEQFRQLLSTPSYNNVDSDQSPQQTTTTTSSSNPNQTTFYRQNKVVVPQSSSTTTKPPAK", "text": "FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. May have a role in DNA repair mechanism and support vegetative growth of the cells. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily."}
+{"protein": "MAIQTLDYRDFQYGGQEQHRTFCHNLCETLSTWGFIKIQNTSIPDAVIDELFSYNKKFFALPEHIKQKARHPAAPNPHRGWSAVGQEQLSRIAGFEKDEETDGFVPEYRESFDQGAADDELFPNRWIDEDDLPGFRKFMENYYEMCYNFHTQLLRAISTGLSLPEDLLLSRHQTDTSELRMNHYPAIACENLKFGMRIGEHSDFGTLTLLLQDSTGGLQVEDQKKLGTFIPVESDSRYEVIVNVGDCLQRWTNRRLRSANHRVHLPEGKNFKSDEVLADRYSVAYFGKPDRNVLVDSFPEFCRGGESKYNDHMNALEYNQTKLLRTYA", "text": "FUNCTION: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase (PubMed:27705900). The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 (PubMed:27494047). The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain (PubMed:27494047). The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide (PubMed:27494047). L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl- L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L- proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain (PubMed:25270390, PubMed:25879325, PubMed:25527531). The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively (PubMed:25879325). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
+{"protein": "MKTALPLLLLTCLVAAVQSTGSQGCPTYVSEKCTARLQECSNNQQQEPLQNCTAVHADCVVQATEDCQREQSQLNHDHLNNHTTTQQP", "text": "FUNCTION: A component of the complex of water-borne protein pheromones that stimulates attraction and mating behavior. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MGGLGSPCGGCKFLRRKCVEGCVFAPYFCYEEGSSNFAAIHKVFGASNFSKLISHLPDHDRCDAVRTISYEAHSRLHDPIYGCVSQIFSLQQQVVSLQAQVVLLREEASRRFPQDDPGCNMKQQEKVLAQQMPQDLHNWFHQGILDSDFDPMSGTTRDNERSMDHNESPCSSNESLNYYQEVNFPWSV", "text": "SIMILARITY: Belongs to the LOB domain-containing protein family."}
+{"protein": "MSSGVQGGPAANANAYQTHPLRDAASALGTLSPQAYVDVVSAAQRNFLERMSQLASEQCDAQPAAHDARLDDKPALRAPQERDAPPLGASDTGSRASGAAKLTELLGVLMSVISASSLDELKQRSDIWNQMSKAAQDNLSRLSDAFHRATDEAKAAADAAEQAAAAAKQAGADAKAADAAVDAAQKRYDDAVKQGLPDDRLQSLKAALEQARQQAGDAHGRADALQADATKKLDAASALATQARACEQQVDDAVNQATQQYGASASLRTPQSPRLSGAAELTAVLGKLQELISSGNVKELESKQKLFTEMQAKREAELQKKSDEYQAQVKKAEEMQKTMGCIGKIVGWVITAVSFAAAAFTGGASLALAAVGLALAVGDEISRATTGVSFMDKLMQPVMDAILKPLMEMISSLITKALVACGVDQQKAELAGAILGAVVTGVALVAAAFVGASAVKAVASKVIDAMAGQLTKLMDSAIGKMLVQLIEKFSEKSGLQALGSRTATAMTRMRRAIGVEAKEDGMLLANRFEKAGTVMNVGNQVSQAAGGIVVGVERAKAMGLLADVKEAMYDIKLLGDLLKQAVDAFAEHNRVLAQLMQQMSDAGEMQTSTGKLILRNARAV", "text": "FUNCTION: Plays a role in the bacterium-induced formation of multinucleated giant cell (MNGC), which is formed after host cell fusion, as well as in the intercellular spreading of bacteria and in the induction of apoptosis in macrophages. May act in concert with other effector proteins to induce fusion of host cell membranes (By similarity). SUBCELLULAR LOCATION: Secreted Host membrane Note=Secreted via the bsa type III secretion system, and probably inserted into host membranes. SIMILARITY: Belongs to the invasin protein B family."}
+{"protein": "MFRAAAPGQLRRATSLLRFQSTLVIAEHANDTLAPITLNTITAAKHLGGEVSCLVAGTKCDKVAQDLCKVAGVAKVLVAQHDAYKGLLPEELTPLILATQKQFNHTHICAGASAFGKNLLPRIAAKLDVAPISDIIAIKSPDTFVRTIYAGNAICTVKCDEKVKVFSVRGTSFEAAAASGGSASSEKASSTSPVGISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVTNDLQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLFKVVPEMTELLKKK", "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 (ETF dehydrogenase). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the ETF alpha-subunit/FixB family."}
+{"protein": "MGKAAKKKYSGATSSKQVSAEKHLSSVFKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPVEKKLEIMLGDFMKTELPYFDICISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWANVTHIMKVGKNNFRPPPQVESSVVRLEIKNPRPQVDYNEWDGLLRIVFVRKNRTISAGFKSTTVMDILEKNYKTFLAMNNEMVDDTKGSMHDVVKEKIDTVLKETDLGDKRAGKCDQNDFLRLLYAFHQVGIHFS", "text": "FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family."}
+{"protein": "MVLANKLDRNLRAAEESSDGEDYYEVTDRSSSASVIEADEGGNVISSDDDMSDASDHDDDKIKAQMSKVSFGALAKAQDALSSKQSVDRKRKRGDDTSKSQEDKLEALRERLRQIKAEKLANGTQPSKKAKKSKTKTKTTQDDNVEEKEDSDSDAAPHARSSKHAPAVQSSKRMVSRKRNVVEVKKPVFRDPRFDNVSGPRPEDYVVEKRYSFLKDYRASEIAELRNTIKKTKNEGEKEQLKKKLLSMESQQKARENKERLQDVTREHKKKEKELVKEGKKPFFLKKSEQKKIALVDRFQNMKAKQRDKVIERRRKKVTAKERKNMPDERRTA", "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": "MAPTLATAHRRRWWMACTAVLENLLFSAVLLGWGSLLIMLKSEGFYSYLCTEPENVTNGTVGSTAEPGHGEASWMNGWLSCQAQDEMLNLAFTVGSFLLSAITLPLGIVMDKYGPRKLRLLGSACFAVSCLLIAYGASKPNALSVLIFIALALNGFGGMCMTFTSLTLPNMFGDLRSTFIALMIGSYASSAVTFPGIKLIYDAGVSFIIILVVWAGCSGLVFLNCFFNWPLEPFPGPEDMDYSVKVKFSWLGFDHKITGKQFYKQVTTVGRRLSVGSSMRSAKEQVVLQEGHKLCLSTVDLEVKCQPDAAAAPSFMHSVFSPILLLSLITMCVTQLRLIFYMGAMNNILKFLVSGDQKTVGLYTSIFGVLQLLCLLTAPVIDYIMDWRLKECEDASEEPEEKDANQGEKKKKKRDRQIQKITNAMRAFAFTNLLLVGFGVTCLIPNLPLQILSFILHTIVRGFIHSAVGGLYAAVYPSTQFGSLTGLQSLISALFALLQQPLFLAMMGPLQGDPLWVNVGLLLLSLLGFCLPLYLICYRRQLERQLQQRQEDDKLFLKINGSSNQEAFV", "text": "FUNCTION: Uniporter that mediates the transport of the stereospecific L-phenylalanine, L-methionine and L-branched-chain amino acids, between the extracellular space and the cytoplasm and may control the transepithelial (re)absorption of neutral amino acid in kidney and small intestine. The transport activity is mediated through facilitated diffusion and is sodium ions-, chloride ions- and pH-independent. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane Note=Located at the basolateral membrane in the small intestine enterocytes, kidney proximal tubule, thick ascending limb and, to a minor extent, of distal convoluted tubule epithelial cells. SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family."}
+{"protein": "MDCRTKANPDRTFDLVLKVKCHASENEDPVVLWKFPEDFGDQEILQSVPKFCFPFDVERVSQNQVGQHFTFVLTDIESKQRFGFCRLTSGGTICLCILSYLPWFEVYYKLLNTLADYLAKELENDLNETLRSLYNHPVPKANTPVNLSVNQEIFIACEQVLKDQPALVPHSYFIAPDVTGLPTIPESRNLTEYFVAVDVNNMLQLYASMLHERRIVIISSKLSTLTACIHGSAALLYPMYWQHIYIPVLPPHLLDYCCAPMPYLIGIHSSLIERVKNKSLEDVVMLNVDTNTLESPFSDLNNLPSDVVSALKNKLKKQSTATGDGVARAFLRAQAALFGSYRDALRYKPGEPITFCEESFVKHRSSVMKQFLETAINLQLFKQFIDGRLAKLNAGRGFSDVFEEEITSGGFCGGNPRSYQQWVHTVKKGGALFNTAMTKATPAVRTAYKFAKNHAKLGLKEVKSKLKHKENEEDYGTCSSSVQYTPVYKLHNEKGGNSEKRKLAQARLKRPLKSLDGALYDDEDDDDIERASKLSSEDGEEASAYLYESDDSVETRVKTPYSGEMDLLGEILDTLSTHSSDQGKLAAAKSLDFFRSMDDIDYKPTNKSNAPSENNLAFLCGGSGDQAEWNLGQDDSALHGKHLPPSPRKRVSSSGLTDSLFILKEENSNKHLGADNVSDPTSGLDFQLTSPEVSQTDKGKTEKRETLSQISDDLLIPGLGRHSSTFVPWEKEGKEAKETSEDIGLLHEVVSLCHMTSDFQQSLNISDKNTNGNQT", "text": "FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB35 that acts as a regulator of T-cell receptor (TCR) internalization in TH2 cells (PubMed:20154091, PubMed:20937701, PubMed:24520163, PubMed:26774822). Acts by promoting the exchange of GDP to GTP, converting inactive GDP- bound RAB35 into its active GTP-bound form (PubMed:20154091, PubMed:20937701). Plays a role in clathrin-mediated endocytosis (PubMed:20154091). Controls cytokine production in TH2 lymphocytes by controlling the rate of TCR internalization and routing to endosomes: acts by mediating clathrin-mediated endocytosis of TCR via its interaction with the adapter protein complex 2 (AP-2) and GEF activity (PubMed:26774822). Dysregulation leads to impaired TCR down-modulation and recycling, affecting cytokine production in TH2 cells (PubMed:26774822). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasmic vesicle, clathrin-coated vesicle."}
+{"protein": "MNLIAAAIAIGLGALGAGIGNGLIVSKTVEGIARQPEAGRELRTLMFIGVALVEALPIIAVVIAFLAFFG", "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. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family."}
+{"protein": "MALATQSNRIKIGIRPTIDGRRMGVRESLETQTIRMAQSVAQLLQTHIRHTDGTFVECVVADSTIGGVAEAAACADKFKRENVGLTITVTPCWCYGSETIDMDPHMPKAIWGFNGTERPGAVYLAAALAGHSQLGLPAFSIYGTEVQEADDTNIPEDVKEKLLRFARAGLAVASIRGKSYLSIGSVSMGIAGSIVNQAFFQEYLGMRNEYVDMMEIKRRLDRKIYDQEEVDLALSWVKQYCKEGVDVNSLENQRNAEERAELWENVVKMTIITRDLMVGNPKLATLNYAEEALGHNAIAAGFQGQRHWTDHLPNGDFMEAMLNSTYDWNGVRPPYILATENDSLNAIGMLFGHQLTGKAQIFADVRTYWSQDSVERVTGWRPESGFIHLINSGSAALDGTGEHQDAQGNPTLKPAWDVTEEEAKRCLENTRWCPAVHEYFRGGGLSSQFLTKGGIPFTIHRINLIKGLGPVLQIAEGWSIDLPQDVHNKLNQRTNETWPTTWFVPRLTGKGAFTDVYSVMANWGANHCVATHGHVGADLITLASMLRIPVCMHNVSEKNIFRPSAWNGFGQDKEGQDYRACQNFGPLYK", "text": "FUNCTION: Converts the aldose L-fucose into the corresponding ketose L- fuculose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the L-fucose isomerase family."}
+{"protein": "MDGGQPIPSSLVPLGNESADSSMSLEQKMTFVFVILLFIFLGILIVRCFRILLDPYRSMPTSTWADGLEGLEKGQFDHALA", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cortexin family."}
+{"protein": "MAIRHFKKQVQESSDSENSSSDEKSTTARDDNYSSNPMNESELHLSTKANSDSDSGKDGPDSSSSSSSSSSSSSDDEVTLHKPVFLKRKRKDEQNQPEETGENGSLVRAAYLAKALRQKQYTENIVASETSDQSILSQIIAIDDTDNTNPEQEQLQWEQRQQARLKRERQKKLDKQLLIEEQEMQRASQLSKVDDPWLKELDLNDDSNLNSFDLKASSRNRHPVNSKKDISIPARLQKGQLQLASSHTNNDTEDTEYGYIEE", "text": "FUNCTION: Component of the spliceosome and rRNA processing machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP particle, required for splicing of pre-mRNA (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SPP381 family."}
+{"protein": "MEHNNNPGTPQMSSEFPASTTQTSSSAAAYDNSSHFEKEQSLMRWEQDLKLRERALANNQSAADITGPHVVVPAPATAHPRQANFPSSYPMIRLNLEEDIAIREYRQIVKFGIFVFLWEAAALVYNWVVSIGTIVYSAVDNFFLALFYMIVGVPTLYFLTRKLYRAASVPERARKSYAYLMALLGVVLFNIIFFVGFKRSGMNGLIWVISLFHNDHNAVGAMATVSLFFWFVGVFLTIALFIMYLRLNNTKRQRGEIQNAGFREYIKSR", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Spore coat. Note=Associated with the inner face of spore coat. SIMILARITY: Belongs to the SCAMP family."}
+{"protein": "MAAELTSTKLNAENHLLLDQPLLRLPHELARRNFKSVQRLVEREREYVIPALKEAANASLSNAQTPDQTLAALDSMLARMQNLKRKMESIQQEEKKVQNQSRKRIQHLEHLHQIPSLADVKYDQWSRIRLDRLVVDHMLRSGYTESAQQLAQEKGIEDLVDLDVFVQCQRIAQSLRRGETKDALQWCNENKAALKKSQFNLEFELRLQQYIEMLRTGDRGKLMDAMAHAKRYLTPYTETQSKEIHRAAGLLAFPQDTKAEPYKLTDLQSMYSFDRWNYLSDLFIRTHHELLSLPSSPLLHIALSAGLSALKTPSCHSAYTSSSSNFLSTTTSVCPICSTELNELARNMPYAHHAKSYVESDPIVLPNGRIYGQQRLLDMSKKLGCVETGKVKDPTTGEIFDKSEMKKVYIM", "text": "FUNCTION: Involved in the proteasome-dependent degradation of fructose- 1,6-bisphosphatase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the FYV10 family."}
+{"protein": "MKFVSFNINGLRARPHQLEAIVEKHQPDVIGLQETKVHDDMFPLEEVAKLGYNVFYHGQKGHYGVALLTKETPIAVRRGFPGDDEEAQRRIIMAEIPSLLGNVTVINGYFPQGESRDHPIKFPAKAQFYQNLQNYLETELKRDNPVLIMGDMNISPTDLDIGIGEENRKRWLRTGKCSFLPEEREWMDRLMSWGLVDTFRHANPQTADRFSWFDYRSKGFDDNRGLRIDLLLASQPLAECCVETGIDYEIRSMEKPSDHAPVWATFRR", "text": "FUNCTION: Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'- 5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and ribonuclease H activities. SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family."}
+{"protein": "MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKKLTLQSAKSRVAFFEEL", "text": "FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex (By similarity). Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell projection Cytoplasm, cytoskeleton Nucleus Note=Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with DCAF1 in the nucleus. The intramolecular association of the FERM domain with the C-terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions (By similarity)."}
+{"protein": "MSAAPTTAPVAAVSKKGKKSGDTINSKLALTMKSGKYVLGYKSTLKTLRSGKAKLILIAANAPPLRKSELEYYAMLSRCSVHHYSGNNIDLGTACGKLFRVGVLAVIDAGDSDILAA", "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 eL30 family."}
+{"protein": "MAKVTANDLLERFQLELLSGEEGIHRSITTSDISRPGIEMAGFFTYYPAKRLQLLGRTELSFYKQLSPVDKEERMSKLCTYDTPGIIISRGLEVPPELLKASEKVGVPVLRSNITTTRLSSMLTNFLESQLAPTTAVHGVLVDIYGIGVLITGSSGVGKSETALDLVRRGHRLVADDSVEIRREHEDTLVGRSPELIQHLLEIRGLGIINVMTLFGAGAVRPFKRIALCVNLELWDQKKVYDRLGLSEDYLRIMNVDIPKLTIPVRPGRNLAVIIEVAAMNFRLKRLGINAAQQFSDRLNDVIEEGEQEF", "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. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on a specific serine residue. Therefore, by controlling the phosphorylation state of HPr and crh, 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 (By similarity). SIMILARITY: Belongs to the HPrK/P family."}
+{"protein": "MAVLWRLSAVCGAQGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPGHHSGSKAASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAATLTLHGHWGLGQVVTDYVHGDASQKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL", "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": "MRSAIAAPILFLLVSFFVQECESVGFAPELYCGLENCYDVLEVNREEFDKQKLAKAYRALARKHHPDRVKNKEEKLLAEERFRVIATAYETLKDDEAKTNYDYYLDHPDQRFYNYYQYYRLRAAPKVDLRIVIVGTILIISLFQFLSAKHKFSEAIEYATGVGKFRNMAIKDGIDKGLLEMDRNGKLKKNKGVDNDEVIKQIIIDNLDVTGGYKRESIYDTLAWHTIIFPLTIFRYIKWTALWYWRFAIQKEEYDDDAKLYLIRKYIGVSQMEFDQKYTDEDIDDLFERECWLKRNCATWKAERDAAEQEKMAQSGRYKRYKRYMKNAGTISFVDED", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DNAJC25 family."}
+{"protein": "MLARALLLCAAVVCGAANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPDTVHYILTHFKGVWNIVNKISFLRNMIMRYVLTSRSHLIESPPTYNVHYSYKSWEAFSNLSYYTRALPPVPDDCPTPMGVKGRKELPDSKEVVKKVLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTDIERGPAFTKGKNHGVDLSHVYGESLERQHNRRLFKDGKMKYQMINGEMYPPTVKDTQVEMIYPPHIPEHLKFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDVFQIDGQEYNYQQFIYNNSVLLEHGVTQFVESFTRQIAGRVAGRRNLPAAVEKVSKASLDQSREMKYQSFNEYRKRFLLKPYESFEELTGEKEMAAELEALYGDIDAMELYPALLVEKPAPDAIFGETMVEAGAPFSLKGLMGNPICSPEYWKPSTFGGEVGFKIINTASIQSLICSNVKGCPFTSFSVQDAHLTKTVTINASSSHSGLDDINPTVLLKERSTEL", "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 (PubMed:9448728, PubMed:10438452). 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 (PubMed:10438452). 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 (By similarity). 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 (By similarity). 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 (By similarity). Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response (By similarity). Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation (By similarity). Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs) (By similarity). 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 (By similarity). 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 (By similarity). In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). 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 (PubMed:9448728). SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein Endoplasmic reticulum membrane; Peripheral membrane protein Nucleus inner membrane; Peripheral membrane protein Nucleus outer membrane; Peripheral membrane protein Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. SIMILARITY: Belongs to the prostaglandin G/H synthase family."}
+{"protein": "MTSRTKSSKNLGTIALAGMVVSSIIGGGIFSLPQNMAATAGAGAVILSWILTGFGMFFIANTFRILSTIRPDLKEGIYMYSREGFGPYIGFTIGWGYWLCQIFGNVGYAVITMDALNYFFPPYFQGGNTLPAILGGSILIWVFNFIVLKGIRQASIINVIGTIFKIIPLIIFIILTAFFFKLAVFKTDFWGHAVTKAQPSLGSVSSQLKGTMLVTLWAFIGIEGAVVMSGRAKNPLSVGQATVLGFLGCLTIYILFSLLPFGSLFQHQLANIPNPSTAGVLDILVGKWGEVLMNVGLIIAVLSSWLSWTIIVAEIPFSAAKNGTFPEIFTIENKEKSPSVSLYITSSVMQLAMLLVYFSSNAWNTMLSITGVMVLPAYLASAAFLFKLSKSKTYPKKGSIKAPLAMITGILGVVYSLWLIYAGGLKYLFMALVLLALGIPFYIDAGKKKKNAKTFFAKKEIVGMTFIGLLALTAIFLFSTGRIKI", "text": "FUNCTION: Catalyzes the exchange of L-arginine for agmatine. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response. 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": "MIATIVTSVSIIFVVLGALISAFAATGLIRLRDVYSRAHAAGKAATLGAMFLLFGAFLYFIGTEGYVNMQLIIGIIFVFITGPLSSHLIMKAAYNIKTPYTKDTKIDEIKEDMKHTKL", "text": "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 G family."}
+{"protein": "MPIAGTKYAPFPAPQLDDRTWPSKRIEKAPIWCSVDLRDGNQALIDPMGHDRKERMFRLLIDMGFPEIEIGFPSASQTDFDFCRWAIEQGDVPDDVDLQVLVQCRPELITRTFEALEGAKTPIIHFYNSTSELQRRVVFAKDVGGIKQIATDAAKMIMDMAAKAGGGYRFQYSPESFTGTELDVALEICNAVIEIVKPTPDNKLIVNLPSTVEMNTPNVYADQIEWMCRNLDNRESLIISLHPHNDRGTGIAATELGLMAGADRGEGTLFGNGERTGNVDVVTLALNMYTQGIDPGLDCTDINRMKEVYEYSNQLKIAERHPYVGELVYTAFSGSHQDAINKGMKARRSANSPVWEVPYLPIDPQDVGRSYEAIIRINSQSGKGGIAYILQADYGLNLPRNLQVEFREIIQHITDEEGKELPSKRIYEEFQKLYVTQPDARIKFVDHHTYPHPEQKGRRILTAEITDNGVTKTIEGKGTGPIDGFVDALSKYLGVKMSVVDYSEHSLQQGSDASAISYVEMVYPGGKLFGVGINDNIVSASLEAVVSAANRVIAK", "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": "SGSCTLKTCWKKMPTFRDVGNRLKSYFDGAVKVTGGNSGENLIPEDETVKQPTIKDLVYSMESHDFCEPDRKSGSLGTEGRRCNSTSMDVGGCDIMCCGRGYHEVLAEKRENCRCRF", "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": "MAAQRKAQDEYGAASITILEGLEAVRKRPGMYVGSTGERGLHHLIWEVVDNSVDEAMAGYATQVDVRLFDDGSVEVADNGRGIPVAVHATGVPTVDVVMTQLHAGGKFGGKDSGYNVSGGLHGVGVSVVNALSTRVEVDIKRDGYEWSQFYDKAVPGILKQGEATEATGTTIRFWADPDIFETTKYDFGTVARRIQEVAFLNKGLTINLVDERVKQDEVVDDVVSDTAEAPVAMTVEEKSTESSAPHKVRHRTFHYPGGLVDFVKHINRTKTPIQQSIIDFDGKGAGHEVEVAMQWNGGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDKKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQRVCNEQLIHWFEANPVDAKAVVNKAISSAQARIAARKARELVRRKSATDLGGLPGKLADCRSTDPRSSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDISRLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIEHGYVFLAQPPLYKLKWQRMDPEFAYSDSERDGLLETGLKLGKKINKEDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV", "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 (PubMed:17325221). 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": "MSQNITLIKDKILSDNYFTLRNITYDLTRRNGKVIRHKREVYDRGNGATILLYNSTKKTVVLVRQFRVATWVNGNEDGMLIETCAGLLDNDEPEVCIRKEAIEETGYDVGEVRKIFELYMSPGGVTELIHFFIAEYRDSERASTGGGVEDEDIEVLELPFSRALEMARSGEIRDGKTVLLLNYLHMSHLMG", "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": "MLYELIGLVRITNSNAPKLEAKELSSTIGKLIIQNRGVVRDIVPMGIRYLPKIMKKDQEKHFRAYHFLMLFDSSAAVQSEILRTLKKDPRVIRSSIVKVDLDKQLDRASSLHRSLGKKSILELVNEDYQSI", "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 bacterial ribosomal protein bS6 family."}
+{"protein": "MDAMDLTVAKFKEFTQLQSSAILLTVVSGIIVIVILLLRSKRRSSLKLPPGKLGLPLIGESLSFLWALRSNTLEQFVDKRVKKYGNVFKTSLLGQPTVVLCGAAGNRLILSNQEKLLSRTVSDRVAKLTGDTSISVIAGDSHRIIRAAVAGFLGPAGLKIHIGEMSAHIRNHINQVWKGKDEVNVLSLARELVFAISASLFLNINDREEQHQLHKTLETILPGYFSVPINFPGFAFRKALEGNSKRRKHFSVLQEKRRRDLSVGLASRTQDLLSVLLAYEDDKGNPLTDEEVLDNISALIDGSYESTSSQMAMLLKLLSDHPECYEKVVQEQLEIASHKKEGEEITWKDVKAMRYTWQVMQETLRMFAPVFGPRGKAITDIHYDGYTIPKGWQLSWATYSTHQNDTYFNEPDKFMPSRFDEEGGRLAPYTFVPFGGGRRKCPGWEFAKTEILLFVHHFVKTFSAYTPIDPHESIWGRPLPPVPANGFPIKLISRS", "text": "FUNCTION: Catalyzes the conversion of taxusin to 2-alpha-hydroxytaxusin in taxol biosynthesis (PubMed:15178487). Catalyzes the conversion of 7- beta-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis (PubMed:15178487). SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MPGGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPAEKDEKGMPGTARVVFVFGPDKKLKLSILYPATTGRNFDEILRVVISLQLTAEKRVATPVDWKDGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGRKYLRYTPQP", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (By similarity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (By similarity). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity). SUBCELLULAR LOCATION: Cytoplasm Lysosome Note=Also found in lung secretory organelles (lamellar bodies). SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily."}
+{"protein": "MGAYKYLEELQRKKQSDVMRFLYRVRCWEYRQKNVIHRASRPSRPDKARRLGYKAKQGFVIYRIRVRRGGRKRPVPKGATYGKPTNQGVNQLKYQKSLRSTAEERVGRRASNLRVLNSYWVNQDSTYKYFEVILVDPSHKAIRRDARYNWIVNPVHKHREARGLTSAGKKSRGINKGHLFNKTKAGRRHTWKKHNTLSLWRYRS", "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": "MAGSLSSAIFNVLKYSGMASLAVTLIALGFLYKYQKTLVYPSAFPQGSRENVPTPKEFNMEYERIELRTRDKVTLDSYLMLQSESPESRPTLLYFHANAGNMGHRLPIARVFYSALNMNVFIISYRGYGKSTGSPSEAGLKIDSQTALEYLMEHPICSKTKIVVYGQSIGGAVAIALTAKNQDRISALILENTFTSIKDMIPTVFPYGGSIISRFCTEIWSSQDEIRKIKKLPVLFLSGEKDEIVPPPQMVLLFGLCGSAKKKFHSFPKCTHNDTCLGDGYFQVIADFLAENDINTPAS", "text": "FUNCTION: Suppressor of bem1/bud5. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the serine esterase family."}
+{"protein": "MARHSIKMIALLTAFGLASAAMTVQAAERIAFIPKLVGVGFFTSGGNGAQEAGKALGIDVTYDGPTEPSVSGQVQLVNNFVNQGYDAIIVSAVSPDGLCPALKRAMQRGVKILTWDSDTKPECRSYYINQGTPKQLGSMLVEMAAHQVDKEKAKVAFFYSSPTVTDQNQWVKEAKAKISKEHPGWEIVTTQFGYNDATKSLQTAEGIIKAYPDLDAIIAPDANALPAAAQAAENLKRNNLAIVGFSTPNVMRPYVQRGTVKEFGLWDVVQQGKISVYVANELLKNMPMNVGDSLDIPGIGKVTVSPNSEQGYHYEAKGNGIVLLPERVIFNKDNIDKYDF", "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": "MSAYYRNNWSEEDPDYPDYSGSQNRTQGYLKTQGYPDVPGPLNNPDYPGTRSNPYSVASRTRPDYPGSLAEPNYPRSLSNPDYSGTRSNAYSAASRTSPDHPTSLPEPDYSEFQSHPYHRASSRQPDYPGSQRNPDFAGSSSSGNYAGSRTHPDHFGSLEPDYPGAQSNSDHPGPRANLNHPGSRKNLEHTSFRINPYADSLGKPDYPGADIQPNSPPFFGEPDYPSAEDNQNLPSTWREPDYSDAENGHDYGSSETPKMTRGVLSRTSSIQPSFRHRSDDPVGSLWGENDYPEGIEMASMEMANSYGHSLPGAPGSGYVNPAYVGESGPVHAYGNPPLSECDWHKSPQGQKLIASLIPMTSRDRIKAIRNQPRTMEEKRNLRKIVDKEKSKQTHRILQLNCCIQCLNSISRAYRRSKNSLSEILNSISLWQKTLKIIGGKFGTSVLSYFNFLRWLLKFNIFSFILNFSFIIIPQFTVAKKNTLQFTGLEFFTGVGYFRDTVMYYGFYTNSTIQHGNSGASYNMQLAYIFTIGACLTTCFFSLLFSMAKYFRNNFINPHIYSGGITKLIFCWDFTVTHEKAVKLKQKNLSTEIRENLSELRQENSKLTFNQLLTRFSAYMVAWVVSTGVAIACCAAVYYLAEYNLEFLKTHSNPGAVLLLPFVVSCINLAVPCIYSMFRLVERYEMPRHEVYVLLIRNIFLKISIIGILCYYWLNTVALSGEECWETLIGQDIYRLLLMDFVFSLVNSFLGEFLRRIIGMQLITSLGLQEFDIARNVLELIYAQTLVWIGIFFCPLLPFIQMIMLFIMFYSKNISLMMNFQPPSKAWRASQMMTFFIFLLFFPSFTGVLCTLAITIWRLKPSADCGPFRGLPLFIHSIYSWIDTLSTRPGYLWVVWIYRNLIGSVHFFFILTLIVLIITYLYWQITEGRKIMIRLLHEQIINEGKDKMFLIEKLIKLQDMEKKANPSSLVLERREVEQQGFLHLGEHDGSLDLRSRRSVQEGNPRA", "text": "FUNCTION: Probable ion channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMC family."}
+{"protein": "MYTLSVADHSNTPPAIKIPERYNAADDLIGRNLLAGRGGKTVYIDDAGSYTYDELALRVNRCGSALRTTLGLQPKDRVLVCVLDGIDFPTTFLGAIKGGVVPIAINTLLTESDYEYMLTDSAARVAVVSQELLPLFAPMLGKVPTLEHLVVAGGAGEDSLAALLATGSEQFEAAPTRPDDHCFWLYSSGSTGAPKGTVHIHSDLIHTAELYARPILGIREGDVVFSAAKLFFAYGLGNGLIFPLAVGATAVLMAERPTPAAVFERLRRHQPDIFYGVPTLYASMLANPDCPKEGELRLRACTSAGEALPEDVGRRWQARFGVDILDGIGSTEMLHIFLSNRAGDVHYGTSGKPVPGYRLRLIDEDGAEITTAGVAGELQISGPSSAVMYWNNPEKTAATFMGEWTRSGDKYLVNDEGYYVYAGRSDDMLKVSGIYVSPIEVESALIAHEAVLEAAVVGWEDEDHLIKPKAFIVLKPGYGAGEALRTDLKAHVKNLLAPYKYPRWIEFVDDLPKTATGKIQRFKLRSA", "text": "FUNCTION: Catalyzes the ligation of benzoate and CoA to form benzoyl- CoA at the expense of ATP. The enzyme also ligates 2-aminobenzoate and CoA. The enzyme shows activity toward a number of benzoate derivatives. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. Benzoate-CoA ligase subfamily."}
+{"protein": "MGPLQGDGGPALGGADVAPRLSPVRVWPRPQAPKEPALHPMGLSLPKEKGLILCLWSKFCRWFQRRESWAQSRDEQNLLQQKRIWESPLLLAAKDNDVQALNKLLKYEDCKVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVVNQNMNLVRALLARRASVSARATGTAFRRSPCNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDRHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHTQWTYGPLTSTLYDLTEIDSSGDEQSLLELIITTKKREARQILDQTPVKELVSLKWKRYGRPYFCMLGAIYLLYIICFTMCCIYRPLKPRTNNRTSPRDNTLLQQKLLQEAYMTPKDDIRLVGELVTVIGAIIILLVEVPDIFRMGVTRFFGQTILGGPFHVLIITYAFMVLVTMVMRLISASGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPEELGHFYDYPMALFSTFELFLTIIDGPANYNVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQIVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIQRYAQAFHTRGSEDLDKDSVEKLELGCPFSPHLSLPMPSVSRSTSRSSANWERLRQGTLRRDLRGIINRGLEDGESWEYQI", "text": "FUNCTION: Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:11097838, PubMed:11278579, PubMed:11248124, PubMed:15184369, PubMed:23612980, PubMed:29258289). Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification (PubMed:15184369). Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV6 sub-subfamily."}
+{"protein": "MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYPDSAERSETERSPHRPIERADAVDTGDRPGLRTTRMSWPSSFHGTGTGGGSSRRLEAENGPTPSPGRSPLDSQASPGLVLHAGATTSQRRESFLYRSDSDYDMSPKAVSRSSSVASEAHAEDLIVTPFAQVLASLRSVRSNFSLLTNVPIPSNKRSPLGGPPSVCKATLSEETCQQLARETLEELDWCLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNEVEIPSPTPRQRAFQQPPPSVLRQSQPMSQITGLKKLVHTGSLNTNVPRFGVKTDQEDLLAQELENLSKWGLNIFCVSEYAGGRSLSCIMYTIFQERDLLKKFHIPVDTMMMYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEENCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNRDWYHSAIRQSPSPPLEEEPGGLGHPSLPDKFQFELTLEEEEEEDSLEVPGLPTTEETFLAAEDARAQAVDWSKVKGPSTTVVEVAERLKQETASAYGAPQESMEAVGCSFSPGTPILPDVRTLSSSEEAPGLLGLPSTAAEVEAPRDHLAATRACSACSGTSGDNSAIISAPGRWGSGGDPA", "text": "FUNCTION: [Isoform 1]: Efficiently hydrolyzes cAMP. FUNCTION: Hydrolyzes the second messenger 3',5'-cyclic AMP (cAMP), which is a key regulator of many important physiological processes. FUNCTION: [Isoform 2]: Efficiently hydrolyzes cAMP. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily."}
+{"protein": "MNKILFYLFVYGVVNSAAYDLLKAPNYFEEFVHRFNKDYGSEVEKLRRFKIFQHNLNEIIIKNQNDSAKYEINKFSDLSKDETIAKYTGLSLPIQTQNFCKVIVLDQPPGKGPLEFDWRRLNKVTSVKNQGMCGACWAFATLASLESQFAIKHNQLINLSEQQMIDCDFVDAGCNGGLLHTAFEAIIKMGGVQLESDYPYEADNNNCRMNTNKFLVQVKDCYRYITVYEEKLKDLLRLVGPIPMAIDAADIVNYKQGIIKYCFNSGLNHAVLLVGYGVENNIPYWTFKNTWGTDWGEEGFFRVQQNINACGMRNELASTAVIY", "text": "FUNCTION: Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system (By similarity). SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MSQSETRRGRRGTREETLEKWITARKKAEELEKDLRKARKTIKKLEEENPWLGNILGIIRKGKDGEGAPPAKRPRTDQMEVDSGPGKRPHKSGFTDKEREDHRRRKALENKKKQLSAGGKILSKEEEEELRRLTDEDEERKRRVAGPRVGDVNPSRGGPRGAPGGGFVPQMAGVPESPFSRTGEGLDIRGTQGFP", "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": "MSIDTDFLTSVEVKEDELHGNVLIAVTQIALGRTIGVIDKATPNDSNALLILNLIKEADDGEDANICMRQEDRKTFLQTSKIINIGERLLLQRLSEEECDEEDQDDLENLILLKDEDRPDSTQSCTKSSSEDSNLNGFEEYIREHGELVPGQTPPDGSHKCGVCPKSFSSASGLKQHSHIHCSLKPFRCHLCPKSYTQFSNLCRHRRVHSDGWTCPTCQSQMPSQAALTKHRPVCEMTALYKPLMAQLAGLSGAGGLGSVPYWPHILQMATQAPHFPLAFLAANPEAYKLMQQTTCASPDAECSSGHASESSPTTTEPVDLTATPKPPSTSEMETTSKSDDGEDRDSIGDSGNDDDDDSEAGVLDESSTTTSTKKRPTSHTISDILAAPQLGAQALNSTFLGMLQRSLNYNPAVPSPHSFLRAMSGAKASSSPSSSSGSGKDRYTCKFCQKVFPRSANLTRHLRTHTGEQPYKCQYCERSFSISSNLQRHVRNIHNKPNTSLTPHNHHRQRSLHNSTSTSTTTTTVHHPLLHLPGTSVPVPKV", "text": "FUNCTION: Probable transcription factor, required for migration of the hermaphrodite-specific motor neurons (HSNs) from the tail to the gonad primordium during HSN cell differentiation (PubMed:8224840, PubMed:10049362). Required for phasmid neuron development (PubMed:8224840). Required to specify the pi-cell fate of ventral uterine precursor cell (VU) cells (PubMed:17573066). FUNCTION: [Isoform b]: Dispensable for anchor cell (AC) invasion and for preventing AC proliferation. FUNCTION: [Isoform a]: Probable transcription factor, involved in lin- 12 (Notch)-dependent anchor cell (AC) and ventral uterine (VU) precursor cell fate specification and in AC invasion (PubMed:17215301, PubMed:17573066, PubMed:32203506). Prevents AC proliferation after AC cell specification by repressing lin-12 expression (PubMed:32203506). May form a positive feedback loop, together with the transcription factor fos-1, that maintains mutual high levels of expression and so activates AC invasion (PubMed:32203506). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "ESARNPTIYPLTLPPALSSDPVIIGCLIHDYFPSGTMNVTWGKSGKDITTVNFPPALASGGRYTMSNQLTLPAVECPEGESVKCSVQHDSNPVQELDVNCSGPTPPPPITIPSCQPSLSLQRPALEDLLLGSDASITCTLNGLRNPEGAVFTWEPSTGKDAVQKKAVQNSCGCYSVSSVLPGCAERWNSGASFKCTVTHPESGTLTGTIAKVTVNTFPPQVHLLPPPSEELALNELLSLTCLVRAFNPKEVLVRWLHGNEELSPESYLVFEPLKEPGEGATTYLVTSVLRVSAETWKQGDQYSCMVGHEALPMNFTQKTIDRLSGKPTNVSVSVIMSEGDGICY", "text": "FUNCTION: Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system."}
+{"protein": "MIPLEKPGSGGSPSAAASGSGPGGLLTEIRTAIRTEPFQDCYSLSPGRELGRGKFAVVRKCIQKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQDNPWVINLHEVYETSSEMILVLEYAAGGEISDQCVADRDEAFNEKDVQRLMRQILEGVHFLHTHDVVHLDLKPQNILLTSESPLGDIKIVDFGLSRIVKNSEELREIMGTPEYVAPEILSYDPISMATDMWSIGVLTYVMLTGISPFLGDNKQETFLNISQMNLSYSEEEFDTVSESAVDFIKKLLVKKPEDRATAEECLKHPWLTQSSIQDPVLRVKEALEEANALQKGDSVPEISSATEKPGTEESIVTEELIVVTSYTLGQCRQSEKEKMEQKAISKRFKFEEPLLQEIPGEFIY", "text": "FUNCTION: Acts as a positive regulator of apoptosis. May also act as a regulator of cellular reactive oxygen species. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily."}
+{"protein": "MEAALAVTRLPPNDPRTPALSVVDMHTGGEPLRIVHAGCPEVAGPTLLAKRRYMRQHLDYIRRRLVFEPRGHRDMYGAILVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGLVPAPPKGAREAQVNIHCPCGLVTAFVECEGGRSCGPVRFHSVPAFVLASDLTVDVPGHGKVLVDIAYGGAFYAFVSAEKLGLDVCSAKTRDLVDAASALTGAVKAQFKINHPESEDLGFLYGSILTDGKDAYSEEATTNICVFADEQVDRSPTGSGVTARIALQYHKGLLQLNQTRAFKSSATGSVFTGCAVREAKCGDFKAVIVEVAGQAHYTGTANLTVEDGDPLRDGFLLK", "text": "FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline to delta-1-pyrroline-2-carboxylate (Pyr2C). SIMILARITY: Belongs to the proline racemase family."}
+{"protein": "MGSDRSALGRPGCTGSCLSSRASLLPLLLVLLDCLGHGTASKDAEVYAAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQSFYGIPVTGVLDEETKTWMKRPRCGVPDQFGVHVKANLRRRRKRYTLTGKAWNNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVSYDDIRLRRRAEADIMVLFASGFHGDSSPFDGVGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTDNFQLPEDDLRGIQQLYGSPDGKPQPTRPLPTVRPRRPGRPDHQPPRPPQPPHPGGKPERPPKPGPPPQPRATERPDQYGPNICDGNFDTVAVLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGNISAAYERQDGHFVFFKGNRYWLFREANLEPGYPQPLSSYGTDIPYDRIDTAIWWEPTGHTFFFQADRYWRFNEETQHGDPGYPKPISVWQGIPTSPKGAFLSNDAAYTYFYKGTKYWKFNNERLRMEPGHPKSILRDFMGCQEHVEPRSRWPDVARPPFNPNGGAEPEADGDSKEENAGDKDEGSRVVVQMEEVVRTVNVVMVLVPLLLLLCILGLAFALVQMQRKGAPRMLLYCKRSLQEWV", "text": "FUNCTION: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein; Extracellular side. SIMILARITY: Belongs to the peptidase M10A family."}
+{"protein": "MKPYLFDLKLKDTEKLDWKKGLSSYLKKSYGSSQWRTFYDEKATSELDHLRNNANGELAPSSLSEQNLKYYSFLEHLYFRLGSKGSRLKMDFTWYDAEYSSAQKGLKYTQHTLAFEKSCTLFNIAVIFTQIARENINEDYKNSIANLTKAFSCFEYLSENFLNSPSVDLQSENTRFLANICHAEAQELFVLKLLNDQISSKQYTLISKLSRATCNLFQKCHDFMKEIDDDVAIYGEPKWKTTVTCKLHFYKSLSAYYHGLHLEEENRVGEAIAFLDFSMQQLISSLPFKTWLVEFIDFDGFKETLEKKQKELIKDNDFIYHESVPAVVQVDSIKALDAIKSPTWEKILEPYMQDVANKCDSLYRGIIPLDVYEKESIYSEEKATLLRKQVEETETANLEYSSFIEFTNLPRLLSDLEKQFSDGNIFSNTDTQGQLMRDQIQTWCKFIQTNEFRDIEEQMNKIVFKRKQILEILSALPNDQKENVTKLKSSLVAASNSDEKLFACVKPHIVEINLLNDNGKIWKKFDEFNRNTPPQPSLLDIDDTKNDKILELLKQVKGHAEDLRTLKEERSRNLSELRDEINNDDITKLLIINKGKSDVELKDLFEVELEKFEPLSTRIEATIYKQSSMIDDIKAKLDEIFHLSNFKDKSSGEEKFLEDRKNFFDKLQEAVKSFSIFASDLPKGIEFYDSLFNMSRDLAERVRVAKQTEDSTANSPAPPLPPLDSKASVVGGPPLLPQKSAAFQSLSRQGLNLGDQFQNLKISAGSDLPQGPGIPPRTYEASPYAATPTMAAPPVPPKQSQEDMYDLRRRKAVENEERELQENPTSFYNRPSVFDENMYSKYSS", "text": "FUNCTION: Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinase to the endosomes, leading to deubiquitination of cargo proteins prior to the lumenal sequestration. Its association to the endosomes depends on SNF7 and its dissociation requires VPS4. Interacts functionally with the Pkc1p- mitogen-activated protein kinase pathway. SUBCELLULAR LOCATION: Cytoplasm. Endosome."}
+{"protein": "MADAPPTDEGWFVLHDCYTVDWDAWRDAPERDRTAALDDAASFLADREALADADEGESGVFSITGQKADLLFVHFRESLDELDRIQRAFEQTAFAEYTERAHSYVSVVEISGYTAPDYFEDPDSVDDGLRQYFESKLTPEIPDDTYVSFYPMSKRRQPEQNWYDLPIEERAEMMDVHGDLGKQYAGKVSQVIASSVGLDDMEWGVTLFADDLTDIKDIVYEMRFDEVSAKYGAFGDFFVGRRFPPADLPAFMAGERVPAPEGGADAHGEGERTHHHGDSDHHDGDDGEQHHHSTGDEADDGIRGELADEDIYAGQPHGEDVYATVLYSEAGADDLFEEVEGLRGNFEHYDTHVKTAVYDGHEADRRAVVSIWDTASAADTAAGFLADLPEVVERAGEESGFGTMGMFYETKPEHTAEFVEKFDTVAGVLADMDGHFDTDLMVNVENDDDMFIASQWRSQEDAMAFFRSDDFGDTVDWGRDVLADRPRHVFLA", "text": "SIMILARITY: In the N-terminal section; belongs to the ChdC family."}
+{"protein": "MDSAVDGPRQPPARAGSRLCTRCGERKAALKRPKTLEQICRECFYVVFEDEIHQTIVDNNLFKPGDRVAIGASGGKDSTVLAYVLSELNRRHKYCLDLFLLSVDEGITGYRDDSLETVKRNEIQYGLPLKIVSYKDLYGWTMDDIVKAIGLKNNCTFCGVFRRQALDRGAALLKVDKIVTGHNADDIAETVLLNILRGDIARLSRCTFITTGEDGPIPRCKPFKYTYEKEIVMYAYFKKLDYFSTECIYSPNAYRGFAREFIKDLERMRPRAILDIIKSGENFRISTTTRMPEQGTCERCGYISSQKLCKACVLLDGLNRGLPKLGIGRTKGIAGGDGDCEQQATRSERNRSSLQGKHGNFDF", "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": "MAALTLLSSRLRLCASAYRSGGAWSQGCAGYFSTSTRRHTKFYTDAVEAVKDIPNGATVLVGGFGLCGIPENLIGALLKTGVKELTAVSNNAGVDNFGLGLLLQSKQIKRMISSYVGENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSIAIASKPREVREFNGQHFILEEAIRGDFALVKAWKADQAGNVTFRKSARNFNLPMCKAAETTVVEVEEIVDIGSFAPEDIHIPKIYVHRLVKGEKYEKRIERLSVRKEEDVKTRSGKLGDNVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGILGLGPYPLQNEVDADLINAGKETVTVLPGASYFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKLVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDSKKGLTLIELWEGLTVDDIKKSTGCDFAVSPKLIPMQQVTT", "text": "FUNCTION: Key enzyme for ketone body catabolism (By similarity). Catalyzes the first, rate-limiting step of ketone body utilization in extrahepatic tissues, by transferring coenzyme A (CoA) from a donor thiolester species (succinyl-CoA) to an acceptor carboxylate (acetoacetate), and produces acetoacetyl-CoA. Acetoacetyl-CoA is further metabolized by acetoacetyl-CoA thiolase into two acetyl-CoA molecules which enter the citric acid cycle for energy production (PubMed:11327867, PubMed:17718512) (Probable). Forms a dimeric enzyme where both of the subunits are able to form enzyme-CoA thiolester intermediates, but only one subunit is competent to transfer the CoA moiety to the acceptor carboxylate (3-oxo acid) and produce a new acyl- CoA (PubMed:11327867). Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (PubMed:17718512). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family."}
+{"protein": "MALLKSFIDVGSDSHFPIQNLPYGVFKPESNSTPRPAVAIGDLVLDLSAISEAGLFDGLILKDADCFLQPNLNKFLAMGRPAWKEARSTLQRILSSNEPILRDNDVLRRKSFHQMSKVEMIVPMVIGDYTDFFASMHHAKNCGLMFRGPENAINPNWFRLPIAYHGRASSIVISGTDIIRPRGQGHPQGNSEPYFGPSKKLDFELEMAAVVGPGNELGKPIDVNNAADHIFGLLLMNDWSARDIQAWEYVPLGPFLGKSFGTTISPWIVTLDALEPFGCQAPKQDPPPLPYLAEKESVNYDISLEVQLKPSGRDDSCVITKSNFQNLYWTITQQLAHHTVNGCNLRPGDLLGTGTISGPEPDSYGCLLELTWNGQKPLSLNGTTQTFLEDGDQVTFSGVCKGDGYNVGFGTCTGKIVPSPP", "text": "FUNCTION: Converts fumarylacetoacetate to acetoacetate and fumarate (PubMed:22980205). Involved in tyrosine catabolic pathway. Catalyzes the final step in the tyrosine degradation pathway (PubMed:22980205, PubMed:23743712, PubMed:27097641). SIMILARITY: Belongs to the FAH family."}
+{"protein": "MSCFSQVLNPITGENSWQEREDDYDYHQEVANAGFGDMLHDWERNQKYFAALRKTIAEMRTAGKEVHVLDIGTGTGILSMMALEAGADSVTACEAFLPMANCAEKILAANGAADKVRLIRKRSTDIQIGEDMPRKANLLVAELLDTELIGEGAIGIYNHAHDELLTEDALCIPARARCYAQVAQSPLAAQWNSLKSLANLDGEPLLQPPAQLKGCKGEAGLHDVQLSQLPSHTFRPLTDPVEIFQFDFQRKKQREKKRDQLLKVQSNQPGSAELVFYWWDIQLDDGGEILLSCAPYWAHPEIHELSGKKGKDLPLPNVVPWRDHWMQAIYYIPKPLQLLEAGKSFHLSCHHDEYSLWFDAREEAPAKSVSRHTCTCDLHMTYSRSRIGQMNQSTRNKRYLRYLEENIEAEKSKVLVLGNGCLLGLASSALGATSVQLHEPHRFSRRLLESIVQHNQLKNVEFVDKVEEVEDSQLAGLTHVFAEPYFLNAILPWDNFYFGTLLAKIKDKLPEDVKISPCSARIYALPVEFLDLHKIRAPVVSCEGFDLRLFDEMVERSAEQAVTLVEAQPLWEYPCRALSEPQEILNVDFNKFSEEHHLKGTIDLKHPGTCNGVALWVDWQLINDSSPRSIVSTGPSEAVTPGEFVKWDMFVRQGVHFPQKTNQTISSLAWSTDFKPLLGQLSFTFGQKKP", "text": "FUNCTION: Essential arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3 (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily."}
+{"protein": "MKEKKGHYVPPSYIPLTQSDADTEVETTTPNLEIAVSESTKDDPRQWSSGICACFDDMQSCCVGLFCPCYIFGKNAELLGSGTFAGPCLTHCISWALVNTICCFATNGALLGLPGCFVSCYACGYRKSLRAKYNLQEAPCGDFVTHFFCHLCAICQEYREIREQSSGSYPLDMKMAITNAPLAQTMESAN", "text": "FUNCTION: May be involved in cadmium resistance. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cornifelin family."}
+{"protein": "MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDRFLEEIMTKREDLVVAPAGVTLKEANEILQRSKKGKLPIVNESDELVAIIARTDLKKNRDYPLASKDTKKQLLCGAAIGTHEDDKYRLDLLALAGVDVVVLDSSQGNSIFQINMIKYIKEKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHGLHSYEKRLF", "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. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytosol Note=Can form fiber-like subcellular structures termed 'cytoophidia' in response to intracellular guanine- nucleotide depletion. SIMILARITY: Belongs to the IMPDH/GMPR family."}
+{"protein": "MSQPSGGRAPGTRIYSWSCPTVMSPGEKLDPIPDSFILQPPVFHPVVPYVTTIFGGLHAGKMVMLQGVVPLDAHRFQVDFQCGCSLCPRPDIAFHFNPRFHTTKPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAVGFLNINPFVEGSREYPAGHPFLLMSPRLEVPCSHALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTLAWISRWGQKKLISAPFLFYPQRFFEVLLLFQEGGLKLALNGQGLGATSMNQQALEQLRELRISGSVQLYCVHS", "text": "FUNCTION: Binds lactose. May participate in the apoptosis of adipocytes. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTTTSNLLLESEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREDQQQQHQQRDVIDEPIIEEPSRLQESVMEASRTNIDESAMPPPPPQGVKRKAGQIDPEPVMPPQQVEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEDDEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII", "text": "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 (PubMed:11509732). The cohesin complex may also play a role in spindle pole assembly during mitosis (PubMed:11590136). In interphase, cohesins may function in the control of gene expression by binding to numerous sites within the genome (By similarity). May control RUNX1 gene expression (Probable). Binds to and represses APOB gene promoter (PubMed:25575569). May play a role in embryonic gut development, possibly through the regulation of enteric neuron development (By similarity). FUNCTION: [64-kDa C-terminal product]: May promote apoptosis. 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 (PubMed:11590136, PubMed:11073952). Before prophase, scattered along chromosome arms (PubMed:11073952). During prophase and prometaphase, most cohesins dissociate from the arms of condensing chromosome, possibly through PLK1-mediated 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 (PubMed:11073952, PubMed:11509732). SIMILARITY: Belongs to the rad21 family."}
+{"protein": "MKVFVLNGPNLGRLGKREPA", "text": "FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. Is involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids. SIMILARITY: Belongs to the type-II 3-dehydroquinase family."}
+{"protein": "MNKARKTYVLKLYVAGNTPNSVRALKTLKNILEQEFQGIYALKVIDVLKNPQLAEEDKILATPTLSKILPPPVRKIIGDLSDRERVLIGLDLLYEELTEEDWEAQSNL", "text": "FUNCTION: 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, KaiA and CikA. KaiA and CikA compete for binding to KaiB(fs), and KaiB(fs) and SasA compete for binding to KaiC, thus the clock oscillator and output signal pathway are tightly coupled. FUNCTION: Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB to form the KaiB(6):KaiC(6) complex, leading to changes in output regulators CikA and SasA. KaiB switches to a thioredoxin-like fold (KaiB(fs)) when bound to KaiC. KaiB(6):KaiC(6) formation exposes a site for KaiA binding that sequesters KaiA from KaiC, making the KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC autodephosphorylation. SIMILARITY: Belongs to the KaiB family."}
+{"protein": "MAHQLKLLKDDFFASDQQAVAVADRYPQDVFAEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVLQNIIYCPERLKLNLDWQGAIPGFSASAGQPHWRLGSMGMAQARQVIGQLEHESSQHVPFANEMAELLFGQLVMLLNRHRYTSDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWRHLNSQKD", "text": "FUNCTION: Activates expression of the rhaSR operon in response to L- rhamnose. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MNTLIAQIEKGKPFFEKISRNIYLRAIRDGFISAMPVILFSSIFLLIAYVPNIFGFTWPKGIENMLMTPYNYTMGIIGFLVAGTTAKSLTDSMNRQLEKTNQINFISTMLASMAGFLIMAADPAKEGGFLSAFMGTKGLLTAFIAAFITVNVYKICVKNNVTIRMPEEVPPNISQVFKDIFPFAFSIIILYAIQLAIKAVIGVNVAQSIGTLLAPLFSAADGYLGITIIFGAYALFWFVGIHGPSIVEPAIAAITYSNVELNAHLIHAGQHADKVITSGTQMFIVTMGGTGATLVVPFMFMWLCKSKRNKAIGRASVVPTFFGVNEPILFGAPIVLNPVFFIPFILAPIVNVWIFKFFVDTLGMNSFFANLPWTTPGPIGIVLGTGFAVLSFVLAALLILVDTVIYYPFVKVYDEQILAEEAEGKSSSDALKEKVAANFDTKKADAILEGAESKEEPATHAITEETNVLVLCAGGGTSGLLANALNKAAEEYGAPVKAAAGSYGAHREILDQYQLVILAPQVASNYEDMKAETDKLGIKLAKTEGAQYIGLTRDGKGALAFVEEQFKD", "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: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MTSSVSFASFRFPWLLKTFVLMVGLATVAFMVRKVSLTTDFSTFKPKFPEPARVDPVLKLLPEEHLRKLFTYSDIWLFPKNQCDCNSGKLRMKYKFQDAYNQKDLPAVNARRQAEFEHFQRREGLPRPPPLLAPPNLPFGYPVHGVEVMPLHTILIPGLQYEGPDAPVYEVILKASLGTLNTLADVPDDEVQGRGQRQLTISTRHRKVLNFILQHVTYTSTEYYLHKVDTVSMEYESSVAKFPVTIKQQTVPKLYDPGPERKIRNLVTIATKTFLRPHKLKILLQSIRKYYPDITVIVADDSKEPLEINDDYVEYYTMPFGKGWFAGRNLAISQVTTKYVLWVDDDFLFSDKTKIEVLVDVLEKTELDVVGGSVQGNTYQFRLLYEQTKNGSCLHQRWGSFQALDGFPGCTLTSGVVNFFLAHTEQLRRVGFDPILQRVAHGEFFIDGLGRLLVGSCPGVIINHQVRTPPKDPKLAALEKTYDKYRANTNSVIQFKVALQYFKNHLYCST", "text": "FUNCTION: Responsible for synthesis of murine T-lymphocyte CT antigen. Can transfer N-acetylgalactosamine moiety from UDP-GalNAc to the low molecular weight acceptor 3'-sialyl-N-acetyllactosamine, to form a non- reducing terminal tetrasaccharide Sda blood group structure. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
+{"protein": "MSDKGELMEEIMEAKVMWYPDSKKITQMDQFRNRVNRNLGLRLANYNELYQWSVEFYPEFWAEFWDFSGIVYSKTYDEVIDRSKGIADVPEWFKGSRLNYAENLLKHKENDKIALYSAREGKENIEKVTFAELRRDVALFAAAMRKMGIKTGDRVAGYLPNCIQTVEAMLAAASIGAIWSATSPDFGVNGVLDRFSQIQPKLILSVESVIYNGKEHCHLEKLQHVVKGLPDLKKVVVIPYVLPKEKIDISKIPNSMFLDEFLATGKVGDQSPQLEFEQLPFNHPLYIMYSSGTTGAPKCMVHSAGGTLIKHLTEHILHGSTTSSDVIMYYTTAGWMMWNWLITAVATGASLVLYDGSPLVPSLNVLWDLVDRLGITILGTGAKWLAVLEDKGLKPCNTHSLQTLHTILSTGSPLKPQSYEYVYKHIKSNVLLGSVSGGTDIIACFMGQNVSVPVYKGEIQARHLGMAIEAWNEEGEAVLGESGELVCLKPLPSQPTHFWNDENGSKYQKAYFAKFPGVWAHGDYCKINPKTGGIVMLGRSDGTLNPNGVRFGSSEIYNIVEAFVEVSDSLCVPQYNKDGDERVILFLKMADKFEFSKELLKRIKDAIRVALSARHVPALILETKDIPYTISGKKVEVAVKQVIAGKEVPHRGAFSNPQSLDLYRNIPELQNF", "text": "FUNCTION: Activates acetoacetate to acetoacetyl-CoA. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "LALLFLVLSAGSGISGPLSCRRKGGICILIRCPGPMRQIGTCFGRPVKCCRSW", "text": "FUNCTION: Has bactericidal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "MEEERGSALAAESALEKNVAELTVMDVYDIASLVGHEFERVIDQHGCEAIARLMPKVVRVLEILEVLVSRHHVAPELDELRLELDRLRLERMDRIEKERKHQKELELVEDVWRGEAQDLLSQIAQLQEENKQLMTNLSHKDVNFSEEEFQKHEGMSERERQVMKKLKEVVDKQRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEPETEPVGEESISDAEKVAMDLKDPNRPRFTLQELRDVLHERNELKSKVFLLQEELAYYKSEEMEEENRIPQPPPIAHPRTSPQPESGIKRLFSFFSRDKKRLANTQRNVHIQESFGQWANTHRDDGYTEQGQEALQHL", "text": "FUNCTION: Plays a role in the regulation of cell shape and polarity (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus (By similarity). Competes with SIAH1 for binding GAPDH (By similarity). Does not regulate lysosomal morphology and distribution (PubMed:14668488). Binds to RAB10 following LRRK2-mediated RAB10 phosphorylation which leads to inhibition of ciliogenesis (PubMed:30398148). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, cilium basal body. SIMILARITY: Belongs to the RILPL family."}
+{"protein": "MPLTRDPFQNPALDKDDSYLGKSRASKKLPYKNPTHLAQQQEPWCRLSSTPTITSMKRDGFFFYSEIPKDDLDFRLAALYNHHTGTFKNKSEILTHQETIQDTRRIKTQFPGEFLPAPQPPLITSRANIRHWINPKKESIHSIQGSIVSPHTAATNGGYSRKNDGGFFST", "text": "FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (PubMed:34715025). May play an important role for the maintenance of myelin-axon integrity (By similarity). May affect intracellular Ca(2+) homeostasis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm Cytoplasm, cytoskeleton."}
+{"protein": "MMSASRLAGTLIPAMAFLSCVRPESWEPCVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQNLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCKDLQVLHQMPLLNLSLDLSLNAMNFIQPGAFKEIRLHKLTLRNSFDSLNVMKTCIQGLAGLEVHHLVLGEFRNEKNLEKFDTSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLANVSSFSLVSVTIKSVKDFSYNFGWQHLELVNCKFGQFPTLELKSLKRLTFTANKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNDVITMGSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLKVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNKTVIGVSVFSVLVVSVVAVLVYKFYFHLMLLAGCIKYGRGENTYDAFVIYSSQDEDWVRNELVKNLEEGVPTFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTG", "text": "FUNCTION: Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (By similarity). Activated by the signaling pathway regulator NMI which acts as damage- associated molecular patterns (DAMPs) in response to cell injury or pathogen invasion, therefore promoting nuclear factor NF-kappa-B activation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Early endosome Cell projection, ruffle Note=Upon complex formation with CD36 and TLR6, internalized through dynamin-dependent endocytosis. Colocalizes with RFTN1 at cell membrane and then together with RFTN1 moves to endosomes, upon lipopolysaccharide stimulation. SIMILARITY: Belongs to the Toll-like receptor family."}
+{"protein": "MAGRISCCLNLPPLDSNSAQSLASLLKTTSKISCRRTENETEPRKNKCSFVLGVAATVVIGGIQINDVASVEAAVVKSPVEEMAAGVVPPRRWSDKRTCPPWLENSLETIVPENLPRPSAHRRLELAGLAKGDAPPVGVVMTRVNRGGCFSV", "text": "FUNCTION: Triggers stress-induced chloroplast degradation, independently of autophagy and senescence-associated vacuoles (PubMed:25538186). After targeting to the chloroplast, triggers its destabilization and subsequent disassembly, inducing the formation of CV-containing vesicles (CCVs) carrying stromal proteins, envelope membrane proteins, and thylakoid membrane proteins which are released from the chloroplasts and mobilized to the vacuole for proteolysis (PubMed:25538186). SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Single-pass membrane protein Plastid, chloroplast thylakoid membrane; Single-pass membrane protein Plastid, chloroplast envelope Vacuole Vesicle Note=Present in vesicle-like spots observed in destabilized chloroplasts; these CV-containing vesicles (CCVs) carrying stromal proteins, envelope membrane proteins, and thylakoid membrane proteins translocate later to the cytosol before being mobilized to the vacuole for proteolysis."}
+{"protein": "MKSIVSVLTLLLLINAVAALRFVLPAKDKNELPFCVRDFVKNGELVVVTVESPKYADGQQLSVVVRDAHGNEYTRIKNVLGREITTFSSHQDTALDVCFHNVANSHQDLGKTKEIDLSVAIGANARDWEQIQASEKLKPAEVQLRKIEEIVDEVDKEMNYLKMREIRLRDTNESTNRRVKFFSVGITLALIALGVWQIIYLRSYFRSKHII", "text": "FUNCTION: Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Golgi apparatus membrane; Single-pass type I membrane protein Note=Recycles between endoplasmic reticulum and Golgi. SIMILARITY: Belongs to the EMP24/GP25L family."}
+{"protein": "MAVRVLCACVRRLPTAFAPLPRLPTLAAARPLSTTLFAAETRTRPGAPLPALVLAQVPGRVTQLCRQYSDAPPLTLEGIKDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE", "text": "FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis (PubMed:1907568). Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (PubMed:1907568, PubMed:10852722, PubMed:18721790). Accessory protein, of the core iron-sulfur cluster (ISC) assembly complex, that regulates, in association with LYRM4, the stability and the cysteine desulfurase activity of NFS1 and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (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). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acyl carrier protein (ACP) family."}
+{"protein": "MGSSHLLNKGLPLGIRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKTFGFNVFFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFTQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPGVVHPELNGGAYRYPQGVVSVAPAGLPAAVEGIVPSAMSLSHAHPAVAHPPHAPSPGQTIKPEADRDHPSDQL", "text": "FUNCTION: Corepressor targeting diverse transcription regulators. Has dehydrogenase activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family."}
+{"protein": "MSTNTDLSLSSYDEGQGSKFIRKAKETPFVPIGMAGFAAIVAYGLYKLKSRGNTKMSIHLIHMRVAAQGFVVGAMTLGMGYSMYQEFWANPKPKP", "text": "FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein Mitochondrion inner membrane."}
+{"protein": "RDLLLSQLCFLASVALLLWSLSSLREQKELDLMDLIGEDRKWMVGRKLMQVNDTLTSEDAGLRSSKNCTEPALHEFPRDIFSNEDRRQGAVVLHVLCAMYMFYALAIVCDDFFVPSLEKICERLHLSEDVAGATFMAAGSSAPELFTSVIGVFITKGDVGVGTIVGSAVFNILCIIGVCGLFAGQVVALSSWCLLRDSIYYTLSVVALIVFIYDEKVSWWESLVLVLMYLIYIIIMKYNACIHQCFERRTKGAGNMVNGLANNAEIDDSSNCDATVVLLKKANFHRKASVIMVDELLSAYPHQLSFSEAGLRIMITSHFPPKTRLSMASRMLINERQRLINSRAYTNGESEVAIKIPIKHTVENGTGPSSAPDRGVNGTRRDDIVAEADNETENENEDENNENDEEEDEDDDEGPYTPFDPPSGKLETVKWAFTWPLSFVLYFTVPNCNKPHWEKWFMVTFASSTLWIAAFSYMMVWMVTIIGYTLGIPDVIMGITFLAAGTSVPDCMASLIVARQGMGDMAVSNSIGSNVFDILIGLGLPWALQTLAVDYGSYIRLNSRGLIYSVGLLLASVFVTVFGVHLNKWQLDKKLGCGCLFLYGVFLCFSIMTEFNVFTFVNLPMCGD", "text": "FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC24A subfamily."}
+{"protein": "MGDVMIQSVKTESGLVDGHHGSCDSLGCVVGALAKVAKLVVALAALVLNGALCVLSLVALCVGATPVGPLAVLVATTLASFLCVAYVLFIAAKDRGWIASTNKC", "text": "FUNCTION: Inclusion membrane protein probably involved in early modification events of the chlamydial inclusion. SUBCELLULAR LOCATION: Secreted Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane; Multi-pass membrane protein Note=Secreted, probably by a type III secretion system (Probable). Localized in the inclusion membrane (PubMed:10447885, PubMed:11207546, PubMed:26416906). Inclusion membrane staining is punctate (PubMed:10447885). The C-terminus faces the host cytosol (PubMed:11207546)."}
+{"protein": "MAFRENVLEILEEITETDEVVQNTNIKLFDEGLLDSMATVQLLIEIEERLDITVPVSEFDRDEWATPEMIITQLEALK", "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": "MKLVMRILLTCFLLTTLVIKAEGQIHTNQPCTSNNTRCRTYCIKVHKINSGKCMNSKCVCHP", "text": "FUNCTION: Blocker of A-type voltage-gated potassium channels of cerebellar granular cells. May also inhibit Kv4/KCND when coexpressed with DPP6 or DPP10. The occlusion of the outer entry of the K(+) conducting pore is partially reversible and affects both open and closed channels. It shares the same target in rat brain than BmTX3 (AC Q8I0L5) and AmmTX3 (AC P60208). Recombinant toxin inhibits mKv1.3/KCNA3 channel (IC(50)=0.49 nM) (PubMed:22580271). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 15 subfamily."}
+{"protein": "MMLQAFQNRNHKLMKKNFSAGKLPSKGKSAVNFHRTFKPKLKPKTLSLDETKVVLFNKPFDVLTQFTDEQGRATLKDFISIPNVYAAGRLDRDSEGLLILTNNGELQHRLADPKFKTEKTYWVQVEGIPEETDLAQLRKGVELKDGVTKSAKVRLISEPNLWERNPPIRERKNIPTSWLEIKISEGRNRQVRRMTAHIGFPTLRLVRVSMGLLSINGLENGSFRLLSLDEIKALFQTVKL", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RsuA family."}
+{"protein": "MASLGAGAEPESVLFGKDGTEACESPEGRRSGRRKRTKIVPVWENKPCGSSRSLVRRIGSHLPLKPCTRACFEALPPASNLYLTDTPMVPTLADVKWLAADEDETYARVRSDTRPLKHKWRPSPLLVMQRNSSVPNLKMKEEKMFCLKKPGLSLNRSSDIQEELSILRSQIARIVAGDSASSCLGSDSIPVNVDLEASLPDYGPSYQSTTSFVISDITEEDELDVSEYSSASLVDSTISLQRQVESNMSDDDEDSLCLSKSNSFADMMGILKDIHKMKLNRDWSNRNQCLHKEEDPVNLISEVLRQKFALCDPDSVKNE", "text": "SIMILARITY: Belongs to the MTFR1 family."}
+{"protein": "MDTNQVNYIIWRYLKECGYSHTKFAFERETGIQNLDKQWGSTCQVGALVEILQKGLQYVELEKHYVDNHSSNEEASKTSIDGESLVNENPCKLPFYLTVPHICETTLTKADSTNGFCEHNNSNDHQLKILQDKGSGSPSSPVMPFKDKIEKRDIDITMADESNVEKDPARPIAVYNSSPVTEITEIKQVTFTGGEDIKSDFFKVIPTKHPVTCADWRPLLQENYHVYEFSIGMTNATLASVSICEEQNDFKAKTDYCLQSSFDNQDITGVAWNNSGSFLAYAFFSGVIEIYDSHGSQILSFHNNKGPVLSLKWSGTDTYLAAGSADGTITLFDQLKQTQYSIDTLASSVLDIEWISFDEFVTSDVEGSLRVYKVDGKAPVSTVSHAHDNSIVALRYNLRISLLLTASSDTTVKLWSRGDAGAFECLHVFSFSSPVNCIDWNLREGTPILAVASNSIVSMYNAISLQQLAVFMRHTAPVSALSFSHNGRYLATGDTSGGVCIWSCKTAKLFKELGSDNSELIAVTNVLPEEQVNFLRWSFDDKDLLIGKQKKEIICCCDFLHDSL", "text": "FUNCTION: Component of the set3 histone deacetylase complex which is involved in chromatin remodeling and transcription regulation, such as repression of the sporulation gene program. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MMEKLKEIEKVTKAIKEKILNHYGYIRVITHHDTDGLSSGGILAKMLMRTNKLFHLTVVEHLSKEVIEKLAKENEVNKPLFIFADMGSGQIEEIIKHNFNAIILDHHPPVIKDSFINENIIQLNPHIFGVDGSREITASGVCYLVAREFGYYDLSVLAIVGIIGDMQYNPLLGLNKFIVNEAREYRYVKIMNDIVYNIYDVEIYKAIAYCTKPYIPDLASEGKAFKFLKDIGIDPNKKQLDDTDKKKLLSAIIFKYPKIENLLIDRYLIEHKVRDAFLLSEMLNAVGRNGLFAVGIGICLEDDECIKIGNQILWEYKKNLINELKSVKLKKLNNIYYFEGKKGMIGIIASILVDDKPVIGYHIEGDIAKFSARGNRDLVNRGLNLSVAMAVAKEFGGNGGGHDVASGAVVSKDKVQEFLKRVDEIIGEQLRR", "text": "SIMILARITY: To M.jannaschii MJ0977."}
+{"protein": "MASVTALIIASIVTVAHGQTIVHITLGHNHTLVGPPITSEVIWTKLGSVDYFDIICNKTKPIFVICNRQNLTLINVSKIYNGYYYGYDRSSSQYKNYLVRITQPKLTVPTMTIIKMANKALENFTSPTTPNEKNIPNSMIAIIAAVALGMALIIICMLLYACYYKKFQHKQDPLLNFNI", "text": "FUNCTION: E3 proteins seem to be dispensable for virus growth in tissue culture cells. They are potentially important for virus growth under special conditions; E3 region may help adenoviruses to evade the immune surveillance of the host. SIMILARITY: Belongs to the adenoviridae E3_20 family."}
+{"protein": "MQSCGRWWGRLAARGAPRHLRPAAGGPRRQQQRWGGGEAARCIEQLLPRHDDFCRRHIGPREREKREMLSAVGVQSVEELMDKTIPASIRLRRPLRMDDHVVENEILETLYNIASKNKIWRSYIGMGYYNCSVPQPIARNLLENAGWVTQYTPYQPEVSQGRLESLLNYQTMVCDITGMDVANASLLDEGTAAAEAMQLCHRQNKRRKFYIDARCHPQTIANYTGVITELKLPHEMDFSGKDVSGVLFQYPDTEGKVEDFSELIERAHQNGTLACCATDLLALCILKPPGEFGVDVVLGSSQRFGVPLCYGGPHAAFFAVKENLVRMMPGRMVGVTRDANGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMYGVYHGSDGLKDIARRVHNATLILAEGLRRAGHKLHHDLFFDTLTVTCGCSVKEVLDRAALRKINVRIYSDGRLGVSLDETVNEKDLDDILWIFGCESSAELVAEGMGEETKGILSTPFKRTSKFLTHQVFNSYHSETNIVRYMKRLENKDISLVHSMIPLGSCTMKLNSSAELAPISWKEFANIHPFVPLDQAQGYQQLFKDLEKDLCEITGYDKISFQPNSGAQGEYAGLAAIKAYLNAKGERHRSVCLIPRSAHGTNPASAQMAGMKIQPIEVDKNGSIDISHLKAMVDKHKENLAAIMITYPSTNGVFEEEIGDVCDLIHKHGGQVYLDGANMNAQVGLCRPGDYGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPYLPTHPVIKIQTDKDACPLGTVSAAPWGSSAILPISWVYIKTMGAKGLKHASEIAILNANYMAKRLEKHYKILFRGVRGYVAHEFILDTRPFKKTANIEAVDLAKRLQDYGFHAPTMSWPVAGTLMIEPTESEDKGELDRFCDAMISIRQEIADIEEGRMDPQVNPLKMSPHTLNCVTSSKWDRPYSREVAAFPLPFVKPESKFWPTIARIDDIYGDQHLVCTCPPMEAYESPFSEQKRASS", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) 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 (GCSH). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvP family."}
+{"protein": "RICTPIPFPMCY", "text": "FUNCTION: Stimulates insulin release from beta cells at a concentration of 1 nM and release of glucagon-like peptide 1 (GLP-1) from enteroendocrine cells in vitro. Reduces secretion of interferon gamma from peritoneal cells in a mouse model. Has no inhibitory activity against Gram-positive bacterium B.megaterium Bm11 or Gram-negative bacterium E.coli ATCC 25922 at concentrations of up to 100 uM. Has no hemolytic activity against mouse erythrocytes. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSPCENDPPINWKRNLIVAWLGCFLTGAAFSLVMPFLPLYVEQLGVTGHSALNMWSGIVFSITFLFSAIASPFWGGLADRKGRKLMLLRSALGMGIVMVLMGLAQNIWQFLILRALLGLLGGFVPNANALIATQVPRNKSGWALGTLSTGGVSGALLGPMAGGLLADSYGLRPVFFITASVLILCFFVTLFCIREKFQPVSKKEMLHMREVVTSLKNPKLVLSLFVTTLIIQVATGSIAPILTLYVRELAGNVSNVAFISGMIASVPGVAALLSAPRLGKLGDRIGPEKILITALIFSVLLLIPMSYVQTPLQLGILRFLLGAADGALLPAVQTLLVYNSSNQIAGRIFSYNQSFRDIGNVTGPLMGAAISANYGFRAVFLVTAGVVLFNAVYSWNSLRRRRIPQISN", "text": "FUNCTION: Confers resistance to fosfomycin and deoxycholate. 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": "NPEHQRYVELFI", "text": "FUNCTION: Snake venom zinc metalloproteinase that cleaves both alpha- and beta-chains of fibrinogen, but not the gamma-chain (PubMed:29761254). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily."}
+{"protein": "MDIQSNVLTITSGSTPTDTSSNGQAAKSTKERIKRSDFPSDFVFGAATASYQVEGAWNEGGKGMSNWDYFTQSQPGGISDFSNGTIAIDHYNMFKDDVVVMKKLGLKAYRFSLSWPRILPGGRLCHGVSKEGVQFYNDLIDALLAADIEPYITIFHWDIPQCLQLEYGGFLHERVVKDFIEYSEICFWEFGDRVKYWITLNEPWSFTVQGYVAGAFPPNRGVTPKDTEETQKHARLHRGGGKLLAAFKYGNPGTEPYKVAHNLILCHAHAVDIYRTKYQESQGGKIGITNCISWNEPLTDSQEDKDAATRGNDFMLGWFVEPVVTGEYPESMIKYVGDRLPKFSEKEEKLVKGSYDFLGINYYTSTYTSDDPTKPTTDSYFTDSHTKTSHERNKVPIGAQAGSDWLYIVPWGIYRVMVDMKKRYNDPVIYITENGVDEVNDKSKTSTEALKDDIRIHYHQEHLYYLKLAMDQGVNVKGYFIWSLFDNFEWAAGFSVRFGVMYVDYANGRYTRLPKRSAVWWRNFLTKPTAVPLKNEPEKSEDRRKRLRGST", "text": "FUNCTION: Major beta-glucosidase activating oleuropein into a potent protein cross-linking agent (PubMed:25697790, PubMed:28483880). No activity with rutin, luteolin or p-nitrophenyl-beta-glucopyranoside as substrates (PubMed:25697790). SUBCELLULAR LOCATION: Nucleus Note=Distinctive compartmentalization of the oleuropein/OeGLU dual partner is a requisite to ensure a correct defense system response and to prevent the autotoxicity. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
+{"protein": "MPKSKELVSSSSSGSDSDSEVEKKLKRKKQVVPEKPVKKQKPGESSRALASSKQSSSSRDDNMFQIGKMRYVSVRDFKGKILIDIREYWMDSEGEMKPGRKGISLNMEQWSQLKEQISDIDDAVRKL", "text": "FUNCTION: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the transcriptional coactivator PC4 family."}
+{"protein": "MIFPVARYALRWLRRPEDRAFSRAAMEMALRGVRKVLCVAEKNDAAKGIADLLSNGRMRRREGLSKFNKIYEFDYHLYGQNVTMVMTSVSGHLLAHDFQMQFRKWQSCNPLVLFEAEIEKYCPENFVDIKKTLERETRQCQALVIWTDCDREGENIGFEIIHVCKAVKPNLQVLRARFSEITPHAVRTACENLTEPDQRVSDAVDVRQELDLRIGAAFTRFQTLRLQRIFPEVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEIFHRIKVTHDHKDGIVEFNWKRHRLFNHTACLVLYQLCVEDPMATVVEVRSKPKSKWRPQALDTVELEKLASRKLRINAKETMRIAEKLYTQGYISYPRTETNIFPRDLNLTVLVEQQTPDPRWGAFAQSILERGGPTPRNGNKSDQAHPPIHPTKYTNNLQGDEQRLYEFIVRHFLACCSQDAQGQETTVEIDIAQERFVAHGLMILARNYLDVYPYDHWSDKILPVYEQGSHFQPSTVEMVDGETSPPKLLTEADLIALMEKHGIGTDATHAEHIETIKARMYVGLTPDKRFLPGHLGMGLVEGYDSMGYEMSKPDLRAELEADLKLICDGKKDKFVVLRQQVQKYKQVFIEAVAKAKKLDEALAQYFGNGTELAQQEDIYPAMPEPIRKCPQCNKDMVLKTKKNGGFYLSCMGFPECRSAVWLPDSVLEASRDSSVCPVCQPHPVYRLKLKFKRGSLPPTMPLEFVCCIGGCDDTLREILDLRFSGGPPRASQPSGRLQANQSLNRMDNSQHPQPADSRQTGSSKALAQTLPPPTAAGESNSVTCNCGQEAVLLTVRKEGPNRGRQFFKCNGGSCNFFLWADSPNPGAGGPPALAYRPLGASLGCPPGPGIHLGGFGNPGDGSGSGTSCLCSQPSVTRTVQKDGPNKGRQFHTCAKPREQQCGFFQWVDENTAPGTSGAPSWTGDRGRTLESEARSKRPRASSSDMGSTAKKPRKCSLCHQPGHTRPFCPQNR", "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-(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. As an essential component of the RMI complex it is involved in chromosome separation and the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity (PubMed:30057030). It is required for mtDNA decatenation and segregation after completion of replication, in a process that does not require BLM, RMI1 and RMI2 (PubMed:29290614). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the type IA topoisomerase family."}
+{"protein": "MEKLSYTFSQQYEEKIRPCIDTIDNLRSLGVEKDLALPAIAVIGDQSSGKSSVLEALSGVPLPRGSGIVTRCPLELKMIRTKDQDRWHGRISYKTCEEDFDDPAEVEKKIRQAQDEMAGAGVGISEELISLQITSADVPDLTLIDLPGIARVAVKGQPENIGDQIKRLIRKFVTRQETINLVVVPCNVDIATTEALQMAQAEDPDGERTLGILTKPDLVDKGTEGTVVDIVHNEVIHLTKGYMIVRCRGQKEIMDQVTLNEATETESAFFKDHPHFSKLYEEGFATIPKLAEKLTIELVHHIQKSLPRLEEQIETKLAETQKELEAYGNGPPSEPAARLSFFIDKVTAFNQDMLNLTTGEDVKCTTDLLLFPELRQEFAKWSHILDRSGDSFNKKIEKEVDNYEVKYRGRELPGFINYKTFEGLVRDQIKLLEEPALKTLKTVSDVVRKKFIQLAQCSFIGFPNLLKIAKTKIEGIKLNKESLAESMLKTQFKMELIVYSQDGTYSQSLKHAKDKLEEMEKERPQPKIKLPLLSSFDLGTDNHATLREMRLHLKSYYTIASKRLADQIPMVIRYMLLQEAALELQRNMLQLLQDKDGVDNLLKEDCDIGQKRENLLSRQTRLIEGTQPLGHLLEVTFIDYCNILMQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
+{"protein": "MAWTEKDVENGKESESLGNNGFLKGGQSSSGSKGSPGRISHVKKIFEDKDAITYANILRSRNKFVDALAIYESVLEKDSKSIESLIGKGICLQMQNTGRLAFESFSEAIKVDPQNACALTHCGILYKDEGRLVEAAESYEKALKADPSYTPAAECLAIVLTDIGTSLKLAGNTQEGIQKYYEAIKIDSHYAPAYYNLGVVYSEMMQYDMALNCYEKAALERPMYAEAYCNMGVIFKNRGDLESAIACYERCLAVSPNFEIAKNNMAIALTDLGTKVKLEGDINQGVAYYKKALCYNWHYADAMYNLGVAYGEMLKFDMAIVFYELAFHFNPHCAEACNNLGVIYKDRDNLDKAVECYQLALSIKPNFSQSLNNLGVVYTVQGKMDAAASMIEKAIIANPTYAEAYNNLGVLYRDAGNISLAIEAYEQCLKIDPDSRNAGQNRLLAMNYINEGTDDKLYEAHRDWGRRFMKLYPQYTSWDNSKVPERPLVIGYVSPDYFTHSVSYFIEAPLAHHDYTNYKVVVYSSVVKADAKTNRFRDKVMKKGGLWRDIYGIDEKKVSSMIREDKVDIMVELTGHTANNKLGTMACRPAPVQVTWIGYPNTTGLPTIDYRITDAMADPPNAKQKHVEELVRLPNSFLCYTPSPEAGPVCPAPALSNGFVTFGSFNNLAKITPKVLKVWARILSAVPHSRLIVKCKPFCCDSVRQRFLSILEQLGLEPQRVDLLPLILLNHDHMQAYSLMDISLDTFPYAGTTTTCESLYMGVPCVTMGGSVHAHNVGVSLLKTVGLENLVARNEDEYVESAIQLASDVTSLSNLRMSLRELMSKSPLCDGAKFTRNIESIYRSMWRRYCDGDVPSLRRMELLQQQQTQTESVVPEESSVNPSERTITSAPTDGSIKENGFTAVPALALKSSTSEENGVQSNHNGNHGNLS", "text": "FUNCTION: Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc transferase subfamily."}
+{"protein": "MNGQKDVVQVSEAWQTLSTYLPPVTADRDYWWQLTGRHVAALVEAAGYPIEKQYEALIFHYHWTVPYMGPAPKADGTPATWKSLLGLDGSPIEYSWKWNTTRSEPDVRYVTEPIGQHPGSHLDPLNQHALRELLQRFSKNMPSSDMNMSWVNHFFARLYDHDNTRYIQEAAAGSSRSTATSVQLGTEFLRRGIGFKTYFFPRKLGQVDDISISQYGASMSQLDVDETSWDARKALVEFLETNPEGKSLRPFSLAVDNVAPSQSRLKWYFHTLHTSIDSVREIMTLGGRINGIDKQLEELEDLIRVVAGLASDFPTNAEIPLPKKSDVYDQSAKDNFGELEDVLTGYLYYFDIAPGQGKLPEVKWFIPSRHYGPNDRELASALGAWMEARGRGAYNEPYMKMLHTLSAHRGLGDGKGLQTFISCLFKPSGDLDITTYLGAEAFHPGRVAKMAKPNGRSPRATLRRGDD", "text": "FUNCTION: Prenyltransferase; 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). The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS pks8/GME11356. Pks8/GME11356 lacks a thioesterase (TE) domain, which is important to the cyclizing of the third ring of atrochrysone carboxylic acid, and the esterase GME11355 might play the role of TE and catalyzes the cyclization reaction of the C ring. The lactamase-like protein GME11357 (or other beta-lactamases in Pestalotiopsis microspora) probably hydrolyzes the thioester bond between the ACP of pks8/GME11356 and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrates to form endocrocin anthrone. Endocrocin anthrone is further converted to emodin via the endocrocin intermediate. Emodin is then oxidized by several enzymes such as the Baeyer-Villiger oxidase GME11358, the oxidoreductase GME11367, the short chain dehydrogenase/reductase GME11373, as well as by other oxidoreductases from the cluster, to modify the A and C rings and open the B ring, and finally yield monodictyphenone. The prenyltransferase GME11375 may catalyze the addition reaction between the C5 side chains and the carbon bone of dibenzodioxocinones. The remaining biochemical reactions to the final product dibenzodioxocinones should be methylation catalyzed by methyltransferase GME11366 and reduction and lactonization reaction catalyzed by a series of oxidordeuctases (Probable). SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family."}
+{"protein": "MRTLWIVAVWLMGVEGNLFQFGNMINHMVGKHAVWSYLSYGCYCGWGGQGKPQDATDRCCFVHDCCYGRANGCDPKLSTYSYNFQNGNIVCGNKYGCLRHICECDRVAAICFQKNMNTYNKKYKNYSSSNCQENSDKC", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 90 nM). 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": "MDIEAYFERIGYQKSSNKLDLQTLTEILQHQIRAIPFENLNIHCGKTMELSLEDTFHQIVRKKRGGWCLQVNHLLYWALAMIGFETTMLGGCVYVPSACKYSNTMIHLLLQVTISGKTYIVDSAFPFSCQLWEPLELTSGKDQPQVPAIFHLREENGTWYLEQTKRQEYVSNQEFIDSNFLEKNTHRKIYSFTLEPRTIEDFWSISTYYQVSRTSVMTNTSLCSLHTKDGVHGLMGTILAYKKFNYKDNIDLVEFKTLKEEEIEEVLKSVFGIHLETKLVPKCGNVFFTI", "text": "FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the arylamine N-acetyltransferase family."}
+{"protein": "MHPALGHPRALSSAPASFPPPPAAARLQPLFLRGGSSRGRRGSGDSSTSTSTSRGGCGGRRGGGGGSPSSSTGAEREDDDESISISKPLVPAAAALPGPPAQGGVPVSATAPAAASSTSTPTSSCSMTAADFGAGAAAGTVGGPGSRSAVGAGGTGTGGAASCCSCCCCCCGRPTRSGRRGRRRGCSPSPGCRWGYQALSVVLLLAQGGLLDLYLIAVTDLYWCSWIATDLVVVVGWAIFFAKNSRGRRGGPANSMHNHHQLHHHSAPPLHLSAAASAGAGAKARGGRGGSGGSGAGPGTTGAAGEFAFAYLAWLIYSIAFTPKVVLILGTSILDLIELRAPFGTTGFRLTMALSVPLLYSLVRAISEAGAPPGSAGPLLLQPQQHRAAGCFLGTCLDLLDSFTLVELMLDGRVPLPAHLRYLLIAVYFLTLASPVLWLYELNTATAAPSWGQTSGPGSCSRLLRLLGGCLVDVPLLALRSLLVVSYQQPLSIFMLKNLFFLGCRGLEALEGCWDRGSWVSPSRARSSYGAPPSAPPPPPPPPPQGGSQRGHLENEGGPHGYVNTLAVASQN", "text": "SIMILARITY: Belongs to the TMEM121 family."}
+{"protein": "MPMNRREMVMATTGAALAAAAAVPLLSGGEGEGAAEAAAAPAKATGRGREHTERYLGRSIRVAAPADGGGVFIDGRPLHIMKFADDAYLSSMCHYEMAPTPLHAARRAVEELRGAALQPSTHGTHVTHL", "text": "FUNCTION: Involved in the transfer of copper ion to the apo form O- aminophenol oxidase GriF in the grixazone biosynthetic pathway. SIMILARITY: Belongs to the melC1 family."}
+{"protein": "MQVIITSSHRFFCHHLHQLKSPTSLSAQKAEFKKHGPRNWLFQTEGSLLYKPVRLNCATSDASYLGNVNEYLESDHSKNSEEKDIQVSRTIQMKGLTEEIKHMLNSMEDGRLNVLAYDTAWVSFIPNTTNNGNDQRPMFPSCLQWIIDNQLSDGSWGEEIVFCIYDRLLNTLVCVIALTLWNTCLHKRNKGVMFIKENLSKLETGEVENMTSGFELVFPTLLEKAQQLDIDIPYDAPVLKDIYARREVKLTRIPKDVIHTIPTTVLFSLEGLRDDLDWQRLLKLQMPDGSFLISPASTAFAFMETNDEKCLAYLQNVVEKSNGGARQYPFDLVTRLWAIDRLQRLGISYYFAEEFKELLNHVFRYWDEENGIFSGRNSNVSDVDDTCMAIRLLRLHGYDVSPDALNNFKDGDQFVCFRGEVDGSPTHMFNLYRCSQVLFPGEKILEEAKNFTYNFLQQCLANNRCLDKWVIAKDIPGEIWYALEFPWYASLPRVEARYYIEQYGGADDIWIGKTLYRMPDVNNNVYLQAAKLDYNRCQSQHRFEWLIMQEWFEKCNFQQFGISKKYLLVSYFLAAASIFEVEKSRERLAWAKSRIICKMITSYYNDEATTWTTRNSLLMEFKVSHDPTRKNGNETKEILVLKNLRQFLRQLSEETFEDLGKDIHHQLQNAWETWLVFLREEKNACQEETELLVRTINLSGGYMTHDEILFDADYENLSNLTNKVCGKLNELQNDKVTGGSKNTNIELDMQALVKLVFGNTSSNINQDIKQTFFAVVKTFYYSAHVSEEIMNFHISKVLFQQV", "text": "FUNCTION: Class-II terpene synthase that synthesizes 8-hydroxy-copalyl diphosphate. Involved in the biosynthesis of cis-abienol, a labdane diterpene that can be used as synthesis precursor of ambergris substitution fragance products. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MSRNAPNGCVPPSQATAPPSPATSLRLTVGEPVSEPATESGERVLQDGFWEHGRFYGSWKPGKYLFPIDKEELNRLDVFHKYFLVARDEKVTSTPLRKDGRPKIMDLGTGTGIWAYNVVEEYAKDAEIMAVDLNQIQPALIPRGVTTKQFDIEEPSWDPLLRDCELIHMRLLYGSIRDDKWPHVYRKAFEHLAPGIGYIEQLEIDWMPRWENEDLPRHSALQEWAQLFQRAMHRYHRSVTVSGEATRRRMEAAGFTDFSETTIRCYVNPWSPDRHQRECARWFNLAFSLGLEAMSMMPMIDKLGMTKDDIVDLCSRAKKEMCILRYRAYCTL", "text": "FUNCTION: Methyltransferase that performs automethylation (By similarity). No other methyl-accepting substrate has been identified yet (By similarity). Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression (PubMed:23390613, PubMed:24909838). Required for the expression of VEL1 (PubMed:23390613). Regulates expression of the carbohydrate-active enzyme gene clusters, but does not act by directly modulating H3K4 or H3K9 methylation (PubMed:22554051). Required for conidiation (PubMed:22554051). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the methyltransferase superfamily. LaeA methyltransferase family."}
+{"protein": "MDTRGSFSCGFLLLLLIQLQPSRANPIYNLSPAKELASMEALLERLEDKFALIEALESNPDLQEPQTQEEIPPELTDDSDEQKAEPKLASNTPLSYRNPFLKRLRGVQMPRMMRDSGCFGRRIDRIGSLSGMGCNGSRKN", "text": "FUNCTION: Hormone playing a key role in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family."}
+{"protein": "MLSSRLQFAQQTARKFSISAKDGSGKLSTLAVKVHGGSRYADKEGIAHLLSRFNFHNTGNKSALRLVRESELLGGKFESSVDREYITLKATFLKEDLPYFVNALGNVLYKTSFRPHELPESVLPAAKYDISVSETNPINKAEDLLYNVSFRKDLGNTVLYRGVEKVTLDDIKAYANKVYTKENIEIVGQGVNEADLKRFVNDSLIGSLPTGSKLAAQAQPKFFSGEARLSAPGASVAAIAVPVTKEQFATYEVLAKYLTSALSELSPLIDSAKLDKYANAGLFSLYVKGEDASVVAENIKKVVDTLKKDVDISAAKEYTALQLSLENAPIDVSNVKNVKLDKFSYAAVGNVAKLPFADEL", "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 peptidase M16 family. UQCRC2/QCR2 subfamily."}
+{"protein": "MADSGLREPQEDSQKDLENDPSVNSQAQETTIIASNAEEAEILHSACGLSKDHQEVETEGPESADTGDKSESPDEANVGKHPKDKTEDENKQSFLDGGKGHHLPSENLGKEPLDPDPSHSPSDKVGRADAHLGSSSVALPKEASDGTGASQEPPTTDSQEAQSPGHSSAGQEGEDTLRRRLLAPEAGSHPQQTQKLEEIKENAQDTMRQINKKGFWSYGPVILVVLVVAVVASSVNSYYSSPAQQVPKNPALEAFLAQFSQLEDKFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVADAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPTSFNHMDSDKLSGLWSRISHLVLPVQPVSSIEEQGCLF", "text": "FUNCTION: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane. SIMILARITY: Belongs to the TOR1AIP family."}
+{"protein": "MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNNCYIWMEKRHRGPGLAPGQLYTYPARCWRKKRRLHPPEDPKLRLLEIKPEVELPLKKDGFTSESTTLEALLRGEGVEKKVDAREEESIQEIQRVLENDENVEEGNEEEDLEEDIPKRKNRTRGRARGSAGGRRRHDAASQEDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGDEAQDQETRSPPNHRNENHRPQKGPDGTVIPNNYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKASAFGCQA", "text": "FUNCTION: Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic 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 post-mitotic 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). 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 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). 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. FUNCTION: [Isoform 2]: Acts as a regulator of myogenesis in cooperation with HDGFL2 (PubMed:32459350). Mediates the interaction of HDGFL2 with the BAF complex (PubMed:32459350). HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters (PubMed:32459350). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the requiem/DPF family."}
+{"protein": "MTGTGPHGDPAEDPAGPDDTAAETDGPAEPTEPVDASEAEMTDTTETTAQTGTTAEADASEEFEGPRRRARRERAERRAARDRAMAIEQARREAKRRAVAGALDPTKSVPRNTIRGLKVLMWAALVSVLAVALGLLLYFTPIMSARNVEVSGLAEIPQEEVLTAAAVAPGTPLLQVDTDAVAERVATIRRVATARVQREYPSTLKISIVERVPVVVKDYPDGPHLFDRDGVDFATGPAPLALPYLDADNPGPNDPATRAALDVMMALPPDVAAQVGRIAAPSVASITLTLIDGRVVVWGTDDRTQEKALKLAALLTQPGTTYDVSSPDLPTVK", "text": "FUNCTION: Essential cell division protein. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Note=Localizes to the division septum. SIMILARITY: Belongs to the FtsQ/DivIB family. FtsQ subfamily."}
+{"protein": "MIRSVLLRALAARPPSAPVPGHLHRCLLGTHRRKIKPEQLELPNQTREFVYSLSPETRSRLLKELQTFESKTEDSGEASRLTAAQLRYILLHNAIPFIGFGFLDNAIMIAAGTQIELSIGLTLGISTMAAAALGNLVSDLAGLGLAGYVEALAVRLGMQIPDLSPRQVDMWQTRVSSHMGKAIGVAIGCILGMFPLLFLSDEEDKKPKKDSN", "text": "FUNCTION: May play an important role in cardiac development and function. May regulate cardiac conduction and the function of the gap junction protein GJA1. May contribute to the stability and proper localization of GJA1 to cardiac intercalated disk thereby regulating gap junction communication (PubMed:26403541). Regulates mitochondrial respiration and mitochondrial DNA copy number maintenance (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Mitochondrion inner membrane; Multi-pass membrane protein Note=Localizes at the intercalated disk in ventricular tissue and cardiomyocytes."}
+{"protein": "MSWQTYVDDHLMCEIEGNYLTSAAIIGQDGSIWAQSASFPQFKPEEITAIMNDFSEPGTLAPTGLYLGGTKYMVIQGEAGAVIRGKKGPGGVTVKKTNQALIIGIYDEP", "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. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family."}
+{"protein": "MAKLSSLLNPIISKILEIYVYSWYSGISKDALFPSQCEQVGGSIVHELEKRLSRQDAMDLLFYEIPFLLIKHIENTEEAKLRFALPQGQILEIDTIYHSLHPHIALEKEENELVYCRLLVEDILKYLLPATNSKSEIECVILREALAVQIHKSIQVASSPETMYKFIIYLSKAILQPSRRPWKESITTAVRWVWHAFRILLITRGVPYFSTAWFQFYLKLFSQKDNVSSSDLTRWFFFYTLLYPWIALVSAFVAETMTLCCIVTIFYDKNVNRQWKQYILTSVSNMDKGNPSGGSQSTNVTTFRRFSQSSYPRRSNYRRRISTSSKSLYELSPSKFKSIPITSNPPPMLNLSKGSTSVEPTFCETNASVALSTVTSTPVFSTDSSPLSSRTRENLLSLIPSAVSSPTKANTNKSHQRSFSIPKATKDSQTPSENSAATLKQAAIDAYSQIPVIPFFLPSDKLIMLVESEYRNKHIFYSLLNSFTMVMFPELRHTK", "text": "FUNCTION: Required for required for normal vacuolar morphology and for vacuolar protein transport. Also required for endosome-to-Golgi protein transport. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein."}
+{"protein": "MAAIPSSGSLVATHDYYRRRLGSTSSSSSCGSVDYSGEVIPHHPGLPKADPGHWWASFFFGKSTHPVMTTVSESPENSGSFRITNGLVPCGLTQESVQKQKVSDSKSNSSPSA", "text": "FUNCTION: Probable regulator of exocrine pancreas development. SIMILARITY: Belongs to the PPDPF family."}
+{"protein": "MDLIQQQIAHEEALVGAAQNDARIALEKAIAQGSIDRIPRARIMLMRMLPIVTEAIFAHQEAKAAGPAAKLRHLLRIIDAQDLAVMALRAGLSMLINYPTITATKYYTHMGKMLCREIEVRLAFKVNQPYYDRTLDYLKTSRTRSVRHIQKTMDALLDAVLPEEARIDLPDGDYLRLGKFIGDPLIQCGLFEPNRFTGRGGTSVHLEPSPEAREFLQDPSAAMTWGGPGRSVMLAPPRPWNDWCDGGYYSAKAQKHHVLVRRTKHQTKRARQAQLRHLGQDKMPKVYEAVNVLQSVAYEINRDVYEIIERVFNSGGGVLGIPQRTYPDKPEFPLGDEWAKENASEQELEAFNRWKRSVHRWYTGEREHTAKLREFAALYRVVREHHGKAVYFPMHVDSRGRMYYWGTPNPQGSDIAKACLRFHDKRVLGKRGLYWLKVHVANSLGCDKVYFDDRAAWVDERWDDFQRALAEGPENYPGLFPEAESPLCAIAGLLELRAAYASGNPEGYRSGFIVHMDATCSGLQHYSAILRDEIGGAYVNLLPPGLAKADIYSRVLGLVNESLERDRAPGAEGEARGYALLWDKAGLSRSLTKKPCMTLVYGTTFKGVVDHCLDYLDESGVEIPEGVPSYRLGSYMATLILDAIRETVPSAVFAMEWLQRLAKALPDASKDLHWITPLGMQVFQSYPKTEEVRVRLRAEAVEYVTLYEAKDELDPMRNANGIAPNFVHGLDSSHLGLTALACAAEDIPIQAIHDSMGTYASDVDRMHVHIREQFIAMYSGPCVLVELAKQLGVEATPPRRGSLNLEAVRDSWAFFC", "text": "FUNCTION: DNA-dependent RNA polymerase that catalyzes the transcription of viral genes. SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase family."}
+{"protein": "MSADSQSIAATENEEKSHEVPGNVQHCGDMLSGQEETVPLGTSQESTHIKAEPEEPHSEGASREDRTPGTQRWMSPCPGPKDKGPFLPGGVVPSPWTPVLSRGGRTRERKMAAALLTAWSQMPVTFEDVALYLSQEEWGRLDHTQQNFYRDVLQGKNGLALGAVEMGKVVPALAVATLEDTKSIRTRARWAPGEDPKCGQHVASGPGTKLTRDTGKAGQLKPAPSESRPLKTPEDSGPEKPSEGEEALKSGEEGLVPDGDTGKKTYKCEQCGKGFSWHSHLVTHRRTHTGEKPYTCTDCGKRFGRSSHLIQHQIIHTGEKPYTCPSCWKSFSHHSTLIQHQRIHTGEKPYVCDRCAKRFTRRSDLVTHQGTHTGAKPHKCPICSKCFTQSSALVTHQRTHTGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFSHSSHLTAHQRTHRGVRPYSCPLCGKSFSRRSNLHRHEKIHTTGPKALAMLMLGAAAAGALTAPPPAST", "text": "FUNCTION: Transcriptional repressor that binds to the promoter region of Mpv17l isoform M-LP short and regulates its age-dependent and heat- induced expression (PubMed:20231359). By regulating Mpv17l expression, contributes to the regulation of genes involved in H(2)O(2) metabolism and the mitochondrial apoptotic cascade (PubMed:20231359) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MPGPRPRKGPKTSGQGAETAKQLGLFVEFNPEDMLLGMDETEDDGDLEAELLALTGETGSTSRKPAPKGRAPLPMAHIEKLAADCMRDVEEEGEEEEGLEDDADLLTELQEVLGVDEETGLVDDSEETSPDLSEEKTRDNTEQPVAPAAFQQALPAAVAQAGGPRGLQALLEERIQNYREAAASAKEAGEAAKARRCERGLKTLESQLATVRKGGKICEDEIPPPVALGKRPPAHQERPSKDSEIDSAGSCAMDPGDLSQPESSLPAVAALPDSDPDPQALLLARQREYKAAALSAKRAGDLDRARELMRIGKRFGTVLEALEKGQPVDLSGMPPAPEDLKALPQASEASAATQVLSPAVEQMQPVMSSDLPATPAAPAEPKTVLDALQQRLNRYREAGIQARASGDERKARMHDRIAKQYQDAIRAHQAGRKVDFAELPVPPGFPPIPGLEPRKDTEEDSVTATLAAAQKLASEDTALVDEDEERDTPAQAPLAKKPAQPLVPSSHLLNEPKASSSKESLSPSVREQVTLLEARKLQYQRAALQAKRRQDLEQAKSHLRVAKSLEAQIIQARAGQPIDLSKVPSPLTDEEGDFILIHHEDLRLSQKAEEVYAQLQKILLEQHEKCLLFSKQFMHQGNVAETTRFEKLAEDRKKQLEILQLAQAQGLDPPSHHFELKTLQTVRIFSELNSTEMHLIIVRGMNLPAPPGVTPDDLDAFVRFEFHYPNSDQAQKSKTAVVKNTNSPEFEQVFKLNINRNHRGFRRVIQSKGIKFEIFHKGSFFRSDKLVGTAHLKLERLEKECEIREIMEVLDGRKPTGGKLEVKVRLREPLSSQDVQMVTENWLVLEPRGL", "text": "FUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CC2D1 family."}
+{"protein": "MAASCVALLVLALLLLVLLLGLWKRGRQTGRARHMVVVVLGDVGRSPRMQYHALSLAQSGFSVTLLGFYNSKPRDELLQNDRIRIVKLTDLRGLGAGPRILQYGVKVVFQAVYLLWKMMRMDPAAYIFLQNPPGLPAIAVCWFVGCICGSKLVIDWHNYGYSIMGLVHGPRHPIVLLAKWYEKFFGRLSHLNLCVTNAMREDLAENWCVRAVTLYDKPASFFKETPLDLQHELFMKLSHTYSPFQSCSDPSHPDTERSAFTERDCQSGVVRRLHGRPALLVSSTSWTEDEDFSILLRALEKFEQQALTGDSLPSLVCVITGKGPLREHYRHLISQKHLQHVRFCTPWLEAEDYPLLLGSADLGVCLHMSSSGLDLPMKVVDMFGCHLPVCAVNFKCLHELVRHGENGLVFKDAEELAAQLQMLFSKFPDPAGKLSQFRKKLQESGQQRWDESWQHTVLPLLAHSQMTPRPHPPCGHPSCRGF", "text": "FUNCTION: Catalyzes the addition of the first of nine mannose moieties to form a dolichol-lipid linked oligosaccharide intermediate required for proper N-linked glycosylation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 33 subfamily."}
+{"protein": "MSAYATQGFNLDDRGRRIVVDPVTRIEGHMRCEVNVDANNVIRNAVSTGTMWRGLEVILKGRDPRDAWAFVERICGVCTGCHALASVRAVENALDIRIPKNAHLIREIMAKTLQVHDHAVHFYHLHALDWVDVMSALKADPKRTSELQQLVSPAHPLSSAGYFRDIQNRLKRFVESGQLGPFMNGYWGSKAYVLPPEANLMAVTHYLEALDLQKEWVKIHTIFGGKNPHPNYLVGGVPCAINLDGIGAASAPVNMERLSFVKARIDEIIEFNKNVYVPDVLAIGTLYKQAGWLYGGGLAATNVLDYGEYPNVAYNKSTDQLPGGAILNGNWDEVFPVDPRDSQQVQEFVSHSWYKYADESVGLHPWDGVTEPNYVLGANTKGTRTRIEQIDESAKYSWIKSPRWRGHAMEVGPLSRYILAYAHARSGNKYAERPKEQLEYSAQMINSAIPKALGLPETQYTLKQLLPSTIGRTLARALESQYCGEMMHSDWHDLVANIRAGDTATANVDKWDPATWPLQAKGVGTVAAPRGALGHWIRIKDGRIENYQCVVPTTWNGSPRDYKGQIGAFEASLMNTPMVNPEQPVEILRTLHSFDPCLACSTHVMSAEGQELTTVKVR", "text": "FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family."}
+{"protein": "MVPGKFIFTATFVLLCTIIAVVLEYQSKKDKPVLDKEKLQEFPLVAKTVLTHNTAIYRFGLPKSTQVLGLPIGQHISVQANINGKDILRSYTPTSLDSDAVGHFELLIKSYEKGNISKHFAQLNIGDKIKVRGPKGFYHYQPNMNEEIGMIAGGTGIAPMYQIMKSIFANDSDKTKVSLVYGNQTEEDILLKKELDAFVERKPDQFKVYYLLDKAPEAWTGGVGYITVDTMKERLPAPAEGVQLLVCGPPPMVSSIKRNAVTLGYEKAKPISKMGDQIFVF", "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": "MADQPMIEMKNVTKVYDNGTVGLKNINLKINKGEFVVIVGLSGAGKSTLLRAINRLHDISEGDILIAGESITKTKGKNLRLMRRKIGMIFQSFNLVKRSSVLRNVSAGRLAYYPTWKTTFNLFTDEDKQRAYEALQSVGMAEKVYSRADELSGGQQQRVAIARVLTQRPEIILADEPTASLDPKTSRQVMEDLKMLNEKFDMTVVANLHSIELAKEFGHRVIGVRAGEIVYDGKMEDTPQSVFDNIYNGGKGKEED", "text": "FUNCTION: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Phosphonates importer (TC 3.A.1.9.1) family."}
+{"protein": "MIKLTAQQIFDKLLDEEKILSANGQIRFFLGDVDIIVKQKDVVGNIIQEWLGGWLRKREIEFDVSTNTQMPPDFFLNKKDRSRELLEVKAFNRNASPGFDIADFKMYSDEIIHKPYMLDVDYLIFGYDMDDNGNVTIKDLWLKKVWQITRSMDGWAINLQVKKGVVHKIRPGVWYSINKKNMPMFECLEDFVSAIEETVYQNPATRHNASLWKRKFEEAYKKHYNRSISIPRWHEIAHKYKKK", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGNNCC-3' and cleaves after N-3."}
+{"protein": "MATAWCLPWTLRRAGAWLLTPPLRCPRRALHKQADGTEFQSIYSLDKLYPESRGSDTAWKVPDDAQQTNKDIPLDRLTISYCRSSGPGGQNVNKVNSKAEVRFHLATAEWIAEPVRQKMAIMHKNKINRSGELILTSECSRYQFRNLADCLQKIRDMIAEASQTPKEPSKEDAALHRIRIENMNRERLRKKRIHSAIKTGRRVDMD", "text": "FUNCTION: Essential peptidyl-tRNA hydrolase component of the mitochondrial large ribosomal subunit. 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": "SCINHGDACDGYKDDCQCCRRNGFCSCSGIFGYKWNCICDVGTTATSYGICMAK", "text": "FUNCTION: Omega-agatoxins are antagonists of voltage-gated calcium channels (Cav). Causes rapid general flaccid paralysis followed by death in 10-30 minutes when injected in mice at dose levels of 5 ug per mouse. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 04 (omega-agtx) family. 03 (type II/III omega-agtx) subfamily."}
+{"protein": "MSPQGPAVLSLGSLCLDTNQAPNWTGLQTLLQQLPPQDIDERYCLALGEEERAELQLFCARRKQEALGQGVARLVLPKLEGHTCEKCRELLKPGEYGVFAARAGEQRCWHQPCFACQACGQALINLIYFYHDGQLYCGRHHAELLRPRCPACDQLIFSWRCTEAEGQRWHENHFCCQDCAGPLGGGRYALPGGSPCCPSCFENRYSDAGSSWAGALEGQAFLGETGLDRTEGRDQTSVNSATLSRTLLAAAGGSSLQTQRGLPGSSPQQENRPGDKAEAPKGQEQCRLETIRDPKDTPFSTCSSSSDSEPEGFFLGERLPQSWKTPGSLQAEDSNASKTHCTMC", "text": "SIMILARITY: Belongs to the prickle / espinas / testin family."}
+{"protein": "MPAKTGPRVVVFLECFHCTQKGAQKKFPGVFRYITKKNRHNKSTPLELKKFCPFCLKHTIHKERKK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
+{"protein": "MSGSRGNSSNSSVSNNSNNNNNNDGGDERLLFLRSVGERNEIGFPSRFKSAHYKKPTRRHKSARQLISDENKRINALLTKANKAAESSTAARRLVPKATYFSVEAPPSIRPAKKYCDVTGLKGFYKSPTNNIRYHNAEIYQLIVKPMAPGVDQEYLKLRGANFVLK", "text": "FUNCTION: Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex. Also involved in the regulation of telomere length. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IES6 family."}
+{"protein": "MTQITERELKKKYLDLLSQRFDTPEKLATEIINLESILELPKGTEHFVSDLHGEYEAFQHVLRNGSGNVRAKINDIFKDKLSTKELNDLTALVYYPEDKLQLIKCDFQNYGQLNVWYITTIEHLIQLIKYCSSKYTRSKLRRALPEQYVFIVEELLYKNNEFKNKKSYYETLVNQVIELKQADDLIIGLAYSVQRLVVDHLHVVGDIYDRGPQPDKIMDTLINYHSLDIQWGNHDVLWVGAYAGSKVCLANLLRICARYDNLDIVEDAYGINLRPLLTLAEKYYDADNPAFKPKKRPDKHERLTQREESQITKIHQAIAMIQFKLEIPVIKRRPNFEMDERLVLEKVNYDTNEITVYRKTYPLKDTCFQTVNRDNPAELLPEEEEVMNKLLLSFQQSEKLRRHMSFLMRKGSLYLPCNGNLLIHGCIPVDENGEMESFEIDGQTYSGQELLDVFEYHVRKSFDEKENTDDLSTDLVWYLWTGKYSSLFGKRAMTTFERYFIADKASHKEEKNPYYHLREDVNMVRKMLSDFGLNPDEGRIINGHTPVKEINGEDPIKADGKMLVIDGGFSKAYQSTTGIAGYTLLYNSFGMQLVAHQQFNAKEKILSEGIEELSIKRIVDKELQRKKIRNTNKGKELQAQIDILKMLMHDRYLD", "text": "SIMILARITY: Belongs to the FBPase class 3 family."}
+{"protein": "MQLFHLCLIISCTCPTVQASKLCLGWLWGMDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMTLATWVGVNLEDPASRDLVVSYVNTNMGLKFRQLLWFHISCLTFGRETVIEYLVAFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC", "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": "MKKVLIAGGNGVIGRLLAEGLISDYEVTVLDKDHFDGKASSIQADAANYEELLKKIPKDTDAILNLLAVKIKYDIMDIAEFEKMTDVFYRASYYLCRAAAELGIQKLVFASSNHVTDVYEKDGRSLLGREITTSDYPLSKNLYGVLKLTSEQIGHLFYLENKLSVINLRIGTVVTDEMDTLHEKERTKKTLLSHPDLLSIFKAAIETNIRYGTYYAVSDNPGRPWSIESAVNELGFSPQINTAELLNEEENGA", "text": "SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
+{"protein": "MAEGVFPGAIGIDLGTTYSCVATYENSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPKNTVFDAKRLIGRRFDEESVQSDMKTWPFKVIDSNGAPLIEVEYLGETKTFSPQEISSMVLTKMKEIAEAKIGKKVEKAVVTVPAYFNDAQRQATKDAGAIAGLNVLRIINEPTAAAIAYGVGAGNSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKTEFKKKTGADISGDARALRRLRTAAERAKRTLSSVAQTTVEVDSLFDGEDFEATITRARFEDINAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMAGDVFGVVVPRNTTVPTIKRRTFTTVADHQTTVTFPVYQGERVNCKENTLLGEFDLKGVPPMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAIGRLSSEEIEQMVNQAEEFKAADEAFAKKHEARQRLESYISSVQQTVTDPVLSAKIKRNAKAKVEAALADAFSTLQIEDASADDLRKAEVGLKRAVTKAMSTR", "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": "MEVKGPSGRSFCCESEGQFKSCLKRHTPSLLLPSSWKGNSGSCLMAEALHRTSPTPNSCPLPLPLCRMSGVLCSRNLFTFKFSLFQLDSGASGEPGHSLGLTLGFSYCGNCQTAVVSAQPEGMASNGAYPVLGPGVTANPGTSLSVFTALPFTTPAPGPAHGPLLVTAGAPPGGPLVLSTFPSTPLVTEQDGCSPSGAGASNVFVQMRTEVGPVKAAQAQTLVLTQAPLVWQAPGALCGGVVCPPPLLLAAAPVVPVMAAQVVGGTQACEGGWSQGLPLPPPPPPAAQLPPIVSQGNAGPWPQGAHGESSLASSQAKAPPDDSCNPRSVYENFRLWQHYKPLARRHLPQSPDTEALSCFLIPVLRSLARRKPTMTLEEGLWRAMREWQHTSNFDRMIFYEMAEKFLEFEAEEEMQIQKSQWMKGPQCLPPPATPRLEPRGPPAPEVVKQPVYLPSKAGPKAQTACLPPPRPQRPVTKARRPPPQPHRRAETKARLPPPRPQRPAETKVPEEIPPEVVQEYVDIMEELLGPSLGATGEPEKQREEGKVKQPQEEDWTPPDPGLLSYIDKLCSQKDFVTKVEAVIHPQFLEELLSPDPQMDFLALSQDLEQEEGLTLAQLVEKRLPPLKEKQHSRAAPSRGTARLDSSSSKFAAGQGAERDVPDPQEGVGMETCPPQTTARDSQGRGRAHTGMARSEDSVVLLGCQDSPGLRAARPTSPPQDHRPTCPGVGTKDALDLPGGSPVRESHGLAQGSSEEEELPSLAFLLGSQHKLLPWWLPQSPVPASGLLSPEKWGPQGTHQSPSAERRGLNLAPSPANKAKKQPLFGSLSPAEKTPHRGPGLRVSGEQSLTWGLGGPSQSQKRKGDPLVSRKEKKQHCSQ", "text": "SIMILARITY: Belongs to the NUT family."}
+{"protein": "MLDDYYTWTYPDIPENVAQELLQLNGSLVVVGVVGRSDCDLANKMLAFGMEPPDDHTPEDGQIQCYYKPGTFSLLLHFESTYDAEISGQMIDVCIEDVDTPFDIDSFFERIRCRFVRMMLLALHVCHIVVYVENGLTFDPTLLTVFQLAKFAREQHLMQFLPQMLRETPAARISERTRLCAPRILFLFENFPGDEPKTRESVSTCEFQMEDCIYELLGRYNIVTNSSSNSLVALPNNKQFVFFNAHEELRDDKLLKAIDCLNETMYKPDLKEEEEDLEILAMAPFDGFVKPFTMPVYEKEWENLQYQEDHTVWNFLQRHVQDALVGCFDAGSFKQHAQQGPFQLLNSQEWHDCMATMHKLLVENAKDPDHETSNEEYKLFLKNFDEDLNYEKKFWAHLCELGLKKGIAAYKNAAPANYGTATHRQLLADATLAFEEEGRGPQAQAALAKLAAICHNHWEDGRQQCELLSLRSHPCTLPKNMPHEKHNSGVIHISTCNCGRTQGRREDPFNLRQANYEFYELIAQMCNLCVKVKQYQFPIFEPSVSDYRAAAFEAAFPLLNTGKSGAPQDEDAGEDEAEEEEGQERELPTKKKLQNTASNCCSHPLSPTFGSDLNMSIAGFGASLKESQASSEQLSNSEQNTTSSGTSSADTENELVVELQEPAKKEAREDVGPTDAVSTSTTEYLPGLVHTVSNFGLLPLFPSWSLACVGPSSIYSHNTGLQEHFQSGFLSGANFLLPWDVQLRLVHALKQQYQQQHHGKKQQRWKKQGDRLSLKIFVGMEYECSRGHRFMMCAPDRVLRGGADIERDTCSKVVHNNMPLYYPCPCRSQRNFLAQLMRIHVVTPKAPVNIIVDPKVCVGRYTFTLGSIVPPRLSQSAYWIIRLPYVYQGDDVLIAPPDHLDPDYPLAGGYLLPGMFGVVETDPTLDLNEPGMMGASAAGNFTRI", "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": "MEVVRYFTSNQKQPPATGPKDSIVQLPDIPPVYECNVEVALRFDSVLDPEKLQQSLKRLLEIGNWRQLGGRLRRRDTNSDACGYDLHVPVEFTTERPAFIYKTLESPAAVDEHPVACKMPQPTDPNKILFYNVRDALTPSMTRTHHPRKAQEWAESDLPPLSFEQLNFRDGTIILLLFPHILMDATGYGLFLKAWTCVLQGRMDDVPQCCGFSESITDMLCHKTPAESFTWHNHLLKGLDRLRFTARLLWENICGKEERIIRVPGKFITQTRDKTLADLSTSQDSPFVSHSDVLVAWFVRVVLASLNPQHQRTLVLTNAFDIRHMLPPERAYLQNSVFLAHTMLPVGEVVSNPASFLANEIRRSLVRERTEEQVQARCAWAKDVGIMPLLGSSDMLLCNVSNWSKGGLLDLDFGPAAITQRPGPCVPSSILNCSQMRGVTPEYGIILGKDSQDGWWMQWRLSKFCWAMIERELDTINQTR", "text": "FUNCTION: O-acyltransferase; 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). SIMILARITY: Belongs to the plant acyltransferase family."}
+{"protein": "MSRGGSAGGGQSSLGYLFGGNEAPKPAAKPAPAAAPAPAPAPAPAAAVAAPAEKPSPAKADATKQIPAGIQGSRSNNNYHRADGQNTGNFLTDRPSTKVHAAPGGGSSLGYLFGGN", "text": "FUNCTION: Acts in maintaining the cortical microtubules organization essential for anisotropic cell growth. SIMILARITY: Belongs to the SPIRAL1 family."}
+{"protein": "MTSFQEVPLQTSNFAHVIFQNVAKSYLPNAHLECHYTLTPYIHPHSKDWVGIFKVGWSTARDYYTFLWSPMPEQYVEGSTVNCVLAFQGYYLPNDDGEFYQFCYVTHKGEIRGASTPFQFRAASPVEELLTMEDEGNSDMLVVTTKAGLLELKIEKTLKEKEELLKLVSVLEKETAQLREQVGRMERELSHEKSRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATSKAHQLEEDIVSVTHKAVEKETELDSLKDKLRKAQQEKEQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNVDGNKESMITHFKEEIGKLQSCLADKENLHRALLLTTSNKEDTLLLKEQLRKAEEQVQATRQELIFLAKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKTDQEKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSASSNGVFTKRMGSQQKVNDASINTDPAASASAVDVKPAASCAAETDFDMSAKDHVCEVTKEMAEKVEKYNKCKQLLQDEKAKCNKYADELAQMELKWKEQVRIAENVKLELAELEDSYSLQLAEKDKEINCLASFLENLSREKELTKSLEDQKGRKMEGQSPQQVSRCLNTCSEQSGLLPTLPAAQPVLQYGNPYTAHETRDGADGAFYPDEIQRPPVRGPSWEDNVVCSQPARNLSRPDGLEDPEDSREDENVPIPPDPANQHLRGHGAGFCFDSSFDVHKKCPLCELMFPPNYDQIKFEEHVESHWKVCPMCSEQFPPDYDQQGFERHVQTHFDQNVLNFD", "text": "FUNCTION: Ubiquitin-binding adapter that participates in inflammatory, antiviral and innate immune processes as well as selective autophagy regulation. Plays a key role in the negative regulation of NF-kappa-B and IRF3 signalings by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to bind and inactivate its substrates. Disrupts the interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN- beta production. Recruits also A20/TNFAIP3 to ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B signaling pathways. Inhibits virus-induced apoptosis by inducing the 'Lys-48'-linked polyubiquitination and degradation of MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-mediated apoptosis signaling. As a macroautophagy/autophagy receptor, facilitates the xenophagic clearance of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium tuberculosis. Upon NBR1 recruitment to the SQSTM1- ubiquitin condensates, acts as the major recruiter of RB1CC1 to these ubiquitin condensates to promote their autophagic degradation. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Preautophagosomal structure Cytoplasmic vesicle, autophagosome."}
+{"protein": "MSHWFFIINPTAGHRNGLRVWKSIQKELIKRKVEHRSFLTEHPGHAEVLARQISTIQEYKLKRLIVIGGDGTMHEVVNGLKDVDDIELSFVPAGAYNDFSRGFSIKKIDLIQEIKKVKRPLTRTFHLGSVNFLQDKSQILYFMNHIGIGFDAYVNKKAMEFPLRRVFLFLRLRFLVYPLSHLHASATFKPFTLACTTEDETREFHDVWFAVVSNHPFYGGGMKAAPLANPREKTFDIVIVENQPFLKKYWLLCLMAFGKHTKMDGVTMFKAKDITFYTKDKIPFHADGEIMGTTPFRLASSPSPLRIKT", "text": "FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids other than diacylglycerol (DAG). In fact, is not able to exhibit diacylglycerol kinase activity in vitro. SIMILARITY: Belongs to the diacylglycerol/lipid kinase family."}
+{"protein": "MAPSRLQLGLRAAYSGISSVAGFSIFLVWTVVYRQPGTAAMGGLAGVLALWVLVTHVMYMQDYWRTWLKGLRGFFFVGVLFSAVSIAAFCTFLVLAITRHQSLTDPTSYYLSSVWSFISFKWAFLLSLYAHRYRADFADISILSDF", "text": "FUNCTION: Heme transporter that regulates intracellular heme availability through the endosomal or lysosomal compartment (PubMed:18418376). In macrophages of the reticuloendothelial system, is the heme transporter for heme-iron recycling. Essential for macrophage iron homeostasis, transports heme from the phagolysosome to the cytoplasm during erythrophagocytosis (EP) (PubMed:23395172). SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein Note=In macrophages, specifically localizes to the phagolysosomal membranes during erythrophagocytosis. SIMILARITY: Belongs to the HRG family."}
+{"protein": "MVSRCSCLGVQCLLLSLLLLAAWEVGSGQLHYSVYEEARHGTFVGRIAQDLGLELAELVQRLFRVASKRHGDLLEVNLQNGILFVNSRIDREELCGRSVECSIHLEVIVDRPLQVFHVDVEVKDINDNPPRFSVTEQKLSIPESRLLDSRFPLEGASDADVGENALLTYKLSPNEYFVLDIINKKDKDKFPVLVLRKLLDREENPQLKLLLTATDGGKPEFTGSVSLLILVLDANDNAPIFDRPVYEVKMYENQVNQTLVIRLNASDSDEGINKEMMYSFSSLVPPTIRRKFWINERTGEIKVNDAIDFEDSNTYEIHVDVTDKGNPPMVGHCTVLVELLDENDNSPEVIVTSLSLPVKEDAQVGTVIALISVSDHDSGANGQVTCSLTPHVPFKLVSTYKNYYSLVLDSALDRERVSAYELVVTARDGGSPPLWATASVSVEVADVNDNAPAFAQSEYTVFVKENNPPGCHIFTVSAWDADAQENALVSYSLVERRLGERSLSSYVSVHAESGKVYALQPLDHEELELLQFQVSARDGGVPPLGSNLTLQVFVLDENDNAPALLASPAGSAGGAVSELVLRSVVAGHVVAKVRAVDADSGYNAWLSYELQSAAVGARIPFRVGLYTGEISTTRALDETDSPRQRLLVLVKDHGEPSLTATATVLVSLVEGSQAPKASSRASVGVAPEVALVDVNVYLIIAICAVSSLLVLTLLLYTALRCSAAPTEGACGPVKPTLVCSSAVGSWSYSQQRRQRVCSGEGLPKADLMAFSPSLPPCPMVDVDGEDQSIGGDHSRKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ", "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: [Isoform 2]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MLLLHRAVVLRLQQACRLKSIPSRICIQACSTNDSFQPQRPSLTFSGDNSSTQGWRVMGTLLGLGAVLAYQDHRCRAAQESTHIYTKEEVSSHTSPETGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPLEPFWALYAVHNQSHVRELLAQYKIGELNPEDKVAPTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEAHVCFEGLDSDPTGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPRKAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYVSP", "text": "FUNCTION: Catalyzes the oxidation of sulfite to sulfate, the terminal reaction in the oxidative degradation of sulfur-containing amino acids. SUBCELLULAR LOCATION: Mitochondrion intermembrane space."}
+{"protein": "MATYGNETVDNYLYSSYNPYYYKYPKFKGWRQKAYFTNYGEGETYFDNHHRAQLKSILSQINPNLTPRLRKANTKDVGVQVNPKTDASIQCSLGPRTLLARKRDALRRRRQEVQTPGSPVSSGGVRFPRTQAVYSPVESRRLVSLFREEGEEEEDTDLEVTETVDSAEKLESAEKNVRKQGKKSAKQPLSPEKNINKQTETNEENTNEPVKTEQDDLKSKARVRFQSLEQKYGFYHCKDCNLRWESAYVWCVQGTNKVYFKQFCRTCQKSFNPYRVEDIACQTCKKARCTCSVKSRHVDPKRPHRQDLCGRCKGKRLSCDSTFSFKYII", "text": "FUNCTION: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation (PubMed:27913641). Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similarity). Binds to the 3'-UTR of zona pellucida mRNAs, inhibiting their translation (PubMed:27913641). SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule. SIMILARITY: Belongs to the ZAR1 family."}
+{"protein": "MFYIIGVGPAPGFITEKAAQILREADCVFYEDYTGPIDVETLRRYARSPPTRLTRRDLEDESGRRVLECLSRGKTAVLATAGDPMLATSHAALISIARSRGYSVEVVPGVSIVCAAFSASCLSIYKLGGVATVTYPRGGVYSARPYELVEQNLARGLHTLLLLDVREDGVFMPPRDAAEIMLKLEEREKRGVFDKGRPVVVVPKLGWGGRPAYLPLGELLGSDLEGPAVFIVPGGLSPVERECIEALSVLKSR", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. SIMILARITY: Belongs to the diphthine synthase family."}
+{"protein": "MALLNIFDIAGSALTAQSQRLNVAASNLANADSVTGPDGQPYRAKQVVFQVNAAPGAATGGVKVADVIESQAPDKLVYEPGNPLADAKGYVKMPNVDVVGEMVNTMSASRSYQANVEVLNTVKSMMLKTLTLGQ", "text": "SUBCELLULAR LOCATION: Bacterial flagellum basal body. SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the flagella basal body rod proteins family."}
+{"protein": "MAGQGSVRLTRKSDNVVIIEKDLATEEMVLSMGPQHPSTHGVLRLECRTDGEVVTEAEPYLGYLHRCFEKYCENVDYPAIVPYTDRMDYLAGMNSEMAYAIAVEKLLDIEIPRRVEFIRVIVSELNRIASHLVAIGTYAIDLGAFTPFLFCFRDREHILNMLEWASGARMLYNYIWIGGLAYDVPADFQKRVGEFVDYFRPKALELSRLLTENEIFVKRTKGIGIMPADVAINYGWSGPMLRGSGVQWDLRRNDPYSIYPELDFAVPVPDGKFSDVGDCLSRHLVRALEIEESLKIIEQCIEKMPSAEGFDPRAAVPKRIRPKAGEVYARAENPRGELGFYILSDGKSTSPVRCKARSSCFVNLSAMKDLSKGQLIPDLVAIIGSIDIVLGEVDR", "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 49 kDa subunit family."}
+{"protein": "MGEVKFYLVEGRMLIRHDRMPEWWKFRKYVRALKPEHAVEKVLSELGSNHKVKRYHVKIERVVEVPPEEVPDRTLLVLASLTRWVKP", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL20 family."}
+{"protein": "MGNKIHPIGFRLGITRDWESRWYAGKKQYRHLLLEDQRIRGLLEKELYSAGLARVDIERAADNVAVTVHVAKPGVVIGRGGERIRVLREELAKLTGKNVALNVQEVQNPNLSAPLVAQRVAEQIERRFAVRRAIKQAVQRVMESGAKGAKVIVSGRIGGAEQARTEWAAQGRVPLHTLRANIDYGFALARTTYGVLGVKAYIFLGEVIGGQKPKARPELPKAEERPRRRRPAVRVKKEE", "text": "FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (By similarity). 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": "MNSILDRNVRSSETTLIKPESEFDNWLSDENDGASHINVNKDSSSVLSASSSTWFEPLENIISSASSSSIGSPIEDQFISSNNEESALFPTDQFFSNPSSYSHSPEVSSSIKREEDDNALSLADFEPASLQLMPNMINTDNNDDSTPLKNEIELNDSFIKTNLDAKETKKRAPRKRLTPFQKQAHNKIEKRYRININTKIARLQQIIPWVASEQTAFEVGDSVKKQDEDGAETAATTPLPSAAATSTKLNKSMILEKAVDYILYLQNNERLYEMEVQRLKSEIDTLKQDQK", "text": "FUNCTION: Transcriptional activator of glycolytic gene expression, such as enolase genes (ENO1 and ENO2), glyceraldehyde-3-phosphate dehydrogenase gene (TDH), phosphoglycerate kinase (PGK1), phosphoglycerate mutase (PGM1), pyruvate kinase (PYK1) and triosephosphate isomerase (TPI1) genes. Binds DNA on E-box motifs: 5'- CANNTG-3'. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSSDEKGISPAHKTSTPTHRSASSSTSSQRDSRQSIHILERTASSSTEPSVSRQLLEPEPVPLSKEADSWEIIEGLKIGQTNVQKPDKHEGFMLKKRKWPLKGWHKRFFVLDNGMLKYSKAPLDIQKGKVHGSIDVGLSVMSIKKKARRIDLDTEEHIYHLKVKSQDWFDAWVSKLRHHRLYRQNEIVRSPRDASFHIFPSTSTAESSPAANVSVMDGKMQPNSFPWQSPLPCSNSLPATCTTGQSKVAAWLQDSEEMDRCAEDLAHCQSNLVELSKLLQNLEILQRTQSAPNFTDMQANCVDISKKDKRVTRRWRTKSVSKDTKIQLQVPFSATMSPVRLHSSNPNLCADIEFQTPPSHLTDPLESSTDYTKLQEEFCLIAQKVHSLLKSAFNSIAIEKEKLKQMVSEQDHSKGHSTQMARLRQSLSQALNQNAELRSRLNRIHSESIICDQVVSVNIIPSPDEAGEQIHVSLPLSQQVANESRLSMSESVSEFFDAQEVLLSASSSENEASDDESYISDVSDNISEDNTSVADNISRQILNGELTGGAFRNGRRACLPAPCPDTSNINLWNILRNNIGKDLSKVSMPVELNEPLNTLQHLCEEMEYSELLDKASETDDPYERMVLVAAFAVSGYCSTYFRAGSKPFNPVLGETYECIREDKGFRFFSEQVSHHPPISACHCESKNFVFWQDIRWKNKFWGKSMEILPVGTLNVMLPKYGDYYVWNKVTTCIHNILSGRRWIEHYGEVTIRNTKSSVCICKLTFVKVNYWNSNMNEVQGVVIDQEGKAVYRLFGKWHEGLYCGVAPSAKCIWRPGSMPTNYELYYGFTRFAIELNELDPVLKDLLPPTDARFRPDQRFLEEGNLEAAASEKQRVEELQRSRRRYMEENNLEHIPKFFKKVIDANQREAWVSNDTYWELRKDPGFSKVDSPVLW", "text": "FUNCTION: Regulates cellular transport and efflux of cholesterol (PubMed:26941018). Plays a role in phosphatidylinositol-4-phophate (PI4P) turnover at the neuronal membrane (By similarity). Binds via its PH domain PI4P, phosphatidylinositol-4,5-diphosphate, phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid (By similarity). Weakly binds 25-hydroxycholesterol (PubMed:17428193). SUBCELLULAR LOCATION: Cytoplasm, cytosol Endoplasmic reticulum membrane; Peripheral membrane protein Nucleus envelope Cell membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Note=Co-localizes with OSBPL3 at contact sites between the plasma membrane and the endoplasmic reticulum. SIMILARITY: Belongs to the OSBP family."}
+{"protein": "MSEDSSALPWSINKDDYELQEVIGSGATAVVQAAYCTPKKEKVAIKRINLEKCQTSMDELLKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKSGVLDEATIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPSLETGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEYLQEKILQRAPTISERAKKVRRVPGSSGRLHKTEDGGWEWSDDEFDEESEEGKAAISQLRSPRVKESLTNSELFSTTHPVGTLLQVPEQISAHLPQSAGQMPAQLTPVSLPPAAELAPVQAAQAQSSGAGSQETKIPISLVLRLRNSKKELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVEEPQSNRSVTFKLASGVEGSDIPDDSKLIGFAQLSIS", "text": "FUNCTION: Phosphorylates RELL1, RELL2, RELT and PAK1. Phosphorylates PLSCR1 in the presence of RELT. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
+{"protein": "MPNPRVFFDMSVGGQPAGRIVMELFADTTPRTAENFRALCTGEKGTGRSGKPLHYKDSSFHRVIPGFMCQGGDFTAGNGTGGESIYGAKFADENFIKKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGQVVEGMDVVKAIEKVGSSSGRTAKKVVVEDCGQLS", "text": "FUNCTION: PPIases accelerate the folding of proteins (By similarity). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:24939849). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cyclophilin-type PPIase family."}
+{"protein": "MTNSSPVYDWFQERLEIQAIADDVSSKYVPPHVNIFYCLGGITLVCFLVQFATGFAMTFYYKPTVTEAYSSVSYLMSDVSFGWLIRSVHRWSASMMVLMLILHVFRVYLTGGFKRPRELTWVTGVVMAVITVSFGVTGYSLPWDQVGYWAVKIVSGVPAAIPVVGDFMVELLRGGESVGQSTLTRFYSLHTFVLPWLLAVFMLMHFLMIRKQGISGPL", "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": "MEKAERRVNGPMAGQALEKLQSFFNRGTKLVTHHLHSLFFYKGFIYVVIGFLLGRAFILSEVLPFALPFFGAMLLIRRDKAFYAVLAVLAGALTISPKHSLLILAALLAFFVFSKVAAFITDDRVKALPIVVFFSMAAARAGFVYAQNGVFTTYDYVMAIVEAGLSFILTLIFLQSLPIFTVKKVKQSLKIEEIICFMILIASVLTGLAGLSYQGMQAEHILARYVVLSFSFIGGASIGCTVGVVTGLILGLANIGNLYQMSLLAFSGLLGGLLKEGKKAGAAIGLIVGSLLISLYGEGSAGLMTTLYESLIAVCLFLLTPQSITRKVARYIPGTVEHLQEQQQYARKIRDVTAQKVDQFSNVFHALSESFATFYQASDEQTDDSEVDLFLSKITEHSCQTCYKKNRCWVQNFDKTYDLMKQVMLETEEKEYASNRRLKKEFQQYCSKSKQVEELIEDELAHHHAHLTLKKKVQDSRRLVAEQLLGVSEVMADFSREIKREREQHFLQEEQIIEALQHFGIEIQHVEIYSLEQGNIDIEMTIPFSGHGESEKIIAPMLSDILEEQILVKAEQHSPHPNGYSHVAFGSTKSYRVSTGAAHAAKGGGLVSGDSYSMMELGARKYAAAISDGMGNGARAHFESNETIKLLEKILESGIDEKIAIKTINSILSLRTTDEIYSTLDLSIIDLQDASCKFLKVGSTPSFIKRGDQVMKVQASNLPIGIINEFDVEVVSEQLKAGDLLIMMSDGIFEGPKHVENHDLWMKRKMKGLKTNDPQEIADLLMEEVIRTRSGQIEDDMTVVVVRIDHNTPKWASIPVPAIFQNKQEIS", "text": "FUNCTION: Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Polar septum."}
+{"protein": "MGSNDRASRSPRSDDQREISDMPATKRTRSDSGKSTDSKIPYLSQPLYDLKQTGDVKFGPGTRSALLGLLGGALPKLSSEQHDLVSKAKKYAMEQSIKMVLMKQTLAHQQQQLATQRTQVQRQQALALMCRVYVGSISFELKEDTIRVAFTPFGPIKSINMSWDPITQKHKGFAFVEYEIPEGAQLALEQMNGALMGGRNIKVGRPSNMPQAQQVIDEVQEEAKSFNRIYVASIHPDLSEEDIKSVFEAFGPILYCKLAQGTSLHTHKGYGFIEYANKQAMDEAIASMNLFDLGGQLLRVGRSITPPNALACPTTNSTMPTAAAVAAAAATAKIQALDAVASNAVLGLSQNTPVMAAGAVVTKVGAMPVVSAATSAAALHPALAQAAPALLPPGIFQAPTPVAPSLLGVPAGLQPLQAVVPTLPPPALLATPTLPMTVGGVGVGLVPTVATLAGAEASKGAAAAAALSAAANNAAVTAANLSENIKKAHEKQQEELQKKLMDEGDVQTLQQQENMSIKGQSARQLVMQRLMRPVDSRVIILRNMVGPEDVDETLQEEIQEECSKFGTVSRVIIFNEKQTENEDDDEAEIIVKIFVEFSAGAEAMRGKEALDGRFFGGRRVVAELYDQGIFDQGDLSG", "text": "FUNCTION: Splicing factor that regulates oogenesis and controls both mitosis and mRNA localization in the germline by regulating mRNA splicing of a subset of genes within the ovary. Probably acts by regulating the alternative splice site selection of the otu transcript. Also regulates the alternative splicing of eIF4E1 and grk, while it is not involved in the splicing of par-1, sqd and psq. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RRM half pint family."}
+{"protein": "MAGIKVFGHPASTATRRVLIALHEKNVDFEFVHVELKDGEHKKEPFILRNPFGKVPAFEDGDFKIFESRAITQYIAHEFSDKGNNLLSTGKDMAIIAMGIEIESHEFDPVGSKLVWEQVLKPLYGMTTDKTVVEEEEAKLAKVLDVYEHRLGESKYLASDHFTLVDLHTIPVIQYLLGTPTKKLFDERPHVSAWVADITSRPSAQKVL", "text": "FUNCTION: Involved in camalexin biosynthesis by probably catalyzing the conjugation of GSH with indole-3-acetonitrile (IAN). 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": "MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFCELPADIGPCDDFTGAFHYSPREHECIEFIYGGCKGNANNFNTQEECESTCAA", "text": "FUNCTION: Serine protease inhibitor (By similarity). Does not inhibit plasmin, and does not reduce blood loss in the mouse tail vein blood loss model. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family."}
+{"protein": "MALDGIRMPDGCYADGTWELSVHVTDLNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKRTWLLKTHWTLDKYGIQADAKLQFTPQHKLLRLQLPNMKYVKVKVNFSDRVFKAVSDICKTFNIRHPEELSLLKKPRDPTKKKKKKLDDQSEDEALELEGPLITPGSGSIYSSPGLYSKTMTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPITSPEILAKMFKPQALLDKAKINQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSKEESSGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPEQITTDITPECLVSPRYLKKYKNKQITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKKEELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV", "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. Recruits FBLIM1 to focal adhesions. 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. 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 ITGB3 at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides. SIMILARITY: Belongs to the kindlin family."}
+{"protein": "MRRTTRARTGLSALLLAASLGLGAAPAGADAPQRPAPTPASDSAAALHALDAAVERTLGDDSAGTYVDAGTGELVVTVTTEAAAAKVRAAGATPRRVQRGAAELDAAMAALEARAKIPGTSWGLDPRTNRIAVEADSSVSARDLARLRKVAASLDGAVSVTRVPGVFQREVAGGDAIYGGGSRCSAAFNVTKNGVRYFLTAGHCTNLSSTWSSTSGGTSIGVREGTSFPTNDYGIVRYTTTTNVDGRVNLYNGGYQDIASAADAVVGQAIKKSGSTTKVTSGTVSAVNVTVNYSDGPVYGMVRTTACSAGGDSGGAHFAGSVALGIHSGSSGCTGTNGSAIHQPVREALSAYGVNVY", "text": "FUNCTION: Serine protease that preferentially cleaves peptide bonds on the C-terminal side of aspartate and glutamate with a 10-fold higher reactivity for a glutamyl bond than an aspartyl bond. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MRRDQKMGEGNYPLAGHHLKQKNLLFGPLENIKTGAQIVITDFKKDYIYSVTSKDIISEMDADVVEETNKKEITLITCDKAVKTEGRLVVKGELVDSFGHTN", "text": "FUNCTION: Seems not to play a major role if any as a sortase. SIMILARITY: Belongs to the bacterial sortase family."}
+{"protein": "MDQPSGRSFMQVLCEKYSPENFPYRRGPGMGVHVPATPQGSPMKDRLNLPSVLVLNSCGITCAGDEKEIAAFCAHVSELDLSDNKLEDWHEVSKIVSNVPQLEFLNLSSNPLNLSVLERTCAGSFSGVRKLVLNNSKASWETVHMILQELPDLEELFLCLNDYETVSCPSICCHSLKLLHITDNNLQDWTEIRKLGVMFPSLDTLVLANNHLNAIEEPDDSLARLFPNLRSISLHKSGLQSWEDIDKLNSFPKLEEVRLLGIPLLQPYTTEERRKLVIARLPSVSKLNGSVVTDGEREDSERFFIRYYVDVPQEEVPFRYHELITKYGKLEPLAEVDLRPQSSAKVEVHFNDQVEEMSIRLDQTVAELKKQLKTLVQLPTSNMLLYYFDHEAPFGPEEMKYSSRALHSFGIRDGDKIYVESKTK", "text": "FUNCTION: Acts as a regulator of tubulin stability. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton."}
+{"protein": "MWRAARGSVCLLCRSAAQPRTALLESAQPWISQRSFAMRRDATRERPSRMVLSDRVARGPRTDAPRRPRDRPDGPWAGANRTVANVDRDRRRRPPGSTQERDGGTRDRDTRDTRERHPGASRNRDDNRFKALKMQRALTSIAYRERVNVKAQGVYNEVLKGMVGVKPTPVQRLAIPALLGQRIGQQRETNHRRAAPESKREEFLLAAETGSGKTLAYLLPIINALKVAEADDVDAKAYNVRLEAEKERRGGTPVSEWIDKFEPHPNHARPRAIVLVPTSELVDQVLAASKKNFPRGQDQTTAASTWSLPPRIFSPTWRIVTLISSRVCTTSSIDEADSLFDRSFAPETSKIVERAMPSLKQLILCSATIPRRLDNYLAAHFPNIVRIATPNLHAIPRRVQLGVIDVSKDPLPPTTSWLASHHGLCQTSARPPRRWPSTLVSKGIDAIALHRDTPEHRQSEMLNSFTTTEPMRLSKAEVEANKQAALAKAGGVSKRHLANTKVIVATDLASRGIDTLAVRHVVLYDVPHTTIDFIHRLGRAGRMGRRGRGVVLVGKDDRRDVVSEVKESMFMGQALI", "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": "KECMVDGTVCYIHNHNDCCGSCLCPNGPLARPWEMLVGNCKCGPKA", "text": "FUNCTION: Insecticidal toxin. It inhibits insect voltage-gated sodium channels (Nav) by partially blocking the channel pore in DUM neurons from the American cockroach, not by acting as a gating modifier. The inhibition is only partially reversible after prolonged washout. In vivo, the toxin causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. It also causes uncoordinated movements followed by full paralysis to sheep blowflies (Lucilia cuprina). When the toxin is fused to snowdrop lectin, it is orally active against larvae of the tomato moth (Laconobia oleracea), the rice brown planthopper (Nilaparvata lugens), and the peach-potato aphid (Myzus persicae). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 16 (SFI) family."}
+{"protein": "MNSFTRALFDEYLRKTGWNRGNLYTNLTQSADEVLNLEIPSGINCDLSSIPSPNFASNWEIQMLPILNGSVSYLYSNVDLRLPQNVFGHFAQHQQKFQHLLPPYRHLKTELTDMGFERKPYLMFGKLHLPTAKLEAIFAKRISPPNNLIIRMCHTKRGILTSTSTLLHWQRDTGRSCTEILYSTDEAMIGFRKLWNSGRLQPSLFESANLTKFDPFWSVGAEVYYGALTKCVGASIGARLYSCANGVHNPYSVTCTLNPIVGHLVSTFATSHNDTRVLCSQFEFNLYSYESRLRLGMELFQRKRLLTNEDNHSDDIRQQGNDGVLRLSVSTDGDLVVAWNGQLRDFLYTVGTKVHMLSINPVFFGIHFQYSH", "text": "FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria. 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 MDM10 family."}
+{"protein": "MQKAMKMVKDEDGPLNAAAKSIPSFPHCLQPEASRGKAPQRHPFPEALRGPFSQFRYEPSPGDLDGFPEVFEGGGSRKRKSMPTKVPYTHPAEEASIAQESKSLGPPNLTLLFPQPQRPKCDSQMIDLCNVGLQFYRTLEHLGGKPVKQEPVKPSAMWPQPTPPAFLPAPYPYYPKVHPGLMFPFFVPSSSPFPFSRHTFLPKQPPEPVLPRKVEPLESEETKQKVERVDVNVQIDDSYYVDVGGAQKRWQCPTCEKSYTSKYNLVTHILGHSGIKPHACSRCGKLFKQLSHLHTHMLTHQGTRPHKCQVCHKAFTQTSHLKRHMMQHSEVKPHNCRVCSRGFAYPSELKAHEAKHASGRENICVECGLDFPTLAQLKRHLTTHRGPIQYNCSECDKTFQYPSQLQNHMMKHKDIRPYICSECGMEFVQPHHLKQHSLTHKGVKEHKCGICGREFTLLANMKRHVLIHTNIRAYQCHLCYKSFVQKQTLKAHMIVHSDVKPFKCKLCGKEFNRMHNLMGHLHLHSDSKPFKCLYCPSKFTLKGNLTRHMKVKHGVMERGLHSQGLGRGRLVLVQSAGVLRNLEQEEPFDLSQKRSANGPMFQSDVDSTQDCLCQEEEEEAGEEDNCYEVEPYSPSLAPESQQLCAPEDLSTKQEQTLQDPGEGCRDQDAPEEQQEDRSEDHEGSDIDCEGKDIDCAIREERLSSRLLQSGGQGPSFSDYLYFKHRDEGLKELLERKMEKQAVLLGI", "text": "FUNCTION: Has transcriptional repression activity. Acts as corepressor of ESR1; the function seems to involve CTBP1 and histone deacetylases. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MPDKVNRRKSQRWVSVSKGNYDGADWDSDYSGEELESSPTRQHETICKLPELPKLNLGGSTEERGRPGSGDGLAPRGAAEEEAASSGRGAATPAHEVQTPRSGAAAQKFSLTSSSRSVSSMNKELDTLMDEISKEMTAGGSEPPLVETRQSPVDFNRVGVPALKPEGHLADDSSDSDGEDAAGGSSLSQSFEHLNMSLKTDTASGQAMPLSSPRGSSALPAGRDSLALKKGASPDRASEGSLSSRSEDLLAVDRTAGENTRLKTTNSSDDDTDSLPELITSDAKFRADGASGPARVVSSGVETVIHRAIAPEVAPRLRITSKTDLSYRYDTSSEDDSEAYSGIEDDYLSYQPSPNISDAATFHGHRSRTGSPARAPHPLVEQEEHIELPVISDDDSTSKSSVRDNYYSEESDNTTSQALVTQDNSSHDTIHDTIRERSFDKSTSGSVTHSIPVIKDDNEDWQNQLRQQSVHLGAWNPDTEGKRGAFLTQASPMSTNKGMCGSQDEETTGDDQQLAEPCNDDSDSVWEGFPSVGEYEDLQSVADIKTIYDNQTLYNVPGIITSSTSVPPLPSSMSELTSRQDTSILSESTSGSGLDSDSLMRVVEGQRHAPKPSMFKENFGQTPEVQVEHLVNSPVPSLDICALIEGPQSHSFKRDKLNSHIEDLNAYSSGAQTWIKYALKSTQSSSNITFDEYVISKHVQDAYAQAEEVSKKHSVTNAVNQNVSQLRKKVFSHSMKEGAKGLLSSIGKKKL", "text": "FUNCTION: Involved in the resistance to unfolded protein response (UPR)-inducing agents. SIMILARITY: Belongs to the FYV8 family."}
+{"protein": "MLNDLKFSPAFKSFVDTSFFHELSRLKLEVFKLDSAEKELFSALDLENITSNTVSLSLRDDSFDPVLNNEAVTLKGSVLNFNTIESFKSCDKVKFIKEKGQQLLEQGLKNGLKECVRFYVISFADLKKYKFYYWVCMPTFQSEGSSYEIISTKSIEDGVKKDIWEQNSFISCVVDGKIQEASPQYLKVCQKVIFKDFSRLKGIPAAVTKNFLTVWSQISTRNTYTICFLRDDNSSFAAEIRVTGSNTGCLKVSGWEKNGLGKLAPKSADLSSLMDPVKIAEQSIDLNLKLMKWRIAPDIDLERIKNIKALILGSGTLGCYVARALLAWGTRHVTFVDNSTVSFSNPVRQPLFNFEDCGRPKAEAASDSLKKIFPSVVSAGYQLEIPMIGHPVSNESKQRKDYEILDELIRTHDVIFLLMDARETRWLPSVLGRMHEKIVINAALGFDSYLVMRHGNNNDNLGCYFCNDIVAPSDSLTDRTLDQMCTVTRPGVALLAASQAVELLVTYLQPSTNVLGSAPHQIRGFLNEFKTVKLETPAYQHCCASNENVILTLKENGWNFVKQALDDYKCVEQLSGLSKVQEEAELAIQEDISFDDDEELSIE", "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": "MAMTVKKNDNEVRIQWRVADIKIPNNEIKNVTQDQDIHAVPEENGKEISRIGSTFGKTNRVLIDTDQHLYIIYTQNDQKVYNELTK", "text": "SIMILARITY: Belongs to the UPF0457 family."}
+{"protein": "MTDLPDSTRWQLWIVAFGFFMQSLDTTIVNTALPSMAQSLGESPLHMHMVIVSYVLTVAVMLPASGWLADKVGVRNIFFTAIVLFTLGSLFCALSGTLNELLLARALQGVGGAMMVPVGRLTVMKIVPREQYMAAMTFVTLPGQVGPLLGPALGGLLVEYASWHWIFLINIPVGIIGAIATLMLMPNYTMQTRRFDLSGFLLLAVGMAVLTLALDGSKGTGLSPLAIAGLVAVGVVALVLYLLHARNNNRALFSLKLFRTRTFSLGLAGSFAGRIGSGMLPFMTPVFLQIGLGFSPFHAGLMMIPMVLGSMGMKRIVVQVVNRFGYRRVLVATTLGLSLVTLLFMTTALLGWYYVLPFVLFLQGMVNSTRFSSMNTLTLKDLPDNLASSGNSLLSMIMQLSMSIGVTIAGLLLGLFGSQHVSIDSGTTQTVFMYTWLSMALIIALPAFIFARVPNDTHQNVAISRRKRSAQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
+{"protein": "MLGRTLREVSSALKQGHITPTELCKKCLSLIKKTKYLNAYITVSEEVALKQAEESEKRYKQGQSLGDLDGIPVAVKDNFSTSGIETTCASNMLKGYLPPYNATVVQRLLDQGALLMGKTNLDEFAMGSGSTDGVFGPVKNPWTYSKQYRERSRQDAQEDSHWLITGGSSGGSAAAVAAFTCFAALGSDTGGSTRNPAAHCGTVGFKPSYGLVSRHGLIPLVNSMDVPGIFTRCVDDTAIVLGVLAGHDPKDSTTVNDPVKPTTLPSVPDVSGLCIGIPKEYLVPELSSEIRSLWSQAADLFEAEGARVIEVCLPHTCYSIVCYHVLCTSEVASNMARFDGLQYGHRSAVDMSSTEALYAATRQEGFNDVVKGRILSGNFFLLKENYENYFVKAQKVRRLIVNDFVNVFGSGVDVLLTPTTLTQAVPYLEFIKEDNRTRSAQDDIFTQAVNMAGLPAVNVPVALSSQGLPIGLQLIGRAFCDQQLLTVAKWFEKQVQFPVIQLQDLMDDGSLVPENGKLTSGSLTQ", "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": "MSRLPVLLLLQLLVRPGLQAPMTQTTPLKTSWVNCSNMIDEIITHLKQPPLPLLDFNNLNGEDQDILMENNLRRPNLEAFNRAVKSLQNASAIESILKNLLPCLPLATAAPTRHPIHIKDGDWNEFRRKLTFYLKTLENAQAQQTTLSLAIF", "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 (PubMed:2556442). Stimulates also mature basophils, eosinophils, and monocytes to become functionally activated (PubMed:10779277, PubMed:32889153). In addition, plays an important role in neural cell proliferation and survival (PubMed:23226269). Participates as well in bone homeostasis and inhibits osteoclast differentiation by preventing NF-kappa-B nuclear translocation and activation (PubMed:12816992). Mechanistically, exerts its biological effects through a receptor composed of IL3RA subunit and a signal transducing subunit IL3RB (PubMed:29374162). Receptor stimulation results in the rapid activation of JAK2 kinase activity leading to STAT5-mediated transcriptional program (By similarity). Alternatively, contributes to cell survival under oxidative stress in non- hematopoietic systems by activating pathways mediated by PI3K/AKT and ERK (PubMed:27862234). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-3 family."}
+{"protein": "MAAVQFAAAGVLTGLLALATLASCNTDGDILYKQRLAWEDPNNVLQSWDPTLANPCTWFHVTCNLNNSVIRVDLGKAGISGPLLPDLGALESLQYMELFGNSLNGSIPSTLGNLTDLISLDLWDNLLTGPIPTTLGSISTLRYLRLYENNLTGPIPPSFGNLTSLLELKLHRNSLSGSIPASLGNIKSLQFLKLNENMLTGTVPLEVLSLVVVGNLTELNIARNNLDGTVRSSGLRVTAVIQDMRIA", "text": "FUNCTION: Contributes to activation of the hypersensitive response, a form of programmed cell death, upon fungal infection (PubMed:36577386). May sense the presence of fungal material and relay the signal to WAK17 isoform 1 (Probable)."}
+{"protein": "MPDNIRKAVGLILLVSLLSVGLCKPLKEYLLIPTQMRVFETQTQAIETSLSVNAQTSESSEAFTVKKDPHEIKVTGKKSGESELVYDLAGFPIKKTKVHVLPDLKVIPGGQSIGVKLHSVGVLVVGFHQINTSEGKKSPGETAGIEAGDIIIEMNGQKIEKMNDVAPFIQKAGKTGESLDLLIKRDKQKIKTKLIPEKDEGEGKYRIGLYIRDSAAGIGTMTFYEPKTKKYGALGHVISDMDTKKPIVVENGEIVKSTVTSIEKGTGGNPGEKLARFSSERKTIGDINRNSPFGIFGTLHQPIQNNISDQALPVAFSTEVKKGPAEILTVIDDDKVEKFDIEIVSTTPQKFPATKGMVLKITDPRLLKETGGIVQGMSGSPIIQNGKVIGAVTHVFVNDPTSGYGVHIEWMLSEAGIDIYGKEKAS", "text": "FUNCTION: Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter. SUBCELLULAR LOCATION: Forespore intermembrane space."}
+{"protein": "MQGHHQNHHQHLSSSSATSSHGNFMNKDGYDIGEIDPSLFLYLDGQGHHDPPSTAPSPLHHHHTTQNLAMRPPTSTLNIFPSQPMHIEPPPSSTHNTDNTRLVPAAQPSGSTRPASDPSMDLTNHSQFHQPPQGSKSIKKEGNRKGLASSDHDIPKSSDPKTLRRLAQNREAARKSRLRKKAYVQQLESCRIKLTQLEQEIQRARSQGVFFGGSLIGGDQQQGGLPIGPGNISSEAAVFDMEYARWLEEQQRLLNELRVATQEHLSENELRMFVDTCLAHYDHLINLKAMVAKTDVFHLISGAWKTPAERCFLWMGGFRPSEIIKVIVNQIEPLTEQQIVGICGLQQSTQEAEEALSQGLEALNQSLSDSIVSDSLPPASAPLPPHLSNFMSHMSLALNKLSALEGFVLQADNLRHQTIHRLNQLLTTRQEARCLLAVAEYFHRLQALSSLWLARPRQDG", "text": "FUNCTION: Together with TGA9, basic leucine-zipper transcription factor required for anther development, probably via the activation of SPL expression in anthers and via the regulation of genes with functions in early and middle tapetal development (PubMed:20805327). Required for signaling responses to pathogen-associated molecular patterns (PAMPs) such as flg22 that involves chloroplastic reactive oxygen species (ROS) production and subsequent expression of H(2)O(2)-responsive genes (PubMed:27717447). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
+{"protein": "MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVKAQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLTYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGVNYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRSLREMLDQSKQWAGTALVVPAFEIRRARRMPMNKNELLQLYQVGEVRPFYYGLCTPCQAPTNYSRWVNLPEETLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAGFDFEVLNEGFLVHKGFKEVLKFHPQKEAENQHNKILYRQFKQELKAKYPDSPRHC", "text": "FUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose- beta disaccharide primer, which is further elongated by LARGE1, during synthesis of phosphorylated O-mannosyl glycan. Phosphorylated O- mannosyl glycan is a carbohydrate structure present in alpha- dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Required for axon guidance; via its function in O-mannosylation of alpha- dystroglycan (DAG1). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. Note=Localizes near the trans-Golgi apparatus. SIMILARITY: Belongs to the glycosyltransferase 49 family."}
+{"protein": "MRKFLKVTLASALIGCGVIGTVSSLMVKEAKAVEIITHWVPHEVYGMPGEPDNSGKVFFSGLKAKYMGYPKDAQRSPYPGKYSKFWKTLPAYRYYIPDYMYNRDEVRPSNPIKGTFKLEQCVACHSVMTPGIVRDYNKSAHSKAEPAPTGCDTCHGNNHQKLTMPSSKACGTAECHETQYNEQGQGGIGSHASCSSFAQVECAWSIERPPGDTAGCTFCHTSPEERCSTCHQRHQFDPAVARRSEQCKTCHWGKDHRDWEAYDIGLHGTVYQVNKWDTEQFDFSKKLSDADYVGPTCQYCHMRGGHHNVQRASIVYTSMGMSMADRGAPLWKEKRDRWVSICDDCHSPRFARENLQAMDESVKDASLKYRETFKVAEDLLIDGVLDPMPKDLCPDWSGQHIWSLKIGAYHDGEAYGGTTGESGEFRMSNCTDVERLCFESVGYFQTYIYKGMAHGSWNDATYSDGSFGMDRWLVNVKQNASRARRLAALEKKVGISWQPEQFWKTGEWLDQLTGPYIVKNHPGKTIFDLCPDPGWLDTHHAPAEEVEYIERKLKELGITAGSHSAHHHESGHDPAARSMKEH", "text": "FUNCTION: Catalyzes the four-electron oxidation of hydrazine to N2 (PubMed:21964329). The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane (PubMed:21964329, PubMed:23210799). Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans (PubMed:21964329). Cannot oxidize hydroxylamine to NO (PubMed:21964329). SUBCELLULAR LOCATION: Anammoxosome."}
+{"protein": "MGWPCRSIIPLLVWCFVTLQAATREQKQPHGFAEDRLFKHLFTGYNRWSRPVPNTSDVVIVKFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPEDFDNVTSIRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSNGKVKWVPPAIYKSSCSIDVTYFPFDQQNCKMKFGSWTYDKAKIDLENMEHHVDLKDYWESGEWAIINAIGRYNSKKYDCCTEIYPDITFYFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIIITVFVLNVHHRSPSTHTMPHWVRSFFLGFIPRWLFMKRPPLLLPAEGTTGQYDPPGTRLSTSRCWLETDVDDKWEEEEEEEEEEEEEEEEEKAYPSRVPSGGSQGTQCHYSCERQAGKASGGPAPQVPLKGEEVGSDQGLTLSPSILRALEGVQYIADHLRAEDADFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPYLAGMI", "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. Alpha-2/CHRNA2 sub- subfamily."}
+{"protein": "MPSRRRTLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVQFEDRLFTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNSMKSFENLNNWREEFLIQASPSDPENFPFVLIGNKVDVDDGNSRVVSEKKAKAWCASKGNIPYFETSAKVGTNVEEAFQCIAKDALKSGEEEELYLPDTIDVGTSNQQRSTGCEC", "text": "FUNCTION: Essential for trafficking from prevacuolar compartments to vacuoles. Involved in the trafficking of newly synthesized protein to vacuoles. Essential for plant growth (PubMed:24824487). Participates in the recruitment of the core retromer components to the endosomal membrane by interacting with VPS35A (PubMed:23362252). SUBCELLULAR LOCATION: Endosome membrane; Lipid-anchor Vacuole membrane; Lipid-anchor; Cytoplasmic side Prevacuolar compartment membrane; Lipid-anchor Note=Partial co-localization with VPS3 at cytoplasmic punctate structures, and with VPS39 at subdomains of the vacuolar membrane. Co-localizes with VPS18. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MKPIVSILLFCALAVVIMGHPMNQGYGIPHDVVKLPNGQWCKTPGDDCSKSSECCKAKDTVTYSSGCSQEWSGQLGGFVKLCHICNVESSMC", "text": "FUNCTION: Probable neurotoxin with ion channel impairing activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 21 family."}
+{"protein": "MADKVQTTLLFLAVGEFSVGILGNAFIGLVNCMDWVKKRKIASIDLILTSLAISRICLLCVILLDCFILVLYPDVYATGKEMRIIDFFWTLTNHLSIWFATCLSIYYXFRIANFFHPLFLWMKWRIDRVISWILLGCVVLSVFISLPATENLNADFRFCVKAKRKTNLTWSCRVNKTQHASTKLFLNLATLLPFCVCLMSFFLLILSLRRHIRRMQLSATGCRDPSTEAHVRALKAVISFLLLFIAYYLSFLVATSSYFMPETELAVIFGESIALIYPSSHSFILILGNNKLRHASLKVIWKVMSILKGRKFQQHKQIG", "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": "MPSATGTKRVRGVSIFRPFVFGSEAQPFDPATKPSNVSSDHTHQWRVYVRGVNGEDISYWIKKVQFKLHETYVQNVRTVEHPPYEVTETGWGEFEIQIKIYFVPESMEKPQTLWHSLKLHPYGPDAEGKKERREVVVSQNYEEVVFNEPVEQFYDYLTGGSGTQQMQKGKSGKNAKQAQQQRGGRTAEIPFNETPENPYSRTAENKELDRLAEANKTVEQMIKDEKERLIAREKRLAELRASEGVPAQPLKKSFSGRIPVHSQQRMAGTVGPPDS", "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 histones H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9 may also be required for viability in conditions in which the structural integrity of the spindle is compromised (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the YAF9 family."}
+{"protein": "MSTQYSILFKQEHAHEDAIWTAAWGRSEKDGSETIVTGSLDDLVKVWKWSDEKLELQWTLEGHQLGVVSVNISQNGAIAASSSLDAHIRLWDLETGKQIKSMDAGPVDAWTVAFSPDSKYIATGSHLGKVNIFGVESGKKEHSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHGSWVLSVAFSPDDTHFVSSSSDKSIKVWDTSSRSCVNTFFDHQDQVWSVKYNPTGSKIVSAGDDRAIHIYDCPM", "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": "MGAQETREDASGSSKKRQRPESEVAAESDAAASSTAHAEKFDELNLSSQTLKAIGKMGFTKMTQVQARTIPPLMAGRDVLGAAKTGSGKTLAFLLPAIEMLHSLKFKPRNGTGVIVITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLAKGVNLLIATPGRLLDHLQNTKGFVFKNLKALVIDEADRILEIGFEDEMKQIIKILPNEDRQSMLFSATQTTKVEDLARISLRPGPLFINVDSEKETSTADGLEQGYVVCDSDKRFLLLFTFLKKFQNKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILVCTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKGKGKSLMFLTPHELGFLRYLKAAKVPLNEYEFPANKIANVQSQLEKLLKTNYELNKIAKDGYRSYLQAYASHSLKTVYQIDKLDLVKVAKSYGFPVPPKVNITIGASGKAPAAHKKRKLARD", "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": "MAAGPRTSMLLAFALLCLPWTQEVGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF", "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 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
+{"protein": "MANTNYINRDETVFNDAQSLMQLNKNILLKGPTGSGKTKLAETLSETMNRPMHQINCSVDLDAESLLGFKTIQTNENGSQEIVFIDGPVIKAMKEGHILYIDEINMAKPETLPILNGVLDYRRKLTNPFTGEVVNAAPGFNVIAAINVGYIGTLPMNEALKNRFVVIQVDYIDGDILSDVIKQQSQLSDDIMIQKIIKFNEDLRTMTKQGQISEEAASIRALIDLSDLATIMPIERAIQRTIIDKLEDEREQQAILNAVELNF", "text": "SIMILARITY: Belongs to the CbbQ/NirQ/NorQ/GpvN family."}
+{"protein": "GTWDDIGQGIGRVAYWVGKAMGNMSDVNQASRINRKKKH", "text": "FUNCTION: Kills Lactococci."}
+{"protein": "MASATDSRYGQKESSDQNFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEKMSESLDTADPAVTGAKQGPQLTDQQAPPHQDCAC", "text": "FUNCTION: Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (By similarity). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (By similarity). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (By similarity). Stimulates insulin secretion through interaction with RIMS2 or RPH3AL effectors in pancreatic beta cells (By similarity). Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9 (By similarity). Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1 (By similarity). Also plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (By similarity). FUNCTION: Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (PubMed:11598194). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (By similarity). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (By similarity). Stimulates insulin secretion through interaction with RIMS2 isoform RIMS2 and RPH3AL effectors in pancreatic beta cells (PubMed:15159548, PubMed:20674857). Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin- 9/MYH9 (By similarity). Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1 (By similarity). Plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (By similarity). FUNCTION: Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (PubMed:21689256). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (PubMed:18407218). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (PubMed:17149709). Stimulates insulin secretion through interaction with RIMS2 and RPH3AL effectors in pancreatic beta cells (By similarity). Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9 (By similarity). Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1 (By similarity). Plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (PubMed:28057568). Interacts with MADD (via uDENN domain); the GTP- bound form is preferred for interaction (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Lysosome Cytoplasmic vesicle, secretory vesicle Cell projection, axon Cell membrane; Lipid- anchor; Cytoplasmic side Presynapse Postsynapse Note=Cycles between a vesicle- associated GTP-bound form and a cytosolic GDP-bound form. SUBCELLULAR LOCATION: Cytoplasm, cytosol Lysosome Cytoplasmic vesicle, secretory vesicle Cell projection, axon Cell membrane; Lipid- anchor; Cytoplasmic side Presynapse Postsynapse Note=Cycles between a vesicle- associated GTP-bound form and a cytosolic GDP-bound form. SUBCELLULAR LOCATION: Cytoplasm, cytosol Lysosome Cytoplasmic vesicle, secretory vesicle Cell projection, axon Cell membrane; Lipid- anchor; Cytoplasmic side Presynapse Postsynapse Note=Cycles between a vesicle-associated GTP-bound form and a cytosolic GDP-bound form. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MFMINILMLIIPILLAVAFLTLVERKVLGYMQLRKGPNVVGPYGLLQPIADAIKLFIKEPLRPATSSASMFILAPIMALGLALTMWIPLPMPYPLINMNLGVLFMLAMSSLAVYSILWSGWASNSKYALIGALRAVAQTISYEVTLAIILLSVLLMSGSFTLSTLIITQEQMWLILPAWPLAMMWFISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFALFFMAEYANIIMMNIFTAILFLGTSHNPHMPELYTINFTIKSLLLTMSFLWIRASYPRFRYDQLMHLLWKNFLPLTLALCMWHVSLPILTSGIPPQT", "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 the catalytic activity and assembly of complex I (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
+{"protein": "MSSRTVIRGGLVITASDEIHADVLIEDGRVAALAATGTPAAEAFTAENVIDASGKYVIPGGVDGHTHMEMPFGGTYAADTFETGTRAAAWGGTTTIVDFAIQSVGHSLREGLDAWHAKAEGNCAIDYGFHMIVSDVNQETLKEMDLLVEEGVTSFKQFMAYPGVFYSDDGQILRAMQRAAENGGLIMMHAENGIAIDVLVEQALARGETDPRFHGEVRKALLEAEATHRAIRLAQVAGAPLYVVHVSATEAVAELTRARDEGLPVFGETCPQYLFLSTDNLAEPDFEGAKYVCSTPLRPKEHQAALWRGLRTNDLQVVSTDHCPFCFSGQKELGRGDFSRIPNGMPGVENRMDLLHQAVVEGHIGRRRWIEIACATPARMFGLYPKKGTIAPGADADIVVYDPHAEQVISAETHHMNVDYSAYEGRRITGRVETVLSRGEPVVTEREYTGRKGHGAYTPRATCQYLT", "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": "PLFDKRQRCCNGRRGCSSRWCRDHSRCCGRR", "text": "FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin blocks rNav1.5/SCN5A (IC(50) is 1.3 uM), rNav1.6/SCN8A (IC(50) is 160 nM), rNav1.7/SCN9A (IC(50) is 1.3 uM), rNav1.1/SCN1A (K(d) is 3.8 nM), rNav1.2/SCN2A (K(d) is 1.3 nM), rNav1.4/SCN4A (K(d) is 0.22 nM), rNav1.6/SCN8A (K(d) is 69 nM), and rNav1.7/SCN9A (K(d) is 260 nM). This toxin is very potent but weakly discriminating among sodium channels. The block of these channels is modified when beta-subunits are coexpressed with alpha subunits. Hence, blocks of channels containing beta-1 and beta-3 subunits are more potent (compared to channels without beta subunits), whereas blocks of channels containing beta-2 and beta-4 subunits are less potent (compared to channels without beta subunits). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily."}
+{"protein": "MMRLRRLLERMLRRCCFRDCSVRLTKSLCFKKLIEFDATKNQIVTKLQRLKKKFNNAVKNARKKGQTEDEVEYAKESEKKRFDLSIMIWGSNGVLVAGKSSKKKVAPKEMKPEETDAKVVNEGLSIGREMVPFGSSCGLDESKLTTGWENVEDGAEKREVEEKWKKFKDKLFELLYERSVLMNKTEAMMFKAES", "text": "SIMILARITY: Belongs to the GeBP family."}
+{"protein": "MSNPILSWRRVRALCVKETRQIVRDPSSWLIAVVIPLLLLFIFGYGINLDSSKLRVGILLEQRSEAALDFTHTMTGSPYIDATISDNRQELIAKMQAGKIRGLVVIPVDFAEQMERANATAPIQVITDGSEPNTANFVQGYVEGIWQIWQMQRAEDNGQTFEPLIDVQTRYWFNPAAISQHFIIPGAVTIIMTVIGAILTSLVVAREWERGTMEALLSTEITRTELLLCKLIPYYFLGMLAMLLCMLVSVFILGVPYRGSLLILFFISSLFLLSTLGMGLLISTITRNQFNAAQVALNAAFLPSIMLSGFIFQIDSMPAVIRAVTYIIPARYFVSTLQSLFLAGNIPVVLVVNVLFLIASAVMFIGLTWLKTKRRLD", "text": "FUNCTION: Part of the ABC transporter complex YbhFSR that could be involved in efflux of cefoperazone. Probably involved in the translocation of the substrate across the membrane. FUNCTION: Part of the ABC transporter complex YbhFSR that could be involved in efflux of cefoperazone. Probably involved in the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-2 integral membrane protein family."}
+{"protein": "MPTIQQLIRSARKKITKKTKSPALKSCPQRRGICLRVYTVTPKKPNSALRKVARVRLTTGFEVTAYIPGVGHNLQEHAVVLVRGGRVKDLPGVRYHIVRGSLDTAGVKNRVQSRSKYGVKMGSKTAAKTAGKK", "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": "GCTKFMGSCKTDADCCEHLECYKYKWCGWDGTF", "text": "FUNCTION: Gating-modifier toxin with very weak activity on Nav1.7/SCN9A and Nav1.8/SCN10A. Shows 22% peak current inhibition (at 10 uM) on Nav1.8/SCN10A sodium channels. Show peak current inhibition and delays fast inactivation on Nav1.7/SCN9A (EC(50)>10 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 47 subfamily."}
+{"protein": "MLNLFILLLERVGLIILIAYILMNINHFKTMMNEREKRRSQWQLIIIFGCFSMISNFTGIQIRGDEIINGTVYNHLDPDASLANTRVLTIGVSGLIGGPFVALAVAVISGMYRVYIGGADAYIYLISSIFIALISGYFGYKAMRANRYPTIVKGACIGGTTEIIQMLCILLFSDNTEHAWTLVKLIAIPMISINSIGTAIFLSIILSTIKQEEETRAIQTHDVLQLANQTLPYFRSGLNEQSAKKAAEIILNLMRVSAVAITNRKDILTHVGVASDHHVAQKAIITNLSKRAIQSGTLKEAYSSEEIGCNHPGCPLEAAIVVPLRVKNDVVGTLKLYFTNKYDVNYSDKQLATGLAEIFSSQLELGQAETQSALIRDAEIKSLQAQVNPHFFFNAINTISALIRIDSEKARELLLQLSQFFRSNLQGARNNTISLEKELQQVESYLSLEQARYPDRFNVSFDIDRTCYGALVPPFAIQILVENAIKHAFKNRKYNNEIIVKAHKAQTGLVISVSDNGHGIPYEKLDKIGKTSVHSESGTGSALENLNRRLDGLFGYEASLQIHSDHQGTQVSCTIPYHNLEEEKIESNHCR", "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": "MTDAGKTARLNRISTDDRLLTIPMDHGITLGAIDGLVDIEATIREVTANGADAVLTQPGIAPRVHPNKGDAGYIVHLNASTTLGPDQTDKRRTGTVEDAVRAGADAVSFHINVGSDHEPDQITALADVAADADRLGVPVLAMAYARGPGVDEHDAANLGHAVRLAEEVGADVIKTAYSGSTESFQRVVDATAKPVIIAGGDPAGDRETLQGIRDAMDAGAAGVSTGRTVFQHATPGAMTAAISAVVHDDADPEAALARAGLVVDA", "text": "FUNCTION: Catalyzes a transaldol reaction between 6-deoxy-5- ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7- dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS subfamily."}
+{"protein": "MSNTTFRPFTGSSRTVVEGEQAGAQDDMSLLQSLFSDKSREEFAKECKLGMYTNLSSNNRLNYIDLVPKNTGSRALNLFKSEYEKGHIPSSGVLSIPRVLVFLVRTTTVTESGSVTIRLVDLISASSVEILEPVDGTQEATIPISSLPAIVCFSPSYDCPMQMIGNRHRCFGLVTQLDGVISSGSTVVMSHAYWSANFRSKPNNYKQYAPMYKYVEPFDRLKRLSRKQLKNYVRGITNQSVNHGYLLGKPLLKTDEQDPEMIVLEEESLTPTDSNGVGKDKIAVTAKSVAGLPTASLSINRR", "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 bromovirus movement protein family."}
+{"protein": "MSTISTTTAPEFIRVKRRRDEDSVQALLIDEGKRVKKQKFIFKLSKTVSSESYQSEQESSTPLLKLAHEDHRHFVLEQRKKSRRDSDDEKSQQRLAAEGSTVDDDGLPPEINQMVNDYLKLNKGVEKTERKKPSRKYFTGDSAKIASLPSLDYVFDIYHLEKIHDDEVARYNNEKNIGFVKIIEHIDLALDEESDPNEARSDDEDSNDENYYQNDYPEDEDDDRSILFGSEGEDIAALGEEIVIGVNKSRFSSWNDDKIQGSNGYHDVEEEYGDLFNRLGGKSDVLKSINSSNFIDLDGQEGEIEISDNEDDSDEGDDIEYPRNEFFPTDVDDPLAHHRDRIFHQLQKKINRS", "text": "FUNCTION: Directs RNA polymerase II nuclear import. Binds RNA polymerase II in the active center cleft between the two largest subunits in the cytoplasm. Then uses an N-terminal bipartite nuclear localization signal that may be recognized by karyopherin alpha to direct the polymerase II complex nuclear import. In the nucleus, is displaced from polymerase II complex by transcription initiation factors and nucleic acids, enabling its export and recycling. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the nucleus and cytoplasm. SIMILARITY: Belongs to the IWR1/SLC7A6OS family."}
+{"protein": "MSTDTGVSLPSYEEDQGSKLIRKAKEAPFVPVGIAGFAAIVAYGLYKLKSRGNTKMSIHLIHMRVAAQGFVVGAMTVGMGYSMYREFWAKPKP", "text": "FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes (By similarity). FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein Mitochondrion inner membrane. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein Mitochondrion inner membrane."}
+{"protein": "MTQPPASTSGIMGTLSSWNLKILQINQLHLVHWNAVKFENFEDAALEENGLAVIGVFLKISETSGSPVSTGRPKPLARKLRPAQKHWVLQSRPFLSSQVQENCKVTYFHRKHWVRIRPLRTTPPSWDYTRICIQREMVPARIRVLREMVPEAWRCFPNRLPLLSNIRPDFSKAPLAYVKRWLWTARHPHSLSAAW", "text": "SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
+{"protein": "MPHVITQSCCNDASCVFACPVNCIHPTPDEPGFATSEMLYIDPVACVDCGACVTACPVSAIAPNTRLDFEQLPFVEINASYYPKRPAGVKLAPTSKLAPVTPAAEVRVRRQPLTVAVVGSGPAAMYAADELLVQQGVQVNVFEKLPTPYGLVRSGVAPDHQNTKRVTRLFDRIAGHRRFRFYLNVEIGKHLGHAELLAHHHAVLYAVGAPDDRRLTIDGMGLPGTGTATELVAWLNGHPDFNDLPVDLSHERVVIIGNGNVALDVARVLAADPHELAATDIADHALSALRNSAVREVVVAARRGPAHSAFTLPELIGLTAGADVVLDPGDHQRVLDDLAIVADPLTRNKLEILSTLGDGSAPARRVGRPRIRLAYRLTPRRVLGQRRAGGVQFSVTGTDELRQLDAGLVLTSIGYRGKPIPDLPFDEQAALVPNDGGRVIDPGTGEPVPGAYVAGWIKRGPTGFIGTNKSCSMQTVQALVADFNDGRLTDPVATPTALDQLVQARQPQAIGCAGWRAIDAAEIARGSADGRVRNKFTDVAEMLAAATSAPKEPLRRRVLARLRDLGQPIVLTVPL", "text": "SIMILARITY: In the C-terminal section; belongs to the ferredoxin--NADP reductase family."}
+{"protein": "MGSSHIPLDPSLNPSPSLIPKLEPVTESTQNLAFQLPNTNPQALISSAVSDFNEATDFSSDYNTVAESARSAFAQRLQRHDDVAVLDSLTGAIVPVEENPEPEPNPYSTSDSSPSVATQRPRPQPRSSELVRITDVGPESERQFREHVRKTRMIYDSLRMFLMMEEAKRNGVGGRRARADGKAGKAGSMMRDCMLWMNRDKRIVGSIPGVQVGDIFFFRFELCVMGLHGHPQSGIDFLTGSLSSNGEPIATSVIVSGGYEDDDDQGDVIMYTGQGGQDRLGRQAEHQRLEGGNLAMERSMYYGIEVRVIRGLKYENEVSSRVYVYDGLFRIVDSWFDVGKSGFGVFKYRLERIEGQAEMGSSVLKFARTLKTNPLSVRPRGYINFDISNGKENVPVYLFNDIDSDQEPLYYEYLAQTSFPPGLFVQQSGNASGCDCVNGCGSGCLCEAKNSGEIAYDYNGTLIRQKPLIHECGSACQCPPSCRNRVTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANILTMNGDTLVYPARFSSARWEDWGDLSQVLADFERPSYPDIPPVDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYGVVDDWNAKLAICN", "text": "FUNCTION: Histone methyltransferase family member that plays a role in gene silencing (PubMed:19043555, PubMed:24463519, PubMed:27171427). Together with MORC6 and SUVH2, regulates the silencing of some transposable elements (TEs) (PubMed:27171427). According to PubMed:19043555, the protein does not bind S-adenosyl-L-methionine and lacks methyltransferase activity. Instead, it may function downstream of DRM2 in RNA-directed DNA methylation, binding to methylated DNA and recruiting DNA-directed RNA polymerase V to chromatin (PubMed:24463519, PubMed:27171427). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Associates with centromeric constitutive heterochromatin. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily."}
+{"protein": "MPEVSNGRRPSVATFLRQFASTIIPLVNVKQSMPTTQINIVLAEPRCMAGEFFNAKVLLDSSDPDTVVHSFCAEIKGIGRTGWVNIHTDKIFETEKTYIDTQVQLCDSGTCLPVGKHQFPVQIRIPLNCPSSYESQFGSIRYQMKVELRASTDQASCSEVFPLVILTRSFFDDVPLNAMSPIDFKDEVDFTCCTLPFGCVSLNMSLTRTAFRIGESIEAVVTINNRTRKGLKEVALQLIMKTQFEARSRYEHVNEKKLAEQLIEMVPLGAVKSRCRMEFEKCLLRIPDAAPPTQNYNRGAGESSIIAIHYVLKLTALPGIECEIPLIVTSCGYMDPHKQAAFQHHLNRSKAKVSKTEQQQRKTRNIVEENPYFR", "text": "SIMILARITY: Belongs to the arrestin family."}
+{"protein": "MASLVTLPAIAFSNPATASGAVRLRAAAFRCWALRRRGWAVAAAVASPNSVLSEHAFKRLQLGSDDEDEEGPYGSDADEGFQGDEEELAIARLGLPDELVATLEKRGITHLFPIQRAVLIPALGGRDLIARAKTGTGKTLAFGIPMIKQLMEQDDGRSTRRGRTPRVLVLAPTRELAKQVEKEIKESAPKLGTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVQYLVLDEADQMLAVGFEEDVETILQQLPADRQSMLFSATMPSWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLHAIPLTATSKRTILSDLITVYAKGGKTIVFTRTKKDADEVSLALTTSIASEALHGDISQHQRERTLNGFRQGKFTVLVATDVAARGLDIPNVDLIIHYELPNDPETFVHRSGRTGRAGKAGTAILMFTSSQKRTVMSLERDVGCKFEFISPPSIEEVLESSAEHVIATLRGVHPESTQYFLGAAEKLTEELGPHALASALAHLSGFSQPPSSRSLISYEQGWVTLQLTREPGYGRGFFSPRSVTGFLSDVCSAAADEVGKIYITADENVQGAVFDLPEEIAKDLLTMEVPPGNTLTKISKLPALQDDSPATDSYGRFSNDRGSRNRRSRGGGASRGRGGWDTDSEDRYRRGGRSLRSDNDSWSDDDWSGGGRKSNRSSSSFGGRSSSYGSRGSPSPSFGVRSSSLGGRESSRSFSGACFNCGESGHRASDCPNK", "text": "FUNCTION: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Required for normal development of chloroplasts. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily."}
+{"protein": "MGGYVNIKTFTHPAGEGKEVKGMEVSVPFEIYSNEHRIADAHYQTFPSEKAAYTTVVTDAADWRTKNAAMFTPTPVSG", "text": "FUNCTION: Capsid decoration protein which helps to stabilize the capsid against extremes of pH and temperature. Once maturation and expansion of the capsid has occured, trimers of soc attach the interfaces between the hexamer of the major capsid protein. Acts as a 'glue' between neighboring hexameric capsomers. Dispensable for the head morphogenesis and phage infection. SUBCELLULAR LOCATION: Virion Note=870 copies decorate the capsid. SIMILARITY: Belongs to the Tevenvirinae Soc family."}
+{"protein": "MNKEKVPQNAVPNGRTKLRQVTSATPLDEVFQYWEEDGAIVIKGLLTSAQVEQLNQEMGPILQKVAIGGHASDVRLQNFHGMKTKRAGDLTNNSAVFRDHLLDNDFIHAVSQRCFAYRGKMGPDAYWLGSASTIHVGPGQKPQTLHRDLGSYPIFWMLGPQGPESQINFLVATTDFTEANGATRIIPGSHKWEFNQHGDRDMTIPAEMKAGDCLLISGKVIHGTGGNKTDQERGCLAVTMCANFLAPEEAHPFIVSMGTAKKLPVRSQRCLGFRSQWPQSSPGLWTKDYSELALHLGLDD", "text": "FUNCTION: Dioxygenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:11728154, PubMed:12620260, PubMed:14602658, PubMed:15066782, PubMed:16536629). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3- keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy- 12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C- 14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C- 15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424). SIMILARITY: Belongs to the PhyH family."}
+{"protein": "NLLQFRKMIKKMTGKEVVWYAFYGCYCGGGGK", "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 II subfamily."}
+{"protein": "MAPVLPLVLPLQPRIRLAQGLWLLSWLLVLVGGLTLLCSGHLLVQLWHLGTFLAPSCPFSALPQVALAASAVALGTGLVGSGASRASLDAEQYPPWRGVLGPLLVAGTAGGGGLLVLALGLALALPGTLDTGLEEGLGSALVHYKDTEVPGRCQAKRLLDELQLRHHCCGRHGYKDWFGIQWVSNRYLDPNDPDVVDRIQSNVEGLYLIDGVPFSCCNPHSPRPCLQSQLSDPHAHPLFDPRQPNLNLWSQGCHEVLLGHLQGLASTLGNMLAVTFLLQTLVLLGLRYLQTALEGLGGVIDGEGEAQGYLFPAGLKDMLKTAWLQGAGPHRPAPGETPPEEKPPKECLPEA", "text": "FUNCTION: Plays a role in rod outer segment (ROS) morphogenesis (By similarity). May play a role with PRPH2 in the maintenance of the structure of ROS curved disks (PubMed:24196967). Plays a role in the organization of the ROS and maintenance of ROS disk diameter (By similarity). Involved in the maintenance of the retina outer nuclear layer (By similarity). SUBCELLULAR LOCATION: Photoreceptor inner segment membrane; Multi-pass membrane protein Photoreceptor outer segment membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PRPH2/ROM1 family."}
+{"protein": "MARPRRAREPLLVALLPLAWLAQAGLARAAGSVRLAGGLTLGGLFPVHARGAAGRACGQLKKEQGVHRLEAMLYALDRVNADPELLPGVRLGARLLDTCSRDTYALEQALSFVQALIRGRGDGDEVGVRCPGGVPPLRPAPPERVVAVVGASASSVSIMVANVLRLFAIPQISYASTAPELSDSTRYDFFSRVVPPDSYQAQAMVDIVRALGWNYVSTLASEGNYGESGVEAFVQISREAGGVCIAQSIKIPREPKPGEFSKVIRRLMETPNARGIIIFANEDDIRRVLEAARQANLTGHFLWVGSDSWGAKTSPILSLEDVAVGAITILPKRASIDGFDQYFMTRSLENNRRNIWFAEFWEENFNCKLTSSGTQSDDSTRKCTGEERIGRDSTYEQEGKVQFVIDAVYAIAHALHSMHQALCPGHTGLCPAMEPTDGRMLLQYIRAVRFNGSAGTPVMFNENGDAPGRYDIFQYQATNGSASSGGYQAVGQWAETLRLDVEALQWSGDPHEVPSSLCSLPCGPGERKKMVKGVPCCWHCEACDGYRFQVDEFTCEACPGDMRPTPNHTGCRPTPVVRLSWSSPWAAPPLLLAVLGIVATTTVVATFVRYNNTPIVRASGRELSYVLLTGIFLIYAITFLMVAEPGAAVCAARRLFLGLGTTLSYSALLTKTNRIYRIFEQGKRSVTPPPFISPTSQLVITFSLTSLQVVGMIAWLGARPPHSVIDYEEQRTVDPEQARGVLKCDMSDLSLIGCLGYSLLLMVTCTVYAIKARGVPETFNEAKPIGFTMYTTCIIWLAFVPIFFGTAQSAEKIYIQTTTLTVSLSLSASVSLGMLYVPKTYVILFHPEQNVQKRKRSLKATSTVAAPPKGEDAEAHK", "text": "FUNCTION: G-protein coupled receptor for glutamate. 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 inhibits adenylate cyclase activity (By similarity). Signaling stimulates TRPM1 channel activity and Ca(2+) uptake. Required for normal vision. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cell projection, dendrite Note=Subject to trafficking from the endoplasmic reticulum to the Golgi apparatus and then to the cell membrane. SIMILARITY: Belongs to the G-protein coupled receptor 3 family."}
+{"protein": "MGLPKSAYKKLLIDCPTRVINKNCAQRVKDVSPLITNFEKWSDKRKKLYFKDEEEMVGHFHLENFNLKNNLYGRLLASPMRAEKISKLKSCRELLIPLKVVPSTGKDQHADKDKLKLVPTLDYSKSYKSSYVLNSASIVQDNLAAATSWFPISVLQTSTPKSLEVDSSTFITEYNANLHAFIKARLSVIPNVGPSSINRVLLICDKRKTPPIEIQVVSHGKGLPITQSVFNLGYLHEPTLEAIVSKDAVTKGIYLDADNDKDLIKHLYSTLLFQSVN", "text": "FUNCTION: Required for respiratory activity and maintenance and expression of the mitochondrial genome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RRG8 family."}
+{"protein": "MAKNSRSQWIAKNLQRLLNVGLIALAAILVVFLIKETFHLGKVLFVNNQDASSYMLIEGIVIYFLYFEFIALIVKYFESGYHFPLRYFIYIGITAIIRLIIVDHENPIDTLIYSGSILLLVVTLYLANTERLKRE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsiE family."}
+{"protein": "MPSSLFADLERNGSGGGGGGGGGGGGGGSGGGETLDDQRALQLALDQLSLLGLDSDEGASLYDSEPRKKSVNMTECVPVPSSEHVAEIVGRQGGSGRDGDRRGFSISPTPSLEPWLPGCKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVAMARREIISAAEHFSMIRASRNKNTALNGAVPGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEAHIALRTGGIIELTDENDFHANGTDVGFDLHHGSGGSGPGSLWSKPTPSITPTPGRKPFSSYRNDSSSSLGSASTDSYFGGGTSGSAAATSRLADYSPPSPALSFAHNGNNNNNGNGYTYTAGEASVPSPDGGPELQPTFDPAPAPPPGTPLLWAQFERSPGGGSAAPVSSSCSSSASSSASSSSVVFPGGGASSTPSNANLGLLVHRRLHPGTSCPRLSPPLHMATGAGEHHLARRVRSDPGGGGLAYAAYANGLGTQLPGLPSSDTSGSSSSSSSSSSSSSSSSGLRRKGSRDCSVCFESEVIAALVPCGHNLFCMECANRICEKSEPECPVCHTAVTQAIRIFS", "text": "FUNCTION: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, P-body Cytoplasmic granule Note=Predominantly expressed in the cytoplasm and shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Localization to P-bodies is dependent on 14-3-3 (By similarity)."}
+{"protein": "MRNVIRRVTTMTFTFLLQSPPLPISPSPPQFSLSSSPLSKTQRFITPSQGSRLRTLCTKVIIPNMQDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYEQTLQKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSMCVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP", "text": "FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). Involved in the PLP salvage pathway. Has a higher preference for PNP over PMP. May also catalyze 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: Plastid, chloroplast. SIMILARITY: In the C-terminal section; belongs to the pyridoxamine 5'- phosphate oxidase family. SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family."}
+{"protein": "MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKVRTRVTNTEQLVFIAALNISYELTQEKAKTRDYAASMEQRIRMLQQTIEQALLDQGRITEKTGQNFE", "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": "KPLWRL", "text": "FUNCTION: Vasodilator. May target bradykinin receptors (BDKRB). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-related peptide family."}
+{"protein": "MPSLMVGGTTSSAGKSLLAAAFCRILARRGYDVAPFKAQNMSLNSFVTSKGKEIAIAQAYQAFAAGIEPDERMNPVLLKPKGNFVSQLVVMGEAVGDVDSRKYYGVKVEWLKRVVEEAYLSLAEEYDFVVIEGAGGMAEINLYERDLPNIHIARFARPDILIVGDIDRGGVFASLYGTYALLPDDVKPLVKGFVINRLRGREDVLESGIRELERLTGIRVLGVLPYLDYNFPSEDSLNIEEWGAEGTVGIVRLPRVSNFTDFEPLREHARFLSLNSSLNGCEVVIIPGSKDTIADLKALKSSKLGEEIVRKAGEIPVIGICGGYQIMCRELVDMGVEHGRIRAKGLGLLDAVTEFREYRKRTVQVEKRVNGNAVILDRIRGEKVWGYEIHKGITRASNPIFEDDGCASEDGMCWGTYLHGLFWNENVLRALGGYLGIKFRQKEDWADLIADEVEGRLDLGVLGL", "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 (By similarity). SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily."}
+{"protein": "MFGPFKLTSPVAGGLLWKIPWRMSTHQKTRQRERLRNVDQVIKQLTLGLHVQRCQDKGLTYQEAMESKKKYKPRSKSLRLLNKPSVFPKENQMSSKDKYWTFDKKAVGYRKGIHKVPKWTKISIRKAPKFF", "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 mL60 family."}
+{"protein": "MTVLYTSASLKKMKCLAFNMGMNCVRTVSHARSGGAKFGGRNVFNIFDSKTPDSVRIKAFKNTIYQSAMGKGKTKFSAMEINLITSLVRGYKGEGKKNAINPLQTNVQILNKLLLTHRLTDKDILEGMNLAAGPVNVAIPRDITPQEEKKKVELRNRKAENMDLHPSRKMHIKELLHSLNLDMCNDEEVYQKISLYLQKNEESRTSVGASQQNHVDIDINSLKRYLQNIEKKARQKSAIDKQKKNQARIYQWNTQSFSEIVPLSAGNILFKREPNRLWKRLQNGISVFLGSNGGGKKSKTTKKVLQGNNILLHSLENNKDMTLSNNFDHSVFNINFTDLFGVINASGSPPDRVLNEINEIELKGWKCVGNLYDNNKIVVFQSSNPLLEDTKIPQKSFTNSKRFLISLSALLASFFAYYRYRLSQRQESKK", "text": "FUNCTION: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post- transcriptional gene expression. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion membrane; Single-pass membrane protein."}
+{"protein": "MASSEGSYRDLEKKLKNGLTSISQDIVDKYGNLKVSLNVNATAKLIFDRLENLEDIAEMSTRNLSNLIDQTAKDSPEMLAEIKSQAQSCENLVEFLQSMKNVEEQLIIMRSKTTNRVEWGTAILACKDFLNDTNMLLEGIGRDGFDMSVPLKHFAAEYSVLSYNCRYQLSADYERAMNVPKLSKQKCGDRTNVSFSVFNVGSVEDQKMLNETLSAMNMIGQLPERLDAWKIVILNVFCEAIVASRDGVDVYIVDNPTPDQTRFLINQKPRGKKDKTIDVAKVLESMEVFFTKLHSVLHSHELLDATGKTFTSMIGSVIEEQLITMILKDVIAIAAPVTETADEDQEMFINLLQIGEVFVERMKELGFFSQKAKLLFTLDTDTIFVTRRCFAIVSKANKLINETYDKLVTVGVDDSAIKDIDLLAKAHTHAEHFAKEYGKDLGRLWSHNEDSQFPSFFAFQKCTVSESTINFVNLLRDNVKAAFACEDEGARAKLALTAENIVRLYVILTPRKHAELFSSIPNMAAIFYNNCHYISHCIMTMSFEASGDNQKTLLEPLLLDSVIRLRTVAADCMEKTLTRCRREMTAYLEDHSIFEHLPASYKTTKNTFAAAEEMSESADILVPREEPKIIKCLAACLLHIRLIAKNLREPLTEVVYCKVIGSLVSFLLDSLVRHVVTTSDFRENDANVMADVFKRLLEVVANIVAYKEQTKVTDFCAREYFRLNEIVFVLGNRMQDIEHRWFNAKGPMAEHLSRSEVVGLIKALFADSQHRSDLIARL", "text": "FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis (PubMed:9298984). Required for the assembly of the dynein-dynactin and mdf-1-mdf-2 complexes onto kinetochores (PubMed:18936247). Its function related to the spindle assembly machinery and kinetochore-microtubule attachments likely depends on its association in the mitotic RZZ complex (PubMed:18936247). The RZZ complex recruits the spindly-like protein spdl-1 to kinetochores (PubMed:18765790, PubMed:18936247). To prevent irregular chromosome segregation, the complex also inhibits the attachment of the kinetochore-associated NDC80 complex to microtubules (PubMed:24231804). The recruitment of spdl-1 to kinetochores relieves this inhibition (PubMed:24231804). Required for embryonic development (PubMed:9298984). SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore Cytoplasm, cytoskeleton, spindle Note=Localizes to the kinetochore during nuclear envelope breakdown and remains there until the metaphase-anaphase transition. Localization of the RZZ complex to kinetochores is dependent upon knl-1. SIMILARITY: Belongs to the ZW10 family."}
+{"protein": "MALISMKNVTLKKQGKILLNNLNWKVKKGENWVILGLNGSGKTTLLKLIMAEYWSTQGQVEILNTRFGQGDIPNMRTKIGVVGSFIAERLPANMLAEKIVLTGKYKSSILYKEYDETELNEARQMLTVIGGKHLLGRIYSSLSQGEKQLLLIARSLMEDPEIIILDEATSGLDLFAREKLLTQVEKITELPHAPTILYVTHHAEEITDKMSHILLLRRGKIVAQGPKKDIITPQVLENFYESPVNIISIDDKRFFIKPQV", "text": "SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MSKIWKFTSFATISSVAAASLYLYAIDKNGYYYEKSKFKQVTDRVRKLIDGDETFKYVTIDDFVSGPTQIQTRSRGETFKDLWNAEVRRTAQWIYSLGGR", "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; Single-pass membrane protein. SIMILARITY: Belongs to the MICOS complex subunit Mic12 family."}
+{"protein": "MNKNIIIKSIAALTILTSVTGVGTTVVEGIQQTAKAEHNVKLIKNTNVAPYNGVVSIGSGTGFIVGKNTIVTNKHVVAGMEIGAHIIAHPNGEYNNGGFYKVKKIVRYSGQEDIAILHVEDKAVHPKNRNFKDYTGILKIASEAKENERISIVGYPEPYINKFQMYESTGKVLSVKGNMIITDAFVEPGNSGSAVFNSKYEVVGVHFGGNGPGNKSTKGYGVYFSPEIKKFIADNTDK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1B family."}
+{"protein": "METRYNLKSPAVKRLMKEAAELKDPTDHYHAQPLEDNLFEWHFTVRGPPDSDFDGGVYHGRIVLPPEYPMKPPSIILLTANGRFEVGKKICLSISGHHPETWQPSWSIRTALLAIIGFMPTKGEGAIGSLDYTPEERRALAKKSQDFCCEGCGSAMKDVLLPLKSGSGSSQADQEAKELARQISFKAEVNSSGKTIAESDLNQCFSLNDSQDDLPTTFQGATASTSYGAQNPSGAPLPQPTQPAPKNTSMSPRQRRAQQQSQRRPSTSPDVLQGQPPRAHHTEHGGSAMLIIILTLALAALIFRRIYLANEYIFDFEL", "text": "FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) and is essential for cells to recover from ER stress. Plays a role in MAPKAPK2-dependent translational control of TNF-alpha synthesis. Acts also as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the E3 ubiquitin- protein ligase RNF26. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "AVXHPGTXVSXAAXXXFIPL", "text": "FUNCTION: Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily."}
+{"protein": "MLRRSLENRDAQTRQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINVYASTETPHLKQGLKNFADEFAKLQDYRQAEVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLTQLERTRQRNPSDRHVISQAETELQRATMDATRTTRHLEETIDNFEKQKIKDIKTIFSEFITIEMLFHGKALEVYTAAYQNIQKIDEEEDLEVFRHSLYPQDYSSRLDIVRANSKSPLQRSLSAKCVSGTGQVLTCRLRKDHQTEDDDEEDEDLDVTEEEN", "text": "FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling (By similarity). Probable regulator of ciliogenesis involved in limb morphogenesis. In cooperation with CBY1 it is involved in the recruitment and fusion of endosomal vesicles at distal appendages during early stages of ciliogenesis (By similarity). Plays an important role in the mitochondrial function and is essential for maintaining mitochondrial morphology and inner membrane ultrastructure (By similarity). In vitro, can generate membrane curvature through preferential interaction with negatively charged phospholipids such as phosphatidylinositol 4,5-bisphosphate and cardiolipin and hence orchestrate cristae shape (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, cilium basal body Cell projection, cilium Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=Weak punctate vesicular distribution throughout the cytoplasm. Localizes at the distal end of mother centrioles. Extensive colocalization with CBY1 at mother centrioles. SIMILARITY: Belongs to the CIBAR family."}
+{"protein": "MMLKTVIYTGVLFLICNKVLVRADPLYSPYSSKDLANLKTLLERFEDTLGQDEGNDNQQDYDIANPEAEGPQAGSPWDRERERQWPASDYKKPQEGYQSQSSRLRDLLMAPRNNRGSSGCFGSRIDRIGSMSSMGCGGSRKG", "text": "FUNCTION: Hormone playing a key role in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. Has a cGMP-stimulating activity (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family."}
+{"protein": "MASRRLALNLAQGVKARAGGVINPFRRGLATPHSGTGIKTQTTTLKNGLTVASQYSPYAQTSTVGMWIDAGSRAETDETNGTAHFLEHLAFKGTTKRTQQQLELEIENMGAHLNAYTSRENTVYFAKALNEDVPKCVDILQDILQNSKLEESAIERERDVILRESEEVEKQLEEVVFDHLHATAYQHQPLGRTILGPRENIRDITRTELVNYIKNNYTADRMVLVGAGGVPHEQLVEMADKYFSKLPATAPVSSASILSKKKPDFIGSDIRIRDDTIPTANIAIAVEGVSWSDDDYFTGLVTQAIVGNYDKALGNAPHQGSKLSGFVHKHDLATSFMSFSTSYSDTGLWGIYLVTDKLDRVDDLVHFSLREWTRLCSNVSEAEVERAKAQLKASILLSLDGTTAVAEDIGRQIVTTGRRMSPAEIERIIDAVSAKDVMDFANKKIWDQDIAISAVGSIEGLFDYARIRGDMSRNAF", "text": "FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:2967109). Preferentially, cleaves after an arginine at position P2 (PubMed:8106471). 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 matrix Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the peptidase M16 family."}
+{"protein": "MGGGNSKEESSSPSSSSWASHQSYPQYGPDSYNYPPPPTYAPAPSPAPAPAPVPAPSPASSYGPQYSQEGYASQPNNPPPPTYAPAPSPASSYGHQYSQEGYASAASQPNYPPPPSQSQVADRKKFDRRYSKISDNYSSLLQVSEALGRAGLESSNLIVGIDFTKSNEWTGAKSFNRKSLHHLSNTPNPYEQAITIIGRTLAAFDEDNLIPCYGFGDASTHDQDVFSFYPEGRFCNGFEEVLARYREIVPQLKLAGPTSFAPIIEMAMTVVEQSSGQYHVLVIIADGQVTRSVDTEHGRLSPQEQKTVDAIVKASTLPLSIVLVGVGDGPWDMMQEFDDNIPARAFDNFQFVNFTEIMSKNKDQSRKETEFALSALMEIPPQYKATIELNLLGVRNGNIPQRIPLPPPVQSGSSFSSSRIPNFEPSVPPYPFESKQMSSADDIQLCPICLSNPKNMAFGCGHQTCCECGPDLKVCPICRAPIQTRIKLY", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates the formation of 'Lys-63'-linked ubiquitin chains. Regulates apical dominance by acting on the auxin transport proteins abundance (PubMed:17586653). Together with RGLG5, mediates the ubiquitination and subsequent proteasomal degradation of the target protein PP2CA. Functions as positive regulator of abscisic acid (ABA) signaling through ABA-dependent degradation of PP2CA, a major inhibitor of ABA signaling (PubMed:27577789). Acts as a negative regulator of drought stress response (PubMed:22095047). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Nucleus."}
+{"protein": "MGTERKRKISLFDVMDDPSAPAKNAKTSGLPDGGINSLINKWNGKPYSQRYYDILEKRRTLPVWLQKEEFLKTLNNNQTLILVGETGSGKTTQIPQFVIDAVDAETSDKRRKWLVGCTQPRRVAAMSVSRRVAEEMDVTIGEEVGYSIRFEDCSSPRTVLKYLTDGMLLREAMADPLLERYKVIILDEAHERTLATDVLFGLLKEVLKNRPDLKLVVMSATLEAEKFQDYFSGAPLMKVPGRLHPVEIFYTQEPERDYLEAAIRTVVQIHMCEPPGDILVFLTGEEEIEDACRKINKEVGNLGDQVGPIKVVPLYSTLPPAMQQKIFDPAPEPVTEGGPPGRKIVVSTNIAETSLTIDGIVYVIDPGFAKQKVYNPRIRVESLLVSPISKASAHQRSGRAGRTRPGKCFRLYTEKSFNNDLQPQTYPEILRSNLANTVLTLKKLGIDDLVHFDFMDPPAPETLMRALEVLNYLGALDDDGNLTKTGEIMSEFPLDPQMAKMLIVSPEFNCSNEILSVSAMLSVPNCFIRPREAQKAADEAKARFGHIEGDHLTLLNVYHAFKQNNEDPNWCYENFINNRAMKSADNVRQQLVRIMSRFNLKMCSTDFNSRDYYINIRKAMLAGYFMQVAHLERTGHYLTVKDNQVVHLHPSNCLDHKPEWVIYNEYVLTSRNFIRTVTDIRGEWLVDVASHYYDLSNFPNCEAKRVIEKLYKKREREKEESKKNRK", "text": "FUNCTION: May be involved in pre-mRNA splicing. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. PRP43 sub-subfamily."}
+{"protein": "MESTTAFSAVTSALGTLDVHIMAPYLWMLVLGFVIAFVLAFSVGANDVANSFGTAVGSGVVTLRQACILASIFETVGSVLLGAKVSETIRKGLIDVTMYNSTQELLMAGSISAMFGSAVWQLAASFMKLPISGTHCIVGATIGFSLVAKGQQGVKWIELLRIVLSWFISPLLSGIMSALLFLFVRMFILRKADPVPNGLRALPVFYACTIGINLFSIMFTGAPLLGFDKVPLWGIILISVGCAVLCALIVWFVVCPRMKRKIECEFKSSPSESPLMDKKNQELRCPILKPDPEDLKLPVDGGIVAEVKVPILDMVSVSRTEERTVTFKMGECDDPIEKEKLNSMETNIDQPTNGSVQLPNGNHVQFSQAVSNQMNSSGQYQYHTVHKDSGLYKDLLHKLHLAKMGDCMGDSGDKPLRRNNSYTSYTMAICGMPLDSLRNRDTEARPDEAEKSTVHGADGKKRIRMDSYTSYCNAVADTHMDVEAEEQEEGSVEDVETDRKSSSSSLEERHDQDKPEVSLLFQFLQILTACFGSFAHGGNDVSNAIGPLVALYLVYETGDVTTKAATPIWLLLYGGIGICIGLWVWGRRVIQTMGKDLTPITPSSGFSIELASALTVVIASNVGLPISTTHCKVGSVVSVGWLRSKKAVDWRLFRNIFLAWFVTVPISGLISAGIMALFKYAILKV", "text": "FUNCTION: Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family."}
+{"protein": "MKRIQIIDSHTGGEPTRLVVSGFPSLGDGTMAERRDVLAREHDRYRTACILEPRGSDVLVGALLCDPVAPDAAAGVIFFNNSGYLGMCGHGTIGVVRTLHHMGRIAPGVHRIETPVGTVEATLHDDLSVSVRNVPAYRHAQGVALDVPGYGPVKGDIAWGGNWFFLISDHGQRVAGDNVAALTAYASAVREGLERAGITGANGGEIDHIELFADDPEHDSRSFVLCPGLAYDRSPCGTGTSAKLACLAADGKLAPGAVWRQASVIGSVFHASYERADGGIVPTIRGSAHLSAEATLLIEEDDPFGWGIGS", "text": "FUNCTION: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Displays no proline racemase activity. SIMILARITY: Belongs to the proline racemase family."}
+{"protein": "MSKAKSPIKSSKKSVNQPKSVLREKKVKDAEKAEHISLQGHVDNSDEEGQDKEFFPGFGSSDDDEEDSPNALVNTSRQIMDLGEDAEKTIKKKVSENKNLQKKKGVLYVGRLPHGFYEKQMRMYFSQFGPVLRLRMSRNRKTGSSKHYAFIEFESLDVANVVAETMHNYLLYGKLLQCKVIPEDQVHENMFKGADVPFKRIPHATIARLQHEKPLSKEKADKLITRHNRKLKLKKRKLKELGITLESDVSHPKAASPVASKKSSKKKNKKVLAAHK", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus."}
+{"protein": "MFKKGLLALALVFSLPVFAAEHWIDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKVYCNAGRQSGQAKEILSEMGYTHVENAGGLKDIAMPKVKG", "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. PspE catalyzes the sulfur-transfer reaction from thiosulfate to cyanide, to form sulfite and thiocyanate. Also able to use dithiol (dithiothreitol) as an alternate sulfur acceptor. Also possesses a very low mercaptopyruvate sulfurtransferase activity. SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MIVLFVDFDYFFAQVEEILNPSLKGKPVVVCVYSGRTKDSGAVATSNYEARKLGIKAGMPIIKAKEIGKDAVFLPMRKEVYQQVSRRVMNIISGYGDKLEIASIDEAYLDITRRVKDFDEAKELARKLKAEVLEKERLRVTVGIGPNKVVAKIIADMNKPDGLGIIYPEEVKDFLYNLDISKVPGVGKITEEILRKVGINRLGDVINKSGELVNLVGKSKANYLLSLANNTYHDPVESREITHRGRYVTLPENTRDLNRILPSLKRSIEEAYSKVDGIPMEIYVVAIMEDLDIVSKGKSFKFGVSQDRALSVAQELLNKILESDKRKLRRVGVRLGKITKSSTLEDFLH", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DNA polymerase type-Y family."}
+{"protein": "MTYEGAIGIDLGTTYSCVGVWQNERVEIIANDQGNRTTPSYVAFVNNEVLVGDAAKSHAARGSNGVIFDAKRLIGRKFSDSVVQSDMKHWPFKVEEGEKGGAVMRVEHLGEGMLLQPEQISARVLAYLKSCAESYLGKQVAKAVVTVPAYFNDSQRQATKDAGTIAGLEVLRIINEPTAAAIAYGLDKADEGKERNVLVFDFGGGTFDVSIISVSGGVFEVKATNGDTHLGGEDVDAALLEHALADIRNRYGIEQGSLSQKMLSKLRSRCEEVKRVLSHSTVGEIALDGLLPDGEEYVLKLTRARLEELCTKIFARCLSVVQRALKDASMKVEDIEDVVLVGGSSRIPAVQAQLRELFRGKQLCSSVHPDEAVAYGAAWQAHVLSGGYGESSRTAGIVLLDVVPLSIGVEVDDGKFDVIIRRNTTIPYLATKEYSTVDDNQSEVEIQVFEGERPLTRHNHRLGSFVLDGITPAKHGEPTITVTFSVDADGILTVTAAEELGSVTKTLVVENSERLTSEEVQKMIEVAQKFALTDATALARMEATERLTQWFDRLEAVMETVPQPYSEKLQKRIAFLPHGKEWVGTQLHTYTDAASIEAKVAKIERLAKRALKSARREGKDGWAPGNEDNGSGDDNDGDDNSDEEDELQRGRGVTEGSGRSPIRKRDRIEAINANTE", "text": "SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MENKETFAFNADIQQLMSLIINTFYSNKEIFLRELISNASDALDKIRYEAITEPEKLKTKPELFIRLIPDKANNTLTIENSGIGMTKADLVNNLGTIARSGTKAFMEALQAGGDISMIGQFGVGFYSAYLVADSVTVVSKHNDDEQYVWESAAGGSFTVQKDDKYEPLGRGTRIILHLKEDQGEYLEERRLKDLVKKHSEFISFPIELAVEKTHEREVTESEDEEEKKADEKAEEKEGEEKKEGEEKKEGEEEKKEKTGKTKKVQEVTREWEQLNKQKPLWMRKPEEVTEEEYASFYKSLSNDWEEHLAVKHFSVEGQLEFKALLFVPKRAPFDLFETRKKRNNIKLYVRRVFIMDDCEDIIPEWLNFVKGVVDSEDLPLNISRESLQQNKILKVIRKNLVKKCLEMFAEIEEKKENYAKFYEQFSKNLKLGIHEDSANRAKIAELLRFHSSKSGEDMVSFKEYVDRMKEGQKDIYYITGESRQTVANSPFLEKLTKKGYEVLYMTDPIDEYAVQQLKEFDNHKLRCCTKEGLEIDESEEEKKKFEELKAEFEPLLKLIKEVLHDKVDKVVLSNRITDSPCVLVTTEFGWSANMERIMKAQALRDNSMTSYMVSKKTMEVNGHHSIMIEIKNKAAVDKSDKTVKDLIWLLYDTALLTSGFSLEEPTQFAARIHRMIKLGLSIDDDEEAKDDDLPPLEEVEGAADEASKMEEVD", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family."}
+{"protein": "MNIRPSQIKHKQRIASFITHAVVVVMGVLIVSVLFQSYQISSRLMAQEGQRTSVQTSSLIQSLFDFRLAALRIHQDSTAKNASLINALVSRDSSRLDEFFSSVDELELSNAPDLRFISSHDNILWDDGNASFYGIAQQELNKLIRRVAISGNWHLVQTPSEGKSVHILMRRSSLIEAGTGQVVGYLYVGIVLNDNFALLENIRSGSNSENLVLAVDTTPLVSTLKGNEPYSLDYVVHSAKDAMRDSFIVGQTFLEVESVPTYLCVYSIQTNQNVLTLRDNFYFWMAFALISMIGVSIASRWWLQKRIQREIETLMNYTHKLMDLDTKSEFIGSKIYEFDYFGRTLEQSFRRLANKEKQFEDLFNFALSPTMLWNTSGRLIRMNPSAQIQFLREDAQNHFLFEILERQLLPTITNAAQGNNPSDVTTEVDGRVYRWNLSPIMVEGQIISIITQGQDITTIAEAEKQSQAARREAEESARVRAEFLAKMSHELRTPLNGVLGVSQLLKRTPLNDEQREHVAVLCSSGEHLLAVLNDILDFSRLEQGKFRIQKNEFRLKELVCAIDRIYRPLCNEKGLELVVNSNITTAAIVRSDQIRINQILFNLLNNAIKFTHQGSIRVELQLIEGDPLAQLVIQVVDTGIGIREQDLTVIFEPFMQAESTTTREYGGSGLGLTIVHSLVEMLSGQLHVSSEYGIGTRFEIQLPIELVEKPDAPQQLLPAPDPQPLFDKTLRVLLVEDNHTNAFIAQAFCRKYGLDVSWVTDGLQAIEELKIHDYDLVLMDNQLPYLDGVETTRTIKKVLHLPVVVYACTADGLEETRQAFFHAGAEYVLVKPLKEQTLHKALEHFKHHHGQKNAGLN", "text": "FUNCTION: At low cell density, in absence of AI-2 (autoinducer 2), LuxQ has a kinase activity and autophosphorylates on a histidine residue. The phosphoryl group is then transferred to an aspartate residue in the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cell density, in the presence of AI-2, the kinase activity is inactivated, and the response regulator domain has a phosphatase activity (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MIGKNIKSLRKTHDLTQLEFARIVGISRNSLSRYENGTSSVSTELIDIICQKFNVSYVDIVGEDKMLNPVEDYELTLKIEIVKERGANLLSRLYRYQDSQGISIDDESNPWILMSDDLSDLIHTNIYLVETFDEIERYSGYLDGIERMLEISEKRMVA", "text": "FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli neutralizes the toxic effect of cognate toxin PezT. Represses transcription of its own operon, PezT acts as a corepressor, considerably increasing repression."}
+{"protein": "MDYYSLKMRASQHVGEGENSHEQHISGAERIVGRDSVEAVCAAMVRRAMNHSKGDPDFINVKIEKVHESDIQVLKSLPVTRVDVETWQEGLEKAFGLITPLMALRQAQGPCDGAKKFKEKLQDLLRETFPMRGAMLYDIATGNRLEPDKDRGVRATYMDALHSSEVDGCKNHFNEAIVLATKVANAPGMVAEFCVSDDPNYVTGYVASKELGYVRIMKMKEMGDENGGRIFLFDSRKASAEECIEYLQKKKVLVDVVGRT", "text": "FUNCTION: Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP. SIMILARITY: Belongs to the BioW family."}
+{"protein": "MASTLPTTWPHESVKFEDVSLTFTEEEWAQLDFQQKCLYREIMMENYSNMISVEHHFSKPNVISQLEKAEDCWPMQREIPQDTLPECSWPSPDPGMNSFPSKSPLMKIEVVEVLTLNKDVAGPRNALIQSLYPEDLNPGNLKPAQQPSKRLTDTEASRQKFRHFQYEESAGPQKAMSQLRKLCHQWLQPNTRSKKQILELLVLEQFLNALPEKFRVWVESQHPEDCKAVVALLENMTSVSKDDASLACSSEATDQLKEKRKGVATLPVTFAAEVPAEEPVTFQDVAVDFNEEEWRLLGPTQKTEYHDVMLETLGNLVSVGWEPTLGNRELTPDSPIPVVKPIHDPNTNDLSRNGTQSTVFESILEDGVKEMHSIESNQVGNLQEKGHPQKKFSESSKSQDQTSRHKSQGSLNEVLPRKYVKVKQKGTGKRKGRTNTISMTRGLRIRKQQKDSVEWQGRSGSTPVTHGSSIKKQQQGSEQGKPGTSRDPITLTVPAKVYQKATGSEESIFMDSSDAMVPDVPPKIHQKGPEWHKVGESNNSMLQGSSVQNHQMESGAGRASDNSLLTHALPVKSHQKGYKEGNVQGNRNSWKHIKPHQKGSKGERVEELSTSEKHVPYVKNHLKTSERGKDREINASIKCDPYIKTYYRGSDVGRLRRANNCRKAFSLHAQQISFIKIHKGSQVCRCSECGKLFRNARYFSVHKKIHTGERPYMCMACGKAFVQSSSLTQHLRIHSGERPFECSECGRTFNDRSAISQHLRTHTGAKPYHCERCGKAFRQSSHLTRHERTHTGERPYVCIKCGKAFTQSSHLIGHQKTHGIKFKKQPKL", "text": "FUNCTION: Transcription regulator involved in NGFR/p75(NTR)-mediated apoptosis. Essential component of the NGFR/p75(NTR) apoptotic pathway: upon ligand-binding and subsequent cleavage of NGFR/p75(NTR), binds to the intracellular domain (ICD) cleavage product of NGFR/p75(NTR), translocates to the nucleus and induces apoptosis, possibly by regulating expression of key regulators of apoptosis. Induces NGFR/p75(NTR)-mediated apoptosis in retina and sympathetic neurons. May also regulate expression of neuronal cholesterol biosynthesis genes. Probably acts as a transcription repressor: specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin-modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates into the nucleus following binding to TRAF6 and subsequent ubiquitination at Lys-15. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "RIQAYRFRTRVPPSPAASGSPRSTRRDVAVQAKGSWLPGLQSPAYLDGSLEGDNGFDPLALAEDPEDLRWFVQADVVNGRWAMLGVAGMLIPEVLTKAGLMNAPEWLRLPGKETYFASSSTALRVHMSSTYVEIRRWQDIKNPGSVNQDPIFKSYSLPPHECGYPGRVFNPLNFAPLENKEKELANGRLAMLAFLGFLVQHNVHGKGPFENLQQHLADPWHNTIIQTISGQ", "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; Single-pass membrane protein. SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family."}
+{"protein": "MPRVKAVKKQAEALASEPTDPTPNANGNGVDENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAAKRARGTKRLADSEIAAALDEPEVDEVPPKAASKRAKKGKMVEPSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAKPTKQRAKKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETKPAKGRKKAPVKAEDVEDIEEAAEESKPARGRKKAAAKAEEPDVDEESGSKTTKKAKKAETKTTVTLDKDAFALPADKEFNLKICSWNVAGLRAWLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMPGGYAGVAIYSKIMPIHVEYGIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRKLVNLEPRMRWEKLFQAYVKKLDALKPVVICGDMNVSHMPIDLENPKNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDRKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRSQCLGSDHCPITIFFNI", "text": "FUNCTION: Plays a role in the cellular response to oxidative stress by promoting DNA repair mechanisms such as base excision repair and possibly homologous recombination repair (PubMed:1713691, PubMed:16507570). Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents (PubMed:16507570). Likely to initiate 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). Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER (PubMed:16507570). Has apurinic endonuclease and double-stranded DNA 3'-exonuclease activities and carries out single-stranded DNA renaturation in a Mg(2+)-dependent manner (PubMed:1713691, PubMed:8918793). Activity is more efficient in purine-rich regions of dsDNA than in pyrimidine-rich regions (PubMed:8918793). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family."}
+{"protein": "MSRKSYPNVNAANQYARDVVRGKIVACQFVIQACQRHLDDLMAEKSKSFRYRFDKDLAERVAKFIQLLPHTKGEWAFKRMPITLEPWQLFVICCAFGWVNKGSRLRRFREVYTEIPRKNGKSAISAGVALYCFACDNEFGAEVYSGATTEKQAWEVFRPARLMCKRTPMLTEAFGIEVNASNMNRPEDGARFEPLIGNPGDGSSPHCAVVDEYHEHATDALYTTMLTGMGARRQPLMWAITTAGYNIEGPCYDKRREVIEMLNGSVPNDELFGIIYTVDEGDDWTDPQVLEKANPNIGVSVYREFLLSQQQRAKNNARLANVFKTKHLNIWVSARSAYFNLVSWQSCEDKSLTLEQFEGQPCILAFDLARKLDMNSMARLYTREIDGKTHYYSVAPRFWVPYDTVYSVEKNEDRRTAERFQKWVEMGVLTVTDGAEVDYRYILEEAKAANKISPVSESPIDPFGATGLSHDLADEDLNPVTIVQNFANMSDPMKELEAAIESGRFHHDGNPIMTWCIGNVVGKNMPGNDDLVKPVKEQAENKIDGAVALIMTIGRAMLKEPDDFLSSLDPDDDLLIL", "text": "SIMILARITY: Belongs to the phage terminase family."}
+{"protein": "MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAASLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPLLRPDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLSYLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPRNLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRKGSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETGKGQAPGPSRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM", "text": "FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (PubMed:17290220, PubMed:19917254, PubMed:19838211). Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (PubMed:17290220, PubMed:19838211). Has no deubiquitinase activity against p53/TP53 (PubMed:17290220). Prevents MDM2-mediated degradation of MDM4 (PubMed:17290220). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (PubMed:19917254). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (By similarity). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (By similarity). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and BMAL1 (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity). FUNCTION: [Isoform 4]: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein NHERF4 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine. SUBCELLULAR LOCATION: [Isoform 4]: Nucleus Membrane; Peripheral membrane protein Cytoplasm Note=Predominantly expressed at membranes. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. SIMILARITY: Belongs to the peptidase C19 family. USP2 subfamily."}
+{"protein": "MAEPHQEFDVTEDHAGTYGLGDRKDQGGYTMLQDQEGDTDAGLKESPLQTPAEDGSEEPGSETSDAKSTPTAEDVTAPLVDERAPGEQAAAQPHMEIPXGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVREGFLGEPGPPGLSHQLVSGMPGAPLLPEGPREATRQPSGIGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKVSPAQDGWPPQAAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDRPSAGGAEGQDAPPEFTFHVEITPNVQKEQAHSEEHLRRAAFPGAPGEGPEAQGPSLGEDAKEADLPEPSEKQPAAAPRGKPISRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTPRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGHKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL", "text": "FUNCTION: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton Cell projection, axon Cell projection, dendrite Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components."}
+{"protein": "MKKSIFSKKLLVSFGSLVTLAAIPLIAISCGQTTDNLSQSQQPGSGTGSGSGTNTENGSNNGSGSGTTNSSGGTNQSGSASGNGSSNSSVSTPDGQHSNPSNPTTSDPKESNPSNPTTSDPKESNPSNPTTSDGQHSNPSNPTTSDPKESNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQNQNK", "text": "FUNCTION: Responsible for the antigenic diversity for host adaptation. Expression in E.coli of a construct containing vlpD, vlpE, and vlpF yields antigenically distinguishable products corresponding to each gene. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
+{"protein": "MAGQRAPHLHLAELSASQFLDVWRHFDADGNGYIEGKELENFFQELESARKGTGVDSKRDSLGDKMKEFMHKYDKNADGKIEMAELAQILPTEENFLLCFRQHVGSSSEFMEAWRRYDTDRSGYIEANELKGFLSDLLKKANRPYDEAKLQEYTQTILRMFDMNGDGKLGLSEMSRLLPVQENFLLKFQGMKLSSEEFNAIFAFYDKDGSGFIDEHELDALLKDLYEKNKKEMSIQQLTNYRRSIMNLSDGGKLYRKELEVVLCSEPPL", "text": "FUNCTION: Calretinin is a calcium-binding protein which is abundant in auditory neurons. SIMILARITY: Belongs to the calbindin family."}
+{"protein": "MAGRWNLEGCTALVTGGSRGIGYGIVEELANLGASVYTCSRNQKELDECLTQWRSKGFNVEASVCDLSSRSEREEFMKTVSNHFHGKLNILVNNAGIVIYKEAKDYTMEDYSHIMSINFEAAYHLSVLAHPFLKASERGNVVFISSISGASALPYEAVYGATKGAMDQLTRCLAFEWAKDNIRVNGVGPGVIATSMVEMTIQDPEQKENLDKLIDRCALRRMGEPKELAAVVAFLCFPAASYVTGQIIYVDGGFMANGGF", "text": "FUNCTION: Catalyzes the stereospecific reduction of tropinone to pseudotropine. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MTKTEKKSFHQSLAEWKLFIYNPTSGEFLGRTSKSWGLILLFYLVFYGFLAALFTFTMWVMLQTLNDEVPKYRDQIPSPGLMVFPKPPTALDYTYSMSDPHTYKKFVEDLKNFLKPYSVEEQKNLTDCPGGALFHQEGPDYSACQFPVSLLQECSGVNDSNFGYSKGQPCVLVKMNRIIELVPDGAPYITCITKEENIANIVTYPDDGLIDLKYFPYYGKKRHVGYRQPLVAVQVIFGADATKKEVTIECQIDGTRNLKNKNERDKFLGRVSFKVIAHA", "text": "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 exact function of the beta-3 subunit is not known. SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein Basolateral cell membrane; Single-pass type II membrane protein Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family."}
+{"protein": "MAAVDLDVQSLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRATRKAQGLRSVFVSGFPRDVDSAQLTQYFQAFGPVASVVMDKDKGVFAIVEMGDVGTREAVLSQPQHTLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLTKALAEAPDVGAQMVKLVGLRELSEAERQLRNLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEESQPAPKAPESPSLDSALASPLDPQALACTPASPPDSQPPSPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLQEDRGEGDLGKALELAEALSGEKTEGVAMLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLSNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEGEQVEVDGWDCSFPRDASGLEPSTNKEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALPVAGDLPSNRWEGLRLGPMNLQDPFDLSHNVAANVTSRVAGRLQNSCQAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSLLSATPIPLPPAPFTQLTAALAQVLREALGCHIEQGTKRLRSDRGGPEESPQGGTSKRLKLDGEEKSCEEGREEQQGYIRDHSEDGVEEMVVEVGEMVQDWVQSPGRPGEPPQMLREQLATGEEGQSGHAALAEQGPKGPEAAREGSQGETGRGVSLSSVSWRCALWHRVWQGRRRARRRLQQQTKERGRGSAGTAEWLAVEAQVTRELRGLSSAAQRPEAEPLLTFVASASQVNQTLTVTPIQDSQGLFPDLHHFLQVFLPQALRNL", "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": "MLSRSIGKAAGGLVLGLSVAAAAHAAPLFEPVTVISRASANSEPALGKLLATPSTATVQEVRVDAAATAQPQLEFELLGKRVQAVRSKVEALPDGGSIWYGQFRSPSDRLTAATSSGQDDPGNSLILVRSGDTITGSIRKDGKLYRLRPLGNRHVLVEVDESRMPADHPADYNQLPKIPMADNDHIGIAQASSGTPATIRVLVVATNAAVTAYGGNMQSLVQLAVAESNQGYVNSNVGLTLQLAGYETTNYSESGNFTTDLSRFRGTSDGYMDSIHTSRNTTAADVGVLLINNSAYCGLASGIGSTASTAFAAVYWDCATGYYSFAHEIGHLQSARHDIATDSSTSPYAYGHGYRYEPATGTGWRTIMAYNCTRSCPRLNYWSNPNISYNGIPMGNASTADNQRVLVNTKATIAAFR", "text": "FUNCTION: Metalloprotease, specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues. SIMILARITY: Belongs to the peptidase M72 family."}
+{"protein": "MASKSDKQVTVEVNNTGRGRSKSRARSQSRGRGRSVKITVNSQNKGRRQNGRNKRQSNQRVRNIVNKQLRKQGVTGPKPAICQKATATLGTIGSNTSGTTEIEACILLNPVLVEDATGSTQFGPVQALGAQYSMWKLKYLNVRLTSMVGASAVNGTVVRVSLNPTSTPSSTSWSGLGARKHLDVTVGKNAIFKLKPSDLGGPRDGWWLTNTNDNASDTLGPSVEIHTLGRTMSSYQNQQFTGGLFLVELASEWCFTGYAANPNLVNLVKSTDKQVNVTFEGSAGTPLVMNVPAASHFARTVAQRSTLPTSMARAGENTASDTVWQVLNTAVSAAELVTPPPFNWLVKGGWWFVKLIAGRVRNGNRSFYVYASYQDALSNKPALCTGSTSGSMRTRPAVMTTLQFTQMNQPSLGHGETPATLGRSIPTSGETLKVLLTVGNPISPNETNKQTWVNKTIEPPGAVVRIGRDTQHYCTLNGFTLITKVDWFTEEFQPSEEPAPVQGLMVLGDNHKKADVYAAQQYKNPITNDKQEVTSVFLVRVNEGFQVTNHLSYFYRNSVNTDAVENIKIRSATRHTTVRFYQGSWYLLTSTVLHTGPPVSGWLWMNQELQNDQAYIIDQGIMHLITPPPVSSQIYFEMATLVPQTRSGGGETGLELVMGLSDDEYPISHVNDEEETEYETESDEDETDEVDRFDLCCTSDSEDDIENNRVTLLSTLINQGVTVDRATMITNRAFPTPNYKPRREPSNDLLAPSDCLATARSHACNETCQLSGSRGHAE", "text": "FUNCTION: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the VP70 virions. This immature virion is composed of 180 VP70 subunits with 90 dimeric spikes and displays a T=3 icosahedral symmetry. The mature virion is obtained by further cleavages resulting in three structural proteins VP25, VP27 and VP34. This forms contains only 30 spikes located on the icosahedral 2-fold axes. Plays a role in the attachment to target host cell. This attachment induces virion internalization through clathrin-dependent endocytosis (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the astroviridae capsid polyprotein family."}
+{"protein": "MGKPRQNPSTLVSTLCEAEPKGKLWVNGYAGTQGTRDATLQTRLIPLSFHLQRGKGLAAPLSALSAPRLPERPADGRVAVDAQPAARSMDSDSGEQSEGEPVTAAGPDVFSSKSLALQAQKKILSKIASKTVANMLIDDTSSEIFDELYKVTKEHTHNKKEAHKIMKDLIKVAIKIGILYRNNQFSQEELVIVEKFRKKLNQTAMTIVSFYEVEYTFDRNVLSNLLHECKDLVHELVQRHLTPRTHGRINHVFNHFADVEFLSTLYSLDGDCRPNLKRICEGINKLLDEKVL", "text": "FUNCTION: Acts as a lipid transfer protein. Preferentially captures and shuttles two lipid second messengers, i.e., phosphatidylinositol 4,5- bisphosphate and phosphatidylinositol 3,4,5-trisphosphate and increases their levels in the plasma membrane. Additionally, may also function as a lipid-presenting protein to enhance the activity of the PI3K-AKT and MEK-ERK pathways. May act as a regulator of tumorigenesis through its activation of phospholipid signaling. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=On PDGF activation, translocates from cytoplasm to plasma membrane. SIMILARITY: Belongs to the TNFAIP8 family."}
+{"protein": "MRVAIVGAGLAGLATAIDLADAGCEVQIFESRPFVGGKVGSWIDGDGNHVEMGLHVFFGCYYQLFELMNKVGAFSHLRLKEHTHTFVNKGGRTGALDFRFFTGAPFNGLKAFFTTSQLSLQDKLQNAIALGTSPIVRGLVDFEGAMKTIRNLDKISFADWFRSHGGSNGSIKRMWNPIAYALGFIDCENISARCMLTIFQFFAVRSEASVLRMLEGSPDEYLHQPILRYLEARGTKVYTRRQVREIKYAEAEGQTRVTGIVVAKGDEVEEITADAYVCACDIPGIQRVLPQEWRKWSEFDNIYKLDAVPVATVQMRFDGWVTELQDENKRKQLKEAAGLDNLLYTADADFSCFADLALTSPSDYYRQGQGSLLQLVLTPGDPFIKESNEAIAQHVLKQVYELFPSSRELNMTWYSVVKLAQSLYREAPGMDVYRPNQKTPIANFFLAGSYTQQDYIDSMEGATVSGRRAAKVILDNIKK", "text": "FUNCTION: Catalyzes the conversion of zeta-carotene to lycopene via the intermediary of neurosporene. It carries out two consecutive desaturations (introduction of double bonds) at positions C-7 and C-7' (By similarity). SIMILARITY: Belongs to the zeta carotene desaturase family."}
+{"protein": "MKPKIFIDGEHGTTGLQIRALLAERGDLEIISIPTERRKETAARAEFLNAADIAILCLPDDAAKESVSLITNDTTKVIDASTAHRVAEGWAYGFAEMDKEQAKAIATAKRVANPGCWPQGPIATLRPLVTSGLLPADFPITVNGISGYSGGGRPMIEDYVAKGEDASEFLPYGLTLQHKHVPELRAYAKLSHDPIMQPAVGNFAQGMITVVPLQLGGLDSVPTGAELHAAIADHFAAIKGGVVEVAPYAHLERMPEIDPEIYNGTNRMKVYVFANDKRAQALLLAVYDNLGKGASGAAVQNMDLMLGL", "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": "MGMSSLKLLKYVLFIFNLLFWVCGCCILGFGIYFLVQNTYGVLFRNLPFLTLGNILVIVGSIIMVVAFLGCMGSIKENKCLLMSFFVLLLIILLAEVTIAILLFVYEQKLNTLVAEGLNDSIQHYHSDNSTMKAWDFIQTQLQCCGVNGSSDWTSGPPSSCPSGADVQGCYNKAKSWFHSNFLYIGIITICVCVIQVLGMSFALTLNCQIDKTSQALGL", "text": "FUNCTION: Required for efficient formation of myofibers in regenerating muscle at the level of cell fusion. May be involved in growth regulation in hematopoietic cells. SUBCELLULAR LOCATION: Cell membrane Cell junction Membrane; Multi-pass membrane protein Note=Concentrates in localized microdomains along the plasma membrane at the contact sites between cells of fused myotubes. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MSEGSEDTKTKLDSAGELSDVDNENCSSSGSGGGSSSGDTKRTCVDCGTIRTPLWRGGPAGPKSLCNACGIKSRKKRQAALGMRSEEKKKNRKSNCNNDLNLDHRNAKKYKINIVDDGKIDIDDDPKICNNKRSSSSSSNKGVSKFLDLGFKVPVMKRSAVEKKRLWRKLGEEERAAVLLMALSCSSVYA", "text": "FUNCTION: Transcriptional regulator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the type IV zinc-finger family. Class B subfamily."}
+{"protein": "MIRTLIALVPADKRGTLGLYTVLTVLSVVIRAAGTVLLVPLVAALFGDTPQDAWPWLGWLTAATAAGWIVDTTTSRLGFDLGFAVLDHTQHDVADRMPNIRLDWLTAENTATARAAIASTGPELVGLVVNLLTPLIGAVLLPAAIAVALVAVSPPLGLAALAGVVVLLGAMWASNRLSRKADTVADETNSAFTERIIEFARTQQALRAARRVEPARSLVGDALGAQHGAGVRLLAMQIPGQLLFSLASQLALILLAGMATWLTVRGELSVPEAVAMIVVVARYLEPFTSLSELTPAIESTRGTLGRIRAVLDAPTLTAGDAAPADTKSAPRIEFDCVTFGYGDHPVLDDVSFVLEPGSTTAIVGPSGSGKSTILSLIAGLHQPTEGRVLIDGVDAASLDDESRRAATSVVFQQPYLFDGSIRDNILVGDPGADEDRLAAAVRLARVDELTARLPNGDASKVGEAGAALSGGERQRVSIARALVKPAPVLLVDEATSALDTENEAAVVDALTADLRHRTRVIVAHRLASIRHADRVLFLDGGRIVEDGTIDGLLAAGGRFDEFWRRQHEAADWQITH", "text": "FUNCTION: Part of the ABC transporter complex IrtAB involved in the import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe- cMBT) (PubMed:32296173). Has a preference for Fe-MBT over Fe-cMBT (PubMed:32296173). Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (PubMed:32296173). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Siderophore- Fe(3+) uptake transporter (SIUT) (TC 3.A.1.21) family."}
+{"protein": "MNSHFASAHTPFYINTKEGRYLVLKAVKVCDVRTVEFEGSKASCVLKVDKPSSPASERRPSSPSRCERMNNPGKQVPFMRTDMLQNMFAANRDNVASRLLS", "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": "MTLIDLANPTRFLALTARVLPWLAAATVILLAIGLYQSALAPDDYQQGATVKIMFIHVPNAWLSMFVWGVMSIASLGTLVWRHPLADVAAKAAAPIGAAFTFLALLTGSLWGRPMWGTYWEWDARLTSVLILFLMYLGLMALWRAVDDPSRAARAAAVLTLVGAINLPIIKFSVDWWNTLHQPASVMRMGGSSLDKSFLIPLLVMAIAFTLLFVTLHLAAMRNEILRRRVRSLQMMQASRMAFSSEMGAGSRQNNASNEVGAA", "text": "FUNCTION: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CcmC/CycZ/HelC family."}
+{"protein": "MKVELCSFSGYKIYPGHGRRYARIDGKVFQFLNAKCESAFLAKRNPRQINWTVLYRRKHKKGQSEEVTKKRTRRAVKFQRAITGASLAEIMAKRNQKPEVRKAQREQAIRAAKESKKAKQATKKPAAASAKTSAKTAQKPKIAKPMKISAPRVGGKR", "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": "MGNPKSNQQPFVPQHIGTKPREAGGNKGKQMQDQSGQHPQVIQTKGE", "text": "SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspN family."}
+{"protein": "MSEFRSGFVCFVGRPNTGKSTLTNALVGTKVAITSNRPQTTRHTIRGIVHRDEFQIILVDTPGLHRPRTLLGQRLNDLVKTTYSEVDVIGLCIPADEAIGPGDRWIHEQIRAVAPRTTLVVIVTKIDKVPKDRVAAQLMAVSELIGPDAEIVPVSATTGEQLDVLTDVLAGKLPPGPAFYPDGELTDEPEETLMAELIREAALEGVRDELPHSLAVVIDEVSPREDRDDLIDVHAILYVERDSQKGIVIGKGGARLREVGTAARLQIEKLLGTKVYLDLRVKIAKNWQRDPKQLGRLGF", "text": "FUNCTION: Exhibits GTPase activity. Binds RNA but is probably not involved in ribosome assembly in mycobacteria. SUBCELLULAR LOCATION: Cell envelope Secreted, cell wall. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family."}
+{"protein": "MVDHLLPVDENFSSPKCPVGYLGDRLVGRRAYHMLPSPVSEDDSDASSPCSCSSPDSQALCSCYGGGLGTESQDSILDFLLSQATLGSGGGSGSSIGASSGPVAWGPWRRAAAPVKGEHFCLPEFPLGDPDDVPRPFQPTLEEIEEFLEENMEPGVKEVPEGNSKDLDACSQLSAGPHKSHLHPGSSGRERCSPPPGGASAGGAQGPGGGPTPDGPIPVLLQIQPVPVKQESGTGPASPGQAPENVKVAQLLVNIQGQTFALVPQVVPSSNLNLPSKFVRIAPVPIAAKPVGSGPLGPGPAGLLMGQKFPKNPAAELIKMHKCTFPGCSKMYTKSSHLKAHLRRHTGEKPFACTWPGCGWRFSRSDELSRHRRSHSGVKPYQCPVCEKKFARSDHLSKHIKVHRFPRSSRSVRSVN", "text": "FUNCTION: Transcriptional regulator that binds to the GA element of the CLCNKA promoter. Binds to the KCNIP2 promoter and regulates KCNIP2 circadian expression in the heart (By similarity). Is a repressor of CCN2 expression, involved in the control of cardiac fibrosis. It is also involved in the control of cardiac hypertrophy acting through the inhibition of MEF2A and GATA4 (By similarity). Involved in podocyte differentiation (By similarity). Inhibits MYOCD activity. Is a negative regulator of TP53 acetylation. Inhibits NF-kappa-B activation through repression of EP300-dependent RELA acetylation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family."}
+{"protein": "MQGAVAGLVFLAVLVIFAIIVVAKSVALIPQAEAAVIERLGRYSRTVSGQLTLLVPFIDRVRARVDLRERVVSFPPQPVITEDNLTLNIDTVVYFQVTVPQAAVYEISNYIVGVEQLTTTTLRNVVGGMTLEQTLTSRDQINAQLRGVLDEATGRWGLRVARVELRSIDPPPSIQASMEKQMKADREKRAMILTAEGTREAAIKQAEGQKQAQILAAEGAKQAAILAAEADRQSRMLRAQGERAAAYLQAQGQAKAIEKTFAAIKAGRPTPEMLAYQYLQTLPEMARGDANKVWVVPSDFNAALQGFTRLLGKPGEDGVFRFEPSPVEDQPKHAADGDDAEVAGWFSTDTDPSIARAVATAEAIARKPVEGSLGTPPRLTQ", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the band 7/mec-2 family."}
+{"protein": "MAASPARPAVLALTGLALLLLLCWGPGGISGNKLKLMLQKREAPVPTKTKVAVDENKAKEFLGSLKRQKRQLWDRTRPEVQQWYQQFLYMGFDEAKFEDDITYWLNRDRNGHEYYGDYYQRHYDEDSAIGPRSPYGFRHGASVNYDDY", "text": "FUNCTION: Probable hormone that may attenuate cell proliferation and induce senescence of oligodendrocyte and neural precursor cells in the central nervous system (By similarity). ECRG4-induced senescence is characterized by G1 arrest, RB1 dephosphorylation and accelerated CCND1 and CCND3 proteasomal degradation (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm Apical cell membrane. SIMILARITY: Belongs to the augurin family."}
+{"protein": "MRKVTLVFSAIAFAFSLNGVVQAKVQMPESVSSGVTTVELSQRQAVHWVSVEQIEKSLQDQPPMAIGFDIDDTVLFSSPGFYRGKLKYSPNDNSYLKNPAFWEKMNNEWDEFSMPKQIGIELVQMHLKRGDNIYFITGRTKTKTETVTKYLQEDLHIPADKMNVVIFAGDDPGKNNKISWMKEHKLKLYYGDADADIAAAHELNIRGIRILRASNSSYQPLPKAGRFGEEVVIKSEY", "text": "FUNCTION: Dephosphorylates several organic phosphate monoesters. 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. SIMILARITY: Belongs to the class B bacterial acid phosphatase family."}
+{"protein": "MLRPATPLAVLLAAAFGLLLISVLSTPIIKAIPLGEYVGVTFGVFGYCINNNARCSPIEIGYDEGLAAALADKNANFDLPSQARRTLSTILIIHPVAALVTLIMFAMSIAAHFHSPSHSARYLLIVFIVGLLNFVICLLAFLVDVLLFVPHMAWGSYLVLAATILVALSGLVACAMRRTLVSRKARKKRIEENAEMSGENFYNRQAQQVTPPAENKPTVPVVSGANGAVGDKLPSFATYEKRDDLSSEDRVPLTANSPANRSPNAQYNDPNRPDGQFNQPRRAPSGRDQYGNPMEGPTDSYGVQRAPSAERMNPGARGGYRGRGYGPPGRGGYGYGPPPGSRGGYGPPGRGGYGPGPNGRGGYGPPPRGGYGPPMRGRAPPPGYQYDRRGSPAEAYGPPPGQGPYGQRQQSPGPPSAPGYGMNGSTPTVSSAAYGHQHTPSDDLPRAESPPPLPGTEPMPPVGQAVAMDAKTGSPQVPQNGFTAMPPPNRFGGGQQFRDSDADIQGMVGLQQGITPAGQQPPSQRHQTLMSEPSHYSQEGPQYVPARQNWNDQRSKTPGAESVIHPSMMPQPLNASRTDLSISRNSPGPGGAPARSRTSEYYEDVAPRFATPDPSLRGTPVPGQAGGRIPPPINLPAGGPDFDEMPDGSRSPAASERSTFTSISQRGINPRWNPPPPSMMPGYGPAPQRRPNRNDMLLNSNPDFELPTNRGGRGGSPPRAPGTSMIPGSAYPNGRL", "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": "MKRYNAKRKTHRNLKSIKKLIPTVLALLAFVSLLAGIITLHNPKTLPFRQIKITVSSDHIKMAELKDIVVHHIQGGFFSFNASALQTALMSLPWVHDVSVRRIWPNELEIQVEEQRPIARWNQNELITQEGEIFSPPIETIPQNIPQLSGPNDSEENVLNRFQQFSQLLIPFHAAVTALSLTKRGAWSLILNGHTQIFLGRENIDQRFEQFVHLYPKIIGANINRVEHVDLRYSNGLAIQWKN", "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. May control correct divisome assembly. 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": "MQVPIEHNGGEQTLLVPFRAHRPPRPLLQLGSRASPVSGFQLGVVEGEWRVVQPAYGQARWTTSPPPASPTSGSLRRPTLSASKATCWGGCTIWTRPIIEAFHGKGVQVIADIVINHRTAEHKDSRGIYCRLPPRLGPAHDLPRRPLRRRHRKPGHRRRTSTTSTSASSGSSSAGSTGSRWTSASTRGASTSPRATPPTWQRSTSMPPSRASPWPRYGRRWRTAGTASRTTTRTRTGRSWSTGSIVSAAPTAMPRRSTSPPRASSTSPWRAIELWRLRGEDGKAPGMIGWWPAKATTFVDNHDTGNPCIFYDHFFDWGLKDEIERLVSIRNRQGIHPARGRCCWLLPS", "text": "FUNCTION: Important for breakdown of endosperm starch during germination. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MASATLPAWIKMPSFLKKILKLRGRRQEDESRSRMLSDSSTQSYQVNQLTSEGTEAGSTIPSTPSKGQALPTESKVRAREKSRHRRPKIIDQVRRVESLGEQASQRQKHMLETLINKIYTGPLGEELVQTLYLRIWAMEETPESLKILQMREDIRDQVLKMKTERWLRTLIRGEKTKLKDFQKRYEEVHPYLMKEKVEQIIMEEAWSLAAHIVQE", "text": "FUNCTION: The different products prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. They inhibit IFN-alpha/beta induced tyrosine phosphorylation of STAT1 and STAT2. Blocking the IFN- alpha/beta pathway requires binding to STAT1 in the cytoplasm. They inhibit IFN-gamma induced serine phosphorylation of STAT1. Block the IFN-gamma pathway by binding to and stabilizing the parallel form of the STAT1 dimer, further inducing high-molecular-weight complex formation and inhibition of transcription by IFN-gamma. May also have a role in preventing the cell to enter apoptosis. Modulate regulation of viral transcription and replication. Overexpression inhibits the viral RNA polymerase. The absence of all C', C and Y1 proteins leads to viral delayed growth. Plays an important role in virion particles release. Modulates virion shape. SUBCELLULAR LOCATION: Host cytoplasm Note=Protein C' seems to localize around the Golgi. SIMILARITY: Belongs to the respirovirus protein C family."}
+{"protein": "MSTNEIKNDYSAKEETAGPGDSNTSEIKTSDVYKVDKNLPSRFNNPDCFRYSHKTTNPLYRTTNQAYGSKKPTVHEMPTSFNGSRHRFSEHLLKSGMYRDNGFNTMLDKSRLSRPNETSVFYDRINFHSLYHTAGKS", "text": "FUNCTION: Microtubule inner protein involved in the attachment of outer dynein arms (ODAs) to dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Functions at the initial step of left-right asymmetry specification of the visceral organs. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SIMILARITY: Belongs to the PIERCE1 family."}
+{"protein": "MTRRGCWPHRIIFSLILLTWTHVTLAALIRSHTFSNWPKPPCKMYYPIDPDYEANCPDVIALVCATNGLNYKNECFFCIDRWEFGPHIEFVKYGKCE", "text": "FUNCTION: May be a serine protease inhibitor (By similarity). Essential for sperm maturation and fertility. Inhibits sperm acrosome reaction, protecting sperm from premature reaction. SUBCELLULAR LOCATION: Secreted Note=Secreted into the lumen of the initial segment of the epididymis and binds to sperm. In the initial segment of epididymis, localizes on the dorsal surface of the acrosomal region of sperm, gradually becomes more restricted to the acrosomal region in spermatozoa during epididymal transit."}
+{"protein": "MSKHKHEWTESVANSGPASILSYCASSILMTVTNKFVVNLDNFNMNFVMLFVQSLVCTVTLCILRIVGVANFRSLNRTDVKNWFPISLLLVLMIYTSLKSLQYLAVPIYTIFKNLTIILIAYGEVLFFGGKVTSMELTSFIMMVLSSVVATWGDQQAIAIKASSLEDLDQELVESTIFVLNPGYLWMFTNCISSALFVLIMRKRIRLTNFKDYDTMFYNNVLALPLLLVFSFIMEDWSTKNLSVNLSADSLAAMVISGLMSVGISYCSGWCVRVTSSTTYSMVGALNKLPIALAGLVFFDAPKNFLSFFSIFLGFLSGLLYAVAKQKKIQQQKVLAATLEK", "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 Note=Recycles between the Golgi apparatus and the endoplasmic reticulum. SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily."}
+{"protein": "MARVKRGNIARKRRNKILRLARGFRGSNGSLFRTANQRVMKALCNAYRDRRRRKRDFRRLWIARINAASRLNGLSYSRLVGSLKKANIKLNRKMLALLALADPTSFANVVVVAKS", "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, organellar chromatophore. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family."}
+{"protein": "MASTASNTSKLEKPVSLIWGCELNEQNKTFVFKVSDEDKSEHQLALRTVCLGDKAKDEFHVVEIVPQVEGSDVQPVPIASLKPSILPMATMVGIELTPPVTFRLKAGSGPVYISGQHIALEEDYSWAEEEGEEEVEEEEEEEDPESPPKAVKRPAASKKGSQAKKKKMDKDEEESSEEDSPVKKGKGAGRGRKPAAKK", "text": "FUNCTION: Acts as a chaperone for histones, such as histone H2A-H2B, and thus regulates the assembly of nucleosome cores. Involved in chromatin remodeling, especially during fertilization and early embryonic development. May be involved in sperm chromatin decondensation during fertilization. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nucleoplasmin family."}
+{"protein": "MTDPIEQAFERIRAEAMRRNGSVPDLNKNDAFRRPPAPKGGVEKRKKGRASGLDGRQKRYVRGAESLGSVLNKEIQRRGWGKDIAGGWVTSNWEELVGAKIAQHTRVEMIKDKKLFITCDSTAWATNLRMMQRQILQVIAEKVGPNIITELRIFGPQAPSWRKGPLHVKGRGPRDTYG", "text": "SIMILARITY: Belongs to the UPF0232 family. SIMILARITY: Belongs to the UPF0232 family."}
+{"protein": "MGRKCRKLLLKGIPICGVILLILWGYSLYNTLRFMVPGKATEPFTLSLSDVSDDTSAPGEMEKIPRVIHQLWKDENIPERWSNTVNSCRRQHPDENGWQFILWTDEKIMSFMNENYSWFMPVFHSYPYNIQKFDAARYFILYHYGGVYMDLDIGCKKPMDPLLSKATFILPSTEPIGYSNDWFAATPKHPFLYQAIHNLSKFNHRYFTKYPTVFLSAGPLFLSYQFCKYLLTPHEPVRVLPALLYGNGPNSFFSHVTGDSWHGTDAKVFIWIDRNSKSVLFFAFLAAFAILFLCLRVVFKRRRKRGIAASHSQIQELYP", "text": "FUNCTION: With imt2 and imt3, is required for the synthesis of mannosyl phosphorylinositol ceramide (MIPC). Catalyzes the addition of mannosyl to phosphorylinositol ceramide (IPC). MIPC is essential for cell morphology, cell-surface distribution of ergosterol, localization for plasma-membrane transporters, and lipid-raft-mediated endocytosis of plasma membrane proteins to the vacuole. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 32 family."}
+{"protein": "MLPGRLCLVPLLLALGVGSGGGSGDGGDSRRRRLLVAKVNKHKPWIETSYHGVITENNDTVILDPPLVALDKDAPVPFAGEICAFKIHGQELPFEAVVLNKTSGEGRLRAKSPIDCELQKEYTFIIQAYDCGAGPREAAWKKSHKAVVHIQVKDVNEFAPTFKEPAYKAIVTEGKIYDSILQVEAIDEDCSPQYSQICNYEIVTTDVPFAIDRNGNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDVKPVCKPGWQDWTKRIEYQPGSGSMPLFPSIHLETCDGAVSSLQVTAELQTNYIGKGCDRETYSEKSLQKLCGASSGIIDLLPSPSAATNWTAGLLVDSSEMIFKFDGRQGAKIPDGIVPKNLTDQFTITMWMKHGPSPGVRAEKETILCNSDKTEMNRHHYALYVHNCRLVFLLRKDFDQADTFRPAEFHWKLDQICDKEWHYYVINVEFPVVTLYMDGATYEPYLVTNDWPIHPSHIAMQLTVGACWQGGEVAKPRFAQFFHGSLASLTIRPGKMESQKVISCLQACKEGLDINSLESLGRGIKYHFNPSQSILVMEGDDIGNINRALQKVSYINSRQFPTAGVRRLRLSSKVQCFGEDVCISIPDVDAYIMVLQAIEPQITLQGTERFWRPAAQFESARGVTLFPDIKIVSTFAKTEASGDMRATGTAPKSAVLEEMLHNLDFCDILVLGGDLDPRQECLELNHSELHQRHLDATNSTAGYSIYGVGSMNRYEQVLHHLRYRNWHPTSLETRRFRIKCSELNGRYTSNEFNLEVSVLHEVRVSDKEHVNHLIVQPPFLQSVHHPETRSSIQRSSVVPSIATVVIIISVCMLVFVVAMGVYRVRIAHQHFIQETEAAKEAEMDWDDSALTITVNPMEKHEGPGNGEDETTEVEEEEEAEEGSSSSSSGSDDSEEEEEEGMGRVRHGQSGTSSQSPERSTWNTAGVINIWK", "text": "FUNCTION: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate synapse formation, and which is involved in learning and memory (PubMed:24613359, PubMed:26171716, PubMed:31529526). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with neurexin-alpha at the presynaptic membrane (By similarity). SUBCELLULAR LOCATION: Postsynaptic 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 Cell projection, dendrite Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. SIMILARITY: Belongs to the calsyntenin family."}
+{"protein": "MAEVTYKGKSFEVDEDGFLLRFDDWCPEWVEYVKESEGISDISPDHQKIIDFLQDYYKKNGIAPMVRILSKNTGFKLKEVYELFPSGPGKGACKMAGLPKPTGCV", "text": "FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrC/TusE family."}
+{"protein": "MHKSAALSLRDAQFADMNMYCDVTDRTPIEAVHSCNNAESLNILNKLLARETDTALSQIFEQPTGKDWKELNTLQTILSLCSTVTMALLLGPDTAPDPVLHHHSTSFGEAIMSSCYRRTGYPRILRPFVWRFSSECRNLRKHFSLVRERLVPEVARRVAAARAADKTKDVRPSSLLDALIAAAFDNGSLSPDDQGRNDAAQVQLLADDLIFYHFELCKPTAFNIIFQLYAIMDHPEYKAPLREEALQALKLTNGDWTVETLKHAPKLESFTKETFRLYDISGFVSFRRVMKPLTLNSIGLSLRPGTILLSPCRNVHLDPEIYEDPTTFNGYRFYDSSREVCSPRVATTSLTFLTFSHGAGSCPARVLATQICRTIFIKFLLQYDVEPVQKEILPYGFTSGPVYMPNPSVMMRIRPRSDGK", "text": "FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin (PubMed:22945023, PubMed:26389790). The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7- dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules (PubMed:17315249, PubMed:22945023). Further O- methylation by ktnB leads to the formation of 7-demethylsiderin (PubMed:17315249, PubMed:22945023, PubMed:26389790). Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin (PubMed:26389790). P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin (PubMed:22945023). SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MDETLAEFFRRTILKIPMTEMMTILKTWNFMSENQLQTVNFRQRKESIVQDLVLLCEENHASLNDAAHLDIIYTQFHRHQKIWDVFQMSKAPGDDIDLFDMEQFKSSFKKILQRALKNVTVSFRDAEENSVWIRIAWGTQYKKPNQYKPAYVVYYSQTPYAFTSSSRLKSNLPLLGQALTVASKHHQIVKMDLRSRYLDSLKAIVFKQYNQSFETHNCTTSLQEGSLGLDINMDSRIIHENKVEKERVQRVTQEIFGDYPQPRLEFAQYKLETKFKSDLNGGILAEREEPLRCLVKFSSPHLLEALKSLAPAGIADAPLSPLLTCIPNKGKNYFKIRDK", "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. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Chromosome, centromere, kinetochore Note=Localizes exclusively in the kinetochore domain of centromeres. Kinetochore-bound levels decrease when cells enter mitosis and increase again when cells exit mitosis. SIMILARITY: Belongs to the CENP-N/CHL4 family."}
+{"protein": "MLAFCRSSLKSKKYFIILLALAAIAGLGTHAAWSSNGLPRIDNKTLARLAQQHPVVVLFRHAERCDRSTNQCLSDKTGITVKGTQDARELGNAFSADIPDFDLYSSNTVRTIQSATWFSAGKKLTVDKRLLQCGNEIYSAIKDLQSKAPDKNIVIFTHNHCLTYIAKDKRDATFKPDYLDGLVMHVEKGKVYLDGEFVNH", "text": "FUNCTION: Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the phosphoglycerate mutase family. Ais subfamily."}
+{"protein": "MGQSPSPRSPHGSPPTLSTLTLLLLLCGQAHSQCKILRCNAEYVSSTLSLRGGGSPDTPRGGGRGGLASGGLCRALRSYALCTRRTARTCRGDLAFHSAVHGIEDLMIQHNCSRQGPTAPPPARGPALPGAGPAPLTPDPCDYEARFSRLHGRAPGFLHCASFGDPHVRSFHNQFHTCRVQGAWPLLDNDFLFVQATSSPVSSGANATTIRKITIIFKNMQECIDQKVYQAEVDNLPAAFEDGSINGGDRPGGSSLSIQTANLGSHVEIRAAYIGTTIIIRQTAGQLSFSIRVAEDVARAFSAEQDLQLCVGGCPPSQRLSRSERNRRGAIAIDTARRLCKEGLPVEDAYFQSCVFDVSVSGDPNFTVAAQTALDDARIFLTDLENLHLFPSDAGPPLSPAICLVPLLSALFVLWLCFSK", "text": "FUNCTION: Acts as a bone morphogenetic protein (BMP) coreceptor. Through enhancement of BMP signaling regulates hepcidin (HAMP) expression and regulates iron homeostasis. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Note=Also released in the extracellular space. SIMILARITY: Belongs to the repulsive guidance molecule (RGM) family."}
+{"protein": "MFSRKQVQKRNNELSSLHCSNSSNSLNRIHKNEETAKGTVGVNARGNNRSDNVASPGQLRPRTSSILTDNSEWILFSPENAEGEYVITSSDGIRRTNSNHYYYNYNEDDILSSSRRSSEDVYDAEQEYTEQPVNNHVQVEDEEDDDSIINDLTHVVDDYDYEEEDDKQDLTTRIDNWRKKQVSELLNELNHDDDLDPVLNRDKIDLIQSWGIENEKLNTKPRAKKRQRKSKRASFYGQDLLSKYSMEDLKIIKQIVAQLRDDLDKVKHDKPSSPLPNYHNTLKQAPSSNSQNPSFISYYSNYLTKNNSQQTPNSQSTSGSLLNNPNLEKYLPLFLKNLLYEDSNGSHQHPETSEKEHFWDNDLKSVNSSILTLSSNSKLKQEIL", "text": "FUNCTION: Acts as the peroxisome receptor for pexophagy. Required for both micropexophagy and macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or autophagy pathways. Required for functional micropexophagic apparatus (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of the vacuole. FUNCTION: Acts as the peroxisome receptor for pexophagy. Required for both micropexophagy and macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or autophagy pathways. Required for functional micropexophagic apparatus (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of the vacuole. SUBCELLULAR LOCATION: Vacuole lumen. Preautophagosomal structure. Peroxisome membrane; Peripheral membrane protein. Note=Surrounds the peroxisome cluster, but a small amount is also inside the vacuole in methanol-grown cells. Upon induction of micropexophagy, localizes inside the vacuolar lumen. Also localizes near peroxisomes during early stages of micropexophagy. SUBCELLULAR LOCATION: Vacuole lumen Preautophagosomal structure Peroxisome membrane; Peripheral membrane protein Note=Surrounds the peroxisome cluster, but a small amount is also inside the vacuole in methanol-grown cells. Upon induction of micropexophagy, localizes inside the vacuolar lumen. Also localizes near peroxisomes during early stages of micropexophagy."}
+{"protein": "MGNRSLTEADHALLSKPLVPTSAEHTQTQEYPRPFVDGSNSQSGSELQASPQGQFGEKALTSTNRFIPLANDDPGMQHEMGLDPSMRRRREEWAERGAAKIVKDVVDPATGELTKHVVKMGIKDFKFGEQLGDGSYSSVVLATARDSGKKYAVKVLSKEYLIRQKKVKYVTVEKLALQKLNGTKGIFKLFFTFQDEASLYFLLEYAPHGDFLGLIKKYGSLNETCARYYASQIIDAVDSLHNIGIIHRDIKPENILLDKNMKVKLTDFGTAKILPEEPSNTADGKPYFDLYAKSKSFVGTAEYVSPELLNDNYTDSRCDIWAFGCILYQMLAGKPPFKAANEYLTFQKVMKIQYAFTAGFPQIVKDLVKKLLVRDPNDRLTIKQIKAHLFFHEVNFEDGSVWDDNPPEIQPYKINAEAMKPLQKVSESDTTVKMANLQLAGNGHADTPLQAPAATSQEHSVISMTAATAAFNKDYTSQPKLGSKSSTSVRSASNNTDREVIQKKVSKNRASVSSPSISTTSRGKDNRSRSSDAFWSRYLQNMDERVLLMKEVALSTRNLEDSPVGLENVALDYKNPLDIEPPTDSAGKFYKKMFLITNLGRALVFVKRRSLSMWEEQEFELQFELELNDVEKIRFISDQVLEIDGSRTIFIGCKERAVLMKLWKLIHNGMTAKPKVVSPKSDHKMFDKFILQKRQNTKKKNQAPPVPQSNRLINGLPDRCILKTPEEGALHTKRPTSLQTRSSSNYSKLLARSTQMRKNMTRTDEK", "text": "FUNCTION: Activates YPK1 by phosphorylating of a threonine residue. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily."}
+{"protein": "MRLTAKQVTWLKVCLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWIILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKSRSLFNRLRKQVHNKLSV", "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": "MSANGAVWGRVRSRLRAFPERLAACGAEAAAYGRCVQASTAPGGRLSKDFCAREFEALRSCFAAAAKKTLEGGC", "text": "FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1) (PubMed:27499296). Required to stabilize NDUFAF5 (PubMed:27499296). SUBCELLULAR LOCATION: Mitochondrion."}
+{"protein": "MAATGGGADDESRSGRSSSDGECAVAPEPLAEAGGLVSFADFGVSLGSGAGLPGRSVGRAQSSLRYLQVLWQQDVEPRDELRCKIPAGRLRRAARPHRRLGPTGKEVHALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNILQEGHSQCLEAVRLEVKQIIHMLREYLERLGRHEQRERLDDLCTRLQMTSTKEQVDEVTDLLASFTSLSLQMQSMEKR", "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. EPO stimulation induces nuclear accumulation."}
+{"protein": "MNDEMKGKSGKVKVMYVRSDDDSDKRTHNPRTGKGGGRPGKSRADGGRRPARDDKQSQPRDRKWEDSPWRTVSRAPGDETPEKADHGGISGKSFIDPEVLRRQRAEETRVYGENACQALFQSRPEAIVRAWFIQSVTPRFKEALRWMAANRKAYHVVDEAELTKASGTEHHGGVCFLIKKRNGTTVQQWVSQAGAQDCVLALENESNPHNLGGMMRSCAHFGVKGVVVQDAALLESGAAIRTAEGGAEHVQPITGDNIVNVLDDFRQAGYTVVTTSSEQGKPLFKTSLPAKMVLVLGQEYEGLPDAARDPNDLRVKIDGTGNVAGLNISVATGVLLGEWWRQNKA", "text": "SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family."}
+{"protein": "MASARVPQQLFLQGVAAVYLFAFASLYTQIPGLYGPEGILPARRTLRPQGKGRWQQLWETPTILWEAPRLGLDTAQGLDLLTLLGTVLALGALLLNSLRHPFIYLLLWAAYLSACQVGQVFLYFQWDSLLLETGFLAILVAPLRRPSKHKIPQGGLAGALPHEDLPFWLVRWLLFRLMFASGVVKLTSRCPAWWGLTALTYHYETQCLPTPAAWFAHHLPVWLHRLSVVATFLIEIAVPPLFFAPIRRLRLSAFYAQALLQILIIITGNYNFFNLLTLVLTTALLDDRHLSAEPELRCHKKMPTSWPKTLLTSLSLMLELTVYGLLAYGTIYYFGLEVDWQQQIVLSKTTFTFHQFSQWLKMVTLPTVWLGTASLAWELLIALWRWIQVQGWSRKFFAGIQLSVLGTATVFLFLISLVPYSYVEPGTHGRLWTGAHRLFSSVEHLQLANSYGLFRRMTGLGGRPEVVLEGSHDGHHWTEIEFMYKPGNVSRPPPFLIPHQPRLDWQMWFAALGPHTHSPWFTSLVLRLLQGKEPVIRLIQNQVANYPFREQPPTYLRAQRYKYWFSKPGDQSRWWHRQWVEEFFPSVSLGDPTLETLLQQFGLKDKSPPRARSSKNALAQTLNWVRAQLSPLEPSILLWGLLGAVVAIRVVRTLLTPRPLQSSKQTREEKRKQAPKKDSRAVSEQTAPNSNSNGSWAPRRKK", "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": "MEGLVVAAGGDVSLHNFSARLWEQLVHFHVMRLTDSLFLWVGATPHLRNLAVAMCSRYDSIPVSTSLLGDTSDTTSTGLAQRLARKTNKQVFVSYNLQNTDSNFALLVENRIKEEMEAFPEKF", "text": "FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome. SIMILARITY: Belongs to the PSMG4 family."}
+{"protein": "MFLKFKNIFFIVLTLSIVFNGLIVNSKNIHINNKNNNNNNNNKDLSSSESGSSSDINPYISQYNSERETLVNQENQIKLGSNTPFNSKEQQANTIFLNILQNEELSFSNNDPSGVNFFIEKQIIENESTIFKIIQNMPKGSALHVHQDSSATYDYLISVGSYLPNCYIYLTYDVNDANNGTFHFYDSQPTDSNWKLLSTIREGVSNVESFDQQLLDSLTLIGQDYGDYVSLWRKFDGIFGRVNGLVTYLPIATGYMEHLFQQMIQDGVQHIEVRKCFGDFYDLTGKIYDDYWFVQTMEELVLTTRQKYNMSEFALKIIGCNGRHNNQSVVYDAMVMSLDLRNKYPSTFVGYDLVGPEDEGYPLIYFIEQFAEIKKLGYQYQYPLDYYFHAGETILYNNTNLYDAILLNTKRIGHGIQLPKHPLLMDLVLKNDIGIEICPISNQILQYVSDMRAHPGLDLLNRGLPVTISPDDPAIFNYGGLSYDFFELTYSWGLNLQQLKQLAINSINHSNTFNQSEYNLLYNAWEVKWFNFIDYIINTYSNI", "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 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. ADGF subfamily."}
+{"protein": "MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK", "text": "FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also Catalyzes the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion intermembrane space. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
+{"protein": "MSWQTYVDEHLMCDVGDGQGHHLTAAAIVGHDGSVWAQSANFPQFKGQEFSDIMKDFDEPGHLAPTGLFMAGAKYMVIQGEPGAVIRGKKGAGGITIKKTGQSCVFGIYEEPVTPGQCNMVVERLGDYLLEQGL", "text": "FUNCTION: Binds to actin monomers and regulates the organization of the actin cytoskeleton (PubMed:29861135). At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (PubMed:29861135). At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate (PubMed:29861135, PubMed:26996265, PubMed:16313636). Acts redundantly with PRF5 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth (PubMed:26433093). Functions probably by favoring formin-mediated actin polymerization at pollen tube tips (PubMed:26433093). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm. SIMILARITY: Belongs to the profilin family."}
+{"protein": "VLIMELINNVAKAHGGYTVFAGVGERTREGNDLYHEMIESGVISLKDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTSKGSITSVQAIYVPADDLTDPA", "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": "MTFRNCVAVDLGASSGRVMLARYERECRSLTLREIHRFNNGLHSQNGYVTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQEQQINDLPALISATQALPACRFIINPNDDRFINPETMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTTANLTTFTPNPDSEIAHYVAQIHSTRQTKELCA", "text": "FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). It could also play a role in the metabolism of some rare sugars such as L-fructose. Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1- phosphate. Uridine triphosphate (UTP), cytidine 5-triphosphate (CTP), guanosine 5-triphosphate (GTP), and thymidine triphosphate (TTP) also can act as phosphoryl donors. It can also phosphorylate L-fuculose and L-xylulose. 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": "MQEVCSSLDTTSMGTQIKSESPLNPLQVQTGQTSLPVGGCGGAGVVGGVGGVGVSVGQPGIGQQGVPPVPSVLMVNKMTPNCDKRSADTAYWMTASEGGFINSQPSMAEFLNHLSPESPKIGTPVGSGAIGGVGVNVNVNVGVGVGYPVGVVPQTPDGMDSVPEYPWMKEKKTSRKSSNNNNQGDNSITEFVPENGLPRRLRTAYTNTQLLELEKEFHFNKYLCRPRRIEIAASLDLTERQVKVWFQNRRMKHKRQTLSKTDDEDNKDSLKGDDDQSDSNSNSKKSCQGCELPSDDIPDSTSNSRGHNNNTPSATNNNPSAGNLTPNSSLETGISSNLMGSTTVSASNVISADSSVASSVSLDEDIEESSPIKVKKKDDGQVIKKEAVSTSSKASPFGYENSTPSLVSFRRDSDASAVGNAPTSKAVGKKRFQSAANAIATPTPLSDSNSGNGSGGGPAGGYFPGYYPSPKQQQQVQQQQLHPQQQQLPQQQPQDYYGKYDIEFAASPHHNPHNKQQALHGEYLSPKPSSANFHQNSQQQQQNDHFYYNYNDTNGTPYLNHQQQHHHHAQHHQQQQHHQNHVADFEGPVNGPSNFNNGAYYDNMSFQQQAQAHQHQTVVFQQQQPHQPAAINHQHMHHLGNGETYSALGLQMENCEGYNNFGAAGTGGGYYEAGQQPPIPATHGHGHHPHHVQVPAQAHAPIHAHHNSAAIPGGVGVGPPPSHIHGFAINGGPAVQGQAFGNNGSTAAGTAAISGLENSNSSDFNFLSNLANDFAPEYYQLS", "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. Controls development of mouthparts, and labial and maxillary palps. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family. Proboscipedia subfamily."}
+{"protein": "MESPFSPVLPHGPGEDWESTLFAELGYFTDTDDVQFDAAHETYENNFDHLNFDLDLMPWESDIWSPSSHFCSDIKAEPQPLSPASSSCSVSSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCHSPSSAEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTPANASVPAKTIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPAVVQLQTPGVLPSAQPVLAVTGGATQLPNHVVNVVPAPVVNSPVNGKLCVTKPVLQSSTRSTGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGSLKRQLDQVVSENQRLKVPSPKRRAVCVMIVLAFIMLNYGPMSMLEQDSRRVKPSVSPANQRRHLLEFSAKEVKDTSDGDNQKNSYRYDHSVSNDKALMVLSEEPLLYIPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNSQQKTRILQGALEQGSNSQLMAVQYTETTSISRNSGSELQVYYASPGSYQGFFDAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININDNVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDHQRNQTSTFFGSPPTATETTHVVSTLPESVQ", "text": "FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP- dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR). FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Transcription factor that initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR. Binds DNA on the 5'- CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT- N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor. May play a role in foveal development and cone function in the retina. SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Nucleus Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus (PubMed:22682248). THBS4 promotes its nuclear shuttling (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Golgi apparatus membrane; Single-pass type II membrane protein Note=Translocates from the endoplasmic reticulum to the Golgi, where it is processed. SIMILARITY: Belongs to the bZIP family. ATF subfamily."}
+{"protein": "MWILIYLFIIWSSLRTWVTAVDSTTTVGDDLNETVSASVWPTMSPQMTVAFRSQRDVMGNLTIDQLPYVGLNLRRVLLNNETSMVNEGNNTRLLTLFKSMLSSEANAFVLDLEQYNNDLRVVDTTLLFSDVLTALQSFIFSTQNNLYANIIVLLLNISAPELDSTEYRHQNQTLNTTYILDKNLGNSFIYKPTDLQSDRAKNNTWNIYGKSSIDGWPTLGSVLYEQKKRLVIGELTDFFNETTAPYIFPHDVFHYEQGNSTLDCPSTVEGLTDLSSIHWRFLDSLFNSVDIKEYISCGLSPIISNSAYVNNVTQLADIIHEGSVWSWDSDQPSVTQSTSKSGSSSGTLEAYNCVLLYYFANNETVTWRVGNCYNSNIGLCRYENMAFRWLVRSNKATYFDFDSYQGSKCPDQYSFNIPRSPLEQRSFIAYMRNSSFSDTQIWIDLNSISVSNCWVSGGPYASCPYEKVISRRNFVTMMVPASVCSFALLCIVVYLSVLRVPIYDNRKNWRRVINKISKSELEGVPS", "text": "FUNCTION: May be involved in telomere capping. FUNCTION: May be involved in telomere capping. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MTC6 family."}
+{"protein": "MSEPERASIEFVSESDSIDFGIMMKKGVKALTDILANHLQHDPEWKNERSMKFVFKNQNGELQPVLNRTARLEDEGVGPSPDDGQVVDGEETASEQDKLAEANCSDGSSTGDLQLDDPESEVLFDYSLDHLPNISYTPDPTIGKHVMEMIESLLPKGAPYREKVLNTMKNNVQGAGMSTAGTAAVETIQHTAGSTISEPAMSYECDRDLGIAESDDWEHQQFAQPHHGTLEADTVAEGHHRCQSRSSESQHAGHQRAGQEYLYECKPKARPDFHALTMFDPLEQPLCMFCEYYLVFGEPPRQMIKWYNKYGSSSGGPSAGSQQGNKGWNGNKKKKKKKGKKGKR", "text": "FUNCTION: Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole. SIMILARITY: Belongs to the IBD2 family."}
+{"protein": "MATFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDFKEFSHLEDFPFDAEY", "text": "FUNCTION: [Isoform 1]: Catalyzes the NADPH-dependent reduction of a variety of carbonyl substrates, like aromatic aldehydes, alkenals, ketones and alpha-dicarbonyl compounds (PubMed:26222439, PubMed:21276782). In addition, catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta- hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs (PubMed:25577493). Displays strong enzymatic activity toward all-trans- retinal and 9-cis-retinal (PubMed:26222439). May play a physiological role in retinoid metabolism (PubMed:26222439). FUNCTION: [Isoform 2]: No oxidoreductase activity observed with the tested substrates. SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MRQPLSWGRWRAMLARTYGPGPSAGYRWASGAQGYVRNPPVGACDLQGELDRFGGISVRLARLDALDRLDAAAFQKGLQAAVQQWRSEGRTAVWLHIPILQSRFIAPAASLGFCFHHAESDSSTLTLWLREGPSRLPGYASHQVGVAGAVFDESTRKILVVQDRNKLKNMWKFPGGLSEPEEDIGDTAVREVFEETGIKSEFRSVLSIRQQHTNPGAFGKSDMYIICRLKPYSFTINFCQEECLRCEWMDLNDLAKTENTTPITSRVARLLLYGYREGFDKIDLTVEELPAVYTGLFYKLYHKELPENYKTMKGID", "text": "FUNCTION: May contribute to the regulation of cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Note=Subcellular location may vary between isoforms. SIMILARITY: Belongs to the Nudix hydrolase family."}
+{"protein": "MDRPAVSGPMDLPIMHDSDRYELVKDIGSGNFGVARLMRDKQSNELVAVKYIERGEKIDENVKREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYASGGELFERICNAGRFSEDEARFFFQQLISGVSYCHAMQVCHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLKKEYDGKVADVWSCGVTLYVMLVGAYPFEDPEEPKNFRKTIHRILNVQYAIPDYVHISPECRHLISRIFVADPAKRISIPEIRNHEWFLKNLPADLMNDNTMTTQFDESDQPGQSIEEIMQIIAEATVPPAGTQNLNHYLTGSLDIDDDMEEDLESDLDDLDIDSSGEIVYAM", "text": "FUNCTION: Activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomata closure in response to drought, darkness, high CO(2), plant pathogens, or decreases in atmospheric relative humidity (RH) (PubMed:30361234). Involved in the resistance to drought by avoiding water loss. Required for the stomata closure mediated by pathogen-associated molecular pattern (PAMPs) (e.g. flg22 and LPS) of pathogenic bacteria such as P.syringae pv. tomato (Pst) and E.coli O157:H7. As a plant defense process, stomata are closed transiently in order to limit invaders, but actively reopened by bacteria after a few hours; virulent strains (e.g. Pst DC3000) are more efficient than avirulent strains (e.g. Pst DC3000 AvrRpt2) in reopening stomata. Mediates the phosphorylation and activation of the S-type anion efflux channel SLAC1, and thus promotes stomata closure. Essential for stomatal closure in response to reactive oxygen species (ROS). Promotes MAPKKK18 activity upon abscisic acid (ABA) treatment (PubMed:26443375). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MLPCFTRKPVDHPLGFLVALSGLLMQLMSYGIDNSYSIFSDDMHKDPSLGYPSVTTISLGNSVSLGLSPAFGVLCGFLVDRVPPRLMMAVSTLMLFAGLWLSSTFAHNVTAVTFSYCLLASISSACMLSPGAAATSSWFNRYQGLAMGINFSGGGVGSAIIPSLAGKWVVAYGWRKTFRLMSAFCAIGVVATLLSARRAPPKKEEAGPSEYDEGQERQEQGEEEQAHTDEENRNNNNSNGETTPARRGLHTHKLNPWELFLTMFSRAFLGNFFCWLIFSWAFYSLIYVAVPYVSSMGKAGTVYADISPIPTDIASTLFTFYGVFQIVGSILVGWLATGTTNEFAYVLCATIGGIFCAFLGFCRSYVAFALLLCVIGFCMAGMFAVMPALIAERLYGPNLGFYMGAVFLAGVVGGFSAPPIQAELQQRHYGNYTYVCVFMSACMTLAAAVCYITMWRDKRVRIVSAAAEAKLA", "text": "FUNCTION: Transporter involved in riboflavin (vitamin B2) uptake. Also transports FMN and FAD. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. RibJ family."}
+{"protein": "MTEIWNFINTGSKNPYYNMAMDEALLNFVSRGEIDPVIRFYTWNPATLSIGYFQRLQKEIDIDKVKEKGYGLVRRQTGGRGVLHDKELTYSVIVPESHPNMPSTVTEAYKIISQGLLEGFKNLGFETYFAIPRSKEERDKLKQPRSSVCFDAPSWYELVVEGRKIAGSAQTRQKGVILQHGSILQDIDIDDLFDMFKFKNERLKAKMKENFVQKAVAINDISNQHITLNEMENAFEAGFKKGLNIDFKPLELTEKQLEEVQELEDKYRSEAWMYRK", "text": "FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation. SIMILARITY: Belongs to the octanoyltransferase LipM family."}
+{"protein": "MRDSHPVEQTVGIEYYVTETDGTGGRLRDRPADFRVREREAFGADCRPLDADPGSYPHLVFRATLREWDTNDFASAVSNALGVSRERVSWAGTKDKHAVTTQLFSVRHDDAALPDLDGADIEPIGRAGRPVLFGDLAGNEFELVIRDPDRPEHAEATAAELCDFGGGEAGVPNYFGTQRFGSRRPITHRVGLDVLDGDWEAAAVRYVCESSEREPERTQEVREGIDADRDWAAAGERLPGSLRFERAIANRLAEGAESPDDYRAALEELPSNLQRMFVNAAQSYVFNRILSERLRRGLPFDEPVVGDVVCFSDSDGNPDPDRTQTVTESRLETVRRHCERGRAFVTAPLVGTETVFGDGEPAEITREVLADVDVSPTDFELPGEFGSSGTRRAVLVTTDLTVEQEPLTLSFSLPKGSYATVVAREFLKADPEALS", "text": "FUNCTION: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family."}
+{"protein": "MATIAGSRAPTEVPSHPYTCNTCQVAFRNSELQRGHMRSDWHRYNLKRRVASLPPISSEVFTEKVLQARAATTAQADKAGFEKTCEVCQKTYYSENSFRNHLSSTKHKSKAAAAARRPANNKVDDDVSSMSFSLGEPARADSVVDSEAEEEFSEVVEGIKNASIHDTASPIKRPSAPQPAVEEQSKTDAQMEETPTTTPKPEALTPSATTCVFCNYESPTPQLNASHMERIHGMFIPEKQYLVDLEGLLKHLWEKVFRYNECLTCGKMKVNVFAIQTHMRDKSHYHIPYTTEEEQLEIGEFYDFRSTYSDGDWETEEEDKGEEDGGVRLGAKRESKVVDENGDEVMEDEEGWETDSDASSLDTDDLHAVPAEGHYHQYERLGKHPHHSRENKKAHREADGIHAPSKRTHAVYYDEYELHLPSGKSVGHRSLARYYRQNLYHYPTPEERAERLAIEAAERENRMDVDGEEPERGRTRTRALVPRDIKGLGVTTMSDPRVRGIVQKGKKEEWKNRDSKWWMHSQVAIKEKAKHPSTYLR", "text": "FUNCTION: Pre-60S-associated factor involved in the cytoplasmic maturation of the 60S subunit. Involved in the dissociation and recycling of other late pre-60S factors before newly synthesized large ribosomal subunits enter translation (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the REI1 family."}
+{"protein": "MIIYKDILTGDEIISDAFNLKEVDNILWEVDCRNITIGDENIQLEGANPSAEGEDDDAGGAGNAEQVLDIKHNFRLNDYPKLEKDEYKKAIKGYMKKVLAKLEEKKAPEETIKEFKENAQTALKRILANYKDYDVLVGESFGADAMHILINYREDGVTPYATFWKHGLEEYKV", "text": "FUNCTION: Involved in protein synthesis. Involved in microtubule stabilization (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TCTP family."}
+{"protein": "MALLPVLFLVTVLLPSLPAEGKDPAFTALLTTQLQVQREIVNKHNELRKAVSPPASNMLKMEWSREVTTNAQRWANKCTLQHSDPEDRKTSTRCGENLYMSSDPTSWSSAIQSWYDEILDFVYGVGPKSPNAVVGHYTQLVWYSTYQVGCGIAYCPNQDSLKYYYVCQYCPAGNNMNRKNTPYQQGTPCAGCPDDCDKGLCTNSCQYQDLLSNCDSLKNTAGCEHELLKEKCKATCLCENKIY", "text": "FUNCTION: May regulate some ion channels' activity and therebye regulate calcium fluxes during sperm capacitation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
+{"protein": "MELVGWLVDKGITSEKQWIQEDQASYISFNAASNSRSQIKAALDNAGKIMSLTKTAPDYLVGQQPVEDISSNRIYKILELNGYDPQYAASVFLGWATKKFGKRNTIWLFGPATTGKTNIAEAIAHTVPFYGCVNWTNENFPFNDCVDKMVIWWEEGKMTAKVVESAKAILGGSKVRVDQKCKSSAQIDPTPVIVTSNTNMCAVIDGNSTTFEHQQPLQDRMFKFELTRRLDHDFGKVTKQEVKDFFRWAKDHVVEVEHEFYVKKGGAKKRPAPSDADISEPKRVRESVAQPSTSDAEASINYADRYQNKCSRHVGMNLMLFPCRQCERMNQNSNICFTHGQKDCLECFPVSESQPVSVVKKAYQKLCYIHHIMGKVPDACTACDLVNVDLDDCIFEQ", "text": "FUNCTION: Plays a critical role during packaging of viral DNA into empty capsids, where they are thought to be part of the packaging motor complex. The single stranded genomic DNA is packaged in a 3' to 5' direction and requires the association between viral DNA and Rep40. Regulates host PKA activity by interacting with host PRKX as a mechanism to interfere with helper virus propagation and to promote its own replication. SUBCELLULAR LOCATION: Host nucleus."}
+{"protein": "MAWNTNLRWRLPLTCLLLEVVMVILFGVFVRYDFDADAHWWSWRTEFYYRYPSFQDVHVMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHFLQGRYIVVGVENLINADFCVASVCVAFGAVLGKVSPIQLLIMTFFQVTLFAVNEFILLNLLKVKDAGGSMTIHTFGAYFGLTVTRILYRRNLEQSKERQNSVYQSDLFAMIGTLFLWMYWPSFNSAISYHGDSQHRAAINTYCSLAACVLTSVAISSALHKKGKLDMVHIQNATPAGGVAVGTAAEMMLMPYGALIVGFVCGIISTLGFVYLTPFLESRLHIQDTCGINNLHGIPGIIGGIVGAVTAASASLEVYGKEGLVHSFDFQGFKRDWTARTQGKFQIYGLLVTLAMALMGGIIVGVGLILRLPFWGQPSDENCFEDAVYWEMPEGNSTVYIPEDPTFKPSGPSVPSVPMVSPLPMASSVPLVP", "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(+) (By similarity). May act as a CO2 channel providing for renal acid secretion (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein 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": "MKASGTLREYKVVGRLLPSAKNPTPPLYRMRIFAPNHVVAKSRFWYFVSQLRKMKKANGETVYCGLVHEQSPLKVKNFGIWLRYDSRSGTHNMYREYRDLTTSGAVTQCYRDMGARHRARAHAIQIMKVQVIAANKCRRAAIKQFHDSKIKFPLPHRVLRRQHKPRFTTRRPQTFF", "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": "MNNKLSDFEKNLYKKLKSGKLEVKVSYRTFLCPYCPDNKKKVGLYVDILQHASGVGNSQSKKRSLTEKASHRALAKYLIKDLAHYATSTISKRLKARTSFIPAETGDAPIIYDDAQFEKLVWPWKGVLVNIPTTSTEDGRSCTGESGPKLKDELIRRGFNPIRVRTVWDRFGHSGTGIVEFNRDWNGLQDALVFKKAYEGDGHGKKDWLCGATDSSLYAWLANADDYYRANILGENLRKMGDLKSIYRFAEEEARKDQKLLQRLNFMVENKQYRLKKLQIKYSQDSVKLKYETEEKEKILRAYSEDLTGRQQKSTDHFNRIFADHEKQKVQLESQIKELEIRKLELAKREAENETQRKIVAKELEQNAAINSYVQLSALEQQKTREKAQRLAVDHKMQKEKLHKRIAALERQLDQKQELELEVQQLKSQLSVMRLVELDSGSEIVNKVETFLRDLSETEGELAHLNQFNQDLVVQERKSNDELQEARRALISNLRDMGLHIGVKRMGELDTKPFMKAMRIKYCQEDLEDWAVEVIQLWEEYLKDPDWHPFKRIKLETAETIVEVIDEDDEKLRTLKNELGDDAYQAVANALLEINEYNPSGRYISSELWNFREDRKATLEEGVNSLLEQWNQAKHLKS", "text": "FUNCTION: Acts in association with FDM4 and FDM5 for RNA-directed DNA methylation (RdDM)."}
+{"protein": "MCLRIGGLNVDEFRKLLMKTGLVLVVLGHVSFIAAAVLHGTMLRFVATTRDAVVLQYCVVDILSVTSAIVVILAGISAVILSRYLPSTPLRWTVFSLSVACALLSLTCALGLLASIAVTFATKGRALLAPCTFENTELPTLAPDCPFDPTRIYSSSLCLWAISLIFCLAESMSAVRCAQLVHRLLELRPWWGKSCHHTIQASPEPLDGHDLLSCTS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM54 family."}
+{"protein": "MHKLAHTSFGIVGMFVNTCIVAKYVIINWEMFSMKKVNNDTVFGILQLETLLGDINSIFSEIESEYKMSREEILILLTLWQKGFMTLKEMDRFVEVKPYKRTRTYNNLVELEWIYKERPVDDERTVIIHFNEKLQQEKVELLNFISDAIASRATAMQNSLNAIIAV", "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": "MAMWRAAAGHLLGRALGSRAAHTSAGSKKIVGVFYKGGEYADKNPNFVGCVEGALGIREWLESKGHHYIVTDDKEGLNSELEKHIEDMHVLITTPFHPAYVSAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNTVSVAEDELMRILILLRNFLPGYQQVVHGEWNVAGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKIDPELEKEIGAKYEEDLDAMLPKCDVIVINTPLTEKTRGMFNKERIAKMKKGVIIVNNARGAIMDTQAVADACSSGQVAGYGGDVWFPQPAPKDHPWRYMPNHAMTPHISGTTIDAQLRYAAGVKDMLDRYFKGEDFPVQNYIVKEGQLASQYQ", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Involved in the cell stress response. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily."}
+{"protein": "PGLAAAIPAPPESQEKKPLKPCCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI", "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": "MARNFELSLILFVLYLSTAAIVMARNLEEESSGDTEFIKASCETTSYPDRCFQSLSSYASEIKKQPRKLAETALAVSIARAKSAKTYVSEMTDYKGITKRQHEAVADCLEEMGDTVDRLSNSLKELKHLEEGDSGEDFWFCLSNVRTWTSAALTDETACMDGFGGKAMAGELKSLIRTHIVSVAEETSNALALINDFASKH", "text": "FUNCTION: Pectin methylesterase (PME) inhibitor that can target the PME3 and may regulate homogalacturonan methylesterification during plant development. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the PMEI family."}
+{"protein": "MGKVWKQQMYPQYATYYYPQYLQAKQSLVPAHPMAPPSPSTTSSNNNSSSSSNSGWDQLSKTNLYIRGLPPNTTDQDLVKLCQPYGKIVSTKAILDKTTNKCKGYGFVDFDSPAAAQKAVSALKASGVQAQMAKQQEQDPTNLYISNLPLSMDEQELENMLKPFGQVISTRILRDSSGTSRGVGFARMESTEKCEAVIGHFNGKFIKTPPGVSAPTEPLLCKFADGGQKKRQNPNKYIPNGRPWHREGEAGMTLTYDPTTAAIQNGFYPSPYSIATNRMITQTSITPYIASPVSAYQVQSPSWMQPQPYILQHPGAVLTPSMEHTMSLQPASMISPLAQQMSHLSLGSTGTYMPATSAMQGAYLPQYTHVQTAAVPVEEASGQQQVTVETSNDHSPYTFQPNK", "text": "FUNCTION: Single-stranded DNA binding protein that interacts with the region upstream of the C-myc gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK", "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. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1- KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side."}
+{"protein": "MEGGVDARFYAILVTSGAEVNVATIIAERARALGLDIRSIIVPPRIKGYVILEAHDPGDVYDATRGLRHVKRRRPLILKFEEVMKLVKPEVEIPALKPGQVVEIVAGAFKGMKARVIDVNQSKGQVTVSLLEPLFRATATIPIDEVRPVEE", "text": "FUNCTION: Stimulates transcription elongation. SIMILARITY: Belongs to the archaeal Spt5 family."}
+{"protein": "MTWELHLLLLLGLGLRSQEALPPPCESQIYCHGELLHQVQMAQLYQDDKQFVDMSLATSPDEVLQKFSELATVHNHSIPKEQLQEFVQSHFQPVGQELQSWTPEDWKDSPQFLQKISDANLRVWAEELHKIWKKLGKKMKAEVLSYPERSSLIYSKHPFIVPGGRFVEFYYWDSYWVMEGLLLSEMASTVKGMLQNFLDLVKTYGHIPNGGRIYYLQRSQPPLLTLMMDRYVAHTKDVAFLQENIGTLASELDFWTVNRTVSVVSGGQSYVLNRYYVPYGGPRPESYRKDAELANSVPEGDRETLWAELKAGAESGWDFSSRWLVGGPDPDLLSSIRTSKMVPADLNAFLCQAEELMSNFYSRLGNDTEATKYRNLRAQRLAAMEAVLWDEQKGAWFDYDLEKGKKNLEFYPSNLSPLWAGCFSDPSVADKALKYLEDSKILTYQYGIPTSLRNTGQQWDFPNAWAPLQDLVIRGLAKSASPRTQEVAFQLAQNWIKTNFKVYSQKSAMFEKYDISNGGHPGGGGEYEVQEGFGWTNGLALMLLDRYGDQLTSGTQLASLGPHCLVAALLLSLLLQ", "text": "FUNCTION: Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the glycosyl hydrolase 37 family."}
+{"protein": "MTEIFSDTSIRQLSQMLLSLIFFHISEYILAITIHGASNVTLSSLLITKHYALAMLLSLLEYLTEIILFPGLKQHWWVSNFGLIMIIVGEIIRKAAIITAGRSFTHLIKINYEEHHGLVTHGVYRLMRHPSYCGFLIWSVGTQVMLCNPVSAVAFAVVVWRFFAQRIPYEEYFLNQFFGVQYLEYAESVASGVPFVN", "text": "FUNCTION: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues, resulting in the modulation of the function of prenylated proteins. Involved in negative regulation of abscisic acid signaling. Carboxyl methylation is a reversible and potentially regulated step in the post-translational modification of prenylated proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family."}
+{"protein": "MASATLAFSCSSLCATLKLPQNLNPLLLNVPPLSKPFSGVVSPPSLSRLSLLPVAAKRRRFQEIPEELKAEFEEFQRPPNQKPQLSDVLPDDFQAPEPGTPEYNDIINQFLPKKGPPPPREEIFAVVVIGSRQYIVIPGRWIYTQRLKGATVNDKIVLNKVLLVGTKASTYIGTPIVTNAAVHAVVEEQLLDDKVIVFKYKKKKNYRRNIGHRQPITRIKITGITGYEDYPASTLEAEVEAKEEAEAEAEAEAVPV", "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 bacterial ribosomal protein bL21 family."}
+{"protein": "MDKLKIAEWGEKLKTGGAQMSRMVSEKVKDMLQAPTLESKMVDEATLETLEEPNWGMNMRICAQINNDEFNGTEIVRAIKRKISGKSPVSQRLSLELLEACAMNCEKVFSEVASEKVLDEMVWLIKNGEADSENRKRAFQLIRAWGQSQDLTYLPVFHQTYMSLEGENGLHARGEENSMPGQSSLESLMQRPVPVPPPGSYPVPNQEQALGDDDGLDYNFGNLSIKDKKEQIEITRNSLELLSSMLNTEGKPNHTEDDLTVSLMEKCKQSQPLIQMIIESTTDDEGVLFEALHLNDELQQVLSSYKKPDETEKKASIVEQESSGSKDTGPKPTEQEEQEPVKKTGADDDKKHSEASGSSNKTVKEEKQAVKIELGLSSDEDEK", "text": "FUNCTION: Binds ubiquitin in vitro (PubMed:24316203). Might contribute to the loading of the ESCRT machinery (Probable). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TOM1 family."}
+{"protein": "MEKRKIILDCEPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRKQIVADNIHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERVGGPAGELFSDIMNFTLKTQFEYYGLAGGPVHDATCIGYLINPDGIKTQDMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH", "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": "MSLATRRFGAAAALLVAACVLCTAPAWAQNETTGTGMVKTKSAFRWIRPPPARPPPFRRPPPAQTPYVHKVEYTELQILCPQTIDSVTGYPMDDPRCNVPRATVAAGEEALTIRNEFELLNGDVLNVTLEEVDTPENPSRRRLLSIIREEQRTGRVLLATSAELPTPTFRLKSLKSILKGSQKEIYAGKPIDLRTIVYIMDFSSCKLSGWSAPATLTPEKVTSDMLRGASAPTNNLANYYGACSYEKTLFNPDNFLVLGPVPVPCIGGVTPPPRPPRPPRPPPRAGSTISSLSRRNDTYDDWWDLSKYCTASEQQAWERAAEAYAQAIVAQDPNSATGKKLQGILQWRERRRNIYILPPGVKCSWSGYADVTCTSATCSAYVRGYSDTNAMQVIMHEAMHNYGLEHAGRGTLEYGDATDVMGDFNKAGKGLLCPNAPNMYRIGWAKPINEPGVAPFQNATGAWGNLTAANFTTDPWIRGLVIPAQGTRDDNMIVVNVGAQSTRDGAMKATGAQAYYFSYRIKNTTAGGYDSGLTLDFHKKVLVHAYNGIQSERVFGFKSNLLDWGPNFQSRSNTWTSPFLAYNNGLGGGVRLVVQSTSDTQAVVDICRISENGKELSCDDGIDNDCDGLQDNEDPDCQ", "text": "FUNCTION: Mediates digestion of the cell walls of the 2 mating type gametes during mating as a necessary prelude to cell fusion. This enzyme acts specifically on the framework proteins (inner wall) of the cell wall, cleaving several model peptides at specific sites. SUBCELLULAR LOCATION: Periplasm. Secreted, cell wall. Note=Stored in the periplasm of gametes until its release. Secreted concurrently with release of the cell walls. SIMILARITY: Belongs to the peptidase M11 family."}
+{"protein": "MIQVLLVTICLAVFPYQVSSKTLKSGSVNEYEVVNPGTVTGLPKGAVKQPEKKHEPMKGNTLQKLPLCTTGPCCRQCKLKPAGTTCWRTSVSSHYCTGRSCECPSYPGNG", "text": "FUNCTION: Recombinant protein inhibits the adhesion of alpha-1/beta-1- K562 (ITGA1/ITGB1) cells to collagen IV with an IC(50) of 80 nM. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the disintegrin family. Short disintegrin subfamily."}
+{"protein": "MIRFEHVSKAYLGGRQALQGVTFHMQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDINLISRRSYRMLTLSDGHLHGGVGHE", "text": "FUNCTION: Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring. FUNCTION: Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Note=Associated with the membrane through an interaction with FtsX. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Note=Associated with the membrane through an interaction with FtsX (PubMed:10048040). Localizes to the septal ring at the later stages of cell growth and remains there until division is complete (PubMed:14729705). This localization is dependent on localization of FtsZ, FtsA and ZipA, but not on the downstream division proteins FtsK, FtsQ or FtsI (PubMed:14729705). SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MTPFSKALRCIQNSPAKQSWKTLGIMPKHGICLPLFSLHTRNSCGIGEFLDLIPMISWCRKHGFQIIQILPINDSGEDSSPYNSISSVALNPLYLSLASLPHAQSVAYANAKLRTMQQLSKLPYVHYPQVKAAKWEFLRDYYQYVVKIGALKDEDFEIFCEKEKYWLRPYTVFRSIKYHLKGAPVNNWPKAYTDIKNFTEFEKQFQDECSFFSYLQYLCFQQMSQVKAFADDNHVFLKGDLPILISKDSCDVWYYRQFFSSSGSAGAPPDIYNTEGQNWHLPIYNMHNLVQDNYTWWKARLRYAENFYSLYRLDHIVGLFRLWVWDTSGNGKFQPDDPKEYLPQGTDILTQILRASRMLPIGEDLGSVPTDVKETLVKLGICGTRIPRWERNWEGDGNFIPLGEYSPLSVTSLSTHDSDTLALWWRHAPKEAQKFAQFLGMFFTPVLAEEDQKHILTLSHKTSSIFHINLINDYLALCPDLVSNNLKYERINMPGTVSKNNWVYRIKPSVEEILTHDAFNANIADIFSKI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the disproportionating enzyme family."}
+{"protein": "MASNQQSYKAGETRGKAQEKTGQAMGTMRDKAEEGRDKTSQTAQTAQQKAHETAQSAKDKTSQTAQAAQQKAHETAQSAKEKTSQTAQTAQQKAHETTQAAKEKTSQAGDKAREAKDKAGSYLSETGEAIKNKAQDAAQYTKETAQGAAQYTKETAEAGRDKTGGFLSQTGEHVKQMAMGAADAVKHTFGMATEEEDKEHYPGSTTTTTATTRTTDPTHQTYQRK", "text": "FUNCTION: Involved dehydration tolerance. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the LEA type 4 family."}
+{"protein": "MLAFAARTVVKPLGLLKPSSLMKVSGRFKAHQDALPRLPVPPLQQSLDYYLKALQPIVSEEEWAHTKQLVDEFQTSGGVGERLQKGLERRAKKMENWLSEWWLKTAYLQFRQPVVIYSSPGVILPKQDFVDLQGQLRFAAKLIEGVLDFKSMIDNETLPVEFLGGQPLCMNQYYQILSSCRVPGPKQDSVVNFLKSKRPPTHITVVHNYQFFELDVYHSDGTPLTSDQIFVQLEKIWNSSLQSNKEPVGILTSNHRNTWAKAYNNLIKDKVNRESVNSIQKSIFTVCLDKQVPRVSDDVYRNHVAGQMLHGGGSKFNSGNRWFDKTLQFIVAEDGSCGMVYEHAAAEGPPIVALVDHVMEYTKKPELVRSPMVPLPMPKKLRFNITPEIKNDIEKAKQNLSIMIQDLDIMMLTFHHFGKDFPKSEKLSPDAFIQVALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASIDSLAFVKGMGDSTVPEQQKVELLRKAVQAHRAYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFNLSTSQVPAKTDCVMFFGPVVPDGYGICYNPMEAHINFSVSAYNSCAETNAARMAHYLEKALLDMRTLLQNHPRAKL", "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": "MSIKVDPVDTNFTVFIRLPFPRGDFVDPPPVEWNASKDQALWDILSRPSKGDIDWKALAENFDVTLQFLLQQAAWLYDRQLSQVRAQMRKVNTTQSTSPSPALGSVSGSAALSGQPQRETLATGSRAPSRQVSQQKDIPLRAPENRRTSFTSTTATNLTPGSRDPTRTGTPTIEDKEPRWDSFGRRPSAVRREQPPVASLPRSPPLEEEPLSSSSPEESGSDEEDTTRRAPLFKRFGKFSTQRSGLRDDEDNEEDTPAFLPLAREHEHTHHERPVQELSTTLRLDAERAAAQRRHPEQRAGPRAPVPTDSSTSSMSSGGRSSLPDGARPTSQGAPVLSPQSAAERQNSRKSTASGREASDGTPSMGSSFSDLDDASVTQSALEEALLSNMQHGGMASRMSTISHALRSRYLQ", "text": "FUNCTION: Plays a role in autophagy. Functions at the preautophagosomal structure (PAS) in order to form normal autophagosomes under starvation conditions. Also plays a role in mitophagy and regulation of filamentous growth (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure Note=Localizes also to other perivacuolar punctate structures. SIMILARITY: Belongs to the ATG29 family."}
+{"protein": "MRPYVILNAAMTLDGKIATATGSSEISGEEDLRRVHELRRECDAIMVGINTVLADDPRLTVHRVDAAPGDNPVRVVVDSMARTPPHFRVLNDEAPTVIGVSESAPPERVAELRKRAEVVVAGTRRVDLHLLLERLHGMGIERLMLEGGSTLNYSMLTGGLVDEVRVCIAPMIVGGRDARTLVDGEGIDEMADAIRLELKRSYTLGEDLIVEYTVKG", "text": "FUNCTION: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6- ribitylamino-4(3H)-pyrimidinone 5'-phosphate. SIMILARITY: Belongs to the HTP reductase family."}
+{"protein": "MMVAAQVIWGSFSLLRVLWCLLPQTGYIHPDEFFQSPEVMAEDILGVQATRPWEFYPSSSCRTVVFPLLTSGSTFWLLRLWEELGLWPGLVSGYMLLVGPRFLLTALSFALDWAVYDLAPLWGADRWNALCLLSGSYVTLVFYTRTFSNTIEGLLFTWLLVLVSPGVVRSPTSKKPTPGPRWHRYLLGVILAAGFFNRPTFLAFALAPLSLWGIHRASELGGIRALIQEALVLLPGAALAAVLCVATDSWYFSSLSRSTGVFLTPANFLYYNLDPQNLARHGTHARLTHLAVNGFLLFGVLHAQALQAAWQQLHACLRASPQTGLSRVRGARGLLSSSKSYLLLFYFTPLLLLSAFSHQEARFLIPLLVPLVLLCSPQTQPIPWKGTLVLFNILGALIFGCLHQGGLVPGLKYLEQIVHTPDLSGTTTHYTLLFTHTYMPPQHLLHLSGLGSPVEVVDMGGAEDRVLCQALNNFSRQPACQLAGEPWPCRLFVVTPGTNRHALEKCRFPLKNETLLFPHLTLEDPPALSSLLSGAWRKHLSLHVIELETPVVTKQPKAQP", "text": "FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers a fourth mannose to some trimannosyl- GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is facultative and only scarcely detected, suggesting that it only exists in some tissues (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGZ subfamily."}
+{"protein": "MIEDQALFGYARYGKVDDVVYPSVIASGNGINYGDSDIEILGDRIPRQILYPAKIKQEILETDKLVIIPNGAELVRKPKDLVRIIMDIHSRYGFSKLIMISGISDPYSIPALVYLGISFFDSSILEMEGKMGYRFTPFGIEKADHDVSSENAIFISDMMHIIQRSISDGTLRELIEKAVISSKAAEMVRIADYSYYQDFESVFPVRTPYIKANTIEDLYRPDLIRYRNYISESYVKPDADIALILPCSAKKPYSRSKSHQKVIGALGNLRRFIHEVIVTSPIGIVPRDLEETYPARFYDIPVIGLWYEDEKIMMKRMMSSYMGRNRYRKVIAFIPEDLDFITEAIPYPHEVIEFKSSNLQRLREVIQREIAGGKAVNQKVAKYNSILRYQFGEWILPLVSGYTIRRNYNQDMIVKDGKILFVYNENLGKFTINKASADMFIKNGKFLVEIDDFKPTSNVYAMGVVDATEDIRQEDEVVLVHSGEVRGVGIAKMPARAMIELKKGIAVKVR", "text": "FUNCTION: Functions in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the addition of L-lysine to the cyano group of 7- cyano-7-deazaguanine (preQ0)-modified tRNAs at position 15, to generate q0kN15-tRNA, a q0N lysine adduct identified as 7-N-[(5S)-5-amino-5- carboxypentyl]formamidino-7-deazaguanosine. SIMILARITY: Belongs to the archaeosine synthase type 1 family."}
+{"protein": "MFYNRWLGTWLAMSALIRISVSLPSSEEYKVAYELLPGLSEVPDPSNIPQMHAGHIPLRSEDADEQDSSDLEYFFWKFTNNDSNGNVDRPLIIWLNGGPGCSSMDGALVESGPFRVNSDGKLYLNEGSWISKGDLLFIDQPTGTGFSVEQNKDEGKIDKNKFDEDLEDVTKHFMDFLENYFKIFPEDLTRKIILSGESYAGQYIPFFANAILNHNKFSKIDGDTYDLKALLIGNGWIDPNTQSLSYLPFAMEKKLIDESNPNFKHLTNAHENCQNLINSASTDEAAHFSYQECENILNLLLSYTRESSQKGTADCLNMYNFNLKDSYPSCGMNWPKDISFVSKFFSTPGVIDSLHLDSDKIDHWKECTNSVGTKLSNPISKPSIHLLPGLLESGIEIVLFNGDKDLICNNKGVLDTIDNLKWGGIKGFSDDAVSFDWIHKSKSTDDSEEFSGYVKYDRNLTFVSVYNASHMVPFDKSLVSRGIVDIYSNDVMIIDNNGKNVMITTDDDSDQDATTESGDKPKENLEEEEQEAQNEEGKEKEGNKDKDGDDDNDNDDDDEDDHNSEGDDDDDDDDDEDDNNEKQSNQGLEDSRHKSSEYEQEEEEVEEFAEEISMYKHKAVVVTIVTFLIVVLGVYAYDRRVRRKARHTILVDPNNRQHDSPNKTVSWADDLESGLGAEDDLEQDEQLEGGAPISSTSNKAGSKLKTKKKKKYTSLPNTEIDESFEMTDF", "text": "FUNCTION: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase S10 family."}
+{"protein": "MSLIPSIFGGPRSNVFDPFSLDMWDPFKDFHVPTSSVSAENSAFVNTRVDWKETQEAHVLKADIPGLKKEEVKVQIEDDRVLQISGERNVEKEDKNDTWHRVDRSSGKFMRRFRLPENAKVEQVKACMENGVLTVTIPKEEVKKSDVKPIEISG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MNISRSEQRVLHVLAQGGYVRHQRADNGRILDVLCFTRDGHVLADCTLEVFVKLRRKRLIESKASSPYRISDKGRRSVRAQLDNR", "text": "SIMILARITY: Belongs to the UPF0386 family."}
+{"protein": "MTKIKQEIYNKRPTSPHLTIYKPQISSTLSILHRMTGVALFFVVSILVWWLILSKYDNNYLQLASCCIIKICLVAFSYSWCYHLCNGIRHLFWDIGYGFSIKAVNITGWCVVVCSILLTMLLWV", "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": "MARAVHRSGLVALGIATALMASCAFAAKDVVVAVGSNFTTLDPYDANDTLSQAVAKSFYQGLFGLDKEMKLKNVLAESYTVSDDGITYTVKLREGIKFQDGTDFNAVAVKANLDRASDPANHLKRYNLYKNIAKTEAIDPTTVKITLKQPFSAFINILVHPATAMISPTALEKYGKEIGFHPVGTGPYELDTWNQTDFVKVKKFAGYWQPGLPKLDSITWRPVADNNTRAAMLQTGEAQFAFPIPYEQATLLEKNKNIELMASPSIMQRYISMNVTQKPFDNPKVREALNYAINRPALVKVAFAGYATPATGVVPPSIAIAYAQSYKPWPYDPVKARELLKEAGYPNGFSTTLWSSHNHSTAQKVLQFTQQQLAQVGIKAQVTAMDAGQRAAEVEGKGQKESGVRMFYTGWSASTGEADWALSPLFASQNWPPTLFNTAFYSNKQVDDFLAQALKTNDPAEKTRLYKAAQDIIWQESPWIPLVVEKLVSAHSKNLTGFWIMPDTGFSFEDADLQ", "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": "MSNEPTSSFYELRLPPSDGISSVNFCPNSVNLLVTSWDSTVRCYDTQNNVQKWQYNHKGPVMDGCFPEKNKVFSGDVFGSVKHYDPVAGVEKEVGSHEDGVRSVVYNSDTQQLFTGGWDQQLKLWDIRSDKMEISNHDLQSKIFTMDVSPISNMLVIGTADKYVTIYDTRQMETHLQKRESSIKYQTRCIRTFTDGKGYALASVEGRIAMEYFDPSPAVQSKKYAFKCHRLTESGVDVVYPVNCIAFNPHYGTFATGGCDKNVFFWDGANRKRLHALKTYPTSISSMSFNTDGNILAVASSYTFEEGEKDHPPDQIFIHNILSEKIIKPIK", "text": "FUNCTION: Involved in cell cycle checkpoint enforcement. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat BUB3 family."}
+{"protein": "MQTATVLVEKSDYRPSEDEPFMNDRQLEYFKQKLLAWKEEILRESRETVSHLQKETENHADLADRASSETDRALELRTRDRQRKLISKIDQALRRVEDGSYGYCEETGEPIGLARLEARPTATMSVEAQERHERRERVHRDD", "text": "FUNCTION: Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DksA family."}
+{"protein": "MASRRRVLLKVIILGDSGVGKTSLMNQFVNRKFSNQYKATIGADFLTKEVQIDDRIFTLQIWDTAGQERFQSLGVAFYRGADCCVLVNDVNVMKSFENLNNWREEFLIQASPSDPENFPFVVLGNKTDVDGGKSRVVTEKKAKSWCASKGNIPYFETSAKDGVNVDAAFECIAKNALKNEPEEEVYLPDTIDVAGARQQRSTGCEC", "text": "FUNCTION: Intracellular vesicle trafficking and protein transport. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MSSDSPAAGDGGEQAAAGTSVPSPSYDKQKEKARVSRTSLILWHAHQNDAAAVRKLLEEDPTLVHARDYDKRTPLHVASLHGWIDVVKCLLEFGADVNAQDRWKNTPLADAEGARKQKMIELLKSHGGLSYGQNGSHFEPKPVPPPIPKKCDWEIEPAELDFSNAAMIGKGSFGEIVKAYWRGTPVAVKRILPSLSDDRLVIQDFRHEVDLLVKLRHPNIVQFLGAVTERKPLMLITEYLRGGDLHQYLKEKGGLTPTTAVNFALDIARGMTYLHNEPNVIIHRDLKPRNVLLVNSSADHLKVGDFGLSKLIKVQNSHDVYKMTGETGSYRYMAPEVFKHRRYDKKVDVFSFAMILYEMLEGEPPFANHEPYEAAKHVSDGHRPTFRSKGCTPDLRELIVKCWDADMNQRPSFLDILKRLEKIKETLPSDHHWGLFTS", "text": "FUNCTION: Serine/threonine protein kinase which may function as an adapter protein for BRL2 (PubMed:19000166). Required during vascular development for the establishment of vein pattern in foliar organs (PubMed:19000166). Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold (PubMed:21838775). SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MAMNTVFLHLSEEAIKRLNKLRGWRKVSRSAILREAVEQYLERQQFPVRKAKGGRQRDEAVGVEELCKQHKE", "text": "SIMILARITY: Belongs to the YiiE family."}
+{"protein": "MSWESGAGPGLGSQGMDLVWSAWYGKCVKGKGSLPLSAHGIVVAWLSRAEWDQVTVYLFCDDHKLQRYALNRITVWRSRSGNELPLAVASTADLIRCKLLDVTGGLGTDELRLLYGMALVRFVNLISERKTKFAKVPLKCLAQEVNIPDWIVDLRHELTHKKMPHINDCRRGCYFVLDWLQKTYWCRQLENSLRETWELEEFREGIEEEDQEEDKNIVVDDITEQKPEPQDDGKSTESDVKADGDSKGSEEVDSHCKKALSHKELYERARELLVSYEEEQFTVLEKFRYLPKAIKAWNNPSPRVECVLAELKGVTCENREAVLDAFLDDGFLVPTFEQLAALQIEYEDGQTEVQRGEGTDPKSHKNVDLNDVLVPKPFSQFWQPLLRGLHSQNFTQALLERMLSELPALGISGIRPTYILRWTVELIVANTKTGRNARRFSAGQWEARRGWRLFNCSASLDWPRMVESCLGSPCWASPQLLRIIFKAMGQGLPDEEQEKLLRICSIYTQSGENSLVQEGSEASPIGKSPYTLDSLYWSVKPASSSFGSEAKAQQQEEQGSVNDVKEEEKEEKEVLPDQVEEEEENDDQEEEEEDEDDEDDEEEDRMEVGPFSTGQESPTAENARLLAQKRGALQGSAWQVSSEDVRWDTFPLGRMPGQTEDPAELMLENYDTMYLLDQPVLEQRLEPSTCKTDTLGLSCGVGSGNCSNSSSSNFEGLLWSQGQLHGLKTGLQLF", "text": "FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. Required for maturation of the 28S rRNA. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Cytoplasm Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (By similarity). Localizes mainly to the granular component, the region implicated in the later steps of rRNA processing and subunit assembly and export. SIMILARITY: Belongs to the LAS1 family."}
+{"protein": "MTQEYDNKRPVLVLQNEALYPQRRSYTSEDEAWKSFLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRERRSSTAKPEVEHPEPDHSKRNSIPIVTEQPLISAGENRVQVLKNVPFNIVLPHGNQLGIDKRGHLTVPDTTVTVSIATMPTHSIKTETQPHGFTVGIPPAVYHPEPTERVVVFDRNLSTDQFSSGAQAPNAQRRTPDSTFSETFKEGVQEVFFPSDLSLRMPGMNSEDYVFDSVSGNNFEYTLEASKSLRQKPGDSTMTYLNKGQFYPITLKEVSSNEGIHHPISKVRSVTMVVFAEDKSREDQLRHWKYWHSRQHTAKQRCIDIADYKESFNTISNIEEIAYNAISFTWDINDEAKVFISVNCLSTDFSSQKGVKGLPLNIQIDTYSYNNRSNKPVHRAYCQIKVFCDKGAERKIRDEERKQSKRKVSDVKVPLLPSHKRMDITVFKPFIDLDTQPVLFIPDVHFASLQRGTHVLPIASEELEGEGSVLKRGPYSTEDDFAVPPSAKLARIEEPKRVLLYVRKESEEVFDALMLKTPSLKGLMEAISDKYDVPHDKIGKIFKKCKKGILVNMDDNIVKHYSNEDTFQLQIEEAGGSYKLTLIEI", "text": "FUNCTION: Transcription factor involved in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' (By similarity). Important regulator of DSG1 in the context of hair anchorage and epidermal differentiation, participates in the maintenance of the skin barrier. There is no genetic interaction with GRHL3, nor functional cooperativity due to diverse target gene selectivity during epithelia development (By similarity). May play a role in regulating glucose homeostasis and insulin signaling (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily."}
+{"protein": "MSTYSIPYYNQMNGNYNNGMPQQTTAANQQAFPQQQQPTTTGNASQQQQQAAATAAAAAVQQPYNYMFYQQQGQPGQQTGQTAGQQQQQQQQQQQYDYNTYNRYQYPAATSQGNYYQQTIPNQLSQPQPQHYNGSNRNYTSAPSGAPIPSNSTSGPSQQPPLPGQQAVPIPPHVSTMQQPTPVQDTLNASSTSTVGQFQPPGIRPRVTTTMWEDEKTLCYQVDANNVSVVRRADNNMINGTKLLNVAQMTRGRRDGILKSEKVRHVVKIGSMHLKGVWIPFERALAMAQREQIVDMLYPLFVRDIKRVIQTGVTPNAAAATAAAAATATSASAPPPPPPPVAAATTTAATAISKSSSGNGNSISATSGGSNVSGASGAGSTTSPVNTKAATTAGTPQGNYYQTYNQQQYPQQYGQYNAPGKNQNTPASQPGSTTNDQYLQQQQQMYGYQSNYYQGGAANSSYYPNYYQQQQPNYASSYPYQQQQQKQQQQQPNQQQQSDQQQTSTPSGGAGTRSVHQSPQVQSLTQGSVHPSPQQHQANQSASTVAKEEK", "text": "FUNCTION: Transcriptional regulator of the switch between 2 heritable states, the white and opaque states. These 2 cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically, at low frequency. Antagonizes the action of WOR1, WOR2 and CZF1, and promotes the white state. In white cells, EFG1 represses WOR1 indirectly through WOR2 to maintain white cell identity. Binds target gene promoters at the EFG1 recognition sequence (EGRbox) TATGCATA. Acts as a major regulator of cell wall dynamics and plays a role in interactions with extracellular matrices. Required for TOR1-dependent cellular aggregation and adhesin expression. Required for both normoxic and hypoxic biofilm formation. Hypoxic biofilm formation is a major cause of perseverance and antifungal resistance during infections. Contributes to virulence by regulating hyphal formation and the factors that enable C.albicans to invade and injure endothelial cells. Required for the formation of thick-walled big resting spores called chlamydospores, which survive in unfavorable conditions. Mediates the expression of virulence factors SAP4, SAP5and SAP6 during infection. Involved in drug resistance by regulating the expression of ERG3. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EFG1/PHD1/stuA family."}
+{"protein": "MAELNTHVNIKEKIYAVRSVVPNKSNNEIVLVLQQFDFNVDKAVQAFVDGSAIQVLKEWNMTGKKKNNKRKRSKSKQHQGNKDAKDKVERPEVGPLQPQAPLVQNGHMNGCEKDSSSPDSTREKLALTPREKKISILEEPPRAQRGVTEGGRLLQQKMSLDGNPRAIHGPSERSDGPQWSAGQPCNPSKPKAKTSPVKSNAPAAHLEIKPDELAKKRGPNIEKSVKDLQRCTVSLTRYRVMIKEEVDSSVKKIKAAFAELHNCIIDKEVSLMAEMDKVKEEAMDILTARQKKAEELKRLTDLASQMAEMQLAELRAEIKHFVSERKYDEELGKAARFSCDIEQLKAQILICGEITHPKNSYSSRTPCSSLLPLLNTHAVASGKQGNFARKSSGHNKPSEGKAANPKMVSGLANTADACHQTMPTNKQQNGPSSQRRRFNPQYHNRLNGPAKSQGGGNEADPMAKSNSRHEHRRQPHNGFRPKNKGGAKNQEAPLGTKAPEAPPHSEKARRRQHAADNLEARPFRGNVSRVSQCNLCPSRIEVSTEATVLSVPAVTLVA", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the SPATS2 family."}
+{"protein": "MPHTHSRHGSSGDDLCSTDEVKIFKDEGDREDEKISSENLLVEEKSSLIDLTESEEKGHKISRPDHSPVFNKLDTHAPSFNMGYLVSPYSYANGSPSGLPVTMANKIGLPPFFCHNADPLSTPPPAHCGIPPYQLDPKMGLTRPALYPFAGGQYPYPMLSSDMSQVASWHTPSVYSASSFRTPYPSSLPINTTLASDFPFRFSPSLLPSVHATSHHVINAHSAIVGVSSKQECGVQDPTTNNRYPRNLEAKHTSNAQSNESKETTNDKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHELSREEQSKYYEKARQERQLHMELYPGWSARDNYGYVSKKKKRKKDRSTTDSGGNNMKKCRARFGLDQQSQWCKPCRRKKKCIRYMEALNGNGPAEDGSCFDEHGSQLSDDDEDDYDDDKLGGSCGSADETNKIEDEDSESLNQSMPSPGCLSGLSSLQSPSTTMSLASPLNMNANSATNVIFPASSNALLIVGADQPTAQQRPTLVSTSGSSSGSTSSISTTPNTSSTVSPVTCMTGPCLGSSQERAMMLGNRFSHLGMGLSPPVVSTSTSKSEPFFKPHPTVCNNPIFALPSIGNCSLNISSMPNTSRNPIGANPRDINNPLSINQLTKRREYKNVELIEASESKTIVAHAATSIIQHVAVNGYHANHSLLNSNLGHLHHQLNNRTENPNRSEQTMLSVSNHSVNSSECHKESDSQAIVSSNPPNAGSSDNGVISVS", "text": "FUNCTION: Segment polarity protein. Functions together with arm to transduce the Wingless (Wg) signal in embryos and in developing adult tissues. Acts as a transcriptional activator, but in the absence of arm, it binds to gro and acts as a transcriptional repressor of wg- responsive genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TCF/LEF family."}
+{"protein": "MVKVTFNSALAQKEAKKDEPKSSEEALIVPPDAVAVDCKDPGDVVPVGQRRAWCWCMCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGLKYIKDDVILNEPSADAPAARYQTIEENIKIFEEDAVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPKNLLELLINIKAGTYLPQSYLIHEHMVITDRIENVDNLGFFIYRLCHDKETYKLQRRETIRGIQKREASNCFTIRHFENKFAVETLICS", "text": "FUNCTION: Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers. FUNCTION: Mature BRI2 (mBRI2) functions as a modulator of the amyloid- beta A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed amyloid-beta protein 40 and amyloid-beta protein 42. FUNCTION: Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites (By similarity). SUBCELLULAR LOCATION: [BRI2, membrane form]: Cell membrane; Single-pass type II membrane protein Endosome membrane; Single-pass type II membrane protein Note=Mature BRI2 (mBRI2) needs to be transported from the endoplasmic reticulum compartment to the cell membrane in order to be able to inhibit APP processing. SUBCELLULAR LOCATION: [Bri23 peptide]: Secreted Note=Detected in the cerebral spinal fluid (CSF). SUBCELLULAR LOCATION: [Integral membrane protein 2B]: Golgi apparatus membrane; Single-pass type II membrane protein Note=Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and Bri23 peptide is secreted. SUBCELLULAR LOCATION: [BRI2C, soluble form]: Secreted. SIMILARITY: Belongs to the ITM2 family."}
+{"protein": "MQNKFLICDDCQAVNCKSLERKLKKLDPEAEIEIGCQSYCGPGRRKTFAFVNNRPLAALTEDELMEKVEKQLQKPRDPEEEERLRKRNEERKRRKEEQDRKLKEKLAKRKQTKA", "text": "SIMILARITY: Belongs to the UPF0741 family."}
+{"protein": "MKPLHLKLNNFGPFLKEEIDFSKIDNNELFLISGKTGSGKTMIFDAMTYALFGKASTEQREENDLRSHFADGKQPMSVTFEFQLNHRIYKVHRQGPYIKEGNTTKTNAKFDVFEMVDGKYEIRESKVISGTQFIIELLGVNADQFRQLFILPQGEFKRFLISNSREKQGILRTLFDSEKFEAIREILKEEVKKEKAQIENRYQQIDLLWQEIESFDDDNIKGLLGVATQQIDKLIENIPLLQARSKEILASVNESKETAIKEFEIIEKKTLENNILKDNINQLNKNKIDFVQLKEQQPEIEGIEAKLKLLQDITNLLNYIENREKIETKIANSKKDISKTNNKILNLDCDKRNIDKEKKMLEENGDLIESKISFIDKTRVLFNDINKYQQSYLNIERLRTEGEQLGDELNDLIKGLETVEDSIGNNESDYEKIIELNNTITNINNEINIIKENEKAKAELDKLLGSKQELENQINEETSILKNLEIKLDRYDKTKLDLNDKESFISEIKSAVNIGDQCPICGNEIQDLGHHIDFDSIAKRQNEIKEIEANIHAIKSNIAVHNSEIKFVNEKISNINIKTQSDFSLEVLNKRLLENENALNNQRDLNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRDLITEFETLSKYNNITNFEVDYKKYVQDVNQHQELSKEIEDKLMQLSQRKLIEQNNLNHYENQLETYNNDLELNEQSIEMEMSRLNLTDDNDIDEIIAWRGEQEELEQKRDTYKKRYHEFEMEIARLESLTKDKELLDSDKLKDEYELKKGKMNTLIDEYSAVHYQCQNNINKTQSIVSHINYLNQELKDQQEIFQLAEIVGGKNNKNLTLENFVLIYYLDQIIAQANLRLATMSDNRYQLIRREAVSHGLSGLEIDVFDLHSNKSRHISSLSGGETFQSSLALALGLSEIVQQQSGGISLESIFIDEGFGTLDQETLETALDTLLNLKSTGRMVGIISHVSELKNRIPLVLEVKSDQYQSSTRFKRN", "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 SMC family. SbcC subfamily."}
+{"protein": "MTEIYDFDKSAWDIKGSIAPIQPTTYSDGRLVPQVRVIDPGLGDRKDECFMYMFLLGVVEDSDPLGPPIGRAFGSLPLGVGRSTAKPEKLLKEATELDIVVRRTAGLNEKLVFYNNTPLTLLTPWRKVLTTGSVFNANQVCSAVNLIPLDTPQRFRVVYMSITRLSDNGYYTVPRRMLEFRSVNAVAFNLLVTLRIDKAIGPGKIIDNTEQLPEATFMVHIGNFRRKKSEVYSADYCKMKIEKMGLVFALGGIGGTSLHIRSTGKMSKTLHAQLGFKKTLCYPLMDINEDLNRLLWRSRCKIVRIQAVLQPSVPQEFRIYDDVIINDDQGLFKVL", "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": "MVEVEHWNTLRLRIYIGENDRWEGKPLYKAIVEKLREMGIAGATVYRGIYGFGKKSRIHSSDVLRLSTDLPIVIEVVDRGHNIEKAVNVIKPMIKDGMITVEPTIVLWVGSKEEIKKFEEDAIAERR", "text": "SIMILARITY: Belongs to the UPF0166 family."}
+{"protein": "MVKSTTRKRTTLDEWDDVWLYLLVFGCLSVLVLVLVHRKLTRQKGTWSRGLRLDHLYRYSPADPITTGGGGKTTDSRGEVECRRFLETTFRVPFPKARPAFLRNPITGNNLEIDCFNPTIGLGVEYNGKQHYAFNDFFHRNKEAAMNQQYRDELKRRMCHENGVVLIEVPYTIKLSDIGPFLYARLKNLGFIAP", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the IIV-6 307L family."}
+{"protein": "MTRSLGKGPFVANHLLKEIEILNFGGSEEVVVTWSRASTIVPVMIGHTIAIHNGREHLPIYITDRMVGHKLGEFAPTRTFRGHARNDKKSRR", "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": "MDPVDPNLEPWNHPGSQPRTPCNKCHCKKCCYHCPVCFLNKGLGISYGRKKRRQRRGPPQGGQAHQVPIPKQPSSQPRGDPTGPKEQKKKVESEAETDP", "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": "FLAKKVAKKLVSHVAQKQLE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 04 subfamily."}
+{"protein": "MSSETTAPMIINEKSSLPVKSEPGQLGNPISDESSEDEQSQIRALEEDQGIYYNEEVVASPKNESDDDIPLRRIQLSHQTSTQQHPEDSEPQEVIDVNDIELPAGEAQPNMERRRSVRFSGRHDEEEDGRNKHFRTPSPESLRYIQALENPMAANGEFEEEFNDLADPQVQPPPMGSPPAYTSADEGPKTPPPRASAGSNMRQESMNELIMRKISDPLQNLIRRASRLEDDSSNDDDDDDDDEDDDYTEDEIAILTYIDAYKTQEVELRPQLRPFTIEYIPAMGDVDLFIKVPRPDEIDDNVGLTQIDEPPSNQSDATIVDMQIRNATKDAAILDDDVPVKLLERADENPDEIKKWISDIKEFHKSKPAQTVHYRTQLPDVETLMQEWPQKLEEVLKTTKIPSAELDVSLEKYVEICLNIVDIPVGKSRIEALHLMFSLLNEFNNSQHFRNLAQNNNLGGETGETMDRLEL", "text": "FUNCTION: Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium (PubMed:28479320). May be required for ciliary entrance and transport of specific ciliary cargo proteins such as che-3 which are related to motility (PubMed:28479320). Required for normal morphology and function of ciliated amphid sensory neurons (PubMed:16648645, PubMed:7705621). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Cell projection, dendrite Perikaryon Note=Highly expressed in the transition zones between the cilium basal body and the dendrites. SIMILARITY: Belongs to the IFT46 family."}
+{"protein": "MDVLTSAADFKKSKVPQLQELDDLLRCHICKDFLKNPVLTPCGHTFCSLCIRGYLSNEPKCPLCLHELRESMLRSEYLVNEITETYKAARQRLLDELNSLETNQDNSVIEVVSDKEPSLLQIDDDVNENSNHITVNDTSDIIDEDNEIQITGTKRTARTILNGSRPTKAAKISDMFTTRKAKTEEKAPCPICSQLFPIRYLERTHLDECLTKPPTSSPPIKQSRLSPKPSESVSHVKRYLNSTNTSTQQRLPKLNFAKMTTSQLKQKLASLSLPVSGTRANMVARYNYYEMLWNSNFIDSINPVSESELRRQLMSWDASHNGNNNSSNGGTNTISQLMKMNSKNKGKEYEKLLKDFKKDSFDKKGWMLLHKNSFNRLLCDAKKTRRKTENETLMTSQSPRESSTQTELSAT", "text": "FUNCTION: E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RAD18 family."}
+{"protein": "MKKTQTWIITCIYLQLLLFNPLVRTQGICRNRVTDDVKDVTKLVANLPKDYKITLKYVPGMDVLPSHCWISEMVEQLSVSLTDLLDKFSNISEGLSNYSIIDKLVKIVDDLVECMEEHSFENVKKSSKSPEPRLFTPEKFFGIFNRSIDAFKDLEMVAPKTSECVISSTLTPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKASDSIEDSSLQWAAVALPAFFSLVIGFAFGALYWKKKQPNLTRTVENIQINEEDNEISMLQEKEREFQEV", "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 (By similarity). SUBCELLULAR LOCATION: 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": "MAFLKKSLFLVLFLGLVSLSICEEEKRETEEEENDQEEDDKSEEKRFLSLLPSLVSGAVSLVKKLG", "text": "FUNCTION: Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Phylloseptin subfamily."}
+{"protein": "MADITLISGSTLGGAEYVAEHLAEKLEEAGFTTETLHGPLLEDLSASGIWLVISSTHGAGDIPDNLSPFYEALQEQKPDLSAVRFGAIGIGSREYDTFCGAIDKLEAELKNSGAKQTGETLKINILDHDIPEDPAEEWLGSWINLLK", "text": "FUNCTION: Probable electron transporter required for biotin synthase activity. SIMILARITY: Belongs to the flavodoxin family. MioC subfamily."}
+{"protein": "MEAQVPLSTDILVIGGGPAGSYAAAVLAREGFKVVLLEKDVFPRYHIGESMLPSCRPFLRFIDFEEKMKNYGFFPKPGAALKLNQDKREGYTDFTANGPDNAAWNVVRSEFDDLLLRHAAELGVHVYEGVQVEKIHFSPDESTRPVSLAWSKGDGTQGDVSFNWLVDASGRNGIMSTRYLKNRTFNKSLKNVAVWGYWTGAGRYAPGTKRENAPWFEALTDETGWAWFIPLHNGATSVGVVLAEDESKRKKAQHRAESNGKSLSEVQHDCYMADLQRAPGLIQLLGSEAKFEGKLMSAGDYSYHASEYAGSHFRIAGDAGAFIDPFFSSGIHLALTGGLSAASTIAASIRGNCTEEEACAFHSSKVETAYTRFLFVVLGIYKQIRAQETAVLYEAEEDNFDRAIDSLRPVIQGCADADENLTEAELQSTLDFCRSVLAPNQQQNNLRTPVDTGAADVKAKHAPSETDAQNPLQSMDDCKRNFGTEVINGFYVKMEQGMLGLVCA", "text": "FUNCTION: Flavin-dependent halogenase involved in the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols. The halogenase catalyzes the transfer of a single chlorine atom to the melleolide backbone, resulting in a 6'-chloromelleolide product. The enzyme acts on free substrate and does not depend on carrier-protein-dependent acceptor molecules. SIMILARITY: Belongs to the flavin-dependent halogenase family."}
+{"protein": "MEEYEAQLLVVEQALENAADDAQRQELLALKNNLQELLALTRDTGDEAPTDELPQQGNDLDDELQRLKSELSALEAAGSSQTALDEERQLADLRTKYTAMVGEKCSAPHEHSWGTCYHNALICGVDDEVVINSEGVLDARLRVLFTNPTHREMLPCSYYLEGECRFDEAKCRFSHGALVTGSSIRKYNPPDFHKLSRSRPVFALLPDRLWHRGRVLCVNFVEQVCRVRLDGQDHKERERDFKFEELYPLTTDQDEDDELSSEESTSSMRDASSDEAESDMDDLEEARRARMVELSLFTYKPTDRLGAWEEFTRGIGSKLMEKMGYIHGTGLGSDGRGIVTPVSAQILPQGRSLDACMELREAANGDKDYFSVERKLKRAQRRQRKADEKAYVRESQRVDVFTFLNDRVLGPGESTQQSEQVAKKAKTNELQQHSTKTLNVETVRIADEIRRKQRDMAKVKQSLERNSGDAQLQKRLQVQMQSHKQELATLQAQERSLSKEQQTRKSKNKMFEF", "text": "FUNCTION: Transcription repressor. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MRRYLILIVALIGITGLSGCYQTSHKKVRFDEGSYTNFIYDNKSYFVTDKEIPQENVNNSKVKFYKLLIVDMKSEKLLSSSNKNSVTLVLNNIYEASDKSLCMGINDRYYKILPESDKGAVKALRLQNFDVTSDISDDNFVIDKNDSRKIDYMGNIYSISDTTVSDEELGEYQDVLAEVRVFDSVSGKSIPRSEWGRIDKDGSNSKQSRTEWDYGEIHSIRGKSLTEAFAVEINDDFKLATKVGN", "text": "FUNCTION: Involved in immunity against exogenously supplied nisin. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
+{"protein": "MFLDYFALGVLIFVFLVIFYGIIILHDIPYLIAKKRNHPHADAIHVAGWVSLFTLHVIWPFLWIWATLYRPERGWGMQSHDSSVMQLQQRIAGLEKQLADIKSSSAE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: To E.coli YibI."}
+{"protein": "MEQIPASIWTLTAGVVVTLISFWVGHHHGLLPEQASEQAPLVDNFFDIMLTIGTALFLVVQGAIILFVIRYRRRAGEEGDGLPVEGNLPLEAFWTAIPALIVIFLGIYSVDIFQRMGGLNPGDHAMHSMHAPKSGMAVVAQAPSKTTSDATALLAAAQPPEIGIGASPDVQGKAPDLVVDVAGMQYAWIFTYPDSGIVSGELHIPVGKDVQLNLSARDVIHSFWVPQFRLKQDAIPGVPTTRFKATKVGTYPVVCAELCGGYHGAMRTQVIVHTPEDFETWRRQNQAIATAPVIPSLRDRHIHEMGVTAELVAQVEAIAHDPSAEKL", "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": "MPVPASWPHLPSPFLLMTLLLGRLTGVAGEDELQVIQPEKSVSVAAGESATLRCAMTSLIPVGPIMWFRGAGAGRELIYNQKEGHFPRVTTVSELTKRNNLDFSISISNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAVRATPEHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPAGDSVSYSIHSTARVVLTRGDVHSQVICEIAHITLQGDPLRGTANLSEAIRVPPTLEVTQQPMRAENQANVTCQVSNFYPRGLQLTWLENGNVSRTETASTLIENKDGTYNWMSWLLVNTCAHRDDVVLTCQVEHDGQQAVSKSYALEISAHQKEHGSDITHEAALAPTAPLLVALLLGPKLLLVVGVSAIYICWKQKA", "text": "FUNCTION: Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK. Triggers activation of myeloid cells when associated with TYROBP (PubMed:10604985). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MDRDEEPLSARPALETESLRFLHVTVGSLLASYGWYILFSCILLYIVIQRLSLRLRALRQRQLDQAETVLEPDVVVKRQEALAAARLRMQEDLNAQVEKHKEKLRQLEEEKRRQKIEMWDSMQEGRSYKRNSGRPQEEDGPGPSTSSVIPKGKSDKKPLRGGGYNPLTGEGGGTCSWRPGRRGPSSGGUN", "text": "FUNCTION: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Cytoplasm. SIMILARITY: Belongs to the selenoprotein S family."}
+{"protein": "MASLQTPVMVGTVVGCVAGVVGFLAMSSNAATSLSVAPASTSTQIIANPSVIAPQYQGSVTSEDVAMEASQTDFAEVAEISSPVQVQSWSMIFSAMLAVPLAAAAMFFMKKSTTEERRPLVSIDDLLSVGKKAVVASAVVGAAAGSANAYPIFAQQAYGNPREATGRIVCANCHLASKPTEIEVPQAVLPDQVFEAVTKVPFSGPSGFFNVVDPSTVVGSVTFAGTQPVGFIQESGVPVSQALVDIATPGTPDTVFKATIKVPYDESLKQVAGNGRAAPLNVGAVLILPEGFRLAPPERIPEKMKEEINGLQFIQYSKDTPNILVVGPVPGKKYAEMTVALLSPDPRVDKKAEFGTLPIYVGGNRGRGQLYPTGEKSNNNIYNVEHSGKIADIQLNEKKRIYTVAVQQKDGEIINEDLPAGAELIVKVGDVVEAGQAISTNPNVGGFGQAESEIVLQNPGRVQAFLFFSFTVLATQTLLVVKKKQYEQVQLSEMNF", "text": "FUNCTION: Translocates protons across the thylakoid membrane and transfers electrons from photosystem II to photosystem I. It receives electrons from the Rieske iron-sulfur protein and passes them to plastocyanin. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome f family."}
+{"protein": "MPPMPSAPPVHPPPDGGWGWIVVGAAFISIGFSYAFPKAVTVFFKEIQQIFHTTYSEIAWISSIMLAVMYAGGPVSSVLVNKYGSRPVVIAGGLLCCLGMVLASFSSSVVQLYLTMGFITGLGLAFNLQPALTIIGKYFYRKRPMANGLAMAGSPVFLSSLAPFNQYLFNTFGWKGSFLILGSLLLNACVAGSLMRPLGPNQTTSKSKNKTGKTEDDSSPKKIKTKKSTWEKVNKYLDFSLFKHRGFLIYLSGNVIMFLGFFAPIIFLAPYAKDQGIDEYSAAFLLSVMAFVDMFARPSVGLIANSKYIRPRIQYFFSFAIMFNGVCHLLCPLAQDYTSLVLYAVFFGLGFGSVSSVLFETLMDLVGAPRFSSAVGLVTIVECGPVLLGPPLAGKLVDLTGEYKYMYMSCGAIVVAASVWLLIGNAINYRLLAKERKEENARQKTRESEPLSKSKHSEDVNVKVSNAQSVTSERETNI", "text": "FUNCTION: Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L- lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate (PubMed:9786900, PubMed:32415067). Dimerization is functionally required and both subunits work cooperatively in transporting substrate (PubMed:32415067). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Cytoplasm Note=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (By similarity). SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
+{"protein": "MFKKFDEKESVSNCIQLKTSVIKGIKSQLTEQFPGIEPWLNQIMPKKDPVKIVRCHEHMEILTVNGELLFFRQRKGPFYPTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAKLYTAAVDTIVAVMAEGKEHALCVGVMKMAAADIEKINKGIGIENIHYLNDGLWHMKTYK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MCTS1 family."}
+{"protein": "MAKQVLTYIDAKEFAYIIDSISVLVEEANFLIRNDGLYLRALDVSRTAMVDLAIPKESFEEFPEVEELRFGLNFKELKKLLRRVKKGDKISMEFEEGRVRIKLIGKSVRSIVVPSIEVVGEELPTPKVVYTAMVKAASDVLATAVKDADAVADEVKFEASEEALIISASSDKGEVEVKLDKNSELVYEFDVKEPASARFSLEYLVDITSKTSKISDIVTIELATAKPIYLSFDIPAGGKISYFIAPRVE", "text": "FUNCTION: Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. SIMILARITY: Belongs to the PCNA family."}
+{"protein": "MKSYPFVTSDRSKNRKRHFNAPSHIRRKTLSSPLSKELRQKYNVRSMPIRKDDEVQVVRGHYKGQQIGKVVQVYRKKYVIYIERVQREKANGTTVHVGIHPSKVVITRLKLDKDRKKILERKAKSRQVGKEKGKYKEETNEKMQE", "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 uL24 family."}
+{"protein": "MAKESTTIDVGEPSTVTKSSSHVVKDAKKKGFVAVASRGGAKRGLAIFDFLLRLAAIAVTIGAASVMYTAEETLPFFTQFLQFQAGYDDLPAFQYFVIAVAVVASYLVLSLPFSIVSIVRPHAVAPRLILLICDTLVVTLNTSAAAAAASITYLAHNGNQSTNWLPICQQFGDFCQNVSTAVVADSIAILFFIVLIIISAIALKRH", "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. 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. SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP) family."}
+{"protein": "MLRKHPIISITGSSGAGTTSVKRTFEQIFRRENVVAAYIEGDAFHRYNRAEMRTRMAEESDKGNKHFSHFSPETNLFAELEGVFRSYGETGTGNTRYYVHDDAESALHGVPPGTFTDWQPLPDASDLLFYEGLHGAVVTDKVNVAQYADLKIGVVPVINLEWIQKLHRDRNARGYSTEAVTDTILRRMPDYVNYICPQFAETDINFQRVPTVDTSNPFISRWIPTPDESMVVIRLKNPRGIDFPYLLSMIPSSFMSRANSIVIHGSKLDLAMQLILTPLILQLIERKKRA", "text": "SIMILARITY: Belongs to the phosphoribulokinase family."}
+{"protein": "MYIQLLCFFLFLFLLLQATMSKRSFKKFVEQELGSLPHFLIYTVLEWSLIVFLFIDGVIAFLSNQFAKFFDLNIPCLLCTRIDHILVPRDPQFYYNESICDSHKKKVSSLAYCHVHKKLSEIKHMCEGCLLSFATEKDSDCDTYKSLIGILHKDLELLIDDERDLPLAFKKDDNLVQTTKNLVDYKTNNIKNDSLKQHCSCCGELLKIKSEKLPKNNNSFLAPAPSPRVSHNKLSENESEFKDMDVDRTPSFVRGGNKFFGIPLSDSAQNSPRWSVRSLKKSVLNKTENASDTTDPTGESILNQLKKEVRLDKKSLIDLYMELDEERSASAVAANEAMAMITRLQAEKAAVQMEALQYQRMMDEQAEYDQEALQSMSSELAKREEEMKELEAEFEVYREKYGCLTDQEDAREEFHKQNGNASAYDDCQETKPVSDLAVSSSNQQENGENIDQNGQSKRSEESTAENVVSADEEKGSESKEGIVKELSEITERLSTLQSNGDLLKHIADVLDVSEGEAILLQISQNLHMLRSFVAMPSESMNL", "text": "FUNCTION: Probable membrane-anchored myosin receptors. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
+{"protein": "MPRGSEAGYCCLSRDSNMPDSRDDQQQGASLGTSQDNSQTSSLIDGQTLSKESPSHGLELSAPEKARAASLDGAEEALWTTRADGRVRLRLEPFCTQRPYTVHQMFYEALDKYGNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYISHDCRANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDALKGTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPSNDLKPFTSRLADYLVLARVRQALGFAKCQKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGIGEICLWGRTIFMGYLNMEDKTCEAIDSEGWLHTGDMGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISSAMLIGDQRKFLSMLLTLKCTLDPETSEPTDSLTEQAVEFCQRVGSKASTVSEIVGQRDEAVYQAIHEGIQRVNANAAARPYHIQKWAILQRDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQEQKQ", "text": "FUNCTION: Catalyzes the conversion of fatty acids such as long-chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (By similarity) (PubMed:11112418, PubMed:12975357, PubMed:14516277). Can activate diverse saturated, monosaturated and polyunsaturated fatty acids (PubMed:11112418, PubMed:14516277). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle. Microsome. Endoplasmic reticulum Cell membrane. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. Bubblegum subfamily."}
+{"protein": "MESRMDQYEIMEQVGRGAFGAAILVNHKIERKKYVLKKIRLARQTERCRKSAHQEMALIARLQHPYIVEFKEAWVEKGCYVCIVTGYCEGGDMDELMKKLNGTYFPEEKLLKWFAQLVLAVDYLHSNYVLHRDLKCSNIFLTKDQDIRLGDFGLAKTLKEDDLTSSVVGTPNYMCPELLTDIPYGFKSDIWSLGCCMYEMAAHRPAFKAFDMAGLISKINRSSIGPLPACYSSSMKTLIKSMLRKSPEHRPTASEILKNPYLQPYVNQCRPLSDAPTPIRMPEKPLSTSRSNQRCTSESQSSSISCSDIDSTQSSDRSTSGGAPSTDSKLNDIRSIQDADRADSDEKCVTPEDLRGNKNISGAELKRQDSSKSVHQHHRGESKQPKIIEKIMTTLREESRLRENNSPVSSSGVKLTSAVSNKNQAEQSSESSRPHSGVSYSSKFGDISSNGWTNTSDECVDPVQVPLQLKQLSPTVEHCPKLKNSGSSTPEPAKQIAENGSSASGMSKTKSSPSSSRRPSPQRQTVAGIPIVPFTVSKRAHIKAESEKTPPRPAHSPNNSLHNLPPLIPISTNLSEENIKLGNSQAMPAPLEFVTAASKEDISFYSNSVVDCVEKAEPSEVFESNSPAYLTPPWTGPVLDAKGENGLIAIPCSEIHTGTLQKSMASNDDSSLSSPLDTFYLSFEQEFVCKDDSQSSKHGHSAVTLLSGEDKFTVQELLASTPVISPFVSSTSNTLPEDKSSYQSFKKQSDSHSGPPVDVPAQTIRLNSFLVSDEWPTSETVQGEARDTAASKLLNVVREDFDVRSSSCSTSTQPSGQTPVRSKLNVPETNLASNISIPSISEAVRLSTAMDVKPYTSEASNGVKEEASPAKEALDVTSFRQRAEALEGLLELSADLLENNRLEELAIVLQPFGKNKVSPRETAIWLARSFKGMMNEEGGRLSM", "text": "FUNCTION: May be involved in plant development processes. SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily."}
+{"protein": "MSGFFTSLDPRRVQWGAAWYAMHSRILRTKPVESMLEGTGTTTAHGTKLAQVLTTVDLISLGVGSCVGTGMYVVSGLVAKEMAGPGVIVSFIIAAVASILSGVCYAEFGVRVPKTTGSAYTYSYVTVGEFVAFFIGWNLILEYLIGTAAGASALSSMFDSLANHTISRWMADSVGTLNGLGKGEESYPDLLALLIAVIVTIIVALGVKNSIGFNNVLNVLNLAVWVFIMIAGLFFINGKYWAEGQFLPHGWSGVLQGAATCFYAFIGFDIIATTGEEAKNPNTSIPYAITASLVICLTAYVSVSVILTLMVPYYTIDTESPLMEMFVAHGFYAAKFVVAIGSVAGLTVSLLGSLFPMPRVIYAMAGDGLLFRFLAHVSSYTETPVVACIVSGFLAALLALLVSLRDLIEMMSIGTLLAYTLVSVCVLLLRYQPESDIDGFVKFLSEEHTKKKEGILADCEKEACSPVSEGDEFSGPATNTCGAKNLPSLGDNEMLIGKSDKSTYNVNHPNYGTVDMTTGIEADESENIYLIKLKKLIGPHYYTMRIRLGLPGKMDRPTAATGHTVTICVLLLFILMFIFCSFIIFGSDYISEQSWWAILLVVLMVLLISTLVFVILQQPENPKKLPYMAPCLPFVPAFAMLVNIYLMLKLSTITWIRFAVWCFVGLLIYFGYGIWNSTLEISAREEALHQSTYQRYDVDDPFSVEEGFSYATEGESQEDWGGPTEDKGFYYQQMSDAKANGRTSSKAKSKSKHKQNSEALIANDELDYSPE", "text": "FUNCTION: May be involved in arginine transport. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Note=Exhibits a punctated pattern in the cytoplasm, which partially ovelaps with lysosomes. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family."}
+{"protein": "MGLTFTKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIASKA", "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": "MLSPSQSLQYQKESVERALTCANCGQKLHVLEVHVCEACCAELMSDPNSSMYEEEDDG", "text": "SIMILARITY: Belongs to the ninF family."}
+{"protein": "MKKIIFICFSLLLALTGGCSMNDNDKNSTNDNKTEAVKPKDMDPKDLPQVPAFQDEKTREYMVSTKEEEPGYYLLESKLKGFRMLFPEDGKYLSRRSSLTGKNKESIGFNSYDKDTNVMFDGHVTYYKEESFANEPKTMLDIVSGKNDYKGEYKKSSKKKTDIYTAKKKDIFDDIDRKYNYSYSYFGYVKSTEEDNLGVEYAFTLGCKNENQPCSLDEEKAKNKVEKLINSITFLIDKKEK", "text": "FUNCTION: Required for complex colony architecture. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
+{"protein": "MGIPMQIYQDGKGVQFYHTRYQNVFDERASKYGNYTVNNDYPQLPDTIKEHIDQLTFSNVGEDGGDVGNYSEEDDDGDEEKELEDVFRSNRGLEFVRINNYFTTHDLQSFKSFRNFNSKYWIFYSNQAEDKKLLLYDFNGQHLIFIKQQFYGQLNLLLSDAIICMDCNFGYNSNTIQILVGFQNGKLLKLNCDLNGNVNNHLLLKDPSTSSHQSHLSILNVWAGLLPHFVVSFSLKDGLLITSLDHQQSNGSFQSFHTNIDLPVDLRTTTNVKSVLNFPQFTLYKGNDMIFHCKNLLGSDASTLNKEINFMLKIDEDVQKIDYLLKTNHILLETNMRYLSIPTRDPIENSNSSPPVSDSEVYPIFYKTQELHVHASGTGRQIANNGKYIFITEQHLYGTALSVYKYSISFKRWLFVGYSDIRAKYGIRSVKDLFVGNCPSVNSPVLTILTDDNNIQTILLK", "text": "FUNCTION: Involved in the regulation of anaerobiotic glycerol metabolism. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MTVTQEASPKRESLHIIDDRTGSYYSIPIVNNAINASDFKKVTAPEDKAYPANQTENGLRVYDPGYSNTAVSHSKITYIDGLKGTIQYRGYSINDIVGRKTFIDTAHLLIWGHWPSTAEAETLQQRLDQVPVPQDFVFNVIKSFPRDGSLMGMVIAGLSALQSSDMNAIPAHVGKTIYLNNPELADQQIIRVMANMSMLTAAAYCHHIGRDFTPPRAGLSYIENFLLMTGHVEAATGLPNPRYVNAIERLWVLIADHEMTCSTAALLQTASALPDVISCMVSAISALYGPLHGGAIEVAYKNIESIGSISNVPAKIARVKAGKERLYGYGHRVYRVTDPRFVFIREILNELSEEVEKDPLLKVAFEVDRVASEDEYFTSRNLRPNADLFAAFVYKALGFPPEFILPLSILSRTQGFMAHWREAMGNPPRIWRPGQIYTGDLNKSMDE", "text": "FUNCTION: Citrate synthase-like protein; part of the gene cluster that mediates the biosynthesis of oryzines, natural products with an unusual maleidride backbone (PubMed:30104550). The two subunits of the fungal fatty acid synthase oryfasA and oryfasB probably form octenoic acid (Probable). This fatty acid is most likely activated by the acyl-CoA ligase oryP to give octenyl-CoA before the citrate synthase-like protein oryE catalyzes condensation with oxaloacetate to form tricarboxylic acid (Probable). The next steps of the pathways are conjectural, but a favorite possible route has been proposed, beginning with decarboxylation and concomitant dehydration by the decarboxylase oryM, followed by tautomerization, which may lead to the production of a diene intermediate (Probable). Reduction of this diene intermediate could give the known metabolite piliformic acid (Probable). On the pathway to oryzine B and oryzine A, however, hydroxylation of the diene by the alpha-ketoglutarate-dependent dioxygenase oryG and lactonisation by the lactonohydrolases oryH or oryL could give oryzine B directly (Probable). Finally, enoyl reduction by the dehydrogenase oryD would then convert oryzine B into oryzine A (Probable). SIMILARITY: Belongs to the citrate synthase family."}
+{"protein": "MKSFVSVPQNSDFPIQNLPYGVFSTKADSSRHIGVAIGDQILNLAEIANLFDGPQLKAHQDVFKQSTLNAFMALPRPAWLEARARIQQLLSEDCAVLRDNAHLRSRALVAQSDATMHLPAQIGDYTDFYSSIHHATNVGIMFRGKENALMPNWKWLPVGYHGRASSIVVSGTDLKRPVGQTKAPDAEVPSFGPSKLMDFELEMAFFVGGPENELGTRVPIEKAEDRIFGVVLMNDWSARDIQAWEYVPLGPFLAKSFATTVSPWVVSIEALRPYFVENPVQDPVPPAYLHHDDPFTLDINLAVSIRPEGDAVDHIVCKTNFKHLYWTLKQQLAHHTVNGCNLRAGDLLGSGTVSGPEEGAYGSMLELSWRGAKEVPVGSEIRKFLKDGDEVNLSGVCEKNGVRIGFGECRGKVLPADI", "text": "FUNCTION: Fumarylacetoacetase involved in the tyrosine degradation pathway. SIMILARITY: Belongs to the FAH family."}
+{"protein": "MEQKQRRFTKNIFVLDANAKTLCGRIAKLSSQPYCQIKIGRVIAFKPVKNPEPKGYVLNVPGPGAYRIQDGQDIISLMLTPHGVEATTERWEEWKFEGVSVTPMATRVQHNGVMVDAEIKYCKGMGIVQPYMRNDFDRNEMPDLPGVMRSNYDIRELRQKIKNERESAPRLQVQSVAPREESRWMDDDEAKVDEEAREMIPGTSRLEKLREARSNVFKEVAAGINWNLDEKDEEDGDEREDEERVKTLSDDDEQGEDASDDEHPKTHITKEYVEKVAKQIKLKDERFMSLSSAMPQASGGFDRMIVTKKLKWQNVPLYCFDESSKRYELQCVGACERVAFVSKDMSLIILRSAFRRL", "text": "FUNCTION: Single-stranded RNA-binding protein. SIMILARITY: Belongs to the orbivirus non-structural protein NS2 family."}
+{"protein": "MKPYKSKINKIRSFALALIFIGFIVMYGGIFFKNSPILVLIFMTLGVLCIIGSTVVYAWIGLLSTRAIQVECPNCHKHTKVLGRVDMCMYCNEPLTLDPTLEGKEFDQSYNHKTKKS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0295 family."}
+{"protein": "MAGDSVKSAIIGIAGGPFSGKTQLCEQLLERLKSSAPSTFSKLIHLTSFLYPNSVDRYALSSYDIEAFKKVLSLISQGAEKICLPDGSCIKLPVDQNRIILIEGYYLLLPELLPYYTSKIFVYEDADTRLERCVLQRVKAEKGDLTKVLNDFVTLSKPAYDSSIHPTRENADIILPQKENIDTALLFVSQHLQDILAEMNKTSSSNTVKYDTQHETYMKLAHEILNLGPYFVIQPRSPGSCVFVYKGEVIGRGFNETNCSLSGIRHAELIAIEKILEHYPASVFKETTLYVTVEPCLMCAAALKQLHIKAVYFGCGNDRFGGCGSVFSINKDQSIDPSYPVYPGLFYSEAVMLMREFYVQENVKAPVPQSKKQRVLKREVKSLDLSRFK", "text": "FUNCTION: Deaminates adenosine-34 to inosine in many tRNAs. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family. ADAT2 subfamily."}
+{"protein": "MADADEGFGLARTPLEPDSKDRSCDSKPESALGAPSKSPSSPQAAFTQQGMEGIKVFLHERELWLKFHEVGTEMIITKAGRQMFPSYKVKVTGLNPKTKYILLMDIVPADDHRYKFADNKWSVTGKAEPAMPGRLYVHPDSPATGAHWMRQLVSFQKLKLTNNHLDPFGHIILNSMHKYQPRLHIVKADENNGFGSKNTAFCTHVFPETAFIAVTSYQNHKITQLKIENNPFAKGFRGSDDLELHRMSRMRSKEYPVVPRSTVRHKVANHSPFSSETRALSTSSNLGSQYQCENGVSGPSQDLLPPPNPYPLAQEHSQIYHCTKRKDEECSSTEHPYKKPYMETSPSEEDTFYRSGYPQQQGLSTSYRTESAQRQACMYASSAPPSEPVPSLEDISCNTWPSMPSYSSCTVTTVQPMDRLPYQHFSAHFTSGPLVPRLAGMANHGSPQLGEGMFQHQTSVTHQPVVRQCGPQTGLQSPGSLQPPEFLYTHGVPRTLSPHQYHSVHGVGMVPEWSENS", "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-338 promotes nuclear retention."}
+{"protein": "MFKEYKIYKFFEQVKQETYKVVWPTRKELVASTLVVVVAVFIFSPICLVLDYSIHNIMQLLLNIGK", "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 inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SecE/SEC61-gamma family."}
+{"protein": "MPNEIFTINLNAQAIIPEAFILLGIVGTLLVDLAGEKTASKWAPIICYLSIGSSLLSLALQWSNPVESAFLGSFNSDNLAISFRAIISLSTLVSLLISWRYTEQSGSPIGEFAAIVLSATLGAMLLCGSTDLISVFISLETLSVASYLLSGYLKRDPRSSEAALKYLLVGSAAAAVYLYGSSFLYGLSGSTNLATIGLEIINKPSFITSLALVFVLSTVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKTAGFAFAIRILSTTFSSFDEEWKLLFTILAILSMALGNVVALAQTSMKRMLAYSSIGQAGFVMIGIVSGTQDGLSAAVLYLAAYLFMNLGAFSCVILFSLRTGSDRILDYSGLYQKDPLITLGLSLCLLSLGGLPPMLGFFGKIYLFFAGWANHQYLLVIVGLVTSVISIYYYISVIKMMVVKEPQEASEIVKSYPEINWGIVGLPPLRVALYTCVAVTALGGILSNPLFKLANTAVSETPFLQDIIATANNIS", "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 subunit 2 family."}
+{"protein": "MASGGGGCSASERLPPPFPGLEPESEGAVGGSEPEAGDSDTEGEDIFTGAAAVSKPQSPKRIASLLPINSGSKENGIHEEQDQEPQDLFADATVELSLDSTQNNQKKVPAKTLISLPPQEATNSSKPQPSYEELEEEEQEDQFDLTVGITDPEKIGDGMNAYVAYKVTTQTSLPMFRSKHFAVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKVGKEDSSSAEFLEKRRAALERYLQRIVNHPTMLQDPDVREFLEKEELPRAVGTQTLSGAGLLKMFNKATDAVSKMTINMNESDIWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTAQFAKSLAMLGSSEDNTALSRALSQLAEVEEKIEQLHQEQANNDFFLLAELLSDYIRLLAIVRAAFDQRMKTWQRWQDAQTTLQKKREAEARLLWANKPDKLQQAKDEIVEWESRVTQYERDFERISTVVRKEVIRFEKEKSRDFRNHVIQYLETLLHSQQQLAKYWEAFLPEAKAIS", "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": "MSQIIDVPETLSLAIDSFLSYIEVERRLSPVTVENYQRQLMTIAQMMVAIKINQWSLLESQHVRMLLAKSHRSGLQPASLALRFSALRSFLDWQVSQGMLAVNPAKGVRTPKSGRHLPKNMDVDEVSQLMNIDLKDPLSVRDRTMLEVMYGAGLRLSELTNLNINDIDLQEGEVRVLGKGSKERKVPLGRKAVEWLQHWFAMRELYSPEDTAVFISTKSGKRLSVRSVQKRFELWGVKQGLSSHVNPHKLRHSFATHLLESSGDLRAVQELLGHANLSTTQVYTHLDFQHLAKVYDAAHPRAKREKS", "text": "FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The 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. In the complex XerC specifically exchanges the top DNA strands. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily."}
+{"protein": "MGNHTLLKQINKLLVLKTILDNKIISRTKISKLVDLNKATVSNLTDELIKEGYVVEKGYGKSKGGRRPVLLQVNKDVGSIIGIDLGVDYIHIILSNFVGEVIFEEYANMKIGEDKEKLLRLLFDLIEKSVKKAPQTPKGILGIGIGVPGIIEKESGTVLLAPNLKWQNVPLRSIVQQKFNLPVYIDNEANAGALGEKWFGEWGKVSDLIYLSVGIGLGAGIIIDNKLFRGAAGFAGEVGHTTINFQDDVCSCGNIGCLENFASERALLSVIKKLVKQGVEDRYISWENVDEITPSRIIQAAKEGSRVCRMAILEVAEKMGIGVANLVNIFNPEMVIIGNKASFFGELFLEKLREVINQRSFIAQFYNLKIEVSKLKDRAVVLGCIAMVISDMLSFPEYA", "text": "FUNCTION: Transcriptional repressor of xylose-utilizing enzymes. SIMILARITY: Belongs to the ROK (NagC/XylR) family."}
+{"protein": "MPATPSLKVVHELPACTLCAGPLEDAVTVPCGHTFCRLCLPALSQMGAQSSGKILLCPLCQEEEQAETPMAPVPLGPLGETYCEEHGEKIYFFCENDAEFLCVFCREGPTHQAHTVGFLDEAIQPYRDRLRSRLEALSMERDEIEDVKCREDQKLQVLLTQIESKKHQVETAFERLQQELEQQRCLLLARLRELEQQIWKERDEYITKVSEEVTRLGAQVKELEEKCQQPASELLQDVRVNQSRCEMKTFVSPEAISPDLVKKIRDFHRKILTLPEMMRMFSENLAHHLEIDSGVITLDPQTASRSLVLSEDRKSVRYTRQKKNLPDSPLRFDGLPAVLGFPGFSSGRHRWQVDVQLGDGGGCTVGVAGEGVRRKGEMGLSAEDGVWAVIISHQQCWASTSPGTDLPLSEIPRGVRVALDYEAGQVTLHNAQTQEPIFTFTASFSGKVFPFFAVWKKGSYLTLKG", "text": "FUNCTION: E3 ubiquitin ligase that plays a role in several processes including innate antiviral immnity, cell migration and chemotaxis. Acts as a 'Lys-63'-specific ubiquitin ligase for MAPK1/ERK2 and MAPK3/ERK1, promoting their activation by facilitating their interaction with MAP2K1 and MAP2K2. Plays also a role in cell migration and chemotaxis by acting as a stable focal adhesion component upon recruitment by multi-adapter protein paxillin/PXN. Functions in the RIGI-mediated interferon induction pathway upstream or at the level of MAVS. Inhibits NF-kappa-B activation by turnover of 'Lys-63'-linked ubiquitination of MAP3K7/TAK1. Mechanistically, prevents TRIM8 cytoplasmic translocation and thus inhibits TRIM8-mediated 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 in the cytoplasm. Plays also an important regulatory effect on the activation of hepatic stellate cells (HSCs). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell junction, focal adhesion Note=Localizes to focal adhesions during the early stage of adhesion biogenesis. SIMILARITY: Belongs to the TRIM/RBCC family."}
+{"protein": "MALAMLVLVVSPWSAARGVLRNYWERLLRKLPQSRPGFPSPPWGPALAVQGPAMFTEPANDTSGSKENSSLLDSIFWMAAPKNRRTIEVNRCRRRNPQKLIKVKNNIDVCPECGHLKQKHVLCAYCYEKVCKETAEIRRQIGKQEGGPFKAPTIETVVLYTGETPSEQDQGKRIIERDRKRPSWFTQN", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
+{"protein": "MQKKVIAAIIGTSAISAVAATQANAATTHTVKPGESVWAISNKYGISIAKLKSLNNLTSNLIFPNQVLKVSGSSNSTSNSSRPSTNSGGGSYYTVQAGDSLSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKVSGTASSSNAASNSSRPSTNSGGGSYYTVQAGDSLSLIASKYGTTYQKIMSLNGLNNFFIYPGQKLKVTGNASTNSGSATTTNRGYNTPVFSHQNLYTWGQCTYHVFNRRAEIGKGISTYWWNANNWDNAAAADGYTIDNRPTVGSIAQTDVGYYGHVMFVERVNNDGSILVSEMNYSAAPGILTYRTVPAYQVNNYRYIH", "text": "FUNCTION: Peptidoglycan hydrolase involved in the splitting of the septum during cell division. Binds to both alpha and beta-chains of human fibrinogen as well as fibronectin, which suggests a role in the colonization of host factor-coated material or host tissue. Also exhibits lytic activity against S.carnosus and S.aureus cells but not against M.luteus cells. FUNCTION: Peptidoglycan hydrolase involved in the splitting of the septum during cell division. Binds to both alpha and beta-chains of human fibrinogen as well as fibronectin, which suggests a role in the colonization of host factor-coated material or host tissue. Also exhibits lytic activity against S.carnosus and S.aureus cells but not against M.luteus cells. FUNCTION: Peptidoglycan hydrolase involved in the splitting of the septum during cell division. SUBCELLULAR LOCATION: Secreted Cell surface. SUBCELLULAR LOCATION: Secreted Cell surface. SUBCELLULAR LOCATION: Secreted Cell surface."}
+{"protein": "MTNGDSSSSALTDNERAVLDDIEAQGIDFLRLQFTDILGTVKNVSIPAHQAEKAFTEGIYFDGSSIEGFVRIQESDMRLDPDPETFAVLPWRSNGDGGSARLICDVVDREGNAFAGGPRQVLKNVLARADDMGYSVSIGPEPEFFLFEKDDDGNATTTAHDQGGYFDLAPKDLASDIRREIIFTLEAMGFEIEASHHEVARGQHEINFKYDDALTTADNIATFRAVVRAVAEQHDVHATFMPKPIGEINGSGMHSHISLFDEDGENVFADNDDEFNLSETAYQFMGGVLEHAPAFTAVTNPTVNSYKRLVPGYEAPVYIAWSGVNRSALIRVPDAAGVSARFEIRSPDPSCNPYLALAAVIAAGLDGIDTDADPGDAVREDIYEFDEDKRDAYGIDTLPGHLGDAVTALESDPVMQDALGEHVCEKFAEAKRHEYAEYKASVSEWETDRYLEKF", "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": "MAEPVIMAFVCYQUGYGAADLAGTSRMQYPASVRAIRVPCTGKFDITYALRAFQKGADAVFVAGUKPNECAFETGNFKAEERVKFGKQILDELGIGGERLEMFFMSGADAGKFTEAVKEMTDRVKKLGPNPIKA", "text": "SIMILARITY: Belongs to the MvhD/VhuD family."}
+{"protein": "MEAALTKLDQEEKRALQAYYRCAWEETKNIINDFLEIPEERCTYKLNSYTKKMELLFTPEFHTAWQEVFECREFIINFLRLITGHRVVLKGPAIVFTKETKNLGIPSTINVDFQANIENMDDLQKGNLIGKMNIKEN", "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": "MTTSSRTCPVPAVNGHMTHYPAAPYPLLFPPVIGGLSLPSLHGLQSHPPTSGCSTPSPATVETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEPTKQESTENYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTSLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPMKVDKLQEPLLEALKIYIRKRRPNKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPTSNGNTAEHSPSISPSSVDNSSVSQSPMVQ", "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 limb and craniofacial development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
+{"protein": "DVSFSLSGGGTASYEK", "text": "SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily."}
+{"protein": "MWGIKGSFAVLLLLFLAYIFASSVNADSLSAPLNVTIKALEGNSAIVTWDILEGDPVIGFAITQQKKDVRMLRFIQEVNTTTRSCALWDLEEDTEYIVHVQSISMSGTSPPSEPVLFRTPKESEKLASKSPDEVTMEEVGQAAQLRAGELIIIVVVLVMWAGVIALFCRQYDIIKDNEPNNNKDKAKNSSECSTPEHPTGGLLRSKV", "text": "FUNCTION: [Irisin]: May mediate beneficial effects of muscular exercise. SUBCELLULAR LOCATION: [Irisin]: Secreted Note=Detected in the blood of individuals subjected to endurance exercise. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Peroxisome membrane; Single-pass type I membrane protein."}
+{"protein": "MLDTTKLTMVGTGSAFSKKFYNNSALVTFTNGYNLLIDCGHSVPKGLHDLGFPLESLDGILITHTHADHIGGLEEVALYNKFVLGGRKIDLLVPEPLVEPLWNDSLNGGLRYDDSRELELDDYFTVRSLKTSDCGAARTQIDENIAFTLYTTLHVSHMKSYAVGLIDRGEEKVFYSSDTVFDEYLLDYALTMFPWVFHDCQLFTGGVHASLDELLGYTRYIPEKQQNKIFLMHYGDNVEEFIGKTGRMRFAEQGREIIL", "text": "FUNCTION: Counteracts the host Pycsar antiviral defense system. Phosphodiesterase that enables metal-dependent hydrolysis of host cyclic nucleotide Pycsar defense signals such as cCMP and cUMP. SIMILARITY: Belongs to the anti-Pycsar protein Apyc1 family."}
+{"protein": "MAPAPVTLLAPGAASSMSCSQPGQRSPSNDFQVLRGTELQHLLHAVVPGPWQEDVADAEECAGRCGPLMDCWAFHYNVSSHGCQLLPWTQHSPHSRLWHSGRCDLFQEKGEWGYMPTLRNGLEENFCRNPDGDPGGPWCHTTDPAVRFQSCSIKSCRVAACVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGKFLDQGLDDNYCRNPDGSERPWCYTTDPQIEREFCDLPRCGSEAQPRQEATSVSCFRGKGEGYRGTANTTTAAYLASVGTRKSHISTDLRQKNTRASEVGGGAGVGTCCCGDLRENFCWNLDGSEAPWCFTLRPGTRVGFCYQIRRCTDDVRPQDCYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKLQALTLGRHALMSGTRAWKWLRLPCHDFAPAPASVHIYLRTACTTGGELLPDPDGDSHGPWCYTMDPRTPFDYCALRRCDQVQFEKCGKRVDRLDQRRSKLRVAGGHPGNSPWTVSLRNRQGQHFCAGSLVKEQWILTARQCFSSCHMPLTGYEVWLGTLFQNPQHGEPGLQRVPVAKMLCGPSGSQLVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTGNDTVLNVALLNVISNQECNIKHRGHVRESEMCTEGLLAPVGACEGDYGGPLACFTHNCWVLKGIRIPNRVCTRSRWPAVFTRVSVFVDWIHKVMRLG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily."}
+{"protein": "TDEITSFSIPKFRPDQPNLIFQGGGYTTKEKLTLTKAVKNTVGRALYSLPIHIWDSETGNVADFTTTFIFVIDAPNGYNVADGFTFFIAPVDTKPQTGGGYLGVFNGKDYDKTAQTVAVEFDTFYNAAWDPSNGKRHIGIDVNTIKSISTKSWNLQNGEEAHVAISFNATTNVLSVTLLYPNLTGYTLSEVVPLKDVVPEWVRIGFSATTGAEYATHEVLSWTFLSELTGPSN", "text": "SIMILARITY: Belongs to the leguminous lectin family."}
+{"protein": "MNTIDWEFMISAFPTLIQALPITLFMAIAAMIFAIIGGLILALITKNKIPVLHQLSKLYISFFRGVPTLVQLFLIYYGLPQLFPEMSKMTALTAAIIGLSLKNAAYLAEIFRAALNSVDDGQLEACLSVGMTKFQAYRRIILPQAIRNAIPATGNTFIGLLKETSLAFTLGVMEMFAQGKMYASGNLKYFETYLAVAIVYWVLTIIYSILQDLFERAMSKPYRT", "text": "FUNCTION: Probably part of the ABC transporter complex YxeMNO that could be involved in amino-acid import. May transport S-methylcysteine. Probably 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": "MSFLCSENSYQQQSKISIDIDKSLKNHKLKLEEEIRVLIYGQKKVGVTTLFKTFLLMGESQITPEELMDNRNNVYKTIINQLKKFIIISNNSKIELENNNNIQMSNLILELDSENFLWNKEIGETCLKLWNDSGIQKIFQSQFSEFFGYFFKHLQRISDENYTPTPQDLNFIKLTQNGIIEGKFTFERCLIKMIEMGIQTSTLKKWINCFSEVQAIIYVIDLSVYDIVESEDCSKSINKLEKSLNGFKEIIESKYLHGCGVIVFFNKKDIFREKLKTVPFKTYDKDYIGENDFESTTNFIKNKLLDYYSNPNKNVYFLINEESEVDICRSTFNILKDIVLNITYNSVKN", "text": "SIMILARITY: Belongs to the G-alpha family."}
+{"protein": "MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMEANGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITRLAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "text": "FUNCTION: Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. 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": "MTATPVYFDISCNGKPKGRVVFKLYDDVVPKTAANFRSLCTGDKGISPKSGKPLSYKDSIFHRVIKDFMCQGGDFTAPSDHLGTGGESIYGEKFEDENFKLNHNKPFLLSMANSGPNTNGSQFFITTVPTPHLDGKHVVFGEVIEGKSIVRQLERSEKGANDRPVEDWKIADCGELPANYEPVASGADDGTGDTYEEILTDNDTIDINNPQSVFAAVSKIKDIGTKLLKEGKLEKSYEKYTKANSYLNDYFPEGLSPEDLSTLHGLKLSCYLNAALVALKLKHGKDAIAAANNALEVEQIDDKSKTKALYRKGMGYILVKDEEQAQKILEEALELEPNDAAIQKGLQEAKHNIKLRRDKQKKAMAKFFS", "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": "MFTMKKPLLLLFFLATINLSLCEQERNAEEERRDEPDERNAEVEKRFLPIVGKLLSGLFGK", "text": "FUNCTION: Antimicrobial peptide active against a variety of Gram- positive bacterial strains but not against Gram-negative bacteria. Has weak antifungal activity against a slime mold isolate. Has weak hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily."}
+{"protein": "MADPSEQKEKVVKEKKEKVKKEKVVKEKVAKASSSGQKKKDVKKETGLGLSVKKDENFGEWYSEVCKQDMIEYYDISGCYILRPWSMAIWEIMQIFFDAEIKKMKVKNCYFPLFVSPGVLEKEKDHIEGFAPEVAWVTKSGKSDLEVPIAIRPTSETVMYPYYSKWIRGHRDLPLKLNQWCNVVRWEFSNPTPFIRSREFLWQEGHTAFATKAEADEEVLQILELYRRIYEEYLAVPVVKGMKSENEKFAGGLYTTSVEAFIPNTGRGVQGATSHCLGQNFAKMFEINFENEKAETEMVWQNSWAYSTRTIGVMIMTHGDDKGLVLPPKVASVQVVVIPVPYKDANTQGIYDACTATASALCEAGIRAEEDLRDNYSPGWKYSDWEMKGVPLRIEIGPRDLENDQVRTVRRDNGVKEDIPRGSLVEHVKELLEKIQQNMYEVAKQKREACVQEVKTWDEFIKALNEKKLILAPWCDEEEVERDVKARTKGETGAAKTLCSPFDQPELPEGTLCFASGKPAKKWTYWGRSY", "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, cytosol. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
+{"protein": "MVLDNLGGSLRGALKKIASATRVDKALVDDAVRDIQRALLQADVNVKLVMSLSNRIRERALNEKPPAGMNPREHVINIVYQELINLIGRGTDIPLKKQTIMLVGLQGSGKTTTAAKLATYFQRRGLRTAVICADTFRAGAYDQLKALCDRQGIFFYGEKGNENAPEVAKNGLEATKKYDVRIVDTAGRHALESDLIQEMKDIHAVVNADHKLLVMDAAIGQQASEQARAFNEAVGITGVIITKLDGTAKGGGALSAVAETKTSVAFIGVGETASDLEKFEADRFISRLLGMGDIKGLIEKAQEVQIESDVDVDAMMKGKFTLKDMYKQLEAMNKMGPLKQIMQMLPFGGIGIELSDKEYQVTKERLEAYRFIMDSMTDEELEDPKIINASRIKRIARGSGTRPELVKELLKSHAAMQKAIKGMRGGMGRMNMKKLMKRLGQPKV", "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": "MNRQKNNLIFQYSAVVIFFLIVMFGLSLFLAGHYTPGGGFVGGLLLSSALVIITVAFDIKTMRKIFPWDFKILIGIGLLFCLATPMASWFYNKNFFTHTPFEIPLGILPPMEMHTATFFDLGVMCAVVGTVMTIILSIGENE", "text": "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": "MLRLGLCAAALLCVCQPGAVRADCWLIEGDKGYVWLAICSQNQPPYETIPQHINSTVHDLRLNENKLKAVLYSSLNRFGNLTDLNLTKNEISYIEDGAFLGQTSLQVLQLGYNRLSNLTEGMLRGMSRLQFLFVQHNLIEVVTPTAFSECPSLISIDLSSNRLSRLDGATFASLASLMVCELAGNPFNCECDLFGFLAWLVVFNNVTKNYDRLQCESPREFAGYPLLVPRPYHSLNAITVLQAKCRNGSMPARPVSHPTPYSTDAQREPDENSGFNPDEILSVEPPASSTTDASAGPAIKLHQVTFTSATLVVIIPHPYSKMYVLVQYNNSYFSDVMTLKNKKEIVTLDKLRAHTEYTFCVTSLRNSRRFNHTCLTFTTRDLVPGDLAPSTSTTTHYIMTILGCLFGMVIVLGAVYYCLRKRRMQEEKQKSVNVKKTILEMRYGADVDAGSIVHAAQKLGEPPVLPVARMSSIPSMVGEKLPASKGLEAGLDTPKVATKGNYIEVRTGAAGDSLARPEEELPEIENGQGSAAEISTIAKEVDKVNQIINNCIDALKLDSASFLGGGGGGGGGGDSDLAFECQSLPAAPAASSAATPGALERPSFLSPPYKESSHHPLQRQLSADAAVSRKTCSVSSSGSIKSAKVFSLDVPDHPTPTGLAKSDSKYIEKGSPLNSPLDRLPLVPTGSSGSSGGGGGIHHLEVKPAYHCSEHRHSFPALYYEEGADSLSQRVSFLKPLTRSKRDSTYSQLSPRHYYSGYSSSPEYSSESTHKIWERFRPYKKHHREEVYMAAGHALRKKVQFAKDEDLHDILDYWKGVSAQQKL", "text": "FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
+{"protein": "MGLFDKLAGWLGLKKKEVNVLCLGLDNSGKTTIINQLKPSNAQAQDIVPTIGFSIEKFKTSSLSFTVFDMSGQGRYRNLWEHYYKEGQAIIFVIDSGDKLRMVVAKEELDTLLNHPDIKHRRIPLLFFANKMDLRDALSAVKVSQLLCLENIKDKPWHICASDAVKGEGLLEGVDWLQDQIRAMKT", "text": "FUNCTION: Probably involved in membrane protein trafficking at the base of the ciliary organelle. May function in cilia biogenesis. Isoform 2 is required for proper retinal function and organization. SUBCELLULAR LOCATION: Cell projection, cilium membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body. SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
+{"protein": "MSYRVAKASQYLAITGGGITDIKLAKKSWVFPWQSCTVFDVSPVNYTFEVQAMSSEKLPFVIPAVFTIGPRVDDPHALLLYAMLMSQHDKHSNHVNELVQGVIEGETRVLVASMTMEEVFKGTKEFKKEVFDKVQLELNQFGLVIYNANVKQLVDVPGHEYFSYLGQKTQMEAANQAKIDVAEAKMKGEVGAKERTGLTIQNAAKIDAESKIISTQRLGEGTKEEIKVKTEVKVFQNEKEALVAKADAALAIQKAALSQNSRVAEVEAAKAVALREAELQTKVEKMNALTRTEKLKAEFLSKASVEYETKVQEANWELYNKQKQAEAVLYEKQKQAEATKAAADAAFYSKQKDAEGLVAMADAQGTYLKTLLGAVNNDYSAMRDFLMINNGIYQDIAKTNAVAIRDLQPKISVWNHGGAEQGMNGGGKATMNDIAGLYKMLPPVLDTVYEQTGMQPPAWIGTLRGAEPKQSLHAQQHRG", "text": "FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Membrane, caveola. SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily."}
+{"protein": "MKKTAIALAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFYGNGYQNGIGNGPTHKDQLGAGAFLGYQANQYLGFELGYDWLGRMPYKGSVNNGAFKAQGVQLAAKLSYPIADDLDIYTRLGGMVWRADSKANYGRTGQRLSDHDTGVSPLAAVGVEYALTKNWATRLDYQFVSNIGDAGTVGARPDNTMLSLGVSYRFGQDDVVAPAPAPAPAPVVETKRFTLKSDVLFNFNKSTLKAEGQQALDQLYTQLSSMDPKDGSVVVLGYTDAVGSDQYNQKLSEQRAQSVVDYLVSKGIPSDKISARGMGEADAVTGNTCGYKSGRATKAQIVCLAPDRRVEIEVKGIKDVVTQPQG", "text": "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": "MKSKLICIIMVIAFQAHFNMAVKADSVGEERLRNNIQAKRNPADLKTLPDSCEAKDFYKNFKILDMTKDKLGVTHYTLALSSDGYLTDNDEIKVHVTPDNKITFINGDLQQGQLRITNQIKITEKNAIEKAFEAIGQSEAHVKSYIGNPVKEKEIIINSRTKRLVYNIKLIFAEPEVASWIIQVDAETGAILKKQNMLSEVERADTHKDFQALGKGANRLLQRPLHVMKINDLFYLVDRTHKGLIRTFDLNHKTDASFGKVVSNKTNMFTDPEFSSAVDAHFYASEVYDYYKNVHQLESLDGKGGEIDSFVHYGLNCNNAFWDGREILYGDGDKKNFKPFSCAKTIVGHELTHAVIQYSAGLEYEGQSGALNESFADVFGYFIAPNHWLIGEDVCVRGLRDGRIRSIKDPDKYNQAAHMKDYESLPITEEGDWGGVHFNSGIPNKAAYNTITKLGKEKTEQLYFRALKYYLTKKAQFTDAKKALQQAAKDLYGEDASKKVAEAWEAVGVN", "text": "FUNCTION: Probably linked to the pathogenesis of listerial infection. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M4 family."}
+{"protein": "MNPQIRNPMKAMYPGTFYFQFKNLWEANDRNETWLCFTVEGIKRRSVVSWKTGVFRNQVDSETHCHAERCFLSWFCDDILSPNTKYQVTWYTSWSPCPDCAGEVAEFLARHSNVNLTIFTARLYYFQYPCYQEGLRSLSQEGVAVEIMDYEDFKYCWENFVYNDNEPFKPWKGLKTNFRLLKRRLRESLQ", "text": "FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase- dependent and -independent mechanisms. 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. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non- LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
+{"protein": "MDALSQAISSGISVPYKNNSSSLVPSHGLTSLILRKSRSPVNPSSRSRVSVRASEIQHSKTSASSIDLSDPDWKLKYEKDFEQRFSIPHITDVLPDAEAIRSTFCLKMRSPTEDFVGGYPSDEEWHGYINNNDRVLLKVISYSSPTSAGAECLDHDCSWVEQWIHRAGPREKIYFRPEEVKAAIITCGGLCPGLNDVIRHIVITLEIYGVKNIVGIPFGYRGFSDKDLTEMPLSRKVVQNIHLSGGSLLGVSRGGPSVSEIVDSMEERGINMLFVLGGNGTHAGANAIHNECRKRKIKVAVVGVPKTIDNDILHMDKTFGFDTAVEEAQRAINSAYIEAHSAYHGIGVVKLMGRNSGFIAMQASLASGQVDICLIPEVPFNLHGPNGVLKHLKYLIETKGSAVICVAEGAGQNFLEKTNAKDASGNAVLGDFGVYIQQETKKYFKEISTPIDVKYIDPTYMIRAVRANASDGILCTVLGQNAVHGAFAGYSGITVGIINTHYAYLPITEVIAYPKSVDPNSRMWHRCLTSTGQPDFI", "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: Plastid, chloroplast. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily."}
+{"protein": "MNAALKTFAPSALALLLILPSSASAKEAETQQKLANVVILATGGTIAGAGASAANSATYQAAKLGVDKLIAGVPELADIANVRGEQVMQIASESISNDDLLKLGKRVAELAESKDVDGIVITHGTDTLEETAFFLNLVEKTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASDKQSRGKGVLVTMNDEIQSGRDVSKAVNIKTEAFKSAWGPMGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYGYGNVTDTAYKALAQNGAKALIHAGTGNGSVSSRVVPALQELRKNGVQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPQKARILAMVAMTKTQDSKELQRIFWEY", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the asparaginase 1 family."}
+{"protein": "MINTNMKYWSWMGAFSLSMLFWAELLWIITH", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein."}
+{"protein": "MTTVKRTVRLITDQNVLPGGEAAVLNDQSFPVREWSIKLVCLNPQGEETDASFVDRVTYKLHPTFQNPTRTIRKPPFQIKEQGWGEFEMEIIIYYADKGGEHRFLHYLHFQQEHYHEDIELNINATRPGLLKALTATGEVPGYSDEGEEARKDKRKNESEVGAGKKKAKAKPVDMDKLAEGLQKLQEDDLLQVVQMVNENKTPDMYVRNDIEGGEFHIDLYTLPDNLLLLLYSFCAKRVTM", "text": "FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID, and the RNA polymerase II associated general transcription factor complex TFIIF. 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, facilitation of DNA opening and initiation of transcription. TFIIF is essential for the initiation of transcription by RNA polymerase II. TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA- TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. The TAF14 subunit has stimulatory activity. 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. 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: Nucleus, nucleoplasm. SIMILARITY: Belongs to the TAF14 family."}
+{"protein": "MLSVIRVHLPSEIPIVGCELTPYVLLRRPDKTPSTDDVPESAPLEGHFLKYRWFRVQSDKKVAICSVHPSETATLQCLGCLKSKVPVAKSYHCSTKCFSDAWQHHRVLHERAASAATEGNDEEELPRLNSSGSGSGVLSTSVSLTNGSSSVYPSAITQKTGAGGETLVEVGRSKTYTPMADDICHVLKFECVVVNAETKQNVGLSCTILTSRVIPAPSPSPRRLISISGTDVTGHLDSNGRPLSMGTFTVLSYNILSDTYASSDIYSYCPTWALAWTYRRQNLLREIVKYRADIVCLQEVQNDHFEEFFLPELDKHGYQGLFKRKTNEVFIGNTNTIDGCATFFRRDRFSHVKKYEVEFNKAAQSLTEAIIPVSQKKNALNRLVKDNVALIVVLEAKFGSQAADNPGKRQLLCVANTHVNVPHELKDVKLWQVHTLLKGLEKIAASADIPMLVCGDFNTVPASAPHTLLAVGKVDPLHPDLMVDPLGILRPHSKLTHQLPLVSAYSQFAKMGGNVITEQQRRRLDPASSEPLFTNCTRDFIGTLDYIFYTADTLTVESLLELLDEESLRKDTALPSPEWSSDHIALLAEFRCMPRARRNNIL", "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": "MADGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDMKEKLSYIALDFEQELETSKTSSSVEKSFELPDGQVITIGAERFRCPEVLFQPSMIGMENPGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFGGIGDRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF", "text": "FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. This is considered as one of the reproductive actins. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family."}
+{"protein": "MQSIPHSDEADVAGMTHASEGHHGLGTSMLVPKNPQGEEDSKLGRNCSGFEDAQDPQTAVPSSPLLSMASCSSQEGSSPCHLLTVRIIGMKNVRQADILSQTDCFVTLWLPTASQKKLKTRTISNCLHPEWDESFTFQIQTQVKNVLELSVCDEDTLTQNDHLLTVLYDLSKLCLRNKTHVKFPLNPEGMEELEVEFLLEENFSSSETLITNGVLVSRQVSCLEVHAESRRPRKRKKNKDLLVMVTDSFENTQRVPPCQEPCYPNSACFHYPKYSQPQLYAEAPKSHCNFRLCCCGTHRNDPVCQPLNCLSDGQVTTLPVGENYELHMKSSPCSDTLDVRLGFSLCQEEVEFVQKRKMVVAKTLSQMLQLEEGLHEDEVPIIAIMATGGGTRSMVSLYGHLLGLQKLNFLDASTYITGLSGATWTMATLYSDPEWSSKNLETVVFEARRHVVKDKMPALFPDQLYKWREDLQKHSQEGYKTTFTDFWGKLIEYSLGDKKNECKLSDQRAALCRGQNPLPIYLTINVKDDVSNQDFREWFEFSPYEVGMQKYGAFIPSELFGSEFFMGRLMKRIPEPEMCYMLGLWSSIFSLNLLDAWNLSHTSEEFFYRWTRERLHDIEDDPILPEIPRCDDNPLETTVVIPTTWLSNTFREILTRRPFVSEFHNFLYGMQLHTDYLQNRQFSMWKDTVLDTFPNQLTQFAKHLNLLDTAFFVNSSYAPLLRPERKVDLIIHLNYCAGSQTKPLKQTCEYCTEQKIPFPSFSILEDDNSLKECYVMENPQEPDAPIVAYFPLISDTFQKYKAPGVERSPDELELGQLNIYGPKSPYATKELTYTEAAFDKLVKLSEYNILNNRDKLIQALRLAMEKKRMRSQCPS", "text": "FUNCTION: Calcium-dependent N-acyltransferase involved in the biosynthesis of N-acyl ethanolamines (NAEs) in the brain (PubMed:27399000). Transfers the sn-1 fatty acyl chain of phosphatidylcholine (fatty acyl donor) to the amine group of phosphatidylethanolamine (fatty acyl acceptor) to generate N-acyl phosphatidylethanolamine (NAPE). Similarly can use plasmenylethanolamine as a fatty acyl acceptor to form N-acyl plasmenylethanolamine (N-Acyl-PlsEt). Both NAPE and N-Acyl-PlsEt can serve as precursors of bioactive NAEs like N-arachidonoyl phosphatidylethanolamine also called anandamide (PubMed:27399000, PubMed:29447909). Has weak phospholipase A2 and lysophospholipase activities (PubMed:27399000, PubMed:15866882). Regulates intracellular membrane trafficking that requires modulation of membrane curvature as it occurs by enrichment in lysophospholipids. Promotes tubule formation involved in clathrin-independent endocytotic trafficking and cargo recycling (PubMed:24413173). SUBCELLULAR LOCATION: Cytoplasm, cytosol Early endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=Targeted to clathrin-independent endocytotic vesicles through binding to phosphoinositides, especially phosphatidylinositol 4,5-bisphosphates."}
+{"protein": "MMDAAGRTTQETLARTLESEQGHNALNLSWVRLLATSAVLIVSLYFGRVRGMTDWDVYTPPFAAYWSVTALTLVALYRFERLRRWAGLSLALVDVPAIYWLQHIALPLSPSPGGVAGFTLGLYATLILLSALSLRRTMTLVVTACAAVGEVALQREAHISLGAQLTAVVVLGACAAGACHLLLRIRTLLTTATQQELKRARLGRYFSPAVAERLQDLDRSETSPELREVTLLFADIRDFTSLSERLRPEQVVTLLNEYYGRMVEVVFRHGGTLDKFIGDALMVYFGAPIADPAHARRGVQCALDMVQELETVNALRSARGEPCLRIGVGVHTGPAVLGNIGSATRRLEYTAIGDTVNLASRIESLTKTRDVPILASRATREQAGDTFLWNEMAPASVPGKSQPVAIFTPRNRTPAQQAGAPAAA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the adenylyl cyclase class-3 family."}
+{"protein": "MSRYTGPKIRIIRRLGELPALTTKKVKNNYPPGREWSTNEELSEYAIRLQEKQKIRFNYGINEKQLRRYVKKAKKSRGSTGSYLLNLLEMRLDNIVLRAGLAPTIAASRQLVSHKHIEVNNKIVNIPSFQCSIGDTIHVKKSNKSRQLIDLNSRRDTTKFFPKYLEVNKDNMGARVVKTMDKQDVNLTINELLVVEFYSRKG", "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": "MSDTVEELVQRAKLAEQAERYDDMAAAMKKVTEQGQELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGSEKKQQLAKEYRVKVEQELNDICQDVLKLLDEFLIVKAGAAESKVFYLKMKGDYYRYLAEVASEDRAAVVEKSQKAYQEALDIAKDKMQPTHPIRLGLALNFSVFYYEILNTPEHACQLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDVGAEDQEQEGNQEAGN", "text": "FUNCTION: Required to modulate lifespan, in concert with hcf-1, acting redundantly with 14-3-3-like protein ftt-2. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the 14-3-3 family."}
+{"protein": "MSKISQQNSTPGVNGISVIHTQAHASGLQQVPQLVPAGPGGGGKAVAPSKQSKKSSPMDRNSDEYRQRRERNNMAVKKSRLKSKQKAQDTLQRVNQLKEENERLEAKIKLLTKELSVLKDLFLEHAHNLADNVQSISTENTTADGDNAGQ", "text": "FUNCTION: Transcription factor that binds to the promoter and the enhancer regions of target genes. Binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene (PubMed:7665092). Binds to the promoter and the enhancer of the immunoglobulin heavy chain. Binds to GPE1, a cis-acting element in the G-CSF gene promoter. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. C/EBP subfamily."}
+{"protein": "MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLTHRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRLLPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALVGCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPTVTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDIDPFVNPDAGQRISAAAEAIGAPILIGTLMDVPGRPRENPEWTNTAIVWNPGTGPADRHDKAIVQPFGEYLPMPWLFRHLSGYADRAGHFVPGNGTGVVRIAGVPVGVATCWEVIFDRAPRKSILGGAQLLTVPSNNATFNKTMSEQQLAFAKVRAVEHDRYVVVAGTTGISAVIAPDGGELIRTDFFQPAYLDSQVRLKTRLTPATRWGPILQWILVGAAAAVVLVAMRQNGWFPRPRRSEPKGENDDSDAPPGRSEASGPPALSESDDELIQPEQGGRHSSGFGRHRATSRSYMTTGQPAPPAPGNRPSQRVLVIIPTFNERENLPVIHRRLTQACPAVHVLVVDDSSPDGTGQLADELAQADPGRTHVMHRTAKNGLGAAYLAGFAWGLSREYSVLVEMDADGSHAPEQLQRLLDAVDAGADLAIGSRYVAGGTVRNWPWRRLVLSKTANTYSRLALGIGIHDITAGYRAYRREALEAIDLDGVDSKGYCFQIDLTWRTVSNGFVVTEVPITFTERELGVSKMSGSNIREALVKVARWGIEGRLSRSDHARARPDIARPGAGGSRVSRADVTE", "text": "FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo- inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM). FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors (works best on C20-C95 lipid monophosphate substrates in which the lipid can be modified, tested with the C-terminal domain expressed in M.smegmatis) to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo-inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: In the C-terminal section; belongs to the glycosyltransferase 2 family. SIMILARITY: In the N-terminal section; belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily."}
+{"protein": "MALEMRLPKARKPLSESLGRDSKKHLVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVERVNKLICVKALKTRYNGEVGDIVVGRITEVQQKRWKVETNSRLDSVLLLSSMNLPGGELRRRSAEDELAMRGFLQEGDLISAEVQAVFSDGAVSLHTRSLKYGKLGQGVLVQVSPSLVKRQKTHFHDLPCGASVILGNNGFIWIYPTPEHKDEDAGGFIANLEPVALSDREVISRLRNCVVLLVTQRMMLFDTSILYCYEASLAHQIKDILKPEVMEEIMLETRQRLLDQEG", "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. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus. SIMILARITY: Belongs to the RRP4 family."}
+{"protein": "MKVFILALLALTATTAIAQLDTTCSQGFRQYQQQQQPGQRQLLEQMRPCVAFLQQQCRPLRMPFLQTQVEQLSSCQIDQYQCCQQLAQIPEQIRCHAIHNVVEAIMQQQSQQHRQERQQQAQHKSMRMLLETLYLMCNIYVPIQCQQQQQLGQQQQQQLQEQLTPCATFLQHQCSPVTVPFPQIRVDQPTSCQNVQHQCCRQLSQIPEQYRCQAIHNVAEAIRHQQPQQQCQGMYQPQQPAKLESIRMSLQALRSMCRIYIPVQCPAPTAYNIPMVATYTGGAC", "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": "MDAPLTDAERTALQTSLEALNRQVEATRNILRSNSQKALLQTLHTDQELPDPALEALAGKTINLLHETQQLLEPGHLVLADHFLGYVSTKCLCAAVELKLVDILADADEAGMTVDELADASGAHPDRLQQVLRVLRNDNIFDYDAVSHRYRNNRVSALLHSEHWTQWHNWVDLYGNEFYDIARGIPRSIRREEARWAAQINFDTNDDMFTYFQAQGWLPRLHRTLGGGAIAQAPGIVADYPWHEIGSRTVLDVGGGGGGFLASLLREYPQMRGGILDLPRTIEHACTLFHEPQGPYFDLRERVPRENLIAGDFLKAVPAFEIYTMKWVLHDWKDPDVLTILRCIRASLIPGPDSRLVILESNLSDGQMGRLSRYGDINMMMTANGQERSEEQWRALAAASGWEVSRIYPMRRAWVCAIDLRPSASESGDRKHS", "text": "FUNCTION: O-methyltransferase; 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 class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
+{"protein": "MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELNALQTSCSSSINKQKTRLKDLKLTLQRYKRHASREEAELVQQMGANIKERQNVFFDMEAYLPKKNGLYLNLVLGNVNVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAVACRFFLHYRVTDEVFNFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGLIYQKFRNQFLAFSIFQSCVQFLQYYYQRGCLYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSSHEECREWQVFVLALTFLVLFLGNFLTTLKVVHTKLQQNRSKAKKP", "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": "MTQDVTSGYSNLDLDLRDNGVCVVTLNRPDKRNALDVATIEELVTFFSTAHRKGVRAVVLTGAGDHFCAGLDLVEHWKADRSADDFMHVCLRWHEAFNKMEYGGVPIIAALRGAVVGGGLELASAAHLRVMDQSTYFALPEGQRGIFTGGGATIRVSDMIGKYRMIDMILTGRVYQGQEAADLGLAQYITEGSSFDKAMELADKIASNLPLTNFAICSAISHMQNMSGLDAAYAEAFVGGIVNTQPAARERLEAFANKTAARVRPNS", "text": "FUNCTION: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by catalyzing both the hydration and the hydrolysis of 3-(methylthio)acryloyl-CoA (MTA-CoA) to acetaldehyde, CO2, MeSH, and CoA (PubMed:21562561, PubMed:23704947). SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
+{"protein": "MKTLLLTLVVVAIVCLDLGYTLTCLICPEKDCQKVHTCRNEEKICVKRSYDKNQLGWRAQRGCAVSCPKAKPNETVQCCSTDKCNK", "text": "FUNCTION: Binds with low affinity to muscular (alpha-1-beta-1-delta- epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral subfamily. Orphan group II sub-subfamily."}
+{"protein": "MIRGLLLGIIWMIFCVCSSFQQETPFVYNNFGHVDHLHLDGSARIIPSGGILQLTNATNSQIGHVFYEKPIEFKSSESVSFSTYFVCALLPAGDPSGHGMTFFVSHSTDFKGAEATRYFGIFNRNGSTSTRVLAVELDTSLASDVKDISDNHVGIDVNSAESITSANASYFSDKEGKKIDIKLLSGDPIQVWVDYEGTTLNVSLAPLRNKKPSRPLLSSTSINLTDILQGRRMFVGFSGSTGSSMSYQYILGWSFSKSMASLPNIDISKLPKVPHSSTKKKSTSPVLSVLLGLIAFIVLGILVVAYLYRRNLYSEVREEWEKEYGPIRYSYKSLYKATKGFNRSEFLGRGGFGEVYKGTLPRSRELREVAVKRVSHDGEHGMKQFVAEIVSMRSLKHRSLVPLLGYCRRKHELLLVSEYMPNGSLDHYLFNHDRLSLPWWRRLAILRDIASALSYLHTEADQVVIHRDIKAANVMLDAEFNGRLGDFGMSRLYDRGADPSTTAAVGTVGYMAPELTTMGASTGTDVYAFGVFLLEVTCGRRPVEPGLPEAKRFLIKWVSECWKRSSLIDARDPRLTEFSSQEVEKVLKLGLLCANLAPDSRPAMEQVVQYLNGNLALPEFWPNSPGIGVLSPMALSPAPLVIPSLSFSSSSSNNSMFITHSVLYGSGR", "text": "FUNCTION: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici. 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": "MTITQPDLSVFETVESEVRSYCRGWPTVFDRAQGSRMYDEDGHAYLDFFAGAGSLNYGHNNPVLKRALIDYLERDGVTHGLDMSTAAKRAFLESFQNLILRPRDLPYKVMFPGPTGTNAVESALKLARKVKGREAIVSFTNAFHGMSLGSLAVTGNAFKRAGAGIPLVHGTPMPFDNYFDGKVPDFLWFERLLEDQGSGLNKPAAVIVETVQGEGGINVARPEWLRALAELCKRQDMLLIVDDIQMGCGRTGAFFSFEEAGVTPDIVTVSKSISGYGLPMSLCLFKPELDIWEPGEHNGTFRGNNPAFVTAAAALQTYWADGSAMEKQTLARGEQVEQALISITEENLADVKEYRGRGLVWGIEFKDKDRAGRIAQRAFELGLLIETSGPESEVVKLLPALTITPEELDEGLRTLARAVRETA", "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": "MAFMKKYLLPILGIFLAYYYYSANEEFRPEMLRGKRVIVTGASKGIGREMAYHLARMGAHVVVTARSEESLKKVVSRCLELGAASAHYVAGTMENMTFAEQFVAKAGELVGGLDMLILNHIHYTPLGVFSNDIHLLRRTLEVNLLSYVVLSTAALPMLKQTNGSIVVVSSIAGKIACPLVAAYSASKFALDGFFSSLRMEYEATKVNVSITLCILGLIDTDTAMKAVAGIFNAKASPKEECALEIIKGGTLRQDEVYYDSSILTPLLLRNPGRKIMEFFFLKKYNMERFINN", "text": "FUNCTION: Controls the reversible conversion of biologically active glucocorticoids such as cortisone to cortisol, and 11- dehydrocorticosterone to corticosterone in the presence of NADP(H) (PubMed:17470521). Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic processes (By similarity). Plays a role in the secretion of aqueous humor in the eye, maintaining a normotensive, intraocular environment (By similarity). Bidirectional in vitro, predominantly functions as a reductase in vivo, thereby increasing the concentration of active glucocorticoids (By similarity). It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates. Interconverts 7-oxo- and 7-hydroxy-neurosteroids such as 7- oxopregnenolone and 7beta-hydroxypregnenolone, 7- oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en- 17-one), among others (By similarity). Catalyzes the stereo-specific conversion of the major dietary oxysterol, 7-ketocholesterol (7- oxocholesterol), into the more polar 7-beta-hydroxycholesterol metabolite (By similarity). 7-oxocholesterol is one of the most important oxysterols, it participates in several events such as induction of apoptosis, accumulation in atherosclerotic lesions, lipid peroxidation, and induction of foam cell formation (By similarity). Mediates the 7-oxo reduction of 7-oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in its free form and when conjugated to glycine or taurine, providing a link between glucocorticoid activation and bile acid metabolism (By similarity). Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which 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: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MTQQPLRGVTSLHFNQDQSCFCCAMETGVRIYNVEPLMEKGHLDHEQVGSVGLVEMLHRSNLLALVGGGSSPKFSEISVLIWDDAREGKDSKDKLVLEFTFTKPVLAVRMRHDKIVIVLRNRIYVYSFPDSPRKLFEFDTRDNPKGLCDLCPSLEKQLLVFPGHKCGSLQLVDLASTKPGTSSAPFTINAHQSDVACVSLNQPGTVVASASQKGTLIRLFDTQSKEKLVELRRGTDPATLYCINFSHDSSFLCASSDKGTVHIFALKDTRLNRRSALARVGKVGPMIGQYVDSQWSLASFTVPAESACICAFGRNTSKNVNSVIAICVDGTFHKYVFTPDGNCNREAFDVYLDICDDEDF", "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). Activated by the STK11/AMPK signaling pathway upon starvation, WDR45 is involved in autophagosome assembly downstream of WIPI2, regulating the size of forming autophagosomes. Together with WIPI1, promotes ATG2 (ATG2A or ATG2B)-mediated lipid transfer by enhancing ATG2-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes. Probably recruited to membranes through its PtdIns3P activity. SUBCELLULAR LOCATION: Preautophagosomal structure Cytoplasm Note=Diffusely localized in the cytoplasm under nutrient-rich conditions. Localizes to autophagic structures during starvation-induced autophagy. SIMILARITY: Belongs to the WD repeat PROPPIN family."}
+{"protein": "MASSEETPRSLAGKVALVTGAGRGIGKGIAVELAKRGASVVVNYNSAEKPAQEVVDEIAKTGSRAVAIKADITKVPEVSRLFQEALQHFGHLDIVVSNSGTEVFKPEDEVTEEDYDRVFNLNTRAQFFIAQHAYVHLRNGGRIVLMSSVAANMSGIPNHALYAGSKAAVEGFTRSFAVDAGHKKITVNAIAPGGVKTDMYDANAWHYVPNGKPGMPMEEIDKGLAAFCPLGRVAVPQDIGRVVAFLAHPDSEWVNGQVILLTGGSVT", "text": "FUNCTION: Hydroxynaphthalene reductase-like protein; part of the Pks2 gene cluster that mediates the formation of infectious structures (appressoria), enabling these fungi to kill insects faster (PubMed:29958281). The product of the Pks2 gene cluster is different from the one of Pks1 and has still not been identified (PubMed:29958281). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MEAFAQNLAKMVEEGGKAVAAYMRPREEGKPDDMTDDIADALKTIGEVANYWMSDPKRSFEAQSRLMMGYMGVWAGALQKLSGEKAEPIAKADPKDGRFKDPEWESPFFDALKQTYLVTSNWAESMVKEAEGLDPHTKHKAEFLVRQLSNAVAPSNFLMTNPELIRETLSSSGENLVRGMKNLAEDLVEGKGDLKIRQTDMSAFEVGRNLALSPGKVIFETELMQLIQYAPSTPSVKKTPVLIVPPWINKFYILDLTPEKSLIKWMVDQGLTVFVISWVNPDARLADKGFDDYMRDGIFAALDAVEKATGEHQAHTIGYCVGGTLLAVTLAYMAATGDDRVASSTFLTTQIDFTHAGDLKVFVDEAQLSVIERRMKEMGYLEGRKMADAFNMLRSNDLIWPYVVNNYLKGKQPFPFDLLFWNADSTRMPAANHSYYLRNCYLQNNIAKGLAEIAGVKIDMGKVTIPVYSLATREDHIAPPNSAYIGAGLLGGPVRFVLAGSGHIAGVVNPPVKHKYQYWTGGPTGGDYDVWLKGAQEHKGSWWPDWAQWFSALHPDEVPAREPGGSAFNPIEDAPGRYVREKS", "text": "FUNCTION: Polymerizes D(-)-3-hydroxybutyryl-CoA to create PHB which consists of thousands of hydroxybutyrate molecules linked end to end. PHB serves as an intracellular energy reserve material when cells grow under conditions of nutrient limitation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PHA/PHB synthase family. Type I PhaC subfamily."}
+{"protein": "MASTSLSLPSLKLQFPSHTSSSSRKNSSSYRVSIRPIQASVSEIPPYISSPSQSPSSSSSPPVKQAKLPAQKVPGDYGLPLVGPWKDRLDYFYNQGKNEFFKSRIQKHQSTVFRTNMPPGPFISFNPNVVVLLDGKSFPVLFDVSKVEKKDLFTGTFMPSTDLTGGYRVLSYLDPSEPNHAKLKKLMFYLLSSRRNEVIPEFHNSYSELFETLENELSTKGKAGLNAANDQAAFNFLARSLYGINPQDTELGTDGPKLIGKWVLFQLHPLLILGLPKVLEDLVMHTFRLPPALVKKDYQRLYNFFYENSTSVLDEAEKIGISREEACHNLLFATCFNSFGGIKIFFPNMLKWIGRAGAKLHSQLAQEIRSVISSNSGKVTMAAMEKMPLMKSVVYESLRIEPPVASQYGRAKHDMVIESHDASFEIKEGELLYGYQPFATKDPKIFDRSEEFVADRFIGEEGEKLLKHVLWSNGSETENASINNKQCAGKDFVVLVSRLLLVELFLRYDSFEIEVGASPLGAAITLTSLRRASF", "text": "FUNCTION: Cytochrome P450 of the CYP74A subfamily involved in the biosynthesis of jasmonic acid from lipoxygenase-derived hydroperoxides of free fatty acids. Catalyzes the synthesis of unstable allene oxide, which is further converted spontaneously by hydrolysis or cyclization. Can use 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid (13- HPOT) and 13S-hydroperoxy-9(Z),11(E)-octadecadienoic acid (13-HPOD) as substrates. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPGAHSPGATPGPGTATAERSSGVAPAASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAASRVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMAQALPRQRQRDASPGRGSHGQTPSPGALPLGRQTSQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPPPQGQQHLSGLGPPAGSPLPQRLPSPTSAPQQPASQAAPPTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQTSVSGPAPPKASGAPPGGQQRQGPPQKPPGPAGPTRQASQAGPVPRTGPPTTQQPRPSGPGPAGRPKPQLAQKPSQDVPPPATAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD", "text": "FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (PubMed:21441247, PubMed:23406870). Also involved in the regulation of axon outgrowth and synaptogenesis (By similarity). The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level (By similarity). SUBCELLULAR LOCATION: Synapse Golgi apparatus Presynapse Cytoplasmic vesicle, secretory vesicle, synaptic vesicle Note=Dissociates from synaptic vesicles and redistributes into the axon during action potential firing, in a step that precedes fusion of vesicles with the plasma membrane. Reclusters to presynapses after the cessation of synaptic activity. SIMILARITY: Belongs to the synapsin family."}
+{"protein": "HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDIYRYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC", "text": "FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (PubMed:8513799). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4) (PubMed:8513799). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit (PubMed:12657321). At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor (PubMed:12657321). In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity (By similarity). Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported (By similarity). FUNCTION: Monomer CBd: The basic subunit of crotoxin is a snake venom phospholipase A2 (PLA2) that exhibits weak neurotoxicity (10-fold less than the heterodimer) and very strong anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (By similarity). In addition, it shows the same effects described for the heterodimer and binds the nucleotide-binding domain (NBD1) of CFTR chloride channels and increases the channel current (By similarity). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:8513799). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
+{"protein": "MDTGKEKDRLDTENPSLIAGNTKQQATSQSSESKTKLAVEKDTDPPLPSRPTTRSATGRSKAAPDTVLSIRHASKNVLQSKPTTAVSLQDINSQTFQEGSNDIYSLLGARSGNEEAIKSKCSLSRPGSGKESDAADSASIKSVIPGEGTPVEVGSIFGDFTGAGQPQPLWDTKRKQVNIFDRSEPGLEDDDLSLDFESEFDCVEDIAADDNGDKILEEWRQKRKHYFILSAAGKPIYTRHGDDGLISPYIAIIQTIISFHQESSNPLKSFSAGRTKIVILSQGPLHLVAISRLLESDSQLRNQLDALYMQILSTLTLPALQHIFAVRPSTDLRRPLQGTESLLSSLADSFTKGSPSTLVSALECLKLRKSYRQQINSILLKSRVEPLLYGLVVAGGRLVSVIRPKKHSLHPGDLQLIFNMIFEADGVKAGGGESWIPICLPGFNSRGYLYMYVSFLDLHDHLPEDDKDINKDDAVAIILISADKESFFVLREMRDSVVQELEKSNSKNIIRAAIEKGRPATTDIVPGTVLRHFLYKSKSNVQFTMSSYSPDFTTLVARRRLLSTYHGLHSSVHSKNTHVKVQHCASRFMNSLAWVTPNFELYCVASPNSNRNALSQSANKIAQWVQQEDERVFIIGGAVF", "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": "MEIPKLLPARGTLQGGGGGGIPAGGGRVHRGPDSPAGQVPTRRLLLPRGPQDGGPGRRREEASTASRGPGPSLFAPRPHQPSGGGDDFFLVLLDPVGGDVETAGSGQAAGPVLREEAKAGPGLQGDESGANPAGCSAQGPHCLSAVPTPAPISAPGPAAAFAGTVTIHNQDLLLRFENGVLTLATPPPHAWEPGAAPAQQPRCLIAPQAGFPQAAHPGDCPELRSDLLLAEPAEPAPAPAPQEEAEGLAAALGPRGLLGSGPGVVLYLCPEALCGQTFAKKHQLKMHLLTHSSSQGQRPFKCPLGGCGWTFTTSYKLKRHLQSHDKLRPFGCPAEGCGKSFTTVYNLKAHMKGHEQENSFKCEVCEESFPTQAKLGAHQRSHFEPERPYQCAFSGCKKTFITVSALFSHNRAHFREQELFSCSFPGCSKQYDKACRLKIHLRSHTGERPFLCDFDGCGWNFTSMSKLLRHKRKHDDDRRFMCPVEGCGKSFTRAEHLKGHSITHLGTKPFVCPVAGCCARFSARSSLYIHSKKHLQDVDTWKSRCPISSCNKLFTSKHSMKTHMVKRHKVGQDLLAQLEAANSLTPSSELTSQRQNDLSDAEIVSLFSDVPDSTSAALLDTALVNSGILTIDVASVSSTLAGHLPANNNNSVGQAVDPPSLMATSDPPQSLDTSLFFGTAATGFQQSSLNMDEVSSVSVGPLGSLDSLAMKNSSPEPQALTPSSKLTVDTDTLTPSSTLCENSVSELLTPAKAEWSVHPNSDFFGQEGETQFGFPNAAGNHGSQKERNLITVTGSSFLV", "text": "FUNCTION: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ZXD family."}
+{"protein": "MLENLWEVRQALPIYLLTATIGLAVSCCFTLICPHVCRLIPALTTYGKAADQLEENSLVARISVPKKWFKHFYALGLLTLLLCLHCIHSLIHNPDFLPTIPIKFLTILTRSYSIPPIAPSTAVLALLLITFHVARRLYETLFVSVYSDSRMNVFHYIVGIVHYIILPISIMCETQGVITKKEIFHVSVDDITLTQWAGAVLFWVCNWKQHQIAEQIANTRKGPRGLIRNYAYGICFGRWFNLVSCPHFLFEICIYLSLLLVIPTAYVYRFVVLFVCVNQTFAALITHSWYHKTFPKYPKTRKALIPYVL", "text": "FUNCTION: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N- glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily."}
+{"protein": "MVDSDDDGDRRRDKFARERRDEDYRRGGGGFNRYDNKRPGGRRDDYQVKRSRGDDADDSFDPVSRSGNGSDLPTESDSIYSGPLQTFKKFLTSQEDDISEEDAIKKYNEYKTEHRKHQLERFFRAHKDEEWFRLKYKPDDAKKLREAHLENVQKRLQVFNELKEQGQFNKFSLDFGDAEAIIRMLDSVVVKLENGTEDELKAVLAQKLEDESLADIKKDENGNGTEQPKEEPEVKQESGATEELEEGAIEDGTEKSSNKVNIHRTCSVFLRNIPPGLTYEELEGLCKKSPGFLRLALTDGIAERKFYRRGWATFKRDINIKEICWALNAHRLRETDLNAIINRDITRRVRTNNGIASHKQVAINDLKLAVKLTVLYDKKIGLFNAADEADADREMDIRMGVDLVAASTNPLIKEVKSLVPHDVLNDISEEEAELLGVSNGGEAPAEKIRFERDDNILKALDLLIVYLRIVHSIDFYNHGHYAQEDSMPNRCGLIHVRGQPPSGVSITTDEDGALVVPQKFVNDFISGFNSRIEKGLIEKQYVSEEELEKMGKKDGEKEVEAFIQKNTVELAKDKWLCPLSGKKFKGPEFIRKHLQSKHEDKLEEARAEADFFNNYLADAQRPVDCEPKQAPRDDHRGGGGGERGGYGRERDDDRGPGGGGRNSFGGGGYDRRPQFPPRHSLGGRGGGGRYFEDAPRRQPVSYRDLDAPDDIP", "text": "FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex, thereby playing a role in RNA- mediated gene silencing (RNAi) by miRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARS2 family."}
+{"protein": "MELSYTTTMHYRDVVFYVTTDRNRAYFVCGGCVYSVGRPYASQPGEIAKFGLVVRGTGPDDRVVANYVRSELRQRGLQDVRPIGEDEVFLDSVCLLNPNVSSELDVINTNDVEVLDECLAEYCTSLRTSPGVLISGLRVRAQDRIIELFEHPTIVNVSSHFVYTPSPYVFALAQAHLPRLPSSLEALVSGLFDGIPAPRQPLDAHNPRTDVVITGRRAPRPIAGSGAGSGGAGAKRATVSEFVQVKHIDRVGPAGVSPAPPPNNTDSSSLVPGAQDSAPPGPTLRELWWVFYAADRALEEPRADSGLTREEVRAVRGFREQAWKLFGSAGAPRAFIGAALGLSPLQKLAVYYYIIHRERRLSPFPALVRLVGRYTQRHGLYVPRPDDPVLADAINGLFRDALAAGTTAEQLLMFDLLPPKDVPVGSDVQADSTALLRFIESQRLAVPGGVISPEHVAYLGAFLSVLYAGRGRMSAATHTARLTGVTSLVLAVGDVDRLSAFDRGAAGAASRTRAAGYLDVLLTVRLARSQHGQSV", "text": "FUNCTION: May participate in DNA packaging/capsid maturation events. Promotes efficient incorporation of tegument proteins UL46, UL49, and US3 into virions. May also play a role in capsid transport to the trans-Golgi network (TGN) (By similarity). SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus. SIMILARITY: Belongs to the alphaherpesvirinae UL21 protein family."}
+{"protein": "MPGDPTATAKGNEIPDTLMGYIPWTPELDSGEVCGIPTTFKTRDEWKGKKVVIVSIPGAYTPICHQQHIPPLVKRVDELKAKGVDAVYVIASNDPFVMAAWGNFNNAKDKVVFATDIDLAFSKALGATIDLSAKHFGERTARYALIIDDNKIVDFASDEGDTGKLQNASIDTILTKV", "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": "MNFKYIFAVSFLIASAYARSVQNDEQSLSQRDVLEEESLREIRGIGGKILSGLKTALKGAAKELASTYLHRKRTAEEHEEMKRLEAVMRDLDSLDYPEEASERETRGFNQDEIANLFTKKEKRILGPVLGLVSDTLDDVLGILG", "text": "FUNCTION: Maximin-H5 shows antibacterial activity only against the Gram-positive bacteria S.aureus. The other bacterial and fungal strains tested were resistant to it. The presence of metal ions, like Zn(2+) and Mg(2+), did not increase its antimicrobial potency. Does not show hemolytic activity (in a concentration up to 80 uM). FUNCTION: Maximin-3 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans, but not against A.flavus nor P.uticale. It has little hemolytic activity. It possess a significant cytotoxicity against tumor cell lines. It possess a significant anti- HIV activity. It shows high spermicidal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
+{"protein": "MSETLNTPPTYAWVLKAFSSKLAGTVTKPVTKMSSYIEDAESDAELPQDAKEDLRPTETLTPLKSKAAQNGILKTPGTLQIKKTVNFKDISKDAATWNRPTKNNFLFTRLDDENPLMGHEEFKSPLLQSTPKPNINNPDNENKSKHDEFDNRYNININESYKNETKSNQRLGEDVPSKKKYPHSMDAEISKFKWDSNNNNDWSSLMKDCFRDVVNNNRKMKEIIKDVMIDTSQAFPSESLDEPDYTINLDAPRSSSGKYWKQKFSMLDSAHSDLELELTSIRERLESLILEKQEEINFWKQRCRALETEKIHNHQGQQSKYKGKEFVGNRFSQMRELYTAKPSPITTKVVSRPSQSDVREPQEQVPSKNLHRGADMSHLAAQMLTHSSKKSHTTNLIPSEGIISSTPISAASKVRMNLMQSNQTPTPAPFSIAAKKSHLPSKLSFPQDGGSLSSATTLQQLPKARVTPNVLSSLSSNLGKTNPTSVYQSKANVTTSADVEKPQVKVATSSRVDYDLKSPNQRTANAKKRLEERRRRRKLKLQELQLNS", "text": "FUNCTION: Required for bipolar spindle formation. May act as a regulator of the p34cdc2/cyclin B kinase. Required for full activation of the plo1 kinase. However, in cut12.1 cells at restrictive temperature the H1 kinase does rise concomitant with entry into mitosis, indicating that cut12 is not required for activation of p34cdc2/cyclin B. The cut12.s11 allele may promote cdc2-independent phosphorylation of SPB proteins thereby overcoming the requirement for cdc25 in cell cycle progression. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body."}
+{"protein": "MQNRHIAMGILLLSLLLSSWLYWGSDFKLEQVLTSREWQSKMVSLIKTNSNRPAMGPLSRVDVTSNVKYLPNGTYLRVSIVKLFSDDNSAESVINISEFGEWDISDNYLLVTPVEFKDISSNQSKDFTDEQLQLITQLFKMDAQQSRRVDIVNERTILFTSLSHGSTVLFSNS", "text": "FUNCTION: Interacts with ToxR and stimulates its activity. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein; Periplasmic side."}
+{"protein": "MADLSLLQEDLQEDADGFGVDDYSSESDVIIIPSALDFVSQDEMLTPLGRLDKYAASENIFNRQMVARSLLDTLREVCDDERDCIAVLERISRLADDSEPTVRAELMEQVPHIALFCQENRPSIPYAFSKFLLPIVVRYLADQNNQVRKTSQAALLALLEQELIERFDVETKVCPVLIELTAPDSNDDVKTEAVAIMCKMAPMVGKDITERLILPRFCEMCCDCRMFHVRKVCAANFGDICSVVGQQATEEMLLPRFFQLCSDNVWGVRKACAECFMAVSCATCQEIRRTKLSALFINLISDPSRWVRQAAFQSLGPFISTFANPSSSGQYFKEESKSSEEMSVENKNRTRDQEAPEDVQVRPEDTPSDLSVSNSSVILENTMEDHAAEASGKPLGEISVPLDSSLLCTLSSESHQEAASNENDKKPGNYKSMLRPEVGTTSQDSALLDQELYNSFHFWRTPLPEIDLDIELEQNSGGKPSPEGPEEESEGPVPSSPNITMATRKELEEMIENLEPHIDDPDVKAQVEVLSAALRASSLDAHEETISIEKRSDLQDELDINELPNCKINQEDSVPLISDAVENMDSTLHYIHSDSDLSNNSSFSPDEERRTKVQDVVPQALLDQYLSMTDPSRAQTVDTEIAKHCAYSLPGVALTLGRQNWHCLRETYETLASDMQWKVRRTLAFSIHELAVILGDQLTAADLVPIFNGFLKDLDEVRIGVLKHLHDFLKLLHIDKRREYLYQLQEFLVTDNSRNWRFRAELAEQLILLLELYSPRDVYDYLRPIALNLCADKVSSVRWISYKLVSEMVKKLHAATPPTFGVDLINELVENFGRCPKWSGRQAFVFVCQTVIEDDCLPMDQFAVHLMPHLLTLANDRVPNVRVLLAKTLRQTLLEKDYFLASASCHQEAVEQTIMALQMDRDSDVKYFASIHPASTKISEDAMSTASSTY", "text": "FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4. May play a role in regulation of cell division in renal glomeruli. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3."}
+{"protein": "MLSLQTLAKKVVACNYLSSDYDYMLQRFGLWWDLGPIHLCNNCKQIFSYKHLQCFSEDDLCLEAALVKAVKSDNLELIRLFVDWGANPEYGLIRVPAVHLKRLCTELGGLTPVSEPRLLEILKEVAKLKSCAGVLLGYDMFCHNPLLETVTRTTLDTVTYTCSNIPLTGDTAHHLLTKFWFALALRHNFTKAIHYFYKRHKNHLYWRVACSLYFNNIFDIHELCREKEICISPNLMMKFACLRKKNYAAIYYCYRLGASLDYGMNLSIYNNNTLNMFFCIDLGATDFDRAQRIAHKTYMYNLSNIFLVKQLFSRDVTLALDVTEPQEIYDMLKSYTSKNLKRAEEYLTAHPEIIVID", "text": "FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Inhibits also the host cGAS/STING-mediated type I interferon production by inducing host IRF3 degradation through the proteasome pathway. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the asfivirus MGF 360 family."}
+{"protein": "MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTDKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLESKDSIKLQDCSALCDEEDEEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKADAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM", "text": "FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C- terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8- phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATG3 family."}
+{"protein": "MYLLVFKLFLFLSLLQISVSARNLASQEPNQFQLLKYHKGALLSGKISVNLIWYGKFKPSQRAIISDFITSLTHTSPTSKTLHQPSVATWWKTTEKYYKLATPSKNSSPLSLTLGKQIIDESCSLGKSLTDKKIQTLASKGDQRNAINVVLTSADVTVTGFGMSRCGTHGHARGLGKRGSKFAYIWVGNSETQCPGQCAWPFHAPVYGPQSPPLVAPNNDVGLDGMVINLASLLAGTATNPFGNGYYQGPQNAPLEAASACPGVYGKGAYPGYAGDLLVDTTTGGSFNAYGANGRKFLLPALYDPTTSACSTMV", "text": "FUNCTION: Required for cell expansion in leaves. May mediate brassinosteroid (BR)-induced leaf growth. May play a role in the control of BR responses in roots. May be involved in signaling processes that coordinate BR responses with environmental or developmental signals. SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the EXORDIUM family."}
+{"protein": "METKKYGLGTTAIHAGTLKNLYGTLAMPIYQTSTFIFDSAEQGGRRFALEEAGYIYTRLGNPTTTVLENKIAALEEGEAAVATSSGMGAISSTLWTVLKAGDHVVTDKTLYGCTFALMCHGLTRFGIEVTFVDTSNLDEVKNAMKKNTRVVYLETPANPNLKIVDLEALSKLAHTNPNTLVIVDNTFATPYMQKPLKLGADIVVHSVTKYINGHGDVIAGLVITNKELADQIRFIGLKDMTGAVLGPQDAYYIIRGMKTFEIRMERHCKNAKKVVEFLNKHPKIERVYYPGLETHPGHEIAKKQMKDFGAMISFELKGGFEAGKTLLNNLKLCSLAVSLGDTETLIQHPASMTHSPYTKEEREAAGITDGLVRLSVGLENVEDIIADLEQGLEKI", "text": "FUNCTION: Plays an important role in the resistance of F.nucleatum to the antibacterial agent 3-chloro-DL-alanine (3CA), thanks to its 3CA chloride-lyase (deaminating) activity. FUNCTION: Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia; methanethiol (methyl mercaptan) is considered to be one of the main causes of the oral malodor associated with periodontitis. Also displays homocysteine desulfhydrase activity, degrading homocysteine to produce hydrogen sulfide, 2-oxobutanoate and ammonia. L-cysteine and S-methyl-L-cysteine are poor substrates for the enzyme. SIMILARITY: Belongs to the trans-sulfuration enzymes family. L- methionine gamma-lyase subfamily."}
+{"protein": "RLISAVILAVCSLISRRKPSPGSKKKRPPGPWRLPLIGNLLHLATSQPHVALRDLAMKHGPVMYLRLGQVDAVVISSPAAAQEVLRDKDTTFASRPSLLVADIILYGSMDMSFAPYGGNWRMLRKLCMSELLNTHKVRQLAAVRDSETLSLVRKVVYAAGAGGGGRGQRGEAPVVNLGRLVLSCSMAITGRATLGKLCGDEIMSVVDVAVLYGSGFCAGDLFPSLWFVDVVTGLTRRLWTARRRLDAIFDRILAECEARQRQEEKMTGDDGFLGVLLRIRDDDGEPETGGISTTSIKAILFDMLAGGTETTSSAAEWIMSELMRKPEAMAKAQAEVRGALDGKSPEDHEGQMDKLSYTRMVVKEGLRLHPVLPLLLPRSCQETCDVGGFEVTKGTKVIVNAWALARSPERWHDPEEFRPERFADDDGSSAAVAVDYRGSQFEYIPFGSGRRMCPGNTFGLAALELMVARLLYYFDWSLPDGMRPEELDMDTVVGSTMRRRNHLHLVPSPYKETELTVGI", "text": "SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MNDLNVLVLEDEPFQRLVAVTALKKVVPGSILEAADGKEAVAILESCGHVDIAICDLQMSGMDGLAFLRHASLSGKVHSVILSSEVDPILRQATISMIECLGLNFLGDLGKPFSLERITALLTRYNARRQDLPRQIEVAELPSVADVVRGLDNGEFEAYYQPKVALDGGGLIGAEVLARWNHPHLGVLPPSHFLYVMETYNLVDKLFWQLFSQGLATRRKLAQLGQPINLAFNVHPSQLGSRALAENISALLTEFHLPPSSVMFEITETGLISAPASSLENLVRLRIMGCGLAMDDFGAGYSSLDRLCEFPFSQIKLDRTFVQKMKTQPRSCAVISSVVALAQALGISLVVEGVESDEQRVRLIELGCSIAQGYLFARPMPEQHFLDYCSGS", "text": "FUNCTION: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG (PubMed:18344366, PubMed:19376848). Cannot use cyclic AMP or cyclic GMP (PubMed:18344366). Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster (PubMed:15687209, PubMed:15659157). Negatively regulates the expression of cup genes by antagonizing the activity of RocA1 (PubMed:15659157)."}
+{"protein": "MRRKLTFQEKLLIFIKKTKKKNPRYVAIVLPLIAVILIAATWVQRTEAVAPVKHRENEKLTMTMVGDIMMGRHVKEIVNRYGTDYVFRHVSPYLKNSDYVSGNFEHPVLLEDKKNYQKADKNIHLSAKEETVKAVKEAGFTVLNLANNHMTDYGAKGTKDTIKAFKEADLDYVGAGENFKDVKNIVYQNVNGVRVATLGFTDAFVAGAIATKEQPGSLSMNPDVLLKQISKAKDPKKGNADLVVVNTHWGEEYDNKPSPRQEALAKAMVDAGADIIVGHHPHVLQSFDVYKQGIIFYSLGNFVFDQGWTRTKDSALVQYHLRDNGTAILDVVPLNIQEGSPKPVTSALDKNRVYRQLTKDTSKGALWSKKDDKLEIKLNHKHVIEKMKKREKQEHQDKQEKENQVSVETTT", "text": "FUNCTION: Essential for the synthesis of the polyglutamate capsule of B.anthracis which is one of the principal virulence factors during anthrax infection. May form a polyglutamyl synthetase complex together with proteins CapB and CapC. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CapA family."}
+{"protein": "MLKCKQPGARFIHGAVHLPSGQIVFHTIHSPTLASALGLPGENVPIPALFRASGLNVRESLPMTNMRAPIISLARLILAPNPYILEGQLTVGMTQDNGIPVLFARPVIEVKSGPESNIKASSQLMIAEDSCLNQIAPFSASEHPAFSMVESVKRVRVDEGANTRRTIRDILEIPVTVLSSLQLSPTKSILKKAPEPPPPEPQATFDAAPYARIFYDIGRQVPKLGNAPAAQVSNVLIANRSHNSLRLVPNPDLLPLQHLYLKHVVLKSLNLENIVQDFEAIFTSPSDTISEAETKAFEKLVEQAKNTVENIVFCLNSICSTSTLPDVVPDVNNPNISLALEKYFLMFPPSGTIMRNVRFATPIVRLLCQGAELGTMAQFLGKYIKVKKETGMYTLVKLYYLLRI", "text": "SIMILARITY: Belongs to the lymphocryptovirus BTRF1 family."}
+{"protein": "MGQESSKPVWPNPTGGYQSNTGRRYGRRHAYVSFRPPTSQRERIASQRKTNSEVPMHRSAPSQTTKRSRSPFSTTRRSWDDSESSGTNLNIDNEDYSRYPPREYRASGSRRGMAYGHIDSYGADDSEEEGAGPVERPPVRGKTGKFKDDKLYDPEKGARSLAGPPPHFSSFSRDVREERDKLDPVPAARCSASRADFLPQSSVASQSSSEGKLATKGDSSERERREQNLPARPSRAPVSICGGGENTSKSAEEPVVRPKIRNLASPNCVKPKIFFDTDDDDDMPHSTSRWRDTANDNEGHSDGLARRGRGESSSGYPEPKYPEDKREARSDQVKPEKVPRRRRTMADPDFWTHSDDYYKYCDEDSDSDKEWIAALRRKYRSREQTLSSSGESWETLPGKEEREPPQAKVSASTGTSPGPGASASAGAGAGASAGSNGSNYLEEVREPSLQEEQASLEEGEIPWLQYHENDSSSEGDNDSGHELMQPGVFMLDGNNNLEDDSSVSEDLEVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDALPEILVTEDHGAVGQEMCCPICCSEYVKGEVATELPCHHYFHKPCVSIWLQKSGTCPVCRCMFPPPL", "text": "FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting."}
+{"protein": "MNDIAHNLAQVRDKISAAATRCGRSPEEITLLAVSKTKPASAIAEAIDAGQRQFGENYVQEGVDKIRHFQELGVTGLEWHFIGPLQSNKSRLVAEHFDWCHTIDRLRIATRLNDQRPAELPPLNVLIQINISDENSKSGIQLAELDELAAAVAELPRLRLRGLMAIPAPESEYVRQFEVARQMAVAFAGLKTRYPHIDTLSLGMSDDMEAAIAAGSTMVRIGTAIFGARDYSKK", "text": "FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. May have a carrier function to deliver PLP to the target enzymes or a protective function so that PLP does not inactivate essential lysines in proteins (PubMed:26872910). Does not have amino acid racemase activity (PubMed:24097949). SIMILARITY: Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. SIMILARITY: Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family."}
+{"protein": "MSNTLFSLAFGVGSQNRQGAWLEVFYAQPLLNPSAELVAAVAPVLGYEGGNQAIAFSNAQAAQLAEALKGVDAAQAALLTRLAESHKPLVATLLAEDAALSSTPEAYLKLHLLSHRLVKPHGVSLAGIFPLLPNVAWTNQGAVDLGELAELQLEARLKGELLEVFSVDKFPKMTDYVVPAGVRIADTARVRLGAYIGEGTTIMHEGFVNFNAGTEGPGMIEGRVSAGVFVGKGSDLGGGCSTMGTLSGGGNIVIKVGEGCLIGANAGIGIPLGDRNTVEAGLYITAGTKVNLLDENNELVKVVKARDLAGQTDLLFRRNSLNGAVECKTHKSAIELNEALHAHN", "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": "MRLTSKGRYAVTAMLDVALHSHEGPVPLADISERQGISLSYLEQLFSRLRKNGLVASVRGPGGGYLLGKAADAIAVGAVITAVDESVDATKCQGKEGCQGGERCLTHVLWRDLSERISDFLNNITLAELVNNQEILVVADRQNSNEIRRAPHGRMHETINVNLRA", "text": "FUNCTION: Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins."}
+{"protein": "MAKQTLLLSPPSLSSQPGKLNETLQSYNRNATDLQMLDRLALGLASLPDSAYSSIVILAGGDNSFSESLKLINRQIFNQIIGSLRRGGYIYGQDAVSGIAFDHNEAILAGLIHVGNGKYQKPDIKEMQAVPLRLGRKNDHLAGAPSLQESAAEHPCPPETMISASTMNSNEASDDELINEDNLLDDSELSAPIIQRGPAPECRPKAGKRRRACKDCTCGLAQKLQEEDAVKRADADEQLDAMRLLHDDLAEVDFTVQGKVGSCGNCSLGDAFRCEGCPFIGLPAFQPGEEVRLLNNDVQL", "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": "MEVPSYFDPDYDPSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSKLRRAKNGLISMTELQQKNVPPSSRSPRRRVAGVTNNVTARISSKRKINMVDEANDTEISKTSQFEDNVMGMLQDENVQVLNTNTITISEESEFHASKIAKIDSRNEEITHIPFETQTELNAAVVNLDNSMESSFSIVQNLTNKDSSVDTATYDFSAEVGNIVTPASKFLDYDQSYLVNASVSGDPTPVKVLNTTSPKSENPLNQSSFLSFLGENLKPKFTSRSSSVYASPIKSSLNSLECNPSNLLSVRKNFQQSSDSYLKSNKSFDQLNNLVGLSTGNSENFTPENNSFSWTHPKKNSSSPLPQSQSSSIFVEHLNQLYEANASIHRPVNPAFSTNFGLEASNTSTPEKKKFDSQKPDDDSVNEISSDLGLSTTGIDRVEENISLTKDRQPKRPYFSLGSFISLIFSFTKVVNSLWLVLLVVPLLGFVGFWHQEVQRVGFCGVPAEPYPSSLYYLQPGVLRSSIESAYSFAHSLGIEASCQPCPENAECGFNRQLFCKEGLKASFPLLADFGLKPYPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKNLNGKSFVDNFKDRYYMYKQDIDNVVGLKDFKVYLKTTLNRLYNSKLTRKVLYYLFSPLFTLELWKLRVRGALSKFPTNCLRSVYSHTVSLMKYLTSAVISCWRIYLLIGILAAITGTVVWRIRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPRVEVVQLRSDCFVSGVADDKGLFELVHLPLSIQLEIWEKVVSVLEGMVSVKVWDSERLAKNRAWEWIGVFSDDIAL", "text": "FUNCTION: Required for correct meiotic chromosome segregation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein."}
+{"protein": "MNPDNTIAVITETIPIGMQFDKVYLTTFNMWREILSNTIKTLDISSFYWSLSDEVGTNFGTVILNEIVQLPKRGVRVRVAVNKSNKPLKDVERLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNRNLAADLTQIFEVYWYLGVNNLPYNWKNFYPSYYNTDHPLSINVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIGNASKFVYVSVMNFIPIIYSKAGKILFWPYIEDELRRSAIDRQVSVKLLISCWQRSSFIMRNFLRSIAMLKSKNIDIEVKLFIVPDADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDICGASINITPDDGLGLRQQLEDIFIRDWNSKYSYELYDTSPTKRCRLLKNMKQCTNDIYCDEIQPEKELPEYSLE", "text": "FUNCTION: DNA nicking enzyme that cleaves extruded cruciform DNA at its tip. Probably nicks viral hairpins. SUBCELLULAR LOCATION: Virion. Note=Virion core. SIMILARITY: Belongs to the orthopoxvirus OPG042 family."}
+{"protein": "MAPSVPAAEPEYPKGIRAVLLGPPGAGKGTQAPRLAENFCVCHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVVELIEKNLETPLCKNGFLLDGFPRTVRQAEMLDDLMEKRKEKLDSVIEFSIPDSLLIRRITGRLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSDDNEKALKIRLQAYHTQTTPLIEYYRKRGIHSAIDASQTPDVVFASILAAFSKATCKDLVMFI", "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. 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": "MSPLKIYGPIRIRSMQTGITKWKEGSFEIVEKDNRVSLLVHYNTGGIPRVFQLSHNIKNVVLRPSGIKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLHAAMKASQGSGSFGTILGSRTSQKETNRQLSYSDNQASSKRGSLETKDEIPFRKVLGSPGRGPIKTVTGGGMAVTRTIPSLTLTSTPLRSGLLENRTEKRKRMLSGSELTEDYPKENDSSSNNKAMTDPSRKYLTSCREKQLSLKQAEENRTSGLLPLQSSSFYGSRAGSKDYSSGVTNLDRCNVSSQTPSAKRSLGFLPQPTPLSVKKLRCNQDYAGWNRPRVPLSSHQQQLQGFSNLGNTCYMNAILQSLFSLQSFANDLLKQSIPWKKIPFNALIRRFANLLIKKDICNSETKKELLKKVKNAISATAERFSGYVQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVLGEENLPDTSATKVFTCPVITNLEFEVQHSIICKACGETIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKLGQQVIIPRFLTLASHCTESTKPPVTLGWSAPVAISRPLRACQMMNSCITSPSAPSKKFTFKSKSSVTSCLDSDSEDELKRSVVLSQRLCDLPGNEQYQEDVEKDLKLCRLEPGKAELENSGFDRMSEEEVLAAVLEISRREASPVLSPEDDDKPTSSPDTGFAEDDIPEMPENPDAMEIEKSKTITEPGPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDVDREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFLDSLGSDEDSGNEDVFDMEYTEAEAEELKRNAETGALPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFYMHKEIFDELLETEKTSQALSMEVGRAARQAS", "text": "FUNCTION: Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1. SIMILARITY: Belongs to the peptidase C19 family."}
+{"protein": "ADTIVAVELDSYPNTDIGDPNYPHISIADENSLHFSFHKFSQNPKDLIL", "text": "FUNCTION: D-mannose/D-glucose-binding lectin. SIMILARITY: Belongs to the leguminous lectin family."}
+{"protein": "MPLASPRQLFLLAFLACVAIMGGALYLEHVVGLEACPLCVVQRIFFILIGLTCLAGAIQGPGLRGRRIYSVLVFLLALGGGATAARQVWLQTVPLDQLPACLPSLDYMMQALPFQEVIRLVLHGTADCAQVSWTLFTLSIPEWSLLAFVAYLGFSIVQFLRRA", "text": "FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein. 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. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. SIMILARITY: Belongs to the DsbB family."}
+{"protein": "MKISRILLAAVILSSVFSITYLQSDHNTEIKVAADRVGA", "text": "FUNCTION: Intercellular signaling molecule that inhibits excision of the mobile genetic element ICEBs1 when cells are crowded by cells that contain ICEBs1 and produce the PhrI peptide (PubMed:16105942). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Acts by inhibiting RapI activity (PubMed:16105942). SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Produced through an export-import maturation process. SIMILARITY: Belongs to the Phr family."}
+{"protein": "MENSALSNCVRRTNFSNQQRTMQEGLEESSWTMYFETEDGLGHYDDSSMMSDAASPMGCVEEDTASSPSNRTEGYSGMEDNTIEEKTMNNGKIEEKILNKNGIKIEEYCAELKKRGLCLVPLSMLSNYIG", "text": "FUNCTION: Involved in the regulation of plant growth."}
+{"protein": "MAEAHQAVAFQFTVTPDGIDLRLSHEALKQICLSGLHSWKKKFIRFKNGVITGVYPASPSSWLIVVVGVMSTMYAKIDPSLGIIAKINRTLDTTGYMSSQTKNIVSGVLFGTGLWVALIITMRYSLKVLLSYHGWMFAEHGKMSRATRIWMCMVKIFSGRKPMLYSFQTSLPRLPVPAVKDTVNRYLESVRPLMKDEDFKRMTALAQDFAVNLGPRLQWYLKLKSWWATNYVSDWWEEYVYLRGRGPLMVNSNYYAMDLLYVIPTHLQAATAGNGIHAILLYRHKLDREEIKPILFLGSTVPLCSAQWERMFNTCRIPGEETDTIQHLRDSKHIVVFHKGRYFKVWLYHDGRLLKPREIEQHIQRILDDPSEPHAGEAKLAALTAGERVPWAKCRQAYFGRGKNKQSLDAVEKAAFFVTLDETEQGYREEDPDASMDSYAKSLLHGRCSDRWFDKSFTFIVFKNGKMGMNAEHSWADAPVVGHLWEYVMSTDCFQLGYAEDGHCKGDTNPNIPYPTRLQWDIPEECQDVIETSLNTANILASDVDFHSFPFHAFGKGLIKKCRTSPDAFVQLALQLAHYKDMGKFCLTYEASMTRLFREGRTETVRSCSSESCNFVLAMVDPTQTVKQKLRLFKIASEKHQHLYRLAMTGSGIDRHLFCLYVVSKYLAVDSPFLKEVLSEPWRLSTSQTPQQQVELFDLERNPEYVSSGGGFGPVADDGYGVSYILVGENLINFHISSKFSSPETDSHRFGKHLKQAMNDIMALFGFSSNSRKEFH", "text": "FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion (By similarity). Plays an important role in hepatic triglyceride metabolism (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the carnitine/choline acetyltransferase family."}
+{"protein": "MRKLYCVLLLSAFEFTYMINFGRGQNYWEHPYQKSDVYHPINEHREHSKEYEYPLHQEHTYQQEDSGEDENTLQHAYPIDHEGAEPAPQEQNLFSSIEIVERSNYMGNPWTEYMAKYDIKEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLKPVATGNQDLKDGGFAFPPTNPLISPMTLDHMRDFYKNNEYVKNLDELTLCSRHAGNMNPDNDKNSNYKYPAVYDYNDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDKSFQNYTYLSKNVVDNWEKVCPRKNLENAKFGLWVDGNCEDIPHVNEFSANDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNASMIKSAFLPTGAFKADRYKSRGKGYNWGNYNRKTQKCEIFNVKPTCLINNSSYIATTALSHPNEVEHNFPCSLYKDEIKKEIERESKRIKLNDNDDEGNKKIIAPRIFISDDIDSLKCPCDPEIVSNSTCNFFVCKCVEKRAEVTSNNEVVVKEEYKDEYADIPEHKPTYDKMKIIIASSAAVAVLATILMVYLYKRKGNAEKYDKMDEPQDYGKSNSRNDEMLDPEASFWGEEKRASHTTPVLMEKPYY", "text": "FUNCTION: Involved in parasite invasion of erythrocytes. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the apicomplexan parasites AMA1 family."}
+{"protein": "MYSGQNKIHKDKGVAPTEFEEQVTQALFDLENTNQELKSELKDLYINQAVQMDISGNRKAVVIYVPFRLRKAFRKIHLRLVRELEKKFSGKDVIFVATRRIMRPPKKGSAVQRPRNRTLTSVHEAMLEDVAYPAEIVGKRTRYRLDGTKIMKVFLDSKLKNDTEYKLETMVGVYRKLTGKDVVFEYPVIEA", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS7 family."}
+{"protein": "MEAAIEFDEIVKKLLNIYINDICTMGEKRLLNNYEKSILDRIYKSCEYIKKNYELDFNSMYNQININDITTSDIKSKIIESLLIDSRPSVKLATLSFISLIAEKWGEKNRTKIMEILSNEIVEKISNNGKDFIDFIDRDDDDIVDDYVLITNYLKITIFGAILGITAYYICKYLLKSIF", "text": "FUNCTION: Plays a role in the inhibition of host apoptosis by sequestering and inactivating several proapoptotic BCL-2 proteins, including BAK1 and BAX. Prevents the conformational activation of both of them. SUBCELLULAR LOCATION: Host mitochondrion Host membrane; Single-pass membrane protein."}
+{"protein": "MAQHQGGKGNFAEDPKRASEAGKKGGQASGGNFKNDPQRASEAGKKGGQRSHGGN", "text": "FUNCTION: May be involved in the regulation of the production of pyocyanine, one of the major virulence factors secreted by P.aeruginosa, and other virulence factors. SIMILARITY: Belongs to the con-10 family."}
+{"protein": "METPAGKADRPRDHDSEQSQDNVVSWEGEDDPTNPLNWSPLAKWVHVAIISIGTFTIAREKSPLASSIFAPGVVELAHEFHEENQLLTTIVVSIFVLGLAFGPLLAAPISEMYGRWICYTVFNILYTIFTVACGVSTNISMLIVFRFFAGVTGSAPLTIGGGTVADLFPMHQRGLALSFVTLGQAVAPAIGPVAGGFLTQNLGWRWVFWLLTIVNGTITICQILFTRETYAMTILNRRAKRLRKTTVHSSVTHRSVNFAIFFYSLVRPCKLLLLSPISLIVALCCAVIYGILYVLVTTFSPVFQDTYHFSIGISGLGYLGLGIGNLVGLWIFSMTSDRYMVAQANRFGSAKPEHRLPMMILSGPVIAAGLFWYGWSVQARIHWMMPIVGSGIVGLGNMFFFMPMVSYLVDSFPTYAASAIAANAVLRSIGGAVLPLAGQRMYDTLGFGWGNSILAFMALVFNPLLIAIYRYGEYIRTRWQVKL", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy sauce brewing (PubMed:30466366). Might be required for efficient secretion of heptelidic acid (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MEGEERGYWRWSKRDFFPEESFQSFGSYRAALSQTCSRFKNRLVSRSDDENERFELKKQSEHEMKRCLTWWDLVWFGFGSVIGAGIFVLTGQEAHEQAGPAIVLSYVVSGLSAMLSVFCYTEFAVEIPVAGGSFAYLRIELGDFAAFITAGNILLESIVGTAAVARAWTSYFATLLNRSPNALRIKTDLSSGFNLLDPIAVVVIAASATIASISTRKTSLLNWIASAINTLVIFFVIIAGFIHADTSNLTPFLPFGPEGVFRAAAVVYFAYGGFDSIATMAEETKNPSRDIPIGLLGSMSIITVIYCLMALSLSMMQKYTDIDPNAAYSVAFQSVGMKWGKYLVALGALKGMTTVLLVGALGQARYVTHIARTHMIPPIFALVHPKTGTPINANLLVAIPSALIAFFSGLDVLASLLSISTLFIFTMMPIALLVRRYYVRQDTPRVHLIKLITCLLFVVVSSMGTSAYWGMQRKGSWIGYTVTVPFWFLGTLGIVFFVPQQRTPKVWGVPLVPWLPCLSIATNIFLMGSLGAMAFVRFGVCTLAMLLYYFLLGLHATFDMAHQQIVPRT", "text": "FUNCTION: High-affinity permease involved in the transport of the cationic amino acids (e.g. arginine, and, to a lower extent, citrulline and glutamate). Transport mostly basic amino acids, and, to a lower extent neutral and acidic amino acids. 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": "MRLSFGKQRYHGGTTVTLTEQGASDSLRAAQAIFQNHSNEVSSPCPPVTVSRNPQTRLSEPSLQKSGRKQEQKKARIRTKQVPKIKTTAPNDVELSKKHRSSPAGKDNVSSTAQMAAALAHSQSKLSSDNNSSHSSALDTLKVLETPNLNGLLGIHSRSSSRNGSNESLTPGQRTPDNRSQENLLTSFSSGRRLSSSSMEPATNKDSNKALPKRRPSPPLQSSLVGSGQLHENENLSSISIDSRHSLNPDTSDVISNRSQTSLSQTINQLSLCESEPSIASSNTTTTTSNQGSGLPNLVPNYSSDMRKKKLVNKFKRKVFGSKPKHLSSQYEMDASSEELGQHEQQPSMRFKTTLRKTSVSTNAENDHASSLHEGNLRYKYNPSNDTYDVYDDTDSDSESDQNQDALTKPRKRDRIKRKIRNSANKTAHHRPIHRTRDRKFNEDKPWKSHTDITFVTDNERKRYESMWVSNRHRHLNLLSWWPSITGDSGAINTLPEDGLILGIIVRDIWKRSNLPNSLLAEIYTKVDTRKDGTLDRKSFIVGMWLVDQCLYGRKLPNVVEQCVWDSVDRYASTTVVPVSTLKAMAKQKRKQMKEEIKNIKKENRVVLVDHNSSS", "text": "FUNCTION: With TAX4, acts as a positive regulator of INP51 activity and phosphatidylinositol 4,5-bisphosphate turnover. Negatively regulates signaling through the cell integrity pathway, including the MAP kinase SLT2. Seems also to be involved in rDNA silencing. SIMILARITY: Belongs to the IRS4 family."}
+{"protein": "MASGAARWLVLAPVRSGALRSGPSLRKDGDVSAAWSGSGRSLVPSRSVIVTRSGAILPKPVKMSFGLLRVFSIVIPFLYVGTLISKNFAALLEEHDIFVPEDDDDDD", "text": "FUNCTION: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria (PubMed:24231807, PubMed:26774479, PubMed:27099988). Required to bridge the calcium-sensing proteins MICU1 and MICU2 with the calcium-conducting subunit MCU (PubMed:24231807). Plays a central role in regulating the uniplex complex response to intracellular calcium signaling (PubMed:27099988). 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 (PubMed:27099988). 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) (PubMed:27642048). SIMILARITY: Belongs to the SMDT1/EMRE family."}
+{"protein": "MGIHSLLYCERLFYLEEVEGILVADDRVYAGRTLHEELEPNEDSSGRIESFHYTSEKLEVSGKVDRIQKRDGDWIPYEHKRGRARIGTNGPEAWESDQCQVTVYALLLEEATGRNISEGKIRYHGSKDLVKIEIDEELRSKALKTIDRAKGLSTSTNRPPVAQNENLCKNCSLAPVCLPEETRVITENEYEPIRLFPEKREKTTLHVFGHDSRIKKSDNVLLVEKVTETGEKSKSEKIPIQEIESVNIHGNCQISSQMIKFLVSEEIPVHWFSGGGNYIGGININPSGVQRRIRQFKALTKETIRLNLAKKLVSAKCESQLRYLLRATRGKDETRNETESYLATIRSGLKNIESADSPSQLLGIEGSSARAYFSGLPALLKNSDPFLVPNGRSKRPPKDPFNATLSFLYSLLYKSVRQAIIAVGLDPSFGFYHTPRSSAEPLVLDLMELFRVSLCDMTLIGSINRKSWIDEDFEITKNKVWLSESGRKKATQLYETRLDDTWKHPVVNYSLSYYRMIELEVRLLEKEWSGEANIFAQARLR", "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": "CYINNCPLG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the vasopressin/oxytocin family."}
+{"protein": "GCCSHPACNVNNPHICG", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=11 nM), alpha- 7/CHRNA7 (IC(50)=27.1-59 nM (rat)/ 290 nM (human)), alpha-3-beta- 4/CHRNA3-CHRNB4 (IC(50)=160 nM), and alpha-6/alpha-3-beta-2-beta-3 (CHRNA6/CHRNA3-CHRNB2-CHRNB3) (IC(50)=201 nM) nAChR (PubMed:16803900, PubMed:30025921, PubMed:34955864). In the OmIA-AChBP complex, this toxin occupies all five binding pockets located between two adjacent subunits of the homopentamer (PubMed:34955864). Despite a competitive binding mode observed in the co-crystal structure, it displays functional insurmountable antagonism at alpha-7 and alpha-3-beta-4 nAChRs (PubMed:34955864). It also shows biphasic-inhibition at alpha-7 nAChRs in the presence of the positive allosteric modulator PNU120596, with a preference for the high-affinity binding site following prolonged exposure (PubMed:34955864). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
+{"protein": "MHCPICHHRAHVVYCAHCINTSPSLLLKLKLDLILLKDENKELNGKVEQILNEAMNYDQLDIKRMEKKKDPLMNSLMKLDVLRMKKNNNLIRHRIEQLNERIYSKRNHISELKVEIDNYKCYKVGTGTDKLIEQVEISDAKNKLAQVSKICESVRDYKLNLLNNWFVIQKLQDNFQIPFAIAFQPLISLKNFRVLPLAITNDSINIMWKYISFFSDILMIKLPYTNKICEQPMFEFSDSIQTVVQRLIKLIINILQICRHLKLVPSTPMDIPWLLDQYDVDGLFYNMVKRNKMKCRSVSLYWTFGMLYSMVLDNMNNPQRGHPARRTAPPPTVTGPHDRWYVVG", "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 pre-autophagosomal structure. ATG14 mediates the specific binding of the VPS34 PI3-kinase complex I to the preautophagosomal structure (PAS) (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Note=TRS85 is required for the recruitment of ATG14 to the PAS. SIMILARITY: Belongs to the ATG14 family."}
+{"protein": "MEVLSTSSPLTLHSHRLLSASSSSSHVTSIAASSLSSFASSYLGISLSNRTIHRFSTTPTNLRRFPQRKRKKFTPISAVFERFTERAIRAIIFSQKEAKSLGKDMVYTQHLLLGLIAEDRDPQGFLGSGITIDKAREAVWSIWDEANSDSKQEEASSTSYSKSTDMPFSISTKRVFEAAVEYSRTMDCQYIAPEHIAVGLFTVDDGSAGRVLKRLGANMNLLTAAALTRLKGEIAKDGREPSSSSKGSFESPPSGRIAGSGPGGKKAKNVLEQFCVDLTARASEGLIDPVIGREKEVQRVIQILCRRTKNNPILLGEAGVGKTAIAEGLAISIAEASAPGFLLTKRIMSLDIGLLMAGAKERGELEARVTALISEVKKSGKVILFIDEVHTLIGSGTVGRGNKGSGLDIANLLKPSLGRGELQCIASTTLDEFRSQFEKDKALARRFQPVLINEPSEEDAVKILLGLREKYEAHHNCKYTMEAIDAAVYLSSRYIADRFLPDKAIDLIDEAGSRARIEAFRKKKEDAICILSKPPNDYWQEIKTVQAMHEVVLSSRQKQDDGDAISDESGELVEESSLPPAAGDDEPILVGPDDIAAVASVWSGIPVQQITADERMLLMSLEDQLRGRVVGQDEAVAAISRAVKRSRVGLKDPDRPIAAMLFCGPTGVGKTELTKALAANYFGSEESMLRLDMSEYMERHTVSKLIGSPPGYVGFEEGGMLTEAIRRRPFTVVLFDEIEKAHPDIFNILLQLFEDGHLTDSQGRRVSFKNALIIMTSNVGSLAIAKGRHGSIGFILDDDEEAASYTGMKALVVEELKNYFRPELLNRIDEIVIFRQLEKAQMMEILNLMLQDLKSRLVALGVGLEVSEPVKELICKQGYDPAYGARPLRRTVTEIVEDPLSEAFLAGSFKPGDTAFVVLDDTGNPSVRTKPDSSTIRVTDKTSIA", "text": "FUNCTION: Molecular chaperone that interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast (PubMed:21737456). The ATPase activity of CLPD is stimulated by CLPT1 (PubMed:25149061). Has no ADPase activity (PubMed:21737456). Interacts with transit peptides with a positional preference (PubMed:21737456, PubMed:22545953). Localization of the signal sequence at the N-terminal end of a protein seems mandatory for interaction to take place (PubMed:22545953). SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the ClpA/ClpB family. ClpD subfamily."}
+{"protein": "FLGGLMKIGAKLLPSVIGLFKKKQ", "text": "FUNCTION: Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Medium-length antimicrobial peptide (group 3) family. Ponericin-W subfamily."}
+{"protein": "MQVRTPFVALDQRSPLTVDSSCPKRKKCDMDRERERDVKALEPRDLSSTGRIYARSDIKISSSPTVSPTISNSSSPTPTPPASSSVTPLGLPGAVAAAAAAVGGASSAGASSYLHGNHKPITGIPCVAAASRYTAPVHIDVGGTIYTSSLETLTKYPESKLAKLFNGQIPIVLDSLKQHYFIDRDGGMFRHILNFMRNSRLLIAEDFPDLELLLEEARYYEVEPMIKQLESMRKDRVRNGNYLVAPPTPPARHIKTSPRTSASPECNYEVVALHISPDLGERIMLSAERALLDELFPEASQATQSSRSGVSWNQGDWGQIIRFPLNGYCKLNSVQVLTRLLNAGFTIEASVGGQQFSEYLLARRVPM", "text": "FUNCTION: Functions with the transcription factor TfAP-2 to regulate octopamine neuronal signaling pathways that control behaviors such as male aggression, male mating, and the initiation of feeding (PubMed:30231996, PubMed:24142897, PubMed:25187989). Required for TfAP- 2 transcriptional activity in octopaminergic neurons (PubMed:24142897, PubMed:25187989). Functions with TfAP-2 to regulate expression of genes which are involved in promoting octopamine production and secretion from octopaminergic neurons, such as Tbh and Vmat (PubMed:24142897, PubMed:25187989). Octopamine then modulates feeding and male aggression by regulating the expression of the satiation hormone Dsk in insulin- producing cells (IPCs) (PubMed:24142897, PubMed:25187989). Functions with octopamine and Dsk as part of a negative feedback loop to prevent overeating; acts with TfAP-2 to regulate octopamine signaling pathways that initiate feeding, then octopamine activates expression of Dsk which inhibits consummatory behavior (PubMed:25187989). May also be involved in negatively regulating nociception in larvae to prevent spontaneous pain and hyperalgesia (PubMed:30231996)."}
+{"protein": "MSSSSDKTDPCKPEACAIQDCLQQNNYNESKCSKIIDNLYLCCKKYYEKNGSDKQTTCCPKFNLLQLKLKQRELGKIDAEMVDSRKG", "text": "SUBCELLULAR LOCATION: Mitochondrion intermembrane space Note=Imported into the mitochondria via the mitochondrial disulfide relay system. SIMILARITY: Belongs to the CMC4 family."}
+{"protein": "MAENHCELLPPAPSGLGAGLGGGLCRRCSAGMGALAQRPGGVSKWVRLNVGGTYFLTTRQTLCRDPKSFLYRLCQADPDLDSDKDETGAYLIDRDPTYFGPVLNYLRHGKLVINKDLAEEGVLEEAEFYNITSLIKLVKDKIRERDSRISQMPVKHVYRVLQCQEEELTQMVSTMSDGWKFEQLVSIGSSYNYGNEDQAEFLCVVSKELHNTPYGTTSEPSEKAKILQERGSRM", "text": "FUNCTION: Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex (By similarity). Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Nucleus Note=Predominantly cytoplasmic, translocated to the nucleus upon interaction with Rep proteins."}
+{"protein": "MLAFCYSLPNAGDVIKGRVYEKDYALYIYLFDYPHFEAILAESVKMHMDRYVEYRDKLVGKTVKVKVIRVDYTKGYIDVNYKRMCRHQ", "text": "FUNCTION: Viral mimic of EIF2S1/eIF-2alpha that acts as a pseudosubstrate for EIF2AK2/PKR kinase (PubMed:8099586, PubMed:9199350). Inhibits therefore EIF2S1/eIF-2alpha phosphorylation by host EIF2AK2/PKR kinase and prevents protein synthesis shutoff (PubMed:8099586, PubMed:9199350). Determinant of host species specificity (PubMed:32056708). SIMILARITY: Belongs to the poxviridae K3 protein family."}
+{"protein": "MFKVVICDDERIIREGLKQIIPWGDYHFNTIYTAKDGVEALSLIQQHQPELVITDIRMPRKNGVDLLNDIAHLDCNVIILSSYDDFEYMKAGIQHHVLDYLLKPVDHAQLEVILGRLVRTLLEQQSQNGRSLAPCHDAFQPLLKVEYDDYYVNQIVDQIKQSYQTKVTVSDLIQHIDVSESYAMRTFKDHVGITIVDYLNRYRILQSLQLLDRHYKHYEIADKVGFSEYKMFSYHFKKYLQMSPSDYCKQAK", "text": "FUNCTION: Member of the two-component regulatory system HptS/HptR that regulates genes involved in hexose phosphate transport system in response to changes in extracellular phosphate sources. Activates uhpT expression to facilitate glucose-6-phosphate/G6P utilization by directly binding to its promoter. Antagonizes CcpA-dependent transcription of a subset of CcpA-regulated genes involved in antibiotic susceptibility. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MQTDNTKSNTNKTAKQEWWSCAFVICIALLIRILIMEPFTVPTGSMKATILENDYIFSTKYSYGYSNYSLSFFDFIPLFKGRIFAREPERGDIVVFRPPNDMNVRYIKRLIGLPGDKIQLIDDVIYINDKKIERTEVGTYTSEDGIKYLKFKETLPNGRTYFSYKLAPIFSVIYNDRYGNTDVFYVPEGKYFFLGDNRDQSNDSRVNLGFVPFENFIAKAQFIWFSTKINWWDNDIGVMNLVLRLKPWIESVRLNRIFRNLYNTDE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S26 family."}
+{"protein": "MSTVESALTRRIMGIETEYGLTFVDGDSKKLRPDEIARRMFRPIVEKYSSSNIFIPNGSRLYLDVGSHPEYATAECDNLTQLINFEKAGDVIADRMAVDAEESLAKEDIAGQVYLFKNNVDSVGNSYGCHENYLVGRSMPLKALGKRLMPFLITRQLICGAGRIHHPNPLDKGESFPLGYCISQRSDHVWEGVSSATTRSRPIINTRDEPHADSHSYRRLHVIVGDANMAEPSIALKVGSTLLVLEMIEADFGLPSLELANDIASIREISRDATGSTLLSLKDGTTMTALQIQQVVFEHASKWLEQRPEPEFSGTSNTEMARVLDLWGRMLKAIESGDFSEVDTEIDWVIKKKLIDRFIQRGNLGLDDPKLAQVDLTYHDIRPGRGLFSVLQSRGMIKRWTTDEAILAAVDTAPDTTRAHLRGRILKAADTLGVPVTVDWMRHKVNRPEPQSVELGDPFSAVNSEVDQLIEYMTVHAESYRS", "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. 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": "MKKLGTLLVLFLSVIALVACASGKKDATSGQKLKVVATNSIIADITKNIAGDKIDLHSIVPVGQDPHEYEPLPEDVKKTSEADLIFYNGINLETGGNAWFTKLVENAKKTENKDYFAVSEGVDVIYLEGQNEKGKEDPHAWLNLENGMIYAKNIAKQLIAKDPSNKEFYEKNLKDYTEKLDKLDKEAKEKFNNIPAEKKLIVTSEGCFKYFSKAYGVPSAYIWEINTEEEGTPEQIKTLVEKLRQTKVPSLFVESSVDDRPMKTVSQDTNIPIYAQIFTDSIAEEGKEGDSYYSMMKYNLDKIAEGLSK", "text": "FUNCTION: Part of an ATP-driven transport system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 9 family. Lipoprotein receptor antigen (Lrai) subfamily."}
+{"protein": "MGLPKSFVSMSLLFFSTLLILSLAFNAKNLTQRTNDEVKAMYESWLIKYGKSYNSLGEWERRFEIFKETLRFIDEHNADTNRSYKVGLNQFADLTDEEFRSTYLGFTSGSNKTKVSNRYEPRVGQVLPSYVDWRSAGAVVDIKSQGECGGCWAFSAIATVEGINKIVTGVLISLSEQELIDCGRTQNTRGCNGGYITDGFQFIINNGGINTEENYPYTAQDGECNLDLQNEKYVTIDTYENVPYNNEWALQTAVTYQPVSVALDAAGDAFKHYSSGIFTGPCGTAIDHAVTIVGYGTEGGIDYWIVKNSWDTTWGEEGYMRILRNVGGAGTCGIATMPSYPVKYNNQNHPKPYSSLINPPAFSMSKDGPVGVDDGQRYSA", "text": "FUNCTION: Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH. SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MSTAGDDAVGVPPACGGRSDAVGVPQLARESGAMRDQDCSGELLRSPTHNGHLLVGALKRHQNKPVLFLGDTRLTGGQLADRISQYIQAFEALGAGTGVAVGLLSLNRPEVLMIIGAGQARGYRRTALHPLGSLADHAYVLNDAGISSLIIDPNPMFVERALALLEQVDSLQQILTIGPVPDALKHVAVDLSAEAAKYQPQPLVAADLPPDQVIGLTYTGGTTGKPKGVIGTAQSIATMTSIQLAEWEWPANPRFLMCTPLSHAGAAFFTPTVIKGGEMIVLAKFDPAEVLRIIEEQRITATMLVPSMLYALLDHPDSHTRDLSSLETVYYGASAINPVRLAEAIRRFGPIFAQYYGQSEAPMVITYLAKGDHDEKRLTSCGRPTLFARVALLDEHGKPVKQGEVGEICVSGPLLAGGYWNLPDETSRTFKDGWLHTGDLAREDSDGFYYIVDRVKDMIVTGGFNVFPREVEDVVAEHPAVAQVCVVGAPDEKWGEAVTAVVVLRSNAARDEPAIEAMTAEIQAAVKQRKGSVQAPKRVVVVDSLPLTGLGKPDKKAVRARFWEGAGRAVG", "text": "FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MIVVKIGGRVVKNSLDKVILDIANINDKVILVHGGGDIVTDYTKRLGIEPVFVTSPEGIRSRYTTKEELEVYIMAMSLINKMITSKLCSLGKNAIGITGADGGLLLAERKKRIIVIDERGKKRIIEGGYTGKVKEVRSEVINHLMKLFDIIVVSPLALDVEESTPLNIDGDQAAFAISKAVKVNVLVILSDVEGVLVEGKVVDRLTPEEAKELSKKIGPGMNRKLLMAAESVENGVNKVIIGSGVKDRPVSSALELNGTVIVNG", "text": "FUNCTION: Involved in both the arginine and lysine biosynthetic pathways. Phosphorylates the LysW-bound precursors glutamate (for arginine biosynthesis), respectively alpha-aminoadipate (for lysine biosynthesis). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetylglutamate kinase family. LysZ subfamily."}
+{"protein": "MSFLRRHISLFRSQKQLIDVFAPVSPNLELAEIHRRVIEDQGPALLFHNVIGSSFPVLTNLFGTKHRVDQLFSQAPDNLIARVAHLISSTPKLSSLWKSRDLLKRISSLGLKKARFRRFPFVSMSSVNLDHLPLLTSWPEDGGAFLTLPLVYTESPTLTTPNLGMYRVQRFNQNTMGLHFQIQKGGGMHLYEAEQKKQNLPVSVFLSGNPFLTLSAIAPLPENVSELLFATFLQGAKLLYKKTNDHPHPLLYDAEFILVGESPAGKRRPEGPFGDHFGYYSLQHDFPEFHCHKIYHRKDAIYPATVVGKPYQEDFYIGNKLQEYLSPLFPLVMPGVRRLKSYGESGFHALTAAVVKERYWRESLTTALRILGEGQLSLTKFLMVTDQEVPLDRFSVVLETILERLQPDRDLIIFSETANDTLDYTGPSLNKGSKGIFMGIGKAIRDLPHGYQGGKIHGVQDIAPFCRGCLVLETSLEDRCIKSLLHHPDLKSWPLIILADNLRETIQSEKDFLWRTFTRCAPANDLHALHSHFATHRPNYNFPFVIDALMKPSYPKEVEVDPSTKQKVSERWHAYFPNKETFYI", "text": "FUNCTION: Catalyzes the reversible decarboxylation of 4- hydroxybenzoate. SIMILARITY: Belongs to the UbiD family."}
+{"protein": "MRSSLVLFFVSAWTALASPIRREVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSFRGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLRGNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEGIDATGGNNQPNIPDIPAHLWYFGLIGTCL", "text": "SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
+{"protein": "MKVQGSVDRRRLQRRIAGLLPPPARRLNISRGSEFTRDVRGLVEEHAQASSLSAAAVWRAGLLAPGEVAVAGGGSGGGSFSWSGWRPPVFGDFLIHASSFNNAEATGTPLFQFKQSDPFSGVDAVFTPLSLFILMNHGRGVAARVEAGGGLTRMANLLYDSPATLADLVPDFGRLVADRRFHNFITPVGPLVENIKSTYLNKITTVVHGPVVSKAIPRSTVKVTVPQEAFVDLDAWLSGGAGGGGGVCFVGGLGLQPCPADARLYVALTYEEAGPRFTFFQSSRGHCQIMNILRIYYSPSIMHRYAVVQPLHIEELTFGAVACLGTFSATDGWRRSAFNYRGSSLPVVEIDSFYSNVSDWEVIL", "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 TRX1 protein family."}
+{"protein": "MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDANNGKLYSAGRDAIIRVWNTRTDSSEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAQKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRIMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCVQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKTLVCEEQAPVLSLGYNIDKTGVWATTWNSDIRCWKLPMYDRCTLNSSGGMDAQWTQGGTEVACIKGGAAIKECAVLNDKRYIITKDSQDQVVVYDVLRVVKKEQLGAVDYEAEVKKRNKQVYIPNWFTVDLKTGMPTIVLGQEEVDCFSAWVSIEAGLPECVDPTTEIKINYGKLLLEALLEYWTPPHSIPPNEMEPDMHGNGYFQVPKHTPVIFSEVGGRTVCRLLVRDAAGDSESTLLHETAPQWVTDVVIEKNIPKFLKIPFFLQPHPQMTKPERTKKDRLVANEFIQCRKVCEHVLEKVLNAETTPSGGNANNSLQNSQSDANSEGSQLPAEERIELWCNDVVVDPNMDLRTVRHFIWKQSTDLTFQYKTKQNFNYDGSIGDSLERVTRKY", "text": "FUNCTION: Regulator of deubiquitinating complexes. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (By similarity). SIMILARITY: Belongs to the WD repeat WDR48 family."}
+{"protein": "MALIVEFICELPNGVHARPASHVETLCNTFSSQIEWHNLRTDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWLRDEFPHCDAPLAEVKSDELEPLPVSLTNLNPQIIRARTVCSGSAGGILTPISSLDLNALGNLPAAKGVDAEQSALENGLTLVLKNIEFRLLDSDGATSAILEAHRSLAGDTSLREHLLAGVSAGLSCAEAIVASANHFCEEFSRSSSSYLQERALDVRDVCFQLLQQIYGEQRFPAPGKLTQPAICMADELTPSQFLELDKNHLKGLLLKSGGTTSHTVILARSFNIPTLVGVDIDALTPWQQQTIYIDGNAGAIVVEPGEAVARYYQQEARVQDALREQQRVWLTQQARTADGIRIEIAANIAHSVEAQAAFGNGAEGVGLFRTEMLYMDRTSAPGESELYNIFCQALESANGRSIIVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYEEYASLFTTQLRSILRASAHGSLKIMIPMISSMEEILWVKEKLAEAKQQLRNEHIPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQYLLAVDRDNAKVTRHYNSLNPAFLRALDYAVQAVHRQGKWIGLCGELGAKGSVLPLLVGLGLDELSMSAPSIPAAKARMAQLDSRECRKLLNQAMACRTSLEVEHLLAQFRMTQQDAPLVTAECITLESDWRSKEEVLKGMTDNLLLAGRCRYPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQAPVRWGDDEAQFIIMLTLNKHAAGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQHELEL", "text": "FUNCTION: Multifunctional protein that includes general (non sugar- specific) and sugar-specific components 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 enzyme II FrwABC PTS system is involved in fructose transport. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PEP-utilizing enzyme family."}
+{"protein": "MAQMAKKVHWSSAAAGAAAAAKISKLEKTTKRFKLIKKRNPSSKLPKRSSHSLLCSLSRSCCCCRCRCCCYCRCCRCCCSRSRRFRSRTTLKFFQITEKGEQSLQRRIRRQLTRSQLELIEPEPTMALEPSEITVAFFSHKNANVSDPEEVPPCLDSDPFPNGDLASS", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, perinuclear theca Note=Found in the postacrosomal region of the perinuclear theca."}
+{"protein": "MPAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC", "text": "FUNCTION: Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway. SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family."}
+{"protein": "MNRFTVRSKFIKFSFQLFRNYSVCLNSSKSLIRVEGVDAVKFLQGLTTNKITLDNPVYTGFLNTQGRVLFDSFIYPKVSNNGTENERSDELYVEIDKVAESDFLKHLKKYNLRSRCSIAKIPSEELSIKVIWDVKEESRLKDTVAYAKDPRFSKQRLLRMIVPTSTCTSSSSGSLDDYKVFRYRNGIPEGPQEIIPSISFPLESNMDWMKGIDFHKGCYLGQELTVRTYYTGVTRKRIFPFIIPNYEDNPSQVIEPSAPLSIVAKQGEPVSRRSPGKIIAILGKVGLALVRLQYLKSDLACNGIPIQLNTSIWLDELSSTPSENS", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvT family. CAF17 subfamily."}
+{"protein": "MTDSPFLELWQSRAVSVREQLGLGDRPNDSYCYNSAKNSTVLQGVTFGGIPTVLLIDVSCFLFLILVFSIIRRRFWDYGRIALVSEADSEPRFQRLSSTSSSGQQDFENELGCCPWLTAIFRLHDDQILEWCGEDAIHYLSFQRHIIFLLVVVSFLSLCVILPVNLSGDLLDKDPYSFGRTTIANLQTDNDLLWLHTIFAVIYLFLTVGFMRHHTQSIKYKEENLVRRTLFITGLPRDARKETVESHFRDAYPTCEVVDVQLCYNVAKLIYLCKERKKTEKSLTYYTNLQVKTGQRTLINPKPCGQFCCCEVQGCEWEDAISYYTRMKDRLLERITEEERHVQDQPLGMAFVTFQEKSMATYILKDFNACKCQSLQCKGEPQPSSHSRELYTSKWTVTFAADPEDICWKNLSIQGLRWWLQWLGINFTLFLGLFFLTTPSIILSTMDKFNVTKPIHALNNPIISQFFPTLLLWSFSALLPSIVYYSTLLESHWTKSGENQIMMTKVYIFLIFMVLILPSLGLTSLDFFFRWLFDKTSSEASIRLECVFLPDQGAFFVNYVIASAFIGNGMELLRLPGLILYTFRMIMAKTAADRRNVKQNQAFQYEFGAMYAWMLCVFTVIMAYSITCPIIAPFGLIYILLKHMVDRHNLYFIYLPAKLEKGIHFAAVNQALAAPILCLFWLYFFSFLRLGMKAPATLFTFLVVLLTILVCLAHTCFGYFKHLSPLNYKTEEPASDKGSEAEAHMPPPFTPYVPRILNGLASERTALSPQQQQQQTYGAIHNISGTIPGQCLAQSATGSVAAAPQEA", "text": "FUNCTION: Acts as an osmosensitive calcium-permeable cation channel (By similarity). Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family."}
+{"protein": "MIMPKKERKVEGEEVIRVPLPEGNQLFGVVEQALGAGWMDVRCEDGKIRRCRIPGKLRRRVWIRVGDLVIVQPWPVQSDKRGDIVYRYTQTQVDWLLRKGKITQEFLTGGSLLVE", "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 (By similarity). SIMILARITY: Belongs to the eIF-1A family."}
+{"protein": "MSIAVGLSACALSSVLFGSMFVPVKKCHSGNGIFVQWIMSTAILLVGIVVYSTQGFPEFEPLAMLGGMFWALGNATAVPIMNTIGIGMGMLVWGTTNCVAGWAAGRFGLFGINSTVPEYPFLNYFGLVLVVFGGFLFSQIRPNEPQTASERSPLMVAPDDDLTDDVAPDDSDIVVPRGGAVPTRAHRNQKRLLAIITSLVAGVFYGFTFVPVIYIQDHPEIYPTAPKTGLGYVFSHYIGIFCTASALMIGYVIYSRNNPFASSRLVGPSMTAGSMWGIAQASWFVANDNLSQAVSFPIISMVPGVIAALWSVFYFRDISGSRNLRLLSIAVAITLIGAICVGVSK", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM144 family."}
+{"protein": "MRSFLYLIVVIFLFSSSVNACDRCLHRSKASYFSSASALSSGACAYGPMATSFFAGHIAAAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLVLSSRAFRAMAKPVVGVDKYLLKQGIVDVEYQRVPCNYGKRNLNVRVEEASKKPNYLAIKLLYQGGQTEVVGIDIAPVGSSQWSYMSRSHGAVWATDKVPTGALQFKFTVTGGYDGKTVWSKRVLPANWNSGRIYDAGVQITDIAQEGCDTCGHIWN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the expansin family. Expansin-like A subfamily."}
+{"protein": "AEKIKICLQKQVNSSFSLHNGFGGNLYATEEKRMFELVKPKAGASVLNQSTWICFGDSRTDQSNSAFPRSADVSAKTAEKFRSLSGGSLMLSMFGPPGKVDYLYQGCGKHKVFYEGVNWSPHTAIDCYRKNWTDIKLNFQKSIYELASQSHCMSLVNALDKTIPLQATKGVAKNCNNSFLKNPALYTQEVKPLEQICGEENLAFFTLPTQFGTYECKLHLVASCYFIYDSKEVYNKRGCGNYFQVIYDSSGKVVGGLDNRVSPYTGNSGDTPTMQCDMLQLKPGRYSVRSSPRFLLMPERSYCFDMKEKGLVTAVQSIWGKGRKSDYAVDQACLSTPGCMLIQKQKPYIGEADDHHGDQEMRELLSGLDYEARCISQSGWVNETSPFTEEYLLPPKFGRCPLAAKEESIPKIPDGLLIPTSGTDTTVTKPKSRIFGIDDLIIGLLFVAIVEAGIGGYLLGSRKESGGGVTKESAEKGFEKIGNDIQILRSSTNIAIEKLNDRISHDEQAIRDLTLEIENARSEALLGELGIIRALLVGNISIGLQESLWELASEITNRAGDLAVEVSPGCWIIDNNICDQSCQNFIFKFNETAPVPTIPPLDTKIDLQSDPFYWGSSLGLAITTPISLAALVISGIAICRTK", "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": "MNYANFGLDFLNSVANAAVEGKKLDLASRGLQLRSRALDTERDFNYAKLAFERHKFDTNNDLRIYGDAMRIQALRAAGLRINPYSNGRQIYQDEADLANLHSYYSFYKTD", "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": "MNPSQQHLPKLCPKRLFLFFTPFLLFSLYYILTTIKTITISSQDRHHPPQLHVPSISHYYSLPETSENRSSPPPLLLPPPPSSSSSLSSYFPLCPKNFTNYLPCHDPSTARQYSIERHYRRERHCPDIAQEKFRCLVPKPTGYKTPFPWPESRKYAWFRNVPFKRLAELKKTQNWVRLEGDRFVFPGGGTSFPGGVKDYVDVILSVLPLASGSIRTVLDIGCGVASFGAFLLNYKILTMSIAPRDIHEAQVQFALERGLPAMLGVLSTYKLPYPSRSFDMVHCSRCLVNWTSYDGLYLMEVDRVLRPEGYWVLSGPPVASRVKFKNQKRDSKELQNQMEKLNDVFRRLCWEKIAESYPVVIWRKPSNHLQCRKRLKALKFPGLCSSSDPDAAWYKEMEPCITPLPDVNDTNKTVLKNWPERLNHVPRMKTGSIQGTTIAGFKADTNLWQRRVLYYDTKFKFLSNGKYRNVIDMNAGLGGFAAALIKYPMWVMNVVPFDLKPNTLGVVYDRGLIGTYMNWCEALSTYPRTYDLIHANGVFSLYLDKCDIVDILLEMQRILRPEGAVIIRDRFDVLVKVKAITNQMRWNGTMYPEDNSVFDHGTILIVDNSIK", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISALNIVGDLLRKVGALESKLASCRNLVYDQSPNRTGGPASGRSSKNRDGGERRPSSTSVPLGDKGLDTSCRWLSKSTTRSSSSC", "text": "FUNCTION: Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Note=Localizes to the interphase and S phase centrosome. During mitosis, partially associated with the mitotic spindle. Concentrates at the plus ends of microtubules coincident with kinetochores in metaphase and anaphase in a CENPF-dependent manner. Also localizes to the cleavage furrow during cytokinesis. manner. Also localizes to the cleavage furrow during cytokinesis. SIMILARITY: Belongs to the nudE family."}
+{"protein": "MSFLNNDFGSPPATSSPPTTMPKLPTIQDMLNNIGASTVNLMQPNPYLMQNQIPLPVPNLPLNPFLHLNPAISQEIIQQFIAMSFNTPNVLASIANMGDDEGPSCNPKMRRGDLLKSVSMDSTEDPPSITLDNNGDMIVPNNDKEGWCRNKKYIEQTENGYMCTVCRKVYGRYNSVSYHVTIYHRNPPIKCNVPNCQFTTREARYIHFHKNYRHGIPLPESIDQGSRKCPHCRHVSKSPAMLEKHIRRHQIKDGLSNINEAIRERTSTICDEAMEIEPAETEVDPIETKPRSCTL", "text": "FUNCTION: Zinc finger transcription factor which acts as both a transcriptional activator and repressor (PubMed:23911329, PubMed:30956009). Binds to the promoters of genes that contain the 5'- CTTATCA-3' DNA consensus sequence in their regulatory region (PubMed:23911329, PubMed:31532389). Functions downstream of the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:23911329, PubMed:27401555). Involved in normal development, lifespan, stress response, lipid metabolism, innate immunity and exit from the developmentally arrested larval state known as dauer (PubMed:23911329, PubMed:27401555, PubMed:29949773, PubMed:31532389, PubMed:33009389). Required for stress-induced expression of hsp-90 and resistance to heat stress, perhaps as part of a systemic stress signaling pathway (PubMed:29949773). Involved in maintenance of proteostasis (PubMed:29949773). Under hypoxic stress increases lipid levels by positively regulating fatty acid synthesis via fat-7 expression (PubMed:33009389). Associates with homeobox protein ceh-60 at the promoters of some stress-responsive genes to regulate expression; may require phosphorylation for transcriptional repression activity (PubMed:30956009). Acts downstream of nhr-14 to activate transcription of intestinal metal transporter smf-3, modulating innate immunity and iron uptake (PubMed:31532389). May act downstream of the mTORC2 signaling mediated pathway (PubMed:27401555). May act in a mutually exclusive manner with the FOXO transcription factor daf-16 (PubMed:23911329, PubMed:27401555). SUBCELLULAR LOCATION: Chromosome Nucleus Cytoplasm Note=Nuclear localization under normal conditions, cytoplasmic as a result of heat-stress (PubMed:23911329). Nuclear localization declines over normal lifespan (PubMed:23911329). Exposure to Gram-negative bacterium P.aeruginosa enhances nuclear localization (PubMed:31532389). Hypoxic stress enhances nuclear localization (PubMed:33009389). SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MASADEKVVEEKASVISSLLDKAKGFFAEKLANIPTPEATVDDVDFKGVTRDGVDYHAKVSVKNPYSQSIPICQISYILKSATRTIASGTIPDPGSLVGSGTTVLDVPVKVAYSIAVSLMKDMCTDWDIDYQLDIGLTFDIPVVGDITIPVSTQGEIKLPSLRDFF", "text": "SIMILARITY: Belongs to the LEA type 2 family."}
+{"protein": "MPKERRSRRRPEPIIRWVSLTLTLLALCQPIQTWRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPFCAKSPRYTLDSVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADRFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISSSGPGLALPDAQIFWVNTSSFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTASSAPPTRVRRSPVAALTLGLALSVGLTGIKVAVSALSHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQSLCPTINEPCCFLRIQNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALLLLFLAPCLIKCLTSRLSKLLRQAPHFPEISFPPKPDSDYQALLPSAPEIYSHLSPTKPDYINLRPCP", "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": "MVVHALIYIFFNYDKPGLIKGWAVPIATDTAFVLGIVSFFSRHISLELRTFIIGFSLIDDAFAPIILS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family."}
+{"protein": "MRTLWIMAVLLLGVKGNLLQFELMIKKMSGRSGIRWYSDYGCYCGKGGHGQPQDATDRCCFVHDCCYGKVSGCDPKMAFYKYSSDNNDIVCGGNNPCLKEICECDRAAAICFRDNLSTYDNKYWNVPSETCQVESEPC", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that impairs hemostasis. It weakly inhibits ADP-induced platelet aggregation when tested on platelet rich plasma from human and rabbit blood (15-25% of inhibition at 5-10 ug of enzyme), and dose-dependently inhibits blood coagulation, possibly by inhibiting thrombin activation. Exhibits high hydrolytic activities toward L-dipalmitoyl phosphatidylcholine. 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": "MNEAVSPGALSTLFTDARTHNGWRETPVSDETLREIYALMKWGPTSANCSPARIVFTRTAEGKERLRPALSSGNLQKTLTAPVTAIVAWDSEFYERLPLLFPHGDARSWFTSSPQLAEETAFRNSSMQAAYLIVACRALGLDTGPMSGFDRQHVDDAFFTGSTLKSNLLINIGYGDSSKLYARLPRLSFEEACGLL", "text": "FUNCTION: May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. FUNCTION: May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation. SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily. SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily."}
+{"protein": "MATFKDACYHYKRINKLNHTVLKLGVNDTWRPSPPTKYKGWCLDCCQHTDLTYCRGCTMYHVCQWCSQYGRCFLDNEPHLLRMRTFKNEVTKDDLKNLIDMYETLFPMNQRIVCRFINNTRQHKCRNECMTQWYNHLLLPITLQSMSIELDGDVYYVFGYYDNMNSINQTPFSFTNLVDIYDKLLLDDVNFTRMSFLPASLQQEYALRYFSKSRFISEQRKCVNDSHFSINVIENLHNPSFKVQITRNCSELSFDWNKACKLVKKISAYFDILKTSHIEFYSVSTRCRIFTQCKLKMASKLIKPNYITSNHKTLATEVHNCKWCSVNNSYTVWNDFRIKNIYDNIFNFLRALVKSNVNIGHCSSQEKIYEYVEDVLNVCDDERWKTSIMEIFNCLEPVELDDVKYVLLNHEINWDVINVLVHSIGKVPQILTLENVIAIMQSIIYEWFDIRYMRNTPMVTFTIDKLRRLHTGLKTVDYDSGISDIE", "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": "MERGRDRLHLRRTTEQHVPEVEVQVKRRRTASLSNQECHLYPRRSQQQQVPVVDFQAELRQAFLAETPRGG", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNURF family."}
+{"protein": "MEASSEPPLDAKSDVTNQLVDFQWKLGMAVSSDTCRSLKYPYVAVMLKVADHSGQVKTKCFEMTIPQFQNFYRQFKEIAAVIETV", "text": "FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Down-regulates activation of NF- kappa-B. Inhibits TNF-induced NFKB1 activation. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MKCLILSFAIFVVLASQATAGNVIIGGVCQDCSPPVAENVVVGGQSYRTGRPGQGTVYINSPGAYLGALDGPIRRTGAGGGGGGGAQYPDGYSGRLPGGTYLHNKDCVGCSISGGGD", "text": "FUNCTION: Secreted immune-induced peptide induced by Toll signaling (PubMed:9736738). Has a role in resistance to bacterial and fungal infections (PubMed:25915418, PubMed:29920489). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bomanin family."}
+{"protein": "MNPLQSIQHNITTPPISGGQPLDAVGPQAQKSHPKRISPSQLSQSAHQALERLSANAEHQRLASLVRKALQDGTFQFQSSNHTQVTYKASICLPADTDTVRTDLLINNELTVKARLNDQSEYDIVSAHLHGSSKAISFDVPSPPPAHGSASSVLSERTHLVMSRVLSQDAVDSSRLETSLLSSPDHSRPPSQPKPVHLGSVRRESGSLVSDNPVVQALLSFAQADQAFPPQAASIAGVQLEMRPRRDIEKALEEFKGAFTVEKAQLMSGANSSERVDEDVNADIHIPLLLKAIERGAAAFGPNASIGQNSAKAFLASCAPKITSNDDVLSEFINQKLKGDDDLQVRLGAQELLHVATKKEFQLGGLAGSIGVSSILGSAWELGASELLKNAIFGKNFSPSQYALQLAGIDSVPPLIIESMDTMCVLAIIKGMKGEEWSMSDLLPKALKAGAISSVVSFPNNVLQYAGFKSRVGDLAANSVTTEAAIFGAASGIPPEVKESEELMRAGLFQSMKDGVMAHPGEGVDTKKTIERMTRHALDIAPGESTAVKSMGLASIVGMIPLIASNKATGLLSEQVLRIFRSAVFNPIEAIALNALALGGRVNVPGLFDSDNAKHARVVQTILARASQHMEAGDRDISAEELHQMLAPRSEFLRHVGSAIVNGMNASFEAIPALVRKLGYGEAPLAERIPYQDLAVPDTSRQPAP", "text": "FUNCTION: Effector protein involved in non-host recognition. SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion system (TTSS)."}
+{"protein": "DRDSCVDKSRCAKYGYYQECQDCCKKAGHNGGTCMFFKCKCA", "text": "FUNCTION: Blocks Kv11/ERG potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 1 subfamily."}
+{"protein": "MESVNKCGKSASTRNCTVKMSRKMWVLSLLALAALQLHSGSEVAAHLNVFLNPVEVMRLLGVSAEVYYVREGHINNYALNFIVPVPANVKDISFTWQSLAGRGLPYSINVVSSDQEVLPRPAINVSHSGEIPTTIQTWSIALKCSGLKAAEVDVTVSLEVVLNRSLNNVTHLVFRRKKICLMNDSAEDLSEDVDDPQLLETVMLPPTGLITLVVGVSVAMGSVCLLLMIAYCVKGAANKRQHHQHGGQPMRTSSFQRLNTHPPCQSSMGSAAYMTPSIIAPIHGSSLPRKVPVSVEQQHPEELHRRISELTVERCRVRLSSLLQEGTFGRVYRGTYNDTQDVLVKTVAQHASQMQVLLLLQEGMLLYGASHPGILSVLGVSIEDHTTPFVLYPALNNTRNLKQFLLDPACARTVTTIQIVMMASQLSMALDHLHSHGVVHKDIATRNCVIDDQLRVKLSDSSLSRDLFPSDYNCLGDSENRPVKWMSLEALQHKQFSEASDSWAFGVLMWELCTSAKQPYAEVDPFEMEHYLKDGYRLAQPFNCPDELFTIMAYCWALLPAERPTFAQLQSCLSEFYSQITRYV", "text": "FUNCTION: May play an essential role in neuronal pathway recognition and ventral muscle attachment site selection. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family."}
+{"protein": "MIIMNGPWVEKYRPQKLDDIVGQEHIIPRLKRYVEEKSMPNLMFTGPAGVGKTTAALALAREILGEYWRQNFLELNASDARGIDTVRTSIKNFCRLKPVGAPFRIIFLDEVDNMTKDAQHALRREMEMYTKTSSFILSCNYSSKIIDPIQSRCAIFRFLPLKGHQIIKRLEYIAEKENLEYEAHALETIVYFAEGDLRKAINLLQSAASLGEKITESSIYDVVSRARPKDVRKMIKTILDGKFMEARDMLREIMVLQGISGEDMVTQIYQELSRLAMEGEVDGDRYVGLIDAIGEYDFRIREGANPRIQLEALLARFLEHA", "text": "FUNCTION: Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. The complex possesses DNA-dependent ATPase activity which is further stimulated by PCNA. In conjunction with PCNA stimulates DNA synthesis by PolB, relieving inhibition by replication protein A (RPA). SIMILARITY: Belongs to the activator 1 small subunits family. RfcS subfamily."}
+{"protein": "MKLPIFIADAFTVTAFHGNPAAVCLLESILQEDAHQQIAREMNLSETAFIRKLQPTDSFSQSSCFGLRWFTPVSEVPLCGHATMASAAVLFHKIKNVNSTLTFVTLSGELKARRAEDGIVLDFPLYPTFPQDFHEVKDLIKAAIGDTTVQDIQYSPDTRKLLVRLSDSYDRSFLESLKVNTEPLPGIEKTGKVKGLILTVKGESGGQTTPYDFYSRYFAPWVGVPEDPVTGSAHTVLSSYWSQQLGKKEMRAFQCSCRGGELDISLRPDGRVDMKGGAAVVLEGMLTA", "text": "SIMILARITY: Belongs to the PhzF family."}
+{"protein": "MKLYCLSGHPTLPCNILKFKSSTIMLDCGLDMTSTLSFLPLPLVHSTRLSKLPGWVTKDGNNQFEKELKECSGRVFVDSVPEFCLPETELIDLSTVDVILISNYHCMMALPYITERTGFTGTVYATEPTVQIGRLLMEELVNFIERVPKAQSATVWKHKDVQRLLPAPLKDAVEVFTWKKCYSMQEVNAALSKIQLVGYSQKIELFGVVQVTPLSSGYALGSSNWVIQSHYEKVSYVSGSSLLTTHPQPMDQTSLKNSDVLILTGLTQIPTANPDGMVGEFCSNLAMTIRSGGNVLVPCYPSGVIYDLLECLYQYIDSAGLSNVPFYFISPVANSSLEFSQIFAEWLCHNKQNKVYLPEPPFPHAELIQSNKLKHYPNIHGDFSNDFKQPCVVFTGHPTLRFGDVVHFMELWGKSSLNTVIFTEPDFSYLDALAPYQPLAMKCVYCPIDTRLNFIQVTKLLKEVQPLHVVCPEQYTQPPATQSHRSDLMIDCQPPPMSYHRAEVLTLPFKRRYEKIEIMPELAQSLVPFEMKPGVSLATVSAVLHSKDNKHVLQPPPKPVAPPGSKKRKRPAEESPETPPFKPLLSGSIPVEQFVQTLEKNGFSDVKIEDTAKGHIVHLQEAETLIQFEEDSTHIICEHDERLRVRLRDLVLKFLQKF", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. INTS9 subfamily."}
+{"protein": "MLSARNSLKNISRQFPKALTRAQSTAAAPTGPVIGIDLGTTNSAVAVMEGKTPKILENSEGGRTTPSIVAFTKDGERLVGIPAKRQAVVNPSDTLFATKRLIGRRYEDPEVQRDINQVPYKIVKHGNGDAWLEARGEQYSPQQIGGFILNKMKETAEAALSKKVNSAVVTCPAYFNDAQRQATKDAGKIVGLNVLRVINEPTAAALAYGLEKKDGEVVAVFDLGGGTFDVSILDIGAGVFEVKSTNGDTHLGGEDFDIALVRYIVDAFKKESGIDLEKDKMAIQRIREAAEKAKIELSSTVSTEINLPFITADASGPKHINQKISRAQFEQLVEPLIKKTIEPCKKALKDAGLSTSDVSEVILVGGMSRMPKVVETVKSIFGKEPSKGINPDEAVAMGAAIQGGILAGEVKDVVLLDVTPLSLGIETMGGVFARLISRNTTIPAKKSQIFSTAAAGQTSVEIRVFQGERELTRDNKLIGNFTLSGIPPAPKGVPQIEVTFDIDTDGIIKVSARDKATNKDASITVAGSSGLSDAEIEKMVNDAEKFAESDKARREAIEFANRADQLCNDTENSLNEHKEKLSSESVQKVQDQIQQLREIVLKAQAGEEVSPEELKQKTEELQNEAINLFKDLYKDGGESSGSSEQPKN", "text": "FUNCTION: Required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Constitutes the ATP-driven core of the motor and binds the precursor preprotein (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MKEFRKILEDKAFFFTTLYILISFLVFKIFPDVFAVIVLMVFFTLLLDPVIRFLEKLKFGKYFSRVAALLLFFFVMVYSLYMIIPPVFNEFGSFIEFMTKVFESKIWKDYIKSPELMPVFDKIMNFLEPKLTDFLNYVFSLVTTNFVSVTTIIVFTLFGLGYTVFYIREIASFFVLIYPKSVRAEAREFFRDVYASMGRYIRVIFINAVIIGLSYWIVFEAFNLKYSAIISLWAFVTNFIPIVGVVLEYIPVLLFSLTLGVKGVLLIALFAILIHAVAFVVFIQLMKGLEKLNPVYIILSILFFGKLFGLFGSFVGVPLALFFKVFWRKFLRPLFEAG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family."}
+{"protein": "MPKRGKKAAADDGEEPKSEPETKKSKGAAKKTEKEAAGEGPVLYEDPPDQKTSPSGKSATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLTHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFESFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKDLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTAYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL", "text": "FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. 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. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'- terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down- regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA. SUBCELLULAR LOCATION: [DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]: Mitochondrion. Note=Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress (By similarity). The cleaved APEX2 is only detected in mitochondria. SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus Nucleus speckle Endoplasmic reticulum Cytoplasm. Note=Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA- irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1- dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 63-79). S-nitrosylation at Cys-92 and Cys-309 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm. Detected in the cytoplasm of B-cells stimulated to switch (By similarity). SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family."}
+{"protein": "MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEAPLLTYAYAHHLTSIDDSNVKRTDMTLQSATKGPMTALVGNEWTLRETELSPVEWLPLQAAPNPTTINEIMTEINKDIASNYTQETAKEDNYFSGKGLQKFAMLALILNKSDQTQLRNPELAQIALDKLKAAFLPYLQNEQADPFRYDTLYKGIVAKAGLPTSMGGTDDLSAEFGHSYYSDHHYHQGYFVVTAAIIHHLDPTWNADRLKAWTEALIRDVNNANDGDEYFAAFRNWDWFAGHSWAGGIKPDGALDGRDQESVPESVNFYWGAKLWGLATGNTPLTKLASLQLAVTKRTTYEYFWMLDGNKNRPENIVRNKVIGIYFEQKTDYTTYFGRFLEYIHGIQQLPMTPELMEYIRTPEFVSQEWDEKLGAIAPTVQSPWAGVLYLNYAIINPAEAYPALRKVQMDDGQTRSYSLYLTATRPHFFRRSLLAALARHGSTRRPSLPSSGDDDKHEDGFLLRFRRLNPFNLKHRIY", "text": "FUNCTION: Cleaves internal linkages in 1,3-beta-glucan. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the glycosyl hydrolase 81 family."}
+{"protein": "MKSIVFVALFGLALLAVVCSASEDAHKELLKEVVRAMVVDKTDAVQAGERECRWYLGGCSQDGDCCKHLQCHSNYEWCIWDGTFSK", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 17 (Hntx-9) subfamily."}
+{"protein": "MASGGAFCLIANDGKADKIILAQDLLNSRISNIKNVNKSYGKPDPEPTLSQIEETHLVHFNAHFKPYVPVGFEYNKVRPHTGTPTLGNKLTFGIPQYGDFFHDMVGHHILGACHSSWQDAPIQGTSQMGAHGQLQTFPRNGYDWDNQTPLEGAVYTLVDPFGRPIVPGTKNAYRNLVYYCEYPGERLYENVRFDVNGNSLDEYSSDVTTLVRKFCIPGDKMTGYKHLVGQEVSVEGTSGPLLCNIHDLHKPHQSKPILTDENDTQRTCSHTNPKFLSQHFPENSHNIQTAGKQDITPITDATYLDIRRNVHYSCNGPQTPKYYQPPLALWIKLRFWFNENVNLAIPSVSIPFGERFITIKLASQKDLVNEFPGLFVRQSRFIAGRPSRRNIRFKPWFIPGVINEISLTNNELYINNLFVTPEIHNLFVKRVRFSLIRVHKTQVTHTNNNHHDEKLMSALKWPIEYMFIGLKPTWNISDQNPHQHRDWHKFGHVVNAIMQPTHHAEISFQDRDTALPDACSSISDISPITYPITLPIIKNISVTAHGINLIDKFPSKFCSSYIPFHYGGNAIKTPDDPGAMMITFALKPREEYQPSGHINVSRAREFYISWDTDYVGSITTADLVVSASAINFLLLQNGSAVLRYST", "text": "FUNCTION: Capsid protein that self-assembles to form the pseudo- hexameric capsomers of the icosahedral capsid (By similarity). The capsid is constructed of 2760 pseudo-hexameric capsomers and 12 pentameric capsomers, with a T=277 symmetry, about 200 nm in diameter (By similarity). The capsid encapsulates the DNA-containing nucleoid, the core shell and the inner membrane (By similarity). Plays an essential role in virion assembly (By similarity). Involved in virus attachment to the host cell (By similarity). SUBCELLULAR LOCATION: Virion Host endoplasmic reticulum membrane; Peripheral membrane protein Host cytoplasm, host cytosol Note=Present in the outer part of the capsid shell (By similarity). Localizes to the viral factory at 16 hpi (By similarity). SIMILARITY: Belongs to the NCLDV major capsid protein family."}
+{"protein": "MKHINDYFWAKKTEENSRLLWLPLTQHLEDTKNIAGLLWEHWLSEGQKVLIENSINVKSNIENQGKRLAQFLGAVHDIGKATPAFQTQKGYANSVDLDIQLLEKLERAGFSGISSLQLASPKKSHHSIAGQYLLSHYGVDEDIATIIGGHHGRPVDDLDGLNSQKSYPSNYYQDEKKDSLVYQKWKSNQEAFLNWALTETGFNSVSQLPKIKQPAQVILSGLLIMSDWIASNEHFFPLLSLDETDVKNKSQRIETGFKKWKKSNLWQPETFVDLVTLYQERFGFSPRNFQLILSQTIEKTTNPGIVILEAPMGIGKTEAALAVSEQLSSKKGCSGLFFGLPTQATSNGIFKRIEQWTENIKGNNSDHFSIQLVHGKAALNTDFIELLKGNTINMDDSENGSIFVNEWFSGRKTSALDDFVVGTVDQFLMVALKQKHLALRHLGFSKKVIVIDEVHAYDAYMSQYLLEAIRWMGAYGVPVIILSATLPAQQREKLIKSYMAGMGVKWRDIENIDQIKIDAYPLITYNDGPDIHQVKMFEKQEQKNIYIHRLPEEQLFDIVKEGLDNGGVVGIIVNTVRKSQELARNFSDIFGDDMVDLLHSNFIATERIRKEKDLLQEIGKKAIRPPKKIIIGTQVLEQSLDIDFDVLISDLAPMDLLIQRIGRLHRHKIKRPQKHEVARFYVLGTFEEFDFDEGTRLVYGDYLLARTQYFLPDKIRLPDDISPLVQKVYNSDLTITFPKPELHKKYLDAKIEHDDKIKNKETKAKSYRIANPVLKKSRVRTNSLIGWLKNLHPNDSEEKAYAQVRDIEDTVEVIALKKISDGYGLFIENKDISQNITDPIIAKKVAQNTLRLPMSLSKAYNIDQTINELERYNNSHLSQWQNSSWLKGSLGIIFDKNNEFILNGFKLLYDEKYGVTIERLDKNESV", "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). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Functions as a ssDNA-dependent ATPase; dsDNA, ssRNA do not stimulate ATPase activity, while other nucleotides (aside from dATP) are not hydrolyzed. Functions as a ssDNA nuclease; activity does not require ATP. Functions as an ATP-dependent helicase; helicase activity requires hydrolysable ATP. Unwinds both DNA/DNA hybrids and RNA/DNA hybrids, moving mostly in a 3' to 5' direction. SIMILARITY: In the central section; belongs to the CRISPR-associated helicase Cas3 family. SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family."}
+{"protein": "MELVSIIIAAYNCKDTIYATVESALSQTYKNIEIIICDDSSTDDTWDIINKIKDSRIICIKNNYCKGAAGARNCALKIAKGRYIAFLDSDDYWVTTKISNQIHFMETEKVFFSYSNYYIEKDFVITGVFSSPPEINYGAMLKYCNIACSTVILDRTGVKNISFPYIDKEDYALWLNILSKGIKARNTNLVDTYYRVHAGSVSANKFKELIRQSNVLKSIGIKAHHRIICLFYYAINGLIKHCFSYRDKRNA", "text": "FUNCTION: Catalyzes the addition of Glc, the second sugar moiety of the O56-antigen repeating unit, to GlcNAc-pyrophosphate-undecaprenol. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
+{"protein": "MNSNKEETTADGSVSTTEEQQQQQQPQQQEQINTTTASTTSNGENTASDNNNNSNNNNNNNTNNTNTNNNCDISMTEDNSKEEDTGIKVIGEGELWGKLISLNPTYPTIEIRQDSIILGRSKGVCNYTFTSPTVSGKHCKIYRDPTVKSRNVAFVDDTSTNGTFINNEVIGKGSKILIENGCEISVIPKKGSEKISFIYQDCFEEQKEMEQGGPQQKYDLREVLGTGNFASVRLGVEKETGNKYAIKIIDKKKMSMTSKRKDSLMDEVNVLTKVKHQNIISIKEVFETQKNLYLVLELVTGGELFDKIVSERKFQEDTCRYILKQLCDSVRYLHSNGIAHRDLKPENILLATPNSFLLKISDFGLSRAMDEGTYMKTMCGTPQYVAPEILTKGEREGYGKSVDLWSIGVITYILLCGFPPFGDPQTKDFFEKIKNGGFSFPSPYWDEISDEAKSLIKNLIKVDVEKRFTIDQALNHPWFTNHEEKTKEFYEKDKLEFPPPSTNDDHQPTPNTTSSNSQLVPESKCDQIQDNTTDNNNNNNNNNNNNNNNNNNNTTNNSNNIDNNNGNDESKSSKKRQLSEDSNINDEHEQKKVKN", "text": "SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHK2 subfamily."}
+{"protein": "MSASSLLEQRPKGQGNKVQNGSVHQKDGLNDDDFEPYLSPQARPNNAYTAMSDSYLPSYYSPSIGFSYSLGEAAWSTGGDTAMPYLTSYGQLSNGEPHFLPDAMFGQPGALGSTPFLGQHGFNFFPSGIDFSAWGNNSSQGQSTQSSGYSSNYAYAPSSLGGAMIDGQSAFANETLNKAPGMNTIDQGMAALKLGSTEVASNVPKVVGSAVGSGSITSNIVASNSLPPATIAPPKPASWADIASKPAKQQPKLKTKNGIAGSSLPPPPIKHNMDIGTWDNKGPVAKAPSQALVQNIGQPTQGSPQHVGQQANNSPPVAQASVGQQTQPLPPPPPQPAQLSVQQQAAQPTRWVAPRNRGSGFGHNGVDGNGVGQSQAGSGSTPSEPHPVLEKLRSINNYNPKDFDWNLKHGRVFIIKSYSEDDIHRSIKYNIWCSTEHGNKRLDAAYRSMNGKGPVYLLFSVNGSGHFCGVAEMKSAVDYNTCAGVWSQDKWKGRFDVRWIFVKDVPNSQLRHIRLENNENKPVTNSRDTQEVPLEKAKQVLKIIASYKHTTSIFDDFSHYEKRQEEEESVKKERQGRGK", "text": "FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)- containing RNAs, and regulates their stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT and ribonuclease P/MRP complexes, depending on the context. The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation. M6A-containing mRNAs containing a binding site for RIDA/HRSP12 (5'-GGUUC-3') are preferentially degraded by endoribonucleolytic cleavage: cooperative binding of RIDA/HRSP12 and YTHDF2 to transcripts leads to recruitment of the ribonuclease P/MRP complex. Other m6A-containing mRNAs undergo deadenylation via direct interaction between YTHDF2 and CNOT1, leading to recruitment of the CCR4-NOT and subsequent deadenylation of m6A- containing mRNAs (By similarity). Required maternally to regulate oocyte maturation: probably acts by binding to m6A-containing mRNAs, thereby regulating maternal transcript dosage during oocyte maturation, which is essential for the competence of oocytes to sustain early zygotic development. Also required during spermatogenesis: regulates spermagonial adhesion by promoting degradation of m6A-containing transcripts coding for matrix metallopeptidases (By similarity). Also involved in hematopoietic stem cells specification by binding to m6A- containing mRNAs, leading to promote their degradation (By similarity). Also acts as a regulator of neural development by promoting m6A- dependent degradation of neural development-related mRNA targets (By similarity). Inhibits neural specification of induced pluripotent stem cells by binding to methylated neural-specific mRNAs and promoting their degradation, thereby restraining neural differentiation. Regulates circadian regulation of hepatic lipid metabolism: acts by promoting m6A-dependent degradation of PPARA transcripts. Regulates the innate immune response to infection by inhibiting the type I interferon response: acts by binding to m6A-containing IFNB transcripts and promoting their degradation. May also act as a promoter of cap- independent mRNA translation following heat shock stress: upon stress, relocalizes to the nucleus and specifically binds mRNAs with some m6A methylation mark at their 5'-UTR, protecting demethylation of mRNAs by FTO, thereby promoting cap-independent mRNA translation. Regulates mitotic entry by promoting the phase-specific m6A-dependent degradation of WEE1 transcripts. 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. The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules. May also recognize and bind RNAs modified by C5-methylcytosine (m5C) and act as a regulator of rRNA processing (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, P-body Cytoplasm, Stress granule Nucleus Note=Localizes to the cytosol and relocates to the nucleus following heat shock stress. Can partition into different structures: into P- bodies in unstressed cells, and into stress granules during stress. SIMILARITY: Belongs to the YTHDF family. YTHDF2 subfamily."}
+{"protein": "MREESWEDHDTIQLTAQRKYLAEVQALETLLTRELSVFLTEPGSKKTNIINRITGKTYALPSTELLRLYEHLEQCRKQGALMYFLERQGTYSGLMLDYDLKLNTNAAPPLEPPALSRLCHRIFVHIKNSSVLPEGSHKIHFFFTLKPEVVQGKYGFHVLIPGLKLAASTKKSIIGSLQHDATVQKILHEQGVANPESCLDPHSASVPSLLYGSSKLNHKPYQLKTGFELVFDSSDPDYIPIHQIKNIESYNLVSELSLTNEQGSLVRPVYCAADIAAEKEEEIPTEDHSLSILMLHDPEARYLHKILNLLPPEYYVEYPLWSNVVFALANTSANYRPLAEWFSQKCPEKWNTGGKEKLEQLWNDASRHTEKKITKRSIMYWAHKHAPQQYKEIVEQGYFSILAEYVYSYNGMLEHYMIAKVIYAMMGNKFVVDVDSNGKYVWFEFVLPGQPMNQGEIWKWRKEVNPDELHIYISENFSRVMDRITEHIKYHLSQPHETNILNYYKKLLKAFERSKSKIFNDSFKKGVIRQAEFLFRQRSFIQTLDTNPHLLGVGNGVLSIETIPAKLINHFHEHPIHQYTHICYVPFNPENPWTKLLLNALQDIIPELDARLWIMFYLSTAIFRGLKEALMLLWLGGGCNGKTFLMRLVAMVLGDHYASKLNISLLTSYRETAEKPNSAFMRLKGRGYGYFEETNKSEVLNTSRLKEMVNPGDVTARELNQKQESFQMTATMVAASNYNFIIDTTDHGTWRRLRHYRSKVKFCHNPDPNNSYEKKEDPRFIHEYIMDPNCQNAFFSILVYFWEKLQKEYNGQIKKVFCPTIESETEAYRKSQDTLHRFITERIVESPSAETVYNLSEVVTAYAEWYNANINVKRHIALELSQELENSVLEKYLQWSPNKTRILKGCRILHKFETLQPGESYIGVSTAGTLLNTPICEPKNKWWEWSPNPSAPPEKEASAPTP", "text": "SIMILARITY: Belongs to the asfivirus helicase C962R family."}
+{"protein": "MTGGKSGGKASGSKNAQSRSSKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVLPNIHQNLLPKKTPKSGKGPSQEL", "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. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H2A family."}
+{"protein": "MLQETISLTPLGQPLIAGFVVVSAVLYLLYNTQQWRPNNLPLLNDGGPFDFLQVTAVNRFRRDARRLIKSGFDSYKNVFAMRTDVGVELFASPEYADQFRNHPSLKVFPFTAKMHHGHLPGFELCRSQPVEDRILIESVRTQLAQSLGKLIQPLASDIGEAISDRWPSESGWQEIVLGSVVERTIAQGTSSVYCLDEAWPEFVVKMEMALGMASAALSAWPVMLRRIVAKFLPECLELYRIMKSGRELMSRDMRRRTALQASTGEEPLNFFEWFKEASHGEEYDELILNLRIAFASMHGLCDHLVKILLRLSEDPQLVSDLRKEVIQVYETHGWSKTALYHLKLMDSAFKEVQRVDPILFVGRVAVADVTLKDGLIIQKGQSIRISGHTMWDEDKYPDAAHFDPYRFYRLRQAPGQENTAQFTSPTSDHLGFGYGGRACPGRFFAAAVLKISLCHVLMKYDIKPANGETGQHVWEFAAAINANMTAKVLVRRRQPEIQI", "text": "FUNCTION: Cytochrome P450 monooxygenase; 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). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MATIRGIVISKQLVYDPSGARYIKVDIIEEKELPGPVAAFSAQDEQTAQLMREVMPLVTQIVRSLPFGGGKIAVPRLTLWLTDEELEMFGDVDVGDVVLISVENGEIKVKPEA", "text": "FUNCTION: Part of an actin-like archaeal cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Forms cell-spanning helical structures. Colocalizes with crenactin."}
+{"protein": "MGARGAPSRRRQAGRRPRYLPTGSFPFLLLLLLLCIQLGGGQKKKENLLAEKVEQLMEWSSRRSVFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSVCRLANEEYQILANSWRYSSAFCNKLFFSKVDYDEGTDIFQQLNINSAPTFMHFPPKGRPKRADTFDLQRIGFGAEQLAKWIADRTDVHIRVFRPPNYSGTIALALLVSLVGGLLYLRRNNLEFIYNKTGWAMVSLCIVFAMTSGQMWNHIRGPPYAHKNPHNGQVSYIHGSSQVQFVAESHIILVLNAAITMGMDLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPYSFLIK", "text": "FUNCTION: Magnesium transporter. FUNCTION: Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with MAGT1. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OST3/OST6 family."}
+{"protein": "MKDKGKLVIWPAYIDQTKSRSSGRIISRKNSIKEPHLNEIKEAARQLGLNPEVEPEKAYPKSWWEVSGRVLVDDNGPKSVIAKQIALAIKKMRGQEVPAKT", "text": "FUNCTION: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SRP19 family."}
+{"protein": "DPITAALSQRAMVLGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPRGAEQPRAEPGHAGLAPGPALTDWARIREELASTGPPVVAM", "text": "SUBCELLULAR LOCATION: [Matrix protein p19]: Virion."}
+{"protein": "MSDSDGSKRPSETPDAADSDSKRQRGSSKSPVDVDEELNAILGANGISELEAASGNANQQDIMDIDFDNLPAELLQKDDIQADRNSVGRSTSGSQTPQPIKSESMINVPQSSQISRPIIRPAMPSAPVVPSSSAPVNRMNPLVQQANSIHGLNTSSIDNRTAPNFSTGHSTGQAGGNNQDRFHTNDPSKLNDALAAAGVDIGREEELLQQQQYNRAPRINVQQPSYLQSRPARQIQRTPFLNSYHLGTFMQRVARENGVLQSFMSDNELLELMSASCEQWISHIATKTVLLSRHRRRGIPALKNKKLAANQIPRSEVSKELRNLALKQKELEEQRVSRRILLGLENKDANSESNKVGAEETLHRAANETAAMMTSNKKKYSWMSSGAGNGDDSKAMEREKDKQSHLLALRGDNGLRFRDIRTGDSVTMKDLLAALEDERMGVNKAIMKGYARLKD", "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": "MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQMWQHRNDPQFSRQFQHGDGQSFNAEDFDDIFSSIFGQHARQSHQRPATRGHDIEIEVAVFLEETLTEHKRTISYNLPVYNAFGMIEQEIPKTLKVKIPAGVGNGQRIRLKGQGTPGENGGPNGDLWLVIHIAPHPLFDIVGQDLEIVVPVSPWEAALGAKVTVPTLKESILLTIPPGSQAGQRLRVKGKGLVSKKQTGDLYAVLKIVMPPKPDENTAALWQQLADAQSSFEPRKDWGKA", "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": "MNRSPGEFQRYAKAFQKQLSKVQQTGGRGQVPSPRGAFAGLGGLLLLGGGALFINNALFNVDGGHRAIVYSRIHGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNVASLTGTKDLQMVNITCRVLSRPDVVQLPTIYRTLGQDYDERVLPSIVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVEAKQIAQQDAQRAAFVVDKARQEKQGMVVRAQGEAKSAELIGEAIKKSRDYVELKRLDTARDIAKILASSPNRVILDNEALLLNTVVDARIDGRGK", "text": "FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass type II membrane protein; Intermembrane side. SIMILARITY: Belongs to the prohibitin family."}
+{"protein": "MFQQNKHHQQQQQQQQQQGVVQSGVASATVNNPSESIVAGNIYECSLHGILSTPSSTFIQRAKGMMRCEHPVSYKEMVFKSTVQSAGPSWAEGSILPSEIHVRYEKNTVYVRYVGVPQIKDNINAMIRNVVDIKSSETFFIYLENLGYVKDYEYFVDGYQYSTYNLSLFLVNHRRVLNDGTKGELLNKHSMVELQCLSGEEGFVAAAEYLNTYAEYLYPFVELIKFDHRLLTAENSNTPTTNVNVVGGYNR", "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 18 family."}
+{"protein": "MDEFREASSVSSSPSTPLRTPLHSPNLFNGDFSVSNRFSFKSSSDYSLSSSFSNGLCSPEDSSSPFSSPPFNGIIPKHNHTSSSPVSFDSLFFKDHEKSHVNGTDDLGLCEDLYRMNIKEDVEEDQIRYARTETLKDPLPKSDHTDFTPDPLYNFSPKHYEPSNGGFVSGGFPYGFFRPPKESSINQSCASWSGFDQSKNDDKRNMFGNNPQQFGWPSYSSSNSGTSPYNNGQEIFENRGGMREYSAYSPPHQPEVSYKHQNYRTTTSDILPLFCQRTQVPMVSKCSEPFSSDESFFMNGKSIDHQRSNTRALMSNNGNPTEICHPSLPNMCDIQGYVYLMAKDQHGCRFLQRIFDEGTSVDAMIIFNEVIAHVVELMMDPFGNYLMQKLLDVCTEEQRTQIVLVATEEPGQLIRISLNAYGTRVVQRLVETIRSGKQISLVKLALRPGFLDLIKDLNGNHVIQRCLQCLSTEDNKFIFDAATKFCTEIATHRHGCCVLQKCIAYSMRQQREKLIAEISRNSLLLAQDPFGNYAVQFVIELRIPSAVAMMLAQLKGHYVQLSMQKFSSHMVERCLMHCPESRPQIVRELVSVPHFDQLLQDPYANFVIQAALAATKGPLHASLVEVIRPHSILRNNPYCKRIFSRNLLKK", "text": "FUNCTION: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. SUBCELLULAR LOCATION: Plastid, chloroplast Cytoplasm."}
+{"protein": "MSKPSSSPFFSETTSRLQDETVFFSLFPDSSLSSAALQSLHLEIIDFVSPFTSPYIWQHEPFSLSIALSSSCACTNTAIPHLHGKLKYGDNLEDEWFAVFLLFRISAAFPSNSIRVWDTDGEFLLIEAAFHLPRWLNPETSLNRVFIRGGDLHIVPRSRLPDPSLVASLRFLIERGNESRASDSVQSALKNRISDYPERAWRNMHRVRVRVPVSVAQVIRHEPFLISLAVEGFYDRDMDSMKHAAKMEKFLSKGREEKLVLVLVKMSRAMYGQLVQQKFQAPNCYPMPSVSDRDAFSEAELGMKIACGMEMMYQQRKKEGEDGKGISWSKYKDNLEKYGYFEGLLSGSKEYKRLMENAEEYHQKSSSFSRTRDIMSAPVRRIDEILALPYSEDDFKGQEVPASDNDSWLYDGEDELNSVLQERQKEMEFYNSKKERKNKGKEKQEAGSSSDANMNNFDLGDISKSMQQFMHKVSSYKGAEVPENRDFKEVSIDVDRFMKDIESMLGSQGRDEQADDDSDGSEGSSMDMDFDDVEDDSEGEESNEDAKESFEESYYGAMNEELKNSTLEKSFENVNQQHSSKQNEESSKTRDEKDDEFTPVDADFNLVKNLLESYSSQQGLPGPASNLLGLMGLQLPKDSGDKN", "text": "SIMILARITY: Belongs to the ECD family."}
+{"protein": "MRFLVWVFFVGLVTFVSGTHAISKLANSNEPQSTQLTMKDIDTLTRLLFVEDGDAAKRFLRSNANQDLTTANDDSDVKEEERGLLPSKVTNLISKAKNGWAKWKANALEKAFQHMMKQGETPTSLAKRLEIGGAAELRYEKVYEKYTAWWINYHTVAGT", "text": "FUNCTION: Effector protein that contributes to pathogen virulence (PubMed:29671919). Targets members of the RABA GTPases subfamily to inhibit vesicular secretion, leading to an accumulation of secretory proteins in the endoplasmic reticulum (PubMed:29671919). SUBCELLULAR LOCATION: Secreted Host cell membrane Host endomembrane system Note=The subcellular localization to plasma and vesicular membranes is most likely the result of binding of RxLR24 to membrane-localized RABA proteins. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MKVSVLITLAVLGVMFLLTSAEERGSDQMDSPAWLKSMERIFQSEERECRWLFGGCEKDSDCCEHLGCRRAKPSWCGWDFTVGK", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 05 (F4a) subfamily."}
+{"protein": "MRYVIAVKSPIYGKQGAFLAYQFAESLIKKEHEISQIFFFQDGVSNGNALVYPANDEVNLQKHWQMFSITYNVPLHLCVAASQRRGVVDNLTTPTTAHYNLAEGFTIAGLGEFIAASLNADRVITL", "text": "FUNCTION: Could be part of a sulfur-relay system. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrE/TusD family."}
+{"protein": "MDFILLIILSGVFLPDIISLQPIVGQEPGVTLSDEEQYYADEENNTDGNSVALHKLEENEMDTPANEKTGNYYKDIKQYVFTTPNIKGSEVSVTATTNLEFAVKKNYKASKPTASGEEEKPSESSRKTSTPNIPAFWTILSKAVNETAVSMDDKDQFFQPIPASDLNATNEDKLSELEEIKLKLMLGISLMTLVLLIPLLIFCFATLYKLRHLRDKSYESQYSINPELATLSYFHPTEGVSDTSFSKSADSNSYWVHNSSEMRRSRTRRSKSKPMDFSAGSNQTVLTDESSFLPPEETRFLLPEEPGKELIVERGPMQAMNEIDAQLLLNKEGSPSN", "text": "FUNCTION: Acrosomal membrane-anchored protein involved in the process of fertilization and in acrosome biogenesis. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane; Single-pass type I membrane protein. Note=In the anterior acrosome region, enriched on the inner acrosomal membrane but minimal on the outer acrosomal membrane; in contrast in the posterior acrosome region enriched on both the inner and outer acrosomal membranes."}
+{"protein": "MFKVIICDDERIIREGLKQMVPWEDYHFTTVYTAKDGVEALSLIRQHQPELVITDIRMPRKNGVDLLDDIKDLDCQIIILSSYDDFEYMKAGIQHHVLDYLLKPVDHTQLEHILDILVQRLLERPHSTNDDAAYHTAFQPLLKIDYDDYYVNQILSQIKQHYHKKVTVLDLINPIDVSESYAMRTFKEHVGITIVDYLNRYRILKSLHLLDQHYKHYEIAEKVGFSEYKMFCYHFKKYLHMSPSDYNKQSK", "text": "FUNCTION: Probable member of the two-component regulatory system SERP2405/SERP2406. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MLKCTIKNEQIETLRSGDTFVSYEIETESDLPVFEDKKFSVRRRYKDFEMLHNILSHDYNGYAIPPLPRKYTVSSFSGGSLSPIFIARRMQSLQTFLDRCSTHPVISNSMHMYQFLENNSWKSYYHNAWMQSENTKSKGNNVSGGIESSIQNLDPYAQSLYETAKQLLQNADTDLSKLEKTCVQYMNSVQNFPTDIPVPSNLSISNLDVVSVEFKRLKRNSIFLINSFHSKVITSIQDLEDYMVVFKSLIKSREQKVKQFEHFQQIVQSNSNNPDQSSRSDPNFVEATPVVQQTPELKPSPNTTIRTSSLFSIPKFFKKKRYSLGQDDANPMELLQLSFQELCIFNEKLEQELNFLRERIDVEMRKTLQMVCDCHVEYFSGILEQHAVKE", "text": "SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "HTDGIFSSDYSKYLDNRRTKDFVQWLLSTKRNGANT", "text": "FUNCTION: Promotes hydrolysis of glycogen and lipids, and raises the blood sugar level. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family."}
+{"protein": "MRAAAISTPKLDKMPGMFFSANPKELKGTTHSLLDDKMQKRRPKTFGMDMKAYLRSMIPHLESGMKSSKSKDVLSAAEVMQWSQSLEKLLANQTGQNVFGSFLKSEFSEENIEFWLACEDYKKTESDLLPCKAEEIYKAFVHSDAAKQINIDFRTRESTAKKIKAPTPTCFDEAQKVIYTLMEKDSYPRFLKSDIYLNLLNDLQANSLK", "text": "FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors (PubMed:10480894). Inhibits B cell chemotaxis toward CXCL12 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form (PubMed:10480894, PubMed:18434541). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytosol."}
+{"protein": "MGSKMLFSLTSPRLFSAVSRKPSSSFSPSPPSPSSRTQWTQLSPGKSISLRRRVFLLPAKATTEQSGPVGGDNVDSNVLPYCSINKAEKKTIGEMEQEFLQALQSFYYDGKAIMSNEEFDNLKEELMWEGSSVVMLSSDEQRFLEASMAYVSGNPILNDEEYDKLKLKLKIDGSDIVSEGPRCSLRSKKVYSDLAVDYFKMLLLNVPATVVALGLFFFLDDITGFEITYIMELPEPYSFIFTWFAAVPVIVYLALSITKLIIKDFLILKGPCPNCGTENTSFFGTILSISSGGKTNTVKCTNCGTAMVYDSGSRLITLPEGSQA", "text": "FUNCTION: Ferredoxin-plastoquinone reductase involved in cyclic electron flow (CEF) around photosystem I. The homodimer is probably not involved in CEF. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein Note=Predominantly located in the appressed regions of the thylakoids and less abundant in the stroma lamellae. SIMILARITY: Belongs to the PGR5 family."}
+{"protein": "MKVTLIAILTCAAVLVLHTTAAEELKTESQLMEVGMPDTELATVDEERLFKCSVSCEIEKESNKDCKKKKCKGGWKCKFNMCVKV", "text": "FUNCTION: Postsynaptic neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 02 (Hwtx-2) subfamily."}
+{"protein": "MSRVLLRGIQCHACRSNVIRSFISLSDVAITPLAGGSRSTAQARPPPLSRNFSSQHAKLFSNQPSDNAELSVDPIPEIHNGEEPEGQPEESQEHIPWYLKEEQVEETIPHPLRRQQPLPPLPENPPPILENLLEHISVDIGLDNLSLLDLRRLDPPPALGANLIMIFGTARGVKHLNVSADRLCRWLRTTYKLRPDADGLLGRNELKIKLRRKARRAKLAKSAKSTLTQPDDGITTGWICVDVGTVEGGQFRKPEEELRKVGFVGFGTVVEGTRIVVQMMTEEKREEIDLEGLWRQKLERNSLENEGLPQPQAAAPQEAGDIHEQLTIPPTNINHQISHATQISPNYEQRRGISTGSRYQDATSDTWGTSRISPNGETTHLEPSAPSSPTSLSHRFKNIPPHEAIYDLGQGTHDRCSTAFLQQFYQEVARAPSELASSRRIELMCIAIELHHPGYRKPDLFQAIQEHILSNYALTRAQFLQILDAFLSFKPDLTSNPPRLLLPNADMELALQIIDHAGLRGLNLLDSTILVKLFVGVSFRAQVYPVEQKDLPNSPVIGNRIPVPLNTCDAVKRVQSRLTRVKTAAKISFTAEQYMKILRVLFDQGSYSGFWNTWEDMALAGVARDKALYVFLFQLHAESDGWQCFTTQLLNCIPMMERENPPVHLDGELAEVTQKCITIAYPEIIDRVERNEQNPLVRMWHRCRVAIENAAAAGGRGQDSTAPYVCNHSDI", "text": "FUNCTION: Probable mitochondrial mRNA stabilization factor. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the ATP25 family."}
+{"protein": "MLLLQSILITKIMVIQLILFFEYALASGFEDKNILKEGKMMFDTLLKQFLEIDKVISLLYKDFVDNYIDFKNLEIVKIKKENEIENKLKSLLKSENIDYALVVAPEDEDILYNLTKIIESYPVKNLGCSSEAIKIAGNKYLTYLAIKDAVKTPKTFPPKKYVVKKIDSCGGKFNLFDENFLIQEFIDGENLSVSLIVGKKIHPLSLNRQYIDKRGFVGGEVNINHKLKDKIFNEAIKAVKCINGLNGYVGVDVIVNNDGIYIIEINPRITTTIYGLKTNPSLAELLIKNANNEELKFKVKGEKFTIDK", "text": "FUNCTION: Catalyzes the formation of an amide bond between tyramine and the gamma carboxy group of L-glutamate. The enzyme also accepts phenylethylamine in vitro."}
+{"protein": "MMRTLITTHPLPLLLLPQQLLQPVQFQEVDTDFDFPEEDKKEDFEEYLEQFFSTGPTRPPTKEKVKRRVLIESGMPLNHIEYCTHEIMGKNVYYKHRCVAERYFLLMQYDELQKICYNRFVPCKNGIRKCNRSKGLVEGVYCNLTEAFEIPACKYESLYRKGYVLITCSWQNEMQKRIPHTINDLVEPPEHRSFLSEDGVFVIPP", "text": "FUNCTION: Does not exhibit any ribonuclease activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pancreatic ribonuclease family."}
+{"protein": "MAVACAAPGSTFSKQLLFFLLVLVLFCDACQKVSLHVPSHLKAETPVGKVNLEECLKSPSLILSSDPAFRILEDGTIYTTHDLLLSSEKRGFSILLSDGQGQEQKKLEVVLSAREKKVFRKRHTKEPVHNRSKRRWAPIPCSLMENSLGPFPQHIQQIQSDAAQNYTIFYSISGPGVDKEPYNLFYIEKDTGDIYCTRSIDREQYDQFLVYGYATTADGYAPDYPLPLLFKVEDDNDNAPYFETKLTVFSVPENCRSGTSVGQVTAIDKDEPGTLHTRLKYKILQQIPDQPKHFSIHPDTGVITTTTPLLDREKCDTYKLVMEVRDMGGQPFGLFTTGTITISLEDENDNSPYFTQTSYTTEVEENRIDVEILRMVVHDQDLPNTPHSKAVYTILKGNENGNFKITTDPNTNEGVLCVVKPLNYEVSRQVTLQIGVLNEAQFTNAANAQPPTMCTTTVTVKIKDRDEGPECQPPVKVIQSKDGLPAGQELLGYKAVDPETSSGEGLRYEMVGDEDNWFEINKITGDLRTVKVLDRESKFVKNNQYNISVVATDTAGRSCTGTLVVLLEDFNDHPPQIDKEVTICQQEKDFAVLEPIDLDGPDNGPPFQFLLDNSSSKLWTLESQDGKRAILRQRHNLNYNYYSVPIQIQDRHGFSAKHVLSVRVCDCTTPTECRMAVKEERDAKPNIILGKWAILAMVLGSALLLCILFTCFCVTTTKRTVKKCFPDDVAQQNLIVSNTEGPGEEVTEANIRLPTQTANICDTSMSVGTLGGQGIKTQQSFEMVKGGHTLESHKGGVLGAAEPGRYAYTDWQTFTQPRLGEKVYLCGQAEEHKHCEDYVRPYNYEGKGSMAGSVGCCSDRQEEEGLEFLDQLEPKFRTLAKTCVKK", "text": "FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. Linked to the keratinization of epithelial tissues. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, desmosome."}
+{"protein": "MVSPRMSGLLSQTVILALIFLPQTRPAGVFELQIHSFGPGPGPGAPRSPCSARLPCRLFFRVCLKPGLSEEAAESPCALGAALSARGPVYTEQPGAPAPDLPLPDGLLQVPFRDAWPGTFSFIIETWREELGDQIGGPAWSLLARVAGRRRLAAGGPWARDIQRAGAWELRFSYRARCEPPAVGTACTRLCRPRSAPSRCGPGLRPCAPLEDECEAPLVCRAGCSPEHGFCEQPGECRCLEGWTGPLCTVPVSTSSCLSPRGPSSATTGCLVPGPGPCDGNPCANGGSCSETPRSFECTCPRGFYGLRCEVSGVTCADGPCFNGGLCVGGADPDSAYICHCPPGFQGSNCEKRVDRCSLQPCRNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGAHRCSCALGFGGRDCRERADPCAARPCAHGGRCYAHFSGLVCACAPGYMGARCEFPVHPDGASALPAAPPGLRPGDPQRYLLPPALGLLVAAGVAGAALLLVHVRRRGHSQDAGSRLLAGTPEPSVHALPDALNNLRTQEGSGDGPSSSVDWNRPEDVDPQGIYVISAPSIYAREVATPLFPPLHTGRAGQRQHLLFPYPSSILSVK", "text": "FUNCTION: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MTNKNTSKDMHKNAPKGHNPGQPEPLSGSKKVKNRNHTRQKHNTSHDM", "text": "SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspP family."}
+{"protein": "MTQPVPRLSVPAALALGSAALGAAFATGLFLGRRCPPWRGRREQCLLPPEDSRLWQYLLSRSMREHPALRSLRLLTLEQPQGDSMMTCEQAQLLANLARLIQAKKALDLGTFTGYSALALALALPADGRVVTCEVDAQPPELGRPLWRQAEAEHKIDLRLKPALETLDELLAAGEAGTFDVAVVDADKENCSAYYERCLQLLRPGGILAVLRVLWRGKVLQPPKGDVAAECVRNLNERIRRDVRVYISLLPLGDGLTLAFKI", "text": "FUNCTION: Putative O-methyltransferase. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family."}
+{"protein": "MAVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFCKDPWYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPGTARTICQDALPLLLDHRKRELQARQECYRWKIYAPGFPRMVDVSSFEEMESDKKFALTKTAPCADQDDNSGNRYLPGFPMKVDIPSLLHMEPNIRYSATKTASLIFNALPASLGMKIRGLLDRKGSWKRLDDIRNIFWCHKTFTSEYVTEHWCEDSFFGYQYLNGVNPIMLHCLSSLPSKLPVTNDMVAPLLGPGTCLQTELERGHIFLADYWILAEAPVHCLNGRQQYVTAPLCLLWLNPQGVLLPLAIQLSQIPGPESPIFLPTDCELDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFSMATLRQLPLCHPVYKLLLPHTRYTLQVNTIARATLLNPDGLVDKVTSIGRRGLIYLMSTGLAHFTYTDFCLPDSLRARGVLTIPNYHYRDDGLKIWAAIERFVSEIVSYYYPNDACVQQDSELQAWVGEIFAQAFLGRESSGFPSRLCTPGELVKYLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGNTTMESYLETLPEVNTTCSNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRQSIAAFQKCLAQISKDIRARNESLALPYAYLDPPLIENSVSI", "text": "FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega- hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites (By similarity). Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (By similarity). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia (PubMed:23382512). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lipoxygenase family."}
+{"protein": "MNDNNSCKLTMLTRRLENMTQEYGQPDLPVPFLNGDEPGKLKLPLSERHEDVDYLTKEQCIQYFNGYSIHLIPPRISS", "text": "SIMILARITY: Belongs to the UPF0612 family."}
+{"protein": "MALPIIIDCDPGHDDAIALVLALASPELEVKAITSSAGNQTPEKTLRNVLRMLTLLKRPDIPVAGGAVKPLMRELIIADNVHGESGLNGPALPEPSFAPQSGTAVELMAKTLRESAQPVTIVSTGPQTNVALLLNSHPELHTKIARIVIMGGAMALGNWTPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHAADIERFRAIGNPISTIVAELLDFFMEYHKDEKWGFVGAPLHDPCTIAWLLKPEIFTTVERWVGVETKGKYTQGMTVVDYYFLTGNKPNATVMVDVDRQGFVDLLAERLQYYA", "text": "FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. SIMILARITY: Belongs to the IUNH family. RihA subfamily."}
+{"protein": "MRAQTLPAGSDHAPVLACGAWLKNAACLLRGAEVLWSPIHGDLGDPANCDALDQSVEQLLDSAHGQVQAVAHDLHPDFYSTQLAQRLAARLCVPAVAVQHHHAHIAALMAEYDLREPVIGLALDGVGLGTDGTAWGGELLWVSPSEWCRLGHLQSLPLPGGDVAAREPWRMAAAALHVLDRTGEIGRRYGAVVGEQAARTVAAMLERQLNCPRSSSAGRWFDAAAGALGVSVRQQAEAQAAIALEALAADYLSALSPPECVGTYVVDQDGVLDLRGLLEQLFALADEGQAGQAARGAALFHVALAEALVGWAADAAQGHGLKTVALGGGCFMNGILSASVQAGLAARGLQALLPRAVSCGDAGLALGQAWVAARQPTAALAPQTHLQEEGAPCA", "text": "SIMILARITY: Belongs to the carbamoyltransferase HypF family."}
+{"protein": "MRFHTILLAALASLVIATPLPSDTDVSLERRQSMNSNDLEKGDCKSVAFIFARGSTEIGNMGFVVGPGVCSNLKSTLGSDKVACQGVGGAYTAGLIQNALPANTDSGSIKEAVKMFDLAAKCPDTQIVAGGYSQGSAVIDNAIQKLDDSTRDRVKGVVLFGFTRNLQDKGQIPGYPKDQTKVYCAVGDLVCSGTLIITASHMTYGLNAGDAAKFLASQVSV", "text": "FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:16844780). 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 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family."}
+{"protein": "MNLIHKVSTICQCVLVILAKYCMQIIALSLMSGVQWLAWGIYKINKNRVGIIILFLYIMIVTCYVLTNLTPPGSPSETSFDPNSTRQYMTLQNGKSRFCEKCQEYKCDRSHHCSQCNKCILRMDHHCMWFKNCVGFRNHKFFFLECFYLNLYSICVLYSTFVAITKTFTAEGANISAIYLVFWGFLFAFAVGMSIVMTAFTFYHTSLLIHNLSTLESMSSSWSRYTHSTQPFNVGWYENWCQIMGKSPFLWLLPFPNSIGEGVEYPLNANALPYLPQTEEKNDKLYKSSVPASIAGAEGWSSDEEQYAMKNRRWNPHMGQYEWIEDFLV", "text": "FUNCTION: Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA3 subfamily."}
+{"protein": "MTALFNFWRIMYANISSIWLLVVSFFEWLFSATSISQQRGSGPRKGKVVMNKDCRSWEDWKVLATTIDKASGRWKWRFTPASDKYDYLLIDRCTVSLKRYRQRKSVYPMLMFLRSSLLRNFGNIGNSSLYTENYSGTKILIEEYVREVNNCLEFLYHTKRLSYDVKCDFFSAARISFGTTCLYFNGGTAFGLYHFGVAKTLWKRNLLPQILAGCASGALIASLLSVYRDEELNGLFDTFPSELWKICQQTSDYSLSKVVEYGNMLDISMIASFVRQRLGTITFQEAFERTGRIVNIVAPPSAVSGSPQVLNYFTAPNVLIWSAVCSSNSWAAIYRSSPLLAKLPDGSTEVCTPKNFIWPYAGLPNTGRSNPYARISEIFNVNHFVITQSRPSLFPTFYDELHHHRVSGYSLKMIRLVGLEMAYRFRQLDILGLLPPRLRRFFVDDYVPSAYITLTPTFSFSDIKHAFTKPSLSDIQYWILVGERATWQAIPLLQVRCKTEISLRHLSKNLTNSYVEPLSVNNLASPFVTNLEENQEKMLKIFKVK", "text": "FUNCTION: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways. SUBCELLULAR LOCATION: Lipid droplet Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols."}
+{"protein": "MTKSYSESGPAGEPQAQAPPGWAAGCLSPPADGPEADKKEEDLEALHGEAEEDALRNGEEEDEEDELDEEEEEEEEEEDDEQKPKRRGPKKKKMTKARLERFKLRRMKANARERNRMHGLNAALDNLRKVVPCYSKTQKLSKIETLRLAKNYIWALSEILRSGKSPDLVSFVQTLCKGLSQPTTNLVAGCLQLNPRTFLPEQSADAAPHLPPAGAPFAPPPFPYASPGLPSPPYGTMDSSHLFHLKPPHAYGAALEPFFEGGLPEGAGPAFDGPLSPPLSINGNFSFKHEPAADFDKSYAFTMHYPAGPLPAAPAHAAVFSGAAARCELPGDGLAPYEGHPHHERVLSAQLSAIFHE", "text": "FUNCTION: Acts as a transcriptional activator that mediates transcriptional activation by binding to E box-containing promoter (5'- CANNTG-3') (PubMed:9310321, PubMed:9740021). Acts as a differentiation factor during neurogenesis (PubMed:9310321). Induces photoreceptor cell overproduction in vivo and de novo generation in vitro (PubMed:9740021). May play a role in photoreceptor cell production (PubMed:9740021). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MCYTLGFVTGVLFLLFDRSPFVRFHAVQSTLTFSTITALVILLPVLPGGALLSRVVMAFSIILWAFCIVKASRGEAFKLPIFGDIAEEQLSLNYT", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0132 family."}
+{"protein": "MGKLTILFLVAAALLSTQVMVQGDGDQPADRDAVPRDDNPAGTIEKFMNLLRQVRCRWTPVCG", "text": "FUNCTION: Its target is unknown, but this toxin may modulate voltage- activated calcium channels (Cav) or calcium-dependent potassium channels (KCa). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the O2 superfamily. Contryphan family."}
+{"protein": "MQTLKCVVVGDGAVGKTCLLISYTTNQFPADYVPTVFDNYAVTVMIGDEPYTLGLFDTAGQEDYDRLRPLSYPSTDVFLVCFSVVSPPSFENVKEKWFPEVHHHCPGVPCLIVGTQIDLRENKMVIEKLQRQRLRPITPEQGEKFARELRAVKYVECSALTQRGLKNVFDEAIVAALEPPVIKKSKKCTIL", "text": "FUNCTION: Involved in development of cell polarity during the cell division cycle. Required for the establishment of actin polarization in germ cells. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily."}
+{"protein": "MAMLEARPYRPFKSSEEYLEAMREDLAEWLSTLYPELSINADNFMDRLDTGVALCKHANYVRQAAVDYLARRQARNKSMTRSMTSGLAGPILAMGNVHYLPAAKSGTFFARDNVSNFITWCRKSLKIIECLLFETDDLIMRKNEKHVILCLLEVARRGAKFGMLAPMLVQMERQIDREIAADIKANGAGCSENGTQTDALETGNSSAATMTTITTTTVETDLYDDSDDSETEDDGDQNPVLMYGPQPQIITNDLKSLDEMVRDLVEKCTCPSQFPMVRVSEGKYRIGDTKVLIFVRILRSHVMVRVGGGWDTLSHYLDKHDPCRCRAQHRSSVAARLIPRQSPNHNPSNGIELHKAQVIFERSPPAARRVFNSPNCNGGPGTGSSCGTGVVGVAVPPTLQNGHSLSPNSGKYRSRSPTPQRKFLNQQANGGGIASATGSSQTVTTDTSSGQLLGSPSLARRSMSPSPRRLIDMRKKQSSLDSYSSGPKSLPGYSCSMEEANGGSGVGSAAGGVSSGSAGSGVAGEQGGANKFENISDNGSEISDEGYRSLGVIQSGAQKRESLHSQASIEDAESNARLDQTSSDSQISPSDEPAEKATTDILEEEDLNGQDREEDQEDYSVCDGPQSLPAILSGAHKLSDKFEQSGVFITDDEITVDIAKTEDQSVANTMGNPTPNLSKIPRSPLAQRRRRSIDNSTCGGAGGSLQDLSSRSGLPAPAFSRKQPVYRSVRTRNSTGATTTPVAPPRSRQATQLPMVRDVTNTWSGRTTGAPKRRPPCTADTFVAPTNGTGPAGSFERNGKGRSSQILYDSNGRRVRSGAPGCTSSLTTSPVKNHASSPLAQQLLEAASSAKNDAQILEKMKSLLSRYAAGNQTKAGVGATATAANKINSNGKKTPVYEDFTTAWVHSNGNLERSESCSPPAKARSKRSSAASSCESNNSNAGAGSGAAAGSASVVSPRRERGMSKIPAPVRHHTELY", "text": "FUNCTION: Essential for development and viability. Required for ovary development and oogenesis, and is essential for the development of the indirect flight muscles. May act as a negative regulator of the Notch signaling pathway in certain tissues, such as the muscle precursors and ovaries. May function as a linker protein between the actin and microtubule cytoskeletons. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cell cortex Note=In the cytoskeleton associates with both actin and the microtubules. SIMILARITY: Belongs to the GAS2 family."}
+{"protein": "MNAYNKADSFSLESDSIKDVIHDYICWLSMTDEMRPSIGNVFKAMETFKIDAVRYYDGNIYELAKDINAMSFDGFIRSLQTIASKKDKLTVYGTMGLLSIVVDINKGCDISNIKFAAGIIILMEYIFDDTDMSHLKVALYRRIQRRDDVDR", "text": "FUNCTION: Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factors 3/IRF3 and 7/IRF7, transcription factors critical for the induction of interferons alpha and beta. This blockage is produced through the inhibition of host TBK1, by binding host TBK1 adapter proteins TBKBP1 and AZI2, thereby producing a strong inhibition of the phosphorylation and activation of IRF3 and IRF7. Acts also as an inhibitor of the cellular response to type I IFN by interacting with host STAT2. Mechanistically, exerts its inhibitory effect after host ISGF3 complex (composed of STAT1, STAT2 and IRF9) binding to the interferon stimulated response element (ISRE). SIMILARITY: Belongs to the orthopoxvirus OPG029 family."}
+{"protein": "MSQFKRQRINPLPGGRNFSGAASTSLLGPPPGLLTPPVATDLSQNARHLQSGEKQRVFTGIVTSLHDYFGVVDEEVFFQLSVVKGRLPQLGEKVLVKAAYNPGQAVPWNAVKVQTLSNQPLLKSPAPPLLHVAALGQKQGILGAQPQLIFQPHRIPPLFPQKPLSLFQTSHTLHLSHLNRFPARGPHGRLDQGRSDDYDSKKRKQRAGGEPWGAKKPRHDLSPYRVHLTPYTVDSPTCDFLELQRRYRSLLVPSDFLSVHLSWLSAFPLGQPFSLHHPSRIQVSSEKEAAPDTGAEPSPEDSDPTYSSKVLLLSSPGLEEFYRCCMLFVDDMAEPRETPEHPLKQLKFLLGRKEEEAVLVGGEWSPSLDGLDPQADPQVLVRTAIRCAQAQTGIDLSTCTKWWRFAEFQYLQPGPPRQLHTVVVYLPDVWTIMPTLEEWEALCQQKATEAAPQPHEASGEAEATEQAPDVSEQADTSKQNTETMEATTQQDVDTDLPEAPPPPLEPAVMARPRCVNLSLYGIVEDRRPKERISFEVVVLAELFVEMLQRDFGYRIYKTLLSLPEKVVSPPEPEKEEAAKEDAVKEEEAVKEEAVKVSKDEVQNEGTAAESDSPLKEDGLLPKRPSSGGEEEEKARGEAAEDLCEMALDPDLLLLRDDGEDEFAGAKLEETEVRSVASNQSEMEYSSLQDMPKELDPSTVLPLDCLLAFVFFDANWCGYLHRRDLERVLLTLGIRLSAEQAKQLVSRVVAQNICQYRSLQYSRAEVLDDGLPEDVLFGNLDLLPPSGKSTKPGAAPTEHKGLVPHNGSLINVGSLLQRAEQQDSGRLYLENKIHTLELKLEESHNRFSATEVTNKTLAAEMQELRARLAEAEETARTAERQKNQLQRQMQDFRRRLTPLHLEMQRIVEKADSWVEKEEPTPSN", "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 (By similarity). Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (By similarity). Inhibits SUV39H1 methyltransferase activity (PubMed:19218236). Mediates ligand- dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (By similarity). Regulates the circadian expression of the core clock components NR1D1 and BMAL1 (PubMed:23398316). Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation (PubMed:23398316). Represses the ligand-dependent transcriptional activation function of ESR2 (By similarity). Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway (By similarity). Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3 (By similarity). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional activator activity of BRCA1 (By similarity). Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton, spindle Note=Recruited to chromatin, post-UV irradiation. Sequestered to the cytoplasm in the presence of MCC. Translocated to the cytoplasm during UV-induced apoptosis."}
+{"protein": "MKLNFLVTTVALLVAFPPPYECRAIDSSSNQPATDPDGERQSAPVLARLGEEYFIRLGNRYQNSLRSSPDTYPETSQYPKRALQLQLTQRLLEGKVGNVGRWDGNYALRALDSEERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKMMEIFGK", "text": "FUNCTION: This hormone from hypothalamus regulates the release of corticotropin from pituitary gland. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sauvagine/corticotropin-releasing factor/urotensin I family."}
+{"protein": "MRKLRRLVHMVLFCPISKGLQSRLPGIKVKYLFLAWLSVFVGSWVVYMHYSSYSELCRGHVCRMIICDQYKKGIISGSACKDLCDERTLVFQQCLSSSPTQQVYSGRWRDREVIIKCGVEETLKADSNPDSPPRRELVLFDKPTRGTSMDEFKEMLGNFLKANLGEQVSLTALVSQILTMADVNNDGKVSLAEAKSIWALLHLNEILLMLSLREKEHTSQLLGHCGDLYVTEKIPHDSLYGSQIPGFLQTLLPSPVHRLVHQWCAPAWPRRAKIAIGLLEFVEEIFHGTYGSFFICDSSFKNIGYNEKYDFKVVDLRKVATEMTIRGFLKGRHCEQNSDCTFGSDCTAACDKLMKQCRNDVIQPNLAKACQLLQDYLLYGSPSDLREELQKQLRTCMTLSGLASQMEVHHSLILNNLKTLLWKKISNTKYS", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the DIPK family."}
+{"protein": "MAIKVHGSPMSTATMRVAACLIEKELDFEFVPVDMASGEHKKHPYLSLNPFGQVPAFEDGDLKLFESRAITQYIAHVYADNGYQLILQDPKKMPSMSVWMEVEGQKFEPPATKLTWELGIKPIIGMTTDDAAVKESEAQLSKVLDIYETQLAESKYLGGDSFTLVDLHHIPNIYYLMSSKVKEVFDSRPRVSAWCADILARPAWVKGLEKLQK", "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": "MSFKSIFLTGGVVSSLGKGLTAASLALLLERQDLKVAMLKLDPYLNVDPGTMNPYEHGEVYVTDDGVETDLDLGHYHRFSSVQLSKYSTATSGQIYTKVLTKERNGEFLGSTVQVIPHVTNEIINVIQSCADHHKPDILIVEIGGTIGDIESLPFLEAVRQFRCEHPQDCLSIHMTYVPYLRAAKEIKTKPTQHSVQNLRSIGISPDVILCRSEAPLSTEVKRKISLFCNVPEHAVFNAIDLERSIYEMPLLLAKENISDFLLNKLGFSPKPLDLSDWQDLVEALCDKERQHVRIGLVGKYLEHKDAYKSVFESLFHASVPANCSLELVPIAPESEDLLEQLSQCDGCLIPGGFGTRSWEGKISAARYCRERNIPCFGICLGMQALVVEYARNVLDKPLANSMEINPETPDPVVCMMEGQDSVVKGGTMRLGAYPCRIAPGSLASAAYKTDLVQERHRHRYEVNPSYIERLEEHGLKIAGVCPLGELCEIVEIPNHRWMLGVQFHPEFLSKLAKPHPLFIEFIRAAKAYSLEKANHEHR", "text": "FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. May be involved in lipopolysaccharide biosynthesis, potentially channelling CTP directly to CMP-KDO synthetase (PubMed:8951811). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity). SIMILARITY: Belongs to the CTP synthase family."}
+{"protein": "MDPSPLLALLLLLGAARALSTCQRLDLEAAKKKRIEAVRGQILSKLRLTAPPPASETPPRPLPDDVRALYNSTQELLKQRARLRPPPDGPDEYWAKELRRIPMETTWDGPMEHWQPQSHSIFFVFNVSRVRAEVGGRALLHRAELRMLRQKAAADSAGTEQRLELYQGYGNASWRYLHGRSVRATADDEWLSFDVTDAVHQWLSGSELLGVFKLSVHCPCEMGPGHADEMRISIEGFEQQRGDMQSIAKKHRRVPYVLAMALPAERANELHSARRRRDLDTDYCFGPGTDEKNCCVRPLYIDFRKDLQWKWIHEPKGYMANFCMGPCPYIWSADTQYTKVLALYNQHNPGASAAPCCVPQTLDPLPIIYYVGRNVRVEQLSNMVVRACKCS", "text": "FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. FUNCTION: Transforming growth factor beta-1: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency- associated peptide (LAP) and Transforming growth factor beta-1 (TGF- beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix. At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus. TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin- binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1. Once activated following release of LAP, TGF- beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency- associated peptide chain (LAP) and 'milieu molecules'. Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation. Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner (By similarity). Can induce epithelial- to-mesenchymal transition (EMT) and cell migration in various cell types (By similarity). FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1. Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1. SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix. SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
+{"protein": "MNRLRNAKIYVERAVKQKKIFTIQGCYPVIRCLLRRRGWVEKKMVHRSGPTLLPPQKDLDSSAMGDSDTTEDEDEDEDEEFQPSQLFDFDDLLKFDDLDGTHALMVGLCLNLRNLPWFDEVDANSFFPRCYCLGAEDDKKAFIEDFWLTAARNVLKLVVKSEWKSYPIQAVEEEASGDKQPKKQEKNPVLVSPEFVDEALCACEEYLSNLAHMDIDKDLEAPLYLTPEGWSLFLQRYYQVVHEGAELRHLDTQVQRCEDILQQLQAVVPQIDMEGDRNIWIVKPGAKSRGRGIMCMDHLEEMLKLVNGNPVVMKDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFSLKNLDNSVHLCNNSIQKHLENSCHRHPLLPPDNMWSSQRFQAHLQEMGAPNAWSTIIVPGMKDAVIHALQTSQDTVQCRKASFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLRVVIDRMLDRNCDTGAFELIYKQPAVEVPQYVGIRLLVEGFTIKKPMAMCHRRMGVRPAVPLLTQRGSGEARHHFPSLHTKAQLPSPHVLRHQGQVLRRQHSKLVGTKALSTTGKALRTLPTAKVFISLPPNLDFKVAPSILKPRKAPALLCLRGPQLEVPCCLCPLKSEQFLAPVGRSRPKANSRPDCDKPRAEACPMKRLSPLKPLPLVGTFQRRRGLGDMKLGKPLLRFPTALVLDPTPNKKKQVKYLGLDSIAVGGSRVDGARPCTPGSTARA", "text": "FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction (By similarity). Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (By similarity). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (By similarity). Involved in microtubule glycylation of primary cilia in colon which controls cell proliferation of epithelial cells and plays an essential role in colon cancer development (PubMed:25180231). Together with TTLL8, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, cilium Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, flagellum axoneme."}
+{"protein": "MLTVTTLVQLMKRTLAVGAVALAAVSLQPGTATAGPAPVVGGTRAAQGEFPFMVRLSMGCGGALYTQQIVLTAAHCVSGSGNNTSITATAGVVDLNSSSAIKVKSTKVLQAPGYNGKGKDWALIKLAKPINLPTLKIADTKAYDNGTFTVAGWGAAREGGGQQRYLLKANVPFVSDASCQSSYGSDLVPSEEICAGLPQGGVDTCQGDSGGPMFRRDNNNAWIQVGIVSWGEGCARPNYPGVYTEVSTFAAAIKSAAAGM", "text": "FUNCTION: Involved in mycelium differentiation. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MSRADDDAVGVPPTCGGRSDEEERRIVPGPNPQDGAKDGAKATAVPREPDEAALAAMSNQELLALGGKLDGVRIAYKEPRWPVEGTKAEKRAERSVAVWLLLGGVFGLALLLIFLFWPWEFKAADGESDFIYSLTTPLYGLTFGLSILSIAIGAVLYQKRFIPEEISIQERHDGASREIDRKTVVANLTDAFEGSTIRRRKLIGLSFGVGMGAFGLGTLVAFAGGLIKNPWKPVVPTAEGKKAVLWTSGWTPRYQGETIYLARATGTEDGPPFIKMRPEDMDAGGMETVFPWRESDGDGTTVESHHKLQEIAMGIRNPVMLIRIKPSDLGRVVKRKGQESFNFGEFFAFTKVCSHLGCPSSLYEQQSYRILCPCHQSQFDALHFAKPIFGPAARALAQLPITIDTDGYLVANGDFVEPVGPAFWERTTT", "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. 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": "MNSTNSTNSTTTATSTNTSTQQVVTSLVSNGTIFGVFVIAFLILRIKLKRIYEPKSSFNLINEEKKPEPLPQGVWQWLKPLLKKSDNFVIQQAGLDGYFFLRYLFIIAIYCAVSMSYIFPILLSINASNGNHESGLNQLAYQNVKHRGRYFAHVFCGWIFFWGFLYIIYRELYFYTSMKQAVLASPRYAKKLSSRTVLFQTVPKQYLSEEEFSKLFDGVKRVWIARGSGSIEAMVKARDNMAIQLEGAETKYLKAALKKIKKLNKKSPQLSVSDNIAEYVPDKKRPHHKINKVAKFFFGKKVDTISYIKEELPKLNQKVKALQEDHENSSPFNSVFVEFESQYQAQVAAQITTYHAPLFMTPVYIGIEPSDVVWFNLRMFWWERLGREVSAVSAIVALVILWAFPVAFVGMISNITSLTNEVKWLKFIYKLPKQLLGLLTSLAPTVALAVLMSFLPKFIRGMAITQGAPSKQNVEYFTQQAYFAFQVIQVFLVTTLSSAATSTVTEIVKEPTKAMDLLASNLPKASNFFMSYVILQGLSISSGALLQIVPLILFYVLGAFLDGTVRKKWNRFCGLSSMQWGTAFPVYTNLAVITFSYSIISPLILLFAAVAFFLLYIAYLYNLTYVYQESPDARGIYYPRALFQTIVGIYIGQICLLGLFAVGKGWGPIVLQVIGICVTVLIHLHLSAAFDHLSKVIPVDTMKPLDGVSDTPSFKNIYKGIESTKVKKNTFGANIDMDGIKELPEFPIKKYHKRSESVTEQQVENSIFSENTFEYQFNPANEANADGHAINAENLIEDVPLLADGDTMKIPPAPWWKRFLKPHIYYSYKAVKSRLPEIYGLVDPDERVNDFDISHAYDYPAVSAQCPELWIPRDPFGFSKLLISDVSGVVEMNDENATIDENLKFTLRDVPPPYNDVKDEANGEANGEFDTASKENNPFADPKYKEEESRSAV", "text": "FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family."}
+{"protein": "MALDKSIVVNFTSRLFADELAALQSKIGSVLPLGDCHRLQNIQALGLGCVCSRETSPDYIQIMQYLSKCTLAVLEEVRPDSLRLTRMDPSDNLQIKNVYAPFFQWDSNTQLAVLPPFFSRKDSTIVLESNGFDLVFPMVVPQQLGHAILQQLLVYHIYSKISAGAPDDVNMAELDLYTTNVSFMGRTYRLDVDNTDPRTALRVLDDLSMYLCILSALVPRGCLRLLTALVRHDRHPLTEVFEGVVPDEVTRIDLDQLSVPDDITRMRVMFSYLQSLSSIFNLGPRLHVYAYSAETLAASCWYSPR", "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": "MTINYQFGDVDAHGAMIRAQAGLLEAEHQAIVRDVLAAGDFWGGAGSAACQGFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWA", "text": "SUBCELLULAR LOCATION: Secreted Note=Probably secreted via the ESX-5 / type VII secretion system (T7SS). SIMILARITY: Belongs to the WXG100 family. ESAT-6 subfamily."}
+{"protein": "MYATQPYLELRERLSQIWINRYTLLLMLCMVKILLFTSSLRFSLNNSKVHVLEECSNIEHYYNILRNGTPHYMGKMGNYLVAHALEATVESLLALLTSLATVVEVVAHFMIELWLGTYACLLFSAAHGAVEVATNVTEKVIGVANKTLIAAANELDNGLDGLSKVLNKIIETGTKVSHLFKDDDEEHASPEGQFKKINLTIASLRTVKIPESVNDKLRSLAEKTPDFEDVKNKTKGLVSIPFQTLKNEINGINATSMLKNRKLMSVPPIDMGDAADGVCSANRDGIESVYRNLNSALIYSLVATAVSLAIVALLCLIPAAWHEYRQWERLSALRDHERTVDCKDPFADTHSSASASTASSTRCDVIQNYQGVFHRAPTLIGEWVARHTAHTQEGALRIQWLLAYVLSPRALVPLALGLAGVLVCGCQFLIIHALRIQLASTSTRDSLQRLETDTAGLVAHDLSRWADSTNAYINGTEASVNAGLLGWVTTATTALNTTVAALLADIDSTVDRAFADTPLHRPMVTVVSCVIGNKLRAIEAGLTWTHDHVRIALPRIHTARLRDAVAEPDLPTHPAYTAVLQSLSDRLRHSVDRVLHQCCAAVRIELYVSLALLGLWILQTPLGLAMLLFKSHCRRRNLRRRVP", "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": "MTTKFVFDLLAPDDILHPFNHVKLIIIRPIEVEHIIIATTMPAV", "text": "SIMILARITY: Belongs to the coronaviruses ns4.9 protein family."}
+{"protein": "MPLHVSLANGNRDLDYDSVQPYFMCDDEEEDVHHQQPPQPPAPSEDIWKKFELLPTPRPSPGHAGLYSPPCEAVAVSFAPRDHDGDSFSIADLPELPGGDAVKQSFVCDPDDETFVKNIILQDCMWNGFSASAKLVSKLDPYQAVRKEGTGVSLAADVEPATPPDCTCNT", "text": "FUNCTION: Seems to act as an inhibitor of cellular proliferation. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MTATTHAPYRLEGKVALVTGSGRGIGAAMALELGRLGAKVVVNYANSREPAEKLVQEIKELGTDAIALQANIRNVSEIVRVMDDAVAHFGGLDIVCSNAGVVSFGHLGEVTEEEFDRVFSLNTRAQFFVAREAYRHLNTHGRIILMSSNTAKEFSVPRHSVYSGSKGAIESFVRVMAKDCGDKQITVNAVAPGGTVTDMFYDVAQHYIPNGEKHSAEELQKMAATVSPLKRNGFPVDIAKVVGFLASREAEWVNGKIITVDGGAA", "text": "FUNCTION: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213, PubMed:22909031, PubMed:26266881). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751, PubMed:22909031). The short chain dehydrogenase mdpC converts the tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-thracen-1(2H)-one derivative (PubMed:22909031, PubMed:26266881). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MSTQWWKESVVYQIYPRSFQDYNGDGIGDIPGIISRLDYLKTLGVDVIWLSPVYDSPNDDNGYDIRDYKAIMDEFGTMADWETLLAEIHTRGMKLIMDLVVNHSSDEHAWFVESRKSKDNPYRDFYIWRPGKDGKEPNNWASNFSGSAWTYDETTGEYYLHLFSKKQPDLNWENPKLREKIYEMMTWWLDKGIDGFRMDVINFISKVDGLPDAEPQPGQPYVSGSNYFMNGPNIHTYLQEMHENVLQHYDLMTVGEMPGVTLELAQLYTGEERNELNMVFQFEHVGLDQGPNGKWDLKPLELKDLKASLSRWQKGLQDIGWNSLYWNNHDQPRIVSRFGDDQSYRVESAKMLATLLHCMKGTPFIYQGEEIGMTNVRFDSIEQYQDIETLNMYKEKRAQGVPHETLMASIHAKGRDNARTPMQWDETKHGGFTDGTPWLEVNPNYKEINVKQALKDPNSIFYHYQKLIQLRKEHAILVHGSYDLILEDDPEIFAYKRTYNGQTLLVVCNFYGRITDFECPAEVVLSEPTLLLSNYDEEENGSYTSFRLRPYEARVYLGKNE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MSEAARDLSPGAPPAVAAAAPEERKGKEPEREKLPPIVTAGAAAGLDRGSKGQISTFSSFVSTVTQKKEAAENRSSPTHLALPNIRNVRDLPPICLDVRQKQRMSVEALPSEVKVPPLPEPSLPSQPKTVKDFEEDLEKAEATGNWKTVHAFYITAFDSFTELNTAFKKDATASFNTIEDSGLNANLVNAVFDALLNTPQDIQKSVLKGIINSLLQEWKGPRTKDDLRAYFILLQNPQFNITSTYVIYAHLLRQIATLVEADHHFLVHWLKKLSQKKFKQLVERLLQFVSLRLFPAKPEEFPPLTKCTWWIPSAAKVLALLNTANNLVHPPLVPYTDFYNSTLDHIDLMEEYHTWQSFGNSHRFSFCQYPFVISIAAKKIIIQRDSEQQMISIARQSLVDKVSRRQRPDMNMLFLNMKVRRTHLVSDSLDELTRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFSSFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVVPSDQSTPVGICSVTIDDLCQVMPELAHGLKELLSYEGNVEEDFYSTFQVFQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHALQRSTQYDGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFKISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE", "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."}
+{"protein": "MAVTECEWASLGSRIGLRAALVLLSGSLLVVLFPLSGLEHQYRTALNILLQCNLWGGDDRHTFTGQTRGLAVASTAIELLVLKQKPTSDVKFEAKAALNQALEMKRQGKKEKAHKLLHHALKMDPDHVDALNELGILLEEEKDIIQADYLYSKALTISPHNEKALINRDRTLPLVEEIDQRYFSLIDSKVKKLMSIPKGNPALRRVMEESYYHHIYHTVAIEGNTLSLSEIRHIIETRYAVPGKSLEEQNEVIGMHAAMKYVNATLVSRIGSVTIDNILEIHRRILGYVDPVEAGRFRRNQVFVGHHIPPHPRDVEKLMQEFVQWLNSEEAMSLHPVEFAALAHYKLVYIHPFVDGNGRTSRLLMNLILMQAGYPPITVRKEQRSEYYHVLEIANEGDVRPFIRFIAKCTESTLDLLLIATAEHPVGLPEPNHGFSECKQTITIKT", "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-222 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (By similarity). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the fic family."}
+{"protein": "MKSTVKKSAPREFGGAKGALAIMTGFPCLMYYLWACSKFNDSQFIKPESFTIAGFQNFFRTLGHYIYVGAYPTRYAFLVFWSFCIVQAVMYLTLPGVRTQGLPLKHRNNERLPYLCNAIWSFYTTIVILAVLHVTHVFPITTFIDMFGPLMSVAIITAFVCTFVLYTGTLLFGDRLFDKPHRLSGNPIYDAFMGACLNPRLGKLLDFKMFFEVRIPWFILFFISVGAAVRQYETYGTVSPQVLFVCLGHYLYANACSKGEQLIVPTWDMAYEKFGFMLIFWNMAGVPFTYSHCTLYLFSHDPSVYNWSTQYTTGIYVLLLCCYYIFDTCNGQKNHFRNQIYGTEVHRKTFPQLPWLIIKNPTFIRCANGGTLLTSGWYRYARKIHYTADFFQSLSWALITGFQSPLPYFYPCFFFVVLVHRVSRDIKKCKAKYGADFDEYCRICPYLFIPYIF", "text": "FUNCTION: C-24(28) sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PubMed:8125337, PubMed:18310029). Erg4 catalyzes the last step of ergosterol biosynthesis by converting ergosta-5,7,22,24(28)-tetraen- 3beta-ol into ergosterol (PubMed:8125337, PubMed:18310029). 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. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. The lanosterol 14-alpha- demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C- 4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol. Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins. 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-desaturases erg31 and erg32 then catalyze 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:18310029) (Probable). In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (PubMed:8586261) (Probable). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERG4/ERG24 family."}
+{"protein": "NLFQFAKMINGKLGAFSVWNYISYGCYCGWGGQGTPKDATDRCCFVHDCCYGRVRGCNPKLAIYSYSFKNGNIVCGKNLGCLRDICECDRVAANCFHQNKNTYNKNYRFKSSSRCRQTSEQC", "text": "FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that shows presynaptic neurotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). FUNCTION: Heterodimer: postsynaptic neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
+{"protein": "MSTAGKVIKCRAAVLWEKNKPFSIEEVEVAPPKAYEVRIKIVATGICRSDDHVVNGSIITPLPAILGHEAGGIVESIGEGVTTVKPGDKVIPLFVPQCGKCRACKHPESNLCTHGDLGRAQGTLMDGTSRFTCKGKPIHHFLGVTTFSEYTVVSEISVTKIDAASPLEKVCLIGCGFSTGYGSAVKVGKVARGSICACVWSGRVGLSAIIGCKAAGAARIIAVDINKDKFAKAKELGATECVNPQDYDKPIYEVLQEMTDGGVDFSFEVIGRLDTKVSALMCCQESHGVSVIVGVPPNAQSLTIDPKVLLSGRSWKGAVFGGYKGKDDVPKLVADFMAKKFPLEPLITNVFPLAKINEGFDLLRAGKSIRTVLTF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily."}
+{"protein": "MPPVSASKAKRDAKKAEREAKKAAAGKTIRKLGRKKEAAAEESEVDAAAREIKMMKLQQDKDGLSDRVVTGVLSSLETSRDIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSALDYVVTEAQHELKRIEDLVEKTILEDGPESELLEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTRSELETNQMKQYNKQQEEIQHIKKFIASAGTYANLVKQAKSRQKILDKMEADGLVQPVVPDKVFSFRFPQVERLPPPVLAFDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQDQLDLTKSALEFVRDKYSNISQDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKTATRWDGSILQYKNKLAKNVVL", "text": "FUNCTION: ATPase that stimulates 40S and 60S ribosome biogenesis (PubMed:16260602). Also involved in ribosome-associated quality control (RQC) pathway, a pathway that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation: localizes to the ribosomal E-site and stimulates VMS1-dependent tRNA cleavage (PubMed:31189955). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the cytoplasm and the nucleus. SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily."}
+{"protein": "MEEKQILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSQVTWQSQGDTPCSCCIVNNSNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPLPQKVRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQPAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQGFDGIV", "text": "FUNCTION: Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate. SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
+{"protein": "MTDSAINKKSKRSIWIPLLVLITLAACATAGYSYWRMQQQPTTNAKAEPAPPPAPVFFALDTFTVNLGDADRVLYIGVTLRLKDEATRARLNEYLPEVRSRLLLLFSRQNAAELSTEAGKQKLIAAIKETLAAPLVAGQPKQVVTDVLYTAFILR", "text": "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": "MKIQDRSLLIFLVLGILKSDAFNTRVKRHAPIRFQRSTRQSVVHFEFLDQEYVVDLEPNHSTFHENFKVFTQDGPQIVPRDEYIGTVREPRAGRAVLTQLEENVYIGSLYFVDDTLHLEPSYPHQLSDDLGPVVGYFESDLDLNLDLSAMPVRNQVSFRRANPFLKHRRAIAIPSDRRKDVLNVKRNRCTLKLVADYSFYSIFGKNNTGIVTKFLVNMIARVNEIYTPINWDVGKEDDISGRGRFQNMGFSIKEIKVLDRPNASDSHYNSYSRIWEVERLLREFAFAEGSKDFCLVHLVTARTFREVATLGLAYVSYKKWDETAGGICSKQETFNGRVAYINVLLSTSFANSEQSTYPLITKEIDIVVSHEYGHAWGATHDPTIDSDDPDVEECSPNDQNGGKYLMSQYAQKGYDANNVLFSPCSRKLIRDVLIGKWESCFQEEMTSFCGNGIVEDGEECDNGVDTDNEFNCCDKFCRLAVGAKCSPLNHICCTPTCQFHNSTHVCLPGDSLLCKADAVCNGFSGECPSAPPVRDGQECLEGGECLNGVCLPFCEKMSIGKKSCICEDLELSCRLCCRDYNGTCAPVPGHVYLRDGVRCSKGSCRDRKCVNEVVDNVRNYFLITFQTTGGVLEFIKTHIVVIAIIFFTLIFVGIYKIVKYGENFTEKVTHKTAGGCRSVFVKADVN", "text": "FUNCTION: Metalloprotease (By similarity). Acts together with protease sup-17 to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision (PubMed:16197940). By modulating glp-1/Notch signaling, plays a role in germline development (PubMed:16197940). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MSQDLSLQKFGFIKRDTPRTVNLDPLQTGGLLTPEAREALLEWGDGYSVCDYCGGMLDQIKTPPIFDFVHKSLPSFIGMDHARVTNGARESKFAIMHAMTSPGDWIVMDGNAHYSSIVAAQRARLNVKLVPKTPAPDYKITPEAYAAAIEEVKQQSGKPPALALLTYPDGSYGNLADAKAITNLAHDFGVPIIINGAYAIGRMPFKGKDLGADFVAGSGHKSMAASGPVGVLGVNEQYAAKVLQKSPTHKNKEIEFLGCTARGATIMTMIASFPAVVERTKPESWEKEVSNARWFSEQMESIGMKQLGDKPHNHDLMFFEGTVFYDISQKTDRYFLYRELKEKSIHGIKPGLTKNFKLSTLGVGREKLGFVMDTLKDIIKKYDG", "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": "MSQQTTPAEQKSLQRKKPPFRADQVGSLLRSEPVKKARLQKAAGEMTAEQLRQIENDEIIRIVEKQKETGLNVVTDGEFRRAWWHFDFLENLDGVEPFTPEQGIQFHNVQTKARGIKVTGDIDFSTHPMLEDYSFLHSIAGDATPKMTIPSPNMLFFRGKLEKDEYKNDYQLFQHDVSKAYKKAIQAFYDRGCRYLQLDDTAWAVFLSEKGLKQIEAFGTTPDELRQLFAKSINDAIADRPDDLTVTMHICRGNFQSTWTAEGGYDAAAETIFDGLNLDGLFLEYDDSRSGGFEPLRYVKRSDLQLVLGLVTSKFGELENPDDVKRRIEEASRYVSLDQLCLSPQCGFASTEEGNKLTEEQQWAKLRHVVEIANDVWK", "text": "SIMILARITY: To B.subtilis YxjH."}
+{"protein": "MIRRWLTSRLYDAFLVCAFFVSAPRIFYKVFFHGKYIDSWKIRFGVQKPFVKGEGPLVWFHGASVGEVSLLAPLLNRWREEFPEWRFVVTTCSEAGVHTARRLYESLGATVFVLPLDLSCIIKSVVRKLAPDIVIFSEGDCWLHFLTESKRLGAKAFLINGKLSEHSCKRFSFLKRLGRNYFAPLDLLILQDELYKQRFMQIGISSDKIHVTGNMKTFIESSLATNRRDFWRAKLQISSQDRLIVLGSVHPKDVEVWAEVVSHFHNSSTKILWVPRHLEKLKEHAKLLEKAGILFGLWSQGASFRQYNSLIMDAMGVLKDIYSAADIAFVGGTFDPSVGGHNLLEPLQKEVPLMFGPYIYSQSVLAEKLREKEAGLSVNKETLLDVVTDLLQNEKNRQAYIEKGKSFLKQEENSFQQTWEILKSQITCMKI", "text": "FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of three 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the trisaccharide alpha-Kdo-(2->8)-alpha-Kdo- (2->4)-alpha-Kdo. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 30 subfamily."}
+{"protein": "MIRFKKTKLIASIAMALCLFSQPVISFSKDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKAGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN", "text": "FUNCTION: A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A conformation change leads to insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host cell membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation. SUBCELLULAR LOCATION: Secreted Host cell membrane; Multi-pass membrane protein Note=Secreted as soluble protein that then inserts into the host cell membrane and forms huge pores formed by transmembrane beta-strands. SIMILARITY: Belongs to the cholesterol-dependent cytolysin family."}
+{"protein": "MWHSVGLTLLVFVATLLIVLLLMVCGWYFVWHLFLSKFKFLRELVGDTGSQEGDHEPSGSETEEDTSSSPHRIRSARQRRAPADEGHRPLT", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMIM13 family."}
+{"protein": "MRSHLVKPGSVYDGIEPGELGESTESVQDRVRQLESRNSFLEEQCSQIESEKRYLENQKIKYEREIRKLQSELDRMKTSPLIIGTVIDVIKNDRIIVRSSNGPQFLVNVSQYIDEKKLLPGAKVALNQHTLAIAEVIPSTEEPFVAAMEVIESIEVDYDQIGGLDEQIQELQEAVELPLIEPERFARIGIEPPKGVLLYGLPGTGKTLLAKAVAHRTNATFIRVVGSELVQKYIGDGSKLVREIFEMARKKAPSIIFIDELDSIAARRLNETTGADREVQRTLMQLLAEMDGFDKRKNIRIIAATNRPDVLDPAILRPGRFDRLVHVPMPGIEARGKILKIHCGKMTLAGDIDFKKLAKVTEGMSGADLKAIATEAGMFAVRKDKALVEMEDFLEAVEKVSMAADTQKMMPGNLPETTMFV", "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": "MKKIVGALAVFVITYALFSAAGYLFPVDQEWYNSLKKPDWTPSGTAIGIIWAILFALISLSAAIVYAAFSFKGAKSFWFTLLINYVLNQAFSYFQFTQKNLLAASLDCLLVAITAIVLLIIAKKYSRAASYLLLPYFLWSAFATFLSFTINSMNL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TspO/BZRP family."}
+{"protein": "MGSDSTLSLPSSSPPCNNRSSVPPTFTTRIFSDVAGDIIVVVDGESFLLHKFPLVARSGKMRKMVRDLKDSSSMIELRDFPGGPSTFELTMKFCYGINFDITAFNVVSLRCAAGYLEMTEDYKEQNLIFRAENYLDQIVFRSFHESVLVLCSCETQEIAETYEIPDRCVEAIAMNACRKQLVSGLSEELKGRDCLEMWTEELSALGIDYYVQVVSAMARLSVRSESIVASLVHYAKTSLKGIIDRNCQEQRKIVEAMVNLLPNDEKGSYSLSIIPLGFLFGMLKVGTIIDIEISCRLELERRIGHQLETASLDDLLIPSVQNEDSMYDVDTVHRILTFFLERIEEEDDECGYDSDSTGQHSSLLKVGRIMDAYLVEIAPDPYLSLHKFTAIIETLPEHSRIVDDGIYRAIDMYLKAHPLLTEEERKKLCNFIDCKKLSQEASNHVAQNDRLPVQMVVRVLYTEQLRLKKALSGDSEEGSWVLPSGVQSRAVSPRDTYAALRRENRELKLEISRMRVRVSELEKEHNLMKHEMMEKSGNNGGTFLTSLSKGIGRIATFGGETRQKVNRKSRSVSERKSSRSGR", "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. SIMILARITY: Belongs to the NPH3 family."}
+{"protein": "MEIAVEREEENYLELRIQGEDHTLGNLIAGRLRSVKGVILATYYLPHPLKDELVIKIKTDGTISPREALNRAIEDVKVLGESFLDELEQV", "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": "MNTMNNMHLYADSLGIHPADHYPTMNEIETTDNTYPRYTSPPHPSILHHPQAPEPAPPRAQTAHPPAWALTSQSGYQMNEPSLSLTPEHRPAAGPPNGPNLNHDSDPRRPARRQQPCGVGTTRPLPGCPGQGQEPSRRRTTFTDSISNPDSTIRCWDHGCEGRKFSSVGNYRRHLREKNGQAKMHPCPDCGRVFTRSTARNFHRQSGTCGLIPSQLMLQMGMGMQLQVQMQPVSQHSLASGHPPAFNLAPPVLLEPLADWSEPSQMDLYAASGVVFD", "text": "FUNCTION: C2H2-type zinc-finger transcription factor that controls the expression of the nonribosomal peptide synthases inpA and inpB, as well as of the other inp cluster-associated genes (PubMed:20952652, PubMed:27294372). Mediates also the expression of the asperfuranone biosynthesis gene cluster by binding to the afoA promoter (PubMed:20952652). Probably recognizes the 5'-CT/C/AAAAGGAT/AT/GG/CA-3' motif in the promoters of teget genes (PubMed:20952652). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family."}
+{"protein": "MARDFKLIFSISILLLLLDCCYGGKVGVCYGRSADDLPTPSKVVQLIQQHNIKYVRIYDYNSQVLKAFGNTSIELMIGVPNSDLNAFSQSQSNVDTWLKNSVLPYYPTTKITYITVGAESTDDPHINASSFVVPAMQNVLTALRKVGLSRRIKVSTTLSLGILSRSFPPSAGAFNSSYAYFLRPMLEFLAENKSPFMIDLYPYYAYRDSPNNVSLDYVLFESSSEVIDPNTGLLYKNMFDAQVDALYYALTALNFRTIKIMVTETGWPTKGSPKEKAAASSDNAETYNSNIIRHVVTNQGTPAKPGEAMNVYIFSLFNENRKAGLDSERNWGLFYPDQTSVYQLDFTGKSNGFHSNSSGTNSSGSSNSWCIASSKASERDLKGALDWACGPGNVDCTAIQPSQPCFQPDTLVSHASFVFNSYFQQNRATDVACSFGGAGVKVNKDPSYDKCIYITAGGNKTKATNATALTSSASTPRGNELLQWILKLCLMISLFFSLQTMNSQAL", "text": "SUBCELLULAR LOCATION: Secreted, cell wall Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. SIMILARITY: Belongs to the glycosyl hydrolase 17 family."}
+{"protein": "MGEEFKPAIQEKRWDIGEEEKLLSLWDAEDLHKSTLDPDDPREIVVIDTPPPYPSGKWHVGGAAHYTQIDMIARYFRLKGYNVVAPFYADRNGLPVEVQVEKTYGVVAHEMARTTEGRERFLALCSEFLDKVESEIVQLWRRLGCGFDYWREGTDSPRYRSMTQATFIDLWRRGLIYEAERPVRWCPRCKTTLAEAEIEHKEDEDFIYYVKYRLEEDGRDLVVATTRPELLAGCAALAYHPEDERYKGLAGKTAIAPLYGHRVKIVEHPAVKKDFGTGLMMICSYGDEEDVRLFLELDLKPKVLIDENGVMNENAGPIAGLPVKEARRRIAEILEREGLLVKKERIVHSVPVCWRCKTPLQIIHRRELFLRQLDFKDAVKQAAAKMDFKPEMHRKKLYDWIDSIKMDWPISRERFYGTEIPLWTCEKCGAKLVPEPGRYYRPWAEEPPWDSCPRCGAPRRYLKGETRVFDTWFDSSISPLYVTRWMWDKRFYERASRNVLRPQGQDIIRTWLYYSILRVLQLTGKPAFRWVRITGLGLDPKGRPMHKSLGNVIDPEPIIAKYGGDAFRFWAAIAAKLGYDYRFDENKVKTGRNFATKLWNLARFVSSFPRPEGSPLEKATEVDKAFLALADEYLEAADKAYGELDVYEPANLIYELAWDIFASHYVELVKERSYNRSGLFTREEQEAAWATLHELLRRILVALSPIMPFVTDAIHRRLYGSSVHRQRWPDPLFTPEERRELAGKARLIVSVNKAVWNLKRSMGKKLYEPLDTVEVLVPSGIESARRDLEALHKAAIRTYTGAPPEGSEEAIPGSSVYYIAKKS", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily."}
+{"protein": "MRRHRQSGFTLLEVLLVAMLMGLVATAVTLSMGGARGDRELDKQARRFMATLQQAQEYSVMDGRLVGLRIEDHGWQFMQRAAKDRKWQALTGDKILGQVQLPDTMLLAIELEGFSWRTESDEKTERGRDEKERTPQVLIFPGGELSPFVLTLTQQDEDVRYLRTVKADEFGRLRLLQDEEEEE", "text": "FUNCTION: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP H family."}
+{"protein": "MSGVWVFNNGVIRLVENPNQSGGVSTQSHGRRNVLVYLPTGEAVSSYSSLEQILRSLGWERYFSGDSDLIQYHKRSSIDLISLPRDFSKFNSVYMYDIVVKNPNSFHVRDFN", "text": "FUNCTION: Modulates the competence to flowering of apical meristems. SIMILARITY: Belongs to the FPF1 family."}
+{"protein": "MSTANTVAIVIYSTYGHVVKLAEAEKAGIEKAGGKAVIYQFPETLSPEILEKMHAAPKPNYPVVTLDVLTQYDAFLFGYPTRYGTPPAQFRTFWDSTGGLWVQGALHGKYFGQFFSTGTLGGGQESTALTAMTSFVHHGMIFVPLGYKNTFSLMANVESIHGGSSWGAGSYAGADGSRNVSDDELEIARIQGETFFKTVFRK", "text": "FUNCTION: Unknown. Target of pap1 transcription factor. Confers brefeldin A resistance in S.pombe. SIMILARITY: Belongs to the WrbA family."}
+{"protein": "MTDLSKEELLQRIQQLENENEQLKAVALQSLHTLRYNQSCSHSLQQSNSVNEEPLSLEEFKRYGRQMIVPKFGSLNAQKKLRSSKILVVGAGGLGSPALQYLCAAGIGEIGIIDDDTVDVSNLHRQIIHKSSLVGILKCESAKQSMKDLNPFVKVETYPERLTVFNAFEIIDKYDLVLDCTDHPAVRYLINDVCVLLGKTIVSGSGLRAEGQLTILNYDQVGPCYRCFYPQAPEPSSITSCSDGGVIGPAIGLVGVAMAMETIKLLTGTYTRENFTPFLASYSAYPLQQMKTFKMRPKQSSCKVCGDRPEITKEMVENGSIDYVSFCGHIDEKNPPLQKKYRITVQEYSSLLNSQSREHTLIDVRPKEQFEITNLPGSINLDWPLVFSKCDNDKIDLLLPQDITKADQLYVICRFGNDSQLATAKLIEAGYLNAKDIIGGLNKWSEDIDAAFPKY", "text": "FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. 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: In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily."}
+{"protein": "MAMQAHYQAEATEEENFGPQAITRLEQCGINANDVKKLEDAGFHTVEAVAYAPKKELLNIKGISEAKAEKILAEAAKLVPMGFTTATEFHQRRSEIIQIGTGSKELDKLLQGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMAESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD", "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": "MASSSNSYNSPCAACKFLRRKCMPGCIFAPYFPPEEPHKFANVHKIFGASNVTKLLNELLPHQREDAVNSLAYEAEARVRDPVYGCVGAISYLQRQVHRLQKELDAANADLAHYGLSTSAAGAPGNVVDLVFQPQPLPSQQLPPLNPVYRLSGASPVMNQMPRGTGGSYGTFLPWNNGHDQQGGNM", "text": "FUNCTION: Not known; ectopic expression of LOB leads to alterations in the size and shape of leaves and floral organs and causes male and female sterility. SIMILARITY: Belongs to the LOB domain-containing protein family."}
+{"protein": "MERAVPLAVPLGQTEVFQALQRLHMTIFSQSVSPCGKFLAAGNNYGQIAIFSLSSALSSEAKEESKKPVVTFQAHDGPVYSMVSTDRHLLSAGDGEVKAWLWAEMLKKGCKELWRRQPPYRTSLEVPEINALLLVPKENSLILAGGDCQLHTMDLETGTFTRVLRGHTDYIHCLALRERSPEVLSGGEDGAVRLWDLRTAKEVQTIEVYKHEECSRPHNGRWIGCLATDSDWMVCGGGPALTLWHLRSSTPTTIFPIRAPQKHVTFYQDLILSAGQGRCVNQWQLSGELKAQVPGSSPGLLSLSLNQQPAAPECKVLTAAGNSCRVDVFTNLGYRAFSLSF", "text": "FUNCTION: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap- dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Plays a role in apoptosis negative control involved in brain development. SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the WD repeat THOC6 family."}
+{"protein": "MSDINDPNSISLPVGSSCTSRGASTETFTTSRSTTLFSSQQESKDEGNVELRESITLPTINHRVLLSLKESAKVIGTKGSTIQNVREINHVKIGLSEKQLGCSDRVLSCAGRIINVAHSLGQIVSVLKEGSTVSSAEKYAFHFLNPILPPPTRDEFQDLTLDEINKIGTSRLMVTNSQLSSIIGKGGARIKSLKERHRVKIVASRDFLPDSDERILEIQGLPNAITNVLLQISKILLNELDITFASERRYYPHLRSSSPSNAVSLAASTSGVQTGASNYLNNEFKATLKIPESYVGAIAGRRGNRIANLRKFTKTKIIVEKKIDKTVIDVDPDNRTFIILGDHFKNVKLAESMLLKNLDVEIEKRKSRLAKK", "text": "FUNCTION: RNA-binding protein involved in the correct localization of transcripts in the cell. RNA localization is a widespread mechanism for achieving localized protein synthesis. Involved in structural and functional organization of telomeric chromatin and regulates silencing at the HMR locus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, P-body Nucleus Chromosome, telomere. SIMILARITY: Belongs to the HEK2 family."}
+{"protein": "MLNRFSYSSNAWHNLRVDGPDADGIAVIVLARSQSRNALTLPMLTDMVQLLSAMDADDSVKCIVFTGEGPFFCSGVDLTEGFGEIGKTRDTHRDAGGKLALAIHNCRKPTIAAINGTAVGVGITMTLPMSIRIAAKTAKISFPFVRRGIVADAASSFYLPRLVGYGRALHLFTTGALYPAESGLLHGLFSETVNPASSTLPRALEVARDIAVNASQVGVYLTRDLVYRSPRSPEQAHLLESAALYTRYQSRDFEEGVKSFLEKRKPRFQDTMREQSSEGVLERGDCVVGLASKPKL", "text": "FUNCTION: Enoyl-CoA hydratase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype (PubMed:10975654, PubMed:10432635, PubMed:20348386). AK- toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA) (PubMed:22846083). On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment (PubMed:22846083). The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety (PubMed:10432635, PubMed:10975654, PubMed:22846083). Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes (PubMed:20348386). The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated (PubMed:10432635, PubMed:10975654, PubMed:22846083). The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK- toxin, probably via the catalysis of a side reaction of EDA or its precursor (PubMed:24611558). SUBCELLULAR LOCATION: Peroxisome Note=The peroxisomal location requires the C-terminal tripeptide peroxisomal targeting signal. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
+{"protein": "MVCDTLVYHPSVTRFVKFLDGSAGREKVLRLLQYLARFLAVQNSSLLARQLQAQFTTVRKFLRFLKPLNHLQAAAKFYDNKLASDNVVRVCNVLKNIFFAAYLSLDQVNLLRILKVIPVTVLTGKKIPRWSNWCWLFGLLSGLAMDLRKIQTSHAQIAAFVKAKSQSQGDEHEDHKKVLGKAYQDRYTALRRLFWDAADSFIVLNNLGYLSSNEEYVALSGVVTSILGMQDMWKAT", "text": "FUNCTION: Involved in peroxisomal proliferation. Promotes peroxisome division and biogenesis. SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the peroxin-11 family."}
+{"protein": "MKINKNNYFKIIIFIIYVIINLINASDNVKLSNCGQARAEPTFKQSENGGQCQLPPPSIGTAALSLSAFNGGARCGQCYELTGPLGKTVVMVTDGCNSGEACTQKDLFNFIISNKDFDKIGNSSSYVNIYSLGYQEVSCGFLGNIKIKFGGSLGHNGKVDYSYYFTVSFSNFNIGIKQVQILGTGMVSYMKLKRSLGGFTWNQESGGSKLQFPATLVLTGVDGQIISYKFRQPPANIAIDMKKQFIPQVGLLSSKFNQSEICGMGNVPEYIYEDSLTFGWIVSNSWRFNVFNLSSQDTDDNPTLGESVIKMDLAANGGLAFTREGGFQTKYLESLKVMIKVLPPTNSLQCFFGASGIYVIPGPLGGDWQEISIPISVLKPQKVEYSLSFYNNQGQSITMWIDNIKWIFSPEAPPTPLIITDPTVTPPPLPQSIVTAAAGVVGLNSIGITSNKGGVANLVDGSSNDDDGTGGTGGGASNKVGKRVDGEDGDNFMGGNNAFSYYNDDNSSNILLFSFNITLTFLLLSLIINILLLLF", "text": "FUNCTION: May serve to lubricate the movement of the cellulose microfibrils during cell growth and wall extension and/or may serve to maintain the fluid state of the slug cell wall. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the expansin family. Expansin A subfamily."}
+{"protein": "MPRSSRWVNQRATSKIKKFILFLGVAFVFYLYRYPSSPSTVEQSSTSIYNISVKDIEGKDVSLSKFTGKVLLIVNVASKCGLTHGNYKEMNILYAKYKTQGFEILAFPCNQFGSQEPGSNMEIKETVCNIFKAEFPIFDKIEVNGKNTCPLYNFLKEQKGGLFGDAIKWNFAKFLVDRQGNVVDRYAPTTSPLEIEKDIVKLLASA", "text": "FUNCTION: May constitute a glutathione peroxidase-like protective system against oxidative stresses. Involved positively in abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, seed germination and inhibition of vegetative growth. Oxidizes and represses target proteins (e.g. the phosphatase activity of ABI1 and ABI2) when oxidized by H(2)O(2), probably after ABA signaling. Modulates the calcium channel activity in guard cells in response to ABA or H(2)O(2). Confers tolerance to drought stress, by enhancing the ABA-dependent stomatal closure. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the glutathione peroxidase family."}
+{"protein": "MAMPRNLPGQAAHDEADQEILRLDGIRKRFPGVLALDGIRLDLRRGEVHAVCGENGAGKSTLMKIISGQYLPDEGAVHYRGAPVRFRSASEAQAAGISIIHQELNLVPHLSVAENLFLAREPRRGPFVDTKRMNAEAARCIARIGLNVAPTTKVGVLSIAQQQMVEIAKALSHDARVLIMDEPTSSLTEAETVQLFRIIEELRADGVAILYISHRLDEMAQIVDRVTVLRDGRHISTDDFADVSIDDIVARMVGRTLDDAYPSRQSVPTDDVLLDVRDLRRDGVFGPVSFALRRGEILGFAGLMGAGRTEIARAIFGADRPDGGTIALHGRPVTIRSPREAIRHGIAYLSEDRKKEGLALPMPVAANLTLANVRGIASRFGFLRFDDEIDVARRYVQDLAIRTPSVHQRVRNLSGGNQQKVVIGKWLYRGSKILFFDEPTRGIDVGAKFAIYGLMDRLAADGVGVVLISSELPELLGMTDRIAVFHEGRMTAILDTKHTSQEEIMHYASGRSHA", "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 inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Carbohydrate importer 2 (CUT2) (TC 3.A.1.2) family."}
+{"protein": "MRKGQGYSYSVIASVLVLLCVVVSRIECSSQVHALSRLYLSKRGVGGSSTMDTSHFKAVKDLKPSSLRSAANQEGLRKRDLIRRLPGQPPVSFDQYGGYVTVNESAGRSFFYYFVEASKSKDSSPLLLWLNGGPGCSSLAYGALQELGPFRVHSDGKTLFRNRYAWNNAANVLFLESPAGVGFSYTNTTSDLEKHGDRNTAADNYIFLVNWLERFPEYKGRDLYIAGESYAGHYVPQLAHTILLHHRSFFNLKGILIGNAVINDETDLMGMYDFFESHALISEDSLARLKSNCDLKTESASVMTEECAVVSDQIDMDTYYLDIYNIYAPLCLNSTLTRRPKRGTTIREFDPCSDHYVQAYLNRPEVQAALHANATKLPYEWQPCSSVIKKWNDSPTTVIPLIKELMGQGVRVWVFSGDTDGRIPVTSTKYSLKKMNLTAKTAWHPWYLGGEVGGYTEEYKGKLTFATVRGAGHQVPSFQPKRSLSLFIHFLNDTPLPDTSRY", "text": "FUNCTION: Probable carboxypeptidase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S10 family."}
+{"protein": "MGVIQTLDGLMNNPTPEGRVDDILRPEGDNPLLEKGFVTTSVDALLNWARTGSMWPMTFGLACCAVEMMHAGAARLDLDRYGVVFRPSPRQSDVMIVAGTLVNKMAPALRKVYDQMPDPKWVISMGSCANGGGYYHYSYSVVRGCDRVVPVDVYVPGCPPTAEALVYGILQLQKKIWRTQTIAR", "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. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
+{"protein": "MERPLCSHLCSCLAVLALLSPLSLAQYDSWPHYPEYFQQPAPEYHQPQAPANVAKIQLRLAGQKRKHSEGRVEVYYDGQWGTVCDDDFSIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNLHCTGNEATLAACTSNGWGVTDCKHTEDVGVVCSDKRIPGFKFDNSLINQIENLNIQVEDIRIRAILSTYRKRTPVTEGYVEVKEGKTWKQICDKHWTAKNSRVICGMFGFPGERTYNAKVYKMFASRRKQRYWPFSMDCTGTEAHISSCKLGPQVSLDPMKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYKPEQPLVRLRGGAYIGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEAVTGSRLGQGIGPIHLNEIQCTGNEKSIIDCKFNTESQGCNHEEDAGVRCNTPAMGLQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGQNWGIVEAMVVCRQLGLGFASNAFQETWYWHGDVNSNKVVMSGVKCSGTELSLAHCRHDGEDVACPQGGVQYGAGVACSETAPDLVLNAEMVQQTTYLEDRPMFMLQCAMEENCLSASAAQTNPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKNYECANFGDQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNFEVAESDYSNNIMKCRSRYDGHRIWMYNCHIGGSFSEETEKKFGHFSGLLNNQLSPQ", "text": "FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. 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). 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. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. 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. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. 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": "MNLFLVLFVFSFSVSQFFAVEAGGRKHKHQEVCIGSDGKGHQLNQFWYDNGNCRRFYCYKDEDGLVIEQTTNCELAVAENDCRIKPGKAGRYPDCCPSVECPQESKAS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-16 family."}
+{"protein": "MPEGPEIRRAADHLEAAIKGKLLTDVWFAFAQLKPYESQLTGQMVTRIETRGKALLTHFSNGLTLYSHNQLYGVWRVIDTGEIPHTTRILRVRLQTADKTILLYSASDIEMLTAEQLTTHPFLQRVGPDVLDARLTPEEVKARLLSPRFRNRQFSGLLLDQAFLAGLGNYLRVEILWQSELTGQHKAKDLSEAQLNTLSHALLDIPRLSYATRGQTDENKHHGAQFRFKVFHRDGEACERCGGIIEKTTLSSRPFYWCPHCQK", "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": "MLKPSDKWSWYFSDSEGYLMLNLGDDMLFRTNLSRNLLVDCAFIENPFTVDDASDFQLYKEHIACLPLSEPRKAELALYCVAAKRFHKPVQPKSWFFDVQGTGYTPQQGQLISLRNSLNSGIFIALEVGENATLCAYSDLVSFALNGSKTLEFGQVIKVMHDRMSDVNTLLYTPQMAMVS", "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": "FGFHQQMLNYILSPFFYYQPDPWLTHKWKDEKRNMRKHSISFKGLIRAVLFSQTLIKSALAKRVRCTVLYATETGKSKTLAKKLNTMMNYAFSSKVVCMEDYNFSELEKESLLFVVTSTFGNGDCPGNGESFKKQLLSLNNLRNQVRYSVFGLGSRMYPHFCAF", "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 COX2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the NOS family."}
+{"protein": "MEKMLLKSTTRHVRIFTAEVVDEELKFHPNKLTLDLDPDNEFIWNEDSLNKINEKFNELIKERAGKDLDDYELRKIGSEIEGLIKFLLQNGQLSYNPDCRVMNYSMGLPKTNEVL", "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 NdhM subunit family."}
+{"protein": "MEYQSGKRVLSLSLGLIGLFSASAWASDSRTVSEPKTPSSCTTLKADSSTATSTIQKALNNCDQGKAVRLSAGSTSVFLSGPLSLPSGVSLLIDKGVTLRAVNNAKSFENAPSSCGVVDKNGKGCDAFITAVSTTNSGIYGPGTIDGQGGVKLQDKKVSWWELAADAKVKKLKQNTPRLIQINKSKNFTLYNVSLINSPNFHVVFSDGDGFTAWKTTIKTPSTARNTDGIDPMSSKNITIAYSNIATGDDNVAIKAYKGRAETRNISILHNDFGTGHGMSIGSETMGVYNVTVDDLKMNGTTNGLRIKSDKSAAGVVNGVRYSNVVMKNVAKPIVIDTVYEKKEGSNVPDWSDITFKDVTSETKGVVVLNGENAKKPIEVTMKNVKLTSDSTWQIKNVNVKK", "text": "FUNCTION: Involved in maceration and soft-rotting of plant tissue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
+{"protein": "MVALPRQGIIILTYVLAALELTCLFMQFSIIPYLSRTLGLDSVSFGYLQTTFGVLQLLGGPVFGRFADQRGARAALTLSFLAASALYLLLVASCSPALPGVFLLFASRLPAALMHTLPAAQMVITDLTAPTKRPTALSRLGLCFGIGVIFGSLLGGTLSTAYGIQCPAFLAFVVTLLGAVLSFTCIPVTTKEASVQSAHQGGTSVFDLKAISRLLLLPRVLPVFLVKVISGFPSGLFMVMFSIISMDFFQLEAAQAGYLMSFFGILQMMIQGLVIGRLSTRFPEEALLRSSVLVFAVVGLGMALMSNVFHFCLLLPGLVFSLCALNIVTDSMLTKAVSASDTGTMLGLCASVHPLTRTVGPTLGGLLYRSYGVSILGHVQLMVNLLVLLVLWKKPLSQKGDKAR", "text": "FUNCTION: May act as a transporter of organic cations based on a proton efflux antiport mechanism. May play a role in the transport of chloroquine and quinidine-related compounds in kidney (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=Localized at the apical membrane surface of renal proximal tubules. SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family."}
+{"protein": "MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQNRQTGAPDAGQE", "text": "FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
+{"protein": "MNAKTDFSGYEVGYDIPALPGMDESEIQTPCLILDLDALERNIRKMGDYAKAHGMRHRSHGKMHKSVDVQKLQESLGGSVGVCCQKVSEAEAFARGGIKDVLVTNEVREPAKIDRLARLPKTGATVTVCVDDVQNIADLSAAAQKHGTELGIFVEIDCGAGRCGVTTKEAVVEIAKAAAAAPNLTFKGIQAYQGRDAAHGQLRGPQGQAGRRHCPGERGRGRAGGRGLAPEFVSGGGTGSYYFESNSGIYNELQCGSYAFMDADYGRIHDAEGKRIDQGEWENALFILTSVMSHAKPHLAVVDAGLKAQSVDSGLPFVYGRDDVKYIKCSDEHGVVEDKDGVLKVNDKLRLVPGHCDPTCNVHDWYVGVRNGKVETVWPVSARGKGY", "text": "FUNCTION: Catalyzes the condensation of glyoxylate and glycine into (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate). Functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC) (By similarity). In vitro catalyzes the cleavage of both D-erythro- and D-threo-3-hydroxyaspartate to glycine and glyoxylate. Also acts on D- threonine, D-3-phenylserine and D-3-3,4-methylenedioxyphenylserine (PubMed:12835921). SIMILARITY: Belongs to the DSD1 family."}
+{"protein": "MAPWPHGNGSLASWPDAPTLTPNTANTSGLPGVPWAVALAGALLALAVLATVGGNLLVIVAIARTPRLQTMTNVFVTSLATADLVVGLLVVPPGATLALTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRRARAAVVLVWVVSAAVSFAPIMSKWWRVGADAEAQRCHSNPHCCAFASNIPYALLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRGELGRFPPGESPPAASRSMSPAPAGPCASPAGVPSYGRRPARLLPLREHRALRTLGLIMGTFSLCWLPFFVANVVRALGGPSLVPSPAFLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCRLEERHAAASGAGETSDAPAALTRPAESGLPGGIS", "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 (By similarity). 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": "MATLTNGQVDAAVHGGAASTNGLVNGISHTHSPASCATIPMKDHDAIKLFIGQIPRNLDEKDLRPLFEEFGKIYELTVLKDRFTGMHKGCAFLTYCARESALKAQTALHEQKTLPGMNRPIQVKPADSESRGEDRKLFVGMLNKQQCEDDVRRLFESFGSIEECTILRGPDGNSKGCAFVKYSTHAEAQAAISALHGSQTMPGASSSLVVKFADTDKERTIRRMQQMAGQMGIFNPMALQFGAYGAYAQVQQQAALMASVGQGGYLSPMAAFAAAQMQHMATINGLPGAPMTPTSGGSTPPGITAPTVTSIPSPISVNGFTGLPPPQANGQAPAEAMFTNGIHPYPVLQEVVFREDSEKGGLGVAQRSCFGVQGSCFLSSLSEAQSPTAADPLQQAYAGVQQYAAFPAAYGQISQAFPQPPPIIPQQQREGPEGCNLFIYHLPQEFGDGELMQMFLPFGNVISSKVFVDRATNQSKCFGFVSFDNPGSAQAAIQSMNGFQIGMKRLKVQLKRPKDANRPY", "text": "FUNCTION: RNA-binding protein that may be implicated in the regulation of pre-mRNA alternative splicing. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the CELF/BRUNOL family."}
+{"protein": "MYVMKVVGKTTTTHFTFESLEKIRFGEYVIAKNVDGRDVLGVIKNVVADVEKFVGEVKVIGVLDGNKIIPNRTPILPNSEVRLCDDEILNNIYLTPDGLNIGHLLTRDNVRVYLDTNKLVSRHFAILSITGGGKSNTASVLCRELAKKNGTVIMIDPHGEYISLYHEDMEGKIKVINPIINPVLLAPSEFANLIGIGDNEIEKRVYVEFAYHTVKHECPDAKGIEFIEKIENLLYEWSKIASVGWEIKYYNPLRRNYDRRKLEKEDFVILMSLIDTISKFKLDYALNIGDRDVIEEFEIGKINIVNLSGLEIPQMVTFVGFIAKHLLLKRITYLKSLKDVYSINEEIRRVAQSNLNIIESHYKVVTKPVLLIVEEAHIFIPVNEQNSASLWLGKIAREGRKFGVGLGLVSQRPKQLHPDVLSQTNTKIILKIVEPEDQKYIQRASEELGEDLVKDLASLGIGEAVIVGAAISLPSIVKIDKFDGVYGGKDINIVGEWMGLDDW", "text": "FUNCTION: Involved in DNA double-strand break (DSB) repair (By similarity). 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 (By similarity). SIMILARITY: Belongs to the HerA family."}
+{"protein": "MSRRPDLLRGSVVATVAATFLLFIFPPNVESTVEKQALFRFKNRLDDSHNILQSWKPSDSPCVFRGITCDPLSGEVIGISLGNVNLSGTISPSISALTKLSTLSLPSNFISGRIPPEIVNCKNLKVLNLTSNRLSGTIPNLSPLKSLEILDISGNFLNGEFQSWIGNMNQLVSLGLGNNHYEEGIIPESIGGLKKLTWLFLARSNLTGKIPNSIFDLNALDTFDIANNAISDDFPILISRLVNLTKIELFNNSLTGKIPPEIKNLTRLREFDISSNQLSGVLPEELGVLKELRVFHCHENNFTGEFPSGFGDLSHLTSLSIYRNNFSGEFPVNIGRFSPLDTVDISENEFTGPFPRFLCQNKKLQFLLALQNEFSGEIPRSYGECKSLLRLRINNNRLSGQVVEGFWSLPLAKMIDLSDNELTGEVSPQIGLSTELSQLILQNNRFSGKIPRELGRLTNIERIYLSNNNLSGEIPMEVGDLKELSSLHLENNSLTGFIPKELKNCVKLVDLNLAKNFLTGEIPNSLSQIASLNSLDFSGNRLTGEIPASLVKLKLSFIDLSGNQLSGRIPPDLLAVGGSTAFSRNEKLCVDKENAKTNQNLGLSICSGYQNVKRNSSLDGTLLFLALAIVVVVLVSGLFALRYRVVKIRELDSENRDINKADAKWKIASFHQMELDVDEICRLDEDHVIGSGSAGKVYRVDLKKGGGTVAVKWLKRGGGEEGDGTEVSVAEMEILGKIRHRNVLKLYACLVGRGSRYLVFEFMENGNLYQALGNNIKGGLPELDWLKRYKIAVGAAKGIAYLHHDCCPPIIHRDIKSSNILLDGDYESKIADFGVAKVADKGYEWSCVAGTHGYMAPELAYSFKATEKSDVYSFGVVLLELVTGLRPMEDEFGEGKDIVDYVYSQIQQDPRNLQNVLDKQVLSTYIEESMIRVLKMGLLCTTKLPNLRPSMREVVRKLDDADPCVSNSQDTTGKITV", "text": "FUNCTION: Receptor kinase involved in the perception of C-terminally encoded plant signaling peptide (CEP) and subsequent regulation of root and shoot development. Together with CEPR1, mediates systemic nitrogen (N)-demand signaling upon the perception of root-derived peptides (e.g. CEP1) via the up-regulation of genes involved in N uptake and assimilation pathways. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MPEPGPRMNGFSLGELCWLFCCPPCPSRIAAKLAFLPPEPTYTVLAPEQRAPAPAATPAPAPAAQPAPAEEGAGPGACSLHLSERADWQYSQRELDAVEVFFSRTARDNRLGCMFVRCAPSSRYTLLFSHGNAVDLGQMCSFYIGLGSRINCNIFSYDYSGYGVSSGKPSEKNLYADIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYECAAVILHSPLMSGLRVAFPDTRKTYCFDAFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDIELYAQYLERLKQFISHELPNS", "text": "FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards DLG4/PSD95. FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards DLG4/PSD95. SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Cell projection, dendritic spine Postsynaptic density membrane. 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": "PAKEAYRLAAATFRDAQVKHLNSQPWQTIKNTLTHNGHQYTNMQLPAADMKIGTQDIFPSAYQGKGVCSWDTKNIHHANNLWMSTVSAHEDGKDKTLFCGIRHGVLSPYDVKDPLLRQTGAENEAKEVLTAALFSKPELLTRALEGEAVNLKLVSVGLLTASNVFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGELQTVKIKPEIAAFNVGVNELALKLGFGLKTSDSYNVEALHQLLGNDLRPEAKPGGWVGDWLAQYPDNYEVVNILARQIKDIWKNNLHHKDGGEPYKLAQRLAMLANEIDAVPAWNCKSGKDRTGMMDSEIKREIICLHQTHTLNAPGSLPDRSGQEIFQKVLLNSGNLEIQKQNTGGAGNKVMKNLSPEVLNLSYQKRVGDENIWQSVKGISSLITS", "text": "FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicles, which are essential to create a favorable environment where Salmonella can replicate and avoid immune defenses of the host cell (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted via the type III secretion system 1 (SPI-1 TTSS). SIMILARITY: Belongs to the phosphatase IpgD/SopB family."}
+{"protein": "MPAYGLTYRFRFPVALRRRRRSRFSGGSLYARRRRRRVRVKGGFLPALIPLGAALISAIPGIASVAMQASQLKK", "text": "FUNCTION: The role of the precursor might be to condense the viral prochromatin for encapsidation by virtue of the two basic domains. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the adenoviridae pX family."}
+{"protein": "MALVSAVPLDSRLCLCRTLFGLTHELKAIRRTIPNLGMCRGGKSIAPSMSMSSTTFVSSEDGVPRRIGGHHSNLWDDDSIDSLSTSYEAPSYRERADRLIGEVKDMFHLISVEDGVSTSPLNDLHHRLWMVDSVERLGIDRHFKNETNAALDHVYSYWTEKGIGRGRESGATDLNSTALGLRTLRLHGYMVSSHVLDHFKNEKGQFACSAIQTDGEIRDVLNLFRASLIAFPGEKIMEEAEMFSTMFLKDALQKIPPSGLSQEIEYLLEFGWHTNLPRMETRMYIDVFGEDTTFETPYLIRERLLELAKLEFNIFHSLVKRELQSLSRWWKDYGFPEITFSRHRHVEYYTLAACIANDPKHSAFRLGFAKICHMVTILDDIYDTFGTMEELELLTAAFKRWDPSSIECLPDYMKGVYMAVYDNINETAREAQKIQGWDIVSYARKSWEALFDAHMQEARWISSGYLPTFEEYLENGKVSFGSRLTTLEPMLTLGFPLSPRILQEIDFPSNFNELICAILRLRGDTQCYKADMARGEEASSVSCYMKDHPGITEEDAVNQINALVNNLTKELNWELLRPDSGVPISYKKFYFDIWRVFHYGYKYRDGFSVASIEIKNLVTRTVVETVPL", "text": "FUNCTION: Monoterpene 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. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
+{"protein": "MTGVTVCCGTVNSIKALWETRIKKTKDDLKKEKEQKDRRAVGRLTGAWEDRIILAKLKEKIVTEEGRVILRIEKEEWKTLPPALVQLSQIQEWQLHRIGLQRIPRFISSFQSLIVLDLSRNSVTEIPKEIGKLTRLRELLLSYNRVSYVPEELGCCENLEKLELAMNRDLDELPTQLSNLKKLSHLDLSMNQFTTIPDCVVNLPSLEWLDMGSNILETLPDNIHRMEKLHTLWLPRNELEYLPDNISRMKSLDTLVLSKNKLRDIPPLMEGMSNLRFVNFRDNPLTYDVTLPDLNEDVEEEENDREMFGREFMNFYIQEARKRGSQNFTSVLNVMLEGVSETA", "text": "FUNCTION: Component of the sarcomeric M-band which plays a role in myocyte response to biomechanical stress (By similarity). May regulate expression of other M-band proteins via an SRF-dependent pathway (By similarity). Important for normal contractile function in heart (PubMed:20847312). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line."}
+{"protein": "MLVAAGQFAVTSVWEKNAEICASLMAQAAENDASLFALPEALLARDDHDADLSVKSAQLLEGEFLGLYGEKVNVT", "text": "FUNCTION: Pseudogene resulting from a nucleotide deletion that introduces a premature stop codon at position 66. This is the N- terminal fragment. The intact protein (AC A0A140NCB4) hydrolyzes deaminated glutathione (dGSH, 2-oxoglutaramate) to alpha-ketoglutarate (alpha-KG) and cysteinylglycine, has less activity against alpha- ketoglutaramate (a-KGM) and no activity on glutathione or L-glutamine (By similarity). May function as a metabolite repair enzyme (By similarity). SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family."}
+{"protein": "MGAFIAKMLLPTISSLVFVPAASVAAKRGFHMEAMVYFFTMFFTAIYHACDGPGLSILCFMKYDILEYFSVYGTAISMWVTLLALGDFDEPKRSSLTMFGVLTAAVRIYQDRLGYGIYSGPIGTAVFMITVKWLQKMKEKKGLYPDKSVYTQQVGPGCCFGALALMLRFYFEEWDYAYVHSFYHVSLAMSFILLLPKKNRYAGTGRNAAKLNCYTLCCCV", "text": "FUNCTION: Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers (PubMed:25078621, PubMed:28681861, PubMed:28161523, PubMed:30016436). Actively participates in the membrane fusion reaction by mediating the mixing of cell membrane lipids (hemifusion) upstream of mymx (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes on the cell surface of myoblasts. SIMILARITY: Belongs to the TMEM8 family."}
+{"protein": "MDVPEPQPDPDGGDGPGHEPGGSPQDELDFSILFDYDYLNPIEEEPIAHKAISSPSGLAYPDDVLDYGLKPCNPLASLSGEPPGRFGEPDSIGFQNFLSPVKPAGASGPSPRIEITPSHELMQAGGALRGRDAGLSPEQPALALAGVAASPRFTLPVPGYEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNAGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVAPLPAASPQRSRSPSPQPSPHVALQDDSIPAGYPPTAGSAVLMDALNTLATDSPCGIPSKIWKTSPDPTPVSTAPSKAGLARHIYPTVEFLGPCEQEERRNSAPESILLVPPTWPKQLVPAIPICSIPVTASLPPLEWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQRSAHELPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPSDEYEPSLICSPAHGGLGSQPYYPQHPMLAESPSCLVATMAPCQQFRSGLSSPDARYQQQSPAAALYQRSKSLSPGLLGYQQPSLLAAPLGLADAHRSVLVHAGSQGQGQGSTLPHTSSASQQASPVIHYSPTNQQLRGGGHQEFQHIMYCENFGPSSARPGPPPINQGQRLSPGAYPTVIQQQTAPSQRAAKNGPSDQKEALPTGVTVKQEQNLDQTYLDDVNEIIRKEFSGPPSRNQT", "text": "FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway (By similarity). Is involved in the negative regulation of chondrogenesis (PubMed:10620601). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin- mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription."}
+{"protein": "MNRIFGKSKPKVPPPTLTDCITNVDGRAESIEKKISRLDAELIKYKDQMKKMREGPSKNMVKQKALRVLKQKRMYEQQRDNLNQQSFNMEQANYTIQTLKDTKTTVDAMKVGAKEMKKAYKQVKIDQIEDLQDQLEDMMENANEIQEALSRSYGTPEIDEDDLEAELDALGDELLLDDDTSYLDEAASAPAIPEGVPNDSKNKDGVLVDEFGLPQIPAT", "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": "MNDFSFEDKGLISRSGFGSRHVRRVVKALALIFSLLILYLTISNVSDSPPKRDSLSLDDIVLQKYKPSYKQVNWIDSQGLKDTFLVKYGDLINIQDPYNLNKTLFSVSDLVYNGIQLDYDSYSISFDAKYVLVSVNKSQRWRHSSFAQYYLYNTETKDVNMLGQDNEHWTISLAEWSPTGHQLSFVYNNDLYVRKNDGNVQRLTYDGTVDVFNGLTDWIYEEEVLSSPSTIWWSPDSDKIAFLKLNESEIPTYHYPLYTAELDPSLPEFDYNKDMAIKYPKPGNPNPSVSLFVADLNSNASSNFSLWHNEPLAEPVVQNVLWVNTSSVLVQFTNRNSTCITARLLDTELKSIHTVKTECLEEGWYEVQQSAKMFPLNNSLVWENWSDGYFDILALDDYNHLAFIPFNGSSPIYLTSGAWDVTDGPIHIDGDFGNVYFLATLKDSTERHLYYVSLDTLEIYGITDNGEDEGYYSTSFSPFGDFYVLNYHGPDVPWQELRSTKDKDYCLSLETNSRLKQQLSSITLPSVEYGKLTFNDTTFNFMERRPRNFDVNKKYPVLFFAYGGPGSQQVAKLFRVDFQAYLASHPDFEFIVVTLDGRGTGFNGNAFRYSVSRHLGEWESYDQGQAGKFWADLPFVDENHVGIWGWSYGGYLTLKTLETQDVFSYGMAVAPVTDWRLYDSVYTERYMDLPQYNKEGYKNSQIHDYEKFKQLKRFFVAHGTGDDNVHFQHSMHLMDGLNLANCYNYDMAVFPDSAHSISYHNASLSIYHRLSEWIGDALGRIDPSTGVRQHRWD", "text": "SUBCELLULAR LOCATION: Vacuole membrane; Single-pass type II membrane protein Note=Lysosome-like vacuoles. SIMILARITY: Belongs to the peptidase S9B family."}
+{"protein": "MEIRQHEWLSASPHEGFEQMRLKSRPKEPSPSLTRVGANFYSSVKQQDYSASVWLRRKDKLEHSQQKCIVIFALVCCFAILVALIFSAVDIMGEDEDGLSEKNCQNKCRIALVENIPEGLNYSENAPFHLSLFQGWMNLLNMAKKSVDIVSSHWDLNHTHPSACQGQRLFEKLLQLTSQNIEIKLVSDVTADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKETDPLTFNFISSLKAICTEIANCSLKVKFFDLERENACATKEQKNHTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTGLVINQADVRNNRSIIKQLKDVFERDWYSPYAKTLQPTKQPNCSSLFKLKPLSNKTATDDTGGKDPRNV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the phospholipase D family."}
+{"protein": "MSRIELGGVLGKTFGKVHHRLISRVSEAGVALAKTVPGFEQFMISSQRRGLTYSVFKGKKNIGVDDLGFPVTGDVIRIVPVIIGSKKAGVLQTILGAVLVAVGVVLNFTPWAAASPFFYKLGAAVMLGGVVQMLSPQPAGLASKQSSDNRASYAFGGVTNTAAQGYPVPLLYGRRRIGGAIISAGIYVEDQQ", "text": "FUNCTION: Plays a role in tail tip complex assembly. The tail tip complex is assembled successively with three tail tip proteins J, one tail tip protein I, one tail tip protein L and one tail tip protein K. The tail tip complex interacts with tail measure protein to initiate tail tube assembly. The formation of the tail tip complex is completed by the addition of tail tip protein M, which is followed by tail tube polymerization. May be excluded form tail tip during maturation and would be absent from virions. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the lambda-like tail tip protein I family."}
+{"protein": "MIWFLAFILFLAAGELVSSSGLLNCEPSEIAYEEITRQGQKSTNTLCKCKYEPYKFSTATSKDKTTVTVQYKCKQVRPCVYGQKCQSLEDGPQEKALKTHCTCAKGQQCHSTPEHADESRIFGDTKYYSFVCV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-11 family."}
+{"protein": "MAPERRSRLSETAGLFVSLLALTSIVPVQAVATVPQTDYAKRAERVLRSAPLIDGHNDLPYAIRKSTRDQIYDGKLPFETSLKGHTDLPRMRKGRMGGQFWSVFIACPSDPNAPIDLPTFATRDTLEQIDVARRLVDKYSKDLMFCDNPGCAKRAFRQGKIGSFLGIEGGHQVGSSIAALRQAFYAGARYMTITHNCDNAWATAASTVRAGKPDLGMTDFGPALIKEMNRLGMLVDLSHVSHQSMRDILKVTKAPVIFSHSSAYEVSKHLRNVPDDVLKTVAKNNGVVMVTFVRTFVNVDDPDSVDVNTIVKHIFHIAKVAGWDHVGLGGDYDGTTELPKGLEDVSKYPYLIEKVLEAGATEEQARKLVGENVLRVWTEVEQIAKKIQRSGALPVEEVWKGRNGTALSERSTFIEGPAPLAYGCD", "text": "FUNCTION: Hydrolyzes a wide range of dipeptides. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family."}
+{"protein": "MFLSLPMLTVLIPLVSLAGLFYSASVEDDFPQGCTSTTSLCFYSLLLPITIPVYVFFHLWTWMGIKLFRHN", "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. May act by regulating the catalytic subunit PIGA. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
+{"protein": "MENFLDNKNMLYALKMISPGTPLRLGLNNVLRAKTGGLIVIATNEDVMKIVDGGFAINAEYSPSYLYELAKMDGAIVLSGDVKKILFANAQLIPDYFIETSETGTRHRTAERVAKQTGAIVIGISQRRNVITVYRGNEKYVVEDISKIFTKANQAIQTLEKYKTVLDQAVTNLNALEFNDLVTIYDVALVMQKMEMVMRVTSIIEKYVIELGDEGTLVSMQLEELMGTTRIDQKLIFKDYNKENTEIKELMKKVKNLNSEELIELVNMAKLLGYSGFSESMDMPIKTRGYRILSKIHRLPTAIIENLVNYFENFQQILDASIEELDEVEGIGEIRATYIKNGLIKMKQLVLLDRHI", "text": "FUNCTION: Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (PubMed:25965978). 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. 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. SIMILARITY: Belongs to the DisA family."}
+{"protein": "MAAPSWRGARLVQSVLRVWQVGPHVARERVIPFSSLLGFQRRCVSCVAGSAFSGPRLASASRSNGQGSALDHFLGFSQPDSSVTPCVPAVSMNRDEQDVLLVHHPDMPENSRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPGKQKRHHLELSLLEDPWKSMESADLVVVLVDVSDKWTRNQLSPQLLRCLTKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVVNGKKLKMRQAFHSHPGTHCPSPAVKDPNTQSVGNPQRIGWPHFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICANIIREKLLEHLPQEVPYNVQQKTAVWEEGPGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLCDVDIRLSVKLLK", "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. 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": "MLHPIDTTIYRAGTSRGLYFLASDLPAEPSERDAALISIMGSGHPLQIDGMGGGNSLTSKVAIVSASTQRSEFDVDYLFCQVGITERFVDTAPNCGNLMSGVAAFAIERGLVQPHPSDTTCLVRIFNLNSRQASELVIPVYNGRVHYDDIDDMHMQRPSARVGLRFLDTVGSCTGKLLPTGNASDWIDGLKVSIIDSAVPVVFIRQHDVGITGSEAPATLNANTALLDRLERVRLEAGRRMGLGDVSGSVVPKLSLIGPGTETTTFTARYFTPKACHNAHAVTGAICTAGAAYIDGSVVCEILSSRASACSASQRRISIEHPSGVLEVGLVPPENAAQSLVDVAVVERSVALIAHARVYYTTPDRRRSYDSPLTSPSTPADTHNLFDAAYRPVIQPSDTDVEAPHMLALENKEQCVSRCDTALHHIVASYGASDAHASDRSLS", "text": "FUNCTION: Aconitate-delta-isomerase; part of the gene cluster that mediates the biosynthesis of itaconic acid and 2-hydroxyparaconate (PubMed:26639528, PubMed:27750034). Cis-aconitate is secreted by the mitochondrial tricarboxylate transporter MTT1. In the cytosol cis- aconitate is converted into trans-aconitate via isomerization by the aconitate-delta-isomerase ADI1 (PubMed:26639528). Decarboxylation of trans-aconitate by the trans-aconitate decarboxylase TAD1 then leads then to the production of itaconic acid (PubMed:26639528). The cytochrome P450 monooxygenase CYP3 further converts itaconate to 2- hydroxyparaconate via oxidation of the double bond, leading to a transient epoxide, which can subsequently be lactonized to produce 2- hydroxyparaconate (PubMed:27750034). Secretion of itaconate and possibly 2-hydroxyparaconate into the medium is mediated by the major facilitator ITP1 (PubMed:26639528, PubMed:27750034). The glyoxalase domain-containing protein RDO1 is not involved in the biosynthesis of itaconate and 2-hydroxyparaconate, however, it might play a role in the further conversion of 2-hydroxyparaconate to itatartarate (PubMed:27750034). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the PrpF family."}
+{"protein": "MVAAVLLGLSWLCSPLGALVLDFNNIRSSADLHGARKGSQCLSDTDCNTRKFCLQPRDEKPFCATCRGLRRRCQRDAMCCPGTLCVNDVCTTMEDATPILERQLDEQDGTHAEGTTGHPVQENQPKRKPSIKKSQGRKGQEGESCLRTFDCGPGLCCARHFWTKICKPVLLEGQVCSRRGHKDTAQAPEIFQRCDCGPGLLCRSQLTSNRQHARLRVCQKIEKL", "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 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the dickkopf family."}
+{"protein": "MSREEDEKLLFPSFAFPAECFPEAATSGGEQKKARQRRRRKVKPEAAAALAGESGGDEQAKKRRLSDEQARFLEMSFKKERKLETPRKVQLAAELGLDAKQVAVWFQNRRARHKSKLMEEEFAKLRSAHDAVVLQNCHLETELLKLKERLADVEEEKAKLAAVAAATTGGGGGGGGGSSSPTSSSFSTVTYHPALAGQFGVEAAAEEADLTYMSEYAYNSYMLELAAAGYCGGVYDQFS", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class I subfamily."}
+{"protein": "MNLKKYTDYALRVLIFTGLKSDQELANIKEIAEVYQISQEHLRKVVHELTKMELVVTIRGRNGGIKLAKPASEINIGLLIRQLENDFVLLECFDKGTNHCVISPGCTLKHVINKALVAFFKVLEEYTLEDLIKNEEELLALMGIEKV", "text": "FUNCTION: Nitric oxide-responsive transcriptional regulator."}
+{"protein": "MESAIGEHLQCPRTLTRRVPDTYTPPFPMWVGRADDTLHQVVMGYLGVQFRGEDQRPAALRAMRDIVAGFDLPDGPAHHDLTHHIDNQGYENLIVVGYWKDVSSQHRWSTSPPVSSWWESEDRLSDGLGFFREIVAPRAEQFETLYAFQDDLPGVGAVMDGVSGEINEHGYWGSMRERFPISQTDWMQASGELRVVAGDPAVGGRVVVRGHDNIALIRSGQDWADAEADERSLYLDEILPTLQSGMDFLRDNGPAVGCYSNRFVRNIDIDGNFLDLSYNIGHWASLDQLERWSESHPTHLRIFTTFFRVAEGLSKLRLYHEVSVFDAADQLYEYINCHPGTGMLRDAVITAEH", "text": "FUNCTION: Catalyzes the dehydration of aldoximes to their corresponding nitrile (PubMed:14556637). Is active toward various arylalkyl- and alkyl-aldoximes, and to a lesser extent toward aryl-aldoximes (PubMed:14556637). SIMILARITY: Belongs to the heme-containing dehydratase family."}
+{"protein": "MFPEPPTPGSPAPETPPDSSRIRQGAVPAWVLATILLGSGLLVFSSCFCLYRKRCRRRMGKKSQAQAQVHLQEVKELGRSYIDKVQPEIEELDPSPSMPGQQVLDKHQLGRLQYSLDYDFQTGQLLVGILQAEGLAALDLGGSSDPYVSVYLLPDKRRRHETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVRVPMSSVNLGRPVQAWRELQVAPKEEQEKLGDICFSLRYVPTAGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQKVQVELTVLDYDKLGKNEAIGRVAVGTAVGGAGLRHWADMLANPRRPIAQWHSLRPPDRARPIPAP", "text": "FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein Recycling endosome membrane; Single-pass membrane protein Note=In mast cells, localizes to the endocytic recycling compartment. SIMILARITY: Belongs to the synaptotagmin family."}
+{"protein": "DCLGFLWKCNPSNDKCCRPNLVCSRKDKWCKYQI", "text": "FUNCTION: Potent inhibitor of Nav1.2/SCN2A voltage-gated sodium channels (IC(50)=0.6-0.7 nM) (PubMed:16267209, PubMed:29703751). Also weakly inhibits Nav1.1/SCN1A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.7/SCN9A and Nav1.8/SCN10A (IC(50)=20-610 nM) (PubMed:16267209, PubMed:29703751). It 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 low affinity for lipid bilayers (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. 08 (Gtx1-15) subfamily."}
+{"protein": "MSSSREMRDLPLVRLPEPYKTKYELYQASSGPNGRIFQLRLSSDQNNGAISPPDLLHHQMLYFSELIPGPQATLPAESDNTAWARACRSLVSFVTWDGESAPTVGQIWMLVYAIFSLRPSEESFRLSLSGAQKDQLYAECNAAGLSTRFPTPVQPQPLYTTIEDVVVSRAAFWQGAGSPLGTRPAWLVPSISGSARKLPSEYPAFPLQYTLTSQLTNRPVHTQHPVRPAKPARGAPIYSRYIPHLDEFFAMDHLDYTNETHLQLFHTWQNDPRVAVNWKEAGTLDQHREYLRKIDEDPHQIAVLARFNNTYFAYFEIYWAKEDHMGTYYPALDWDRGRHSLVGDARFRGPHRAMAWWTSLIHYIFLDEPRTTCVVGEPKATNGPVLGYDAAHGFHVHKWGDLPHKRSAMVRCERVRFFEVVNFGNVTSNGTAKPSKSKL", "text": "FUNCTION: Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of hydroxamate-containing siderophores that play a critical role in virulence via intracellular iron acquisition during macrophage infection (PubMed:18404210). SUBCELLULAR LOCATION: Peroxisome Note=Targeted to peroxisomes via its PTS1-type peroxisomal targeting signal (By similarity). SIMILARITY: Belongs to the lysine N-acyltransferase mbtK family."}
+{"protein": "MRLAAGALLACAALGLCLAVTEKTVRWCAVNDHEASKCANFRDSMKKVLPEDGPRIICVKKASYLDCIKAIAAHEADAVTLDAGLVHEAGLTPNNLKPVVAEFYGSKENPKTFYYAVALVKKGSNFQLNELQGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVASFFSGSCVPCADGADFPQLCQLCPGCGCSSVQPYFGYSGAFKCLKDGLGDVAFVKQETIFENLPSKDERDQYELLCLDNTRKPVDEYEQCHLARVPSHAVVARSVDGKEDLIWELLNQAQEHFGKDKSGDFQLFSSPHGKNLLFKDSAYGFFKVPPRMDANLYLGYEYVTAVRNLREGICPDPLQDECKAVKWCALSHHERLKCDEWSVTSGGLIECESAETPEDCIAKIMNGEADAMSLDGGYVYIAGQCGLVPVLAENYESTDCKKAPEEGYLSVAVVKKSNPDINWNNLEGKKSCHTAVDRTAGWNIPMGLLYNRINHCRFDEFFRQGCAPGSQKNSSLCELCVGPSVCAPNNREGYYGYTGAFRCLVEKGDVAFVKSQTVLQNTGGRNSEPWAKDLKEEDFELLCLDGTRKPVSEAHNCHLAKAPNHAVVSRKDKAACVKQKLLDLQVEYGNTVADCSSKFCMFHSKTKDLLFRDDTKCLVDLRGKNTYEKYLGADYIKAVSNLRKCSTSRLLEACTFHKH", "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. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the transferrin family."}
+{"protein": "MLDRIRVVLVNTSHPGNIGGAARAMKNMGLSQLVLVQPESFPHGDAVARASGATDILDAARVVDTLEEALSGCSVVLGTSARDRRIPWPLLDPRECATTCLEHLEANGEVALVFGREYAGLTNEELQRCQFHVHIPSDPEFGSLNLAAAVQVLTYEVRMAWLAAQGKPTKMEKFESTSMLNTELVTADELELYYAHLERTLIDIGFLDPEKPRHLMSRLRRLYGRSAISKLEMNILRGILTETQKVARGLSYKRSDD", "text": "FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32), 2'O-methylated uridine (Um32) or 2'O-methylated adenosine (Am32) at position 32 in tRNA. Confers resistance to oxidative stress. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family."}
+{"protein": "MPQLNSGGGDELGANDELIRFKDEGEQEEKSPGEGSAEGDLADVKSSLVNESENHSSDSDSEVERRPPPRETFEKPRDYLSEAFRRQQDAAFFKGPPYAGYPFLMIPDLGGHYLPNGALSPSARAYLQMKWPLLDSPSTAGLKDARSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNEHFSPGTPPGHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPQQGQPMYSIPPGGFRHPYPALAMNASMSSLVSSRFSPHMVPPPHHSLHTSGIPHPAIVSPIVKQEPSSGNISPNLSTKSNVVVKKEEEKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHSLSREEQAKYYELARKERQLHSQLYPSWSARDNYGKKKKRKREKQSPEMENYTKTKKMCVQHFPSDKSCDSPASSHGSMLDSPATPSAALASPAAPAATHSEQAQPLSLTTKPEARALSHSAAFLASKSPSSSSLSGHLPSPVGSPLLSRPIPLTSSILSPPGVFPSALQALPLLQAQPLSLVTRSSD", "text": "FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA and acts as a repressor in the absence of ctnnb1-A and possibly ctnnb1-B, and as an activator in the presence of these proteins. Required early in development for the establishment of the dorsal body axis in response to maternal Wnt signaling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TCF/LEF family."}
+{"protein": "MPIKLLMPALSPTMTEGNLARWLKKEGDKINPGEVIAEIETDKATMEVEAVDEGTLAKIIIPQGSQNVPVNSLIAVLIEEGEELSGIEEFIAKNNSNSPKKEEISKPAETIAPQNVKEENITTASDQNNIKVFASPLAKRLAKIQNVRIEEIKGSGPHGRIIKQDVLSHKGGSKALSNKIVSRNPEEYRLAPNNNIRKIIAKRLLESKQTVPHFYLSIECNVDKLLDIREDINKSFGDDKSAKISVNDFIILAVAKALQEVPNANASWGDDAIRYYNNVDISVAVAIENGLVTPIIRNADQKNIVDLSSEMKGLIKKARENKLTPEEFQGGGFTISNLGMYGIKNFNAIINPPQSCIMGVGSSSKRAIVKNDQISIATIMDVTLSADHRVVDGAVGAEFLAAFKRFIESPALMLLYTR", "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). SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family."}
+{"protein": "MAGFSKVIATIFLMMMLVFATGMVAEARTCESQSHRFKGLCFSKSNCGSVCHTEGFNGGHCRGFRRRCFCTRHC", "text": "FUNCTION: Plant defense peptide with antifungal activity against F.oxysporum and B.cinerea. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family."}
+{"protein": "MNVSLFVTCLADIFYPGVGKDTVEVLERHGCNVKFPENQICCGQPAFNSGYHEDTKKAAKHTIETFADADYVVLPSGSCAAMLLEYKELFADDPEWEKRAEELASKTYELTQFLVRVLKVEDIGAVCHKKATYHTSCHMSRLLRETEAPFSLLEQVKGLELAPLANKESCCGFGGTFSVKMPAISEQMVEEKVGHIEATGADLLIGADCGCLMNIGGRIERNGKTIEVKHIAQVLNSKE", "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": "MIPKLIVFGGNGFLGKRICQEAVTSGYQVVSVSRSGKAPHSNELNDKQWMQEVQWTAADIFKPDSYHELLNNATNVVHSLGILLENENYKQTLSKSPTYDSKSRLLSFGAGPNPLKKSSPYFTYEMMNKQSAIILADTFKQKILKKSKKEQEKANQRSFTYISADKGFPLIPSGYINSKREAEIELEKMQRYFRPIIVRPGFMFDEHRNAIGPRSFIHTALELLYCGNKFLLRNKLQLLNDLIRPTVSTQQVSKSVLKNIENPDFKGVVTLEEILKA", "text": "FUNCTION: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post- transcriptional gene expression (PubMed:25683707). Component of a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis (PubMed:25631044). SUBCELLULAR LOCATION: Mitochondrion."}
+{"protein": "MWPKILLRGGRVAAGLCPALGPRLAARFPPQRTPENRLAPQRNLHATAARALPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTSGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYSIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPELVQKEPGEPTAVEPAPASA", "text": "FUNCTION: Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase S14 family."}
+{"protein": "MELILSTSPAELTLDPACQPKLPLDSTCQPEMTFNPGPTELTLDPEHQPEETPAPSLAELTLEPVHRRPELLDACADLINDQWPRSRTSRLHSLGQSSDAFPLCLMLLSPHPTLEAAPVVVGHARLSRVLNQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQVHFYTHLGYQLGEPVQGLVFTSRRLPATLLNAFPTAPSPRPPRKAPNLTAQAAPRGPKGPPLPPPPPLPECLTISPPVPSGPPSKSLLETQYQNVRGRPIFWMEKDI", "text": "FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of the acidic amino terminus of processed forms of beta- and gamma-actin (ACTB and ACTG, respectively) (PubMed:30028079, PubMed:29581253). N-terminal acetylation of processed beta- and gamma- actin regulates actin filament depolymerization and elongation (PubMed:29581253). In vivo, preferentially displays N-terminal acetyltransferase activity towards acid N-terminal sequences starting with Asp-Asp-Asp and Glu-Glu-Glu (PubMed:30028079, PubMed:29581253). In vitro, shows high activity towards Met-Asp-Glu-Leu and Met-Asp-Asp-Asp (PubMed:10644992, PubMed:29581307). May act as a tumor suppressor (PubMed:10644992). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the acetyltransferase family."}
+{"protein": "MKVGILDSTLREGEQTPGVVFTIDQRVEIAKALSDVGVQMIEAGHPAVSSDIYEGIKRIMKLKREGLITSEIVGHSRAVKKDIEVAAELEVDRIAIFYGVSDIHLKAKHHVTREEALNIIAETISYAKSHGVKVRFTAEDGSRTDLDYLIKVCKTARDAGADRVSIADTVGILYPTKTRELFSTLVREVPGLEFDIHAHNDLGLAVANALAAIEGGATIIHTTVNGLGERVGIVPLQVIAAAIKYHFGIEVVKLNKLQQLASLVEKYSGIPMPPNYPITGDYAFIHKAGIHVAGVLNDPSTYEFMPPETFGRSRDYVIDKYTGKHALKDRFEKLGVKLSDVELDQVLAKIKSNPNVRFYRDVDLLEIAESVTGRVLKPKPPENIEALISVKCESNVYTTAVTRRLSVIPGVKEVMEISGDYDILVKVEAKDPNELNQIIENIRAVKGVSSTLTSLVLKKM", "text": "FUNCTION: Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. Homocitrate synthase LYS20/LYS21 subfamily."}
+{"protein": "MTLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK", "text": "FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. 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": "MRSAMLFAAVLALSLAWTFGAVCEEPQGQGGRLSKDSDLYQLPPSLLRRLYDSRPVSLEGLLKVLSKASVGPKETSLPQKRDMHDFFVGLMGKRNSQPDTPTDVVEENTPSFGILK", "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. Is a critical central regulator of gonadal function (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the tachykinin family."}
+{"protein": "PRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSSTAASRVPGPEDATQAGSGPGPAEPSSEDPPPSRSPGPERASLCPAGGGPGEALSPSGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGRETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCSGKLGNYRINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELKPNSVSKDV", "text": "FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy- inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm. Nuclear export requires functional XPO1."}
+{"protein": "MRILYLLFSLLFLALQVSPGLSSPRRDMLFCKGGSCHFGGCPSHLIKVGSCFGFRSCCKWPWNA", "text": "FUNCTION: Potent antibacterial activity against the Gram-negative bacterium E.coli ML-35, and against the Gram-positive bacterium L.monocytogenes EGD. Lacks antifungal activity against C.albicans. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "MAGAQPFLADGNQELFPCEVCGRRFAADVLERHGPICRKLFNKKRKPFNSLKQRLRGTDIPTVGKAPQSKPQPVRKSNWRQHHEDFINAIQSAKQCTLAIKEGRPLPPPPPPTVNPDYIQCPYCKRRFNETAASRHINFCKDQESRRVFDPAQTAARLASRAQGRAQMSPKKELTVTSAVGALLQNRALEASAAPTRPAVDPASGAKLRQGFAKSSKKD", "text": "SIMILARITY: Belongs to the ZC2HC1 family."}
+{"protein": "MQEHLVVTLDGKDYLVEPGTNLLEFIKSQDTFVPSICYNESMGPIQTCDTCTVEIDGKIERSCSTVIDRPMTVNTVNNDVKDAQKEALDRILEKHMLYCTVCDYNNGDCEIHNTMDAWGLQHQTYEYKEKPYEKDYGPFYRYDPNQCILCGRCVEACQDIEVNETIRIDWDREHPRVIWDNDVPINESSCVSCGQCATVCPCNAMMEVNMEGNAGYMTDTEPGSLAAMIDLTKKAEPGYGPLFAISDSEAEMRKERIKKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNGEFHEVEWDEALNVIADNFTAIKEKHGPDALSFISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFIDEWVDDFDEYYKSLETFTMAFAEEATGIPESELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTGAYPLRGHNNVQGCSDMGSMPDKITGYQSIEADDIRAKFEKEYGVKLNPKAGKDNHEMVEGIHDGEVHSLYLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAIANRLGFDWNYKHPSEIMDEVARLTPLYAGVSYDRLEGFNSLQWPVQPDGTDEPILYLEGFNFDNGKAKLFPLSFDNYFKQDEIYDIHVNNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIPLNNDAMENGDLGAINLLTNSDVDQYTDTPSYKRTSCRLEVITKRGKSPLNPNNFRVNKKRQPQYSVQVQKKWERSDYVFPGNQVDK", "text": "SIMILARITY: In the C-terminal section; belongs to the prokaryotic molybdopterin-containing oxidoreductase family."}
+{"protein": "MVNFTAEEKTLINGLWSKVNVEEVGGEALGRLLVVYPWTQRFFDSFGNLSSASAIMGNPRVKAHGKKVLTAFGESIKNLDNLKSALAKLSELHCDKLHVDPENFKLLGNVLVIVLASHFGNEFTAEMQAAWQKLVAGVATALSHKYH", "text": "FUNCTION: Hemoglobin epsilon chain is a beta-type chain found in early embryos. SIMILARITY: Belongs to the globin family."}
+{"protein": "MAATEHRGLSGGDYNVDLLPIDQDDSPPSSWRLSLDTFRLPSSSPLSSGRHNGRTRLSRYLRTPKKERKVSEYYKQQEKLLEGFNEMETINETGFVSGAPTEEELKKLAKSERLAVHISNAANLVLFVAKVYASVESRSMAVIASTLDSLLDLLSGFILWFTANAMRTPNNFRYPIGKRRMQPVGIIVFASVMATLGLQVILESTRLLVSKNGSHMSSTEEKWMIGIMASATVVKFLLMLYCRSFQNEIVRAYAQDHLFDVITNSVGLATAVLAVKFYWWIDPSGAILIALYTISTWARTVLENVHSLIGRSAPPDFLAKLTFLIWNHHEKIKHIDTVRAYTFGSHYFVEVDIVLPEDMRLHEAHNIGETLQEKLEQLSEVERAFVHIDFEFTHRPEHKCKV", "text": "FUNCTION: Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily."}
+{"protein": "MGMRMRMMFTVFLLVVLANTVVSFPSDRDSDGADAEASDEPVEFERDENGCCWNPSCPRPRCTGRR", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
+{"protein": "MNRDNINSNKTVKQEFGSFAFVICIALVIRILIMEPFTVPTGSMKATILENDYIFSTKYSYGYSNYSLSFFDFIHLFKGRVFAREPERGDIVVFRPPNDMSVRYIKRLIGLPGDKIQLIDDVIYINDKKIERTEVGTYIGEDGIKYLKFKETLPNGRTYFSYKLAPIFGVIPSDRYSNTDVFYVPEGQYFFLGDNRDRSNDSRVNLGFVPFENFIAKAQFIWFSTKITWWDNDIGIINLILKLKPWIESVRLSRIFKNLYNVDE", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S26 family."}
+{"protein": "MAQRSVMFRDVAIDFSQEEWDCLDSAQRDLYRDVMLENYSNLVSLDLPSRGANKLLSPKKDIYETGLSQWEMSARLENCDLENSSSRDYLEVKGTLEKQQENQAYFSQGMIIYDNMSIFNQHAYLSQHPRCHSTEKPYKCKECGKAFRRASHLTQHQSIHTGEKPYECKQCGKAFSRDSQLSLHQRLHTGEKPYACKECGKAFTQSSQLILHHRIHTGEKPYKCEECGKAFIRSSQLTRHQKVHTGEKPYECKECGKAFTQNSQLTLHQRLHTGEKLYECKECRKVFTQLSQLILHKRIHTGEKPYECKECGKAFICGSQLSQHQKIHNGEKPYECQECGKAFIRGSLLMQHQRIHTGEKPYKCEECGKAFIRGSQLTQHQRIHTNEKPYECKECGKTFSHGSQLTQHQRIHTGEKPYQCKECGKAFNRGSLLTRHQRIHTGEKPYECKECGKTFSRGSELTQHERIHTGEKPYECKECGKSFIRGSQLTQHQRIHTGEKPYECKECRMAFTQSSHLSQHQRLHTGEKPYVCNECGKAFARGLLLIQHQRIHTGEKPYQCKECGKAFIRGSQLTQHQRIHTGEKPYGCKECGKAFSHGSQLTLHQRIHTGEKPYECKECRKAFTQSSHLSRHQRVHTGEKPYQCRECGKAFTRGSQLTQHQRIHISEKSFAYKECGIDFSHDSQVYI", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MGDILTGVSGAEAATAMIAAAAIIALVGFTKWGAKKVASFFG", "text": "FUNCTION: Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity). SUBCELLULAR LOCATION: Virion Host membrane; Single-pass membrane protein. Note=prior to assembly, the major capsid protein is found associated with the bacterial host inner membrane. SIMILARITY: Belongs to the inovirus capsid protein family."}
+{"protein": "MASLKKSLFLVLFLGLVSLSICEKEKRENEGNENEEEEENHEEGSEEKRGLLDLAKHVIGIASKLGKRSEEKRGLLDFAKHVIGIASKLGK", "text": "FUNCTION: Fallaxidin-3.1 shows antibacterial activity against the Gram- positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=100 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram- negative bacteria E.cloacae and E.coli. FUNCTION: Fallaxidin-3.2 shows antibacterial activity against the Gram- positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=500 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram- negative bacteria E.cloacae and E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
+{"protein": "MTTNRLVLSGTVCKTPVRKVSPSGIPHCQFVLEHRSTQQEAGFSRQTWCRMPIVVSGQQSQALTHSITVGSQLTVEGFISCHQGRNGLNKLVLHAEQIEFIDSGD", "text": "FUNCTION: Binds single-stranded DNA at the primosome assembly site (PAS). SIMILARITY: Belongs to the PriB family."}
+{"protein": "MATEEAIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPVRMVTVPPRHYCIVANPVSRDTQSSVLFDITGQVRLRHADQEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKNGDKVMAGDEWLFEGPGTYIPQKEVEVVEIIQATVIKQNQALRLRARKECFDREGKGRVTGEEWLVRSVGAYLPAVFEEVLDLVDAVILTEKTALHLRALQNFRDLRGVLHRTGEEWLVTVQDTEAHVPDVYEEVLGVVPITTLGPRHYCVILDPMGPDGKNQLGQKRVVKGEKSFFLQPGERLERGIQDVYVLSEQQGLLLKALQPLEEGESEEKVSHQAGDCWLIRGPLEYVPSAKVEVVEERQAIPLDQNEGIYVQDVKTGKVRAVIGSTYMLTQDEVLWEKELPSGVEELLNLGHDPLADRGQKGTAKPLQPSAPRNKTRVVSYRVPHNAAVQVYDYRAKRARVVFGPELVTLDPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFELKNRNDPAEAAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRMAVFGFEMSEDTGPDGTLLPKARDQAVFPQNGLVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEAMSMAVESTGNAKAEAESRAEAARIEGEGSVLQAKLKAQALAIETEAELERVKKVREMELIYARAQLELEVSKAQQLANVEAKKFKEMTEALGPGTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSSPINLFSTAFGLLGLGSDGQPPAQK", "text": "FUNCTION: Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MALLQLLLFAMLAACGFSEEQTEGITIAYKVLEVYPQSRRVLITCDAPEASQPITYSLLASRGILVAKKVVHDSVPASFNINITIKSSPDLLTYSCQATSNSGTYGPSSRLQMYQELWAKPVSQLQADFVLRHGDSGPTVELSCLASSGSPPITYRLVGNGGRVLAQQRPLHGKPANFSLPLSQTTGWFQCEAENDVGVDSSARIPLPRAEARAKLVTTLAGELPLTPTCILAGSLVSIAVIASRMLSSTGL", "text": "FUNCTION: Probable B cell-associated cytokine that plays a role in the regulation of humoral immune responses (PubMed:28978694). Involved in lymphocyte B cell development and immunoglobulin/IgA production (PubMed:28978694). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MPASNFPTGVHDMRLGVIADDFTGATDIAGFLVGNGLRTIQLNGVPADDLAVDADAVVISLKARSCPTGQAIAESLAALKWLQKNNCQQFFFKYCSTFDSTPKGNIGPVTDALLEALGEEFTVICPALPVNGRTIYNGYLFVNGVLLSETGMRNHPVTPMTDSNIMRVMESQSRGRAGNISSTIVDQGSDAVRDALRKLQSEGIRYAVLDALNDQHIETLGRAVSQMKLVTGGSGLADGMARAWTQLRGKNVAAAEAAGAPVKGRTVILSGSCSQMTNAQVAAYKAKAPALAMDVEKAINDAAYIDVLAEWVLAQSGDALPPLVYATMPPEALKAVQERFGGERASAAIEDLFGQLAKRLEAEGFTRFIVAGGETSGAVTQALAIDGFTIGPQIAPGVPWVRGIGKPLSLALKSGNFGTEAFFFEAQKIANQEGDK", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of 3-oxo- tetronate to 3-oxo-tetronate 4-phosphate. SIMILARITY: Belongs to the four-carbon acid sugar kinase family."}
+{"protein": "MTASSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKHALSAGYRHIDCASVYGNETEIGEALKESVGSGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTVRYDSTHYKETWKALEVLVAKGLVKALGLSNFNSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCHARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAEKHGRSPAQILLRWQVQRKVICIPKSINPSRILQNIQVFDFTFSPEEMKQLDALNKNWRYIVPMITVDGKRVPRDAGHPLYPFNDPY", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (By similarity) (PubMed:22820017, PubMed:15769935, PubMed:20410296). Plays an important role in ascorbic acid biosynthesis by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone (PubMed:20410296, PubMed:15769935, PubMed:22820017). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic (By similarity). Involved in the detoxification of lipid- derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Displays no reductase activity towards retinoids (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Apical cell membrane. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MAPKKDVKKPAAAAAPAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQDEFKEAFLLYDRTGDSKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMLQAISNNKDQGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALMAGQEDSNGCINYEAFVKHIMSI", "text": "FUNCTION: Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function."}
+{"protein": "MPTVEELYRNYGILADATEQVGQHKDAYQVILDGVKGGTKEKRLAAQFIPKFFKHFPELADSAINAQLDLCEDEDVSIRRQAIKELPQFATGENLPRVADILTQLLQTDDSAEFNLVNNALLSIFKMDAKGTLGGLFSQILQGEDIVRERAIKFLSTKLKTLPDEVLTKEVEELILTESKKVLEDVTGEEFVLFMKILSGLKSLQTVSGRQQLVELVAEQADLEQAFSPSDPDCVDRLLQCTRQAVPLFSKNVHSTRFVTYFCEQVLPNLSTLTTPVEGLDIQLEVLKLLAEMSSFCGDMEKLETNLRKLFDKLLEYMPLPPEEAENGENAGNEEPKLQFSYVECLLYSFHQLGRKLPDFLTAKLNAEKLKDFKIRLQYFARGLQVYIRQLRLALQGKTGEALKTEENKIKVVALKITNNINVLIKDLFHIPPSYKSTVTLSWKPVQKVEIGQKRTSEDTSSGSPPKKSPGGPKRDARQIYNPPSGKYSSNLSNFNYERSLQGK", "text": "FUNCTION: Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mainly nuclear. SIMILARITY: Belongs to the API5 family."}
+{"protein": "MAAGAGARPAPRWVKALGEPLSAAQLRRLEEHRYTAVGESLFEPPLQLYWTWLLQWIPLWMAPNTITLIGLAINLVTTLVLIFYCPTVTEEAPYWTYLLCALGLFIYQSLDAIDGKQARRTNSCSPLGELFDHGCDSLSTVFMAIGASIAVRLGTHPDWLFFCSFVGMFMFYCAHWQTYVSGVLRFGRVDVTEIQVALVIVFMLSTFGGATMWDYTIPILEIKLKIVPVLGVVGGLIFSCSNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATNMFEKHPCLYTLMFGCVFAKVAQKLVIAHMTKSELYLQDTVFIGPGLLFLDQYFNNFIDEYVVLWIAMVISSFDMMIYFTSLCLQISRHLHLNIFKTSCQQAPEQVYKHID", "text": "FUNCTION: Catalyzes phosphatidylcholine biosynthesis from CDP-choline. It thereby plays a central role in the formation and maintenance of vesicular membranes. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family."}
+{"protein": "MAANSKTAIRLSLRAGERIFINGAVLRADRKVSLELLNDATFLLENHVLQPEDTTTPLRQLYFAAQMMLIEPAMREQAGATFAQMLKGMFATFKDAEILNALKLVDELVHNGRVFEALKTIRAQYPREAELMGAQPVVWPVTKSGKSAGANP", "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": "MNFKYIVAVSFLIASAYARSVQNDEQSLSQRDVLEEESLREIRSIGAKILGGVKTFFKGALKELASTYLQRKRTAEDHEEMKRLEAVMRDLDSLDYPEEASERETRGFNQEEIANLFTKKEKRILGPVISKIGGVLGGLLKNLG", "text": "FUNCTION: Maximin-5 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. The only exception is the resistance of E.coli. Shows also antimicrobial activity against fungi C.albicans, A.flavus and P.uticale. It has little hemolytic activity. It does not possess a significant cytotoxicity against tumor cell lines. It does not possess a significant anti-HIV activity. FUNCTION: Maximin-H4 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": "MVSKSLIVLLLVSVLVSTFYTSEAYPASFDDDFDALDDLDDLDLDDLLDLEPADLVLLDMWANMLDSQDFEDDFE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily."}
+{"protein": "MGVCTEERPVMHWQQSARFLGPGAREKSPTPPVAHQGSNQCGSAAGANNNHPLFRACSSSSCPDICDHSTKPFGNAYGTESFRSYETADRATFEDSAAKFSISRSRTDCTEVSDETTSGISFKTEPFGPPSSPESTSDSKITRNLDDCSGCGRQIQDRFYLSAVEKRWHASCLQCYACRQPLERESSCYSRDGNIYCKNDYYSFFGTRRCSRCLASISSNELVMRARNLVFHVNCFCCTVCHTPLTKGDQYGIIDALIYCRTHYSIAREGDTASSSMSATYPYSAQFGSPHNDSSSPHSDPSRSIVPTGIFVPASHVINGLPQPARQKGRPRKRKPKDIEAFTANIDLNTEYVDFGRGSHLSSSSRTKRMRTSFKHHQLRTMKSYFAINHNPDAKDLKQLSQKTGLPKRVLQVWFQNARAKWRRMMMKQDGSGLLEKGEGALDLDSISVHSPTSFILGGPNSTPPLNLD", "text": "FUNCTION: Required for the normal development of the wing and halter imaginal disks. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MTAQMFTIALLLSLSAIAAAGTIKTAPARTPSTQDDASFPPDGAPVKRFDAFTTGFGHSKRNFDEIDRSGFGFAKKNFDEIDRSGFGFNKRNFDEIDRSGFGFNKRNFDEIDRSGFGFNKRNFDEIDRSGFGFNKRNFDEIDRSGFGFNKRNFDEIDRSGFGFNKRNFDEIDRSGFGFVKRVYVPRYIANLYKRNFDEIDRSGFGFNKRNFDEIDRTGFGFHKRDYDVFPDKRNFDEIDRSGFGFVRRNVE", "text": "FUNCTION: Myotropic peptides that enhance both the frequency and amplitude of spontaneous hindgut contractions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the orcokinin family."}
+{"protein": "METAIEDAGLDRGPTLTSSWDAACGALTQSLFLTRTGPRAQDLDFEQLLEPPAPSQDPVSLKSSLSPRDENPCFIYLNCGPNGGEEILSVGVLSSARNMEVYLGEEYCGTSRGKTACTVLDDSEHEKILLYKKYLKLDSPTHACKIKLLSFGEKQCVLVSKVVVHLRPRSADPSPRSAALGSRIDLDNIQTIMESMGSRLSPGAQQLMSMIRFQQQNRLPIGDQLQSVLGSAGHKHLMALQSSPSPAVLDKASSTPFPFRTGLTPSAITENLKALIDKSAQPSGEGNTTNHDEGHLMPQNHSLESDLKNAVSSFLPKKASGSSSVPSSELLPFLQNLCSQVNHLRVGHNARWQENISKPREGMVGVPMEEQPVCSYLEKILSKNMELMEKKLMDHIDERIYQLQEHIDAKMALLVDLLRGPNSPPPGMPLRHYDSRERLSNGER", "text": "FUNCTION: ATPase that regulates mitochondrial ABC transporters ABCB7, ABCB8/MITOSUR and ABCB10. Regulates mitochondrial ferric concentration and heme biosynthesis and plays a role in the maintenance of mitochondrial homeostasis and cell survival. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion."}
+{"protein": "MATDQKRGLLIVFEGLDRSGKSTQAKRLVESINKKSTESGDASSSPSAVLQAFPDRSSSIGKLIDQYLRKEIDMDEHALHLLFSADRFSKNQMIRDNIAKGIDVICDRYCYSGVAYSLAKGLPEQWVRSSDVGLPKPDAVLFFDVSPEVAAQRGGFGEERLETATIQQKVAAVMPTLRDDAYWKTVNADGDLDSVEKNVFRIYENLDREKPFESLEKI", "text": "FUNCTION: Catalyzes the conversion of dTMP to dTDP. SIMILARITY: Belongs to the thymidylate kinase family."}
+{"protein": "MEMTLFLNESYIFHRLRMWSIVLWHSCVFVCAECGNANYRVPRCLIKPFSVPVTFPFSVKKNIRILDLDPRTEAYCLSPYSVCSKRLPCKKYFYLLNSYNIKRVLGVVYC", "text": "SIMILARITY: Belongs to the UPF0377 family."}
+{"protein": "MAKLIFLTGLAFLLNAQLGSAYQLVCYFSNWAQYRPGLGSFKPDNIDPCLCTHLIYAFAGMSNSEITTIEWNDVALYSSFNDLKKKNSQLKILLAIGGWNFGTAPFTAMVATPENRKTFISSVIKFLHQYGFDGLDFDWEYPGFRGSPSQDKHLFTVLVQETREAFEQEAKQTNKPRLLVTAAVAAGISNIQAGYEIPQLSQYLDFIHVMTYDFHGSWEGYTGENSPLYKYPTDTGSNTYLNVEYAMNYWKKNGAPAEKLIIGFPAYGHNFILRDASNNGIGAPTSGAGPAGPYTREAGFWAYYEICAFLKDGATEAWDDSQNVPYAYKGTEWVGYDNVNSFRIKAQWLKENNFGGAMVWAIDLDDFTGTFCNQGKFPLINTLKDALGLKSATCNASTQSSEPNSSPGNESGSGNKSSSSEGRGYCAGKADGLYPVADNRNAFWNCVNGITYKQNCLTGLVFDTSCHCCNWA", "text": "FUNCTION: Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding (By similarity). SUBCELLULAR LOCATION: Cytoplasm Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily."}
+{"protein": "MSMDVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSGSMVSKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELVPTADQCPAEELKEFAHVNRADSPPKEEQGRTILLDSEENSYLLFDDEQFVVKAFRLFHRIPSFGFSVVEKKRPGKLNAQKLKDLGVPPGPAYGKLKNGISVVLENGVTISPQDVLKKPIVGRKICILGDCSGVVGDGGVKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYKPVALAREGETDGIAELKKQAESVLDLQEVTLAEDFMVISIPIKK", "text": "FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity (PubMed:12711671, PubMed:32075755). Specifically involved in tRNA repair: acts downstream of the ribosome- associated quality control (RQC) pathway by removing a 2',3'-cyclic phosphate from tRNAs following cleavage by ANKZF1 (PubMed:32075755). tRNAs are then processed by TRNT1 (PubMed:32075755). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=Mainly cytosolic. SIMILARITY: Belongs to the RNase Z family."}
+{"protein": "MASSTFYIPFVNEMGEGSLEKAIKDLNGSGFKNALIVSDAFMNKSGVVKQVADLLKTQGINSAVYDGVMPNPTVTAVLEGLKILKDNNSDFVISLGGGSPHDCAKAIALVATNGGEVKDYEGIDKSKKPALPLMSINTTAGTASEMTRFCIITDEVRHVKMAIVDRHVTPMVSVNDPLLMVGMPKGLTAATGMDALTHAFEAYSSTAATPITDACALKAASMIAKNLKTACDNGKDMPAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGYYNLPHGVCNAVLLPHVLAYNASVVAGRLKDVGVAMGLDIANLGDKEGAEATIQAVRDLAASIGIPANLTELGAKKEDVPLLADHALKDACALTNPRQGDQKEVEELFLSAF", "text": "SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family."}
+{"protein": "MSEIILTPKEQPEVPLEAPNIKPDVFAGKSIDEIKNIQIMHGNEVVKLGDFFEVSGEPADAPEDIKIIIDGDVYNTKRIGQEMTAGEIIVRGNVNMYVGAGMKGGKITVEGNAGSWAGQDMRGGEIEILGDADDYVGSSYRGDWRGMSGGTITVHGNADNEIGEYMNGGKIIIKGDVNIMPGIHMNNGLIIIEGNVVARAGGEMAGGTIVVKGMMQEFLAGFKYLGVEKDIELMVKNSPGAFYKFEGDHAIKGAKGIVYAAVGCNGHIAP", "text": "FUNCTION: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile. SIMILARITY: Belongs to the FwdC/FmdC family."}
+{"protein": "MEMTLYSSSSFSLPSAPSNPSLSLFTSSFRFSSFKTSPFSKCRIRASLAVEQQTQQNKTALIRIGTRGSPLALAQAHETRDKLMASHTELAEEGAIQIVIIKTTGDKILSQPLADIGGKGLFTKEIDEALINGDIDIAVHSMKDVPTYLPEETILPCNLPREDVRDAFISLSAASLADLPAGSVIGTASLRRKSQILHRYPSLTVQDNFRGNVQTRLRKLSEGVVKATLLALAGLKRLNMTENVTSTLSIDDMLPAVAQGAIGIACRSNDDKMAEYLASLNHEETRLAISCERAFLTTLDGSCRTPIAGYASRDKDGNCLFRGLVASPDGTRVLETSRIGSYTYEDMMKIGKDAGEELLSRAGPGFFNS", "text": "FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the HMBS family."}
+{"protein": "MCSSRCLLFLATLAFLIHLSLARATPVSTPAQCLAHSQNLLRTTNHMLEKAIQTLKHYPCTAEDIDHEDITEDKTSTLNACLPPELAKNESCWASGKTSSVTRGSCLPPQKTSSMMTLCLSSIYEDLKMYQTEFKAINAELLDHNRKQIILDENMLTAIDELMQALNLNGETRPQKPSLEEADPYKVKIKLCILLHAFSIRAITINRVMSYLNSA", "text": "FUNCTION: Heterodimerizes with IL12B to form the IL-12 cytokine or with EBI3/IL27B to form the IL-35 cytokine. IL-12 is primarily produced by professional antigen-presenting cells (APCs) such as B-cells and dendritic cells (DCs) as well as macrophages and granulocytes and regulates T-cell and natural killer-cell responses, induces the production of interferon-gamma (IFN-gamma), favors the differentiation of T-helper 1 (Th1) cells and is an important link between innate resistance and adaptive immunity. Mechanistically, exerts its biological effects through a receptor composed of IL12R1 and IL12R2 subunits. Binding to the receptor results in the rapid tyrosine phosphorylation of a number of cellular substrates including the JAK family kinases TYK2 and JAK2. In turn, recruited STAT4 gets phosphorylated and translocates to the nucleus where it regulates cytokine/growth factor responsive genes (By similarity). As part of IL- 35, plays essential roles in maintaining the immune homeostasis of the liver microenvironment and functions also as an immune-suppressive cytokine (By similarity). Mediates biological events through unconventional receptors composed of IL12RB2 and gp130/IL6ST heterodimers or homodimers. Signaling requires the transcription factors STAT1 and STAT4, which form a unique heterodimer that binds to distinct DNA sites (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily."}
+{"protein": "MEGLDEKKPWGKLSRLLGAETDSSSELFLYKKEWTIGRKKACDLSFPGNKLVSGEHCKITVNEESGEVSLEDTSTNGTVINKLKVIRKQTYPLKNGDVIYVVYRKNEPEQNVAYLYKSLNQGQDSLHDPADTSGSEEAETQTLSSQDDQLSYEEPQPSTSTSSLFSTPTTSAIPGVQLESAEKSGESLGGHSSTSDASPAIRASIPKSNLSTQEQGSLGPPKKRIRTEDHWTTNKNFVPASCPIGASDESKTPSMKPDKMEETLTCIICQELLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPEKCRSEEDRCSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYTVCRQCPGFVRHSMQPPPYPPPSDTETSRTQGDAPSTSTNFPTATQEYVCPSHGSHVICTCCFQPMPDRRAEREHNSHVAPQQCTICLEPFCHMYWGCNRMGCFGCLAPFCELNLGDKCLDGVLNNNNYESDILKNYLASRGLTWKDMLNESLAAVQRGVFMLPDYRINGTTVLCYFCGLRNFRILTYQYRQNIPASELPVTVTSRPNCYWGRNCRTQVKAHHAMKFNHICEQTRFKN", "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": "MSSNKTSSFVPWKVATILKHQKTLEAVIQKAFLPGDPAEALNSSQFCETTAALDSTAPCKICQCLHQLCTHHSPDLSFYGDYAIICYYALHAPKTMASNLMLLADCLELIQLYFPDAPSPPPNINGLDIYLHFFVNRCFRLANTEKIMEWSNLDMLKTEFLRATLSGSLSGAFCFKTLWPSLTRAPVRMADECTCTPITNPGCGLDGGKLFHPACIGKDNFLDLILIFWKNTDAMTPANSLLADTLSRHQVYFQNLTPVETNASLDPSPALDTTQGPCLLSPALCLQKKNHTSSLCLLCECLASHSEAASVFQTFKHLVLNSINNKVKLLDRILFLQQDADSLSFIQDRELLKSVLVNCSPQEIHKHLFCDPLCALNSSLTDSVVLFGEVPDFEFTAFKATLATGNSLVHRSFQSCEILETLILLFKSLQTVKANKTTVSEIIKEVDASLKKHKFSLLSCYYTFNIYT", "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": "MDLTGSAFVIGASGIGKACALAFARYGVRGIVIADLTLEAASAVAAECKSQATHPHFLAEAVAIDVTKEESVYQAIAYAHQVLGRIDYAVNSAGVGVQLANEIAEASVSEFEKMFKVNVTGTFIVTRALSALMKTQDPVPVDEAVPARGVSRGSIVNVGSASGFVATPGMVQYTAAKHAVVGITKNAALDNAKHGIRVNSVCPSWVDTPMIRKAMDDIPELGEMIQKAVPLGRIALAEEVADAVMFLSSPKASYATGCNMILDGGTTLAAHV", "text": "FUNCTION: Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sordarial, a salicylic aldehyde structurally related to the phytotoxin pyriculol (PubMed:19277664, PubMed:28485098, PubMed:30908040). The most interesting aspect of this pathway is formation of an aromatic product from the highly reducing polyketide synthase srdA (PubMed:30908040). SrdA synthesizes a reduced polyketide chain from one molecule of acetyl-CoA and five molecules of malonyl-CoA (PubMed:30908040). The polyketide chain is then reductively released as an aldehyde (PubMed:30908040). The oxidoreductases srdC, srdD and srdE then oxidize one of the hydroxy groups to facilitate the intramolecular aldol condensation, followed by dehydration to yield a salicylic aldehyde (PubMed:30908040). This aldehyde can undergo facile reduction by endogenous reductases to yield the alcohol 1-hydroxy-2- hydroxymethyl-3-pent-1,3-dienylbenzene (PubMed:30908040). The flavin- dependent srdI counteract against the propensity of the aldehydes to be reduced under physiological conditions and is responsible for reoxidizing 1-hydroxy-2-hydroxymethyl-3-pent-1,3-dienylbenzene back to the salicylic aldehyde (PubMed:30908040). This salicylic aldehyde is then selectively epoxidized by the cupin-domain-containing oxidoreductase srdB to yield the epoxide, which can be hydrolyzed stereoselectively by the hydrolase srdG to give the final product sordarial (PubMed:30908040). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MVAITSLAQSLEHLKRKDYSCLELVETLIARCEAAKSLNALLATDWDGLRRSAKKIDRHGNAGVGLCGIPLCFKANIATGVFPTSAATPALINHLPKIPSRVAERLFSAGALPGASGNMHELSFGITSNNYATGAVRNPWNPDLIPGGSSGGVAAAVASRLMLGGIGTDTGASVRLPAALCGVVGFRPTLGRYPGDRIIPVSPTRDTPGIIAQCVADVVILDRIISGTPERIPPVPLKGLRIGLPTTYFYDDLDADVALAAETTIRLLANKGVTFVEANIPHLDELNKGASFPVALYEFPHALKQYLDDFVKTVSFSDVIKGIRSPDVANIANAQIDGHQISKAEYELARHSFRPRLQATYRNYFKLNRLDAILFPTAPLVARPIGQDSSVIHNGTMLDTFKIYVRNVDPSSNAGLPGLSIPVCLTPDRLPVGMEIDGLADSDQRLLAIGGALEEAIGFRYFAGLPN", "text": "FUNCTION: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid (IAA). FUNCTION: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid (IAA). SIMILARITY: Belongs to the amidase family."}
+{"protein": "MGEVTAEEVEKFLDSNIGFAKQYYNLHYRAKLISDLLGAKEAAVDFSNYHSPSSMEESEIIFDLLRDFQENLQTEKCIFNVMKKLCFLLQADRMSLFMYRTRNGIAELATRLFNVHKDAVLEDCLVMPDQEIVFPLDMGIVGHVAHSKKIANVPNTEEDEHFCDFVDILTEYKTKNILASPIMNGKDVVAIIMAVNKVDGSHFTKRDEEILLKYLNFANLIMKVYHLSYLHNCETRRGQILLWSGSKVFEELTDIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEFFDVWPVLMGEVPPYSGPRTPDGREINFYKVIDYILHGKEDIKVIPNPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFAFQKEPLDESGWMIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDEMDETLMESLTQFLGWSVLNPDTYESMNKLENRKDIFQDIVKYHVKCDNEEIQKILKTREVYGKEPWECEEEELAEILQAELPDADKYEINKFHFSDLPLTELELVKCGIQMYYELKVVDKFHIPQEALVRFMYSLSKGYRKITYHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKTLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYESEQEWTQYMMLEQTRKEIVMAMMMTACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTVLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEITPMLDGITNNRKEWKALADEYDAKMKVQEEKKQKQQSAKSAAAGNQPGGNPSPGGATTSKSCCIQ", "text": "FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP (PubMed:20940301). This protein participates in processes of transmission and amplification of the visual signal. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cell projection, cilium, photoreceptor outer segment. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family."}
+{"protein": "MAAAAASRAVGAKLGLREIRVHLCQRSPGSQGVRDFIVQRYVELKKAHPNLPILIRECSEVQPKLWARYAFGQEKTVSLNNLSADEVTRAMQNVLSGKA", "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 NDUFA2 subunit family."}
+{"protein": "MLADKVKLSAKEILEKEFKTGVRGYKQEDVDKFLDMIIKDYETFHQEIEELQQENLQLKKQLEEASKKQPVQSNTTNFDILKRLSNLEKHVFGSKLYD", "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 (By similarity). 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. 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": "MRIIKYLTILVISVVILTSCQSSSSQESTKSGEFRIVPTTVALTMTLDKLDLPIVGKPTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMSEEVKKMFQKEFKQNDIWKHFKAVKNNHVYDLEEVPFGITANVDADKAMTQLYDLFYKDKK", "text": "FUNCTION: Involved in heme (porphyrin) scavenging. Binds Fe(2+) and Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions as a high-affinity heme binding protein and probably has a role in relaying heme-iron from cell wall-anchored isd proteins receptors to the probable permease IsdF (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 8 family."}
+{"protein": "MGNRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQMSDRRENDMSPSNNVVPIHVPPTTENKPKMQCCQNI", "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. The small Rab GTPase RAB11A regulates endocytic recycling (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Recycling endosome membrane; Lipid-anchor Cleavage furrow Cytoplasmic vesicle, phagosome Cytoplasmic vesicle membrane. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "GICACRRRFCLNFEQFSGYCRVNGARYVRCCSRR", "text": "FUNCTION: Microbicidal activity and inhibits corticotropin (ACTH) stimulated corticosterone production. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MRQFVIIGHDAPTTPEFSLDDLAGAAGRLDVLCRCVTSAFFLSHAIREDVRVHLILGDEYTVTFEGSDLRRLNPDERSTAALIRKALEEREEAIGHIPVETSPGVSLTRRGFEGTLDDVARRGTVVQLHEDGDPIVGVAPPSDPVFVLSDHHDFRDEEAALLADRADERVSLGPKALHADHSITVAHNYLDTAGFERY", "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": "MVLMIVSGRSGSGKSVALRALEDMGFYCVDNLPVVLLPDLARTLADRQISAAVSIDVRNIPESPEIFEQAMNNLPGAFSPQLLFLDADRNTLIRRYSDTRRLHPLSSKNLSLESAIDKESDLLEPLRSRADLIVDTSEMSVHELAEMLRTRLLGKRERELTMVFESFGFKHGIPIDADYVFDVRFLPNPHWDPKLRPMTGLDKPVAAFLDRHTEVHNFIYQTRSYLELWLPMLETNNRSYLTVAIGCTGGKHRSVYIAEQLADYFRSRGKNVQSRHRTLEKRKT", "text": "FUNCTION: Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6- phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis. Under low GlcN6P concentrations, RapZ is sequestered and inactivated by an other regulatory small RNA, GlmY, preventing GlmZ degradation and leading to synthesis of GlmS. SIMILARITY: Belongs to the RapZ-like family. RapZ subfamily."}
+{"protein": "METRTLEDWRALLEAEKTLDSGVYNKHDLLIVRGQGARVWDAEGNEYIDCVGGYGVANLGHGNPEVVEAVKRQAETLMAMPQTLPTPMRGEFYRTLTAILPPELNRVFPVNSGTEANEAALKFARAHTGRKKFVAAMRGFSGRTMGSLSVTWEPKYREPFLPLVEPVEFIPYNDVEALKRAVDEETAAVILEPVQGEGGVRPATPEFLRAAREITQEKGALLILDEIQTGMGRTGKRFAFEHFGIVPDILTLAKALGGGVPLGVAVMREEVARSMPKGGHGTTFGGNPLAMAAGVAAIRYLERTRLWERAAELGPWFMEKLRAIPSPKIREVRGMGLMVGLELKEKAAPYIARLEKEHRVLALQAGPTVIRFLPPLVIEKEDLERVVEAVRAVLA", "text": "FUNCTION: Catalyzes the transfer of the amino group of L-glutamate to [LysW]-aminoadipate 6-semialdehyde, generating [LysW]-gamma-L-lysine (Probable). In vitro, can use N(2)-acetyl-L-ornithine and N(2)-acetyl- L-lysine (PubMed:11489859). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. LysJ subfamily."}
+{"protein": "MPLVELLTSAALGLSLQLLHDAIIRAKERSLITRCILDRLDATLHKITPFVIKIDTLTEEVDEPFRKVIEELKRLLEKAIRLVDAYAELKLRNLLRKYRYKRRIKELDSSLRWMIDVDVQVNQWLDIKKLMGKMSEMNTKLDDITRQPMDIIEATGRSSEEDGCTKPTIDIHFRWKNQTKEHEIRFIFK", "text": "FUNCTION: Probable disease resistance (R) protein. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the plant RPW8 protein family."}
+{"protein": "LGKLLDVYESRLLDVYESRVLDIYESRLGKVLDIYESR", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. In plants, may have a detoxification role against certain herbicides (By similarity). SIMILARITY: Belongs to the GST superfamily. Phi family."}
+{"protein": "MSGLWRLRNLKSLALHARSISPVSNLYSLELGSCPRRRIQERFKSEQGGGGGGGDDFPVPVTRRKLRAEPNCPRCSKQMDLLFSNRQFPSSNLLQRPDDSDSSGAGDKTNFQSVNFCPTCKTAYGFNPRGVSPLQGTFIEIGRVQSPTTTTTNATTSKSTRKQQQHSKDPNQGFNYRNKLRSSFWDTLRSYGAEPPEDWSPPPPHSPLNSSPPNTIPVNASPSAVDTSPLPDAVNDVSRWGGAGLGRDFPTPKEICKWLDKFVIGQSRAKKVLSVAVYNHYKRIYHTSMKKGSAAQPIDDDDNVELDKSNVLLMGPTGSGKTLLAKTLARLVNVPFVIADATTLTQAGYVGDDVESILHKLLTVAEFNVQAAQQGIVYIDEVDKITKKAESLNISRDVSGEGVQQALLKLLEGTIVNVPGKGARKHPRGDHIQIDTKDILFICGGAFVDLEKTIVDRRQDSSIGFGAPVRANMATSGVTSGAITSSLLESVESADLTAYGLIPEFVGRFPILVSLSALTEDQLIRVLVEPKNALGKQYKKLFSMNNVKLHFTEKALEIISKQAMVKNTGARGLRALLESILTEAMFEIPDDKKGDERIDAVIVDEESTSSEASRGCTAKILRGDGAFERYLSENKSKDATEPMVDERVGSAKAMRL", "text": "FUNCTION: ATP-dependent specificity component of the mitochondrial Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ClpX chaperone family."}
+{"protein": "MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLRETLVIFVADMSRPWTIMESLQKWASVLREHIDKMKIPPEEMRDLERKFMKDFQDYIEPEEGCQGSPQRRGPLTSGSDEDNVALPLGDNVLTHNLGIPVLVVCTKCDAVSILEKEHDYRDEHLDFIQAHLRGFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTIPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQESPARGPSGSPRTQGRGGPASVPSASPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPSAGGVQSTAKKSGTEGEPQSFRSLTEQCCQTGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA", "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. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the dynein light intermediate chain family."}
+{"protein": "MERREGGRDNSSCSNVNQLFGVKDSESLLYDDVFIVRDRNGDSYFAYWDIEKNTFLSEPFYSYRSRNSSYLPKIKAFMSEDRSQIHEVKNGFRSEDHSKINKINGVENLFHNYNMNVLTDDYNFKMGMNGFHRPQSKIHINRFIDSYLQSQICIATTPGSGSDNDSYIHGSRVYGESESYTRSEGRSSSIRTRTKGVELTLRERPGILDRTKKYMYLWLQCDNCYGLNYKKVLKSKMTICEQCGYHLQMSSSDRIELLIDPGTWDPMDEDMVSRDPIKFDSGGGEAYKDRLYFYQRKTGLTEAVQTGIGQLNGIPVAIGVMDFKFMGGSMGSVVGEKITRLIEHATNKFLPLIIVSASGGARMQEGSLSLMQMAKISSALYDYQSNKRLVYVSILTSPTAGGVTASFGMLGDIIIVEPRAYVAFAGKRVIEQTLNQTIPNDSQEAEFLFHKGLFDLIIPRHLLKSVISELFTLHDLFPLNQNSNQYSQYRALLNPIF", "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. SIMILARITY: Belongs to the AccD/PCCB family."}
+{"protein": "MDDLESTCASLRAQISATETQLAGLKRALHEAEQAAAHAKAQSAAATTAGDNHDKPRRWPLLDEEYRRYGRQMIVPQLGLPGQLKLRSARVLIVGAGGLGCPAALYLAGAGVGTLGLIDGDMVDVSNLHRQVLHRSANVGKLKVDSAIEYLRELNPHPTYIPHRAHLTPQEAPEIFQNYDVILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNNPPRPAGDKTGGPCYRCVFPKPPPANSILSCADGGILGPVVGTMGVLQALEAIKVITSTEDEVRPPSLHIFSAYSSPPFRSIKLRSRRANCAVCSAERQVTLDTLRSGLTDYVFFCGSVSPEAVLTAEERIAPREYRAMYPAPTEGAPEKTPTLIDVREKVQYDICNLAESINIPISTIQASAAGSGDETGSSLPAWLPPEIASTDSTDPIYVVCRMGNDSQLAVRRLKELGLDRGGARVVADIQGGFRAWREQVDPEWPEY", "text": "FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (- COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily."}
+{"protein": "MNGYGSPYLYMGGPVSQPPRAPLQRTPKCARCRNHGVLSWLKGHKRYCRFKDCTCEKCILIIERQRVMAAQVALRRQQANESLESLIPDSLRALPGPPPPGDAAAAAPQPPPTSQPSQPPPPQRPAAELAAAAALRWATEPQPGALQAQLAKPDLTEERLGDGSSADNTETFSDKDTDQRSSPDVVKSKGCFTPESPEVVSVDEGGYAVQKNGGTSESRPDSPKYHGEQNHLLIEGPSGTVSLPFSLKANRPPLEVLKKIFPNQKPTVLELILKGCGGDLVSAVEVLLSSRSSASAADRTSAEPESLVLPSNGHIFEHTLSSYPISSSKWSVGSAFRVPDTLRFSADSSNVVPNPLAVPLQHPFPQPPRYPLMLRNTLARNQSSPFLPNDVTLWNTMTLQQQYQLRSQYVSPFPGSSPSVFRSSPVLPTRAPEDPRISIPDDGCPIVSKQSLYTEDDYDERSDSSDSRILNTSS", "text": "FUNCTION: Probable transcription factor that plays a role in configuring the spinal circuits controlling stride in vertebrates. Involved in neuronal specification within a specific subdivision of spinal cord neurons and in the development of a coordinated locomotor network controlling limb movements. May regulate transcription during sexual development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DMRT family."}
+{"protein": "MSRIGKKPINLPQNINITIIENNVQIQGPKGELSYKIPKLIQIKQDTKNNKLFLYKTEDNKEAQKLHGLCRTLINNMIIGVSQGFEKKLQIQGVGYRSQLDGDNLLLNVGYSHTVIVKPPKNIILEVENNTSITIKGIQKEQVGEIAAQIRRIRPPEPYKGKGIRYLNETINLKVGKSGK", "text": "FUNCTION: Binds 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL6 family."}
+{"protein": "MPSRRRTLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVQFEDRLFTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNSVKSFDNLNNWREEFLIQANPSDPENFPFVVIGNKIDIDGGNSRVVSEKKARAWCAAKGNIPYFETSAKEGINVEEAFQTIAKDALKSGEEEELYLPDTIDVGNSSQPRSTGCEC", "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": "MAKVSELYDVTWEEMRDKMRKWREENSRNSEQIVEVGEELINEYGSKLGDDIWIIYEQVMIAALDYGRDDLALFCLQELRRQFPGSHRVKRLTGMRFEAMERYDDAIQLYDRILQEDPTNTAARKRKIAIRKAQGKNVEAIRELNEYLEQFVGDQEAWHELAELYINEHDYAKAAFCLEELMMTNPHNHLYCQQYAEVKYTQGGLENLELSRKYFAQALKLNNRNMRALFGLYMSASHIASNPKASAKTKKDNMKYASWAASQINRAYQFAGRSKKETKYSLKAVEDMLETLQITQS", "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; Peripheral membrane protein; Cytoplasmic side Note=May also localize to the nuclear envelope. SIMILARITY: Belongs to the EMC2 family."}
+{"protein": "MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAERVGIENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHTRQSPFLVTLHYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVMLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQHLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAALPQSSEKLFQGYSFVAPSILFKRNAAVIDPLQFHMEVERPGVTNVARSAMMKDSPFYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDENDNLEIKIIDFGFARPKPPDNQPLKTPCFTLHYAAPELLNQNGYDESCDLWSLGVILYTMLSGQVPFQSHDRSLTCTSAVEIMKKIKKGDFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRLKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGAAVHTCVKATFHAFNKYKREGFCLQNVDKAPLAKRRKMKKTSTSTETRSSSSESSHSSSSHSHGKTTPTKTLQPSNPADSNNPETLFQFSDSVA", "text": "FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress- induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro- inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury (By similarity). Phosphorylates TRIM7 at 'Ser-107' in response to growth factor signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin ligase activity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily."}
+{"protein": "LKDGYIVDDKNCTFFCGRNAYCNDECKKKGGESGYCQWASPYGNACWCYKLPDRVSIKEKGRCN", "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. Is active on mammals and bind with high affinity to rat brain synaptosome. Does not display phospholipid-binding activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
+{"protein": "MLPLLDSVSLPYLILSACLSVILLRRFLAHDKGGSKSIAQGCLPEPRLRQWDPIFGFGIVISQARALRGHRYLEWLRDLHASMPHTKTFSANYGGYRWIFSIEPEILKAVYATNLQNFGVEPIRQHPPGFQPFAHKGVSTSDGDDWSFSRTLIKPFFERSVYISTDRIKPFADKFMTLLPDDGETFDIQPLLQRWFLDITSEFIFGKSQDSMTHADRAEVTWAMADVLRGGRQRAQTHRILWAFNWDWWFEAVEKVHGFLNPYIRSTLKELEERQQRIKDGLPVDEERTDLLWSMATMLPDEEELRSQVCLIFVPNNDTTSMFIGHCLYFLARNSNAWKRLRDEVDAVGDAPITFEMLRNMKYLNGILNETHRLIPNNVTQVRAALSDVVLPLGGGPNGKAPLDVRKGDIVSVTKTVMYRDPEQWGPDANEYRPERWDGMRGGWHFLPYGGGPRRCPAQMMVQNESAYMLFRLAQKYSTIVARDPEPFRARMRIGPSSMHGVKIAFYK", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection (PubMed:17216664, PubMed:19067514, PubMed:20575135, PubMed:34903054). TenA catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to the production of pretenellin B and pyridovericin, respectively (PubMed:19067514, PubMed:34903054). The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13- hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl- 15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined (PubMed:34903054). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "NQEGLFHGR", "text": "FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) 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. 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 antibacterial immune response via both innate and T-cell mediated pathways. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MEDERGRERGGDAAQQKTPRPECEESRPLSVEKKQRCRLDGKETDGSKFISSNGSDFSDPVYKEIAMTNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESSAGDSYYDYICIIDFEATCEEGNPAEFLHEIIEFPVVLLNTHTLEIEDTFQQYVRPEVNAQLSEFCIGLTGITQDQVDRADAFPQVLKKVIEWMKSKELGTKYKYCILTDGSWDMSKFLSIQCRLSRLKHPAFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHSGLDDSKNIARIAVRMLQDGCELRINEKILGGQLMSVSSSLPVEGAPAPQMPHSRK", "text": "FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Required for binding the 5'- ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA (PubMed:18438418). Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs. In vitro, does not have sequence specificity. In vitro, has weak DNA exonuclease activity. In vitro, shows biphasic kinetics such that there is rapid hydrolysis of the last three unpaired RNA nucleotides in the 39 flanking sequence followed by a much slower cleavage through the stem that occurs over a longer incubation period in the order of hours (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, nucleolus."}
+{"protein": "RETLDAVALLYMATQIASGMSYLEARNYIHRDLAARNCLVGDNKLVKVADFGLARLMRDDTYTAHAGAKFPIKW", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily."}
+{"protein": "MYSKIRIVGKIDVLTGLHIGGGGETSMIGAIDSPVVRDPYSRLPIIPGSSIKGKMRSLLAKHIGLIPGQKMHNQDAPEILRLFGSSQKGAIQSSRLQISDAFFSKASQEEFDKKDLAYTETKFENTISRLTAVANPRQIERVTRGASFDFHIIYNVENINEVMADFENIKTAIHLLENDYLGGGGTRGNGRIRFVIDSIDTVVGDFDSSNLSIK", "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). 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. In a heterologous host the appropriately targeted Csm effector complex prevents growth of dsDNA phage phiNM1-gamma6. FUNCTION: This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals. SIMILARITY: Belongs to the CRISPR-associated Csm3 family."}
+{"protein": "MLNTARLDNPAVIFDNGSGLCKVGISGEIVPRHVINSVVGHPKFNIPSARSNRKRYFVGEEAQCMYDGLYLHYPIERGLVTRWDDMEKLWKDLFEWELGVKPNEQPVFMTEPSLNPRETREKTTEIMFEKFNVPALYLCNHAVGALCASACITGLVLDSGDGVTCTVPIYEGYSLPRAITKLYVAGRDITEHLTRLLLAKGYTFPCILNKAVVDDIKEKLCTVSWGSKDSEKCYQRSLSEYKLPDGNTIQMSDHLCQVPEVLFTPEHLGIHDLGISKMVCNSIMKCDTDIQENLFAEIVLSGGTTLFPGLQDRLLKELEVLAFEGTPIKITASPDRCYSAWIGGSVMTSLTTFKQMWVTAEDFKEYGAFVVQRKCF", "text": "FUNCTION: Negatively regulates the Hedgehog (SHH) signaling. Binds to the promoter of the SHH signaling mediator, GLI1, and inhibits its expression. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm Nucleus Note=Both detected in the nucleus and cytoplasm, localizes to the nucleus where it binds chromatin upon stimulation of the Hedgehog pathway. SIMILARITY: Belongs to the actin family."}
+{"protein": "MSGPMQRSSQPQFISSVERNNQSNGPGTPLIDSIDVDQIVIPEKNSWKNLFSYIGPGFLVSIAYIDPGNFETDLQAGAQYKYELLWIILIASCAALIIQSLAARLGVVTGKHLAEHCRAEYPKATNFILWILAELAVVACDIPEVIGTAFALNMLFKIPVWCGVLITGLSTLMLLLLQQYGVRKLEFLIAILVSLIATCFLVELGYSKPNSSEVVRGLFVPELKGNGATGLAISLLGAMVMPHNLFLHSALVLSRKVPRSVHGIKEACRFYMIESAFALTIAFLINISIISVSGAVCGSDNLSPEDQMNCSDLDLNKASFLLKNVLGNWSSKLFAVALLASGQSSTITGTYAGQYVMQGFLDLRMTPWIRNLLTRSLAILPSLIVSIIGGSSAAGQLIIIASMILSFELPFALVPLLKFTSSRTKMGQHTNSKAISVITWGIGSFIVVINTYFLITSFVKLLLHNGLSTVSQVFSGIFGFLGMLIYMAAILYLVFRKNRKATLPLLEGDSTVRIVGRDTATEGEGSLGHLPREDISSMQLPQQRTASDLD", "text": "FUNCTION: Probable metal transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP (TC 2.A.55) family."}
+{"protein": "MGSSSFLVLMVSLALVTLVAVEGVKKGIEKAGVCPADNVRCFKSDPPQCHTDQDCLGERKCCYLHCGFKCVIPVKELEEGGNKDEDVSRP", "text": "FUNCTION: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSGRRKGCSAATASSSSSSPPSRLPPLPGHARRPRRKRCLVPEVFCTRDLADLCVRRDYEGLRRYLRRFEGSCVSLGWPSQCIYVVGGEHSPHSLTEIDLEHCQNDFFGEFRALHLIGTVSHATCRYQVFVDAYGAVFAYDAQEDCLYELASDLAGFFAKGMIRCDPVHESICARLQPNVPLVHPDHRAELCRRSRASARGRYLRSLLAFRELLACEDTAARCAYVEAHREAQLTLIWPEKHSLVLRTARDLGLSASMLRRFQRSLYTREPVMPLGEIEGAEDKTFFHRVRILCGDTGTVYAALVGQDKLVRLARDLRGFVRVGLALLIDDFRYESIGPVDRSSLYEANPELRLPFKKRRLVVGYFDSLSSLYLRGQPKFSSIWRGLRDAWTHKRPKPRERASGVHLQRYVRATAGRWLPLCWPPLHGIMLGDTQYFGVVRDHKTYRRFSCLRQAGRLYFIGLVSVYECVPDANTAPEIWVSGHGHAFAYLPGEDKVYVLGLSFGEFFENGLFAVYSFFERDYVDEIVEGAWFKHTFAGMYELSQILHDRANLLRVCQLHAGSKIRLGGSPACTFTFGSWNVAEADEANNFVIGVLEQAHFVVIGWMEPVNKAVFMDAHGGIHVLLYGTMLVKLAETLRGFIRQGSFWFRCPRRFCFSPLDSSATVAAKPVSSHTSPAYDVSEYVFSGRSVLDSVSGTGAS", "text": "FUNCTION: Contributes to activation of immediate-early gene expression. SUBCELLULAR LOCATION: Virion Host nucleus Host cytoplasm Note=Expressed exclusively within the host nucleus in early times of infection and then present in both nucleus and cytoplasm at 72 hours post infection. SIMILARITY: Belongs to the herpesviridae US22 family."}
+{"protein": "MKRYLTWIVAAELLFATGNLHANEVEVEVPGLLTDHTVSSIGHEFYRAFSDKWESEYTGNLTINERPSARWGSWITITVNQDVIFQTFLFPMKRDFEKTVVFALAQTEEALNRRQIDQTLLSTSDLARDEF", "text": "FUNCTION: May be involved in the biogenesis of curli organelles. FUNCTION: May be involved in the biogenesis of curli organelles."}
+{"protein": "MVSTHNRDKPWDTDDIDKWKIEEFKEEDNASGQPFAEESSFMTLFPKYRESYLKTIWNDVTRALDKHNIACVLDLVEGSMTVKTTRKTYDPAIILKARDLIKLLARSVPFPQAVKILQDDMACDVIKIGNFVTNKERFVKRRQRLVGPNGNTLKALELLTKCYILVQGNTVSAMGPFKGLKEVRRVVEDCMKNIHPIYHIKELMIKRELAKRPELANEDWSRFLPMFKKRNVARKKPKKIRNVEKKVYTPFPPAQLPRKVDLEIESGEYFLSKREKQMKKLNEQKEKQMEREIERQEERAKDFIAPEEEAYKPNQN", "text": "FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth. FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the KRR1 family. SIMILARITY: Belongs to the KRR1 family."}
+{"protein": "MPLFDLISPKAFVKLVASEKVHRIVPVDATWYLPSWKLDNKVDFLTKPRIPNSIFFDIDAISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRVGNFSSPRCAWTLGVMGHPKVYLLNNFNQYREFKYPLDSSKVAAFSPYPKSHYESSESFQDKEIVDYEEMFQLVKSGELAKKFNAFDARSLGRFEGTEPEPRSDIPSGHIPGTQPLPYGSLLDPETKTYPEAGEAIHATLEKALKDFHCTLDPSKPTICSCGTGVSGVIIKTALELAGVPNVRLYDGSWTEWVLKSGPEWIAENRD", "text": "FUNCTION: Required for formation of the 2-thio group of the 5- methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs. SUBCELLULAR LOCATION: Mitochondrion Cytoplasm."}
+{"protein": "MSDADVSKQIQQMVRFIRQEAEEKANEISVSAEEEFNIEKLQLVEAEKKKIRQEYEKKEKQVEIRKKIEYSMQLNASRIKVLQAQDDVVNAMKESASKDFLNVSHDHHVYKRLLKDLIVQSLVRLKEPGVLLRCRKEDLHLVESVLDSAKEEYASKVNVHPPEIIVDDVHLPPGPSHHHGFFHHHAEAHGPFCSGGVVIASRDGKIVFENTLDARLDVAFNKKLPEIRKWLFGQVAA", "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": "DYMGWMDF", "text": "FUNCTION: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family."}
+{"protein": "MGNPVVIKAKKDYDCVFEPEPMSWLRLQYYRYQVTAGTYLFTYKEAFVFNTVVFIIVFLTGWAAKSIIVKLLPSLWRLSTLIPSFFASFFMSLLGKDASSQ", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
+{"protein": "IIYPGTLWCGNGNIANGTNELGLWKETDACCRTHDMCPDIIEAHGSKHGLTNPADYTRLNCECDEEFRHCLHNSGDAVSAAFVGRTYFTILGTQCFRLDYPIVKCKVKSTILRECKEYEFDTNAPQKYQWFDVLSY", "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": "MSDAATRRLMKELAQLKSEAPEGLLVDNTSTSNDLKQWKIGVVGAEGTLYAGEVFMLQFTFGPQYPFNSPEVMFVGETIPAHPHIYSNGHICLSILSDDWTPALSVQSVCLSILSMLSSSKEKKHPIDDAIYVRTCSKNPSKTRWWFHDDSV", "text": "FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (By similarity). Together with ubc-18, required for the ubiquitination of membranous organelles, and the removal of paternal mitochondria from early embryos (PubMed:31153831). SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "MTVSCSKVLLSLCLFLMLLKATHESNQQRTNFREFFEIQLAQETREINEKNNQPLNQQLPQLNRRKRLWRDEDRRTFCTTLCPCEDRRKRAAVTPPTRKVPCCCP", "text": "SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scolopendra neurotoxin 10 family."}
+{"protein": "MDQLPAAELTNFISPSGPESRPVFHSICGIHDTANVQQKQTLDQNKVISAPLDYLLSFPGKDIRGQLISSFNEWLQIPEEKLSLIKRVVELLHTASLLIDDIQDSSQLRRGLPVAHNIFGVAQTINSANYAYFKAQSELHKIGDPRAVEIFTEELLRLHKGQGMDLYWRDSLTCPTEEEYLEMVSNKTGGLFRLAIKLMQLCSASEKDCVPLVEYLGIIFQIRDDYQNLQSEKYIENKGFGEDLTEGKFSFPIIHSIRSNSDSFQLINILKQKSEDTTVKLYAIKLLESTGSFEFCRQRIAQLTTQARSLLMEMGDPSQTAGIQGILAFLELK", "text": "FUNCTION: Geranylgeranyl pyrophosphate synthase; 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). SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MGSGLPLVLLLTLLGSSHGTGPGMTLQLKLKESFLTNSSYESSFLELLEKLCLLLHLPSGTSVTLHHARSQHHVVCNT", "text": "FUNCTION: Putative surfactant protein. SUBCELLULAR LOCATION: Secreted Cytoplasmic vesicle, secretory vesicle Golgi apparatus."}
+{"protein": "MKLLELIEKWAIETPDQTAFVWRDAKITYKQLKEDSDALAHWISSAYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLLLSAAAVTVTDLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSESMLPNMKTFLFCGEVLPNEVARKLIERFPNATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEVTA", "text": "FUNCTION: Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. 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 ATP-dependent AMP-binding enzyme family. DltA subfamily."}
+{"protein": "MKLKQRVVLLAILLVIFIFTKVFLIDNLDTSAANREDQRAFHRMMTGLRVELAPKLDHTLQSPWEIAAQWVVPREVYPEETPELGAVMHAMATKKIIKADVGYKGTQLKALLILEGGQKVVFKPKRYSRDHVVEGEPYAGYDRHNAEVAAFHLDRILGFHRAPLVVGRFVNLRTEIKPVATEQLLSTFLTVGNNTCFYGKCYYCRETEPACADGDIMEGSVTLWLPDVWPLQKHRHPWGRTYREGKLARWEYDESYCDAVKKTSPYDSGPRLLDIIDTAVFDYLIGNADRHHYESFQDDEGASMLILLDNAKSFGNPSLDERSILAPLYQCCIIRVSTWNRLNYLKNGVLKSALKSAMAHDPISPVLSDPHLDAVDQRLLSVLATVKQCTDQFGMDTVLVEDRMPLSHL", "text": "FUNCTION: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O- phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT- I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the FAM20 family."}
+{"protein": "MTPSLVFLIVVIVVVEGQGWRPWDRFNHPGNFGNWGGNNWGTRQRNQEPHDIPPPVPPPGFRGNNDRFGGNIIKVVEIIDLGKSKNRGDILSDFKDVHKKHRHLGRKEWKGKVKQFCHRFPGHPNCRRGKVPDQKELEEMIGQFSKGGIGRFLKRVPKIYIEDPLARVDPKLKGFLENAGRGFGHVSSEHVNKLRDICKRRKCREQPESAKKTRELFTQKLADFETKIAGKDKTDSVQLRFDRTLQIKEALLEKGNLTADIVPVDNGVYDLDTMLTEEQANILLNELNKAGVGDDEIPLPDADTDDEDDDDSTNSASGAAPGSSRLKKSALYFEGNLIKKWDPSSPIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPTGSHIVYYKVDSPTFCGLSYVGRADPANPVYLSFGCDNNKGVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKLYTSYGVKYAYDSIMHYNGYTAAQNIAIPTMNPKTNSAVNLKVLGQRQKMGTTDIELLKKMYCQPGCDDKNVYCGAWALKDLCKNPGHDQYMAANCKKSCGLCAIGK", "text": "FUNCTION: Metalloprotease. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MKITQLTTYRVPPRWMFLRIETDEGLIGWGEPVVEGHARAVQAAVHELEPYLIGQDPARINDLWQVMYRAGFYRGGAVFMSAIAGVDQALWDIKGKALGVPVYQLLGGLVRDRMRTYGWVGGDRPADVIDGIRQRVDAGFTHFKLNGCEELGIIDSSRAVDAAVARVAQIRAAFGNTVEFGLDFHGRVSVAMAAVLIKELEYLRPLFIEEPVLAEQAEHYPKLAAKTHLPLAAGERMYSRFEFKRVLAAGGIAILQPDLSHAGGISECLKIAAMAEAHDVAIAPHCPLGPIALASCLHVDYVSWNATLQEQGMGMHYNRGGEVLDYVLNPQDFRLDNGFIAPFTKPGLGVEINEALVLERSRDCPDWRNPVWRHADGSVAEW", "text": "FUNCTION: Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy- D-galactonate. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. GalD subfamily."}
+{"protein": "MPPAAPSVARSREGGGIGQRRLVFPKSARRTLPCPIALCLGLCLAAAAATTTRASAAAFASAGDTTAMSAFNLLHLVTKSQPVAPRACGLPSGSCRDKKNCKVVFSQQELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPAFHDVISSEAIEFTDDFSYGMHRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSASLSFTPADSSEAEGSGIKESGSPAAADRAEL", "text": "FUNCTION: Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine. SUBCELLULAR LOCATION: Endoplasmic reticulum Note=Not detected in the mitochondrion. SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family."}
+{"protein": "MRFNVVLFMLIVALLGGLSTCSSEVPIGFDTDELSFDMSLVLLTGDMQTKASDPNYTYATTEELTIQNCHVAVFDKDGKRIYFKNFYSKDLGEMKTIGNLSGYELQLEGVRTFGKEDKKVSVLVVANANNANNSPFDNLTTYDGVDNSYTAKTIAKGPVTASLLVKIGKSETTLKYNQDNAPVTVSLIQLSAKIEYTGVYKKENGELLEGFSLTKVAGLNASSKITIFNTSAVENGAFSDLAYPTTKPVTFYTYEISDAFKEVILSVQSGVEPKEYPFPANKFIKGNYYRIKGLKSSTEIEWVLENVEDKEVTLDPFE", "text": "FUNCTION: Putative component of the fimbrium tip. Fimbriae are filamentous appendages on the cell surface that mediate cell adhesion and biofilm formation. SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily. FimA/Mfa1 family."}
+{"protein": "MWLINWFYDLLASLGLLNKHAKLLFLGLDNAGKTTLLHMLKNDRVAILQPTAHPTSEELAIGNNRFTTFDLGGHQQARRLWKDYFPEVSGIVFLVDAKDHECFPESKAELDALLAMEELAKVPFLILGNKIDHPDAVSEDDVRHQLGLYQTTGKGKVPLEGIRPIEVFMCSVVMRQGYGEGIRWLSQYV", "text": "FUNCTION: Small GTPase 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. Sar1 controls the coat assembly in a stepwise manner. Activated Sar1-GTP binds to membranes first and recruits the sec23/24 complex. These sec23/24-sar1 prebudding intermediates are then collected by the Sec13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to sar1-GDP triggers coat release and recycles COPII subunits (By similarity). SUBCELLULAR LOCATION: 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 small GTPase superfamily. SAR1 family."}
+{"protein": "MSSTVSLLFCCLFLQLCPSAQQYHGEKGISVPDHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLEQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDNSPSGPTARPSPYLPDSITFQPHPHRDFTCPRQLKVPPYLAYRFLGEKDCGAPCEPGKANGLMYFKEEEVRFARLWVGIWAILCCISTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAYTAGFLLEERAVCVERFSEDSYRTVAQGTKKEGCTILFMILYFFGMASSIWWVILSLTWFLSAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDVLSGVCYVGINSVDSLRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVMYTVPATIVLACYFYEQAFRDTWEKTWLVQTCKGYAVPCPNYNFAPMSPDFTVFMIKYLMTMIVGITSSFWIWSGKTLQSWRRFYHRLSNGSKGETAV", "text": "FUNCTION: Receptor for Wnt proteins. Acts in both canonical and non- canonical Wnt pathways. Although different papers report differing Wnt preferences, wnt5a, wnt8b and wnt11 have been proposed as synergists. In the canonical Wnt pathway, acts via beta-catenin to promote the expression of the dorsal genes siamois, twin and nodal3 and to establish the dorsal axis of the embryo and induce dorsal mesoderm formation. In a non-canonical Wnt/planar cell polarity (PCP) pathway, acts with sdc4 and dvl2/dsh to regulate convergent extension cell movements during gastrulation. Triggers phosphorylation of dvl2/dsh and its translocation to the plasma membrane. In a third branch of Wnt signaling, acts in a non-canonical pathway via trimeric G proteins, and independently of dvl2/dsh, to recruit protein kinase C (PKC) to the membrane and thus activate PKC. PKC signaling controls cell sorting and tissue separation during gastrulation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Note=Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other conditions. SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family."}
+{"protein": "MSFVKDFKPQALGDTNLFKPIKIGNNELLHRAVIPPLTRMRALHPGNIPNRDWAVEYYTQRAQRPGTMIITEGAFISPQAGGYDNAPGVWSEEQMVEWTKIFNAIHEKKSFVWVQLWVLGWAAFPDNLARDGLRYDSASDNVFMDAEQEAKAKKANNPQHSLTKDEIKQYIKEYVQAAKNSIAAGADGVEIHSANGYLLNQFLDPHSNTRTDEYGGSIENRARFTLEVVDALVEAIGHEKVGLRLSPYGVFNSMSGGAETGIVAQYAYVAGELEKRAKAGKRLAFVHLVEPRVTNPFLTEGEGEYEGGSNDFVYSIWKGPVIRAGNFALHPEVVREEVKDKRTLIGYGRFFISNPDLVDRLEKGLPLNKYDRDTFYQMSAHGYIDYPTYEEALKLGWDKK", "text": "FUNCTION: Flavin-dependent enoate reductase that catalyzes the chemo- and stereoslective hydrogenation of electron-poor alkenes. The enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta- unsaturated aldehydes and ketones can act as electron acceptors to complete catalytic turnover. The physiological oxidant remains elusive. SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family."}
+{"protein": "MELEAVLKERTAAAGDPGRVLGAWVRSGWSAAGPSVLESEGGSGGPLAFESTSSRILELASKDNEPEYEALPDGSNVTTHMLAGAVAGVMEHCLMYPVDCVKTRMQSLQPDPAARYRNVMDALSKIVRTEGFWRPLRGLNVTATGAGPAHALYFACYEKLKKTLSDIIHPGGNSHIANGTDYSCPA", "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": "MSNLLGPRDANGIPVPMTVDESIASMKASLLKKIKRSAYVYRVDCGGCNGCEIEIFATLSPLFDAERFGIKVVPSPRHADILLFTGAVTRAMRSPALRAWQSAPDPKICISYGACGNSGGIFHDLYCVWGGTDKIVPVDVYIPGCPPTPAATLYGFAMALGLLEQKIHARGPGELDEQPAEILHGDMVQPLRVKVDREARRLAGYRYGRQIADDYLTQLGQGEEQVARWLEAENDPRLNEIVSHLNHVVEEARIR", "text": "SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
+{"protein": "MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLSRPL", "text": "FUNCTION: Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1- methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway (PubMed:8182091, PubMed:21823666, PubMed:23455543). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases. Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3 (PubMed:26571212, PubMed:23455543, PubMed:31043742). In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (PubMed:26571212). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis. In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway (By similarity). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (By similarity). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (PubMed:30044909). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family."}
+{"protein": "MKKKWKPSASIKDLMKRSKIIADIRSFFLKKNIMEVETPILSQSGVTDVNLMPFITNYFSFNDNIKKKNLWLITSPEYHMKRLLSAGSGSIYQICRSFRNQEFGQYHNPEFTMLEWYQLSCSMEKMIEEIDFFFQKILNFNKADKISYQEVFMKFLKIDPLSTSLSELFQCYKKFNLKNLIYLENDLNQLIENIFTLQIQPFLGKEKPLFVYHFPSEQACLASINKKDSRVSERFEIFFKGIELGNGFHELTDYFEQRKRFIKDNRKRCDMNLPEQKIDDYFLDAIHHGLPTCSGVAIGLDRLIMIALNKNSIDQVMSFSFERS", "text": "FUNCTION: With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily."}
+{"protein": "MSTFFTNLRRVNKVYPNQATFLTDNTRLLTTTPAGFTNVLRAPSTRNLGNGRFEPGYNLSNNQFVSAGDINRITRGNDVPRIRNVFQGISDPQIGSLNQLRRADNVPDAGLHVKRTRSDAVKQNFPETNVRSADGVDRALQQNPRLNTYLQGAKTAGVGVLLAGGAYLTFSAATLVQDIIQALNNTGGSYYVRGADGGDTADACLLLSRTCQRDPNMNTSDVVICNHDPLIADTAQLQAICSGFNYQQEQTVCRQSDPAADPDSPQFVDVSDLLPGQTIMCIEPYNLGDLIGDLGLDHLLGEDGLVGKSSNSSDSVSNKLMPLIWLIGAVLFLGLIIYLIYRFVIKGGAGAAGAARAPPVIVLPPPPTQQTYNSTKQQI", "text": "FUNCTION: Structural protein that is specific for occlusion-derived virus (ODV) envelopes but not of budded virus (BV). SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Note=Localized to the envelope region of preoccluded bundles of virions. SIMILARITY: Belongs to the baculoviridae E56 family."}
+{"protein": "MGVVVAETSQNGDISLLSEKKFTVPQPPSIEEFSIVKPISRGAFGKVYLARRKNNNKLFAVKVVKKADMINKNMVQQVQAERDALALSKSPFIVHLYYSLQSANNIYLIMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLKRELSMMDILTTPSMAKPKRDYSRTPGQVLSLISSLGFNTPVGGRTQGSIAQQTEGMRGNASTPLLMKKKENSVKGNKLMISCPEAGLSSPSMPVKCLTPNLLKCRTPFTTSSTSSQSRICLSSLESECGMSPRWENCSQDAEAPPYLNSSRVKDCSSEQARSKKPMGSSASQNLKHLEFAFSPIVDRRTGKKAGFQDETGELSDTPLATLGAKGVIRKCLYDNNAQEKHKDLGKDDQGELEKLTISPDSPPWLANGSVAPIQFNDDEIIEKMGIKRNYDLVEKSPEQEVLQDKKTNTDYKRGCTITGYPVSQSTGLTMEINSLFLSELRSSTNNYASDRKSEDDYISAPRTHENLGSGNTIAKNLLCELDDNCERDGEANSNSGCEEGENQKESLNQDSESSSADMSVTENQIERELCQVDKSIKELSFEESPSESNEETTPENKGMAFMAENDALKREPNRSVLPETLHNVLASPAPTSAMAHPRRKPMVAFRSYNSPINGSNLSEPSRISMNSADKIHFSLGCTGSFPMAVTPAQKKVQGLTETPYRTPKTVRRGGLQAENERILGTPDYLAPELLLGKSHGPAVDWWALGVCLFEFLTGIPPFNDETPSQVFQNILNRDIPWPEEEETLSVNAQSAIEILLAIDQTKRAGLKDLKAHHLFHAIEWDDLQNLPMPFIPQPDDETDTTYFEARNNAQHLKVSGFSL", "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- 67', 2 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": "MPSDRPFKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSVSTPIADIYEQEKDEDGFLYMVYASQETFGF", "text": "FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20713600, PubMed:24290141). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20713600). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006538, PubMed:31006537). SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor Endomembrane system; Lipid-anchor Cytoplasm, cytoskeleton Note=LC3-II binds to the autophagic membranes. SUBCELLULAR LOCATION: Endomembrane system; Lipid-anchor Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor Cytoplasmic vesicle, autophagosome Cytoplasm, cytoskeleton Note=LC3-II binds to the autophagic membranes. SUBCELLULAR LOCATION: Endomembrane system; Lipid-anchor Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor Cytoplasmic vesicle, autophagosome Cytoplasm, cytoskeleton Note=LC3-II binds to the autophagic membranes. SIMILARITY: Belongs to the ATG8 family."}
+{"protein": "MKMTGWKKKLCRGHHLWALGCYMLLAVVALRLSLRLKCDVDSLDLESRDFQSQRCRDILYKNLKLPAKRSINCSGITRGDQEAVVQALLDNLEVKKKRLPFTDTYYLNITRDCERFKAQRKFIQFPLSKEELDFPIAYSMVVHEKIENFERLLRAVYAPQNIYCVHVDVKSPETFKEAVKAIISCFPNVFMASKLVPVVYASWSRVQADLNCMEDLLQSSVPWKYLLNTCGTDFPIKTNAEMVLALKMLNGKNSMESEIPSEYKKNRWKYRYEVTDRLYLTSKMKDPPPDNLPMFTGNAYFVASRAFVQHVLENPKSQRLIEWVKDTYSPDEHLWATLQRAPWMPGSVPYHPKYHISDMTAIARLVKWQDHEGDVSMGAPYAPCSGIHQRAICIYGAGDLYWILQNHHLLANKFDPRVDDNVLQCLEEYLRHKAIYGTEL", "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": "MKEMVDYGIIGFLIFLSVIVIAIAIERLWFFATLRVDDYTDRRKLELALHKRLTLVATIGSNAPYIGLLGTVMGIMLTFMDLGSASGIDTKAIMTNLALALKATGMGLLVAIPAIVIYNLLVRKSEILVTKWDIFHHPVDTQSHEVYSKA", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ExbB/TolQ family."}
+{"protein": "MSSHITLIKTNTNNENKMTQFNYKVDNDVMIIRAMVNNVAKQMTPVWPLEKFIACNALHGFESMSFEEAVIQNQTAKKGTPFNEKLERVNWHMIKWCGSFLDIGQGTLEMPHRDKGLYFGFLKLAPFDSALHQNSKSIKSWLSNLPEMPEQAIRLCLDKLGVLNQKQEDFLQSTLSHLPGWAGYIKWISEWKNRNGKEENPVSLVDFIAVRLVITCILWPEASQEEKKKKKDSADTKQLIQNIKNKEDDYRQLLLKKLLPELSKAHIKENRANAQMVFCIDVRSEPFRRCIEKLGHYETLGFAGFFGLPVSIKDYDGETIKDSCPVLLKPRFNIHEKAIAANEHCLEHHEKGKEFKNILNRVYQQLKYNFSTPFALVESLGIWCGITMFLKSCSPIFARRLTKDLNEMICPSIQTQPVFELDLLEKEVGISLQEQIAYAEMALRLMGLTDNFAKLVIFCGHGSSTQNNPYASALDCGACGGNQGGKNAQLLASILNKIIVRRALAENGINIPQDTLFYGAQHDTTTDEVEIYHSNVSQFIHQDILDQLRTDLNMAKHNNNLERINYLNSIDCAEKDIARRSTDWSETRPEWGLARNAAFIVAPRQLTKNINLEGRCFLHSYDWSQDKDGALLETILTAPMVVAQWINTQYLFSTIDNVAYGSGSKITHNVAGKIGVMQGNASDLMHGLPLQSVMSHDDKSFHEPQRLLTIVYAPREIISELVEKHDVLKTLFFNEWVHLVAIDPRSHLFYKLEKTNNWSVIQ", "text": "FUNCTION: Part of an energy-coupled inorganic carbon pump. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family."}
+{"protein": "MGKAKNKKKVLKNKQQVLVPGILFVHPKKGFGFVSPDQPDLYPFDIFVPASDLKGALDGDHVLVALPFSQRGGEKRKGVIHKVLSRGKTVLVGTIISLISPTLAMVCVNAISPEVPLKAELLPKRTYKIGDRLLLKTPGWKENYPSKEPPPLAMLEFMGNISNAKTDFPVIKAEFSITEEFPEAVVQEASQFLQKHVTQALHSRKDLRDLLCFTIDSASAKDFDDAVSLTYDHEGNYILGVHIADVSHYVTPNSALDQEAAKRCNSIYFPGKVIPMLPSALSDNLCSLKPNVDRLAVSVFMTFSKEGFLSDYRILRSVIRSKYRMTYDEVDEIIEKKLAHPISKTILEMAELSRIFSDIREQRGCTRLVLPSFTMSLDNLQEPVALVENKQTAAHKLIEEFMLKANEVIAYHISHQGITMPFRIHEPPNEENLLLFRETAKAMGFTITQTPTQEPDYQYLLQETSAGHPLEPILHSQFVRSMKTASYSTENKGHYGLCLDYYTHFTSPIRRYVDLIVHRLLFHPLSVEEGHLEQIVRACSSQERVAAKAEGAFINIKKARFLKKFLDEQPATLYKAFIITVSPEGLSFVLPELCHEGFIPAAKLPKKYVIKTKLGLEELPEHLLPGIPISVQLASVTLLTQAIEWTLIESKERSSSKKKKAKAKSNATQVKKKSSSKKKKAVSKAKKNRGGK", "text": "FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily."}
+{"protein": "MNSNLLVLPILLPLLCALVLVFTKEKNRLSKILYIGTMSVNTVISLCLLIYVLQHKPITLDFGGWAAPYGIQFLGDSLSLVMVTVASFVVTLIMSYGFGRGEDRVNRYYLPTFILFLTTGVIGSFLTSDLFNLYVMFEIMLLASFVLVTLGQSVEQLRAAIIYVVLNIVGSWLFLLGIGLLYKTVGTLNFSQVALRLDQIHDNKAIIIISIVFIVAFGSKAALVLFMWLPKAYAVLNTELAALFAALMTKVGAYALIRFFTLLFDQHTGVTHPLLVFMSCITMLIGAFGVIAYRDIKKVASYQVILSIGFVILGLGSNTFAGVHGAIFYLANDIIVKTMLFFIIGSLVYMSGYREYKYLCGLAKKEPFFGVAFVVMIFAIGGVPPFSGFPGKVLIFQGAIENGNFIGLALMIITSLLAMYSLFRILFIMYFGDNDGEQVDFNPLPKHRKTILGILVAVVLAMGIAAPVVMNATENATKLNMDDNYFHSIVNSHLKEGNK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit D family."}
+{"protein": "MAKYRGKPFQLYVKLSCSTMMATSIILTNILPYDAQAASEKDTEITKEILSKQDLLDKVDKAIRQIEQLKQLSASSKEHYKAQLNEAKTASQIDEIIKRANELDSKDNKSSHTEMNGQSDIDSKLDQLLKDLNEVSSNVDRGQQSGEDDLNAMKNDMSQTATTKHGEKDDKNDEAMVNKALEDLDHLNQQIHKSKDASKDTSEDPAVSTTDNNHEVAKTPNNDGSGHVVLNKFLSNEENQSHSNRLTDKLQGSDKINHAMIEKLAKSNASTQHYTYHKLNTLQSLDQRIANTQLPKNQKSDLMSEVNKTKERIKSQRNIILEELARTDDKKYATQSILESIFNKDEAVKILKDIRVDGKTDQQIADQITRHIDQLSLTTSDDLLTSLIDQSQDKSLLISQILQTKLGKAEADKLAKDWTNKGLSNRQIVDQLKKHFASTGDTSSDDILKAILNNAKDKKQAIETILATRIERQKAKLLADLITKIETDQNKIFNLVKSALNGKADDLLNLQKRLNQTKKDIDYILSPIVNRPSLLDRLNKNGKTTDLNKLANLMNQGSDLLDSIPDIPTPKPEKTLTLGKGNGLLSGLLNADGNVSLPKAGETIKEHWLPISVIVGAMGVLMIWLSRRNKLKNKA", "text": "SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor Note=Distributed in a discrete, punctate pattern with up to 3 loci per cell over the surface (PubMed:18800056). Does not localize with ClfA (PubMed:18800056). Exchanging the ClfA and SasF signal peptides retargets the mature protein on the cell surface (PubMed:18800056). Anchored to the cell wall by sortase A (Probable)."}
+{"protein": "MTAHDQELRRRAYEEVEKKEPIANSDPHRQHFHIMPPVGLLNDPNGVIYWKGSYHVFFQWQPFQTGHGAKFWGHYTTQDVVNWKREEIALAPSDWFDKNGCYSGSAVTKDDRLYLFYTGNVRDQDGNRETYQCLAVSDDGLSFEKKGVVARLPEGYTAHFRDPKVWEHEGTWYMVIGAQTENLKGQAVLFASDNLTEWRFLGPITGAGFNGLDDFGYMWECPDLFSLQGSDVLIVSPQGLEADGFRYQNVYQSGYFVGRLDYNKPELKHGEFTELDQGFDFYAPQTLEDDQGRRILFAWMAVPDQDEGSHPTIDCHWIHCMTLPRQLTLSGQKLIQQPLPELKAMRRNEKKIHINMHGSSGALPVEKPERTEILLEDIHTESGFSISIRGTATFSFHKDEGIVTLERKSFDGKRTEARHCRIKDLHTVHMFLDASSVEIFINNGEEVLSARYFPFPGNHEVTASATGKSEMNVGIWTLM", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 32 family."}
+{"protein": "MRGLDRWIAEAIRSESLDHNGQIICGGLFLEESLPSSSVSFLSSKDCSVNSCRFSQKSSFLKFRRRNGTREPLFLSVSLSINESNGEEEEGEGYNGQNGFKSEKGSVLIGGGQESKEKRRVKENGAGALNTTKHLWAGAFAAMVSRTCIAPLERMKLEYIVRGEQGNLLELIQRIATNEGIRGFWKGNLVNILRTAPFKSINFYAYDTYRGQLLKLSGNEETTNFERFVAGAAAGVTASLLCLPLDTIRTVMVAPGGEALGGVVGAFRHMIQTEGFFSLYKGLVPSLVSMAPSGAVFYGVYDILKSAYLHTPEGKKRLEHMKQEGEELNAFDQLELGPMRTLLYGAIAGACSEAATYPFEVVRRRLQMQSHAKRLSAVATCVKIIEQGGVPALYAGLIPSLLQVLPSAAISYFVYEFMKVVLKVESSA", "text": "FUNCTION: Probable mitochondrial adenylate carrier that catalyzes the transport of ATP, ADP and AMP. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MTSGEQAKTPLQAPILLTNVKPVGFGKGASQSSTDILIGGDGKIAAVGSALQAPADTQRIDAKGAFISPGWVDLHVHIWHGGTDISIRPSECGAERGVTTLVDAGSAGEANFHGFREYIIEPSRERIKAFLNLGSIGLVACNRVPELRDIKDIDLDRILECYAENSEHIVGLKVRASHVITGSWGVTPVKLGKKIAKILKVPMMVHVGEPPALYDEVLEILGPGDVVTHCFNGKSGSSIMEDEDLFNLAERCAGEGIRLDIGHGGASFSFKVAEAAIARGLLPFSISTDLHGHSMNFPVWDLATTMSKLLSVDMPFENVVEAVTRNPASVIRLDMENRLDVGQRADFTVFDLVDADLEATDSNGDVSRLKRLFEPRYAVIGAEAIAASRYIPRARKLVRHSHGYSWR", "text": "FUNCTION: Esterase that catalyzes the deacetylation of acetyl-(R)- mandelate (in vitro). Can also hydrolyze acetyl glycolate, but with lower efficiency. Has very low N-acetyl-D-amino acid deacetylase activity with N-acetyl-D-serine and N-acetyl-D-threonine (in vitro). Theoretical substrate docking studies suggest that other N-acetylated amino acids may optimally occupy the active site and may in fact be the physiological substrates. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Atu3266/EF_0837 deacetylase family."}
+{"protein": "MDGDRTPEEQIEIAESDQGPQLDDNVELANVFSYSLDQRIMEGCVISAILEPRGLETIVAVSVTNKIIIKDKETSLNITETIRCIAAAPFGDGYDCIIIGTDSSVICYDVHNNLTVFRNDVPDGVSCFVYGKLGELDEAIYCGGNCCIWGFDKTGANTYWTVTGDQVTTMCLSDYDNDGETELVIGSPDFEIRVFKNDLMRTELMETDEITCLAHVANGCFAYSLNNGTIGTYVLKERQWRIKSKSNVSKIFNFEEEGLMVVVWKQGKVDLRFAHNGEVLSRDSVSSHVASASVSKKGDESFITVVCLDGKVKGFKIQRAQNGSIDKTQQLIREFGQKKHNLMMELSNYEQEEQLADVEKDRDFRIPVDTEVAVVFVVNTELQLLSLRVEASHNIPIRGVLIFAEGLFEGESYIWIPPNEYQSRSVIDIPLVIDKDSTNDLHTKVFLGQVDSNKLMVMENTRILPKFCRFTLLREEYSKFFYMPTAYIQFDINSRAAKLSEWVQESFTIDASLVEMFDEPEGEFKFMGLRPKHEKSLMFKISHSEKTCKIYHDKIETMGAIVQSYASFYQIQNMESVAHFPDVFKEADEILEEIDPMTEVRDRLTAELQERQAAVKEIIIRAEDSIAIDNIPDARKFYIRLKANDAAARQAAQLRWNNQERCVKSLRRLNKIIENCSRLRVGEPGRQIVVSCRSAIADDNKQIITKILQYGASV", "text": "FUNCTION: Component of the BBSome complex (By similarity). The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function (By similarity). Required for proper BBSome complex assembly and its ciliary localization (PubMed:22922713). Required for cilia biogenesis and both the assembly and movement of intraflagellar transport proteins along the ciliary axoneme (PubMed:15231740, PubMed:22022287, PubMed:22922713). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, cilium axoneme."}
+{"protein": "MGRKLYYVLATLQLVAVFLFCGGFFPQKVVLKNDSKFIVNPEVQLASKPVFKKLVLVVIDALRSDFLFQKDSSDFEFLHGLLNSGEAWGYTAYSNPPTVTLPRLKGITTGSAPNFLDAILNVAEDDTSSNLKEQDSLLKQFHTHHYKMNFFGDDTWLKLFPLEFFSEYDGTNSFFVSDFEEVDFNVTRHVPYQMEHQKNWDVLILHYLGLDHIGHKGGSKSHFMPSKHREMDSVIKQIYEKIDGDTLMVVLGDHGMNDLGNHGGSSSGETSAALAFLSKRLKKYQSSDIQQSSNVPVEDAHPDYKYLKEVEQIDIVPTLSMLFNLPIPKNSMGVIIDELLQLLPSKLAAIKVQDNYLQLTKLKPGYEAQLEKKSAGTLLEEMREIQSSLAMAATNYNYTFLTYGTTLMIIGTLIVTVWNFQLSQEYIEHVGTSVLLGISMFASSFIEEEHQIWWWITISVLLLMQISNGKKLVVLSGLRLIRGWNNSGQKYIYDNVLHTLLKSHTSVLWWLNVVTFLSVGFPFLRNKDESEKMVSLLSVSFLALSSITYKICFAIVNGDKVPSGLYTFALRSCAMYLANENATESDISQCLVPIARIFFQICGVSIIILLFMKYALNKSTNMLNKLLSVIKFVLLLQTSSANIPLFLIFEILTSVTPDITPIFSLCLQNLTFFQFGGTNSIATVNLTNAYNGVSSNYNIYVVGVLMFLSNYAPSIYWALSLIPQSYKQKTLRLQHYYITGTCLMIACIALRYHLFIWSVFSPKLCYYAAWSLYNVVMDFAITLLGVL", "text": "FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily."}
+{"protein": "MKRFSTAYLLLGILCSAAVFLIGAPSRALGAEVEHYEPLQVHVQLEKVYLDGDVSIEHKHEKVFSMDDFWAAYAGWTLVEQKKGYVLFRKQMDDISPLSKVNGYIGVSDNGVISTFHGRPEPASEPIQSFFQIDLERLESHMQKNLLKGIPFRTKAEFEDVIEHMKTYSG", "text": "FUNCTION: Inhibits the SpoIVB zymogen from undergoing autocatalytic activation by an unknown mechanism, and in this way plays a role in the sigma-K checkpoint of sporulation. SUBCELLULAR LOCATION: Forespore intermembrane space."}
+{"protein": "MPHSYGIRARTRYTFQRGFREHGQIRLSTYLKTYKVGDIVDIKVNGAVQKGMPHKYYHGKTGVVYNVTQSSVGVLIYKVVGNRYMEKRVNVRIEHVKHSKCRQDFLDRVKANEAKRKEAKAQGKTVQLRRQPAPPAKAHFVSTENNEPVTLHPVAYDTTI", "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 eL21 family."}
+{"protein": "MSDLEVQVPTAFDPFADANAEDSGAGTKEYVHIRVQQRNGRKSLTTVQGLKKEYSYSKILKDLKKEFCCNGTVVQDSELGQVIQLQGDQRKNVSTFLVQAGLVKKDNIKIHGF", "text": "FUNCTION: Probably involved in translation. SIMILARITY: Belongs to the SUI1 family."}
+{"protein": "MPKPEIVFVTGNANKLREVSMILGGDASPFTLVNEPLDLEELQGADLQEIALAKLQQAVHALGPGRPVFVEDTALSFDEFNGLPGAYIKWFIKSMGLAKVVKMLDSFENKGAYAITTIAYADSKGQLHVFQGKTHGTIVDSRGHTNFGWDSIFQPDESQNNETYAEMAKEDKNKISQRGRAFAQLKEYLYNTGI", "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": "MQAGNNGGAKLKNDEFDNLYQKNINRRETETVIRRSIPVQRDLTGKILPNQVAYYEEIEREVTFGATHHILDKDNFDSYIYPTNFEVREYQFNIVQKSLYQNTLCAIPTGMGKTFIASTVMLNFFRWSKNGKIIFTAPTRPLVAQQIKACLGITGIPHDQAAILLDKSRKNREDIWTQKRVFFTTPQVIENDLKRGVLNPKDIICLVFDEAHRATGSYAYTNVVKFIDRFNSSYRILALTATPGTDIASVQEVVNNLNISNIEIRTEESMDIIRYMKKRYKEKIEIGLTTEIEMIIEQLGIAVKPVLQQAVELGIYDECHPSQINSFVAMQKSQQIIANPTIAEGIKWRNFFILQLLNHVGQMLKRIKIYGIRSFYGYFRNKFSEFTTKYNMGKSTNKIAASFYYHPILKILMKNCDVYTSNSSFIGHDKLQKIINELSDFFLNSRLDSRVIIFTELRESALEIVKTIDNMGSSSIRPHIFIGQARGKENFDDEGFIRKNKPKGRKKADRLKRLEEDKQKQLSKAKQKEQEKVERSSRRTGSSEEAQISGMNQKQQKEVISKFKNGDYNVLVCTSIGEEGLDIGEVDMIICFDTTGSPIKNIQRMGRTGRKRDGKILLLFSGNESRKFEKAMEDYYDLQRLIGQNFVEYKKSDRILPSNITPECRKEFIHISAENNELNNMEDSDEVIRYATQCMLGKVPKSKKSKAKAAKEPKGKSKTFFMPDNVETGIVSAIALVNKKKSNSNESETVIKTECFPNLDDIEKDMLASLSSPVKPEVDDYKDGTFQKTDRFEEKITGSNLKDMLMSFSKRDEESKVTSFSSDGNYVNEPFGNISLGEKLDINDDFASTPIVKADMNIGQYDRSLIENNSRGGVLFKNAFEKEEGLLKKSEKVYFRDHYSIDNTVVIEPIPNFKRYNKSCLINHNPQVENILNLFKGINENKTQITIEMNRSRCIARGIEKGSIQLTGSDFSLANVMVAQKNNEADIVWDTSKTNKNSHENLNELLDSDSDF", "text": "FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily."}
+{"protein": "MLRVIVLGAAAGGGVPQWNCGCPVCRAALDDPRLARTQASLAISADNAHWFLINASPDLRQQIVATPQLHPRAGALRHSPIAGVILTNGEVDAVAGLLSMREGSPFSIYAHDKVLAILRANSIFNVLNESIVPRRPIATDQPFEPLLPDGALSGLQITAFEVPGKGAWYLEGRAHPGGDSQSGDTLGLTITDKSTGQSLHVLTACARVTDDLKARLAGAPLLLFDGTVWRDDELITAGLGTKTGQAMGHIAMAGDDGAIAALADLGIGQKLFLHINNSNPALLAHSAERGQLETAGWQIPADGTEVTL", "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": "MILKILNEIASIGSTKQKQAILEKNKDNELLKRVYRLTYSRGLQYYIKKWPKPGIATQSFGMLTLTDMLDFIEFTLATRKLTGNAAIEELTGYITDGKKDDVEVLRRVMMRDLECGASVSIANKVWPGLIPEQPQMLASSYDEKGINKNIKFPAFAQLKADGARCFAEVRGDELDDVRLLSRAGNEYLGLDLLKEELIKMTAEARQIHPEGVLIDGELVYHEQVKKEPEGLDFLFDAHPENSKVKDFTEVAESRTASNGIANKSLKGTISEKEAQCMKFQVWDYVPLVEVYGLPAFRLKYDVRFSKLEQMTSGYDKVILIENQVVNNLDEAKVIYKKYIDQGLEGIILKNIDGLWENARSKNLYKFKEVIDVDLKIVGIYPHRKDPTKAGGFILESECGKIKVNAGSGLKDKAGVKSHELDRTRIMENQNYYIGKILECECNGWLKSDGRTDYVKLFLPIAIRLREDKTKANTFEDVFGDFHEVTGL", "text": "FUNCTION: DNA ligase, which is expressed in the early stage of lytic development, has been implicated in T4 DNA synthesis and genetic recombination. It may also play a role in T4 DNA repair. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
+{"protein": "MEAEGSSVPARAGSHEGSDSSGGAALKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPPPPPSPQPQLQPPPPPPLPPPPPPPGATRGRYASSGASRVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQANFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQHEVEIPSPTQKEKEKKKRPMSQISGVKKLMHSSSLTNSCIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMAIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAPDDQEDGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPLDEQVEEEAVAEEESQPQTGVADDCCPDT", "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. Colocalized with SHANK2 to the apical membrane of colonic crypt cells. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily."}
+{"protein": "MKNKLPPFIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASIGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTALRPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTFNELNGLLNDALAPVSERWPGRLTVDELHPPIPGYECPPNHQLVEVVEKLLGAKTEVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELIIQVIHHFCWH", "text": "FUNCTION: Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily."}
+{"protein": "MASAAPASRGAARASTAARDAPFAAAARGPGRFRRDGNGRNRLVAVRAPRRWTTRAAATSGDANVVIKPKKERAKVDPNAVLQVPPSQIRNFSIIAHIDHGKSTLADTLLSKTKTVAARDMEAQLLDSMDIERERGITIKLNSARMNYVANDGETYVLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANVYLALENDLEIITVLNKIDLPGAEPERVKVRSIHWFPYDRVGVREIEDVLGLDTEDAVVASAKANIGMEDILENIVKMIPPPPDTGDEPLRALIFDSYFDPYRGVVVIFRVVDGNLGVGDAVKFMNTGKSYTIDEIGIMRPQKVPVNRLSAGEVGYMIANIKSVADARVGDTITTTKDSSTEPLPGYSEATPMVYCGLFPTDSDQYEDLRVALGKLQINDAALRYEPEQSSAMGFGFRCGFLGLLHMEIVQERLEREYDLGLITTAPSVVYKVYTSDGACVDIANPADLPDASVRDRIEEPFVKLEMFAPSDYVGSLMELAQQRRGEFIDMTYLSESRTCLKYDIPLGEVVTDFFDELKSRSKGYASMEYSFNEYRKSDLVRLDVLINYEPADPLACICHRDKSYVMGRGLVDKLKELIPRQMFRIPIQASIGTKVIASTSISAMRKDVLAKCYGGDISRKKKLLKKQAAGKKRMKQFGKVEVPQEAFMAVLKVDQNAGSGG", "text": "FUNCTION: Promotes chloroplast 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. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily."}
+{"protein": "MDESFDAFEIKPNSSIIEHFNNHPTCIDKEFNFILQKTELRALETDKFRSALEAKNKLKNRYSNVLPFEETRVKINIDDDDDDEDDNEDDIIVSNNNNNNNNNEKRIKRNSIGSSGQSDVMSNSSDEEDHGGSGDEGTTLSDYINASFINNGTYICTQGPLLNTIVDFWKMIWEQNSNIIVMLTREEENFKTKCDKYWPDKDEERYGNFIVKFDNNITIPDILIRREFTLENLKDNKTRKIYHFQYTTWPDHGTPVSTTGFLKFVSFVDHEKRSGPIVVHCSAGIGRSGTFVAIHSIVAKFAKHYDEKKQAPSINLPKLVVEMRNERPGMVQTRDQYRFCYLAISEAMNTVLKKEQKKRKGLSYSYSSIPLTGPEHD", "text": "SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class subfamily."}
+{"protein": "MQTQEILRILRLPELGDLGQFFRSLSATTLVSMGALAAILAYWFTHRPKALQPPCNLLMQSEEVEDSGGARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM", "text": "FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:22633490, PubMed:24269233). Plays an important role in fatty acid metabolism in brain and the acyl- CoAs produced may be utilized exclusively for the synthesis of the brain lipid. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type III membrane protein Peroxisome membrane; Single-pass type III membrane protein Microsome membrane; Single-pass type III membrane protein Endoplasmic reticulum membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MPKTKLTSPPFKILKCTECDACINVPSILQSNEQAECPRCHHLLASGTRWSLHRCAMIALSILILMPFSLNYPLLSLHLLGIKIDASIWDGIWKMAVGGYEYTAFMIFICAVVMPITFALLVIMLWLAKIFQIKPRSVLLFLGYIKAWVMFDVYLVALGVTIFKVREYATLEINIYLIPFIFTALLTTLLFIKLNLSALWQEFYPECTSVYTKQAVELCPACHYTFTQKSIHYDHQQKICCPRCQSPLNTSDKLKLQATWATLIAGIIMLFPANLLPISGIYLTGALSEDTLISGVISFVKSGSYFVAFVVFFASIFVPISKIFIMLYLLACVHFKWQHSIKWQMRLLHLVHFVGRWSMLDLFVLALMMSLVTRGEIINFTVGPGAFYFGAAVFCTMLSTSQFDSKLIWKIYDREK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PqiA family."}
+{"protein": "MATENKILILGATGAIGRHIVWASIKAGNPTYALVRKTSDNVNKPKLTEAANPETKEELLKNYQASGVILLEGDINDHETLVNAIKQVDTVICAAGRLLIEDQVKVIKAIKEAGNVKRFFPSEFGLDVDRHDAVEPVRQVFEEKASIRRVVESEGVPYTYLCCHAFTGYFLRNLAQIDATDPPRDKVVILGDGNVRGAYVTEADVGTYTIRAANDPNTLNKAVHIRLPNNYLTANEVIALWEKKIGKTLEKTYVSEEQVLKDIQTSSFPHNYLLALYHSQQIKGDAVYEIDPAKDVEAYDAYPDVKYTTADEYLNQFV", "text": "FUNCTION: Reduces achiral isoflavones to chiral isoflavanones during the biosynthesis of chiral pterocarpan phytoalexins. The reduction product (sophrol) is a third isomer, which represents the penultimate intermediate in the synthesis of the phytoalexin (+)-pisatin, the major phytoalexin in pea. SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily."}
+{"protein": "MELFPIIPAGGILALLVALYMTSSVLKEDTGPKEMQTIAAAIREGAMAFLNRQYRTIAGLALIVAVLLALLTRQYHTAVAFITGAFASALSGYIGMYVAVNANLRVAAGARNSLNKALTVAFRGGAVTGLAVTALSLLGVTSLFYAFGGATNPTRAPLDIVGFGFGASFVALFAQLSGGIYTKAADVGADLVGKVEAGIPEDDPRNPAVIADLVGDNVGDCAGRGADLFESTAAENIGAMILGIALVPFFGVKGIVFPLVARAAGIIASIIGMFFVRAEENQDPMAALNRGYIVTSILAIIFLYPISRYMLSGPGVNFIYFYGAGIIGIVLSFIFVLITQYYTSYDYRPVKEIARASITGPATNIISGVAVGFESTALPVVFISLAILGAYWLGLKSGLPGGGLYGTAVATMGMLSTAAYILAMDTYGPITDNAGGIVEMSGAPEEVRRRTDRLDASGNTTKALTKGYAIGSAALATFLLFSAYIDEVKIALNIKGNFPVDIGKPEVFVGAFIAAMMVLLFSSTAIRAVGNAAQYVILEVRRQFKEIPGIMEGTAKPEYGACVDIVTRGALKEMVLPGLIVVITPIIVGLVLKAEAAAAFLMVGTITGVIVALFLNNGGGAWDNAKKYIELGNFGGKGSEAHKAGVVGDTVGDPFKDTAGPSLHVLVKLISTITLVLAGLFI", "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": "MDQTVSENLIQVKKESGGIAVITINRPKSLNSLTRAMMVDLAKAFKDMDSDESVQVVIFTGSGRSFCSGVDLTAAESVFKGDVKDPETDPVVQMERLRKPIIGAINGFAITAGFELALACDILVASRGAKFMDTHARFGIFPSWGLSQKLSRIIGANKAREVSLTSMPLTADVAGKLGFVNHVVEEGEALKKAREIAEAIIKNEQGMVLRIKSVINDGLKLDLGHALTLEKERAHAYYSGMTKEQFRKMQEFIAGRGSKKPSSKL", "text": "FUNCTION: Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
+{"protein": "MSRQSFYADPSSAGRQMKYRKDLFPLLDTREITACLLECEFNVTQELIVKPTADFVTNLFEQFLDTFMGIPLGTIRKKARKMSRINPLESDQANGKPQQSPEEDFNDNQENDKTKDTFSALQLLILHRYLAIFFSTCGINDFVLTDIARPDGYRIRRILSAVINFIRFREDQSPKFDHLANECEATADKVSEVQAENSATMQKINAIKEKLEMDSENDESNRKNLQYINSYNRKLETKLRELKVMQERLTKEHDDYKQEKALLAKKLYDINFLYNETQEQVANLTKYAETDLSILVKITEDLSNDLSSMQTNYKNLEKSYQNMGITIDSIQVNEINLKDLLKLAEDITRNVEKRQIEGKILKDNQDNLDELTRKQMELEGQILIVQNQLNKSNKKYQDLIVQADKKESAVKLKLEETKQEFNDILSEKEKHNEEHKRIMDQIVKIQQETTAIQDAFVKESKEVELKLINLMSIIKRYMSDLRNNI", "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 NUF2 family."}
+{"protein": "MSSFEGQMAEYPTISIDRFDRENLRARAYFLSHCHKDHMKGLRAPTLKRRLECSLKVYLYCSPVTKELLLTSPKYRFWKKRIISIEIETPTQISLVDEASGEKEEIVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLAQGEAARMELLHSGGRVKDIQSVYLDTTFCDPRFYQIPSREECLSGVLELVRSWITRSPYHVVWLNCKAAYGYEYLFTNLSEELGVQVHVNKLDMFRNMPEILHHLTTDRNTQIHACRHPKAEEYFQWSKLPCGITSRNRIPLHIISIKPSTMWFGERSRKTNVIVRTGESSYRACFSFHSSYSEIKDFLSYLCPVNAYPNVIPVGTTMDKVVEILKPLCRSSQSTEPKYKPLGKLKRARTVHRDSEEEDDYLFDDPLPIPLRHKVPYPETFHPEVFSMTAVSEKQPEKLRQTPGCCRAECMQSSRFTNFVDCEESNSESEEEVGIPASLQGDLGSVLHLQKADGDVPQWEVFFKRNDEITDESLENFPSSTVAGGSQSPKLFSDSDGESTHISSQNSSQSTHITEQGSQGWDSQSDTVLLSSQERNSGDITSLDKADYRPTIKENIPASLMEQNVICPKDTYSDLKSRDKDVTIVPSTGEPTTLSSETHIPEEKSLLNLSTNADSQSSSDFEVPSTPEAELPKREHLQYLYEKLATGESIAVKKRKCSLLDT", "text": "FUNCTION: Nuclease involved in DNA non-homologous end joining (NHEJ); required for double-strand break repair and V(D)J recombination (PubMed:11336668, PubMed:11955432, PubMed:12055248, PubMed:14744996, PubMed:15071507, PubMed:15574326, PubMed:15936993). Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments (PubMed:11336668, PubMed:11955432, PubMed:14744996). V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs) (PubMed:11336668, PubMed:11955432, PubMed:14744996). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends (PubMed:11336668, PubMed:11955432, PubMed:14744996). These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively (PubMed:11336668, PubMed:11955432, PubMed:14744996). This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC (PubMed:15071507, PubMed:15574326, PubMed:11955432, PubMed:15936993). The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint (PubMed:11955432). Also required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ (PubMed:15456891, PubMed:15468306, PubMed:15574327, PubMed:15811628). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family."}
+{"protein": "MDGFSNMEQAPLAYQEVQWLAETFVTFMGLGWLINYVLMIWHSRRGEPSSMALIPLCNNIAWELVYTIIYPSPNKVELAAFIAGVTLNFLIMTSAARSARSEWSHSPTMAKHAGLIIVAGILMCFTGHVALAMEIGPALAYSWGAVICQLALSIGGVCQLLQQHSTGGTSWKLWSSRFLGSCCAVGFAFLRWRYWPEAYGWLASPLILWSLATFLVADLTYGVCLLL", "text": "FUNCTION: Terpene cyclase; 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 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 paxB family."}
+{"protein": "MAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILSTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGTKE", "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. 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. SIMILARITY: Belongs to the HIV-1 REV protein family."}
+{"protein": "MDTLTAIGRWLAKQHVVTWCVHHEGELWCANAFYLFDAQNVALYLLTDDKTRHAQMSGACAPVAGTVNGQPKTVARIRGVQFKGEIRRLEGQESDAARKAYLRRFPVARVLPAPVWEIRLDEIKFTDNTLGFGKKLHWLRDSRAQQA", "text": "SIMILARITY: Belongs to the UPF0306 family."}
+{"protein": "MLQVFDIIGPIMIGPSESITAGAVRIXKI", "text": "SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase family."}
+{"protein": "MKSVLDGVADTTFRTITSGLQYLGSNDANYDDPLNDAAFKTGFSLQKPLSAFRSNSFPNKVPADEELIFKGIPFFPTNSTDLFGNRNTTRDENSIQCGENFMDMECFMILTPSQQLAVAVLSLTLGTFTVLENLVVLCVIFQSRTLRCRPSYHFIGSLAVADLLGSVIFVYSFLDFHVFHKKDSPNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYRRIVTRTKAVIAFCMMWTISIIIAVLPLLGWNCKRLNSVCSDIFPLIDENYLMFWIGVTSVLVLFIIYAYIYILWKAHHHAVRMLSRTSQKSLVVYSAEGTKVQTTRPEQTRMDIRLAKTLVLILAVLVICWGPLLAIMVYDLFWKMDDNIKTVFAFCSMLCLLNSTVNPIIYALRSRDLRHAFLSSCHACRGSAQQLDNSLESDCQNRNVNISANRAAESCVKTTVKIAKVTMSVSTETSAEAV", "text": "FUNCTION: G-protein coupled receptor for cannabinoids (By similarity). Mediates many cannabinoid-induced effects in the central nervous system (CNS), as well as in peripheral tissues (By similarity). Regulates cellular respiration and energy production in response to cannabinoids (By similarity). Signaling typically involves reduction in cyclic AMP (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Mitochondrion outer membrane Cell projection, axon Presynapse Note=Unexpectedly, in the mitochondria, the C-terminus is located in the mitochondrial intermembrane space, a compartment topologically considered as extracellular. In canonical seven-transmembrane G-protein coupled receptors, the C-terminus is cytosolic. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MSNDQKWIKSLPSDLQNQVNALVEAHPPSLTVIHKLCEYFKTNASEHEDKRRKLSSDPEIKSEGHVPEALSGPKSEVPGQIHEQEIIFELPQISFQSPIRKKLNLIFHLLVEPGQSPKPVMSLALPTTYVPEISIHNLASSIRLCVLLPILGNSTNNTKRNIGLLCFWIHDDAASDPNKNDPIICQVNFDQVKKQLIKAGKIPAEAETQLKEMNESNQSQDGIKAINEAIINFLQKQFQLCGIHMINYLPSSSATKNKLTINTDAGVAVSSNANSVNDLVMVEAYKGARDGAVLMLTANEYNQPYIIFGFKKPILIFDISKVQHVSYSNITRLTYSMIVTVVNEKKDSKVETLEFGMIDQKYFQIMDEFIKSQGINDNSFDEDLREKVTTNANSGEGEQASEQAAPADSDDEEEDGTFQVGQEEEGESSVDEEYDSNAGSDGDSDVGEEEDDTNENNEGANPAASTEADDVVTQSKEEDDEQ", "text": "FUNCTION: Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by creating a repressive structure at the core histone gene promoter (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the RTT106 family."}
+{"protein": "MGGVLSLLFNISEIAAELSLSTGFTVDAILTGEAFAAVSTEAAWLIEIEAVDLAGLSTLEALSLTGLTTEQFSLLSAIPTALNNAIGIGVFFQTVSGASAVVAAGVTTFGYSKEVPVVNMALVPWFPQVDYLFPGFTSFSYYLNAVLDWGESLFHAVGREVWRHLMRQATLQIGQATRAVAVRSTNELSHTLAQIAENARWALTSGPVHIYSSVQDYYRYLPARNPIQLRQEYRNRGEPPPSRADFEYQENREGQRARRELGYDEPRSGQYVEHYTAPGGAHQRVTQDWMLPLILGLYGDITPTWEVELNKLEKEEDGPSKKKARRSMQKNMPYSRSRPQAPSKRRSRGARSKNRA", "text": "FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C- terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly. The viral progenies exit the cells by lytic release (By similarity). SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane. SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family."}
+{"protein": "GLWETIKNFGKTFTLNILDYTK", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
+{"protein": "MQSKFLWIAAASAATAAAQVPARLCGTAQPTMDDLVIAAGLAAEGKDNRRGLHPEDPIVVPTLFHVLAINETVAGGYLTEKSLQDQLDVMNADFGPSNVIFNLTATTRTVNRRWAQDLDEIPMRRALRQGGQETLNIYFMPYVSGYLGYCTFPNFWDAGSDEFIYDGCAVLSDSLPGGSLARYNLGRTATHEIGHWFDLFHTFSGGCGCVGDMIHDTPAMLNATGGCPVGKDTCPDRPGLDPIHNYMDYSDDACMNEFTPGQNFRMRSAWYNIRTK", "text": "FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M43B family."}
+{"protein": "XSNATDETXLKDVSA", "text": "FUNCTION: 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."}
+{"protein": "MPMRIERDLHMATGNGETSYTKNSRIQEKVMFQIKPVLEEATRAAYSALLPQTMVVADLGCSSGPNTLRFVSEVIGIIARHCKEHDRRHDYPQLQFFLNDLPGNDFNNLFLLIQQFNKSMARNHKGEAAEALPPCYISGLPGSFYTRIFPSESVHLFHSLFSVHWHSQASEQLKDTKNKCLDIYITKNMPPSMVKLFQQQFEKDFSLFLKLRYEELVSGGQMVLTFIGRKHEDVFTGESNHLYGLLAQSLKSLVDEGLVEKEKLESFYLPIYSPSVGEVEAIVKQVGLFNMNHVKVFEINWDPYGDSEGDDVHDSIRSGENVAKCLRAVMEPLVASQFGEHILDKLFKEYARRVAKHLENEKTKHAILVLSIEKAIIHV", "text": "FUNCTION: Methyltransferase involved in the biosynthesis of methyl anthranilate in response to stresses. Utilizes anthranilic acid as substrate. Produces exclusively the O-methyl ester. Can also use benzoic acid as substrate. Low activity with salicylic acid. SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family. SABATH subfamily."}
+{"protein": "MKQLHKQMSSKRDEETIPMSQSSPYSPKTLKHPRSLPRSLHYLFREQRLLFILVGILIGSTFFILQPSLSRLGAAESTSLITRSVSYAVTDSPPSRSTFNSGGGGGRTGRVPVGIGRKRLRIVVTGGAGFVGSHLVDKLIGRGDEVIVIDNFFTGRKENLVHLFSNPRFELIRHDVVEPILLEVDQIYHLACPASPVHYKYNPVKTIKTNVMGTLNMLGLAKRVGARFLLTSTSEVYGDPLEHPQKETYWGNVNPIGERSCYDEGKRTAETLAMDYHRGAGVEVRIARIFNTYGPRMCLDDGRVVSNFVAQTIRKHPMTVYGDGKQTRSFQYVSDLVEGLVALMENDHVGPFNLGNPGEFTMLELAEVVKEVIDPSATIEFKPNTADDPHKRKPDISKAKEQLNWEPKISLREGLPRMVSDFRNRILNEDEGKGL", "text": "FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily."}
+{"protein": "MIVPVLSRQALRHASVARVALPSLTRWYASYPPHTVVKMPALSPTMTSGGIGAWQKKPGDKIEPGEVLVEIETDKAQMDFEFQEEGVLAKILKDSGEKDVAVGNPIAILVEEGTDVNAFKDFTLKDAGGETSPAVPKDEPKNESTASAPTPAPTPAPEPENTSFTGRFQTALEREPNALPAAKRLAREKGIDLRNVKGSGPGGKITEEDVKKALASAPAAGAAAAAYTDVPISGMRKTIAARLKESVTENPHFFVSTNLSVSKLLKLRQALNSSADGRYKLSVNDFLIKAMGIASKRVPTVNSSWRDGVIRQFETVDVSVAVATPNGLITPIVKGVEGKGLESISAAVKELAKKARDGKLKPEEYQGGSISISNMGMNPAVQSFTAIINPPQAAILAVGAPQKVAVPVENEDGTTGVSWDEQIIVTASFDHKVVDGAVGAEWIRELKKVIENPLELLL", "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": "MAATASPGAGRMDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILKTEGLKGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKALIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALVRIAREEGVPTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIVKTRIQNMRMIDGKPEYKNGLDVLLKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG", "text": "FUNCTION: Catalyzes the transport of 2-oxoglutarate (alpha- oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate. Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity. Contributes to several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae (By similarity). Involved in the regulation of apoptosis (PubMed:21448454). Helps protect from cytotoxic-induced apoptosis by modulating glutathione levels in mitochondria (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MPKYLINFVQQYASFRIHELESVARLFNIDIQYNKEDLEFIESLDPEIETPFLYVTVNSEEDIKKICTRSVLIKSVYSIWAETQLLDEILNELHSKFDKQFLSNYMINKTFKIEVESYGSKYNQKEKLEMMQKLKDSPLWDSGKCLMHPTEEQMDKHILWYILTDFGVERQGLVKDFTLLPRKVYFGQRIAKGNRDDIIKYNLSDRKYLGTTSMDPELSLVSANMGLVKKGHFVLDPFVGTGSFILVASHFGAQTVGCDIDIKAMRKEEDCNLETNFKDHGLTSQFLGTILCDNSCPPWRVNSMFDSIITDPPYGIRAGARKIGFKENRKFVPVPEGLRRDHIPQCIDYSVPDVMADLLELAAKTLIVGGRLVYWLPTTPDYKETDLPRHPCLRLITASCLQILTNRWGRRLVTMEKIIEYNDSIHNKSLLVQEDLGQFDPQHKDLRAVVFWKKMGTNEKTKKKEQKKKSVENHLKSKNNNDVINNNSNDTNSNNNCNNENNIENQK", "text": "FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM11 methyltransferase family."}
+{"protein": "MLLATLLLLLLGGALAHPDRIIFPNHACEDPPAVLLEVQGTLQRPLVRDSRTSPANCTWLILGSKEQTVTIRFQKLHLACGSERLTLRSPLQPLISLCEAPPSPLQLPGGNVTITYSYAGARAPMGQGFLLSYSQDWLMCLQEEFQCLNHRCVSAVQRCDGVDACGDGSDEAGCSSDPFPGLTPRPVPSLPCNVTLEDFYGVFSSPGYTHLASVSHPQSCHWLLDPHDGRRLAVRFTALDLGFGDAVHVYDGPGPPESSRLLRSLTHFSNGKAVTVETLSGQAVVSYHTVAWSNGRGFNATYHVRGYCLPWDRPCGLGSGLGAGEGLGERCYSEAQRCDGSWDCADGTDEEDCPGCPPGHFPCGAAGTSGATACYLPADRCNYQTFCADGADERRCRHCQPGNFRCRDEKCVYETWVCDGQPDCADGSDEWDCSYVLPRKVITAAVIGSLVCGLLLVIALGCTCKLYAIRTQEYSIFAPLSRMEAEIVQQQAPPSYGQLIAQGAIPPVEDFPTENPNDNSVLGNLRSLLQILRQDMTPGGGPGARRRQRGRLMRRLVRRLRRWGLLPRTNTPARASEARSQVTPSAAPLEALDGGTGPAREGGAVGGQDGEQAPPLPIKAPLPSASTSPAPTTVPEAPGPLPSLPLEPSLLSGVVQALRGRLLPSLGPPGPTRSPPGPHTAVLALEDEDDVLLVPLAEPGVWVAEAEDEPLLT", "text": "FUNCTION: Probable receptor, which is involved in the internalization of lipophilic molecules and/or signal transduction. May be involved in the uptake of lipoprotein APOE in liver (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Membrane, coated pit. SIMILARITY: Belongs to the LDLR family."}
+{"protein": "MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE", "text": "FUNCTION: Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential. FUNCTION: Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CidA/LrgA family. CidA subfamily. SIMILARITY: Belongs to the CidA/LrgA family. CidA subfamily."}
+{"protein": "MAALEVLFILFVSIASSLASEGVSWLLVYRTENYKRGKANIDRLQIQLDKLVDQESETSSLSKKGNKDKKIEKIEEQLKIANKELSFSKMKSMFAVAISMIALFSYLNRIFDGVVVCKLPFVPIGFLQGISHRTIAGDDYTDCSMTFIYAICSMFIRNNIQLILGTAPPKTKQANPWALPEEKKTR", "text": "FUNCTION: Calcium-selective channel required to prevent calcium stores from overfilling. Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMCO1 family."}
+{"protein": "MGRRPARCYRYCKNKPYPKSRFCRGVPDAKIRIFDLGRKKAKVDEFPLCGHMVSDEYEQLSSEALEAARICANKYMVKSCGKDGFHIRVRLHPFHVIRINKMLSCAGADRLQTGMRGAFGKPQGTVARVHIGQVIMSIRTKLQNKEHVIEALRRAKFKFPGRQKIHISKKWGFTKFNADEFEDKVAKKRLIPDGCGVKYVPNRGPLDKWRALHS", "text": "FUNCTION: Testis-specific component of the ribosome, which is required for the transition from prophase to metaphase in male meiosis I (By similarity). Compensates for the inactivated X-linked RPL10 paralog during spermatogenesis. The ribosome is 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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL16 family."}
+{"protein": "MRLKQGSFLWYLYLDKIYCLLSVRNVKALAEYFHILDVHGKNTLNDVLFYHFLHHVTDLKKAQINIVFDMLDWNAVGEIDFEKFYMLVCMLLAHQNHLEGQFMYRHSRPVFDLLDLKGDLRIGAKNFEMYRFLFNIQKQELKDLFRDFDITGDNRLNYQEFKLYTIIYTDKLQKRQKTEEKEKGERKRSLYSKCHIK", "text": "FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. pH-dependent Ca(2+) sensor required to activate the CatSper channel. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Associates with the CatSper complex via direct interaction with CATSPERZ, and senses intracellular Ca(2+). Together with CATSPERZ, associates with the CatSper channel pore and is required for the two-row structure of each single CatSper channel. SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium, flagellum Note=Localizes to the principal piece of the sperm tail."}
+{"protein": "MYDFVIIGGGIIGMSTAMQLIDVYPDARIALLEKESAPACHQTGHNSGVIHAGVYYTPGSLKARFCLAGNLATKTFCDQNNIRYDTCGKMLVATSELEMARMRALWERTAANGLEREWLSAAELREREPNIIGLGGIFVPSSGIVSYRDVATAMANRFQAKGGEIIYHAEVSALTEHAAGVVIRTSQGREIETATLIGCAGLMADRLVKMLGVEPGFIICPFRGEYFRLAPRHNRIVNHLIYPIPDPAMPFLGVHLTRMIDGSVTVGPNAVLALKREGYRKRDVSFTDTLEVFRSAGIRRVLKNHLLSGLGEMKNSLCKSGYLRRVQKYCPSLTVNDLQPWPAGVRAQAVSPDGKLIDDFLFVATPRSIHTCNAPSPAATSAIPIGAHIVSKVQALRESQSNPGRTLRAARNVDTLHAAFTR", "text": "FUNCTION: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG) to alpha-ketoglutarate and couples to the respiratory chain by feeding electrons from the reaction into the membrane quinone pool. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (By similarity). Also displays some oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological (PubMed:34555022). SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the L2HGDH family."}
+{"protein": "MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERYATTEYCLKTGG", "text": "FUNCTION: An L-glutamate ligase that catalyzes the ATP-dependent post- translational addition of glutamate residues to the C-terminus of ribosomal protein bS6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. SIMILARITY: Belongs to the RimK family."}
+{"protein": "MALLVWSSLVVASLHLLGTAAYPSRSKYTVINENCPGAEWNIMCRDCCEYDQVECACPDGNQKVGYTIPCCRNEENECDSCLIHPGCSIFENCKSCNNGSWGGTLDDFYIKGSYCSECRMGWYGGDCMRCGEVIQAARGEIMLESYPFNARCEWSIQVAPGYTVELRFGMLSLEFDYMCQYDYLEVRDGDNVDAKILKRFCGNQRPLSLRSTGNSLHLLFQSDGSKNFDGFYVTFEEVTGCSSTPCFHDGTCIADKTGSYRCACLAGYTGRHCENVIEEKSCKDPGAPMNGYRKLPDGAGLSLANHIKVGFKIHYFCNNSYVLSGNQERACLQGAQWSGKQPVCIKACKEPKVADLVRQKVLPSLVQSRETPLHQLYSASFTKEKTDILPTKKPALPPGELPPGYQHLHTQLQYDCVSPFYRRTGSSRRTCLKTGKWSGRAPSCIPICGKLENFNITQLGEQRWPWQAALYRRSNGVKDASLRKGSWVLVCSGALLNERTVVMAAHCVTDLGKSSIIKVSDMKVVLGKFYRDDDREEKSQQHLHISAVIVNPNYDPILLDSDIAVIKLLDKARVSDYVQPVCLTLATEMITSPQEYTIVISGWKILSDPRAPGSKNETIRAGAIEPVDSLQCEQQYEENGISVSVTESMFCAKQEPRPSPSICPSETGGITTVLLPSPTSPEGSWHLIGLVSWGYDKSCRKDLYTGYTKVVTFKEWLEKNMK", "text": "FUNCTION: May play a role in regeneration of skeletal muscle. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MTITVLKSAPGLPPAPQGDAADVVQVMLARLRAEGEAAARDYAARLDGWSGEIVVSPDQVARASEQVPEDLKTQIRYAHDNIRRFAEAQRASALDFQTELRPGLIAGQKQIPLAAAGAYVPGGRYAHIASALMSIATARAAGVGQITAVSPPQVGRGVHPAILYAMSLAGADRILALGGVQGVAALAFGLFGAPPADILVGPGNQFVAEAKRQLFGPVGIDMFAGPTDSLVIADSTADPLTVAWDLVGQAEHGYNSPVWLVTDSAALAEAVLAHIPGCIADLPEPNRSSAQAAWDALGEVILCTDREEMAATADRYAPEHLHVQAADLDWWRGRLSAYGSLFLGELTTVAFGDKASGPNHVLPTSGAARYTGGLSVHKFLKTVTWQQVAPQALPDLARATATISRAEGMEGHARTADIRLEKLRPTLRQVGTG", "text": "SIMILARITY: Belongs to the histidinol dehydrogenase family."}
+{"protein": "MGGFLVEKIKIVLADDNKDFCQVLKEYLSNEDDIDILGIAKDGIEALDLVKKTQPDLLILDVIMPHLDGLGVIEKLNTMDIPKMPKIIVLSAVGQDKITQSAINLGADYYIVKPFDFVVFINRIRELVSNRVTQVEPKPRPVQETQMTRSDFVKNVGNIETEITNIIHEIGVPAHIKGYLYLREAMKMVIDNVELLGAVTKELYPSIAKKFNTTPSRVERAIRHAIEVAWSRGKVDTINQLFGYTVHNTKGKPTNSEFIAMIADKLRLEHSMVK", "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": "MLQSIHLRFSSTPSPSKRESLIIPSVICSFPFTSSSFRPKQTQKLKRLVQFCAPYEVGGGYTDEELFERYGTQQNQTNVKDKLDPAEYEALLKGGEQVTSVLEEMITLLEDMKMNEASENVAVELAAQGVIGKRVDEMESGFMMALDYMIQLADKDQDEKRKSLLEVVKETVLSHLTKKCPPHVQVIGLLCRTPKKESRHELLRRVAAGGGAFESENGTKLHIPGANLNDIANQADDLLETMETRPAIPDRKLLARLVLIREEARNMMGGGILDERNDRGFTTLPESEVNFLAKLVALKPGKTVQQMIQNVMQGKDEGADNLSKEDDSSTEGRKPSGLNGRGSVTGRKPLPVRPGMFLETVTKVLGSIYSGNASGITAQHLEWVHQKTLQVLEEIAY", "text": "FUNCTION: Plays an essential role in early steps of chloroplast development. May be involved in the redox control of plastid gene expression by maintening the redox state around chloroplast nucleoids. May positively regulate plastid-encoded RNA polymerase (PEP) activity, through binding to FSD2. SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid."}
+{"protein": "MEEKKPEQDEFGYHLFPERGNGESKKNSILSKSLFSFNHKCQLMLKIALDTSPYAKLLLDAMKQSGCTVYKDRHFSCEECDGSVSGGFDAATSEIVLCQNNIHQQSHMNRVVTHELIHAFDHCRAHVDWFNNVRHLACSEIRAANLSGDCTLANELTRFKFGVKGHHQVCVRDRALRSILAVRNISRETAEKAVDEVFDSCFNDHEPFGRIPHSKADAKFAYRDFQNRDRYYANL", "text": "SIMILARITY: Belongs to the peptidase M76 family."}
+{"protein": "MASPQGGQIAIAMRLRNQLQSVYKMDPLRNEEEVRVKIKDLNEHIVCCLCAGYFVDATTITECLHTFCKSCIVKYLQTSKYCPMCNIKIHETQPLLNHKLDRVMQDIVYKLVPGLQDSEEKRIREFYQSRGLDRVTQPSGEEPALSNLGLPFSSFDHSKAHYYRYDEQLSLCLERLSSGKDKNKSILQNKYVRCSVRAEVRHLRRVLCHRLMLNPQHVQLLFDNEVLPDHMTMKQIWLSHWFGKPSPLLLQYSVKEKRR", "text": "FUNCTION: Component of the Polycomb group (PcG) multiprotein BCOR complex, a complex required to maintain the transcriptionally repressive state of some genes, such as BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. Transcriptional repressor that may be targeted to the DNA by BCL6; this transcription repressor activity may be related to PKC signaling pathway. Represses CDKN1A expression by binding to its promoter, and this repression is dependent on the retinoic acid response element (RARE element). Promotes cell cycle progression and enhances cell proliferation as well. May have a positive role in tumor cell growth by down-regulating CDKN1A. 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. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity. Regulates the expression of DPPA4 and NANOG in the NT2 embryonic carcinoma cells. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAETKKGSESYPIKTIVVLVQENRSFDHTLGWFKELNREIDGVMKSDQKFNPGFSSDLNSHNVVFGDQSQYVDPNPGHSIRDIYEQVFGKPWDSGHPDPNPGPATMSGFAQNAERKMKGMSSAVMNGFKPDALPVYKELVQNFAICDRWFASVPGATQPNRLFIHSATSHGTTNNERKLLIEGFPQKTIFESLDEAGFTFGIYYQCFPTTLFYRNLRKLKYLTRFHDYGLQFKKDCKEGNLPNYVVVEQRWYDLLLNPANDDHPSHDVSEGQKLVKEVYEALRSSPQWNEILFIITYDEHGGFYDHVPTPLDGVPNPDGILGPPPYNFEFNRLGVRVPTFFISPWIEPGTVLHGSNGPYLMSQYEHSSIPATVKKIFKLKDFLTKRDSWAGTFESVITRNSPRQDCPETLSNPVKMRGTVAKENAELSDFQEELVIVAAGLKGDYKNEELLYKLCKKTCVSDASKYVTKAFDKFVEESKKARERGGDENDIVFCVDDDDDHNVVKPPPSQSEPSHATPWSN", "text": "FUNCTION: Non-specific phospholipase C (PLC) which assumes minor PLC activity during inorganic phosphate starvation. Can hydrolyze both phosphatidylcholine (PC) and phosphatidylethanolamine (PE). Required for normal accumulation of digalactosyldiacylglycerol (DGDG) during phosphate limitation and may contribute to the conversion of phospholipids to diacylglycerol, the substrate for galactolipid synthesis. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the bacterial phospholipase C family."}
+{"protein": "MRYSVGVLGATGMVGQKFIQMLAEHPWFKLTSLAASERRVGKKYGEEVDWIVSREVPDIAKDIEMVPMDPKHVDADIVFSALPSDIAREVEPKFAEAGFVVASNASAYRMAEDVPLVIPEVNPEHLGLIEVQKKNRGWDGFIVTNPNCTTIVLVLSLKPLMDLGLRTVRVASMQALSGAGYPGVPSLAITDNVIPFIKGEEDKVEEEPLKLLGKFNGRKIEFADIKVSASCHRVPVIDGHTEAVWVEFDREVSVEEAKAAFESLKPLDLPTSPEKVIIVREEPDRPQPRLDRDAGNGMSITVGRIRKDGERGLKYIVLGHNTVRGAAGASILNAELMIKEKII", "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": "MVLSQEHRDLLDAFQKEVEQRRPGDLLQFAANYFNKKLEEERLFVRSQESLALSKGVVLFPGSEGCGANRAAGSPDARKTGEDEDVMFKLPFVEHDPHSRHIYDDNKHGHDSCDPHTSFSREPGAGLFQGGYNMGQEAQKEAQTDFDPKASEVSSILKQRNVPRKSGVNSKPLPMNFNAERRTSVSGETLKPDHFSDWTPENYTEKTREQLKGLESAVGKNFLFNKLDSDSKTLVINSLEEKLVSKGQEIIRQGDEGDYFYIVEKGTVDFFLDDRKVNTYGPGSCFGELALMYNSPRAVTAVAATDCVLWALDRLTFRRILLSGSFKKRLLYDDFLKSMPLLKSLSNYDRAKLADALETEYYEAGQQVISEGDVGENFYLIEYGEADVSKRGVGVVQHLKKGDYFGEVALLNDLPRQATVTATTKLKVATLGKSGFQRLLGPVVEVLRLNDPTRADKR", "text": "SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain family."}
+{"protein": "MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDAQKESTGVTTLRQRRKPVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKILETSRGADWRVAHVEVAPFYTCKKINQLISETEAVVTNELEDGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLFCGIFIVLNITLVLAAVFKLETDRSIWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRSNLSHQHLFEIAGFLGILWCLSLLACFFAPISVIPTYVYPLALYGFMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSLELKWDESKGLLPNNSEESGICHKYTYGVRAIVQCIPAWLRFIQCLRRYRDTKRAFPHLVNAGKYSTTFFMVTFAALYSTHKERGHSDTMVFFYLWIVFYIISSCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITSTTLLPHSGDIIATVFAPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQDDGVRNRQKNRSWKYNQSISLRRPRLASQSKARDTKVLIEDTDDEANT", "text": "FUNCTION: Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (PubMed:23791524, PubMed:25938945, PubMed:31043717) (By similarity). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5- InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (PubMed:27080106). FUNCTION: (Microbial infection) Confers susceptibility to xenotropic murine leukemia retrovirus (X-MLV) infection in vitro. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family."}
+{"protein": "MYRVSRTVTTCFRKKPLRINIQYRSFTKFDSFGDTPIPASKQRFVPTSGTYPKGFLVGSTNVGIKPSGLSQPDLVLVTSEEQWETCGAAVLTKNEFPAPSVLVTRELIKESRGRGVRGVVANSWCANLLTGEKGLEDSRKMSKEAGMVLEEGSTKGKDPVMVMHTGKLPIDDIIQGFPKLHQNMGTAHNHWLQAARGICTTDTFPKLSSRTFTLPSLPNTKFSIAGITKGAGMIHPNMATTLGIICTDAPITPSALQQLLSTAADKSYNCISIEGDTSTNDMVTMFANGAAAPTHSPIDFDILAASQSADFIAFQRILIEFMADLAKLVVRDGEGATKFITIRVRGAPTYPAGKHIASVIARSVLFKMGVYGKDPNPIGVLAALGYSLMDTEFAGKGIINRELTSVSFVPADGAEELNFVKRGKLMEVDELRVKELMEKEDVEVVVDLRDDGSGNGEEAIYWTCDITHEFVTINGDFRN", "text": "FUNCTION: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the ArgJ family."}
+{"protein": "MSKATKRKHVVKEVLGDYVQPTEHQSIVKVLGSPGNNLHEVETAEGERFLASMPTKFRKNIWIKRGDFLIVDPIVEGEKVKAEIAFILYKDHQRLLQKEGLWPEGFTQDKTGLVAKEKESSGIQSTEAQAKPQGEDSETDDDSGLFVNTNHVHYEDSEEESESEEDEEN", "text": "FUNCTION: May play a role into cellular response to oxidative stress. May decrease cell proliferation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EIF1AD family."}
+{"protein": "MLNMKSFALVMLFATLVGVTIASGPNGQCGPGWGGCRGGLCCSQYGYCGSGPKYCAHNTPLSEIEPTDAGRCSGRGTCSGGRCCSKYGYCGTGPAYCGLGMCQGSCLPDMPNHPAQIQARTEAAQAEAQAEAYNQANEAAQVEAYYQATQAQTQAQPQVEPAVTKAP", "text": "FUNCTION: [Antimicrobial peptide 1.1a]: Antimicrobial peptide active against the fungus A.alternata (IC(50)=8.6 uM) and the oomycetes P.infestans OSV 12 (IC(50)=11 uM) and P.infestans PRILL 2 (IC(50)=6.5 uM)."}
+{"protein": "MSEHQSLPAPEASTEVRVAIVGVGNCASSLVQGVEYYYNADDTSTVPGLMHVRFGPYHVRDVKFVAAFDVDAKKVGFDLSDAIFASENNTIKIADVAPTNVIVQRGPTLDGIGKYYADTIELSDAEPVDVVQALKEAKVDVLVSYLPVGSEEADKFYAQCAIDAGVAFVNALPVFIASDPVWAKKFTDAGVPIVGDDIKSQVGATITHRVLAKLFEDRGVQLDRTMQLNVGGNMDFLNMLERERLESKKISKTQAVTSNLKREFKTKDVHIGPSDHVGWLDDRKWAYVRLEGRAFGDVPLNLEYKLEVWDSPNSAGVIIDAVRAAKIAKDRGIGGPVIPASAYLMKSPPEQLPDDIARAQLEEFIIG", "text": "FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3- phosphate in a NAD-dependent manner. SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family."}
+{"protein": "MACCAPRCCSVRTGPATTICSSDQFCRCGVCLPSTCPHDISLLQPTFCDNSPVPYHVPDTYVPTCFLLNSSHPTPGLSGINLTTFIQPGCENACEPRC", "text": "FUNCTION: In the wool cortex, wool 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 wool shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of wool keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SIMILARITY: Belongs to the KRTAP type 3 family."}
+{"protein": "MSALNWKPFVYGGLASITAECGTFPIDLTKTRLQIQGQTNDANFREIRYRGMLHALMRIGREEGLKALYSGIAPAMLRQASYGTIKIGTYQSLKRLAVERPEDETLLVNVVCGILSGVISSAIANPTDVLKIRMQAQNSAVQGGMIDSFMSIYQQEGTRGLWKGVSLTAQRAAIVVGVELPVYDITKKHLILSGLMGDTVATHFLSSFTCGLVGALASNPVDVVRTRMMNQRALRDGRCAGYKGTLDCLLQTWKNEGFFALYKGFWPNWLRLGPWNIIFFLTYEQLKKLDL", "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. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MKLSSLPSGLGLASLLGLISSATAYSATDLTTMYDWNQIIKPLEWGQLNFIHTTDTHGWLGGHLRDARYKADFGEFKSFALRMKELADFKGVDLLMVDTGDLHDGNGLSDASDPQGIYTNNIFTYLPYDILTIGNHELYQAAISNNTHEYFVPHWNGTYLASNVQIYNSSNELEQFGGESTYFITKHGVRTLAMGFLFNFSSNANNTVVTPVETAIKSEWYQQQINRTDVDLFLLIGHIPVRDYDEWKSLHASIRKVHPNTPIQILGGHSHIRDFAVYDEASVSLEGGRYCETVGWLSIDGLSASNATRQYVGRPVTNETRQSYPNLPKPATPLYYTRRYIDFNRQNFRFHTQQSEDSFDTPEGVELSKVIKQYRDDLNLSYVFGCIPKNYYMTEVSPQAEDSIFKLMVDHILPEVLVNENRSSVPHIIISNGGGVRGSMYEGTFGPDEMFQLNPFLTNYYNYIPDVPYKYAKKLYSILNGGSTLRNVNDYLAALNPGYVTSDDFGEDGDDTVHTYVSTYAVPNVLQAQVGFNTTSAPETVDVVFLNYFQTKVLKALNTMVNETIYTLSNVTQYWVREDGKDSSPYMFAQYVQQEWSDYCD", "text": "SUBCELLULAR LOCATION: Membrane."}
+{"protein": "MVSLKLQKRLAASVMKCGKGKVWLDPNESSDISMANSRQNIRKLVKDGFIIRKPTKIHSRSRARKMKIAKMKGRHSGYGKRKGTREARLPTKVLWMRRMRVLRRLLKKYRETKKIDKHMYHDMYMRVKGNVFKNKRVLMESIHKSKAEKAREKTLSDQFEAKRAKNKASRERKHARREERLAKGPGGDVAPVAAPAPAATPAPTAAVPKKKSKK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family."}
+{"protein": "MSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPAAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG", "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 (By similarity). May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA. 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). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endosulfine family."}
+{"protein": "MSKIEISNDTRIIRHRTPARISHWMLVICFFMTMFTGVAFFFPDFAWLTEILGTPQIARAIHPFTGILMFFAFIYLALLYWDHNIPEKNDIRWAKGVIEVLKGNEHAVADNGKYNLGQKMLFWTLNLAMVTLLVTGIIMWRQYFSHYFSIPVLRIAILLHSASAFMLFTGILVHIYMAFWVKGSIRGIVEGWVTVRWAKKHHPRWYREEVLSKLEEDLLNEQSGKVGKTKVLFKGFGK", "text": "FUNCTION: Allows to use formate as major electron donor during anaerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the formate dehydrogenase gamma subunit family."}
+{"protein": "MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWVPHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMYQAVCEGTWRL", "text": "FUNCTION: May mediate the import of long-chain fatty acids (LCFA) by facilitating their transport across cell membranes (PubMed:20448275, PubMed:20530735). Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:10479480). Mainly functions as a bile acyl-CoA synthetase catalyzing the activation of bile acids via ATP-dependent formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine (PubMed:10749848, PubMed:11980911). Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates (PubMed:10749848, PubMed:11980911). In vitro, activates 3-alpha,7-alpha,12-alpha- trihydroxy-5-beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy- 5beta-cholestan-26-oate or THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol (PubMed:11980911). Plays an important role in hepatic fatty acid uptake and bile acid reconjugation and recycling but not in de novo synthesis of bile acids (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Microsome Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MAEAVFRAPKRKRRVYESYESPLPIPFSQDQSPRKEFRIFQAEMISNNVVVRGTEDMEQLYGKGYFGKGILSRSRPNFTISNPKLAARWKGVQTDMPIITSEKYQHRVEWARDFMRRQGHDESTVQKILTDYTEPLEPPYRERKGESPQHEPLSSKADSSLEGREGKDELSVTTGGAGQSDDLQGLNTHSDCRQEGPGHATLTVASPSSLNGHAIEDPEALSQIPCCSQEALGQQDDLWPEASSQIAGESRAAHEYVLIEEELCDVQEGAAPHDELLKRKRLVCRRNPYRIFEYLQLSLEEAFFLAYALGCLSIYYEKEPLTIVKLWQAFTAVQPTFRTTYMAYHYFRSKGWVPKVGLKYGTDLLLYRKGPPFYHASYSVIIELVDDNFEGSLRRPFSWKSLAALSRVSGNVSKELMLCYLIKPSTMTNEDMETPECMRRIQVQEVILSRWVSSRERSDQDEL", "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": "MTDNIMKDHRHIFLPQPVKADEKPGAFSERFGWKLLLDTPRKKNVYEGTKFMSQDFWPTPLVKTTAPKVKLIPADAPPQSAKFWKAPLLKDTPRQSNVIPGDFLPFSNTFGLATIQRR", "text": "FUNCTION: Seems to be required for the LH-II stabilization."}
+{"protein": "MFARGSRRRRSGRAPPEAEDPARGQPCNSCREQCPGFLLHGWRKICQHCKCPREEHAVRTVPVDLERIMCRLISDFQRHSISDDDSGCASEEYAWVPPGLKPEQVYQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSEAQYCTALEEEEKKELRAFSQQRKRENLGRATVRIFPVTITGAICEECGKQIGGGDIAVFASRAGLGACWHPQCFVCTTCQELLVDLIYFYHAGKVYCGRHHAECLRPRCQACDEIIFSPECTEAEGRHWHMGHFCCFECEASLGGQRYVMRQSRPHCCACYEARHAEYCDGCGEHIGLDQGQMAYEGQHWHASDRCFCCSRCSRPLLGRPFLPRRGLIFCSRACSLGSETTAPGPGRRSWSAGTVTTPLTTSTASFSATEGTSETASKGTCTKAEPAAGPEEPSHFLRGAPHRHSMPELGLRSAPEPPTESPGHPAPHPDDNAFGRQSTPRVSFRDPLVSEGGPRRTLSAPPAQRRRPRSPPPRTPSCHHHHHHRRRRQRHRRRGSHHHHHHPGRHGHHRCDLGSGSDSGSCSSSPSSPSSESSEDDGFFLGERIPLPPHLCRPRTTQDTSTETFNSPAQPLVQESHPVMPRQTRDKNCIVA", "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, PRICKLE3 being part of the core module (By similarity). Distinct complexes of the core module segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (By similarity). 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) (PubMed:32516135). 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": "MNCYPAGHLLGKGHVQLNESGENAELISQEQIGDDLNGWHRDAFEDIASRLTDPGFPCVFSRNAFRKKLVKFVFVEGSGKEDIRHLGAGLKDYVELSRDWDGALDTAYPLVVVFSADAVTADSVEQYHAFGWWVLQELHAIDPTPWPEGVDKGPQSEAWSMCFHGMPLFINMSSPAHQVRRSRNLGRHFALVINPRERFDVFAGDTPSGRKVRSNIRGRIARYDGTPHAQQLGSYGTGALEWMQYGLVEENRERADVCPFTFRGA", "text": "FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Could catalyze the production of N(omega)- hydroxy-L-arginine (NHA) from L-arginine. SIMILARITY: Belongs to the DcsA family."}
+{"protein": "MDKLTDLNYTLSVITLMNSTLHTILEDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVVKYCIVTIFNALLKLAGYKEQITTKDEIEKQTDRVVKEMRRQLEMIDKLTTREIEQVELLKRIHDKLMIRAVDEIDMTKEINQKNVKTLEEWENGKNPYEPKEVTAAM", "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": "MENRVADELIHLPLPEVQAVNVINVRHGDGDGDGENGWERHLDDEQMQAMRLENPQVAMLLDAPHEPPIELHHMLEPVNVPERPRKKRSFLTISKPFHVQPERCALISNGWRAVQCVQPEKRGECFANYLIKHMNSRNYPNGEGLPKRWGQY", "text": "FUNCTION: Post-meiotically transcribed gene that has a role in late spermiogenesis; required for actin cone progression during spermatid individualization. SIMILARITY: Belongs to the male-specific scotti family."}
+{"protein": "MSIQAIVLATFDAKEGYNVENYYPGDFNVEGIEYLLFPSGIQELDNCTIFFRFQDQLCLSVFSKLQHPSFERSAFFTSVGLILSDDINFGEAVVKYGETLLYIANGLSLATLKYKFGEDASETYASEKCTSHQLSDSDFFKSLQTSAVNLEFDSLFEKLQGNKFAILGANSKELSQSYATILLDHLGPAFYCLYKFALQRKRILLISSHDDQLYSIIDMIVRLSSIKRSSDASIPILLSDLHPFYSVGLANTSTLLDNDLEEGWIACTTDTVLLSKSSLYDLALYWPDNSFNANKYPQIFNSNSIRIKPSYDDLINFKGLSRYLSFDGESSWGLTTYSLASKYIFNTSHHNLTDQEFLNENMLDYFQRYNQKLLTVLSSNAESFNVSDMQTLGLNPCHSLDKSFVSEISQIWLKKHINWQYGKYFWLRRVSLIFLASTCFLFILWKLL", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass membrane protein Endoplasmic reticulum membrane; Single-pass membrane protein."}
+{"protein": "MARNKPLAKKLRLAKAAKQNRRVPVWVIVKTNRKVMTHPKRRHWRRTKLKE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family."}
+{"protein": "MRILTFTGKGGVGKTSVSAATAVRLSEMGHRTLVLSTDPAHSLSDSFNIQLGAEPTKIKENLHAIEVNPYVDLKQNWHSVQKYYTRIFMAQGVSGVMADEMTILPGMEELFSLLRIKRYKSAGLYDALVLDTAPTGETLRLLSLPDTLSWGMKAVKNVNKYIVRPLSKPLSKMSDKIAYYIPPEDAIESVDQVFDELEDIREILTDNVKSTVRLVMNAEKMSIKETMRALTYLNLYGFKVDMVLVNKLLDAQENSGYLEKWKGIQQKYLGEIEEGFSPLPVKKLKMYDQEIVGVKSLEVFAHDIYGDTDPSGMMYDEPPIKFVRQGDVYEVQLKLMFANPVDIDVWVTGDELFVQIGNQRKIITLPVSLTGLEPGDAVFKDKWLHIPFDLEKQGQHHRTREYNKA", "text": "FUNCTION: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity). SIMILARITY: Belongs to the arsA ATPase family."}
+{"protein": "MPLLLSGKKFHNDLKKNKCLAMFAPLEGGYETRLLRRMRAKGFKTYITSARGLGDPEVFLLNLHGIRPPHLGHQSIGRNGALGEVQQVIPQASELFNENDKDKLLWLLEGQVLSQSELENLIKLPTADNKLKIVVEMGGSRKLEWKSLNDYVLNEF", "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 NdhN subunit family."}
+{"protein": "MPSTDLKKQADAAVESDVNTNNEAVESSTKEESSNTPSTETQPEKKAEEPEAAAEPSESTSTPTNASSVATPSGTAPTSASLYVGELDPSVTEAMLFELFNSIGPVASIRVCRDAVTRRSLGYAYVNFHNMEDGEKALDELNYTLIKGRPCRIMWSQRDPSLRKMGTGNVFIKNLDPAIDNKALHDTFSAFGKILSCKVAVDELGNAKGYGFVHFDSVESANAAIEHVNGMLLNDKKVYVGHHVSRRERQSKVEALKANFTNVYIKNLDTEITEQEFSDLFGQFGEITSLSLVKDQNDKPRGFGFVNYANHECAQKAVDELNDKEYKGKKLYVGRAQKKHEREEELRKRYEQMKLEKMNKYQGVNLFIKNLQDEVDDERLKAEFSAFGTITSAKIMTDEQGKSKGFGFVCYTTPEEANKAVTEMNQRMLAGKPLYVALAQRKEVRRSQLEAQIQARNQFRLQQQVAAAAGIPAVQYGATGPLIYGPGGYPIPAAVNGRGMPMVPGHNGPMPMYPGMPTQFPAGGPAPGYPGMNARGPVPAQGRPMMMPGSVPSAGPAEAEAVPAVPGMPERFTAADLAAVPEESRKQVLGELLYPKVFVREEKLSGKITGMLLEMPNSELLELLEDDSALNERVNEAIGVLQEFVDQEPGFTE", "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": "MGTRLTTLSNGLKNTLTATKSGLHKAGQSLTQAGSSLKTGAKKIILYIPQNYQYDTEQGNGLQDLVKAAEELGIEVQREERNNIATAQTSLGTIQTAIGLTERGIVLSAPQIDKLLQKTKAGQALGSAESIVQNANKAKTVLSGIQSILGSVLAGMDLDEALQNNSNQHALAKAGLELTNSLIENIANSVKTLDEFGEQISQFGSKLQNIKGLGTLGDKLKNIGGLDKAGLGLDVISGLLSGATAALVLADKNASTAKKVGAGFELANQVVGNITKAVSSYILAQRVAAGLSSTGPVAALIASTVSLAISPLAFAGIADKFNHAKSLESYAERFKKLGYDGDNLLAEYQRGTGTIDASVTAINTALAAIAGGVSAAAAGSVIASPIALLVSGITGVISTILQYSKQAMFEHVANKIHNKIVEWEKNNHGKNYFENGYDARYLANLQDNMKFLLNLNKELQAERVIAITQQQWDNNIGDLAGISRLGEKVLSGKAYVDAFEEGKHIKADKLVQLDSANGIIDVSNSGKAKTQHILFRTPLLTPGTEHRERVQTGKYEYITKLNINRVDSWKITDGAASSTFDLTNVVQRIGIELDNAGNVTKTKETKIIAKLGEGDDNVFVGSGTTEIDGGEGYDRVHYSRGNYGALTIDATKETEQGSYTVNRFVETGKALHEVTSTHTALVGNREEKIEYRHSNNQHHAGYYTKDTLKAVEEIIGTSHNDIFKGSKFNDAFNGGDGVDTIDGNDGNDRLFGGKGDDILDGGNGDDFIDGGKGNDLLHGGKGDDIFVHRKGDGNDIITDSDGNDKLSFSDSNLKDLTFEKVKHNLVITNSKKEKVTIQDWFREADFAKEVPNYKATKDEKIEEIIGQNGERITSKQVDDLIAKGNGKITQDELSKVVDNYELLKHSKNVTNSLDKLISSVSAFTSSNDSRNVLVAPTSMLDQSLSSLQFARAA", "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. SUBCELLULAR LOCATION: Secreted Host cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family."}
+{"protein": "MSTIVTVPRSVSWKGDAIAVLNQTKLPHSTEYKTLTTIEEVWKSIIMLEVRGAPAIGIVAAFGLALAAKKYNTLHIEEFQKKFNRDCNYLGTSRPTAVNLFWAIDRMRESIREITTIKEAQKILEEEALRIQQEDEEVCRNIGEYALTCFKDGDNILTICNAGSIATARYGTALAPFYIGKEKGVRLHAYACETRPVLQGGRLTTWELKQANIDVTLITDNTAAHAIQTKEINAIIVGADRIVANGDTANKIGTMNLAILAKYFNIPFYVAAPLSTFDVTKETGAEIIIEERDETEVTKIFGKQVAPIGTDVYNPAFDITPNELITGIITEKGIIRGDYKREIASLFEKQANT", "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": "MAPTEIKTLSFLDSSKSNYNLNPLKFQGGFAFKRKDSGCTAAKRVHCSAQSQSPPPAWPGRAFPEPGRMTWEGPKPISVIGSTGSIGTQTLDIVAENPDKFRIVALAAGSNVTLLADQVKAFKPKLVSVKDESLISELKEALAGFEDMPEIIPGEQGMIEVARHPDAVTVVTGIVGCAGLKPTVAAIEAGKDIALANKETLIAGGPFVLPLAKKHNVKILPADSEHSAIFQCIQGLPEGALRRIILTASGGAFRDLPVEKLKEVKVADALKHPNWNMGKKITVDSATLFNKGLEVIEAHYLFGAEYDDIEIVIHPQSIIHSMVETQDSSVLAQLGWPDMRLPILYTLSWPERIYCSEITWPRLDLCKVDLTFKKPDNVKYPSMDLAYAAGRAGGTMTGVLSAANEKAVEMFIDEKIGYLDIFKVVELTCDKHRSEMAVSPSLEEIVHYDQWARDYAATVLKSAGLSPALV", "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). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the DXR family."}
+{"protein": "MYSSEELWNSTEQVWINGSGTNFSLGRHEDDEEEEGDKHPFFTDAWLVPLFFSLIMLVGLVGNSLVIYVISKHRQMRTATNFYIANLAATDIIFLVCCVPFTATLYPLPGWIFGNFMCKFVAFLQQVTVQATCITLTAMSGDRCYVTVYPLKSLRHRTPKVAMIVSICIWIGSFVLSTPILMYQRIEEGYWYGPRQYCMERFPSKTHERAFILYQFIAAYLLPVLTISFCYTLMVKRVGQPTVEPVDNNYQVNLLSERTISIRSKVSKMVVVIVLLFAICWGPIQIFVLFQSFYPNYQPNYATYKIKTWANCMSYANSSVNPIVYGFMGASFQKSFRKTFPFLFKHKVRDSSMASRTANAEIKFVAAEEGNNNNAVN", "text": "FUNCTION: Receptor speculated to be essential for sexual development. May regulate gonadotropin-releasing hormone (GnRH) secretion. The receptor expression could be a 'stop signal' for GnRH1, GnRH2, and GnRH3 neuronal migration, leading to suppression of cell growth and modulation of GnRH secretion, which is important for normal sexual development. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MDPSSGGGGGGGGGGSSSSSDSAPDCWDQTDMEAPGPGPCGGGGSGSGSMAAVAEAQRENLSAAFSRQLNVNAKPFVPNVHAAEFVPSFLRGPAQPPLSPAGAAGGDHGAGSGAGGPSEPVESSQDQSCEGSNSTVSMELSEPVVENGETEMSPEESWEHKEEISEAEPGGGSSGDGRPPEESTQEMMEEEEEIPKPKSAVAPPGAPKKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETEKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSNERYEECKEKLVPFLKKVGFNPKKDIHFMPCSGLTGANLKEQSDFCPWYIGLPFIPYLDNLPNFNRSVDGPIRLPIVDKYKDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILCDLNNLCHSGRTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETFKDFPQMGRFTLRDEGKTIAIGKVLKLVPEKD", "text": "FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA. GSPT1/ERF3A mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site. GTP hydrolysis by GSPT1/ERF3A induces a conformational change that leads to its dissociation, permitting ETF1/ERF1 to accommodate fully in the A-site. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Required for SHFL-mediated translation termination which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and cellular genes. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. ERF3 subfamily."}
+{"protein": "MDMADEPLNGSHTWLSIPFDLNGSVVSTNTSNQTEPYYDLTSNAVLTFIYFVVCIIGLCGNTLVIYVILRYAKMKTITNIYILNLAIADELFMLGLPFLAMQVALVHWPFGKAICRVVMTVDGINQFTSIFCLTVMSIDRYLAVVHPIKSAKWRRPRTAKMITMAVWGVSLLVILPIMIYAGLRSNQWGRSSCTINWPGESGAWYTGFIIYTFILGFLVPLTIICLCYLFIIIKVKSSGIRVGSSKRKKSEKKVTRMVSIVVAVFIFCWLPFYIFNVSSVSMAISPTPALKGMFDFVVVLTYANSCANPILYAFLSDNFKKSFQNVLCLVKVSGTDDGERSDSKQDKSRLNETTETQRTLLNGDLQTSI", "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. 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. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MENELPVPHTSSSACATSSTSGASSSSGCNNSSSGGSGRPTGPQISVYSGIPDRQTVQVIQQALHRQPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVSNRQGSTSGSNVSAQAPAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMLIFTPTATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTANLHKPGGSQQCHPPTPDTGPQNGHPEGVPHTPQRRFQHTSAVILQLQPASPPQQCVPDDWKEVAPGEKSVPETRSGPSPHQQAIVTAMPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMTSGNGNSASSIAGTAPQNGENKPPQAIVKPQILTHVIEGFVIQEGAEPFPVGRSSLLVGNLKKKYAQGFLPEKLPQQDHTTTTDSEMEEPYLQESKEEGAPLKLKCELCGRVDFAYKFKRSKRFCSMACAKRYNVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQPTGTVPLSVTAALQLTHSQEDSSRCSDNSSYEEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPSEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKDS", "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. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MVPLEDLLNKENGTAAPQHSRESIVENGTDVSNVTKKDGLPSPNLSKRSSDCSKRPRIRCTTEAIGLNGQEDERMSPGSTSSSCLPYHSTSHLNTPPYDLLGASAVSPTTSSSSDSSSSSPLAQAHNPAGDDDDADNDGDSEDITLYCKWDNCGMIFNQPELLYNHLCHDHVGRKSHKNLQLNCHWGDCTTKTEKRDHITSHLRVHVPLKPFGCSTCSKKFKRPQDLKKHLKIHLESGGILKRKRGPKWGSKRTSKKNKSCASDAVSSCSASVPSAIAGSFKSHSTSPQILPPLPVGISQHLPSQQQQRAISLNQLCSDELSQYKPVYSPQLSARLQTILPPLYYNNGSTVSQGANSRSMNVYEDGCSNKTIANATQFFTKLSRNMTNNYILQQSGGSTESSSSSGRIPVAQTSYVQPPNAPSYQSVQGGSSISATANTATYVPVRLAKYPTGPSLTEHLPPLHSNTAGGVFNRQSQYAMPHYPSVRAAPSYSSSGCSILPPLQSKIPMLPSRRTMAGGTSLKPNWEFSLNQKSCTNDIIMSKLAIEEVDDESEIEDDFVEMLGIVNIIKDYLLCCVMEDLDDEESEDKDEENAFLQESLEKLSLQNQMGTNSVRILTKYPKILV", "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 RIM101 itself), mainly by repressing transcriptional repressors of those genes, and represses transcription of acid- expressed genes. Required for meiosis, sporulation and invasive growth. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pacC/RIM101 family."}
+{"protein": "MSGILTRWRQFGKRYFWPHLLLGMVAASLGLPALSNAAEPNAPAKATTRNHEPSAKVNFGQLALLEANTRRPNSNYSVDYWHQHAIRTVIRHLSFAMAPQTLPVAEESLPLQAQHLALLDTLSALLTQEGTPSEKGYHIDYAHFTPQAKFSTPVWISQAQGIRAGPQRLS", "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": "MKFQSTLLLAAAAGSALAVPHGPGHKKRASVFEWFGSNESGAEFGTNIPGVWGTDYIFPDPSAISTLIDKGMNFFRVQFMMERLLPDSMTGSYDEEYLANLTTVIKAVTDGGAHALVDPHNYGRYNGEIISSTSDFQTFWENLAGQYKDNDLVMFDTNNEYHDMDQDLVLNLNQAAINGIRAAGATSQYIFVEGNSWTGAWTWVDVNDNMKNLTDPEDKIVYEMHQYLDSDGSGTSETCVSETIGKERVTEATQWLKDNKKVGFIGEYAGGSNDVCRSAVSGMLEYMANNTDVWKGASWWAAGPWWGDYIFSMEPPDGTAYTGMLDILEAYL", "text": "FUNCTION: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
+{"protein": "MIQLNNGIRIFVNHSMKKDIYIGISDFGFEKDINDGILGIAHLLEHILISFDNKYFNANASTSRTYMSFWCVALQKRHYEDAIRTAISWFFDKKYILKTDFSRIVLENYITELENEYYYRTEMYHCMDVLAYLYGGDLYNGGRITMLERLPEIRNMLSNRMKFLSGKNIVIFVKRLTNNILTLLTNTFGSIPKYPIIIPLDPQIQDARRKIIMMPCPFYTLLIQVDNTMNNLLAIICLVENYNLIDYETISDKLYVCISFANEDQYEYLLYNIKDMDFNINRIELDLGEDYIMNLYINFPWLKNDIFEYIHTMNTKSAMLLADLKKNMHNSILEHKFMIIYPSFTKLLYNITDKQNHGILVVGDVSFTPEKDPSMHHSNKENNNNYSKTVTKRKSKYVMYRKTPTTNNIVIDYTDSSFFDYATFYHVMKSKYEKTNLFSRLKTSTGMCYKHCFDNDDLNELINSDTFIRYNSSKPAVLYQYILLAYFVTERDIKELVDYKDAIELDMKYYSKNKILFGKNTRYDIRTKSMFVCGLIKGRKLSEKVITDYMWKLKSLGLIYYLTSIKLGISNTFYIFAFTIFPEKVYNFFVGLKEITNRCLIVSNKNTKIEEDDYSSLNKQIVIGIK", "text": "FUNCTION: Seems to be involved in viral proteins maturation by cleavage at Ala-Gly-|-Xaa motifs. SIMILARITY: Belongs to the peptidase M44 family."}
+{"protein": "MHTEDNGLKKEIGLLFALTLVIGTIIGSGVFMKPGAVLAYSGDSKMALFAWLLGGILTLAGGLTIAEIGTQIPKTGGLYTYLEEVYGEFWGFLCGWVQIIIYGPAIIGALGLYFGSLMANLFGWGSGLSKVIGIIAVLFLCVINIIGTKYGGFVQTLTTIGKLIPIACIIVFGLWKGDQHIFTAVNESISDMNFGAAILATLFAYDGWILLAALGGEMKNPEKLLPRAMTGGLLIVTAIYIFINFALLHILSANEIVTLGENATSTAATMLFGSIGGKLISVGIIVSIFGCLNGKVLSFPRVSFAMAERKQLPFAEKLSHVHPSFRTPWIAISFQIALALIMMLISNPDKLSEISIFMIYIFYVMAFFAVFILRKRAKGEKRAYSVPLYPFMPILAIAGSFFVLGSTLITDTMSCGLSILIGLAGLPVYYGMKKRKAS", "text": "FUNCTION: Exhibits an obligate exchange activity for serine, threonine and aromatic amino acids. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family."}
+{"protein": "MPLTPPPNPQKTYQIAILALGLVLLAFVLISDHSPKVGDHLHNLPFGGEYKDGTKSIKYFQRPNQHSLSKTLAKSHNTTIFLLILGLIVTLHGLHYFNNNRRVSSSLHCVLCQNKH", "text": "FUNCTION: Plays a role in viral cell-to-cell propagation, by facilitating genome transport to neighboring plant cells through plasmosdesmata,. SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the Tymovirales TGBp2 protein family."}
+{"protein": "MASASTSKYNSHSLENESIKRTSRDGVNRDLTEAVPRLPGETLITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSSLILDVPLGVISRIEKMGGATSRGENSYGLDITCKDMRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPLFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKDDEKYLDVIRETNKQISKLTIYDARPSVNAVANKATGGGYESDDAYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHTDADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLIIILDHLYSCRFGTFLFNCESARERQKVTERTVSLWSLINSNKEKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYMELLALRDEYIKRLEELQLANSAKLSDPPTSPSSPSQMMPHVQTHF", "text": "FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) (PubMed:11001925, PubMed:10900271, PubMed:12646134, PubMed:14722070). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides (PubMed:9537414). Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome (PubMed:14722070). Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture (PubMed:21135508). Plays a role in mitochondrial morphology and positioning (PubMed:21135508). Required for skeletal muscle maintenance but not for myogenesis (PubMed:21135508). In skeletal muscles, stabilizes MTMR12 protein levels (PubMed:23818870). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Cell projection, filopodium Cell projection, ruffle Late endosome Cytoplasm, myofibril, sarcomere Note=Localizes as a dense cytoplasmic network (PubMed:11001925). Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles (PubMed:12118066). Predominantly located in the cytoplasm following interaction with MTMR12 (PubMed:12847286). Recruited to the late endosome following EGF stimulation (PubMed:14722070). In skeletal muscles, co-localizes with MTMR12 in the sarcomere (By similarity). SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily."}
+{"protein": "MSQTKTLKVRVALLCILVGIVLALVAVVTDHWAVLSPHVEHHNSTCEAAHFGLWRICTKRIFVGDKERSCGPITLPGEKNCSYFRHFNPGESSEIFEVTTQKEYSISAAAIAIFSLGFIIVGTLCALLSFRKKRDYLLRPASMFYIFAGLCLSVSAEVMRQSVQRMVDSEHTAWIAHSLAWSFICACVAAALLLVGGLALLLLALPRMPRDPWESCMDAEPEH", "text": "FUNCTION: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics. SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Multi-pass membrane protein. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily."}
+{"protein": "MAERALEPEAEAEAEAGAGGEAAAEEGAAGRKARGRPRLTESDRARRRLESRKKYDVRRVYLGEAHGPWVDLRRRSGWSDAKLAAYLISLERGQRSGRHGKPWEQVPKKPKRKKRRRRNVNCLKNVVIWYEDHKHRCPYEPHLAELDPTFGLYTTAVWQCEAGHRYFQDLHSPLKPLSDSDPDSDKVGNGLVAGSSDSSSSGSASDSEESPEGQPVKAAAAAAAATPTSPVGSSGLITQEGVHIPFDVHHVESLAEQGTPLCSNPAGNGPEALETVVCVPVPVQVGAGPSALFENVPQEALGEVVASCPMPGMVPGSQVIIIAGPGYDALTAEGIHLNMAAGSGVPGSGLGEEVPCAMMEGVAAYTQTEPEGSQPSTMDATAVAGIETKKEKEDLCLLKKEEKEEPVAPELATTVPESAEPEAEADGEELDGSDMSAIIYEIPKEPEKRRRSKRSRVMDADGLLEMFHCPYEGCSQVYVALSSFQNHVNLVHRKGKTKVCPHPGCGKKFYLSNHLRRHMIIHSGVREFTCETCGKSFKRKNHLEVHRRTHTGETPLQCEICGYQCRQRASLNWHMKKHTAEVQYNFTCDRCGKRFEKLDSVKFHTLKSHPDHKPT", "text": "FUNCTION: Transcriptional repressor. May repress NR5A1, PPARG, NR1H3, NR4A2, ESR1 and NR3C1 transcriptional activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MRHPFKVVVVTGVPGVGKTTVIKELQGLAEKEGVKLHIVNFGSFMLDTAVKLGLVEDRDKIRTLPLRRQLELQREAAKRIVAEASKALGGDGVLIIDTHALVKTVAGYWPGLPKHVLDELKPDMIAVVEASPEEVAARQARDTTRYRVDIGGVEGVKRLMENARAASIASAIQYASTVAIVENREGEAAKAAEELLRLIKNL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal adenylate kinase family."}
+{"protein": "MAILQTFSEQTISSARASDIKEPDYSVNSRPEICFFLNGIMEEKSLISLYLARDSHSAILSSILAVDPQQKLLIMDYGINETLNQIALKRGYLRCITSHNQIRIEFDCDNLQRVQFEGRHAFSADIPESLKRLQRRNFYRVTTSITNPAVCTIPLLRAADEAPVVYSLLDISCGGMALIDQPDADTLLKAGTTLEHCRIDLPGDGNLFSSIEASIQIAYVGTVILNNGNTCPRIGCEFINLPEKSRLLIQRYITKLEQQARKLETESGF", "text": "FUNCTION: Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Binds 1 c-di-GMP dimer per subunit. Increasing levels of c-di-GMP lead to decreased motility. SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the YcgR family."}
+{"protein": "MGLMWGLFSVIIASVAQLSLGFAASHLPPMTHLWDFIAALLAFGLDARILLLGLLGYLLSVFCWYKTLHKLALSKAYALLSMSYVLVWIASMVLPGWEGTFSLKALLGVACIMSGLMLIFLPTTKQRY", "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. 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. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ArnF family. SIMILARITY: Belongs to the ArnF family."}
+{"protein": "MKRNRFFNTSAAIAISIALNTFFCSMQTIAAEPEETYLDFRKETIYFLFLDRFSDGDPSNNAGFNSATYDPNNLKKYTGGDLRGLINKLPYLKSLGVTSIWITPPIDNVNNTDAAGNTGYHGYWGRDYFRIDEHFGNLDDFKELTSLMHSPDYNMKLVLDYAPNHSNANDENEFGALYRDGVFITDYPTNVAANTGWYHHNGGVTNWNDFFQVKNHNLFNLSDLNQSNTDVYQYLLDGSKFWIDAGVDAIRIDAIKHMDKSFIQKWTSDIYDYSKSIGREGFFFFGEWFGASANTTTGVDGNAIDYANTSGSALLDFGFRDTLERVLVGRSGNTMKTLNSYLIKRQTVFTSDDWQVVFMDNHDMARIGTALRSNATTFGPGNNETGGSQSEAFAQKRIDLGLVATMTVRGIPAIYYGTEHYAANFTSNSFGQVGSDPYNREKMPGFDTESEAFSIIKTLGDLRKSSPAIQNGTYTELWVNDDILVFERRSGNDIVIVALNRGEANTINVKNIAVPNGVYPSLIGNNSVSVANKRTTLTLMQNEAVVIRSQSDDAENPTVQSINFTCNNGYTISGQSVYIIGNIPQLGGWDLTKAVKISPTQYPQWSASLELPSDLNVEWKCVKRNETNPTANVEWQSGANNQFNSNDTQTTNGSF", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLGQ", "text": "FUNCTION: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53 (PubMed:11696557). Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M (By similarity). FUNCTION: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53. Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING- based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M. SUBCELLULAR LOCATION: Nucleus Note=Mainly nuclear. SUBCELLULAR LOCATION: Nucleus Note=Mainly nuclear. SIMILARITY: Belongs to the ubiquitin family."}
+{"protein": "MAEAFTSFTFTNLHIPSSYNHSPKQNSGPNHGYWLSKNVNEKRERNLMRGSLCVRKALPHDLPLMAVMVQQIEGMRDIITEKHVWHLSDKAIKNVYMFYIMFTCWGCLYFGSAKDPFYDSEEYRGDGGDGTGYWVYETQEDIEEKARAELWREELIEEIEQKVGGLRELEEAVTK", "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; Single-pass membrane protein."}
+{"protein": "MSDNSKTRVVVGMSGGVDSSVTALLLKEQGYDVIGIFMKNWDDTDENGVCTATEDYKDVVAVADQIGIPYYSVNFEKEYWDRVFEYFLAEYRAGRTPNPDVMCNKEIKFKAFLDYAITLGADYVATGHYARVARDEDGTVHMLRGVDNGKDQTYFLSQLSQEQLQKTMFPLGHLEKPEVRRLAEEAGLSTAKKKDSTGICFIGEKNFKNFLSNYLPAQPGRMMTVDGRDMGEHAGLMYYTIGQRGGLGIGGQHGGDNAPWFVVGKDLSKNILYVGQGFYHDSLMSTSLEASQVHFTREMPEEFTLECTAKFRYRQPDSKVTVHVKGEKTEVIFAEPQRAITPGQAVVFYDGEECLGGGLIDNAYRDGQVCQYI", "text": "FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmA/TRMU family. SIMILARITY: Belongs to the MnmA/TRMU family."}
+{"protein": "MGGCLSGDVKGGKQAIGGVQQRPTSSTIANNAAHNDAVDFFFRSRGQYPLFSQIELTLSASNLLDCDITSKSDPMAVMYLRKKDGRLEEIGRTEVILNNLNPKWIEKITVSFQFEAVQTLVFHVYDVDTRYHNVPVKTLKLKDQDFLGEGTCVLSEIMTRQNRTLTLTLTGNVRAGVNRNLGTLSIQAEETVASKTVAEINFRCVNLDNKDLFSKSDPFLRISRVVETSAAVPICRTEVVDNNLNPMWRPVCLTMQQFGSKDTPLVIECLDFNTSGNHELIGKTEKSVAELERLCLQKEAANFVYPSLSHGRNKVLKGQLIVDRYVEKVQYSFLDYISSGFELNFMVAVDFTASNGDPRTPSSLHYIDPSGRLNSYQQAIMEVGEVIQFYDSDKRFPAWGFGGRTSDGSVSHAFNLNGASYGDEVVGVEGIMVAYASALRNVSLAGPTLFSNVVDKAAHTASQSLSQNSPKYFVLLIITDGVLTDMAGTVDALVRASDLPLSVLIVGVGNTDFKQMEMLDADNGRRLESSTGRIATRDIVQFVPMKDIHSGLVSVVQALLEELPGQFLTYVRSRKINPIGAPAI", "text": "FUNCTION: Negative regulator of cell death and defense responses. Repress a number of R genes and may have effects in promoting growth and development. May function in membrane trafficking and in fusion of vesicles with plasma membrane (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the copine family."}
+{"protein": "MSKHIVILGAGYGGVLSALTVRKHYTKEQARVTVVNKYPTHQIITELHRLAAGNVSEKAVAMPLEKLFKGKDIDLKIAEVSSFSVDKKEVALADGSTLTYDALVVGLGSVTAYFGIPGLEENSMVLKSAADANKVFQHVEDRVREYSKTKNEADATILIGGGGLTGVELVGELADIMPNLAKKYGVDHKEIKLKLVEAGPKILPVLPDDLIERATASLEKRGVEFLTGLPVTNVEGNVIDLKDGSKVVANTFVWTGGVQGNPLVGESGLEVNRGRATVNDFLQSTSHEDVFVAGDSAVYFGPDGRPYPPTAQIAWQMGELIGYNLFAYLEGKTLETFKPVNSGTLASLGRKDAVAIIGANSTPLKGLPASLMKEASNVRYLTHIKGLFSLAY", "text": "SIMILARITY: Belongs to the NADH dehydrogenase family."}
+{"protein": "MIHDTSARSRTAVFSAWRGRCSRLTRDRWRVALLILLSIAVGAVGWSGEALLLPTAMLFPLLWAQSPSRLVAGAVSAGYFLTASRGLPQGVANFYAADFWHGLLLWLAASAGFVAVHAAFWPARLQKRLPGRGALGWGKPVRYLAAAVLMGLPPFGITGWAHPLTAAGILFPGFGWWGLGATTAGLAMMTSRYWPAAAIALGGFWFWSAATWTQPVLPDGWKGVDLEQGQTLGRDGSLDHHRDLIATVRAAAGAETRVIVLPESALGLWTPTVARLWQAGLRGADVTVIAGAAVIDPGGYDNVMVTVSEGETRILYRERMPIPVSMWQPWLQWTGQGGGAQAHFFANPAVDLAGTRIAPLICYEQLIVWPILHSMLFSPAAIVATGNGWWTEGTSIVAIQQAGVIAWAKLFGRPVVTAFNT", "text": "FUNCTION: Enhances conjugal transfer of the Ti plasmid. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MVKSLQLAHQLKDKKILLIGGGEVGLTRLYKLIPTGCKLTLVSPDLHKSIIPKFGKFIQNEDQPDYREDAKRFINPNWDPTKNEIYEYIRSDFKDEYLDLEDENDAWYIIMTCIPDHPESARIYHLCKERFGKQQLVNVADKPDLCDFYFGANLEIGDRLQILISTNGLSPRFGALVRDEIRNLFTQMGDLALEDAVVKLGELRRGIRLLAPDDKDVKYRMDWARRCTDLFGIQHCHNIDVKRLLDLFKVMFQEQNCSLQFPPRERLLSEYCSS", "text": "FUNCTION: Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme. SIMILARITY: Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. MET8 subfamily."}
+{"protein": "MPVLSTPSRPSRVTTLKRTAVVLALTAYGVHKIYPLVRQCLTPARGPQVPAGESTQEASGATTAKAGMNRVFLQRLLVLLRLLFPGVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFSWQLLQWLLIALPATFINSAIRYLEGQLALSFRSRLVAHAYGLYFSQQTYYRVSNMDGRLRNPDQSLTEDMVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAGTAWPSAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQHSYQDLASQINLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATGYAESDSEAMKKAALEMKEEELVSERTEAFTIARNLLTAAADATERIMSSYKEVTELAGYTARVYEMFQVFEDVQHCRFKRTGDLEEAQAGPGSMVHSGVHIEGPLKIQGQVVDVEQGIICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSAEDMRRKGCSEQQLEAILGIVHLRHILQREGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGISLLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAARLSLTEEKQRLEQQLAGIPKMQGRLQELRQILGEAAAPVQPLVPGIPT", "text": "FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)- CoA from the cytosol to the peroxisome lumen (PubMed:12176987). Coupled to the ATP-dependent transporter activity has also a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-dependent transport into peroxisomes, the ACOT activity is essential during this transport process (By similarity). Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (PubMed:25043761). Involved in several processes; namely, controls the active myelination phase by negatively regulating the microsomal fatty acid elongation activity and may also play a role in axon and myelin maintenance. Controls also the cellular response to oxidative stress by regulating mitochondrial functions such as mitochondrial oxidative phosphorylation and depolarization. And finally controls the inflammatory response by positively regulating peroxisomal beta- oxidation of VLCFAs (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein Mitochondrion membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily."}
+{"protein": "MESHLGNGVGSSRSAKNTKNTSSSVDWLSRDMLEMKIRDKTEADEERDSEPDIIDGVGAEPGHVITTTLPGRNGQSRQTVSYIAEHVVGTGSFGMVFQAKCRETGEVVAIKKVLQDKRYKNRELQIMQMLDHPNVVCLKHSFYSRTENEEVYLNLVLEFVPETVNRTARSYSRMNQLMPLIYVKLYTYQICRGLAYLHNCCGLCHRDIKPQNLLVNPHTHQLKICDFGSAKVLVKGEPNISYICSRYYRAPELIFGATEYTTAIDIWSTGCVMAELLLGQPLFPGESGVDQLVEIIKVLGTPTREEIKCMNPNYTEFKFPQIKPHPWHKVFQKRLPPEAVDLLCRFFQYSPNLRCTAVEACIHPFFDELRDPNARLPNGRPLPPLFNFKPQELSGIPPETVDRLVPEHARKQNHFMALHS", "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": "MILIASPFSLAHLEYLHTWHVTIKNIAQQHGLDIKVAIVVSTSHLNTFLPISTALNIECITFPGCGIKEIDLLWARIKLFQHYCAIGARLLWLVSADIRPPVSTWPAIADSLKKGADAVVIPYPSRWNNLIPTVIKEIVVHQKKCLVAVDARHLDTDTQIVGAGMGCIVLTLKALMVRLSIGKQPIKILWPDLHGTAEGIPLEGVEVGWFLNAYAHKLNIRCLGAEHIAQHFI", "text": "SIMILARITY: Belongs to the asfivirus H233R family."}
+{"protein": "MEAAGSPAATETGKYIASTQRPDGTWRKQRRVKEGYVPQEEVPVYENKYVKFFKSKPELPPGLSPEATAPVTPSRPEGGEPGLSKTAKRNLKRKEKRRQQQEKGEAEALSRTLDKVSLEETAQLPSAPQGSRAAPTAASDQPDSAATTEKAKKIKNLKKKLRQVEELQQRIQAGEVSQPSKEQLEKLARRRALEEELEDLELGL", "text": "FUNCTION: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon- exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA- binding activity independently of the EJC. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus, nucleoplasm Note=Shuttles between the nucleus and the cytoplasm (PubMed:14968132). Nuclear export is mediated by XPO1/CRM1 (PubMed:14968132). SIMILARITY: Belongs to the pym family."}
+{"protein": "MSRGRADTAGDCSKNGRRSRILHYLMAIYLLNGLPGGEYARFIKIARLLDVSPSTVSIMTRRLQMKGLVELIPNMGVRLTEQGLKILSNYLWKSAILEVLLARAGVDIDNCRGMGLRMAEGLSDEDAWILYKVLGEPKYCPHKKPIIPPDEINAENARQIALCCGISILQIPNNRLQPPS", "text": "SIMILARITY: Belongs to the DtxR/MntR family."}
+{"protein": "MNMMIKAYKRKLDVANGRIDLSHGAGGRAMGQLIEGIFHKAFDNDWLRAGNDQSAFSVPGGRMVMTTDGYVVSPLFFPGGNIGTLAVHGTINDIAMAGAVPLYLSASFIIEEGFPLVDLERIADSMGAASREAGVPIITGDTKVVERGKADGVFISTAGIGMAPDGLDLRSDAARPGDAVIISGSIGDHGVAVMSKRENLEFDTDIVSDSAALHGLVADMVAAGGAHIRLMRDPTRGGIAATLNEIASQSRVGFRIDEEAIPMKPEVAAACEFLGLDPLNVANEGKLVAVVAPEGADAVLAAIHAHPLGAEAALIGHVVADDNYFVQMVTSFGGGRIVDWLSGEQLPRIC", "text": "FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent dehydration of the carboxamido group attached to its C-terminal cysteine to a cyano group. SIMILARITY: Belongs to the HypE family."}
+{"protein": "MPVFQAKTFRRATTASSSLGERIGAAYRGGLPKHPFLLFGLPFIMVIVAGSFVLTPAAALRYERYDRKVKQLSQEEAMELGLKGPDGEEGIRRNPRRRILGDEREEYYRLMAKDLDNWEQKRVQRFKGEPDGKL", "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": "MSLSRAAIVDQLKEIVGADRVITDETVLKKNSIDRFRKFPDIHGIYTLPIPAAVVKLGSTEQVSRVLNFMNAHKINGVPRTGASATEGGLETVVENSVVLDGSAMNQIINIDIENMQATAQCGVPLEVLENALREKGYTTGHSPQSKPLAQMGGLVATRSIGQFSTLYGAIEDMVVGLEAVLADGTVTRIKNVPRRAAGPDIRHIIIGNEGALCYITEVTVKIFKFTPENNLFYGYILEDMKTGFNILREIMVEGYRPSIARLYDAEDGTQHFTHFADGKCVLIFMAEGNPRIAKATGEGIAEIVARYPQCQRVDSKLIETWFNNLNWGPDKVAAERVQILKTGNMGFTTEVSGCWSCIHEIYESVINRIRTEFPHADDITMLGGHSSHSYQNGTNMYFVYDYNVVNCKPEEEIDKYHNPLNKIICEETIRLGGSMVHHHGIGKHRVHWSKLEHGSAWALLEGLKKQFDPNGIMNTGTIYPIEK", "text": "SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type 4 family."}
+{"protein": "MVSSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIARIGDTKSEIKILSIGGGAGEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKGPVAKTSNLENVKFAWHKETSSEYQSRILEKKELQKWDFIHMIQMLYYVKDIPATLKFFHSLLGTNAKMLIIVVSGSSGWDKLWKKYGSRFPQNDLCQYVTSDDLTQMLDNLGLKYECYDLFSTMDISDCFIDGNENGDLLWDFLTETCNFNATAPPDLKAELGKDLQEPEFSAKKEGKVLFNNTLSFIVIEA", "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": "MLKEFKEFALKGNVLDLAVAVVMGAAFNKIVTALVSYIIMPLIGLIFGTVDFAESWSFMGIKYGMFVQSIIDFIIIAFALFIFVKIANTLMKKEEEEEIEENTVLLTEIRDLLREKN", "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 membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscL family."}
+{"protein": "MTADKYTVAINENALKILGEIVFLMGASQNFAKYPVSFIINYLLPSIYLNQYRIYRTVKDNKPIGFACWAFINDQVEKELIENDINLSVEERNSGENIYVLYFIAPFGHAKQIVHDLKNNIFPNKIVKGLRLDKDGKKVLRVATYYC", "text": "SIMILARITY: Belongs to the RTX toxin acyltransferase family."}
+{"protein": "MSDALNMTLDEIVKKSKSERSAAARSGGKGVSRKSGRGRGGPNGVVGGGRGGGPVRRGPLAVNTRPSSSFSINKLARRKRSLPWQNQNDLYEETLRAVGVSGVEVGTTVYITNLDQGVTNEDIRELYAEIGELKRYAIHYDKNGRPSGSAEVVYMRRSDAIQAMRKYNNVLLDGRPMKLEILGGNTESAPVAARVNVTGLNGRMKRSVFIGQGVRGGRVGRGRGSGPSGRRLPLQQNQQGGVTAGRGGFRGRGRGNGGGRGNKSGGRGGKKPVEKSAADLDKDLESYHAEAMNIS", "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": "MNEVENNNHSFPREDIPTEDEIEEEANSRQGILRYFRVARAEYTKFALLGLMFGIIGFIYSFMRILKDMFVMVRQEPTTILFIKIFYILPVSMALVFLIQYMLGTKTVSRIFSIFCGGFASLFFLCGAVFLIEEQVSPSKFLFRDMFIDGKMSSRSLNVFKSMFLTLNEPLATIVFISAEMWGSLVLSYLFLSFLNESCTIRQFSRFIPPLIIITNVSLFLSATVAGAFFKLREKLAFQQNQVLLSGIFIFQGFLVVLVIFLKIYLERVTMKRPLFIVSSGSRRKKAKANVSFSEGLEIMSQSKLLLAMSLIVLFFNISYNMVESTFKVGVKVAAEYFNEEKGKYSGKFNRIDQYMTSVVVICLNLSPFSSYVETRGFLLVGLITPIVTLMAIVLFLGSALYNTSMEESGLGIVNGLFPGGKPLYVLENYFGVIFMSLLKITKYSAFDICKEKLGMRINPTYRARFKSVYDGIFGKLGKSIGSIYGLLMFEALDTEDLRKATPITAGIIFIFIVMWVKAIIYLSRSYESAVQHNRDVDIDMTEKAKKSLETPEEPKVVD", "text": "FUNCTION: ATP transporter involved in the uptake of ATP from the host cell cytoplasm. Provides the microsporidian cell with host ATP in exchange for ADP. This is an obligate exchange system. This energy acquiring activity is an important component of microsporidian parasitism. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Only found on the surface of parasites living inside host cells. SIMILARITY: Belongs to the ADP/ATP translocase tlc family."}
+{"protein": "MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKADLRFQSSAVAALQEASESYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA", "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 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Chromosome. SIMILARITY: Belongs to the histone H3 family."}
+{"protein": "MMPFAVTTQGAQQPAPAPKQFGISSPISLAAPKDTDRELTQKLIETLQPFGVFEEEEELQRRILILQKLNNLVKEWIREISESRNLPQAVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRNDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDSFRLTLRAIKLWAKCHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVRKFFLVFSEWEWPNPVLLKEPEERNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMIEEFKQGLAITHEILLNKAEWSKLFEAPSFFQKYKHYIVLLASAPTEKQHLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKETADKEEFRTMWVIGLVLKKPENSEILSIDLTYDIQSFTDTVYRQAINSKMFEMDMKIAAMHLRRKELHQLLPNHVLQKKETHLTESVRLTAVTDSSLLLSIDSENSMTAPSPTGTMKTGPLTGNPQGRNSPALAVMAASVTNIQFPDVSLQHVNPIESSGIALSESIPQIPSQPTISPPPKPTMTRVVSSTHLVNHPSRPSGNTATNIPNPILGV", "text": "SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the poly(A) polymerase family."}
+{"protein": "MGLQLSGLDASDSDQRELIWAKRPWAAFRGSWVNRLGRVESVWDLKGVWADQAHSAVSESQAATSSTTTTATGDTLPEHPNALAYQISSTDKDSYKASTQGSGQTNSQNTSPYLHLIKPKKVTASDKLDDDLKNLLDPNEVRVKLRQSFGTDHSTQPQPQPLKTTTPVFGTNSGNLGSVLSGGGTTQDSSTTNQLSPVQRVSGWLVGQLPSTSDGNTSSTNNLAPNTNTGNEVVGVGDLSKRASIESSRLWIALKP", "text": "SIMILARITY: Belongs to the adhesin P1 family."}
+{"protein": "MANRPLDILNNALDTPVIVRLKGAREFRGELKGYDIHMNLVLDNAEELREGEVVSKFSSVVIRGDNVVYVSP", "text": "SIMILARITY: Belongs to the snRNP Sm proteins family."}
+{"protein": "MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPTNTIFDAKRLIGRRFEDSVVQADMKHWPFKVISDGGRPRLEVEYKGEAKNFYPEEISSMVLVKMKEIAEAYLGKSINNAVITVPAYFNDSQRQRTKDAGTISGLNVLRIINEPTAAAIAYGLDKKVGSERNVLIFDLGGGTFDVSILTIEDGIFDLKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISDNKRAVRRLATACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLDPVEKALRDAKMDKAQVHDIVLVGGSTRIPKMEKLLQDFFNGKELNKSINPDEAVAYGAAVQAESSLGDKSENVQDLVLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGIMNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDDVQRDKVSAKNGLESYAFNMKSTVEDEKLKGKISDEDKHKILDKCNEVISWLDKNQTAEKDEYEHQQKDLEKVCNPIITKLYQSDGGMPGGMPDGMPGGFQELGAAPGGGSSGPTIEEVD", "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 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. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MVLTHNVLAVTFGVLGNIISFIVFLAPVPTFVRICKKKSIEGFESLPYVSALFSAMLWIYYALQKDGAGFLLITINAVGCFIETIYIILFITYANKKARISTLKVLGLLNFLGFAAIILVCELLTKGSNREKVLGGICVGFSVCVFAAPLSIMRVVIRTKSVEFMPFSLSLFLTISAITWLFYGLAIKDFYVALPNILGAFLGAVQMILYVIFKYYKTPLVVDETEKPKTVSDHSINMVKLSSTPASGDLTVQPQTNPDVSHPIKTHGGDLEDQMDKKMPN", "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": "MQAQEVRLLYLFREDGVVTNDLEARVLRKITFRIVPFIMLLYFIAFLDRVNIGFAALTMNQDLGFSSTVFGIGAGIFFVGYFLFEVPSNLILNKVGARIWIARVMITWGIVSGLMAFVQGTTSFYILRFLLGVAEAGFFPGIILYLSFWFPARRRAAVTALFMAAAPLSTVLGSPISGALMEMHGLMGLAGWQWMFLIEAAPALILGVVVLFFLTDRPEKAKWLTEEERNWLVKTMNAEQAGRGTASHSVMAGLADIRVIALALVYFGTSAGLYTLGIWAPQIIKQFGLSAIEVGFINAVPGIFAVVAMVLWARHSDRTGERTWHVVGACLLAAAGLAFAAGATSVFMVLIALTIVNVGISCSKPPLWSMPTMFLSGPAAAAGIATINSIGNLGGFVGPSMIGWIKDTTGSFTGGLYFVAGLLLISAILTLILARSSPKAVETRTANQH", "text": "FUNCTION: Component of the tartrate utilization system and may allow entry of tartrate and tartrate dehydrogenase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Phthalate permease family."}
+{"protein": "MKKWTNRLMTIAGVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKDKSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK", "text": "FUNCTION: Transpeptidase that anchors surface proteins to the cell wall (PubMed:10427003, PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Utilizes lipid II as the peptidoglycan substrate for the sorting reaction (PubMed:10446208, PubMed:11856734). Responsible for the display of important virulence factors (PubMed:14769030). Important for interactions with the host and host colonization during infection (PubMed:10805806, PubMed:14769030). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the bacterial sortase family. Class A subfamily."}
+{"protein": "MLSLDNYSYVHNITTQTNIDLSSQQTIHLASINGKGYIIFLRFFCEGSSACFTNVKFSVKANGLVLYSFRYIQLLELGQAIATAIPSSSQGFSTLLSNYNVLISSPIGTLPQLTLYDSYDNRYGAMLQPAFPLPFVNTLSLDVDILPVSQSSYDPIPYSLNDNQISTNAPTGKGNISIEYLLYNCLV", "text": "FUNCTION: VP10 self-assembles, together with capsid protein VP4, to form 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": "MDSLNLNKHISGQFNAELESIRTQVMTMGGMVEQQLSDAITAMHNQDSDLAKRVIEGDKNVNMMEVAIDEACVRIIAKRQPTASDLRLVMVISKTIAELERIGDVADKICRTALEKFSQQHQPLLVSLESLGRHTIQMLHDVLDAFARMDIDEAVRIYREDKKVDQEYEGIVRQLMTYMMEDSRTIPSVLTALFCARSIERIGDRCQNICEFIFYYVKGQDFRHVGGDELDKLLAGKDSDK", "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). 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. Is also part of complex networks important for bacterial virulence, tolerance to antibiotics and stress response. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PhoU family."}
+{"protein": "MAKIVVALGGNALGKSPQEQLKLVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAAEHNQGPAFPFAECGAMSQAYIGYQLQESLQNELHSIGMDKQVVTLVTQVEVDENDPAFNNPSKPIGLFYNKEEAEQIQKEKGFTFVEDAGRGYRRVVPSPQPISIIELESIKTLIKNDTLVIAAGGGGIPVIREQHDGFKGIDAVIDKDKTSALLGANIQCDQLIILTAIDYVYINFNTENQQPLKTTNVDELKRYIDENQFAKGSMLPKIEAAISFIENNPKGSVLITSLNELDAALEGKVGTVIKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the carbamate kinase family."}
+{"protein": "MSPTPALFSLPEARTRFTKSTREALNNKNIKPLLTAFSQLPGSENEKKCTLDQAFRGVLEEEIINHSACENVLAIISLAIGGVTESVCTASTPFVLLGDVLDCLPLDQCDTIFTFVEKNVATWKSNTFYSAGKNYLLRMCNDLLRRLSKSQNTVFCGRIQLFLARLFPLSEKSGLNLQSQFNLENVTVFNTNEQESTLGQKHTEDREEGMDVEEGEMGDDEAPTTCSIPIDYNLYRKFWSLQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCPSFVKERASDTKPTRVVRKRAAPEDFLGKGPNKKILIGNEELTRLWNLCPDNMEACKSETREYMPTLEEFFEEAIEQADPENMVESEYKAVNNSNYGWRALRLLARRSPHFFQPTNQQFKSLPEYLENMVIKLAKELPPPSEEIKTGEDEDEEDNDALLKENESPDVRRDKPITGEQIESFANKLGEQWKILAPYLEIKDSDIRQIECDSEDMKMRAKQLLVAWQDQEGVHATTDNLISALNKSGLSDLAESLTNDTETNS", "text": "FUNCTION: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre- mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation (By similarity). FUNCTION: Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1 (By similarity). Essential for early embryonic development. Required for normal gene expression during postnatal testis development. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, nucleoplasm Nucleus matrix Cytoplasm Note=Can shuttle between the nucleus and cytoplasm. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase of apoptosis execution (By similarity)."}
+{"protein": "MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV", "text": "FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family."}
+{"protein": "MASAQAETNVGLASEQGPVAQRQRKGTGSGADSPKSNRSSPTQQEEKRIKSEDRTSPTGGAKDEDKESQGHAVAGGGGSSPVSSPQGRSSSVASPSSSSQQFCLRWNNYQTNLTTIFDQLLQNECFVDVTLACDGRSMKAHKMVLSACSPYFQTLLAETPCQHPIVIMRDVNWSDLKAIVEFMYRGEINVSQDQIGPLLRIAEMLKVRGLADVTHMEAATAAAAAASSERMPSSPKESTSTSRTEHDREREAEELLAFMQPEKKLRTSDWDPAELRLSPLERQQGRNVRKRRWPSADTIFNPPAPPSPLSSLIAAERMELEQKERERQRDCSLMTPPPKPPMSSGSTVGATRRLETAIHALDMPSPAATPGPLSRSSRPHSQSPQQQQAQQQGQLPLPLPLHPHHHASPAPHPSQTAGSAHHPASPAGDSRFPLGPAAAMAAARELSGLGPGPSAEPRLPPPPPHHHGGGGVGGGGVGGGGAGGVGSGGGSSLADDLEIKPGIAEMIREEERAKMMENSHAWMGATGSTLAADSYQYQLQSMWQKCWNTNQNLMHHMRFRERGPLKSWRPETMAEAIFSVLKEGLSLSQAARKYDIPYPTFVLYANRVHNMLGPSIDGGPDLRPKGRGRPQRILLGIWPDEHIKGVIKTVVFRDTKDIKDESLAAHMPPYGRHSPAFPLQDLPLSYPGASGALAGAPSSMACPNGSGPQTGVGVAGEQHMSQETAAAVAAVAHNIRQQMQMAAVPPGLFNLPPHPGVGGGVGNVPGAAGGRASISPALSSGSGPRHAPSPCGPAGLLPNLPPSMAVALHHQQQQQAAHHHMQQLHLQQQQAHLHHHQQQQQQQQQQHHQGGHQVAHKSGFGASSSSSASSSSMGQHHAPKAKSSPLRSETPRLHSPLGDLGLDMASYKREFSPSRLFAEDLAELVGASVSSSSSSAAAATAPPERSAGAASAATGADAPSSSSSGGIKVEPITTTSE", "text": "FUNCTION: Probably acts as a transcriptional regulator. Required for the specification of the tarsal segment. Also involved in antenna development. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MADTTGRIPLWLIGTVTGIAVIGLIGVFFYGSYSGLGSSL", "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": "MNRKKIIVAAVIVALLATLAYGWHYYRQQNDASLTLYGNVDIRTVNLGFRVAGRLASLAVDEGDDIHPGQTLGKLDDGPYLNALKQAQANVQSAQAQLALLKAGYREEEIAQVRSEVAQRQAAFDYADNFLKRQQGLWASKAVSANELENARTARNQAQANLQAAKDKLAQFLSGNRPQEIAQAEANLAQTEAELAQAQLNLQDTILLAPSAGTVLTRAVEPGTILSASNTVFTVSLTDPVWVRAYVSERHLGQAIPGSEVEVFTDGRPDKPYHGKIGFVSPTAEFTPKTVETPDLRTDLVYRLRIIITDADESLRQGMPVTVRFPQR", "text": "SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the UPF0194 family. SIMILARITY: Belongs to the UPF0194 family."}
+{"protein": "MKSLLLLVLISICGADHRSDNYTLDHDRVIHIQAENGPRLLVEAEQAKVFSHRGGNVTLPCKFLRDPTAFGSGTHKIRIKWTKLTSDYLKEVDVFVSMGYHKKTYGGYQGRVFLKGGSDNDASLVITDLTLDDYGRYKCEVIEGLEDDTAVVALDLQGVVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNYGFWDKEKSRYDVFCFTSNFNGRFYYLIHPTKLTYDEAVQACLKDGAQIAKVGQIFAAWKLLGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPDKKHKLYGVYCFRAYN", "text": "FUNCTION: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the HAPLN family."}
+{"protein": "MARSICFFAVAILALMLFAAYETEAGTCKAECPTWEGICINKAPCVKCCKAQPEKFTDGHCSKILRRCLCTKPCATEEATATLANEVKTMAEALVEEDMME", "text": "FUNCTION: Plant defense peptide with antifungal activity against F.oxysporum and B.cinerea. SUBCELLULAR LOCATION: Secreted Vacuole. SIMILARITY: Belongs to the DEFL family."}
+{"protein": "MKTGSLTQRGALLLLLLLAPAVTPTWYAGSGYSPDESYNEVYAEEVPDTRALDYRVPRWCYTLNIQDGEATCYSPRGGNYHSSLGTRCELSCDRGFRLIGRKSVQCLPSRRWSGTAYCRQMRCHTLPFITSGTYTCTNGMLLDSRCDYSCSSGYHLEGDRSRICMEDGRWSGGEPVCVDIDPPKIRCPHSREKIAEPEKLTARVYWDPPLVKDSADGTITRVTLRGPEPGSHFPEGEHVIRYTAYDRAYNRASCKFIVKVQVRRCPILKPPQHGYLTCSSAGDNYGAICEYHCDGGYERQGTPSRVCQSSRQWSGSPPVCTPMKINVNVNSAAGLLDQFYEKQRLLIVSAPDPSNRYYKMQISMLQQSTCGLDLRHVTIIELVGQPPQEVGRIREQQLSAGIIEELRQFQRLTRSYFNMVLIDKQGIDRERYMEPVTPEEIFTFIDDYLLSNQELARRAEQRDVCE", "text": "FUNCTION: Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases the mitogenic activity of HGF (By similarity). Promotes synapse formation. SUBCELLULAR LOCATION: Secreted Cytoplasm Cell surface Synapse."}
+{"protein": "MTTFDRGEKPDIGTLVAFDHVRFVVGNAKQAAYWYCANFGFEPFAYKGLETGSRITAQHAIKQDKIVFVFESALLPDNTELGEHLVQHGDGVKDVCFEVEDLDSIVAHAKAAGATIVRDITEESDENGSVRFATLRTYGETDHTLLERKKYKGAFLPGFKPHPMPPTFFHSLPRVGLNFLDHCVGNQPDLQMAPAVEWYENILKFHRFWSVDDSMIHTEYSALRSIVVTNFEETIKMPINEPASSNKKAVSQIQEFVDYYGGSGVQHIALNTTDIITAIEALRARGCEFLSIPSSYYDNLRQRLSVSSMKIKEDMDRLQKLHILVDFDENGYLLQIFSKPCQDRPTLFLEIIQRQNHQGFGAGNFKALFESIELEQTKRGNLFYENVKDGQHK", "text": "FUNCTION: Key enzyme in the degradation of tyrosine. SIMILARITY: Belongs to the 4HPPD family."}
+{"protein": "MPTSLKDTVKLHNGVEMPWFGLGVFKVENGNEATESVKAAIKNGYRSIDTAAIYKNEEGVGIGIKESGVAREELFITSKVWNEDQGYETTLAAFEKSLERLQLDYLDLYLIHWPGKDKYKDTWRALEKLYKDGKIRAIGVSNFQVHHLEELLKDAEIKPMVNQVEFHPRLTQKELRDYCKGQGIQLEAWSPLMQGQLLDNEVLTQIAEKHNKSVAQVILRWDLQHGVVTIPKSIKEHRIIENADIFDFELSQEDMDKIDALNKDERVGPNPDELLF", "text": "FUNCTION: Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MEAAAAAAAEEEAGNPDGVEGAAVAAVAPEAAAEGPSEPNAGEASREPDAGQASREPGAAGPSREPDVAGPSREPDAAGPSREPGAAGGSREPGAAGGSRQPVPDAAQLAVVPYVEDIDRYLRSLEAEQTRRPMINYVQEIQGGIINMDVRGILVDWMADVAYVFNLQEETLHHAVSYVDRFLSKIAFPGDKLKLLGTTALFVASKYEEIHPPHVRNFSAVTVNTYTTQQVSKMELDILRFLNFDVGSPTVITFLRKFLTSCCGGNNSSNRKLELMCNYLAELSLLDDYYIRFLPSIVAAACLFVGKFTLNPNTRPWFGSVSTITPPENIKGGVEKYMVSRIYMCVFDLPMLFLMETWSSSGVSNHTKLQLKQNMMELPIENPTFISAS", "text": "SIMILARITY: Belongs to the cyclin family. Cyclin F subfamily."}
+{"protein": "MASGAKLEASHPPKAANAAAPAKKVHYPFWFGGSASCFAAAVTHPLDLVKVRLQTRGPGAPSTMVGTFVHVFKNDGFFGLYSGLSAAILRQLTYSTTRFGIYEELKNHFTSPDSPPGLFTLIGMASASGFIGGMAGNPADVLNVRMQSDAALPPAQRRNYRNAIHGLVTMTRTEGPASLFRGVWPNSTRAVLMTTSQLASYDTFKRLCLENLGMSDNMGTHFTASFMAGFVATTVCSPVDVIKTRVMTASPAEGRSQSIVGLLRDITRKEGLAWAFRGWVPSFIRLGPHTIATFIFLEEHKKLYRLLKGL", "text": "FUNCTION: Mitochondrial transporter that does not mediate citrate export from mitochondria to cytoplasm (PubMed:36177470). Its exact function has still to be determined (PubMed:36177470). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MNYLHNFKDTLFVDLLEVLNIVTIGEEHVNQLNLSGDASLSASSESSNMSFNSGSEENSQEKSVEDLEKQNCEINIHKNSDKEADTKKDPFLVTFNGEDDPLMPYNWSTNKKALIIIQTMLLTCVNYMGSSIYTPGQLEIQNEFHVGHVVGTLNLSLYVLGYGLGPIVFSPLTEISSIGRLPVYMITFFLFTMLQIGCALAPNFAGLVILRFITGVLCSPALSTGGATLGDIVSQNYLALVLGLWSIGAVAAPVLAPLLGASMVVAKDWRWIFWLLFFCCCATMLLLTFFFPETSSDTVLHRKAARIRKLTGDNRYYTEKEREEAQLPKKQFLIETLYRPFSMMITEPIVLAFDLYIALCYGAFYLFFEAFPIVFGGIYHFTLVEQGLAYFGFCVGCIFAYIILLVFSIKVAAKRFANNTFTPETTLILAMCIGWCIPLALFMFGWTAKVHWILPIISEVFFVLGCFNIFQASFSYLAICYPKYVASVFAGNGFARSSFAAAFPLFGQAMYNNLGTKNYPVAWGSSLVGFFTIGLWVIPFVLYKYGPSLRSMSKYNR", "text": "FUNCTION: Multidrug transporter that confers resistance to 5- flucytosine (5-FC) and clotrimazole (PubMed:28066366). Confers also resistance to benomyl, but not 4-nitroquinoline-N-oxide, cycloheximide, or fluconazole (PubMed:17046176). Plays direct roles in extrusion of 5- flucytosine and clotrimazole (PubMed:28066366). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MGMSKSHSFFGYPLSIFFIVVNEFCERFSYYGMRAILILYFTNFISWDDNLSTAIYHTFVALCYLTPILGALIADSWLGKFKTIVSLSIVYTIGQAVTSVSSINDLTDHNHDGTPDSLPVHVVLSLIGLALIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINAGSLLSTIITPMLRVQQCGIHSKQACYPLAFGVPAALMAVALIVFVLGSGMYKKFKPQGNIMGKVAKCIGFAIKNRFRHRSKAFPKREHWLDWAKEKYDERLISQIKMVTRVMFLYIPLPMFWALFDQQGSRWTLQATTMSGKIGALEIQPDQMQTVNAILIVIMVPIFDAVLYPLIAKCGFNFTSLKKMAVGMVLASMAFVVAAIVQVEIDKTLPVFPKGNEVQIKVLNIGNNTMNISLPGEMVTLGPMSQTNAFMTFDVNKLTRINISSPGSPVTAVTDDFKQGQRHTLLVWAPNHYQVVKDGLNQKPEKGENGIRFVNTFNELITITMSGKVYANISSYNASTYQFFPSGIKGFTISSTEIPPQCQPNFNTFYLEFGSAYTYIVQRKNDSCPEVKVFEDISANTVNMALQIPQYFLLTCGEVVFSVTGLEFSYSQAPSNMKSVLQAGWLLTVAVGNIIVLIVAGAGQFSKQWAEYILFAALLLVVCVIFAIMARFYTYINPAEIEAQFDEDEKKNRLEKSNPYFMSGANSQKQM", "text": "FUNCTION: Electrogenic proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Transports neutral and monovalently charged peptides with a proton to peptide stoichiometry of 1:1 or 2:1 (PubMed:7896779, PubMed:9835627, PubMed:8914574, PubMed:15521010, PubMed:18367661, PubMed:19685173, PubMed:26320580) (By similarity). Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen (By similarity). Mediates transepithelial transport of muramyl and N-formylated bacterial dipeptides contributing to recognition of pathogenic bacteria by the mucosal immune system (PubMed:9835627, PubMed:15521010). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=Localized to the apical membrane of enterocytes. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family."}
+{"protein": "MTKSIIASEPPSAESSGRLPWKILGQTTGFPNQDQELWWLNTAPLLNEFLAECQYDVHLQYQYLTFFRHHVIPVLGPFFAPGTTPNFASRLSKHGHPLDFSVNFQESGATVRMSLGAIGSFAGLQQDPLNQFRAREVLDKLAILYPTVDLQLFKHFESEFGINHADALKVAAKLPKLDRATKMIAIDMLKNGSMTFKVYYMVRSKAAATGLPVHTVLFNAVQRLGSAFEPGLSLLKQFLSPLCDAGETDLGLLSFDCVPTESSRIKLYAIKQVGSLDAIRNLWTLGGTMDDPTTMKGLAVLEHVCELLQFGWSGDSRVQPILFNYEIKKGSTPKPQIYIPLADRYDEFDAAKLKAVFQDLDWKRVPFYQDTGKDLASVL", "text": "FUNCTION: Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways (PubMed:28791090). Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I (PubMed:28791090). SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family."}
+{"protein": "MPLIQVTLIEGRTMEAKAALIGSLTQAAVATLGAPRESVRVIIQEVPAAHWGVAGVPKSAAKEPPRDSKA", "text": "SIMILARITY: Belongs to the 4-oxalocrotonate tautomerase family."}
+{"protein": "SLVELGKMILQETGKNPVTSYGAYGCNCGVLGSGKPKDATDRCCYVHKCCYKKLTDCDPKKDRYSYSWKDKTIVCGENNSCLKELCECDKAVAICLRENLDTYNKKYNYLKPFCKKADPC", "text": "FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic activity (PubMed:29067765). Shows moderate cytotoxicity against C2C12 myotubes (activity above 200 ug/mL) (PubMed:29067765). Also shows antibacterial activity against both Gram-positive and Gram-negative bacteria (PubMed:29067765). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (By similarity). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (By similarity). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (By similarity). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (By similarity). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily."}
+{"protein": "MSQKMMYEFKRKLEELEKYKGRGTELITLYIPPDKNIADVSNQLRSELSQASNIKSKQTRTNVLAGIEAILNRLKHFRKPPENGMVIISGVVNINGKEKHITEIIEPPEPVPLYKYHCDSKFYLDPLKEMLTEKKLYGLIVLDRREATVGLLKGKRIEVLDWDTSMVPGKHRQGGQSSVRFERLREIAIHEFYKKVGEMASEALLPYKDKLIGILIGGPSPTKEEFYEGEYLHHELQKKVLGLFDVGYTDESGLYELVEKAKDVLQEVDIIREKNLMQRFLKEVARDGLAAYGEEEVRRYIELGAVDTLLLSEDLRYERVKYRCPKCGKEVEVTVREGIEKPPFCEEDNVEMEEVERRDIVLELSELAESTGAKVEFLSTESEEGEMLYKAFGGIAAILRFKPDGGQ", "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": "PGHPPGIDTPNPQWFWTLLQRNQMPARLLSKEDIETITAIKRFSDEYSAINFINLTPNNIGELAQFYFANLVLKYCDHSQYFINGLTAIVVGSRRPRDPAAVLAWIDRTINGAADVEPAAQEVLQRLGSNPAAWTGTFTSTNMVRYVMDQRPMVVIGLSISKYNGSAGNNRVFQAGNWNGLNGGKNVCPLMAFDRTRRFVLACPRVGFTCEAGGFGTGVRENTLSEQVRGIVSEGGPMVQTAVFAAVLHALGARTQHLAVDDWIGLVDDEFLAASLDALNATVVDQFGEWSVEAAQELVKNMEAQTTAGAVAAGEGAFDFGACVGDTPQQSTSAFNGGLAMAAAPAGQKRSLPDDILFDMGAPPEKKSGLTFDML", "text": "FUNCTION: Single-stranded DNA-binding protein required for DNA replication. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae DNA-binding protein family."}
+{"protein": "MKALIFLAFLGAAVALPLDDDDDKIVGGYTCQKNSLPYQVSLNAGYHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVVEGGEQFIDAAKIIRHPSYNANTFDNDIMLIKLNSPATLNSRVSTVSLPRSCGSSGTKCLVSGWGNTLSSGTNYPSLLQCLDAPVLSDSSCKSSYPGKITSNMFCLGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGYGCAQKGKPGVYTKVCNYVNWIQQTVAAN", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MTYKAQYTPGETQIAENRRKHMDPDYEFRKLREVSDEDLVKVLGHRNPGESYKSVHPPLDEMDFEEDIVRDMVEPIQGAKEGVRVRYIQFADSMYNAPAQPYDRARTYMWRYRGVDTGTLSGRQVIEMRELDLEGVSKELVETELFDPATTGIRGATVHGHSLRLDENGLMFDALQRYVFDEEKGHVVYVKDQVGRPLDEPVDMGQPLGEDELKKITTIYRKDNIAMRDDKEAIEVVENIHTGRTMGGFGMDVFKDDLRKRLGDD", "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": "MAACTMSVCSSACSDSWRVDDCPESCCEPPCGTAPCLTLVCTPVSCVSSPCCQAACEPSPCQSGCTSSCTPSCCQPACCASSPCQQACCVPVCCKPVCCLPTCSKDSSSCCQQSSCQPTCCASSSCQQSCCVPVCCKPVCCVPTCSEDSSSCCQHSSCQPTCCTSSPCQQSCYVPVCCKPVCCKPICCVPVCSGASTSCCQQSSCQPACCTTSCCRPSSSVSLLCRPICRPACCLPISSCCAPASSYQASCCRPASCVSLLCRPACSPLAC", "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": "MQQPSQPTRESTKKPVPFQHEEYPCQNQQRSSTLYVLICLAIFLSKFTNQLLASLLDLLIRIVTTLQQLLT", "text": "FUNCTION: Induces the formation of specific membrane adhesion sites between the inner and outer membranes, apparently leading to host cell lysis. Lysis may be performed via activation of host murein hydrolases. SUBCELLULAR LOCATION: Host cell inner membrane; Single-pass membrane protein Host cell outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Leviviricetes lysis protein family."}
+{"protein": "MSLWRQTPDLEQLNASQKNSIGDLLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQYYCVGLEVNANHLRGLRSGRVTAVARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAVVPLAGRAG", "text": "SIMILARITY: Belongs to the thioesterase PaaI family."}
+{"protein": "MVKRGSKVRILRKESYWYQEVGTVATVDTSGIRYPVVVRFEKVSYSGVNTNNFSLDEVIEVNEK", "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": "MPIKILSPQLANQIAAGEVVERPASVVKELVENSLDAGANKIQIDIENGGANLIRIRDNGCGIPKEELSLALARHATSKIADLDDLEAILSLGFRGEALASISSVSRLTLTSRTEEQTEAWQVYAQGRDMETTIKPASHPVGTTVEVANLFFNTPARRKFLRTDKTEFSHIDEVIRRIALTKFNTAFTLTHNGKIIRQYRPAEAINQQLKRVAAICGDDFVKNALRIEWKHDDLHLSGWVATPNFSRTQNDLSYCYINGRMVRDKVISHAIRQAYAQYLPTDAYPAFVLFIDLNPHDVDVNVHPTKHEVRFHQQRLIHDFIYEGISHALNNQEQINWHTDQSAVENHEENTVREPQPNYSIRPNRATAGQNSFAPQYHEKPQQNQPHFSNTPMFPNHVSTGYRDYRSDAPSKTEQRLYAELLRTLPPTAQKDISDTAQQNISDTAKIISTEIIECSSHLRALSLIENRALLLQQNQDFFLLSLEKLQRLQWQLALKQIQIEQQALLIPIVFRLTESQFQAWQQYSDDFKKIGFEFIENQAQLRLTLNKVPSALRTQNLQKCVMAMLTRDENSSSFLTALCAQLECKTFNALADALNLLSETERLLTQTNRTAFTQLLKPVNWQPLLDEI", "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 (By similarity). SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family."}
+{"protein": "MKIGFLSRWGATCGVGMHAEILAREFIRMGHEVVVFAPTEESASKEVKYYKRTEAQDPEFVKREIYTEVDNVTEEGWVKEEEILKENLDLLIIETFWRVPVKPLTRLIEKLKIPVISVFHEANIFKAREVVKLPCDKIVVFDRRFYDEILEFYEIPREKVEVISYPVMKPYDAEPERPVSEDKFLFFSFGRQPVEEYCDFLNALKKLRKRFDNVHYWIIRSDGRVDYEAEWITQWQKRPTVEKLYSYLKGSNVHLLPKGNTPNVVVSSTLYQIIASETPIVIRDSRFVETIETDVYGFGPIVKYRNIHDLVHKLELLMLDRELVEDIKKEVRVFVEKYGGDKIAQEFLDLAKTITK", "text": "FUNCTION: Catalyzes the transfer of the mannosyl group from GDP-mannose to di-myo-inositol-1,3'-phosphate (DIP), producing mannosyl-di-myo- inositol phosphate (MDIP). Can also use MDIP as an acceptor of a second mannose residue, yielding di-mannosyl-di-myo-inositol phosphate (MMDIP). Minor amounts of the tri-mannosylated form are also formed. SIMILARITY: Belongs to the MDIP synthase family."}
+{"protein": "MMERFPRLAQRVLSVPFTPKYLKSCKKTNPLTSHLMQLRGSQRPIFIQWNLQGRPSVCTDLISKKNYSSATARAGWFLGLGEKKKQAMPDIVKAGDPVLHEPSQDIPLEEIGSERIQKIIEEMVKVMRNAPGVGLAAPQIGIPLKIIVLEDTNEYISYAPKDETKAQDRRPFGLLVIINPKLKKKGNKTALFFEGCLSVDGFRAVVERHLEVEVTGLDRNGKAIKVDASGWQARILQHEYDHLDGTLYVDKMAPRTFRTVENLDLPLAAGCPKLGVC", "text": "FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the polypeptide deformylase family."}
+{"protein": "MRITVLRLGHRPERDKRITTHVGLVARAFGADEILIEGRDESVVESLRDVVNRWGGSFSVTDGIAWRDELRRFRDSGGKIVHLTMYGRRIDEVIGEIRSCERIMVVVGAEKVPPDVYDIADWNVAVGNQPHSEVAALAVFLDRLFMGEELEKDFGGRLKVIPAARGKVVLDRGL", "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": "MEEPPVREEEDGEEDEGALAKSPLQLTTEDVYDISYVVGRELMALGSDPRVTRLQFKIVRVMEMLEALVNEGSLAVEELRMERDNLKQEVEGLRRAGVSGSEVNLGPDKMVVDLTDPNRPRFTLQELRDVLQERNKLKSQLLLVQEELQCYRSGLLPPRETPGGRREKDAMVTMGNGEKEERTIMKKLFSFRSGKHT", "text": "FUNCTION: Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines (PubMed:19812310). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). May function via activation of RAC1 and PAK1 (PubMed:19812310). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium."}
+{"protein": "MTSLHQVLYFIFFASVSSECVTKVFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMAESSSDDPTKWFACILKDSVTEILPMVNMTGAISGYSFKQCPQQLSTCSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPSVDHRKMCLLKYTRTGTPTTITKLNGVVSGFSLKSCGLSNLACIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESQRHLCLLKTSESGLPSTRITKSHALSGFSLQHCRHSVPVFCHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNERNRRGRCYLKLSSNGSPTRILHGRGGISGYSLRLCKMDNVCTTKINPRVVGGAASVHGEWPWQVTLHISQGHLCGGSIIGNQWILTAAHCFSGIETPKKLRVYGGIVNQSEINEGTAFFRVQEMIIHDQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRYRRHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWILEKTQTV", "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": "MGPLQFRDVAIEFSLEEWHCLDTAQRNLYRNVMLENYSNLVFLGIVVSKPDLIAHLEQGKKPLTMKRHEMVANPSVICSHFAQDLWPEQNIKDSFQKVILRRYEKRGHGNLQLIKRCESVDECKVHTGGYNGLNQCSTTTQSKVFQCDKYGKVFHKFSNSNRHNIRHTEKKPFKCIECGKAFNQFSTLITHKKIHTGEKPYICEECGKAFKYSSALNTHKRIHTGEKPYKCDKCDKAFIASSTLSKHEIIHTGKKPYKCEECGKAFNQSSTLTKHKKIHTGEKPYKCEECGKAFNQSSTLTKHKKIHTGEKPYVCEECGKAFKYSRILTTHKRIHTGEKPYKCNKCGKAFIASSTLSRHEFIHMGKKHYKCEECGKAFIWSSVLTRHKRVHTGEKPYKCEECGKAFKYSSTLSSHKRSHTGEKPYKCEECGKAFVASSTLSKHEIIHTGKKPYKCEECGKAFNQSSSLTKHKKIHTGEKPYKCEECGKAFNQSSSLTKHKKIHTGEKPYKCEECGKAFNQSSTLIKHKKIHTREKPYKCEECGKAFHLSTHLTTHKILHTGEKPYRCRECGKAFNHSATLSSHKKIHSGEKPYECDKCGKAFISPSSLSRHEIIHTGEKP", "text": "FUNCTION: Transcription factor specifically required to repress long interspersed nuclear element 1 (L1) retrotransposons: recognizes and binds L1 sequences and repress their expression by recruiting a repressive complex containing TRIM28/KAP1 (PubMed:25274305). Not able to repress expression of all subtypes of L1 elements. Binds to the 5' end of L1PA4, L1PA5 and L1PA6 subtypes, and some L1PA3 subtypes. Does not bind to L1PA7 or older subtypes nor at the most recently evolved L1PA2 and L1Hs. 50% of L1PA3 elements have lost the ZNF93-binding site, explaining why ZNF93 is not able to repress their expression (PubMed:25274305). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MAETLITKPPLSLSFTSLSSMLPSLSLSTANRHLSVTDTIPLPNSNSNATPPLRIAIIGFGNYGQFLAETLISQGHILFAHSRSDHSSAARRLGVSYFTDLHDLCERHPDVVLLCTSILSIENILKTLPFQRLRRNTLFVDVLSVKEFAKTLLLQYLPEDFDILCTHPMFGPQSVSSNHGWRGLRFVYDKVRIGEERLRVSRCESFLEIFVREGCEMVEMSVTDHDKFAAESQFITHTLGRLLGMLKLISTPINTKGYEALLDLAENICGDSFDLYYGLFVYNNNSLEVLERIDLAFEALRKELFSRLHGVVRKQSFEGEAKKVHVFPNCGENDASLDMMRSEDVVVKYEYNSQVSGSVNDGSRLKIGIVGFGNFGQFLGKTMVKQGHTVLAYSRSDYTDEAAKLGVSYFSDLDDLFEEHPEVIILCTSILSTEKVLESLPFQRLKRSTLFVDVLSVKEFPRNLFLQTLPQDFDILCTHPMFGPESGKNGWNNLAFVFDKVRIGMDDRRKSRCNSFLDIFAREGCRMVEMSCAEHDWHAAGSQFITHTVGRLLEKLSLESTPIDTKGYETLLKLVENTAGDSFDLYYGLFLYNPNAMEQLERFHVAFESLKTQLFGRLHSQHSHELAKSSSPKTTKLLTS", "text": "FUNCTION: Involved in the biosynthesis of tyrosine. Has no prephenate dehydrogenase activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family."}
+{"protein": "GKVEFQGKKTKFDSDDERNENGAAGPVKRAREETDKEEPASKQQKTENGAGDQ", "text": "FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAISKASIVVLMMVIISVVASAQSEAPAPSPTSGSSAISASFVSAGVAAVAALVFGSALRI", "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": "MIDEILPKLVQYWYIVLPTLLIIKHVVSYINTQRLMRKFRAKPVTNVLNDGFFGIPNGIKAIKEKNKGRAQEYNDEKFAAGPKPKVGTYLFKLFTKDVLVTKDPENIKAILATQFEDFSLGKRLDFFKPLLGYGIFTLDGEGWKHSRAMLRPQFAREQVGHVKLIEPHFQSLKKHIIKNKGQFFDIQELFFRFTVDSATEFLFGESVESLKDESIGYDQQDFDFDGRKNFAEAFNKAQEYLGTRAILQLFYWLVNGADFKKSVAEVHKFTDYYVQKALDATPEELEKHSGYIFLYELVQQTRDPKVLRDQSLNILLAGRDTTAGLLSFALFELARNPEVWSRLREEIGDKFGLDEDATIEGISFESLKQCEYLKAVVNECLRMYPSVPRNFRIATKHTTLPRGGGPDGKDPIFIKKGAVVSYGINSTHLDPMYYGPDARLFNPDRWSKPETKKLGWAFLPFNGGPRICLGQQFALTEASYVLVRMIQNFKELELTPNTVYPPRRLTNLTMSLYDGAYIKVN", "text": "FUNCTION: Together with an NADPH cytochrome P450 the enzyme system catalyzes the terminal hydroxylation as the first step in the assimilation of alkanes and fatty acids. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MGLKYFSHLPEELREKIVHDHLQQERKKEFLEKAIEDSCRRHVSLLKSDPSPSEMYSLSKFLDSLADYVGRQFNTRCLIKWRKDVPANIKFQVMEEQHLRLYGFLDMDDLSCRELLPPEEDDDITYEDGMIVNCSELDKLFAALGIRVVYITVSNNCICTPLNKDIVIS", "text": "FUNCTION: Interacts with and disrupts the function of host retinoblastoma-related proteins RBR, which are key regulators of the cell cycle. Induces transcriptional activation of E2F-regulated S-phase and G2/M-phase-specific genes. Inactivation of the ability of RBR to arrest the cell cycle leads to the stimulation of viral DNA replication. SIMILARITY: Belongs to the nanovirus Clink protein family."}
+{"protein": "MFNFAPKQTTEMKKLLFTLVFVLGSMATALAENYPYRADYLWLTVPNHADWLYKTGERAKVEVSFCLYGMPQNVEVAYEIGPDMMPATSSGKVTLKNGRAVIDMGTMKKPGFLDMRLSVDGKYQHHVKVGFSPELLKPYTKNPQDFDAFWKANLDEARKTPVSVSCNKVDKYTTDAFDCYLLKIKTDRRHSIYGYLTKPKKAGKYPVVLCPPGAGIKTIKEPMRSTFYAKNGFIRLEMEIHGLNPEMTDEQFKEITTAFDYENGYLTNGLDDRDNYYMKHVYVACVRAIDYLTSLPDWDGKNVFVQGGSQGGALSLVTAGLDPRVTACVANHPALSDMAGYLDNRAGGYPHFNRLKNMFTPEKVNTMAYYDVVNFARRITCPVYITWGYNDNVCPPTTSYIVWNLITAPKESLITPINEHWTTSETNYTQMLWLKKQVK", "text": "FUNCTION: Involved in degradation of plant cell wall polysaccharides. Has acetyl esterase activity towards a broad range of substrates including xylose-tetraacetate, 4-O-methylumbelliferyl acetate, glucose- pentaacetate, cephalosporin C, and acetylated xylo-oligosaccharides smaller than xylo-heptaose. Displays no detectable activity on polymeric acetylated xylan. SIMILARITY: Belongs to the carbohydrate esterase 7 family."}
+{"protein": "MSELVLITGITGFVASHSAEALLSQGYRVRGTYRFQEKLDGLLKNRPEWEKKVEFVQVPDCRAPNAYVEAAKGVDYVIHAATEVHSNLEPPRKDPHELLHIAIQGCENALIAAAQEPKVKRFVYISSEAALKGPVNYFGDGHVFTEKDWNPKTLREAEESDDELLNYTVCKKLGERAMHAFVARNTPRFQAIALNPPLILGPVFHLQSVDNLNFSTWFFWQLIKGRYEVAPESKFFNYVDVRDLAEAQVKALTAKTDKDRFVISGGAFKNDDIVNVALKYFPQFKDKIAKPNGETSPCNYEVDASLSIKELGLTYRPAEETFKDATESLYKLAGLL", "text": "SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily."}
+{"protein": "MAKTKSKFICQSCGYESPKWMGKCPGCGAWNTMVEEMIKKAPANRRAAFSHSVQTVQKPSPITSIETSEEPRVKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHVLSETDMEYISSAIQEMNPSFVVVDSIQTVYQSDITSAPGSVSQVRECTAELMKIAKTKGIPIFIVGHVTKEGSIAGPRLLEHMVDTVLYFEGERHHTFRILRAVKNRFGSTNEMGIFEMREEGLTEVLNPSEIFLEERSAGSAGSSITASMEGTRPILVEIQALISPTSFGNPRRMATGIDHNRVSLLMAVLEKRVGLLLQNQDAYLKVAGGVKLDEPAIDLAIVISIASSFRDTPPNPADCFIGEVGLTGEVRRVSRIEQRVKEAAKLGFKRMIIPAANLDGWTKPKGIEVIGVANVAEALRTSLGG", "text": "FUNCTION: Plays a role in DNA repair (PubMed:9141693, PubMed:11810266). Might stabilize or process Holliday junction intermediates (PubMed:15317759). May work with DisA following methyl methanesulfonate (MMS) but not H(2)O(2) damage; DisA is a DNA integrity scanning protein with c-di-AMP synthase activity. 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": "MVSNIDHKAMEALLRGQGCANNLKILLENGEISSVSTEPLIHTILDSFSLALSFMDSPNHPPYHESSSHNMASHMSRRSSKQVQHRRKLCVAEGLVNYNHDSRTMCPNDGFTWRKYGQKTIKASAHKRCYYRCTYAKDQNCNATKRVQKIKDNPPVYRTTYLGKHVCKAFAVHDDTYSSTMIRFDQVVPEPIMPQLTTIDHQVITVEENSAEHIMNQECDINDYLVDDDPFWASQFPPFPSSDTMFLENISAFD", "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": "MSFLVENQLLALVVIMTVGLLLGRIKIFGFRLGVAAVLFVGLALSTIEPDISVPSLIYVVGLSLFVYTIGLEAGPGFFTSMKTTGLRNNALTLGAIIATTALAWALITVLNIDAASGAGMLTGALTNTPAMAAVVDALPSLIDDTGQLHLIAELPVVAYSLAYPLGVLIVILSIAIFSSVFKVDHNKEAEEAGVAVQELKGRRIRVTVADLPALENIPELLNLHVIVSRVERDGEQFIPLYGEHARIGDVLTVVGADEELNRAEKAIGELIDGDPYSNVELDYRRIFVSNTAVVGTPLSKLQPLFKDMLITRIRRGDTDLVASSDMTLQLGDRVRVVAPAEKLREATQLLGDSYKKLSDFNLLPLAAGLMIGVLVGMVEFPLPGGSSLKLGNAGGPLVVALLLGMINRTGKFVWQIPYGANLALRQLGITLFLAAIGTSAGAGFRSAISDPQSLTIIGFGALLTLFISITVLFVGHKLMKIPFGETAGILAGTQTHPAVLSYVSDASRNELPAMGYTSVYPLAMIAKILAAQTLLFLLI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family."}
+{"protein": "MPPKKAPAAPQASKKTEQKKKEKIIEDKTFGLKNKKGAKQQKFIKNVTHQVKSGQQNPRLVAQAEGDKKNKKDDKMKELQELNDLFKPVVVAQKVSKGADPKSVVCAFFKQGQCTKGDKCKFSHDLSLERKCEKRSVYVDGRDDELEKDTMENWDEKKLEEVVNKKHGEAEKIKAKTQIVCKFFLEAIENNKYGWFWVCPGGGDTCMYRHALPPGFVLKKEKVKEDKDEDISLEDLIEKERAALGPNVTRITLESFLQWKKRKRADRILKLEEEMEKRKEDFKSGKSLGVSGREVFEFRPELINDDDEEADDASYTFELEDSEAEEIDDVQDIDLSRYVLKDVDETGITVASCERFSSYVASTEKDENKLCVASGGVMENENQSEEEQEGDLENGFVDAVPVDENLFTGEDMDELEEELYTLDLEK", "text": "FUNCTION: Protects drg1 from proteolytic degradation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ZC3H15/TMA46 family."}
+{"protein": "MKTFITCTSVKNYFRQHLKTNQRISSELISYVCTILNHICHQYLQNPQAQEEEWFALIKELPIIKDGLSKEERFFSSGVKHFLHEYKITPENQEKSQKMLNAITEQLMSRLCKVFSIMIQRQGFLKTQTLMYSHLFTILNILMVADNLYGEQDPTEFFSLIIEQTKTIKKKKKSSSEEEESHEE", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the asfivirus E184L family."}
+{"protein": "MLMAKPDVPSSILPRSSSILPNSIETLDENESIEAQVNNVQSLALSSPNRDRSDDDDNNNNHDSVSIPPPIYDGYSSSSSDESQSVPSPPINLDHDDDECQIPIRNTSQALDDIDDDIWGDDDLPETRRPWTPNVSPGFGSDDDDDNDDDNSKNEPRKSLFYGFRQEPEPVTGVGAGLWNLGNSCFLNSVFQCFTHTVPLIESLLSFRYEVPCHCGNEFFCVIRAIRYHIEAALRPERCPIAPYFFFDNLNYFSPDFQRYQQEDAHEFLQAFLEKLEICGSDRTSFRGDITSQDVFSGRLISGLRCCNCDYVSETYEKSVGLSLEIEDVDTLGSALESFTRVEKLDEQLTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKNNGLYMEKIYKHVKIPLEIDLQPYMRNIQENEVSTKYHLYALVEHFGYSVAYGHYSSYVRSAPKIWHHFDDSKVTRIDEDMVLSQDSYILFYAREGTRWFSSVYEEMQPLVEASLLNSSPKSVLDSSTNGECLSEISYENGDKASKPCDSAGVCNQHVKTKEDFVSLSNDDVFLSAESSSGEESPMGELLDPLDPDDSYSPCTEKESDSCLAIERATIRDDFFPLLLDQNQESSTSSPKLQERTFEMQLLQMEETTKSQEPWKQPLSSISNIADSMEAEFVYGDLMKKPSPRARELLDQAISTNGSPPKKLKTT", "text": "FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). SIMILARITY: Belongs to the peptidase C19 family."}
+{"protein": "MDSIISAASVIAAGLAIGLAAIGPGIGQGNAAGQAVEGIARQPEAENKIRGTLLLSLAFMEALTIYGLVVALALLFANPFNS", "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: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family."}
+{"protein": "MGSEVWVGTWRPHRPRGPIAALYRGPGPKYKLPTNTGYKLHDPSRPRAPAFSFGSRPPLRHATCGPGPSYLVPARMTVRGTVGSPAFSIYGRLSHTAPVLTPGPGRYYPERARNVTYPSAPRHTIAPRNWGILAKQETPGPGSYTVPSLLGSRVISKVSAPTYSIYSRSPVGSCFEDLSKTPGPCAYHVVNPMIYKTRAPQFTMLGRTLPPRENTKKPGPASYSVDKVVWSRGSRGRG", "text": "SIMILARITY: Belongs to the ODF3 family."}
+{"protein": "YERLDLDVTSQTTGEEYFRFITLLRDYVSSGSFSNEIPLLRQSGGGVEAARFVLVELTNEGGDSITAAIDVTNLYVVAYQAGSQSYFLSGPGTHLFTGTTRSSLPFNGSYPDLEQYAGHRKQIPLGIDQLIQSVTALRFPGNTRTQARSILILIQMISEAARFNPILWRARQYINSGASFLPDVYMLELETSWGQQSTQVQQSTEGVFNNPIRLAIPGNFVTLTNVRDVIASLAIMLFVCGERPSSSDVRYWPLVIRPVIADDVTCSASEPTVRIVGRNGMNVDVRDDDFHDGNQIQLWPSKSNNDPNQLWTIKRDGTIRSNGSCLTTYGYTAGVYVMIFDCNTAVREATIWQIWGNGTIINPRSNLALAASSGIKGTTLTVQTLDYTLGQGWLAGNDTAPREVTIYGFNDLCMESNGGSVWVETCVSQQNDRWALYGDGSIRPEQNQDQCLTSGRDSVAGINIVSCSGGSSGQRWVFTNEGAILNLKNGLAMDVANPGLGQIIIYPATGKPNQMWLPVP", "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). Inhibits growth of the human tumor cell line Molt4. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily."}
+{"protein": "MATEGLLSAETDQDVARFLANFPPTEWGYSFASLLPQDSEFESHTKELDLVKEKVKDMLMQSRKELTENIEFVNCLCRLGVSYHFESEIIEQLSHIFISLPKILEENDYSLYILTLLFRVLRQHGYKMPCDVFNKFKDSNGEFKKCMTADVRGLLSLYEATFLSVHGEDILDEALAFTRQHLETLAEKSSPHLARHIRNALHLPFHHAPERLEILQYICFYEGEKSMNETLLKFAKLDFNRLQLLYRKELGLLSRWWKDINLTEKLPYTRDRIVEAYAWAAGIIIDPQFSRARLQFAKHLILISVMDDTYDSYGTFDELKHFTAALQRFTFEPTIELPEYMKFLYNILWNFFQETEKDETQGCACKTSFAREMLKELARSYFAEAEWYNDGVLPTFDEFMQFGLVSSTFDYHASAFFLGVEDLGMKEFIWLRDNPTIAKTAKLFGRLFNDIAIREDEQKKGDYPSAIKCYMNDHDVSLEKAKEDILKMLEDGWKDMNEELMKPTTVPKILTKFSINFVRMSDFTYRGGIDKYTCGTELKEFVKKLTIFPLQI", "text": "FUNCTION: Catalyzes the cyclization of farnesyl diphosphate to multiple sesquiterpenes, such as olefins and sesquiterpene alcohols. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MNTTFPAVYGPVNSWRYGRSLGIDPIGAISTCSFNCVYCQLGEIEHLSGDRQIFIPTADILRELAQFAPWEVDVITLSGSGEPTLAKNLGEILEGIKKLTGKLTLVLTNATLLNDAQVREELSLADKISVKLDGLWPDQLQRINRPIAGIELEQILTGIQTFQQEFTGELSVQTMVLQPWDQTTENRYLELLSLIKPTEVQLNRPTRPKPLQRELEGRGNHTGTPYGDRPVTQIKCVDGQTLQNLAKKISGAIGIPVRCAPVKVL", "text": "SIMILARITY: Belongs to the UPF0026 family."}
+{"protein": "MFHGKHPGGLSERGRALLLEGGKALGLDLKPHLEAFSRLYALLQEASGKVNLTALRGEEEVVVKHFLDSLTLLRLPLWQGPLRVLDLGTGAGFPGLPLKIVRPELELVLVDATRKKVAFVERAIEVLGLKGARALWGRAEVLAREAGHREAYARAVARAVAPLCVLSELLLPFLEVGGAAVAMKGPRVEEELAPLPPALERLGGRLGEVLALQLPLSGEARHLVVLEKTAPTPPAYPRRPGVPERHPLC", "text": "FUNCTION: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Shows a marked preference for deproteinized 16S rRNA as substrate and is completely inactive with native 30S subunits as substrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family."}
+{"protein": "MNPSEMQRKAPPRRRRHRNRAPLTHKMNKMVTSEEQMKLPSTKKAEPPTWAQLKKLTQLATKYLENTKVTQTPESMLLAALMIVSMVVSLPMPAGAAVANYTNWAYVPFPPLIRAVTWMDNPIEVYVNDSVWVPGPIDDRCPAKPEEEGMMINISIGYRYPPICLGRAPGCLMPAVQNWLVEVPTVSPISRFTYHMVSGMSLRPRVNYLQDFSYQRSLKFRPKGKPCPKEIPKESKNTEVLVWEECVANSAVILQNNEFGTIIDWAPRGQFYHNCSGQTQSCPSAQVSPAVDSDLTESLDKHKHKKLQSFYPWEWGEKRISTPRPKIVSPVSGPEHPELWRLTVASHHIRIWSGNQTLETRDRKPFYTVDLNSSLTLPLQSCVKPPYMLVVGNIVIKPDSQTITCENCRLLTCIDSTFNWQHRILLVRAREGVWIPVSMDRPWEASPSVHILTEVLKGVLNRSKRFIFTLIAVIMGLIAVTATAAVAGVALHSSVQSVNFVNDGQKNSTRLWNSQSSIDQKLANQINDLRQTVIWMGDRLMSLEHRFQLQCDWNTSDFCITPQIYNDSEHHWDMVRRHLQGREDNLTLDISKLKEQIFEASKAHLNLVPGTEAIAGVADGLANLNPVTWVKTIGSTTIINLILILVCLFCLLLVCRCTQQLRRDSDHRERAMMTMAVLSKRKGGNVGKSKRDQIVTVSV", "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 8 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": "MAQALGEDLVQPPELQDDSSSLGSDSELSGPGPYRQADRYGFIGGSSAEPGPGHPPADLIRQREMKWVEMTSHWEKTMSRRYKKVKMQCRKGIPSALRARCWPLLCGAHVCQKNSPGTYQELAEAPGDPQWMETIGRDLHRQFPLHEMFVSPQGHGQQGLLQVLKAYTLYRPEQGYCQAQGPVAAVLLMHLPPEEAFWCLVQICEVYLPGYYGPHMEAVRLDAEVFMALLRRLLPHVHKHLQQVGVGPLLYLPEWFLCLFARSLPFPTVLRVWDAFLSEGARVLFRVGLTLVRLALGTAEQRGACPGLLETLGALRAIPPAQLQEEAFMSQVHSVVLSERDLQREIKAQLAQLPDSAPGPPPRPQVRLAGAQAIFEAQQLAGVRRGAKPEVPRIVVQPPEEPRPPRRKPQTRGKTFHGLLTRARGPPIEGPPRPQRGSTSFLDTRF", "text": "FUNCTION: Inhibits the Ras signaling pathway through its intrinsic Ras GTPase-activating protein (GAP) activity. Acts as a negative feedback inhibitor of the calcineurin signaling pathway that also mediates crosstalk between calcineurin and Ras."}
+{"protein": "MFVNSSPIADGLSALVGLDSQPLQFYERGDVVPPKDQGCWQIYRGILQVSQWTLGGDEVLMGWAQPGSFVGLDFSAHQRETYQIRALTDVYLRGYSLEMITNNANLCRLVLDQTLQQVRQREALLAIAGYKRVDERLQGLLNLLGQELGQPGTGGMRLSVRLTHQMLANAIGTTRVTVTRLLGEFQTQGKVSLDGDRHLVIALGN", "text": "FUNCTION: Probably regulates the expression of genes from the sulfate permease complex. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MITTLLRRSLLDASKQATSINGILFHQLAPAKYFRVPAVGGLRDFSKMTFEKKKTSEEEEGSGDGVKVNDQGNKGEQLIVSYWGVKPMKITKEDGTEWKWSCFRPWETYKADLTIDLKKHHVPSTLPDKIAYWMVKSLRWPTDLFFQRRYGCRAIMLETVAAVPGMVGGMLMHFKSLRRFEQSGGWIKALLEEAENERMHLMTFMEVAKPKWYERALVISVQGVFFNAYLIGYIISPKFAHRMVGYLEEEAIHSYTEFLKELDNGNIENVPAPAIAVDYWRLEADATLRDVVMVVRADEAHHRDVNHYASDIHYQGHELKEAPAPIGYH", "text": "FUNCTION: Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein Note=Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane. SIMILARITY: Belongs to the alternative oxidase family."}
+{"protein": "MSFSQAVSGLNAAATNLDVIGNNIANSATYGFKSGTASFADMFAGSKVGLGVKVAGITQDFTDGTTTNTGRGLDVAISQNGFFRLVDSNGSVFYSRNGQFKLDENRNLVNMQGMQLTGYPATGTPPTIQQGANPAPITIPNTLMAAKSTTTASMQINLNSTDPVPSKTPFSVSDADSYNKKGTVTVYDSQGNAHDMNVYFVKTKDNEWAVYTHDSSDPAATAPTTASTTLKFNENGILESGGTVNITTGTINGATAATFSLSFLNSMQQNTGANNIVATNQNGYKPGDLVSYQINNDGTVVGNYSNEQEQVLGQIVLANFANNEGLASQGDNVWAATQASGVALLGTAGSGNFGKLTNGALEASNVDLSKELVNMIVAQRNYQSNAQTIKTQDQILNTLVNLR", "text": "SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the flagella basal body rod proteins family."}
+{"protein": "MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKAKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE", "text": "FUNCTION: An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region. Protect proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the CpxP/Spy family."}
+{"protein": "MSLVEISGSDAMAAPMPGRVPPPPPRPPPMPRRLPPMFDAFDHTGAGMVWGFPRPAKKRASLKPLHWVKITSDLQGSLWDELQRRHGDSQTAIELDISELETLFFVEAKPEKIRLHDLRRASYRVFNVINLSMPLPDMMTAVLAMDESVVDVDQIEKLIKFCPTNEEMELLKTYTGDKAALGKYEQYLLELMKVPRLEAKLRVFSFKTQFGTKITELKERLNVVTSACEENLLLIHQVRSSEKLKEIMKKIPCLGNTSNQGPDRGKTFLSPVEFKLDRLSVKRMHYFCKLKEIMKKIPCLGNTSKSNPRVGVKLDSSVSDTHTVKSMHYYCKVLASEASELLDVYKDLQSLESASKIQVKSLAQNIQAIIKRLEKLKQELTASETDGPASEVFCNVCWFFVRLMI", "text": "SIMILARITY: Belongs to the formin-like family. Class-II subfamily."}
+{"protein": "MATPSSATSLNVENIVFPSSVKPPGDTNTLFLGGAGVRGMEIQGNFVKFTGIGVYLEDKAIPLLAGKWKGKTAEELVNSVEFFRDIVTGPFKKFTQVTMILPLTGKQYSEKVSEMCVGVWKAHGTYTDADGATIDKFLEVFKDENFPPGASILFTTSPDGSLTISFSKDGMIPEAANIVLENEKLAQAVIESVIGKNGVSPATKQSLASRLADLMNHFDEKATTDAEPNLSKNGL", "text": "FUNCTION: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin (By similarity). SIMILARITY: Belongs to the chalcone isomerase family."}
+{"protein": "MLCCMRRTKQVEKNDEDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKDDAQAAEAEANKKDEAPVADGVEKKGEGTTATEAAPATGSKPDEPGKAGETPSEEKKGEGDAATEQAAPQAPASSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATTPAAEDAAAKATAQPPTETGESSQAEENIEAVDETKPKESARQDEGKEEEPEADQEHA", "text": "FUNCTION: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, growth cone membrane; Peripheral membrane protein; Cytoplasmic side Synapse Cell projection, filopodium membrane; Peripheral membrane protein Perikaryon Cell projection, dendrite Cell projection, axon Cytoplasm Note=Cytoplasmic surface of growth cone and synaptic plasma membranes. SIMILARITY: Belongs to the neuromodulin family."}
+{"protein": "MNGGGVFTDILAASGRIFEVMVEGHWATVGYLFDSLGKGVSRINQNAYGNM", "text": "FUNCTION: Component of the photosynthetic apparatus. The light harvesting B740 complex binds bacteriochlorophyll e. SUBCELLULAR LOCATION: Chlorosome, chlorosome envelope. SIMILARITY: Belongs to the BChl C/E-binding protein family."}
+{"protein": "MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDEDSTTDTDGAAETCVSVQCQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQAVEEMMDRIKKGVHLRPVNQTARPKTKPESSKGCESAVDELKGILGTLNKSTSSRSLKSLDPENSETELERILRRRKVTAEADSSSPTGILATSESKSMPVLGSVSSVTKTALNKKTLEAEFNSPSPPTPEPGEGPRKLEGCTSSKVTFQPPSSIGCRKKYIDGEKQAEPVVVLDPVSTHEPQTKDQVAEKDPTQHKEDEGEIQPENKEDSIENVRETDSSNC", "text": "FUNCTION: Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1- dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Also plays a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons. SUBCELLULAR LOCATION: Perikaryon Cell projection, axon Cell projection, growth cone Cytoplasm, cytoskeleton Cell projection, filopodium Cell projection, lamellipodium Note=Localizes in multiple growth cones at neurite tips before the neuronal symmetry-breaking step. Accumulates in growth cones of a single nascent axon in a neurite length-dependent manner during the neuronal symmetry-breaking step; when absent from the nascent axon's siblings, probably due to competitive transport, prevents the formation of surplus axons. Transported anterogradely from the soma to the axon growth cone in an actin and myosin-dependent manner and passively diffuses back to the cell bodies. Colocalized with L1CAM in close apposition with actin filaments in filopodia and lamellipodia of axonal growth cones in hippocampal neurons. Exhibits retrograde movements in filopodia and lamellopodia of axonal growth cones. Colocalized with KIF20B along microtubules to the tip of the growing cone in primary hippocampal neurons. Recruited to the growth cone of developing axon in a KIF20B- and microtubule-dependent manner. SIMILARITY: Belongs to the shootin family."}
+{"protein": "MAVRILVVDDDRAVRESLRRSLSFNGYSVELAQDGVEALDAITNNRPDALILDVMMPRLDGLEVCRQLRSTGDDLPILVLTARDSVSERVAGLDAGADDYLPKPFALEELLARMRALLRRTVSDDSGDSQKMTFSDLTLDPVTREVTRGGRQISLTRTEFSLLEMLIANPRRVLTRSRILEEVWGFDFPTSGNALEVYIGYLRRKTEAEGEPRLIHTVRGVGYVLRETPP", "text": "FUNCTION: Member of the two-component regulatory system MprB/MprA which contributes to maintaining a balance among several systems involved in stress resistance and is required for establishment and maintenance of persistent infection in the host. Functions as a transcriptional regulator that recognizes a 19-bp nucleotide motif comprizing two loosely conserved 8-bp direct DNA-binding motif repeats separated by a 3-bp spacer region (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MEALNSILTGYAVAALSVYALWFYFLSRRLTGPKVLPFVGSLPYLIANRSRIHDWIADNLRATGGTYQTCTMVIPFVAKAQGFYTVTCHPKNVEHILKTRFDNYPKGPMWRAAFHDLLGQGIFNSDGDTWLMQRKTAALEFTTRTLRQAMARWVNGTIKNRLWLILDRAVQNNKPVDLQDLFLRLTFDNICGLTFGKDPETLSLDLPDNPFSVAFDTATEATLKRLLYTGFLWRIQKAMGIGSEDKLKKSLEVVETYMNDAIDARKNSPSDDLLSRFLKKRDVNGNVLPTDVLQRIALNFVLAGRDTSSVALSWFFWLVMNNREVETKIVNELSMVLKETRGNDQEKWTEEPLEFDEADRLVYLKAALAETLRLYPSVPQDFKYVVDDDVLPDGTFVPRGSTVTYSIYSIGRMKTIWGEDCLEFRPERWLTADGERFETPKDGYKFVAFNAGPRTCLGKDLAYNQMKSVASAVLLRYRVFPVPGHRVEQKMSLTLFMKNGLRVYLQPRGEVLA", "text": "FUNCTION: Catalyzes the omega-hydroxylation of various fatty acids (FA). Acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18 but not on hexadecane. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MPTTIDEGLPAPHNFVSFTTLIARKYQNLIEKTISFIPQRWAFVGFLSFLYILRVSLSSGGWYVITYALGIFLLTRFIAFLSPKWDPELEEDSGDSLPTTLNRNDDEAKPFIRRLPEFLFWHSIFKALFISIFCTFIPFLDLPVFWPILLLYFIIIFSVTMKKQIKHMIKYKYIPFTVGKKTYTKNNS", "text": "FUNCTION: May be involved in protein transport along the secretory pathway. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RER1 family."}
+{"protein": "MVGSHKASGVLLVLLVVMATTIANGTPVVDKAKNAATAVEDTAKNAATAVGGAAASVGAKVSGAKPGAAVDVKASGAKGDSKTDDSAAFAAAWKEACAAGSTITVPKGEYMVESLEFKGPCKGPVTLELNGNFKAPATVKTTKPHAGWIDFENIADFTLNGNKAIFDGQGSLAWKANDCAKTGKCNSLPINIRFTGLTNSKINSITSTNSKLFHMNILNCKNITLSDIGIDAPPESLNTDGIHIGRSNGVNLIGAKIKTGDDCVSIGDGTENLIVENVECGPGHGISIGSLGRYPNEQPVKGVTVRKCLIKNTDNGVRIKTWPGSPPGIASNILFEDITMDNVSLPVLIDQEYCPYGHCKAGVPSQVKLSDVTIKGIKGTSATKVAVKLMCSKGVPCTNIALSDINLVHNGKEGPAVSACSNIKPILSGKLVPAACTEVAKPGP", "text": "FUNCTION: May function in depolymerizing pectin during pollen development, germination, and tube growth. Acts as an exo- polygalacturonase. SUBCELLULAR LOCATION: Secreted. Secreted, cell wall. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
+{"protein": "MAELPTAPNGVPSGDYLHRSIDQLRSLGHLTTAQLVHDYKPFNISEFRQNVAERLDYSLKNGLVQHQQQMVMEQQPHPDQQQQQHLHHPQQQQHPPQLKVSYSAPNSPPTPHEQQEQKYDPNRSPPRQQMSSASGSGSNGSSPEEESRRGDGDQAKPYKCGSCSKSFANSSYLSQHTRIHLGIKPYRCEICQRKFTQLSHLQQHIRTHTGDKPYKCRHAGCPKAFSQLSNLQSHSRCHQTDKPFKCNSCYKCFSDEMTLLEHIPKHKDSKHLKTHICNLCGKSYTQETYLQKHLQKHAEKAEKQQHRHTAQVAAHQQHVPASGIGLNLQRQAMNDVNAAYWAKMGADSAAASLAEAIQQQLPQAGGQPYGNFASLQQQHQQQQQELLHHQRLADTPGHSHSPHEEAAGEDLVLRQSTPQHHLQQQQQQQQQQQAQQQQQAQHQPSPGPGNSAFTPLSATVAPPPHLQQHRGPPGSAAAYLYQQNAAAAAAAFPTQLISLHQIRNYAHQPGAAGLIAGDHLALGLSAVNAAKEKAQ", "text": "FUNCTION: Transcription factor involved in neuronal fate specification. First required in embryonic CNS development to define the number of cells that express apterous (ap) in the ap thoracic cluster of interneurons. Later on, it plays a central role in the combinatorial code of transcription factors that specifies the fate of the Tv neuron in the ap cluster by participating in the transcription regulation of FMRFa in Tv cells. Also required for projection neuron dendritic targeting. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MEYSRKTYLDLNIMAKYILILSLFFGPGLSWDVFYSGDEDQLSLARERRAANYNPSPHMSTWERNEIQQEILNILGLQHRPRPPSLRGGQNQFCAQFTEWSYYRTLNIDEQSGHPSETEPQPGGLASNAIYNSPDSSGIGSVMSGTVFNYTRNEVQAVSQADTIMSLPVHYKDAAIEDTEHRYRFDIGRIPQGETVTSAELRVFRDAGRQGRSLYRIDVLLLRERGSDGSRSPVYLDSTIVGAGDHGWLVFDMTSATSTWRSYPGANVGLQLRVESLQGLNIDPTDAGVVGVGNNEGREPFMVVFFQRNEEVIATNSHLRRNRRAATRQKKGGKRPRKPDTDNDIASRDSASSLNSDWQCKRKNLFVNFEDLDWQEWIIAPLGYVAFYCQGECAFPLNGHANATNHAIVQTLVHHMSPSHVPQPCCAPTKLSPITVLYYDDSRNVVLKKYKNMVVRACGCL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
+{"protein": "MSSLQALCSGLPLRPLPENRGRQAGVPHAPVRTPSLSPVEKQLALRNALRYFPPDVQELLAPEFAQELQLYGHIYMYRFCPDIEMRAYPIEQYPCQTKVAAAIMHMIMNNLDPAVAQFPQELVTYGGNGQVFSNWAQFWLTMFYLSKMTEEQTLVMYSGHPLGLFPSSRSAPRLVITNGMVIPNYSSRTEYEKLFALGVTMYGQMTAGSYCYIGPQGIVHGTVLTVLNAARRYLGIEDLAGKVFVTSGLGGMSGAQAKAAVIVGCIGVIAEVDKAALEKRHRQGWLMEVTDSLDRCIQRLREARKKKEVLSLGYHGNVVALWERLVHELDTTGECLVDLGSDQTSCHNPFNGGYYPVQLSFTEAQSLMASNPAVFKDLVQESLRRQVSAINRLAEEKFFFWDYGNAFLLEAQRAGADVEKKGAGRTEFRYPSYVQHIMGDIFSQGFGPFRWVCTSGDPQDLAVTDELATSVLEEAIADGVKVSVKLQYMDNIRWIREAARHRLVVGSQARILYSDQKGRVAIAVAINQAIACRRIKAPVVLSRDHHDVSGTDSPFRETSNIYDGSAFCADMAVQNFVGDACRGATWVALHNGGGVGWGEVINGGFGLVLDGTPEAEGRARLMLSWDVSNGVARRCWSGNQKAYEIICQTMQENSTLVVTLPHKVEDERVLQQALQL", "text": "SIMILARITY: Belongs to the urocanase family."}
+{"protein": "MSWYEKYNIVLNPPKRCFSSCADNLTTILAEDGNNIRAILYSQPQKLKVLQDFLATSRNKMFLYKILDDEIRRVLT", "text": "FUNCTION: Late protein which probably participates in disulfide bond formation by functioning as a thiol-disulfide transfer protein between membrane-associated OPG072 and OPG08. The complete pathway for formation of disulfide bonds in intracellular virion membrane proteins sequentially involves oxidation of OPG072, OPG128 and OPG08. SIMILARITY: Belongs to the orthopoxvirus OPG128 family."}
+{"protein": "MAAVHDLEMESMNLNMGREMKEELEEEEKMREDGGGKDRAKSKKVHRIVSKWMLPEKSRGTYLERANCFPPPVFIISISLAELAVFIYYAVWKPQKQWITLDTGILESPFIYSPEKREEAWRFISYMLVHAGVQHILGNLCMQLVLGIPLEMVHKGLRVGLVYLAGVIAGSLASSIFDPLRYLVGASGGVYALMGGYFMNVLVNFQEMIPAFGIFRLLIIILIIVLDMGFALYRRFFVPEDGSPVSFAAHIAGGFAGMSIGYTVFSCFDKALLKDPRFWIAIAAYLACVLFAVFFNIFLSPAN", "text": "FUNCTION: Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Known substrate: EFNB3. SUBCELLULAR LOCATION: [Rhomboid-related protein 2, C-terminal fragment]: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase S54 family."}
+{"protein": "MELWVSPKECANLPGLPKTSAGVIYVAKKQGWQNRTRAGVKGGKAIEYNANSLPVEAKAALLLRQGEIETSLGYFEIARPTLEAHDYDREALWSKWDNASDSQRRLAEKWLPAVQAADEMLNQGISTKTAFATVAGHYQVSASTLRDKYYQVQKFAKPDWAAALVDGRGASRRNVHKSEFDEDAWQFLIADYLRPEKPAFRKCYERLELAAREHGWSIPSRATAFRRIQQLDEAMVVACREGEHALMHLIPAQQRTVEHLDAMQWINGDGYLHNVFVRWFNGDVIRPKTWFWQDVKTRKILGWRCDVSENIDSIRLSFMDVVTRYGIPEDFHITIDNTRGAANKWLTGGAPNRYRFKVKEDDPKGLFLLMGAKMHWTSVVAGKGWGQAKPVERAFGVGGLEEYVDKHPALAGAYTGPNPQAKPDNYGDRAVDAELFLKTLAEGVAMFNARTGRETEMCGGKLSFDDVFEREYARTIVRKPTEEQKRMLLLPAEAVNVSRKGEFTLKVGGSLKGAKNVYYNMALMNAGVKKVVVRFDPQQLHSTVYCYTLDGRFICEAECLAPVAFNDAAAGREYRRRQKQLKSATKAAIKAQKQMDALEVAELLPQIAEPAAPESRIVGIFRPSGNTERVKNQERDDEYETERDEYLNHSLDILEQNRRKKAI", "text": "FUNCTION: Promotes replication and thereby lytic development by competing with repressor c (Repc) for binding to the internal activation sequence (IAS) in the enhancer/operator region. The outcome of this competition determines if the virus enters latency or starts replication. FUNCTION: Responsible for viral genome integration into the host chromosome. During integration of the incoming virus, DDE-recombinase A cleaves both viral DNA ends and the resulting 3'-OH perform a nucleophilic attack of the host DNA. The 5' flanking DNA attached to the ends of the viral genome (flaps) are resected by the DDE- recombinase A endonuclease activity, with the help of host chaperone ClpX. The gaps created in the host chromosome by the viral genome insertion are repaired by the host primary machinery for double-strand break repair. FUNCTION: Responsible for replication of the viral genome by replicative transposition. During replicative transposition, DDE- recombinase A is part of the transpososome complex. DDE-recombinase A cleaves the viral DNA and the resulting 3'-OH performs a nucleophilic attack of the host DNA. The 5' flanking DNA is not resected and an intermediary structure is formed. This structure is resolved by target- primed replication leading to two copies of the viral genome (the original one and the copied one). Host ClpX and translation initiation factor IF2 play an essential transpososome-remodeling role by releasing the block between transposition and DNA replication. Successive rounds of replicative transposition can lead up to 100 copies of the viral genome. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the mulikevirus repressor c protein family."}
+{"protein": "MEKSTMSAVVLVLNLLVLHLQYSEVHSLANTSSEHDFGYLKFVYNAVDLELEGSYDYIIVGGGTSGCPLAATLSANYSVLVLERGTIATEYPNTLTVDGFAYNLQQQDDGKTPVERFVSEDGIDNVRSRILGGTTIINAGVYARANESFYNNSGVEWDLDLVNEAYEWVEDAIVYKPSNQSWQSITGTAFLEAGVHPDNGFGLVHEEGTRLTGSTFDNSGTRHASDELLNKGDPDNLKVAVEAAVQKIIFSTESSGLTAVGVVYTDSNGTSHRALVSGKGEVILSAGTLGTPQLLLLSGVGPESYLTSLNISVVASHPYVGQYVNDNPRNFINILPPNPIEPSTVTVLGITSDFYQCSLSSLPFDTPPFSLFPTTSYPLPNQTFAHIVSKVPGPLSAGSLTLQSSSNVSVAPNVKFNYCSDPVDLTHCVSGMKKIGVFLSTDALKPYKVDDLPGIDGFNILGTPLPENQTDDAAFEKFCRDTVASYWHYHGGAIVGKVIDGNFRVTGINALRVVDGSTFPATPASHPQGFYLMLGRYVGTKIVQERSASGEAIHTSTFKPKLMDSLKSALSFAF", "text": "FUNCTION: Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. It is a major seed constituent, and could have the additional role of a storage form for reduced nitrogen (By similarity). SUBCELLULAR LOCATION: Vacuole, aleurone grain Note=Primarily found within protein bodies of the cotyledonary parenchyma cells, with lesser amounts within the procambium. SIMILARITY: Belongs to the GMC oxidoreductase family."}
+{"protein": "MMLIIRYGLLNFETSWVHQKTMVFIQIRKRQKKKLSIYLKHPQVYTLGHRANKEYISFCSNNTLVNLHRVDRGGEVTYHDYGQVIIYNITHLQKINRNVNIYIANLEQLGKRILLLYKTKSTKKEKFPGIWIQQKKIVALGIKIIQRTTFHGLSINFSCSKRNYELILACGIKDGISVNFNEIHKKNSQNQFYWKYKIVLLIVDILAFNNIISF", "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 (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the LipB family."}
+{"protein": "MGDNRKVRVVVGGVFDILHVGHVHFLKMAKELGDELIVIVAHDETVKRRKGRPPINPAEDRAELLKSIRYVDDVVIGEPGEISIDLIKRLKPDVIALGPDQDFSCEELKKRLRKEGINAEVIRLPYLYKSDRAKTSKIIQRIIETFCE", "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": "MNKTKIYINGKLIGTCDNPEEFVEEIRAKRRSGEVSHEMNITHYPENHEIYIFTDPGRARRPLIIVEDGEPLLKEEHLEKLSSGEMEWDDLISQGIIEYLDAEEEENTYIAMSPEEVTEEHTHLEIDPSTMLGICAGIIPFANHNSSPRNTMEAGMTKQALGLYASNYNLRTDTRAHLLHHPQVPIVKTRIIDVTGYDERPSGQNFVVAVMSYEGYNMEDALILNKASLERGLARSSFFRSYEATERRYPGGQEDRFEIPEKGVRGYRSERDYRHLDEDGIINPETEVSSGDVLIGKTSPPRFLEEIDEFGTVAERRRETSVTVRHGEEGIVDAVLLTETVEGSRLAKIRVREQRQPEFIGDKFASRHGQKGVVGLIVSQEDMPFTEDGVVPDLIVNPHAIPSRMSVGQVLEMLAGKAACMEGRRVDGTPFTGEEEKDLKEALKANGFESAGVETLYNGITGERIEAEIFIGVAYYQKLHHMTTDRIYARSRGPVQVLTRQPTEGRAREGGLRFGEMERDCLIAHGAALALKERLLDESDKYEALVCAECGMIAIYDKIRDKKYCPICEDSESFPVEISYAFKLLLDELKSLCIFPKLVLEDKA", "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": "MNYFRYKQFNKDVITVAVGYYLRYTLSYRDISEILRERGVNVHHSTVYRWVQEYAPILYQIWKKKHKKAYYKWRIDETYIKIKGKWSYLYRAIDAEGHTLDIWLRKQRDNHSAYAFIKRLIKQFGKPQKVITDQAPSTKVAMAKVIKAFKLKPDCHCTSKYLNNLIEQDHRHIKVRKTRYQSINTAKNTLKGIECIYALYKKNRRSLQIYGFSPCHEISIMLAS", "text": "FUNCTION: Involved in the transposition of the insertion sequence. FUNCTION: Involved in the transposition of the insertion sequence."}
+{"protein": "KSLFLVLFLGMVSLSICEEEKRENEDEEKQEDDEQSEMKRGLWSTIKNVGKEAAIAAGKAVLGSLGEQ", "text": "FUNCTION: Has antibacterial activity against the Gram-negative bacteria E.coli ATCC 11775 (MIC=0.5 uM), and the Gram-positive bacteria S.aureus ATCC 12600 (MIC=0.5 uM) and M.luteus ATCC 49732 (MIC=2.0 uM). Does not inhibit the growth of the fungus C.albicans. 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": "MRQVCCSALPPPLEKARCSSYSYSDSSSSSSSNNSSSSTSSRSSSRSSSRSSRGSTTTTSSSENSGSNSGSIFRPAAPPEPRPQPQPQPRSPAARRAAARSRAAAAGGMRRDPAPGSSMLLFGVSLACYSPSLKSVQDQAYKAPVVVEGKVQGLAPAGGSSSNSTREPPASGRVALVKVLDKWPLRSGGLQREQVISVGSCAPLERNQRYIFFLEPTEQPLVFKTAFAPVDPNGKNIKKEVGKILCTDCATRPKLKKMKSQTGEVGEKQSLKCEAAAGNPQPSYRWFKDGKELNRSRDIRIKYGNGRKNSRLQFNKVKVEDAGEYVCEAENILGKDTVRGRLHVNSVSTTLSSWSGHARKCNETAKSYCVNGGVCYYIEGINQLSCKCPNGFFGQRCLEKLPLRLYMPDPKQKHLGFELKEAEELYQKRVLTITGICVALLVVGIVCVVAYCKTKKQRRQMHHHLRQNMCPAHQNRSLANGPSHPRLDPEEIQMADYISKNVPATDHVIRREAETTFSGSHSCSPSHHCSTATPTSSHRHESHTWSLERSESLTSDSQSGIMLSSVGTSKCNSPACVEARARRAAAYSQEERRRAAMPPYHDSIDSLRDSPHSERYVSALTTPARLSPVDFHYSLATQVPTFEITSPNSAHAVSLPPAAPISYRLAEQQPLLRHPAPPGPGPGPGADMQRSYDSYYYPAAGPGPRRGACALGGSLGSLPASPFRIPEDDEYETTQECAPPPPPRPRTRGASRRTSAGPRRWRRSRLNGLAAQRARAARDSLSLSSGSGCGSASASDDDADDADGALAAESTPFLGLRAAHDALRSDSPPLCPAADSRTYYSLDSHSTRASSRHSRGPPTRAKQDSGPL", "text": "FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor. SUBCELLULAR LOCATION: [Pro-neuregulin-2, membrane-bound isoform]: Cell membrane; Single-pass type I membrane protein Note=Does not seem to be active. SUBCELLULAR LOCATION: [Neuregulin-2]: Secreted. SIMILARITY: Belongs to the neuregulin family."}
+{"protein": "MLKFMLDTNICIFTIKNKPASVRERFNLNQGKMCISSVTLMELIYGAEKSQMPERNLAVIEGFVSRIDVLDYDAAAATHTGQIRAELARQGRPVGPFDQMIAGHARSRGLIIVTNNTREFERVGGLRTEDWS", "text": "FUNCTION: Ectopic overexpression in E.coli induces the YoeB toxin, but this is not the cause of VapC toxicity. FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. A tRNA-(fMet) endonuclease, it cleaves both charged and uncharged tRNA- (fMet) between positions 38 and 39 at the anticodon stem-loop boundary. Does not cleave tRNA(Met), tRNA(Arg2), tRNA(His), tRNA(Leu), tRNA(Phe) tRNA(Thr1), tRNA(Tyr) or tRNA(Val). Overexpression in E.coli inhibits translation, leads to loss of cell growth and degradation of tRNA(fMet); these effects are neutralized by expression of cognate antitoxin VapB. The VapB/VapC complex probably regulates transcription of its own promoter. SIMILARITY: Belongs to the PINc/VapC protein family."}
+{"protein": "MDTKMQSLPTTHPHPHSSSRPQSHTSNQCNQCTCSHHCRSCSQAGHAGSSSSPSPGPPMKHPKPSVHSRHSPARPSHRGSCPKNRKTFEGKVSKRKAVRRRKRTHRAKRRSSGRRYK", "text": "FUNCTION: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals (PubMed:15163613, PubMed:15189834, PubMed:15083521, PubMed:28366643). In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction (PubMed:28366643). The histone H2AB1-H2BC1/TH2B dimer is required for loading of TNP2 onto chromatin (PubMed:28366643). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Loaded onto the nucleosomes of condensing spermatids (PubMed:28366643). Inclusion of the H2AB1- H2BC1/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition protein TNP2 (PubMed:28366643). Nuclear import is mediated by IPO4. Nucleolar localization requires the protein to be phosphorylated (By similarity). SIMILARITY: Belongs to the nuclear transition protein 2 family."}
+{"protein": "MASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTRVLPAQATEYAFAFIQVPQDDDARTDAVDSVVRDIQNTQCLLNVEHLSAGCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR", "text": "FUNCTION: (Microbial infection) Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). FUNCTION: Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:28546213, PubMed:18453631). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213). Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934). Plays a role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as a transcriptional coactivator for STAT5 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Melanosome Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus (PubMed:12234934). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065)."}
+{"protein": "MDTSKISARYSKVDLLALRYEGKSRQRPQCSTRLELQTLGFWKINLNTAALTVSSAYSNQNKNRLSPEADNSSLICSNSSSISSRRAMRNRERANNYYQRFVPTDSLLISGEDKDKDALSHGQPYKLNIIDHRSISSSHLMPAFAKRRFVISKGSNSEESNEGINTCASKGKAASSPSRKGSELDTAETCLNFVQPDHDQCMSSSPTFSTSRQERRIGSGRLLPRSDNWDYKNEKTVEASIENEKETSPNGSGSTSSLNQHNQSQHRSRTFSGRLVERVPEVTDRRFQYDSKKSFDRQGINNRRISGKEPFSTQSRSKRGNSYLIHEEPEWFSAGPKSQLETIDLHGFEDLEKNEERSVTEDKNNQIQQLDKNLDAQASKDEASMRNSNDSLNFREVIPSDEKKHTDENVVTSIQNSTDLGHPNKNKPIQMQPSQNPESEFNFDAFLNMHPLDNSVLSNDETGKSDSKGTSRFSRWFRQKEAANNNEFPGFRESHAQEKRGIPSVKDLEAQMIKVDMRTDLINPIAGSLCQTVQMEKPIARDTEAFKKLLQQLGSQARQHHPCNDDCRTINLSNIANHVHLESKLHQKINDGHLQQPELSVNVPTMPTSSHVFLQKRLEIQHLIQRLHCGDVSHDFLEKELDNPSTPAATKDVIATVLNEYSHSKRNPVVTGDPNIFTQQSFLQPQSVHQHYSQELHSQNTANHTINQLISHGNSPTPLAFTPTSVLRKMTADKDTQSPSTYCQNPQYHVHQQNAKQVGTRENVLEPQLTATMAVQPRMILGGGNFAIGQNNQHLSPNMSQSRNQQVLKWTSGNMQMVHGKTFGRPILKGGLNSMPHSNSALPFTAHKIEMQPIHQPHLQQQQHRFKAVQSVESNLNTESVHQNITSPVGWHQLYMQHQQQHHHTRQQLSQRVIYGEMHRQSNPQMSPPVPGFSDSSDSGNVIKANSLTSPSYQRDERISSPTNQLAQWFSPELLAKASAGKLPLLNVNQALSLEEFERSIQHSSGVVHN", "text": "FUNCTION: eIF4E1-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (By similarity). Probably plays a role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (By similarity). Acts as a binding platform for multiple RNA-binding proteins. Required for the formation of P-bodies (By similarity). SUBCELLULAR LOCATION: Cytoplasm, P-body Cytoplasm Nucleus Note=Mainly localizes to processing bodies (P-bodies) (PubMed:24335285). Present at low level in other parts of the cytoplasm and in the nucleus (PubMed:24335285). SIMILARITY: Belongs to the 4E-T/EIF4E-T family."}
+{"protein": "MATQKSTTALDAKSKMTTDLVRPLANFPSSIWGDRFMSLSIDKSELKTYDKVIEKQKQELRRLIIDPSMDSNKKLSLINSVYRLGLTYLFEEEIEGQLDKLFKEIDMQEACNEADLYTISVNFQVFRQHGYKLSCNVFNKFKDYTSDHKFKEYIMADVRGMLGLYESTQLRIRGETILEEAFAFTESQLKGVLDTLEGNIARQVKHALTSPFHRGLRTVEARIYFSNYEEECSTYDSLQKLANAHFNYLQLQHKEELASVIKWGEDMDFKTITPYARDRIPDLYLWGLGLFSEPHYSQARILISKMAQLICVLDDTYDAYATIDELHLLTNAINRWELSATEQLPEYMKPLYKVLLNEHVELEKQLSSKGKSNFVNASKKAFQELAMGYLQEAEWRHNGKVPSFQEYLKNGLITSTYNVFAKSSLICMSDIVTEEACTWYDSDPIILQATGLLGRVYNDISTFQFERKRAQQQITSIEAYMKTFGVPENVALEELKKMVEIAWNDINKGCLNTNEISKKLLAPIVNLARMTDVIYRYNDKFTFPEKTIEEYITLLFCESIPKN", "text": "FUNCTION: Sesquiterpene synthase that catalyzes the formation of sesquiterpenes and sesquiterpenoid alcohols (PubMed:27231873). Converts farnesyl diphosphate (FPP) to 10-epi-juneol (PubMed:27231873). Converts FPP to tau-cadinol (PubMed:27231873). 10-epi-juneol is the major product (PubMed:27231873). SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MTSSPVSRVVYNGKRTSSPRSPPSSSEIFTPAHEENVRFIYEAWQGVERDLRGQVPGGERGLVEEYVEKVPNPSLKTFKPIDLSDLKRRSTQDAKKS", "text": "FUNCTION: The phosphorylation status of MCRIP1 functions as a molecular switch to regulate epithelial-mesenchymal transition. Unphosphorylated MCRIP1 binds to and inhibits the transcriptional corepressor CTBP(s). When phosphorylated by MAPK/ERK, MCRIP1 releases CTBP(s) resulting in transcriptional silencing of the E-cadherin gene and induction of epithelial-mesenchymal transition (PubMed:25728771). SUBCELLULAR LOCATION: Nucleus Cytoplasm, Stress granule. SIMILARITY: Belongs to the MCRIP family."}
+{"protein": "TPNSYILQQFENPANPKLIVAIFPSFGER", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family."}
+{"protein": "MTPLRVFRKTTPLVNTIRLSLLPLAGLSFSAFAAQVNIAPGSLDKALNQYAAHSGFTLSVDASLTRGKQSNGLHGDYDVESGLQQLLDGSGLQVKPLGNNSWTLEPAPAPKEDALTVVGDWLGDARENDVFEHAGARDVIRREDFAKTGATTMREVLNRIPGVSAPENNGTGSHDLAMNFGIRGLNPRLASRSTVLMDGIPVPFAPYGQPQLSLAPVSLGNMDAIDVVRGGGAVRYGPQSVGGVVNFVTRAIPQDFGIEAGVEGQLSPTSSQNNPKETHNLMVGGTADNGFGTALLYSGTRGSDWREHSATRIDDLMLKSKYAPDEVHTFNSLLQYYDGEADMPGGLSRADYDADRWQSTRPYDRFWGRRKLASLGYQFQPDSQHKFNIQGFYTQTLRSGYLEQGKRITLSPRNYWVRGIEPRYSQIFMIGPSAHEVGVGYRYLNESTHEMRYYTATSSGQLPSGSSPYDRDTRSGTEAHAWYLDDKIDIGNWTITPGMRFEHIESYQNNAITGTHEEVSYNAPLPALNVLYHLTDSWNLYANTEGSFGTVQYSQIGKAVQSGNVEPEKARTWELGTRYDDGALTAEMGLFLINFNNQYDSNQTNDTVTARGKTRHTGLETQARYDLGTLTPTLDNVSIYASYAYVNAEIREKGDTYGNLVPFSPKHKGTLGVDYKPGNWTFNLNSDFQSSQFADNANTVKESADGSTGRIPGFMLWGARVAYDFGPQMADLNLAFGVKNIFDQDYFIRSYDDNNKGIYAGQPRTLYMQGSLKF", "text": "FUNCTION: FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family."}
+{"protein": "MSIQNEMPGYDEMNRFLNQQGAGLTPAEMHGLISGMICGGNNDSSWQPLLHDLTNEGLAFGHELAQALRKMHAATSDALEDDGFLFQLYLPEGDDVSVFDRADALAGWVNHFLLGLGVTQPKLDKVTGETGEAIDDLRNIAQLGYDESEDQEELEMSLEEIIEYVRVAALLCHDTFTRQQPTAPEVRKPTLH", "text": "SIMILARITY: Belongs to the UPF0149 family."}
+{"protein": "MELSSGVCPATRLQEAEKAAVHKRSPKVLEALRKLNIQADQAPVIAVLGSGGGLRAHIACLGVLSELKELGLLDAVTYLAGVSGSTWALSSLYTKNGNMEGIEEELKHRYEKNEWDFHESLEKAIQASKRENYSLTDFWAYLIVSRQIRELQDSNLSSLKKQVEEGVLPYPIFAAIDEDLLADWRERKTQNSWFEFTPHHAGYPALGAYVPITEFGSRFENGKLVKSEPERDLTFLRGLWGSAFADIKEIKNYILNYFRNPFGKLKFIEGPVTYSEAPRMNVDAMLLDLVMAYFTDMNDPSIKDKLCALQQALGTETDEFGIEMAEIIQNWNETSAEKKEQFLDHLLDRFKKTQEDTTTYSLMNWNTGLVWDRCVFVNETRKCVSKWQWGTVYNFLYKHGKIADETMCSRELLHLVDAGFAINTPYPLVLPPVRETHLILSFDFSAGDPLETIRATADYCQRHEIPFPEVSEDQLKEWAKAPASCYVLRGETGPVVMHFTLFNKDNCGDDIETWRKKYGTVKLSDSYTPDLVRDLLRVSKENVKKNKINILSEMRKVAGNPGNIPRVNKEACLGDRVKDPQGSQTVEFKKSHNISKD", "text": "FUNCTION: Calcium-independent phospholipase, lysophospholipase and O- acyltransferase involved in phospholipid remodeling. Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids with choline and ethanolamine head groups, producing lysophospholipids that are used in deacylation-reacylation cycles. Transfers the sn-1 fatty acyl from one lysophospholipid molecule to the sn-2 position of another lysophospholipid to form diacyl, alkylacyl and alkenylacyl glycerophospholipids. Cleaves ester bonds but not alkyl or alkenyl ether bonds at the sn-1 position of lysophospholipids. Catalyzes sn-2 fatty acyl transfer from phospholipids to the sn-2 position of 1-O-alkyl or 1-O-alkenyl lysophospholipids with lower efficiency. SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus envelope Cytoplasm, cell cortex Cytoplasm, cytoskeleton, spindle Note=In germinal vesicle stage oocytes and early embryos, shows mainly uniform nuclear and cortical expression. During germinal vesicle breakdown, found in intensely stained foci which accumulate near the dissolving nuclear envelope. Also localizes to spindle poles at metaphase II."}
+{"protein": "MAMNFVTFNQDYSYLAVATSKGFRIFTTDPFAKSYETKEGNIAIIEMLFSTSLVALILSPRRLQITNTKRQSTICELTFPTTVLAVKLNRKRLVIVLEDQIYLYDIQTMKLLYTIQTSPNPNAICALSPSSDNCYLAYPLPQKAPPSSFNPPSHTPPGSTHVSPTSGEVLIFDTLKLEAINVIEAHRSPLACITLNSDGTLLATASDKGTIIRVFSVPDGHKLYQFRRGSMPSRIFSMSFNTTSTLLCVSSSTETIHLFKLSHPTSSPDASPSSPVGRDRSLSQSSSGYSPDRGDLTGDVGSSDFPARKHNGTLMGMIRRTSQNVGSTVAAKVGGYLPKGVSEMWEPTRDFAWFKLPKPNQTSGGSVNNGPLRSVVAMSSNTPQVMVVTSDGNFYVFSIDLSKGGEGTLTKQYSVLESNDRLGYSVTDY", "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": "MTEIENIGALEVLFSPESIEQSLKRCQLPSTLLYDEKGLRLFDEITNLKEYYLYESELDILKKFSDSIANQLLSPDLPNTVIELGCGNMRKTKLLLDAFEKKGCDVHFYALDLNEAELQKGLQELRQTTNYQHVKVSGICGCFERLLQCLDRFRSEPNSRISMLYLGASIGNFDRKSAASFLRSFASRLNIHDNLLISFDHRNKAELVQLAYDDPYRITEKFEKNILASVNAVFGENLFDENDWEYKSVYDEDLGVHRAYLQAKNEVTVIKGPMFFQFKPSHLILIEESWKNSDQECRQIIEKGDFKLVSKYESTIADYSTYVITKQFPAMLQLPLQPCPSLAEWDALRKVWLFITNKLLNKDNMYTAWIPLRHPPIFYIGHVPVFNDIYLTKIVKNKATANKKHFWEWFQRGIDPDIEDPSKCHWHSEVPESWPSPDQLREYEKESWEYHIVKLCKAMDELSTSEKRILWLCYEHVAMHVETTLYIYVQSFQNANQTVSICGSLPEPAEKLTKAPLWVNVPETEIAVGMPLTTQYTSVGSNLQSSDLSAHENTDELFYFAWDNEKPMRKKLVSSFSIANRPISNGEYLDFINKKSKTERVYPKQWAEIDGTLYIRTMYGLLPLDDYLGWPVMTSYDDLNNYASSQGCRLPTEDELNCFYDRVLERTDEPYVSTEGKATGFQQLHPLALSDNSSNQIFTGAWEWTSTVLEKHEDFEPEELYPDYTRDFFDGKHNVVLGGSFATATRISNRRSFRNFYQAGYKYAWIGARLVKN", "text": "FUNCTION: Catalyzes the SAM-dependent triple methylation of the alpha- amino group of histidine to form hercynine and subsequent conjugation with cysteine and oxygen to form hercynylcysteine sulfoxide, the first two steps in the biosynthesis pathway of ergothioneine (PubMed:24828577). May play a role in meiosis (PubMed:16303567). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: In the N-terminal section; belongs to the methyltransferase superfamily. EgtD family. SIMILARITY: In the C-terminal section; belongs to the EgtB family."}
+{"protein": "MAASAKRKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYVPPEQAKVVASVHASISGSSASSTSSTPEVKPLKSLLGESAPALHLNKGTPTQSPVVGRSQGQQQEKKQFDLLSDLGSDIFAAPAPQSTATANFANFAHFNSHAAQNSANAEFANFDAFGQSSGSSNFGGFPTASHSPFQPQTTGGSAGSVNANFAHFDNFPKSSSADFGSFSTSQSHQTASTVSKVSTNKAGLQTADKYAALANLDNIFSAGQGGDQGSGFGTTGKAPVGSVVSVPSHSSASSDKYAALAELDSVFSSAATSNNAYTSTSNASSSVFGTVPVGASPQTQPASSGPAPFGATPSTNPFVAATGPSAASSTNPFQTNARGATAATFGTASMSMPAGFGTPAQYSLPTSFSGSFQQPPFPAQAAFPQQTAFSQQPNGAGFATFGQTKPVVTPFGQVAAAGVSSNPFMTGAPTGQFPTGSSSTNPFL", "text": "FUNCTION: Required for vesicle docking or fusion during acrosome biogenesis. May play a role in RNA trafficking or localization (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasmic vesicle."}
+{"protein": "MPKPSSSSSSDSPSLTTAKPAGSEVAKKVLPAKATQTVDVSASTSSLSGSKSTTRRSAATGRTSASRATAATPASRGGKSAAGSSGSGSASGGAIKPPASSSVPSFVQGIALGMIETRGMVPAIEAADAMTKAAEVNLISREYVGGGYVTVMVRGETGAVNAAVRAGADACERVGDGLVAAHIIARPHQEVEPALRPTHAKRRS", "text": "FUNCTION: A probable carboxysomal shell protein found only in Prochlorococcus and Synechococcus strains that grow in low light. SUBCELLULAR LOCATION: Carboxysome Note=This cyanobacterium makes alpha-type carboxysomes. SIMILARITY: Belongs to the bacterial microcompartments protein family."}
+{"protein": "MQIHKLCFLVLFLANAAFAVKFNFDSFDGSNLLFLGDAELGPSSDGVSRSGALSMTRDENPFSHGQGLYINQIPFKPSNTSSPFSFETSFTFSITPRTKPNSGQGFAFIITPEADNSGASDGGYLGILNKTNDGKPENHILAIEFDTFQNKEFLDISGNHVGVNINSMTSLVAEKAGYWVQTRVGKRKVWSFKDVNLSSGERFKAWVEFRNKDSTITVTLAPENVKKPKRALIEAPRVLNEVLLQNMYAGFAGSMGRAVERHDIWSWSFENAAKNN", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the leguminous lectin family."}
+{"protein": "MSKNNATTESNRQIPFTEQRLCDYYQERKRYEISCYIGEYFNIRKQVCIDEANYWVTLSALVKAGKALGFPLVYSVKDHTYGRTIYFEYFKNMKRTNLNINTVCLTKDIILQIVAILYSLYKNNIFSDDFKFDLVSIPRSTISMSINHLVLLFNTESLILLSTNTHLYKSELSQSCYLDYMTAHQDLMTRRNLKSTNYFFEWFIRNHFENISRQYLDIFKIKKNYINTPQIHRLTEPGSLVYVMYNDALIMGITLSDVSLNNIVRVIYSIDGGNIFEIDDFSTNDVFTAKELITRSTNINL", "text": "SIMILARITY: Belongs to the poxviruses L3 family."}
+{"protein": "AVGGIPTDEEQATGLEEIVMVAAQXGADXYDVM", "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; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the cytochrome c oxidase subunit 5B family."}
+{"protein": "MPSASLLKAAAVNALKMSQVGRGLCLPGMNRYMPVMHGAQGCTSFGLVLLVRDFREAIPLQTTAMNEVSSTLGGMENIAKAVLNIRLRAKRDLIAICSTGLTETKGDDVNAYLRLTAEAPRPGRYLTGLCPHALTTGASQDGWAKALEALAGRWESRGRADARQADNLLAGCHLTPADIEEMRDIVQSFGLEPIVLPDVSSWLDGHLPDNFSPTSMGGTTLAEMRALGASIVCIANRRTEAPPTAQAVQELCGVPYVVFDRLTGLQANDRFLAYLEYVSGQPIPARYRRQRSQLQDAMLGWPLLLRPGVKVAIGAEPEPVAVTLRHGWPRWAAELGGCRDHHDLAGARWRSPQPGWWIGANLEAPGTKGARARACAGSCWLTHSHGGQAAERLHIPFHRAGLPPCSTGLGAGHCLSVGYRGTRGLIFEIGQPVAGRGPCTYPG", "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": "MQRVAVMVLAVLLALFSAPPAWAIDPPVIDAGAVPPDETGPDQPTEQRKICATPTVMPNSNFADRPWANDYLRIQEAQKFATGAGVTVAVIDTGVNGSPRVPAEPGGDFVDAAGNGMSDCDAHGTMTAAIIGGRPSPTDGFVGMAPDVRLLSLRQTSVAFQPKGARQDPNDPNTTQTAGSIRSLARSVVHAANLGAQVINISEAACYKVTRRIDETSLGAAINYAVNVKGAVIVVAAGNTGQDCSQNPPPDPSVPSDPRGWREVQTIVSPAWYDPLVLTVGSIGQNGQPSNFSMSGPWVGAAAPGENLTSLGYDGQPVNATPGEDGPVPLNGTSFSAAYVSGLAALVKQRFPDLTPAQIINRITATARHPGGGVDNYVGAGVIDPVAALTWEIPDGPEKAPFRVKEVPPPVYIPPPDRGPITAVVIAGATLAFALGIGALARRALRRKQ", "text": "FUNCTION: May play a dual role in regulation of ESX-1 secretion and virulence. Acts as a protease that cleaves EspB. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Cell wall-associated. SIMILARITY: Belongs to the peptidase S8 family."}
+{"protein": "MTMSTNNCESMTSYFTNSYMGADMHHGHYPGNGVTDLDAQQMHHYSQNPNHQGNMPYPRFPPYDRMPYYNGQGMDQQQQQHQGYSRPDSPSSQVGGVMPQAQTNGLPTGGQLVAQQQQQQPQQQSQTPQQQQAQQPQQQQQQLQQLPQVTQQVTHPQQQQQQQQQQQQPVVYASCKLQAAVGVGLGMVPEGGSPPLVDQMTGHHMNAQMSLPHHMGHPQAQLGYTDVGVPDVTEVHQNHHNMGMYGQQQTGVPPVGAPPQAMMHQGQGPPQMHQGHLPGQHTPPSQNPNSQSSGMPSPLYPWMRSQFGKCQERKRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKENKTKGEPGSGGEGDEITPPNSPQ", "text": "FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that regulates segmental identity in the mesothorax. Provides cells with specific positional identities on the anterior-posterior axis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family."}
+{"protein": "MDMISGSTAATSTPHNNQQAVMLSSPIIKEEARDPKQTRAMPQIGGSGERKPRPQLPEALKCPRCDSNNTKFCYYNNYSMSQPRYFCKACRRYWTHGGTLRNVPIGGGCRKNKHASRFVLGSHTSSSSSATYAPLSPSTNASSSNMSINKHMMMVPNMTMPTPTTMGLFPNVLPTLMPTGGGGGFDFTMDNQHRSLSFTPMSLPSQGPVPMLAAGGSEATPSFLEMLRGGIFHGSSSYNTSLTMSGGNNGMDKPFSLPSYGAMCTNGLSGSTTNDARQLVGPQQDNKAIMKSSNNNNGVSLLNLYWNKHNNNNNNNNNNNNNNNNKGQ", "text": "FUNCTION: Transcription factor that binds specifically to a 5'-AA[AG]G- 3' consensus core sequence. May enhance the DNA binding of the bZIP transcription factor Opaque-2 to O2 binding site elements. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MASFQDRAQHTIAQLDKELSKYPVLNNLERQTSVPKVYVILGLGGIYTFLVFFNIAGQLLVNLAGFILPTYYSLDALFSAGKADDTQWLTYWVVYAFFTVVESAISAPYWFPFYYIFKFALVLWLALPQTNGAQIVFKSLVQPLVGRYFTGGSTSANLRAQADAATKSQ", "text": "FUNCTION: Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the vacuole. Induces high curvature in membranes and causes membrane tubule formation. Involved in membrane/vesicle trafficking. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DP1 family."}
+{"protein": "MSPNPTSEFKQIIEQQSEKILNPIERTKVTQDLSENVILTTVDDLYNWARLSSLWPMLYGTACCFIEFAALIGSRFDFDRFGLVPRSSPRQADLIITAGTITMKMAPALVRLYEEMPEPKYVIAMGACTITGGMFSSDSTTAVRGVDKLIPVDVYIPGCPPRPEAIIDAIIKLRKKVANESIQERGTVLQQTNRYYSTTHKMQATEPILTGKYLQSATRQAPPKELLEATGMPVPPALLTTKQKEEI", "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": "MNTNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKELGGCDKVKWDTFVSQEKKTLPPLNGGQSRRSFLRNVMPENSNFPYRRYDRLPPIHQFSIESDTDLSETAELIEEYEVFDPTRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVDNKLFPNKEAAAGSSDLDPSMILDTGEIIDTGSDYEDQGDDQLNVFGEDTMGGFMEDLRKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLIDGYPREVKQGEEFGRRIGDPQLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDVFLQLCTAIDSIF", "text": "FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylate kinase family."}
+{"protein": "MRKHTDKPQLASKLVLRRVAIDTYRENVAYLHRDCAVYRAEGFQALSKVEVRANGRHILATLNVVDDPNIVACNELGLSEDAFAQMAVIDGQPASVSQAEPPQSIGALRRKLAGERLGREDFLGIVRDIAELHYSKIELSAFVVATNRDELDREEVYFLTEAMVASGRTLNWHEPLVVDKHCIGGIPGNRSSMLVVPIVAAHGLLCPKTSSRAITSPAGTADTMEVLAKVELPVDQLADIVRTHRGCLAWGGAAHLSPADDVLISVERPLAIDSPGQMVASILSKKIAAGSTHLVLDIPIGPSAKVRSMPEAQRLRRLFEYVAGRMHLSLDVVVTDGRQPIGNGIGPVLEARDVMRVLENDPRAPNDLRQKSLRLAGRLIEFDPDVRGGDGFAIARDILDSGRALAKMNAIIAAQGAKPFDHNHPQLGALTFDICASESGVVTGIDNLQVARIARLAGAPKVIGAGIDLFHKLGEAVTSGEVLYRVHAGFQSDLDFARQACAKSTGYTLGRAEDVPHVFTEF", "text": "SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily."}
+{"protein": "MSSNLLPTLNSGGKVKDGSTKEDRPYKIFFRDLFLVKENEMAAKETEKFMNRNMKVYQKTTFSSRMKSHSYLSQLAFYPKRSGRSFEKFGPGPAPIPRLIEGSDTKRTVHEFINDQRDRFLLEYALSTKRNTIKKFEKDIAMRERQLKKAEKKLQDDALAFEEFLRENDQRSVDALKMAAQETINKLQMTAELKKASMEVQAVKSEIAKTEFLLREYMKYGFFLLQMSPKHWQIQQALKRAQASKSKANIILPKILAKLSLHSSNKEGILEESGRTAVLSEDASQGRDSQGKPSRSLTRTPEKKKSNLAESFGSEDSLEFLLDDEMDVDLEPALYFKEPEELLQVLRELEEQNLTLFQYSQDVDENLEEVNKREKVIQDKTNSNIEFLLEQEKMLKANCVREEEKAAELQLKSKLFSFGEFNSDAQEILIDSLSKKITQVYKVCIGDAEDDGLNPIQKLVKVESRLVELCDLIESIPKENVEAIERMKQKEWRQKFRDEKMKEKQRHQQERLKAALEKAVAQPKKKLGRRLVFHSKPPSGNKQQLPLVNETKTKSQEEEYFFT", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome."}
+{"protein": "MKVKCLLAVFLIVLIAAEHCQALFFLPSLIGGLISAIKGRRKRELGTQFRPQQKNFMRREIDLERLFAEMPDY", "text": "FUNCTION: Cationic host defense peptide that have antibacterial activity by breaking membranes. Is more effective on Gram-positive than on Gram-negative bacteria. 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": "MAEKAKAEGNNFVKKLLSSNLTWSIVAFILLVIICTIFQHDFLALSWNSNTGGLAGPLITMLQESARYLMIATGMTLVISTAGIDLSVGSVMAVAGAAAMQTLSNGMNVWLSILIALAVGLAIGCVNGALVSFLGLQPFITTLIMMLAGRGMAKVITSGENTDASAVAGNEPLKWFANGFILGIPANFVIAVIIVILVGLLCRKTAMGMMIEAVGINQEASRMTGIKPKKILFLVYAISGFLAAIAGLFATASVMRVDVVKTGQDLEMYAILAVVIGGTSLLGGKFSLAGSAVGAVIIAMIRKTIITLGVNAEATPAFFAVVVIVICVMQAPKIHNLSANMKRKRALKAQAKAVAA", "text": "FUNCTION: Part of the high-affinity ABC transporter complex FruEKFG involved in fructose uptake. Can also transport ribose and xylose, with lower affinity. 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."}
+{"protein": "LQVDYLVLEVA", "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": "MDGQSEEVDALVQKITGLHAAIAKLPSLSPSPDVDALFTDLVTACVPPSPVDVTKLAPEAQAMREGLIRLCSEAEGKLEAHYSDMLAAFDNPLDHLGVFPYYSNYINLSKLEYELLARYVPGRHRPARVAFIGSGPLPFSSYVLAARHLPDTVFDNYDLCGAANDRATRLFRADKDVGARMSFHTADVADLTDELATYDVVFLAALVGMAAEDKAKVIAHLGAHMADGAALVARHGARGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAQKSNDVHEYGLGSGRGGRYARGTVVPVVSPPCRFGEMVADVTQKREEFANAEVAF", "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": "MNTSELSIAEEIDYEALPSHAPLHSQLLAGAFAGIMEHSLMFPIDALKTRVQAAGLNKAASTGMISQISKISTMEGSMALWKGVQSVILGAGPAHAVYFGTYEFCKARLISPEDMQTHQPMKTALSGTIATIAADALMNPFDTVKQRLQLDTNLRVWNVTKQIYQNEGFAAFYYSYPTTLAMNIPFAAFNFMIYESASKFFNPQNSYNPLIHCLCGGISGATCAALTTPLDCIKTVLQVRGSETVSIEIMKDANTFGRASRAILEVHGWKGFWRGLKPRIVANIPATAISWTAYECAKHFLMKN", "text": "FUNCTION: MRS4 suppresses a mitochondrial splice defect in the first intron of the COB gene. It may act as a carrier, exerting its suppressor activity via modulation of solute concentrations in the mitochondrion (possibly of cations). Not essential. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MAAAAASNGSGMEVDVAAFPTVMAQGVTGSVTVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRNIEVMNSFELLSQINEEKITINKEYYYTKEEQFKQVFKDMEFLGWYTTGGTPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVYESVIDIVNGEATMLLAELSYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVRLILEYVRAAEAGEVPFNHEILREASALCHCLPVLSTDKFKMDFYDQCNDVGLMSYLGTITKTCNTMNQFVNKFNILYDRQGIGRRMRGLFF", "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": "MNEQSQAKSPDTLRAMVAGTLANFQHPTLKHNLTTLKALHHVAWMDDTLHVELVMPFVWNSAFEVLKEQCSADLLRITGAKAIDWKLSYNIATLKRVKNQPGINGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGVLDADIYGPSIPTMLGAEDQRPTSPDGTHMAPIMSHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAQKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESEFTAIYRELADRVAAQLYWQGEVIPGEIAFRAV", "text": "FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins (PubMed:18616280, PubMed:19001370). Can hydrolyze ATP (PubMed:12486045, PubMed:19001370). Both activities are required for function in vivo, but the ability to hydrolyze ATP is not necessary for Fe-S cluster transfer (PubMed:19001370). SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family."}
+{"protein": "MQTVLKYLLLIMCGSFCASEELQNQTNVPAIFFSYKLTPGILKYQEDYDRAVTLPRDTFIEAAEKFLGVCNADTYVFINQPGLRKLDFLEFETEFVSLQRYIRRSSTAIKFEKVDLLPQDLYYDLAEFVKEYCNVDQVLNLRGNNTEDFQPFIDSEKRVIIIEYPKLPEDTNERKEAFRHYDKYLRTILAQIPSPEQNVIYTSLNPGTTLAHESIIPIQIFPDIFDIKSRVGEVEQNNRVLDVPRLSFNDYTPRFSEPPSEYVSIFDSQLIENNRGLLQLIFTILVGYILIQFFFTKKTIVDEKITNKKDNVKQTSPQLLKKVQEIQKKPSQQVS", "text": "FUNCTION: Required for normal beta-1,6-glucan synthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the BIG1 family."}
+{"protein": "MKRHRISIPYVTDQVLRNTSDVVDPNDTVDQLISDDVVNPKQDLKEFLDSRELNYRTRASLASSYDDDDWADSIVDLSQRPHNKMEESSLHDDKAIKQATQLNTDYNQLRSPNANSIGGQSVIKDVSSERKPPVNQIPEDQQIYPSQMYPLLEVPESYHSLIPKLQFFFKYYGLYEDSDYVVDKDNQGYYFYPTKKWTTRDQKELMDNISKGVDHDDNLLDLEEKTSDNLFEENLNVHQLVDFVTKGFYVEKRNIKGKYYFDINNPSLNINKIANVDCQDKILSAKEKIDMIFKASGIYRAMKLKAKW", "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. SUBCELLULAR LOCATION: Virion Host cytoplasm."}
+{"protein": "MNYFTLFDLPRKFNIDKKLLSQNFYKLQLKFHPDLFINDSESKKKIILEKSIQINKGYKTLKNFLNRAIYFLCLNGYEVKKETLLLKNNDFLIRYFSLYEQLDNLKENNFNKKELNNLEQIIQKKIIYCKKKIELEFEKTRYKKVIKIISELLFFEKIKDVLKKEYNIYLSQIN", "text": "FUNCTION: Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA (By similarity). SIMILARITY: Belongs to the HscB family."}
+{"protein": "MAFSGKYEFESEKNYDEFMKRLGLPGDVIERGRNFKIITEVQQDGQDFTWSQSYSGGNIMSNKFTIGKECEMQTMGGKKFKATVKMEGGKVVAEFPNYHQTSEVVGDKLVEISTIGDVTYERVSKRLA", "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 (PubMed:23251388). 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": "MADPARRDPRGRAPELPGDLSSQEEEEEESDSDAGASSLGSCSSASSDTDLEPEWLDSVQRNGELFYLELSEDEEESLLPETQTVNHVNHVRFSEKEVIIEEDDSRERKKYEPKLRRFTKILKSKSLLPKRHHKKKSSNTGPVSILKHQSTQRTGVTVQQRYKDVTVYINPKKLTAIKAREQAKLLEVLVGVIHQTKWSWKRSGKQADGERLVVHGLVPGGSAMKSGQVLVGDVLVAVNDVDVTSENIERVLSCIPGPMQVKLTFENAYAVKKETAQPKKKKAQSSTNDLVKLLCGSEADATQHSTLSIPHITMYLTLQLQSEVAREEQEMLYHYPVSEASQKLKSVRGIFLTLCDMLESVTGTQVTSSSLHVNGKQIHVAYLKESDKLLLIGLPAEEVPLPQLRNMTEDVAQTLKFMYGSLDSAFCQVENTPRLDHFFSLFFERALRPGKLHLSASPSAQQYDAASAVLLDNLPGVRWLLLPQELKVELDTALSDLEAADFQELSEDYYDMRRLYTILGSSLFYKGYMVCSHLPKDDVVEIAAYCRQYCLLPLAAQQRIGQLIIWREVFPQHHLQPATDSDPEAFQEPEGRYFLLIVGLRHYMLCVLLEAGGCASKATGNPGPDCIYVDQARATLHQLEGVESRIEEQLAATPGPCLSCADWFLAAPREKADSLTTSPILGRLQGPSKTAASPTCRRTFFSDYSFKARKPSPSRIGGGREPGEGEENVGLSPHTTPDTVRKQRESEGSDDNVALLKLARKKSTLPNPFHLGTSKKELSEKELEVYNMMKLTSGPENTLFHYVALETVQGIFITPTHEEVAQLGGSVHSQLIKNFHRCCLTIRAVFQQTLKVEKKKALSDGDHLESANSVSSLSPVKEHGVLFECSPENWTDQKKTPPVMSYWVVGRLFLNPKPQELYVCFHDSVSEIAIEMAFRLFFGLTL", "text": "FUNCTION: Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Plays a key role in definition of cell polarity via its role in ciliogenesis but not via conversion extension. Has an indirect effect on hedgehog signaling (By similarity). Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell surface Cytoplasm, cytoskeleton, cilium basal body Note=Enriched at the apical surface in ciliated cells. SIMILARITY: Belongs to the inturned family."}
+{"protein": "MPQYKLTYFDIRGLGEGARLIFHQAGVKFEDNRLKREDWPALKPKTPFGQLPLLEVDGEVLAQSAAIYRYLGRQFGLAGKTPMEEAQVDSIFDQFKDFMAELRPCFRVLAGFEEGDKEKVLKEVAVPARDKHLPLLEKFLAKSGSEYMVGKSVTWADLVITDSLASWESLIPDFLSGHLQLKKYIEHVRELPNIKKWIAERPKTPY", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can also function as a GSH peroxidase. SIMILARITY: Belongs to the GST superfamily. Sigma family."}
+{"protein": "MDTSGPAAFVNGEILKMFVGRRVRTVVQAQREEGGLLIGQSTDGHQLTIKGASGAPMSHYVEIIGIAEPNQAIRAEVCTDFGENFDPAPFNGLCKLANGQMKDLFL", "text": "FUNCTION: As part of the replication protein A (RPA/RP-A), a single- stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the replication factor A protein 3 family."}
+{"protein": "MQRSFYEILGIESDASNIEIKRAYRAMLLETHPDKSGLNYNSNGNNTSSHSVTDIQEAYQTLIDQDLRKKYDEELAESFKKLGFHNAGDGLDLFSLDLFDYSGDEQSFSMNCPRCQITDGFQLTEDALEEHAIDYEGGGYFVLVQCSACSLWLKVLFDVMEE", "text": "FUNCTION: Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DPH4 family."}
+{"protein": "MRTFTLIAILTCAVLVIFHAAAAEELEAQDVIETEALATLDEERLFECSFSCDIKKNGKPCKGSGEKKCSGGWRCKMNFCVKV", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 03 (juruin) subfamily."}
+{"protein": "MAPKKVLLALTSYNDVFYSDGAKTGVFVVEALHPFNTFRKEGFEVDFVSETGKFGWDEHSLAKDFLNGQDETDFKNKDSDFNKTLAKIKTPKEVNADDYQIFFASAGHGTLFDYPKAKDLQDIASEIYANGGVVAAVCHGPAIFDGLTDKKTGRPLIEGKSITGFTDVGETILGVDSILKAKNLATVEDVAKKYGAKYLAPVGPWDDYSITDGRLVTGVNPASAHSTAVRSIDALKN", "text": "FUNCTION: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals (PubMed:24302734). Involved in protection against reactive oxygen species (ROS) (PubMed:17395014). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation (PubMed:24706893). SUBCELLULAR LOCATION: Cytoplasm, P-body Note=Present in processing bodies (P-bodies) and stress granule (SG) foci upon glucose starvation and heat shock. SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily."}
+{"protein": "MNAPESVQAKPRKRYDAGVMKYKEMGYWDGDYEPKDTDLLALFRITPQDGVDPVEAAAAVAGESSTATWTVVWTDRLTACDMYRAKAYRVDPVPNNPEQFFCYVAYDLSLFEEGSIANLTASIIGNVFSFKPIKAARLEDMRFPVAYVKTFAGPSTGIIVERERLDKFGRPLLGATTKPKLGLSGRNYGRVVYEGLKGGLDFMKDDENINSQPFMHWRDRFLFVMDAVNKASAATGEVKGSYLNVTAGTMEEMYRRAEFAKSLGSVIIMIDLIVGWTCIQSMSNWCRQNDMILHLHRAGHGTYTRQKNHGVSFRVIAKWLRLAGVDHMHTGTAVGKLEGDPLTVQGYYNVCRDAYTHADLSRGLFFDQDWASLRKVMPVASGGIHAGQMHQLISLFGDDVVLQFGGGTIGHPQGIQAGATANRVALEAMVLARNEGRDILNEGPEILRDAARWCGPLRAALDTWGDISFNYTPTDTSDFAPTASVA", "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 (By similarity). SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily."}
+{"protein": "MAFKLNIGLLALSLSLSLVHLDGVRAGMATRYWDCCLASASWEGKAPVYAPVDACKADGVTLIDSKKDPSGQSGCNGGNKFMCSCMQPFDDETDPTLAFGFGAFTTGQESDTDCACFYAEFEHDAQGKAMKRNKLIFQVTNVGGDVQSQNFDFQIPGGGLGAFPKGCPAQWGVEASLWGDQYGGVKSATECSKLPKPLQEGCKWRFSEWGDNPVLKGSPKRVKCPKSLIDRSGCQRKDDNTISPYSGKVDSANTAAPAQYKRDRSVCLAGGKKGKSAAGGVDGSGDASGGADASGAGGAAEGSQGQPEGYGQPSGGNDQGSSNGDATTGAGSGSGSDSGSTANGSGSGAPTSGSDGSAVAPPSGGSNPGAAQGGQGGAQPGPSGGHKKCHKKH", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family."}
+{"protein": "MICRFIDTHCHFDFPPFSGDEEASLQRAAQAGVGKIIVPATEAENFARVLALAENYQPLYAALGLHPGMLEKHSDVSLEQLQQALERRPAKVVAVGEIGLDLFGDDPQFERQQWLLDEQLKLAKRYDLPVILHSRRTHDKLAMHLKRHDLPRTGVVHGFSGSLQQAERFVQLGYKIGVGGTITYPRASKTRDVIAKLPLASLLLETDAPDMPLNGFQGQPNRPEQAARVFAVLCELRREPADEIAQALLNNTYTLFNVP", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family."}
+{"protein": "MYSNHNLNSDDCCFDWNEEKAAELQRTGVSFDRSLTPQSLRTSTRRLSEENKQQSGTMHIDTSPSVVSDIISSRRDRSQDFFGPHSSSPIAPSERQRADQRSRLESMRLTRRRDKMTKVRGGLEKMEEMIMQGEHLREMQRLKQEAQKNALPSDMAEYMEWQNNEDLEDDELLAFIEKQETYKNELEHFLNNANKNVYENNSYPNSHT", "text": "FUNCTION: Involved in regulation of Ty1 transposition. Inhibits Ty1 transposition at a post-transcriptional and pre-integrational stage of the Ty1 retrotransposition cycle (By similarity). FUNCTION: Involved in regulation of Ty1 transposition. Inhibits Ty1 transposition at a post-transcriptional and pre-integrational stage of the Ty1 retrotransposition cycle. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MYQQHIFYFITGGIFILWILAHSFFVKIIYLWASGCLLWYCLETRTFENKNNLGTSEPFLVNPAIFQKRARQLALSKLLLRQPLYPGIPEISEEIESIISHFMQKYIKVWSYQIIPEPTISNSIESHLRKCLMVLLSRVDEIDLADVLVKTVLPLITKHLRLFVEAEQLVVGNKAVSFTDHSELSREVAAKYDHGRLHEAVLLSGNPMVAQKRYLRNWTTQVLSIILPNYYETSPLVLSLVTEVIINTTLLPLVSYISDPDFFNYLIIQASGSIIQRRRKIRRLKRAIRKQSNHFQVGARRLRLKDSQHSFEQYIHEIKKISNISDARRLRSELMVQRRQLEQTEAFDFEFKQYRERLQIAIITAEKRISLLSGTPFQHKEAVLFEQVQSLLQILSDSAAVSCFLEFMERKNRSRYLHFWLVVEGLKESQDDPLNAHMIAPFSDIVSDHTDFTAIVKSYFESVDNPLDIPKPLTNTINKFVNQSKDNLNPDLWVEARNAMLMAQEHVFDIMQNSDYSEFVNSEIYYRFLAQDVVSDHKSTNSSATFSRLEELGENIPAISKQPSYLSISSSSKSINSSPSPSIQLSVSSSISRDKNLSPLDLELDDPTYSDEEEVLFAPPGDLQLSESIDELNNNIEELKAQLNAINTLIKKAELVADQKQLKSLTKNHQEIEKAIHRKERQRDQYMSQEEDSKLFNRSRVSIDSFKISKEENTPDFAVYTIRIERLENGHVRSGWMVARRYREFAELHKQLKQTYPGVRSLKFPQKSIITSLNKNVLEYRRGALEEYLQSLFRMPEVCDSKMLRMFLSQQNITAPQMFNPKEVGKKWKQLLEVLGFEVNNSFNASNVNTNSSFSGPISEFLVELFSPNDDAKQQWLPKKTYISILEQLFGGALEKRIRLQLFQLFTPEKIYRKLREFRRGLEGKSNHDHSKDRRHSRARKPAYADRNQLKAEAGILLASMFPGYTPDIAVKRIFRILQNQSLNAHVIYTLLDEILLALKKHARSTNKAT", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "MALRCINNLEIFLRRCTAPTLHRCCVASSRTAHTASSSKGSGGDNSKDQENNGQNKSGYRRFGWRSVFQFCVPFSLGALVSAVLIEGHRDELTPTISARSLKGRRNEFNFIADVVAGCGDSVVYIEIKDTRHFDYFSGQPITASNGSGFVIEQNGLILTNAHVVINKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIHVSGLPVMKLGKSSTLRSGEWVVALGSPLALSNTVTAGVISATQRASQELGLRNRDINYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVTAGISFAIPIDYVKVFLERAAERRKKGSAHKTGYPVKRYMGITMLTLTPDILFELKSRSQNMPNNLMHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALAEGRKDLEIVILRGVKQMHVKITPEDP", "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": "MVRIQRRKLLASCLCVTATVFLLVTLQVMVELGKFERKEFKSSSLQDGHTKMEEAPTHLNSFLKKEGLTFNRKRKWELDSYPIMLWWSPLTGETGRLGQCGADACFFTINRTYLHHHMTKAFLFYGTDFNIDSLPLPRKAHHDWAVFHEESPKNNYKLFHKPVITLFNYTATFSRHSHLPLTTQYLESIEVLKSLRYLVPLQSKNKLRKRLAPLVYVQSDCDPPSDRDSYVRELMTYIEVDSYGECLRNKDLPQQLKNPASMDADGFYRIIAQYKFILAFENAVCDDYITEKFWRPLKLGVVPVYYGSPSITDWLPSNKSAILVSEFSHPRELASYIRRLDSDDRLYEAYVEWKLKGEISNQRLLTALRERKWGVQDVNQDNYIDAFECMVCTKVWANIRLQEKGLPPKRWEAEDTHLSCPEPTVFAFSPLRTPPLSSLREMWISSFEQSKKEAQALRWLVDRNQNFSSQEFWGLVFKD", "text": "FUNCTION: [Isoform 1]: Catalyzes the transfer of fucosyl moiety from GDP-beta-L-fucose to the innermost GlcNAc residue in biantennary N- glycan acceptors. Does not fucosylate GlcNAc within type 2 lactosamine unit. FUNCTION: [Isoform 4]: Catalyzes the transfer of fucosyl moiety from GDP-beta-L-fucose to the innermost GlcNAc residue in biantennary N- glycan acceptors. Does not fucosylate GlcNAc within type 2 lactosamine unit. 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 (PubMed:19088067). Involved in biosynthesis of Lewis X-carrying biantennary N-glycans that regulate neuron stem cell self-renewal during brain development (By similarity). FUNCTION: [Isoform 5]: Catalyzes the transfer of fucosyl moiety from GDP-beta-L-fucose to the innermost GlcNAc residue in biantennary N- glycan acceptors. Does not fucosylate GlcNAc within type 2 lactosamine unit. SUBCELLULAR LOCATION: [Isoform 5]: Endoplasmic reticulum membrane; Single-pass type II membrane protein Golgi apparatus membrane; Single-pass type II membrane protein. SUBCELLULAR LOCATION: [Isoform 4]: Golgi apparatus Lysosome. SUBCELLULAR LOCATION: [Isoform 1]: 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": "MASWNSIPLEISYEIVGWIAFASWSISFYPQLILNFRRRSVVGLNFDFVMLNLTKHSSYMIYNVCLYFSPVIQKQYFDTYGDKEMIPVAANDVAFSIHAVVMTAVTLFQIFIYERGPQKVSRLAIGIVVVVWGFAAICFFIALPTHSWLWLISIFNSIQVFMTCVKYIPQAKMNFTRKSTVGWSIGNILLDFTGGLANYLQMVIQSIDQNSWKNFYGNMGKTLLSLISIFFDILFMFQHYVLYPEKKVSKSPETGEESNEPLIDSSHEHV", "text": "FUNCTION: Thought to transport cystine out of lysosomes. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cystinosin (TC 2.A.43.1) family."}
+{"protein": "MGLCHGKPIEQQSKNLPISNEIEETPKNSSQKAKSSGFPFYSPSPLPSLFKTSPAVSSSSVSSTPLRIFKRPFPPPSPAKHIRALLARRHGSVKPNEASIPEGSECEVGLDKKFGFSKQFASHYEIDGEVGRGHFGYTCSAKGKKGSLKGQDVAVKVIPKSKMTTAIAIEDVRREVKILRALTGHKNLVQFYDAFEDDENVYIVMELCQGGELLDKILQRGGKYSEVDAKKVMIQILSVVAYCHLQGVVHRDLKPENFLFTTKDESSPLKAIDFGLSDYVRPDERLNDIVGSAYYVAPEVLHRTYGTEADMWSIGVIAYILLCGSRPFWARSESGIFRAVLKAEPNFEEAPWPSLSPDAVDFVKRLLNKDYRKRLTAAQALCHPWLVGSHELKIPSDMIIYKLVKVYIMSSSLRKSALAALAKTLTVPQLTYLQEQFNLLGPSKNGYISMQNYKTAILKSSTEATKDSRVLDFVHMISCLQYKKLDFEEFCASALSVYQLEAMETWEQHARRAYELYEKDGNRVIMIEELATELGLGPSVPVHVVLQDWIRHSDGKLSFLGFVRLLHGVSSRTLQKA", "text": "FUNCTION: May play a role in signal transduction pathways that involve calcium as a second messenger. SUBCELLULAR LOCATION: Membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily."}
+{"protein": "MAAELVEAKNMVMSFRVSDLQMLLGFVGRSKSGLKHELVTRALQLVQFDCSPELFKKIKELYETRYAKKNSEPAPQPHRPLDPLTMHSTYDRAGAVPRTPLAGPNIDYPVLYGKYLNGLGRLPAKTLKPEVRLVKLPFFNMLDELLKPTELVPQNNEKLQESPCIFALTPRQVELIRNSRELQPGVKAVQVVLRICYSDTSCPQEDQYPPNIAVKVNHSYCSVPGYYPSNKPGVEPKRPCRPINLTHLMYLSSATNRITVTWGNYGKSYSVALYLVRQLTSSELLQRLKTIGVKHPELCKALVKEKLRLDPDSEIATTGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWMCPVCDKPAPYDQLIIDGLLSKILSECEDADEIEYLVDGSWCPIRAEKERSCSPQGAILVLGPSDANGLLPAPSVNGSGALGSTGGGGPVGSMENGKPGADVVDLTLDSSSSSEDEEEEEEEEEDEDEEGPRPKRRCPFQKGLVPAC", "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 (PubMed:12511558, PubMed:12631292, PubMed:12727872, PubMed:15831457, PubMed:15976810, PubMed:22508508, PubMed:32832608). Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168 (PubMed:12511558, PubMed:12631292, PubMed:12727872, PubMed:15831457, PubMed:15976810, PubMed:22508508). Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway (PubMed:11388671). Involved in gene silencing (PubMed:11248056). In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations (PubMed:12727872, PubMed:15831457). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (PubMed:21965678). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) (By similarity). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:32832608). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin (PubMed:35013556). SUBCELLULAR LOCATION: Nucleus, PML body Note=Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies. SIMILARITY: Belongs to the PIAS family."}
+{"protein": "MGHETMTPATTTLVFTYGTLKRGFSNHVLMQDLIRSGDASFKGVYQTLDKYPLVCGPYRVPFLLNKPGSGYHVNGELYAVSPRGLSRLDELEGISRGHYIRQPIRLAAAEEEEEEEGDLETEAPSSCVVEAYYAHKSYEEELWRRNRGRSFGAYTENEARGYVKRNDRPQHLSFLDHIRIFVSSPCD", "text": "FUNCTION: Putative gamma-glutamylcyclotransferase. SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family."}
+{"protein": "MAQASGLMNGKRGVIMGVANNRSIAWGIAKALAEAGAEIALTWQGDALKKRVEPLAQELGAFMAGHCDVTDLATIDAVFSALEEKWGKIDFVVHAIAFSDKDELTGRYLDTSRDNFARTMDISVYSFTAVAARADRVMNDGGSILTLTYYGAEKVMPHYNVMGVAKAALEASVRYLAVDLGNRGIRVNAISAGPIKTLAASGIGDFRYILKWNEYNAPLKRTVSIEEVGNSALYLLSDLSSGVTGEVHHVDSGYHTVGMKAVDAPDISVLKD", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily."}
+{"protein": "DDVALYFSGQEWEILEKWQKQMYKQEMKTNYQTLDSLGYAFSKPDLITWMEQGRMLFISEQGCLDKTRRTTSPPTDEQLDMKDTGKLPCFDHEGTLRTKEEDCRLNGPQKQDLGAALPGKERKILSARRDTFQSPSLQETEIPNKKVSITASDPDKKDLRHKPRETPGRLEIPTGPRCYSCYVCRKVFQVRRDLLKHKRSHSKSQLRRYPKYRNTSRGKSELRRTQRLLCQKKRFQCSECEKSYFLKGSLVTHQVVHTGQRPYPCPECDKTFRYRANLKKHLCLHRGERPFCCGECGRAFVQQCELTEHLRLHSGEKPFQCPQCDRCFRLKRGMKVHLSQHSGKRPFHCPECGRSFSRKAALKTHQRTHSEEKPFSCDECGRKFIYKIKLDEHIRVHTGEKPFSCPECNKSFRLKRSLKAHGLQHSGKRPFQCPECSRGFFWRNAMRAHQRLHSEQKPFPCAECGKRFTRPSKLACHTRVHDRQKEFPCGECKKTFSQQSRLTQHLKVHNTEKPFSCAECGRSFRRRAHLTEHTRLHSGEEPFQCPECDKSFSWKASMKFHQRMHRDEKPFACSECGKTYTHQSQLTEHLRLHSGEKPYQCPECQKTFRLKGNLKSHLLQHSGQKPFSCVMCGKSFTQQYRLTEHIRVHSGEKPFQCPECDKSYCIRGSLKVHLYTHSGERPFQCPECGKGFLQKRSLKAHLCLHSGERPFSCDECGRSFTYVGALKTHIAVHAKEKPSSL", "text": "FUNCTION: Acts as a transcriptional repressor. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Predominantly expressed in the nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MMSDSSSEIDVVKTRIPTYDEDDNTILYAYETKPEFVNKEPNIVSDASCNTEEQLRTVNDVLLHCQVIYDALQNLDKKTDVIRRKVSKIQRFYARSLWTNRKRSGYKKHSYRPVKKLKLQKMKKNEVYETFSYPQSYSPTLPVSRRENNSPSNLPRPPFCMEEYQRAEPEEDPILSRTPSPVHPSDFCEHNYQSYYASDGAMYGSSSGLCLGNPRADSIHNTYSTDHASAVSPSVTRSPVGNDGCIAEGNITKHPSTWSVEAVVLFLKQTDPVALCPLVDLFRSHEVDGKALLLLTSDVLLKHFGVKLGTAVKLCYYIDRLKQGKCFEN", "text": "FUNCTION: Putative 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. May be involved in spermatogenesis during sexual maturation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SCM family."}
+{"protein": "MSLSSPTSACSSSRCYSSGLSFPIGFGSNPINVGLVCYPKRYSIAARKFVVACSSSSSDPLLVKAAKGQAISRPPAWMMRQAGRYMAVYQKLAKKHPSFRERSENTDLIVEISLQPWQAFRPDGVIIFSDILTPLPAFGVPFDIEEVKGPVIQSPIRTEEDMKRLHPIDFEKLQFVGDSLKILRREVGEHAAVLGFVGAPWTIATYIVEGGTTRTYTVIKNMCHTAPDVLRALLSHLTKAITEYVVYQVEHGAHCIQIFDSWGGQLTPEMWERWSKPYIEEIIHAVKKRCPDTPIVFYINGNGGLLERMKGTGADVIGLDWTVDMADGRRRLGSEVSVQGNVDPAYLFSPLPALTEEIERVVKCAGPKGHILNLGHGVLVGTPEEAVAHFFETARNLDYQTLFQNHVPAEKAEPELVV", "text": "FUNCTION: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family."}
+{"protein": "MATVYDVPADLLIKRVAERLKDMVAPPEWAKYVKTGVHKERSPEQDDWWYLRLASIFRRVYIDGPVGIERLRTFYGGRKRRGSKPPKFRKGSGAIVRNALHQLEQLGFVKKTREGRVVTPMGRSFLDKVATELKSELVSEIPALEKY", "text": "FUNCTION: May be involved in maturation of the 30S ribosomal subunit. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS19 family."}
+{"protein": "MNRIRIHVLPTNRGRITPVPRSQEPLSCSFTHRPCSQPRLEGQEFCIKHILEDKNAPFKQCSYISTKNGKRCPSAAPKPEKKDGVSFCAEHARRNALALHAQMKKTNPGPVGETLLCQLSSYAKTELGSQTPESSRSEASRILDEDSWSDGEQEPITVDQTWRGDPDSEADSIDRDQEDPLKHAGVYTAEEVALIMREKLIRLQSLDIDQVKRLQHLLKEKKRRYLHNRKVEHEALGSSLLTGPEGLLARERENLKRLKCLRRYRQRYGVKALLHRQLKERRMLATDGAAQQAHTTRSSQRCLAFVDDVRCSNQSLPMTRHCLTHICQDTNRVLFKCCQGSEEVPCNKPVPVSLSEDPCCPLHFQLPPQMYKPEQVLSVPDDLEAGPMDLYLSAAELQPTESLPLEFSDDLDVVGDSMQCPPSPLLFDPSLTLEDHPVKEIAEGPVDILGQMQMAGDGCRSQGPRNSEKAPAPLSQSGIATANGKPEPTSVS", "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": "MGCFFSKKAKRKRNSEEEQPQQDGEEPKQYSWDKREKVDPKDYMFTGLKDQTVGKLPDKVAGQQFVIQECENCNIYIFDHSATITIDDCTNCRIFLGPVKGSVFFRDCKDCKCVVACQQFRTRDCRRMDVFLCCSTQPIIESSTSMKFGCFQYYYPELALQFKEAGLSILNNTWSNIHDFTPVAGETNWSLLPPDAVIQDFIPLPDSDELKCVRVSADVHKSIIPVTWGQRLKKSDESCLVVFFAGDYTTANARKMIDEMVGKGLSLIQTKEVAMKIEDAKRVFQDNITDLICLLEKGPVVALEFNGEGAVDSCQTVINNTFSGTKVFVSESKESASRDVDNFYNFADMQMGM", "text": "FUNCTION: Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as a GTPase-activating protein. May act as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Note=Detected predominantly at the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus. SIMILARITY: Belongs to the TBCC family."}
+{"protein": "MSVQGFWGLQLVPGKTYSQVVSAPFRITMASLAADAEAGKRTSVSVLVDEKEFVLCTLVPNKIEQQPLDITFVEGEEVTFSAKGQNNIHLTGNYVFQDDEDDEMGASMIDSDEEDNVEDFLKKLPPNASKEDINKALLGLEVDEEIESDEEVESDEEIESDEEIESEEEEEEPVPVSKKRPAEEVKEIASKKQKAEKKEQPKKEKSKKEEPKKEEPKKEQPKKEEPKKKEEPKKKEEPKKKEEPKKKEEPKKKEEPKKKEEPKKKEEPKKKITKLPNGLIIEDIKMGEGASCKNGQRVGMRYIGKLTNGKVFDKNVSGKPFSFLLGRGEVIKGWDLGIAGMKAGGERKLTIPAPLAYGKRGAPPDIPKNATLVFDVKLLSMK", "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": "MSKVKLTKENIVSLLTQSEDVEFEEDQNQVAFNFKTFCQENLDLIKKMSITSCLTFLKNRQSIMKVVKQSDFTFGKVTIKKNSERVEAKDMTFRRLDSMIRVKLIEETANNENLAIIKAKIASHPLVQAYGLPLDDAKSVRLAIMLGGSIPLIASVDSLEMISVVLAIYQDSQVQELGIEPTKYNTKEALGKVCTVLKSKGFTMDDAQDNKGKEYAKILSSCNPNAKGSIAMDYYSDNLEKFYEMFGVKKEAKIAGVA", "text": "FUNCTION: Encapsidates the RNA. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the tospovirus nucleocapsid protein family."}
+{"protein": "MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY", "text": "FUNCTION: Curlin is the structural subunit of the curli. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. FUNCTION: Curlin is the structural subunit of the curli. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin (By similarity). SUBCELLULAR LOCATION: Fimbrium. Note=Part of the curli surface structure. SUBCELLULAR LOCATION: Fimbrium Note=Part of the curli surface structure. SIMILARITY: Belongs to the CsgA/CsgB family."}
+{"protein": "MPIFVNTVYCKNILALSMTKKFKTIIDAIGGNIIVNSTILKKLSPYFRTHLRQKYTKNKDPVTWVCLDLDIHSLTSIVIYSYTGKVYIDSHNVVNLLRASILTSVEFIIYTCINFILRDFRKEYCVECYMMGIEYGLSNLLCHTKNFIAKHFLELEDDIIDNFDYLSMKLILESDELNVPDEDYVVDFVIKWYIKRRNKLGNLLLLIKNVIRSNYLSPRGINNVKWILDCTKIFHCDKQPRKSYKYPFIEYPMNMDQIIDIFHMCTSTHVGEVVYLIGGWMNNEIHNNAIAVNYISNNWIPIPPMNSPRLYASGIPANNKLYVVGGLPNPTSVERWFHGDAAWVNMPSLLKPRCNPAVASINNVIYVMGGHSETDTTTEYLLPNHDQWQFGPSTYYPHYKSCALVFGRRLFLVGRNAEFYCESSNTWTLIDDPIYPRDNPELIIVDNKLLLIGGFYRESYIDTIEVYNHHTYSWNIWDGK", "text": "FUNCTION: Might have a role in the suppression of host immune response. SIMILARITY: Belongs to the orthopoxvirus OPG047 family."}
+{"protein": "MSSRAHPVDGSPATDGGHVPMKPSPTRHKVGIPPKQNMFKDFMYTFKETFFHDDPLRDFKDQPKSKQFMLGLQSVFPVFDWGRNYTFKKFRGDLISGLTIASLCIPQDIGYAKLANLDPKYGLYSSFVPPLVYACMGSSRDIAIGPVAVVSLLLGTLLRAEIDPNTSPDEYLRLAFTATFFAGITEAALGFFRLGFLIDFLSHAAVVGFMGGAAITIALQQLKGFLGIKKFTKKTDIISVLESVFKAAHHGWNWQTILIGASFLTFLLTSKIIGKKSKKLFWVPAIAPLISVIVSTFFVYITRADKQGVQIVKHLDQGINPSSFHLIYFTGDNLAKGIRIGVVAGMVALTEAVAIGRTFAAMKDYQIDGNKEMVALGMMNVVGSMSSCYVATGSFSRSAVNFMAGCQTAVSNIIMSIVVLLTLLFLTPLFKYTPNAILAAIIINAVIPLIDIQAAILIFKVDKLDFIACIGAFFGVIFVSVEIGLLIAVSISFAKILLQVTRPRTAVLGNIPRTSVYRNIQQYPEATMVPGVLTIRVDSAIYFSNSNYVRERIQRWLHEEEEKVKAASLPRIQFLIIEMSPVTDIDTSGIHALEDLYKSLQKRDIQLILANPGPLVIGKLHLSHFADMLGQDNIYLTVADAVEACCPKLSNEV", "text": "FUNCTION: High-affinity H(+)/sulfate cotransporter that mediates the uptake of the environmental sulfate by plant roots. Plays a central role in the regulation of sulfate assimilation. Unable to transport molybdate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53.1) family."}
+{"protein": "MPSDLAKKKAAKKKEAAKARQRPRKGHEENGDVVTEPQVAEKNEANGRETTEVDLLTKELEDFEMKKAAARAVTGVLASHPNSTDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSDKTPLHCVMEVDTERAMLEKEAERLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQDQIAHMKNYIARFGHGSAKLARQAQSKEKTLQKMMASGLTERVVSDKTLSFYFPPCGKIPPPVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEHLKSKLVDEEPQLTKRTHNV", "text": "SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily."}
+{"protein": "MKLTCMMIVAVLFLTAWTFVTADDSRNGLKNLFPKARHEMKNPEASKLNKRYGCSNAGAFCGIHPGLCCSELCLVWCT", "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": "MDIFRVLTRGASVKKESGPKAKAADYSVINGNDENHKEDNNESQIVKELDFFRNKRIISKVEDDREKTTENDSPNKEEKSGNDDGLIKPVITNTVEASALRKSYKGNVSGIDIPLPIGSFEDLISRFSFDKRLLNNLIENGFTEPTPIQCECIPVALNNRDVLACGPTGSGKTLAFLIPLVQQIIDDKQTAGLKGLIISPTKELANQIFIECFKLSYKIFLEKKRPLQVALLSKSLGAKLKNKVVSDKKYDIIISTPLRLIDVVKNEALDLSKVKHLIFDEADKLFDKTFVEQSDDILSACREPSLRKAMFSATIPSNVEEIAQSIMMDPVRVIIGHKEAANTNIEQKLIFCGNEEGKLIAIRQLVQEGEFKPPIIIFLESITRAKALYHELMYDRINVDVIHAERTALQRDRIIERFKTGELWCLICTDVLARGIDFKGVNLVINYDVPGSSQAYVHRIGRTGRGGRSGKAITFYTKQDSVAIKPIINVMKQSGCEVSEWMDKMAKMTRKEKESIKNGKAHKERKQITTVPKMDKAKRRRQQEMIAASKRRKNEELSKKHFSK", "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. May also have a gene- specific regulatory function since it affects nuclear fusion by regulating KAR4 expression and contributes with KEM1 to ISP-1 sensitivity. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1 subfamily."}
+{"protein": "MAGSGCAWGAEPPRFLEAFGRLWQVQSRLGSGSSASVYRVRCCGTPGSPPGALKQFLPPGTTGAAASAAEYGFRKERAALEQLQGHRNIVTLYGVFTIHFSPNVPSRCLLLELLDVSVSELLVYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQNCLAQAGLQSDTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFSIPFAPHIEDLVMLPTPVLRLLNVLDDDYLENEDEYEDVVEDVKEECQKYGPVVSLLVPKENPGRGQVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFYPLSAYKRGYLYQTLL", "text": "FUNCTION: Upon serum stimulation, phosphorylates CDKN1B/p27Kip1, thus controlling CDKN1B subcellular location and cell cycle progression in G1 phase. May be involved in trafficking and/or processing of RNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MSAYALSQSHRQLTEGHLKDTDPEVDQIIKDEIDRQQHSIVLIASENFTTTAVFDALGTPMCNKYSEGYPGARYYGGNEHIDRMELLCQERALKAFGLTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLDLPHGGHLSHGYQTDSRKISAVSTYFETMPYRVDLETGLIDYDMLEKTAVLYRPKVLVAGTSAYCRLIDYKRMREIADKVGAYLVVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGAMIFFRRGVRSVNPKTGQEILYDLENPINFSVFPGHQGGPHNHTIAALATALKQANTPEFKEYQEQVLKNAKALESEFTKKGYKLVSDGTDSHMVLVSLKDKQIDGARVETVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGLGEEDFKKIVSYIDFAVNYAKEVQSQLPKDANKLKDFKNAVSGDSEKLKAVRDEIYQWAGSFPLAV", "text": "FUNCTION: Interconversion of serine and glycine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family."}
+{"protein": "MAKKAKKDGRSVEPTGNPILEVKYNDPLFSIAAHPTEPIFVSGLATGHVFCNRYDAERLEERMQAIKDEQKKKSKTSVKTTNAAWWTQVEDITNTDEIVTCWKTKRHKGSCRSVLFDPIESSVGKHLFTVGKDHVVKKANTETGKVLTKTDISKDLSSKDAVTKLCHSTTHPFLLSGTENGHVLVYDSNDLSNKFKVENVHEDAVNHILAMPSVSPYHYLTVGSTTLSHIDIRKGIVTQSDDQEDELLSMSFVPDDDRNDTVLVSHGGGIVTIWKNSKNKLMDQLSRIKVNKEASIDVMISAMDAGDDDMAASVWCGDSDGLVHRVNYKKGKVVETRLHGTADEVGFLDIDYEYRLLTAGMDSMKLWSAEGDDEEEEESEGEESEESEESDEESDESSGEESEGDDGNGSNSEESDSNDEDEVESSDDEKEKEEESTETDHKNIEAESGKQANKRQASQPKSAGENVKKQKLKQTSKLAHSHGIRRFDGL", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the WD repeat WDR55 family."}
+{"protein": "MAQEKMELDLELPAGASPAEGGGPGGGGLRRSNSAPLIHGLSDSSPVFQAEAPSARRNSTTFPSRHGLLLPASPVRMHSSRLHQIKQEEGMDLINRETVHEREVQTAMQISHSWEESFSLSDNDVEKSASPKRIDFIPVSPAPSPTRGIGKQCFSPSLQSFVSSNGLPPSPIPSPTTRFTTRRSQSPINCIRPSVLGPLKRKCEMETDYQPKRFFQGITNMLSSDVAQLSDPGVCVSSDTLDGNSSSAGSSCNSPAKVSTTTDSPVSPAQAASPFIPVDELSSK", "text": "FUNCTION: Acts as an inhibitor of serine/threonine-protein phosphatase 2A (PP2A) activity. Potentiates ubiquitin-mediated proteasomal degradation of serine/threonine-protein phosphatase 2A catalytic subunit alpha (PPP2CA) (By similarity). Inhibits PP2A-mediated dephosphorylation of WEE1, promoting ubiquitin-mediated proteolysis of WEE1, thereby releasing G2/M checkpoint (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=The CHEK1-mediated Ser-34 phosphorylated form is sequestered by 14-3-3 proteins in the cytoplasm and fails to translocate to the nucleus, where it otherwise inhibits serine/threonine-protein phosphatase 2A. SIMILARITY: Belongs to the FAM122 family."}
+{"protein": "MEEEDPTASNVITNSNSSSMRNLSPAMNTPVVSLESRINRLINANQSQSPSPSSLSRSIYSDRFIPSRSGSNFALFDLSPSPSKDGKEDGAGSYATLLRAAMFGPETPEKRDITGFSSSRNIFRFKTETHRSLNSFSPFGVDDDSPGVSHSGPVKAPRKVPRSPYKVLDAPALQDDFYLNLVDWSAQNVLAVGLGNCVYLWNACSSKVTKLCDLGAEDSVCSVGWALRGTHLAVGTSTGKVQIWDASRCKRTRTMEGHRLRVGALAWGSSVLSSGSRDKSILQRDIRCQEDHVSKLAGHKSEVCGLKWSYDNRELASGGNDNRLFVWNQHSTQPVLKYSEHTAAVKAIAWSPHVHGLLASGGGTADRCIRFWNTTTNTHLSSIDTCSQVCNLAWSKNVNELVSTHGYSQNQIIVWKYPTMSKIATLTGHTYRVLYLAVSPDGQTIVTGAGDETLRFWNVFPSPKSQNTDSEIGSSFFGRTTIR", "text": "FUNCTION: Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). Necessary and sufficient for endoreduplication and correct cell expansion. Controls meristem size by stimulating endoreduplication in the elongation zone. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family."}
+{"protein": "SGCCKHPACGKNRC", "text": "FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin inhibits rodent (alpha- 1-beta-1-delta-epsilon > alpha-1-beta-1-delta-gamma) and human (alpha- 3-beta-1) nAChRs heterologously expressed in Xenopus oocytes, but has minimal effect on human alpha-7 nAChRs. Has no effect on the frequency of responses from the giant fiber (GF)-dorsal longitudinal and GF-tergo trochanteral muscle pathways in the D.melanogaster GF circuit (PubMed:28917942). Has possibly a distinct nAChR binding mode from other alpha-conotoxins, due to a different three residue motif (lacks the Ser-Xaa-Pro motif) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
+{"protein": "MWAFPELPMPLLVNLIGSLMGFVATVTLIPAFRGHFIAARLCGQDLNKSSREQIPESQGVISGAVFLIILFCFIPFPFLNCFVEQQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPLRPILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELDGDYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRMPRLNTKTGKLEMSYSKFKTKSLSFLGTFILKVAENLGLLTVRHSEDEDGAFTECNNMTLINLLLKVFGPMHERNLTLLLLLLQVVGSAVTFSIRYQLVRLFYDV", "text": "FUNCTION: Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family."}
+{"protein": "MGLLYKGSKLLNIILDSLEDQEGGAMYISCDVSNGGPVEPETGYVPNNPLFGLALDSPQQECAASCVGCLSCQGNTALPISSLTSSDFDCGGCFDPTIGVLGSQINTTPPASNLSASGSGVGNHNNGAALAGNGNSYWSTDEMASTFPGLPPLDIDPLPSLFPFSPCGASYNFASNPHQASLSYTVHPHQMLISPNGSQQQQSQSSTHPHQLQSQHMQQALTQASHGGNALHNHNSSGGNGPGGGGGSGSGSACYYEAATNAPAPPMYPSMSVNVSMNMTMHHGYGADGGPVPMQCSQMNWTPPSNSSAAVNVLYPPLLSPTHYPASATYSFTADFRAPPPTALGALPSLADKESPSPPASSTAAALGYYATGGVGQGYTPPHKSPSYQAAALSLGLAAFEDEEESIEDGDADADGEGSAGGDMKPNLCRLCGKTYARPSTLKTHLRTHSGERPYRCPDCNKSFSQAANLTAHVRTHTGQKPFRCPICDRRFSQSSSVTTHMRTHSGERPYRCSSCKKSFSDSSTLTKHLRIHSGEKPYQCKLCLLRFSQSGNLNRHMRVHGNNANGSGAGGGSGNGSGNGSGSGANGSAGAGSGLIT", "text": "FUNCTION: Transcription factor required for gene expression specific to photoreceptor cells. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MEVNCLTLKDLISRPPRLDFAIEDGENAQKENIFVDLSRMAPKTPIKNEPIDLSKQKIFTPERNPITPVKLVDRQQVEPWTPTANLKILISAASPDIRDREKKKELFRPIENKDDVFTDSLQLDAVDDSAVDEFEKQRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYSWHGRHSLPKTLRNLQRLGEKQKYEEQMAHLQQKELNPIDHKSGERRRDGCPDSQDPQLLDFPEPDCPSSSANSRKDKSLKIMSQKFVMLFLVSKTKIVTLDVAAKILIEESQDIPDHSKFKTKVRRLYDIANVLTSLMLIKKVHVTEDRGRKPAFKWIGPVDFSSTDDDLVDVSTPVLPELKKEIYGHVQFCAKQKLARHSSFNSEQASERTQRKVNSEPSSPYRQKQGLGVYSLEIGSLAAVSRQKMEDNSETVAFASQNMMPLPSSLDPAAPLPSPSVDSEYRVSPLCHQALSAAQTDLKALPAQNGLNGQGGVSLASMALDVEHQPQPLAAAQPLLYVPPAPLFMLCGGLQEGLSPGSGSGSGSVGGGSEVTAAEQPPMPSGQKRLSKERRLQEEEEEPATKRQCRDHEDGPLSLVMPKKPSDSADIASPKTSENRASAPHEDTHMNGQLSAAKAVSGKATTNGFVSSEWGNPCSNTEIEKPSEENESTKGPSPLQYLYVQPPAGLNGLSVLLPSSQSPHAVGLPVGPLPSLSIQYMVLPSPALSGFPVLCSPTMPGPVSSAPSPLPNVGPVNFGLPGLGSTAHLLIGPAAMVNPKSSTLPSTDPQLQGPCSLHLSPVMSRSHGSVQPGSPAYGSLPAATVKLQQSPVPVTPKSIRCTHQETFFKTPGSLGDPVLRRKERNQSRSSSSAQRRLEISSGGTD", "text": "FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. 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. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. 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. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. 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. Acts as a negative regulator of keratinocyte differentiation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the E2F/DP family."}
+{"protein": "MRPTQTMLGGGGGAPIGKHNHYLGGWGNFGGMKQRGIISYGISPNRQNPLAGTAHDAVFNTFRRVSSQFLYWAPSLVAGYYIMNWAIERNHYLNSKAGRAEFAGQEE", "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; Single-pass membrane protein. SIMILARITY: Belongs to the UQCRQ/QCR8 family."}
+{"protein": "MMWWAVWCAAMVAGSVFTAAAPPTDSIDLMQMDPSLADDESLGFAMQSLSGRYAAAPWLYLLADVSHDPQRMAEFSQSSGRARPKRKMPSLSINNPMEVLRQRLLLEVARKQMREANQRQAVANRLFLQNVGKRGAWGEPASYLYNN", "text": "FUNCTION: Regulation of fluid secretion. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sauvagine/corticotropin-releasing factor/urotensin I family."}
+{"protein": "MDRGVLPLPITLLFVIYSFVPTTGLAERVGCDLQPVDPTRGEVTFTTSQVSEGCVAQAANAVREVHVLFLDFPGMLSHLELTLQASKQNGTETQEVFLVLVSNKNVFVKFQAPEIPLHLAYDSSLVIFQGQPRVNITVLPSLTSRKQILDWAATKGAITSIAALDDPQSIVLQLGQDPKAPFLCLPEAHKDMGATLEWQPRAQTPVQSCRLEGVSGHKEAYILRILPGSEAGPRTVTVMMELSCTSGDAILILHGPPYVSWFIDINHSMQILTTGEYSVKIFPGSKVKGVELPDTPQGLIAEARKLNASIVTSFVELPLVSNVSLRASSCGGVFQTTPAPVVTTPPKDTCSPVLLMSLIQPKCGNQVMTLALNKKHVQTLQCTITGLTFWDSSCQAEDTDDHLVLSSAYSSCGMKVTAHVVSNEVIISFPSGSPPLRKKVQCIDMDSLSFQLGLYLSPHFLQASNTIELGQQAFVQVSVSPLTSEVTVQLDSCHLDLGPEGDMVELIQSRTAKGSCVTLLSPSPEGDPRFSFLLRVYMVPTPTAGTLSCNLALRPSTLSQEVYKTVSMRLNIVSPDLSGKGLVLPSVLGITFGAFLIGALLTAALWYIYSHTRGPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA", "text": "FUNCTION: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis (PubMed:10625534). Required for normal structure and integrity of adult vasculature (By similarity). Regulates the migration of vascular endothelial cells (PubMed:17540773). Required for normal extraembryonic angiogenesis and for embryonic heart development (PubMed:10625534). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (PubMed:28530658). May play a role in the binding of endothelial cells to integrins. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:23300529). Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MEAAVLRVKRKRGADPADALILSCKRIRTEDETKESSAVTTQVFRLAATVKSENEPLHKYVREAISRNQSCLTLRPSSESKQRIQEELRASKEAERQVSRYRIISSHRPNSEEDNVGASHLIGCSSQDVPSETQDEAEATEATKSHISSPFQLFDMVQEEPEQKYLEKDSEPETILCNSIKMIREHLTVSEAGQESEHREYVDEYVYDIYYSEASQHGWIQDILYVQPYTEEQELVSEEPEPEEIYEDEDDENEENNWRNDYPDEEDSDREERYIGYYEDGDEEEKSAGHAWKMYHRSSLREIGDDDENADLY", "text": "FUNCTION: Directs RNA polymerase II nuclear import. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the IWR1/SLC7A6OS family."}
+{"protein": "MATLEDGTSEDRVANDEYKIWKKNTPFLYDLVMTHALEWPSLSVQWLPDVAKDNSDHTIHRLILGTHTSDEQNHLLISKICMPTDDAQFDASRYDTERSEYGGFGAVNGKVEPDIRINHEGEVNRARYMPQKSNIIATKSPHADVYIFDYLKHSAVPRDNTFNPLIRLKGHTKEGYGLSWNPNKEGLILSASDDQTVCHWDINANQNVAGELQAKDVFKGHESVVEDVAWHVLHDGVFGSVGDDKKLLIWDVRTSTPGHCIDAHSAEVNCLAFNPYSEFILATGSADKTVALWDLRNLRMKLHSFESHRDEIFQVQWSPHNETILASSGTDKRLHVWDLSKIGEDQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVVCSVSEDNILQVWQMADNIYNEVDEETPADVVERQQ", "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 (By similarity). Required for hcp-3 and his-1 stabilization, localization of hcp-3 to centromeres and for proper chromosome segregation (PubMed:25446273, PubMed:26904949). Synthetic multivulva class B (synMuvB) protein (PubMed:9875852). SynMuvB proteins are required to repress the induction of vulval development by Ras signaling and probably act by forming the multiprotein DRM complex that represses transcription (PubMed:10704416, PubMed:17075059, PubMed:9875852). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Localizes to centromeres during metaphase. Requires hcp-3 and knl-2 for nuclear and centromere localization. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."}
+{"protein": "MADPAIKLFGKTIPLPELGVVDSSSSYTGFLTETQIPVRLSDSCTGDDDDEEMGDSGLGREEGDDVGDGGGESETDKKEEKDSECQEESLRNESNDVTTTTSGITEKTETTKAAKTNEESGGTACSQEGKLKKPDKILPCPRCNSMETKFCYYNNYNVNQPRHFCKKCQRYWTAGGTMRNVPVGAGRRKNKSPASHYNRHVSITSAEAMQKVARTDLQHPNGANLLTFGSDSVLCESMASGLNLVEKSLLKTQTVLQEPNEGLKITVPLNQTNEEAGTVSPLPKVPCFPGPPPTWPYAWNGVSWTILPFYPPPAYWSCPGVSPGAWNSFTWMPQPNSPSGSNPNSPTLGKHSRDENAAEPGTAFDETESLGREKSKPERCLWVPKTLRIDDPEEAAKSSIWETLGIKKDENADTFGAFRSSTKEKSSLSEGRLPGRRPELQANPAALSRSANFHESS", "text": "FUNCTION: Transcription factor that binds specifically to a 5'-AA[AG]G- 3' consensus core sequence (By similarity). Regulates a photoperiodic flowering response. Transcriptional repressor of 'CONSTANS' expression. The stability of CDF2 is controlled by 'GIGANTEA' and redundantly by ADO3, ADO2 and/or ADO1. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "ANCSCSTASDYCPILTFCTTGTACSYTPTGCGTGWVYCACNGNFY", "text": "FUNCTION: Bacteriocin."}
+{"protein": "MAPGANIHIPPAGPPEPGPLYSDFYQQQIERQRNNNYHSTSLRNMVATSVNRTALHPGGVQPGKGHTELEEELHEHAHIDYDRVAIIANPSVAALYEDALVYETGTAITSSGALTAYSGAKTGRSPSDKRIVKEESSEKEVWWGPVNKPMTPDVWRINRERAVDYLNTRNRIYVIDGFAGWDERYRISVRVVCARAYHALFMRNMLIRPSAEELKHFHPDYVIYNAGSFPANRFTEGMTSATSVAINFAEKEMVILGTEYAGEMKKGVFTILFYEMPVKHNVLTLHSSANEGQNGDVTVFFGLSGTGKTTLSADPKRALIGDDEHCWTDRGVFNIEGGCYAKCIGLSAEKEPDIFNAIRFGSVLENVVFDPISRVVDYDDSTLTENTRCAYPIEYIENAKVPCLSDSHPSNIILLTCDARGVLPPISKLTTEQTMFHFISGYTSKMAGTEDGVTEPQATFSSCFAQPFLALHPMRYARMLADKISQHKANAWLLNTGWVGAGATTGGKRCPLKYTRAILDAIHSGELAKAEYETYDVFNLHVPKSCPGVPDELLNPKNSWTATTSFSDEVNKLAKLFNENFQKYADQATKEVIAAGPVVQ", "text": "SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP) family."}
+{"protein": "MDDKQHTTSSDDERAENATSNQDQQTNSSKRVHLKRWQFISILIGTIIITAVITVVAYIFINQKISGLNKTDQANLNKIENVYKILNSDYYKKQNSDKLSKAAIDGMVKELKDPYSEYLTKEQTKSFNEGVSGDFVGIGAEMQKKNDQIMVTSPMKGSPAERAGIRPKDVITKVNGKSIKGKALDEVVKDVRGKENTEVTLTVQRGSEEKDVKIKREKIHVKSVEYKKKGKVGVITINKFQNDTSGELKDAVLKAHKDGLKKIVLDLRNNPGGLLDEAVKMANIFIDKGKTVVKLEKGKDTEAIQTSNDALKEAKDMDISILVNEGSASASEVFTGALKDYNKAKVYGSKTFGKGVVQTTREFKDGSLLKYTEMKWLTPDGHYIHGKGIKPDVTIDTPKYQSLNVIPNTKTFKVGDDDKNIKTIKIGLSALGYKVDNESTQFDQALENLVKAFQQANKLEVTGEFNKETNNKFTELLVEKANKHDDVLDKLINILK", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S41A family."}
+{"protein": "DCAKEGEVCSWGKKCCDLDNFYCPMEFIPHCKKYKPYVPVTTNCAKEGEVCGWGSKCCHGLDCPLAFIPYCEKYRGRND", "text": "FUNCTION: Selectively activates the heat-activated TRPV1 channel. It binds to TRPV1 in an open state-dependent manner, trapping it there to produce irreversible currents (PubMed:20510930, PubMed:26880553, PubMed:27281200). It binds to the outer edge of the external pore of TRPV1 in a counterclockwise configuration, using a limited protein- protein interface and inserting hydrophobic residues into the bilayer (PubMed:26880553, PubMed:27281200). It also partitions naturally into membranes, with the two lobes exhibiting opposing energetics for membrane partitioning (K1) and channel activation (K2) (PubMed:26880553). In addition, the toxin disrupts a cluster of hydrophobic residues behind the selectivity filter that are critical for channel activation (PubMed:26880553). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 23 family. Double-knot toxin subfamily."}
+{"protein": "MREEREDMLSWPLIGEKEKRSRFVKEEVEKQLLLSGPLIAVSLLQFCLQIISVMFVGHLGSLPLSAASIATSFASVTGFTFLMGTASAMDTVCGQSYGAKMYGMLGIQMQRAMLVLTLLSVPLSIVWANTEHFLVFFGQDKSIAHLSGSYARFMIPSIFAYGLLQCLNRFLQAQNNVIPVVICSGVTTSLHVIICWVLVLKSGLGFRGAAVANAISYWLNVILLSCYVKFSPSCSLTWTGFSKEARRDIIPFMKLVIPSAFMVCSLEMWSFELLVLSSGLLPNPVLETSCPRTVWMIPFGLSGAASTRVSNELGSGNPKGAKLAVRVVLSFSIVESILVGTVLILIRKIWGFAYSSDPEVVSHVASMLPILALGHSLDSFQTVLSGVARGCGWQKIGAFVNLGSYYLVGVPFGLLLGFHFHVGGRGLWLGIICALIVQGVCLSLITFFTNWDEEVKKATSRAKSSSEVKEFAVDNGSILV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
+{"protein": "GNVDFDSESPRKPEIQNEIIDLHNSLRRSVNPTASNMLKMEWYPEAAANAERWAFRCILSHSPRDSRVIGGIKCGENIYMSTSPMKWTAIIHKWHGEEKDFVYGQGASPANAVVGHYTQIVWYKSYRSGCAAAYCPSSEYKYFYVCQYCPAGNMQGKTATPYTSGPPCGDCPSACDNGLCTNPCTHEDKFTNCKDLVKQGCNNNYLKTNCPASCSCHNEII", "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 in smooth muscle (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
+{"protein": "MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELTSTSVEHIIVNPNAAYDKFKDKKVGTRSLDFSDRITKSKRTGYESGEYEILGEGIGMKETPQQKYQRLLHEVQELTQEVEKTQSTVKESAAEEKLTPVALAKQVASLKQQLVSTHLEKLLGPDAAINLTDPDGALAKRLLTQLDAAKTRKNPEGKSPAKGPGPDTENLVTYELHCRPEQNKFSQAAKMAELEKRLGELEVAVRCDQDTQNPLTVGLQGSCLMDTVEILQAKVNLLDVASLDQVEARLQSVLGKMNEIAKHKAAIEDADTESKVHQLYETVQKWDSMSGTLPQVVQRLLTLKQLHEQAMQFGQLLTHLDTTQQMIANSLKDNTNALAMVQKAMKENLATVEDNFSNIDGRIKKLSK", "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": "MSRRGPEEEACGVWLDAAALKRQKMQTHLLKLGTKMLTLLPGERKPSIPFTQRRATRQTSITSFVTSQPGMANGGNQKNASSLKENQINRECKSRSQLDCLDQGLEDDCLVSPLATSTPADIREAGHSPQSSQISGCQSLETTSLTMMSFPQPVVLMGTGESKAPLASSFTQFLERSCLLDQREAKRKREGLCGSKTDCPGMGSHIRPPGGKCHQPLDKAKVEKRATAKENRQAPVHLQTYRFGSHSGKKTLLVTKSPCPLSVFSWDIDRKDRDSWSQLFTEDSQGHQVIAHSTKMPFQDVTNARNQGSGQFPDSPQAQGQDGPTLLHLQPHLLFTQDSEGNRVIRH", "text": "FUNCTION: DNA-binding protein that accumulates at DNA double-strand breaks (DSBs) following DNA damage and promotes DNA resection and homologous recombination. 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. Inhibits non-homologous end joining (NHEJ). Required for the dynamic movement of AURKA at the centrosomes and spindle apparatus during the cell cycle. 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. Localizes to the centrosome in interphase and to the spindle pole in metaphase. SIMILARITY: Belongs to the AUNIP family."}
+{"protein": "MTTSSYFLLVALGLLLYLCQSSFGTEHTCEPGASPHPQGKCRPELAEFHETMCEVEESLQGGTDDARKKRGRASLLRKRRGFLSMLKARAKRNEASPLPRAGRGIVCECCKNSCTYEEITEYCPPVTEGSG", "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": "MSESGEMSEFGYIMELIAKGKVTIKNIERELICPACKELFTHPLILPCQHSICHKCVKELLLTLDDSFNDVGSDNSNQSSPRLRLPSPSMDKIDRINRPGWKRNSLTPRTTVFPCPGCEHDVDLGERGINGLFRNFTLETIVERYRQAARAATAIMCDLCKPPPQESTKSCMDCSASYCNECFKIHHPWGTIKAQHEYVGPTTNFRPKILMCPEHETERINMYCELCRRPVCHLCKLGGNHANHRVTTMSSAYKTLKEKLSKDIDYLIGKESQVKSQISELNLLMKETECNGERAKEEAITHFEKLFEVLEERKSSVLKAIDSSKKLRLDKFQTQMEEYQGLLENNGLVGYAQEVLKETDQSCFVQTAKQLHLRIQKATESLKSFRPAAQTSFEDYVVNTSKQTELLGELSFFSSGIDVPEINEEQSKVYNNALINWHHPEKDKADSYVLEYRKINRDDEMSWNEIEVCGTSKIIQDLENSSTYAFRVRAYKGSICSPCSRELILHTPPAPVFSFLFDEKCGYNNEHLLLNLKRDRVESRAGFNLLLAAERIQVGYYTSLDYIIGDTGITKGKHFWAFRVEPYSYLVKVGVASSDKLQEWLRSPRDAVSPRYEQDSGHDSGSEDACFDSSQPFTLVTIGMQKFFIPKSPTSSNEPENRVLPMPTSIGIFLDCDKGKVDFYDMDQMKCLYERQVDCSHTLYPAFALMGSGGIQLEEPITAKYLEYQEDM", "text": "FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Involved in chromosome segregation and cell cycle regulation (PubMed:28087737). May play a role in the acrosome reaction and fertilization. SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, secretory vesicle, acrosome Cytoplasm, cytoskeleton Note=Found in the acrosomal region of elongated spermatids and mature sperm. SIMILARITY: Belongs to the TRIM/RBCC family."}
+{"protein": "MLGQSIRRFTTSAVRRSHYEEGPGKNLPFSVENKWRLLAMMCLYFGSAFATPFLILRHQLLKK", "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 VIIc family."}
+{"protein": "MEHADADRTRVAPEIGSLHDEDAEADPARAREMERLQPWREQVTARGVVAAALIGFVFSVIVMKIALTTGLVPTLNISAALLAFLALRGWTRALERLGFSPRPFTRQENTVVQTCAVACYTIAFGGGFGSTLLGLNKRTYELAGNSPGNVPGSYKEPGIGWMVGLLLAISFAGNLSLIPLRKALVVDYKLTYPSGTATAVLINGFHTAQGDKNAKLQLHGFLKYFGLSLFWSFFQWFYTGGNACGFVQFPTFGLKAWKQSFFFDFSLTYVGAGMICSHLVNLSTLLGAVISWGIMWPLISKHKGDWYPANIPESSMTSLYGYKSFLCIALIMGDGLYHFVKVTGVTAKSLHNRFNRKSVSNTASEEGDMVSLDDLQRDEVFKRGTVPSWMAYSGYFLLSIIAVITIPIMFRQVKWYYVIIAYALGPVLGFANSYGAGLTDINMGYNYGKIALFVFAAWAGKDNGVIAGLVVGTLVKQLVLVSADLMHDLKTGHLTLTSPRSMLVGELIGTGIGCFIAPLTFMLFYRAFDIGNPDGYWKAPYALIYRNMAILGIEGISALPKHCLSLSVGFFAFAVLTNVARDALPARYKKLVPLPTAMAVPFLVGASFAIDMCVGSLVLFAWNKMNKKEAAFMVPAVASGLMCGDGIWTFPSSILALAKIKPPICMKFTPGS", "text": "FUNCTION: Involved in Fe(3+) uptake from the rhizosphere and phloem transport of iron. Plays an important role in iron homeostasis during the early stages of growth. Transports Fe(3+)-phytosiderophore, but not Fe(3+)- or Fe(2+)-nicotianamine. May not transport other chelated metals. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the YSL (TC 2.A.67.2) family."}
+{"protein": "MATAGASSFEDEIMESDIELEGEAVEPDNDPPQKMGDPSVEVSDEKRDQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAAKLDYDEEIGAELKKVEPNVLKIEEHRKKYERLRKERDIKKAEMEKQRKHAEEVSAASAALKDGDVIAIHSSSELDTKLKAASSLSRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGADKNGLERKVAQHGSS", "text": "FUNCTION: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions and act as chaperone under heat shock. May interact with HSP70 proteins through the TPR repeats (By similarity). SIMILARITY: Belongs to the thioredoxin family."}
+{"protein": "LPEQDFMRF", "text": "FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
+{"protein": "MKNNLKVKLEELVIYILKNIKRYPNIIQRLKFYEQIHLGLTLNKIKNKREIYYNSVSIFKKQSIVDMLIKDTCNKLKCTQSDLLISTTLKGVFYGNITFYKNNKLVHVNLKGTSLIPDMNQIDRIEYTQKKCLIIEKDTIFSKTVREYISNDILFICGKGYPCRNTLLLVNKLNIRKYGIFDFDPYGLEICTKYPSIKKIGIDIKDINLIDKQHFMILNKYDIRKINTLLKQKVYEIELFYMLKNNIKIEIEGLFSAKGFDINNYFYTKII", "text": "FUNCTION: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TOP6A family."}
+{"protein": "MHKLFKNAPFFDFEAIRILGTTCYGGADVAEVFEAVDQIKNNDPETWETAWRIQAERAEKLAAEALEHGDRDAALAGYLRASNYTRASGYMYVSRAESSGEALVQDARALPIAEKVGELFRKAIPLMKGSVHTLGIPYEEYALPGYLYLPPPWRRIPGRKIPILVNSGGADSCQEELFYLNPAAGPGQGYAVVTFDGPGQGIMLRKYGLEMRPDWEAVTGRVIDFLEEYAAENPHLELDLNCIAVSGASMGGYYALRAAADQRVKACVSIDPFYDMWDFGTAHVSPIFIHAWTSGWISGGFVDNLMALLSRLSFQLRWEISVTGTFFGLSSPSQILLHMKKYTLRSTEEEPEGFLSRVICPVLLSGAGKSLYLDVDNHTRQCYDGLVNVAERNKQLWIPESEGQGSLQAKMGAFRLCNQRTYRFLDECFGIMRKSL", "text": "FUNCTION: Hydrolyase; part of the gene cluster that mediates the biosynthesis of a family of the mycotoxins cytochalasins E and K (PubMed:21983160). The hybrid PKS-NRPS synthetase ccsA and the enoyl reductase ccsC are responsible for fusion of phenylalanine with an octaketide backbone and subsequent release of the stable tetramic acid precursor (PubMed:21983160, PubMed:27551732). The polyketide synthase module (PKS) of the PKS-NRPS ccsA is responsible for the synthesis of the octaketide backbone (PubMed:21983160). The downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the octaketide with a phenylalanine (PubMed:21983160). A reductase-like domain (R) at the C-terminus catalyzes the reductive release of the polyketide-amino acid intermediate (PubMed:21983160). Because ccsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ccsC (PubMed:21983160, PubMed:27551732). Upon formation of the 11-membered carbocycle-fused perhydroisoindolone intermediate, a number of oxidative steps are required to afford the final cytochalasin E and K, including two hydroxylations at C17 and C18, one alcohol oxidation at C17, one epoxidation at C6 and C7 and two Baeyer-Villiger oxidations (PubMed:21983160). The oxidative modification at C17, C18 and the C6-C7 epoxidation are likely to be catalyzed by the two cytochrome P450 oxygenases ccsD and ccsG (PubMed:21983160). CcsD may be responsible for the epoxidation of the C6-C7 double bond (PubMed:21983160). CcsG may be responsible for the successive oxidative modifications at C17 and C18 (PubMed:21983160). The double Baeyer- Villiger oxidations of ketocytochalasin to precytochalasin and cytochalasin Z(16) are among the final steps leading to cytochalasin E and K and are catalyzed by ccsB (PubMed:21983160, PubMed:24838010). The first oxygen insertion step follows that of the classic BVMO mechanism, generating the ester precytochalasin (PubMed:24838010). Release of precytochalasin into an aqueous environment can generate the shunt product iso-precytochalasin through spontaneous isomerization (PubMed:24838010). Alternatively, precytochalasin can undergo further oxidation by ccsB to yield the in-line carbonate-containing cytochalasin Z(16) (PubMed:24838010). Cytochalasin Z(16) is a precursor to cytochalasin E and cytochalasin K, whereas iso-precytochalasin is a precursor to cytochalasin Z(17) and rosellichalasin (PubMed:21983160, PubMed:24838010). The hydrolyase ccsE may catalyze hydrolysis of epoxide bond in cytochalasin E to afford cytochalasin K (PubMed:21983160). The function of ccsF has not been assigned but it may play a role in post-PKS-NRPS biosynthetic step, resistance or transport of cytochalasins and related PKS-NRPS products (PubMed:21983160). SIMILARITY: Belongs to the AB hydrolase superfamily. FUS2 hydrolase family."}
+{"protein": "MWNLRITPLSFGAACQGIFTSTLLLSALTVPLVCTIVYDSCLYMDINASRALANVYDLPDDFFPKIDDLVRDAKDALEPYWKSDSIKKHVLIATHFVDLIEDFWQTTQGMHEIAESLRAVIPPTTAPVPTGYLIQHEEAEEIPLGDLFKHQEERIVSFQPDYPITARIHAHLKAYAKINEESLDRARRLLWWHYNCLLWGEANVTNYISRLRTWLSTPEKYRGRDAPTIEAITRPIQAAQGGRKTSSGTRKPRGLEPRRRKVKTTVVYGRRRSKSRERRAPSPQRAGSPLPRSSSSHHRSPSPRK", "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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the avihepadnavirus precore antigen family."}
+{"protein": "MDLLKVLSQMILFLLFLYLSPLGGHSYPLGSPSQSPEQFKMQKLLELIREKSEEMAQRQLLKDQGLTKEHPKRVLRSQGSTLRVQQRPQNSKVTHISSCFGHKIDRIGSVSRLGCNALKLL", "text": "FUNCTION: [Brain natriuretic peptide 45]: Cardiac hormone that plays a key role in mediating cardio-renal homeostasis (PubMed:8182124). May also function as a paracrine antifibrotic factor in the heart (PubMed:10737768). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins that drive various biological responses (PubMed:8182124). Likely involved in regulating the extracellular fluid volume and maintaining the fluid- electrolyte balance through natriuresis, diuresis, kaluresis and chloruresis (By similarity). SUBCELLULAR LOCATION: [Brain natriuretic peptide 45]: Secreted Note=Detected in blood. SIMILARITY: Belongs to the natriuretic peptide family."}
+{"protein": "MDSEFFQPVYPRHYGECLSPTSTPSFFSTHMYTILIAIVVLVIIIIVLIYLFSSRKKKAAAAIEEEDIQFINPYQDQQWAEVTPQPGTSKPAGATTASAGKPVTGRPATNRPATNKPVTDNPVTDRLVMATGGPAAAPAAASAHPTEPYTTVTTQNTASQTMSAIENLRQRNTYTHKDLENSL", "text": "FUNCTION: Inner envelope protein involved, through its interaction with host dynein, in the intracellular microtubule-dependent transport of viral capsid toward viral factories (By similarity). Seems to induce caspase-3 activation and apoptosis (By similarity). Plays a role in virion morphogenesis by recruiting and transforming the host ER membranes into the precursors of the viral envelope (By similarity). Involved in virus attachment to the host cell (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Host cytoplasm, host cytoskeleton Host endoplasmic reticulum membrane Note=Detected mainly on membrane-like structures within viral factories. Present in mature extracellular virions. Host DYNLL1 and viral p54 interact at the microtubular organizing center (By similarity). Found in the inner envelope of the virus (By similarity). SIMILARITY: Belongs to the asfivirus envelope protein p54 family."}
+{"protein": "MFKKWSGLFVIAACFLLVAACGNSSTKGSADSKGDKLHVVTTFYPMYEFTKQIVKDKGDVDLLIPSSVEPHDWEPTPKDIANIQDADLFVYNSEYMETWVPSAEKSMGQGHAVFVNASKGIDLMEGSEEEHEEHDHGEHEHSHAMDPHVWLSPVLAQKEVKNITAQIVKQDPDNKEYYEKNSKEYIAKLQDLDKLYRTTAKKAEKKEFITQHTAFGYLAKEYGLKQVPIAGLSPDQEPSAASLAKLKTYAKEHNVKVIYFEEIASSKVADTLASEIGAKTEVLNTLEGLSKEEQDKGLGYIDIMKQNLDALKDSLLVKS", "text": "FUNCTION: Part of the high-affinity ABC transporter complex ZnuABC involved in zinc import (Probable). ZnuABC-mediated zinc transport is required for comF expression and competence development. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor 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 9 family."}
+{"protein": "MKLSVSPPPFDGAPVVVLIAGLGGGGSYWLPQLAALEQEYQVVCYDQRGTGNNPDTLPEEYTLAQMAGELAQALTAVGITRYCVVGHALGALIGLQLALDTPDALKALVCVNGWLTLNAHTRRCFQIRERLLHAGGAQAWVEAQPLFLYPADWMAARAPRLEAEEALALAHFQGKNNLLRRLNALKKADFSRHAARMACPVHLICSADDLLVPSVCSSELQAALPHSHSVVMRQGGHACNVTEPETFNTLLLNGLASLLHSHEPAL", "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": "MIVLGWMFFVGLVCYMGTFPELMPPTLKWQERWPVQESKTQLRRRALGEDLLQNHVEGI", "text": "FUNCTION: [Isoform Polluks]: Regulates sperm development. May be involved in mitochondrial sheath formation. FUNCTION: [Isoform Kastor]: Regulates sperm development. May be involved in mitochondrial sheath formation. SUBCELLULAR LOCATION: [Isoform Kastor]: Mitochondrion outer membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: [Isoform Polluks]: Mitochondrion outer membrane; Single-pass membrane protein."}
+{"protein": "MAAKIRRDDEVIVLTGKDKGKRGKVKNVLSSGKVIVEGINLVKKHQKPVPALNQPGGIVEKEAAIQVSNVAIFNAATGKADRVGFRFEDGKKVRFFKSNSETIK", "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 two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro. 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. SIMILARITY: Belongs to the universal ribosomal protein uL24 family. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
+{"protein": "MSTNNSTQQQDELDQIKSKIQDNLISSGNYDIINKQLKLQLYESGWYDKVSQIASRELMDHQQEVNSSNSNSSNSNKKNELTFDQLFAFVKPKAEELVPNEVKQDILNRITKYLDDIIQ", "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": "MTTLTGQPPLYGGSTGGLLSAADTEEKYAITWTSPKEQVFEMPTAGAAVMREGENLVYFARKEQCLALAAQQLRPRKINDYKIYRIFPDGETVLIHPKDGVFPEKVNKGREAVNSVPRSIGQNPNPSQLKFTGKKPYDP", "text": "FUNCTION: PsaD can form complexes with ferredoxin and ferredoxin- oxidoreductase in photosystem I (PS I) reaction center. FUNCTION: PsaD can form complexes with ferredoxin and ferredoxin- oxidoreductase in photosystem I (PS I) reaction center. SIMILARITY: Belongs to the PsaD family."}
+{"protein": "MLSTAAYRDPDRELVMGPQGSAGPVQMRFSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIEGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLTLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD", "text": "FUNCTION: Non-catalytic 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). 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": "MELMSSLGSLLASSLPIEKKQHALVELVLHTYQPQQRTALFKTVTEYRRNQLELLFPEHQAKSDSVMFEVMDYRDLIQRYPNTLSTEVALLEEAVGQCYIHWLDFWCECEISAIKAKLPLSTHALYPMDLPIKDSAYYGVIIDQIENSQLIVQTPTRPQGLPISDAIALSNLEVFIKGEKWYEMLPLLHLSQTGKHFILLKHPTDEAFPTLVSSALIQDWSKYETWLSYAPPFCNDKWKYSLSRRGYEGLAELHIFTPPALSKCDSIPEFDNKFQLQLAEMQAVCEILRLTVSGNIQQKVYFLYLAQKEMLNLLHQAGYKIGFTIIDQPLILDFYKAIEPQAYLPLGYCDLNETNLLTYRGLWNIELMLKAFNHVNFRDYRRCLRENKNTAWQII", "text": "SIMILARITY: Belongs to the LuxM / VanM family."}
+{"protein": "MPNPSCTSSPGPLPEEIRNLLADVETFVADTLKGENLSKKAKEKRESLIKKIKDVKSVYLQEFQDKGDAEDGDEYDDPFAGPADTISLASERYDKDDDGPSDGNQFPPIAAQDLPFVIKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYDVRMNNTLRKDGKKDCCFEICAPDKRIYQFTAASPKDAEEWVQQLKFILQDLGSDVIPEDDEERGELYDDVDHPAAVSSPQRSQPIDDEIYEELPEEEEDTASVKMDEQGKGSRDSVHHTSGDKSTDYANFYQGLWDCTGALSDELSFKRGDVIYILSKEYNRYGWWVGEMKGAIGLVPKAYLMEMYDI", "text": "FUNCTION: May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. SUBCELLULAR LOCATION: Cytoplasm Note=Membrane ruffles of macrophages. Perikarya and dendrites from neurons. SIMILARITY: Belongs to the SKAP family."}
+{"protein": "MFGVLNSNDHRAAVQQRNIPAFGRTSFEPWTDNPTSNYRCETGGNGRDSGQNRVRRPMNAFMVWSRDQRRKVALENPQMQNSEISKQLGYQWKMLTEAEKWPFFEEAQRLQAMHREKYPDYKYRPRRKALPQKSDKLLPAASSSMLCRQVLVDEKWYPFTYRDSCSRAAHSRMEDQLSSSQPVNIANSLLQQEHHYRSTSLRDSPETLAAHLSADPPFYPKEQLGLSDAYFP", "text": "FUNCTION: Transcriptional regulator that controls a genetic switch in male development. It is necessary and sufficient for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells. Involved in different aspects of gene regulation including promoter activation or repression. Binds to the DNA consensus sequence 5'- [AT]AACAA[AT]-3'. SRY HMG box recognizes DNA by partial intercalation in the minor groove and promotes DNA bending. Also involved in pre-mRNA splicing (By similarity). In male adult brain involved in the maintenance of motor functions of dopaminergic neurons (By similarity). SUBCELLULAR LOCATION: Nucleus speckle Cytoplasm Nucleus. SIMILARITY: Belongs to the SRY family."}
+{"protein": "DHIDLEFDVGQCIQASYTAPTTGRTSVNIVASDGTVVLHVDYRKHWGGNPSTGKPWQNILIINSKLGGSWGTEEKVHDVETTIVNYDYTQCGQDADFSLELNQKDIATYAYRSPVNTVSRVQFDDQGYDAVLRKLCVVYPAPSK", "text": "FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates."}
+{"protein": "MVIMSEDASVPAPSAAQPRPLRVGFYDIERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDPSNLEKIYREVQIMKLLNHPHIIKLYQVMETKDMLYIVTEFAKNGEMFDHLTSNGHLSESEARKKFWQILSAVEYCHSHHIVHRDLKTENLLLDANMNIKLADFGFGNFYKSGEPLSTWCGSPPYAAPEVFEGKEYEGPHLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPYFMSEDCETLIRRMLVVDPTKRITISQIKQHKWMQADPSLRQQQSLSFSMQNYNSNLGDYNEQVLGIMQTLGIDRQRTVESLQNSSYNHFAAIYYLLLERLKEYRSSQLSSRPATGRQQRPRSSEISNAEMPQDSLTSETLRSSLLYQQPQSLIQPSLQAEMDCDMNNPLQPVFFPVDPNFNGLFRNRSISPSSLLETTISEEVRQEKELEDEIKAYDHPIRIPSNTSRRHTLAEVTTHFYQHAPPCIVISSSASPTEGTSSDSCLTSSSNDSSVALSSCLAGQVMTGSPATARMTSAFLASQSDAPVLQVQGCMGGASLLPVSFQEGRRASDTSLTQGLKAFRQQLRKNARAKGFLGLNKIKGFARQVCQSSSSRAARSAMSPFQHAQPNTCIYSSSGSSREGRNLLEEVLQQQRMLQLQHHQLLQPACPQTSQTSATNGLPPSDSAGTCKASNSLLLSELQRENSFELAFGGNSQLLQPHFFGVSVSPVSSAAHLLDTHLYISSNVSPVGTTFSQQQSFSAQSPSYDAVTLQHGDCEMEDLTSNQLGKFVLVK", "text": "FUNCTION: Phosphorylates IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing the CREB- specific coactivators, CRTC1-3 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily."}
+{"protein": "MAVPAALIPPTQLVPPQPPISTSASSSGTTTSTSSATSSPAPSIGPPASSGPTLFRPEPIASAAAAAATVTSTGGGGGGGGSGGGGGSSGNGGGGGGGGGGSNCNPNLAAASNGSGGGGGGISAGGGVASSTPINASTGSSSSSSSSSSSSSSSSSSSSSSSSCGPLPGKPVYSTPSPVENTPQNNECKMVDLRGAKVASFTVEGCELICLPQAFDLFLKHLVGGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFETLYNDCTNASSRPGRPPKRTQSVTSPENSHIMPHSVPGLMSPGIIPPTGLTAAAAAAAAATNAAIAEAMKVKKIKLEAMSNYHASNNQHGADSENGDMNSSVGSSDGSWDKETLPSSPSQGPQASITHPRMPGARSLPLSHPLNHLQQSHLLPNGLELPFMMMPHPLIPVSLPPASVTMAMSQMNHLSTIANMAAAAQVQSPPSRVETSVIKERVPDSPSPAPSLEEGRRPGSHPSSHRSSSVSSSPARTESSSDRIPVHQNGLSMNQMLMGLSPNVLPGPKEGDLAGHDMGHESKRMHIEKDETPLSTPTARDSLDKLSLTGHGQPLPPGFPSPFLFPDGLSSIETLLTNIQGLLKVAIDNARAQEKQVQLEKTELKMDFLRERELRETLEKQLAMEQKNRAIVQKRLKKEKKAKRKLQEALEFETKRREQAEQTLKQAASTDSLRVLNDSLTPEIEADRSGGRTDAERTIQDGRLYLKTTVMY", "text": "FUNCTION: Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator of SIX1, SIX6 and probably SIX5. Corepression of precursor cell proliferation in myoblasts by SIX1 is switched to coactivation through recruitment of EYA3 to the SIX1-DACH1 complex. Transcriptional activation seems also to involve association of CREBBP. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter (By similarity). Inhibits TGF-beta signaling through interaction with SMAD4 and NCOR1. Binds to chromatin DNA via its DACHbox-N domain (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DACH/dachshund family."}
+{"protein": "MLPQTALLLLMSLNLVHGVFYTERYQTPTGIKGPPSNTKTQFFIPYAIKGKGVSLRGEQGIPGPPGPAGPRGHPGPSGPPGKPGTGSPGPQGQPGLPGPPGPSATGKPGLPGLPGKQGERGLNGPKGDIGPAGLPGPRGPPGPPGIPGPAGISVPGKPGPQGPTGEPGPRGFPGEKGTSGVPGLNGQKGEMGHCTPCRPGERGLPGPQGPTGPPGPPGVGKRGENGLPGQPGLKGDQGVPGERGAAGPSGPQGPPGEQGPEGIGKPGAPGIPGQPGIPGMKGQPGAPGTAGLPGAPGFGKPGLPGLKGQRGPVGLPGSPGAKGEQGPAGHPGEAGLPGPSGNMGPQGPKGIPGNPGLPGPKGEMGPVGPAGNPGAKGERGSSGLDGKPGYPGEPGLNGPKGNPGLPGPKGDPGIAGSPGLPGPVGPAGAKGVPGHNGEAGPRGVPGIPGTRGPIGPPGIPGFPGSKGDVGTPGPPGPAGIAVKGLNGPTGPPGPPGPRGNAGEPGLPGPPGPPGPPGQVALPEDFVKAGQRPFVSANQGVTGMPVSAFTVILSKAYPAIGTPIPFDKILYNKQQHYDPRTGIFTCKIPGIYYFSYHIHVKGTHAWVGLYKNGTPVMYTYDEYIKGYLDQASGSAVIDLTENDQVWLQLPNAGSNGLYSPEYVHSSFSGFLVAPM", "text": "FUNCTION: Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
+{"protein": "MAEICKMKYTVLDSPLGKIELSGCERGLHGIRFLSGKTPNTDPTEAPACPEVLGGPEGVPEPLVQCTAWLEAYFHEPAATEGLPLPALHHPVFQQDSFTRQVLWKLLKVVKFGEMVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVIRSDGAIGNYSGGGQTVKEWLLAHEGIPTGQPASKGLGLIGSWLKPSFESSSPKPSG", "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: Nucleus. SIMILARITY: Belongs to the MGMT family."}
+{"protein": "MMGRSPGFAMQHIVGVPHVLVRRGLLGRDLFMTRTLCSPGPSQPGEKRPEEVALGLHHRLPALGRALGHSIQQRATSTAKTWWDRYEEFVGLNEVREAQGKVTEAEKVFMVARGLVREAREDLEVHQAKLKEVRDRLDRVSREDSQYLELATLEHRMLQEEKRLRTAYLRAEDSEREKFSLFSAAVRESHEKERTRAERTKNWSLIGSVLGALIGVAGSTYVNRVRLQELKALLLEAQKGPVSLQEAIREQASSYSRQQRDLHNLMVDLRGLVHAAGPGQDSGSQAGSPPTRDRDVDVLSAALKEQLSHSRQVHSCLEGLREQLDGLEKTCSQMAGVVQLVKSAAHPGLVEPADGAMPSFLLEQGSMILALSDTEQRLEAQVNRNTIYSTLVTCVTFVATLPVLYMLFKAS", "text": "FUNCTION: Mitochondrial potassium channel located in the mitochondrial inner membrane (PubMed:31435016). Together with ABCB8/MITOSUR, forms a protein complex localized in the mitochondria that mediates ATP- dependent potassium currents across the inner membrane (that is, mitoK(ATP) channel) (PubMed:31435016). May contribute to the homeostatic control of cellular metabolism under stress conditions by regulating the mitochondrial matrix volume (PubMed:31435016). SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein."}
+{"protein": "MRDGEGIWGRGRTGGHAHPKEAMHTTFFILGGTMLIGVISDTHLYDRAFELPKAVFDEFSNVDLIIHCGDVTDKEILDSLKDLAKVVAVKGNMDYLNLPRKEILEINDIKIGVIHGDVVYPRGDRLKLRLLGKEMGVDVLISGHTHTPFIDDCRDILLLNPGSPTVPRCPLKSIMKLSVEDKLEAKLIPIEE", "text": "SIMILARITY: Belongs to the metallophosphoesterase superfamily. YfcE family."}
+{"protein": "MNDPRSKMMISPGLLPTESLLDSLILISNEVSSMQKFPLVQIKNVSSMIRRIKLLSSLFEEIQESDSPLPPSSILCFIEIFSVITRVKVLIQECTDGSSLWSLIQLDFISNQFFVLVKEMGRALDILPLNLLNVAQDIKEQVDLLHKQSKRVELELFIDPREVQRRENLFEVMSKNCLQNKKTNNNKGFIDFVKVEEIMCSIGLRTLSDYVEEISKLEVEAQNQAGTGGLIVVSNINNLMSLVSYTKSMVFRNDGESEECKPISMFLYNKSKIHDNDSSSSSSFSQSMMTVNIPDEFRCPISLDLMRDPVIVSSGHTYDRISIAEWINSGHHTCPKSGQRLIHTALIPNYALKSLVHQWCYENNVKMNEAITKNNNSSSKRHKNENAIDHISENKASKDAVKMTAEFLVGKLATGSTDIQRQSAYEIRLLAKTGMDNRRIIAEVGAIPFLVTLLVSKDSRIQEHVVTALFNLSIYDNNKILIMAAGAIDNIVEVLEFGKTMEARENAAAAIYSLSMIDDCKVQIGASSRAIPALVGLLKEGTIIGKRDAATALFNLAVYNPNKLSIVKSGAVTLLVELLMDDKAGITDDSLAVLAVLLGCSEGLEEIKNSKSLVPLLIDLLRFGSVKGKENSITLLLGLCKEEGELVAMRLLANPRSIPSLQSLAADGSLRARRKADALLRLLNRCCSQPHHSL", "text": "FUNCTION: Exhibits U-box-dependent E3 ubiquitin ligase activity in vitro (PubMed:20971894, PubMed:26839127). Negatively modulates successive stages of infection and development of rhizobial (e.g. Sinorhizobium meliloti) and arbuscular mycorrhizal fungi (AM, e.g. Rhizophagus irregularis) symbioses, in an ubiquitin ligase activity- dependent manner (PubMed:26839127). Negative regulator of the LYK3 signaling pathway leading to nitrogen-fixing symbiosis (eg. infection and nodulation) by rhizobia. May be involved in the discrimination of rhizobium strains producing variant Nod factors (PubMed:20971894). SUBCELLULAR LOCATION: Cell membrane."}
+{"protein": "MTQQRQMDLAGFFSAGNVTHAHGAWRHTDASNDFLSGKYYQHIARTLERGKFDLLFLPDGLAVEDSYGDNLDTGVGLGGQGAVALEPASVVATMAAVTEHLGLGATISATYYPPYHVARVFATLDQLSGGRVSWNVVTSLNDAEARNFGINQHLEHDARYDRADEFLEAVKKLWNSWDEDALVLDKAAGVFADPAKVHYVDHHGEWLNVRGPLQVPRSPQGEPVILQAGLSPRGRRFAGKWAEAVFSLAPNLEVMQATYQGIKAEVDAAGRDPDQTKIFTAVMPVLGESQAVAQERLEYLNSLVHPEVGLSTLSSHTGINLAAYPLDTPIKDILRDLQDRNVPTQLHMFAAATHSEELTLAEMGRRYGTNVGFVPQWAGTGEQIADELIRHFEGGAADGFIISPAFLPGSYDEFVDQVVPVLQDRGYFRTEYQGNTLRDHLGLRVPQLQGQPS", "text": "FUNCTION: Catalyzes the second step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Metabolizes DBT-sulfone (DBTO2 or DBT 5,5-dioxide) to 2-(2'-hydroxyphenyl)benzene sulphinate (HBPS). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family."}
+{"protein": "MCLTRSDVYAYVRETINKRKHEVDVSNVLAHIFEFDFQEHVEYIRANIDKALITVGGEQPYCKRLSYHIKRINKIFNLITSLETEYKAAVSKYDGDKHHYERSN", "text": "FUNCTION: Involved in late/very late gene activation. SIMILARITY: Belongs to the baculoviridae LEF-11 family."}
+{"protein": "MEKSSSCESLGSQPAAARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSADNFSPDLRVLRESNKLAEMEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNNLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKINERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPKRTVSLWSYINSQLEDFTNPLYGSYSNHVLYPVASMRHLELWVGYYIRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERASSPAQCVTPVQTVV", "text": "FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3- phosphate and phosphatidylinositol 3,5-bisphosphate (PubMed:11733541, PubMed:12668758, PubMed:21372139, PubMed:14690594). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5- trisphosphate (By similarity). Stabilizes SBF2/MTMR13 at the membranes (By similarity). Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein (By similarity). SUBCELLULAR LOCATION: Cytoplasm Early endosome membrane; Peripheral membrane protein Cytoplasm, perinuclear region Cell projection, axon Endosome membrane; Peripheral membrane protein Note=Partly associated with membranes (PubMed:12668758, PubMed:15998640, PubMed:21372139). Localizes to vacuoles in hypo- osmotic conditions (By similarity). SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily."}
+{"protein": "MDPLLLIGAITAGGVLIGGGVHFVPVGGAPAAMATATGVGTGTAMLAAGAGLTGLITAAAMTGQSPLMIMAAGAVGSMLMIGITMLVGNLIYVYGVGTVPVSAKVAVDPLTGMEQEKYVTPGTEGHGLPTVCFVSGIIGGALGGIGGGLIYWALNEALKTLSYGAIGAAGVAAIFAVGIFFINAVIASYNIGGTIEGFHDPKFKRIGRGIVACLIASIVAGALSTLLVYGGVF", "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 MtrD family."}
+{"protein": "MAAVDSVAQALAYLQVHSPQDGTSMYDHLVKLVSKVLEDQPKNAVDLLETSLLVKKSTFDPKESSPLVPIPVAPDATQTQAAVSIFGDPELPINPATGEPVPADPPNEFEAENMLGAAAVLDCLGVGLGRELGVNIALAAKRIGEDPKLAVRSVRFFGKFLGLYSDYFVFEVAFKKEAAKEAAPAAPAPERVEGEAASSSAPEVPVEEPGKGANKFTYLVCSSLGGPLTRLPDVTPAQVKASRRIKKLLTGRLTSHVSTYPAFPGNEANYLRALIARISAATVVAPSDLFSLNDETGELERAEDWEPPAGREMAAPTAWVHVRPHLKSQGRCEVHKRELPEDADEDEFYNEDELEEGPDLLAALEEDAQLPGEQAAWTPIYSSASEAVKTQAGGLRSLVWPGAVCGGRGSEWTCVYVGWGVKNAPFVPLPPPPVAQEFAWGEVETQELELKPAPPPPEEEAEADE", "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. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme. Note=Radial spoke. SIMILARITY: Belongs to the flagellar radial spoke RSP4/6 family."}
+{"protein": "MSNRVVCREASHAGSWYTASGPQLNAQLEGWLSQVQSTKRPARAIIAPHAGYTYCGSCAAHAYKQVDPSITRRIFILGPSHHVPLSRCALSSVDIYRTPLYDLRIDQKIYGELWKTGMFERMSLQTDEDEHSIEMHLPYTAKAMESHKDEFTIIPVLVGALSESKEQEFGKLFSKYLADPSNLFVVSSDFCHWGQRFRYSYYDESQGEIYRSIEHLDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQKNGMNMSFSFLNYAQSSQCRNWQDSSVSYAAGALTVH", "text": "FUNCTION: May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration. FUNCTION: May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). SIMILARITY: Belongs to the MEMO1 family."}
+{"protein": "MPLYEGLGSGGEKTAVVIDLGEAFTKCGFAGETGPRCIIPSVIKKAGMPKPIKVVQYNINTEELYSYLKEFIHILYFRHLLVNPRDRRVVVIESVLCPSHFRETLTRVLFKYFEVPSVLLAPSHLMALLTLGINSAMVLDCGYRESLVLPIYEGIPVLNCWGALPLGGKALHKELETQLLEQCTVDTGAAKEQSLPSVMGSIPEGVLEDIKVRTCFVSDLTRGLKIQAAKFNIDGNTERPSPPPNVDYPLDGEKILHVLGSIRDSVVEILFEQDNEEKSVATLILDSLMQCPIDTRKQLAENLVIIGGTSMLPGFLHRLLAEIRYLVEKPKYKKTLGTKTFRIHTPPAKANCVAWLGGAIFGALQDILGSRSVSKEYYNQTGRIPDWCSLNNPPLEMVFDVGKSQPPLMKRAFSTEK", "text": "FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family."}
+{"protein": "MSGNTTLLLSNPTNVLDNSSVLNVSVSPPVLKWETPTFTTAARFRVAATLVLFVFAAASNLSVLLSVTRGRGRRLASHLRPLIASLASADLVMTFVVMPLDAVWNVTVQWYAGDAMCKLMCFLKLFAMHSAAFILVVVSLDRHHAILHPLDTLDAGRRNRRMLLTAWILSLLLASPQLFIFRAIKAKGVDFVQCATHGSFQQHWQETAYNMFHFVTLYVFPLLVMSLCYTRILVEINRQMHRSKDKAGEPCLRRSGTDMIPKARMKTLKMTIIIVASFVICWTPYYLLGIWYWFQPQMLHVIPDYVHHVFFVFGNLNTCCDPVIYGFFTPSFRADLSRCFCWRNQNASAKSLPHFSGHRREVSGEAESDLGSGDQPSGQ", "text": "FUNCTION: Receptor for gonadotropin releasing hormone II (GnRH II). 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": "MYHLKCIECGAEYSRDEVIYTCSKCDGLLDVIYDYSSIKIDMEKLKTECPSVWKYAKLLPVEREPVTIQEGGTPLYKCDRLAEKIGIKKLYVKHEGMNPTGSFKDRGMTVGVTKALELGMNTVACASTGNTSAALAIYGAKAGIPVVVLLPAGKVALGKVAQALMHGAKVLSIRGNFDDALALVRTLCSQEKIYLLNSINPYRLEGQKTIGFEIADQLDFKVPDRIVLPVGNAGNITAIYKGFREFKILGITDSLPKMTGIQAEGSCPIVKAIKSGAPAITPEENPETVATAIRIGNPVNATKALSAIRESGGTAESVTDEEILAAQKDLARLEGIGVEPASAASVAGLRKLVDMGVIGRDETVVCITTGHLLKDPQTVIDVCEEPTVVDANIDAIREAIFGKAK", "text": "FUNCTION: Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. Does not catalyze the conversion of O-acetyl-L-homoserine into threonine. SIMILARITY: Belongs to the threonine synthase family."}
+{"protein": "MQKYVCNVCGYEYDPAEHDNVPFDQLPDDWCCPVCGVSKDQFSPA", "text": "FUNCTION: Electron acceptor for cytoplasmic lactate dehydrogenase. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rubredoxin family."}
+{"protein": "MPPSAGLATESLPAATCPAKKDAYAAAASPESETKLAAGDERAPLVRTTRISTTTIKLYRLTIFVRIAIFVLFFKWRITYAARAISSTDAGGIGMSKAATFWTASIAGELWFAFMWVLDQLPKTMPVRRAVDVTALNDDTLLPAMDVFVTTADPDKEPPLATANTVLSILAAGYPAGKVTCYVSDDAGAEVTRGAVVEAARFAALWVPFCRKHGVEPRNPEAYFNGGEGGGGGGKARVVARGSYKGRAWPELVRDRRRVRREYEEMRLRIDALQAADARRRRCGAADDHAGVVQVLIDSAGSAPQLGVADGSKLIDLASVDVRLPALVYVCREKRRGRAHHRKAGAMNALLRASAVLSNAPFILNLDCDHYVNNSQALRAGICFMIERRGGGAEDAGDVAFVQFPQRFDGVDPGDRYANHNRVFFDCTELGLDGLQGPIYVGTGCLFRRVALYGVDPPRWRSPGGGVAADPAKFGESAPFLASVRAEQSHSRDDGDAIAEASALVSCAYEDGTAWGRDVGWVYGTVTEDVATGFCMHRRGWRSAYYAAAPDAFRGTAPINLADRLHQVLRWAAGSLEIFFSRNNALLAGGRRRLHPLQRAAYLNTTVYPFTSLFLMAYCLFPAIPLIAGGGGWNAAPTPTYVAFLAALMVTLAAVAVLETRWSGIALGEWWRNEQFWMVSATSAYLAAVAQVALKVATGKEISFKLTSKHLASSATPVAGKDRQYAELYAVRWTALMAPTAAALAVNVASMAAAGGGGRWWWWDAPSAAAAAAAALPVAFNVWVVVHLYPFALGLMGRRSKAVRPILFLFAVVAYLAVRFLCLLLQFHTA", "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": "MTSGESKTSLKNAYPAAKKLLPKVEEEGEAEEYCTPGAFELERLFWKGSPQYTHVNEVWPKLYIGDEATALDRYGLQKAGFTHVLNAAHGRWNVDTGPDYYRDMAIEYHGVEADDLPTFDLSIFFYPAAAFIDAALRYEHSKILVHCAMGRSRSATLVLAYLMIHRNMTLVDAIRQVAKNRCVLPNRGFLKQLRELDKQLVQQRRGAQHRGEAGEKAGEKEP", "text": "FUNCTION: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (By similarity). Involved in the modulation of intracellular signaling cascades. In skeletal muscle regulates systemic glucose homeostasis by activating, AMPK, an energy sensor protein kinase. Affects MAP kinase signaling though modulation of the MAPK1/2 cascade in skeletal muscle promoting muscle cell differentiation, development and atrophy (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
+{"protein": "MGAGVLVLGASEPGNLSSAAPLPDGAATAARLLVPASPPASLLPPASESPEPLSQQWTAGMGLLMALIVLLIVAGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARGLVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLGGPARPPSPSPSPVPAPAPPPGPPRPAAAAATAPLANGRAGKRRPSRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRELVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAARRRHATHGDRPRASGCLARPGPPPSPGAASDDDDDDVVGATPPARLLEPWAGCNGGAAADSDSSLDEPCRPGFASESKV", "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. Involved in the regulation of sleep/wake behaviors (PubMed:31473062). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome. Note=Colocalizes with RAPGEF2 at the plasma membrane (By similarity). Localized at the plasma membrane. Found in the Golgi upon GOPC overexpression. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB1 sub-subfamily."}
+{"protein": "MTVRYQIEQLGDSAMMIRFGEEINEQVNGIVHAAAAYIEEQPFPGFIECIPAFTSLTVFYDMYEVYKHLPQGISSPFESVKRDVEERLAEIAEDYEVNRRIVEIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHTNGEYVVYMLGFAPGFPFLGGMSKRIAAPRKSSPRPSIPAGSVGIAGLQTGVYPISTPGGWQLIGKTPLALFRPQENPPTLLRAGDIVKFVRISEKDYHAYKEESN", "text": "FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate (PubMed:28830929). In addition, is a potent inhibitor of the autophosphorylation reaction of kinase A (kinA) and its reverse reaction, but does not inhibit phosphate transfer to the Spo0F response regulator once kinase A is phosphorylated. Is an inhibitor of the catalytic domain of kinase A affecting the ATP/ADP reactions and not the phosphotransferase functions of this domain. The inhibition is non- competitive with respect to ATP (PubMed:9334321). SIMILARITY: Belongs to the PxpB family."}
+{"protein": "MLIGVSGTKFCGCEDVINMLVDHFHFELLNHLDNPEEILDYATKNYTKNSVIFLEKLSLLEKLEKRPFFVHLSIDAPVTTRVALYRKTTQAESLSLEQIIQAIDQHDFQPEGIKLREKSHLRFKIVNEDRRGRRQSLINNITTQLKILDDKEKQMAPLMRPSWDSYFMKLATLAASRSNCMKRRVGCVIVRECRVIATGYNGTPRHLTNCFNGGCPRCNDGDSRNLHTCLCLHAEENALLEAGRDRVGQNATLYCDTCPCLTCSVKIVQTGISEVVYSQSYRMDEESFKVLKNAGITVRQFSFTEEPRIVMI", "text": "FUNCTION: Catalyzes the hydrolytic deamination of dCMP to yield dUMP, the nucleotide substrate for thymidylate synthetase. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
+{"protein": "MADRINESHQRFLQALMSHGIMEGSAVRALHRHCCELHKVHYMHDKLDDFVGVLNRHLQPLFMTIEKGVGEEDGLTYYALVNRVENDITKMASDYAENELELFRKTMELIILSDNGFATSISILNLADELQSKKMKKKEVEQLLQSFVQEKWLIGRNGEYTLHTRCIMELEHYIRNTYQDVAKICNVCRKVAIQSQLCENCGIPLHLQCAGKYFHGKANPTCPNCNESWPHEIPDLNQVSSQGPSHSQTETVRGRNQRSKNTSTASRTSR", "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": "MIKMTGVQKFFDDFQALTDINLEVPAGQVVVVLGPSGSGKSTLCRTINRLETIEEGTIEIDGKLLPEEGKDLAKIRADVGMVFQSFNLFPHLTIKDNVTLGPMKVRKMKKSEANEVAMKLLERVGIANQAEKYPAQLSGGQQQRVAIARALAMNPKIMLFDEPTSALDPEMVNEVLDVMASLAKEGMTMVCVTHEMGFARRAADRVLFMSDGAIVEDSDPETFFTNPQTDRAKDFLGKILAH", "text": "FUNCTION: Part of the ABC transporter complex GluABCD involved in glutamate uptake. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MRLLIEQPRTMSSGSSNFLLVPIPEYPVLDCVPNKNVKIVVLGASNVGKTALIVRFLTKRFIGDYEANTGALYSRKINLDGEQVSLQVQDTPCVSLQDDADGLYCQEQINRSIYWADGYVLVFSITDLNSYRTIQPLYQHVRRIHPSGNIPVIIVGNKSDLLRARQVSDPEGKALADELGGLYFEASARENHESVQAAFLHLCQEVSRALGGGNGEKRKGGLHLARPKSPNMQELKRRFRQVLSSKVKSATAL", "text": "FUNCTION: Regulator of rDNA transcription. SUBCELLULAR LOCATION: Nucleus, nucleolus Note=Associates with rDNA transcription unit throughout the cell cycle. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MNDVDASIEPKRIKEVRAYVVKGGGADYHDQSSEHWILGYIATPISIYPEYRASRASWGLNVLGSVVVEVESSDGEVGFGISTGGYPAAWIIENHLSRFVVGKYVGEVEKTWDQMFKATIYYGRRGIVMNAISAVDLALWDLMGKVRGLPVYDLLGGPVRDELTFYATGPRPDVAKSLGFIGGKLPLIHGPADGIEGLRENVRIFKEAREKVGDDFLLMYDCWMSLDLPYAQRLLSELKPYGLFWIEEPFIPDDYWSFGALANIAPPTLVASGEHESTVHGFRLLLELGKVNVIQPDVTWVGGVTPMIKIAALAEAYGAWVIPHGSSVYGYHFIITRVNSPFAEYLVVSPDATKIVPQFHPLLRDEPIPQNGKVRLSRKPGFGVELNRDLLVRPFKST", "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": "MLSARSAQCMVSMATRSCVSRGSAGSAAAGPVEAAIRAKLEQALSPEVLELRNESGGHAVPAGSETHFRVAVVSSRFEGMSPLQRHRLVHEALSEELAGPVHALAIQAKTPAQWRENPQLDISPPCLGGSKKTRGTS", "text": "FUNCTION: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates (Fe-S) cluster insertion into a subset of mitochondrial proteins (By similarity). Probably acts together with the monothiol glutaredoxin GLRX5. May protect cells against oxidative stress (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the BolA/IbaG family."}
+{"protein": "MALTNTTITSWKLQEIVAHSSNVSSLVLGKSSGRLLATGGEDCRVNIWAVSKPNCIMSLTGHTSAVGCIQFNSSEERVVAGSLSGSLRLWDLEAAKILRTLMGHKASISSLDFHPMGEYLASGSVDSNIKLWDVRRKGCVFRYKGHTQAVRCLAFSPDGKWLASASDDSTVKLWDLIAGKMITEFTSHTSAVNVVQFHPNEYLLASGSADRTVKLWDLEKFNMIGSSEGETGVVRSVLFNPDGSCLYSGSENTLRVYGWEPDRCFDVVHVGWGKVSDLAISNNQMIAVSYSHTNVSWYVVDLNRVKKSGSVIQGLIQDKPIPAPSSALGTTLRRNYERPTTSCTGQEMKQSSEADRRSPEGERRSPSSEDEKEDKESSAEITNPEDYKEIFQPRSVISRTPPKTTEPFPAPLEHSFSESVLEKPGPVVKIVTPVIDRAGQLKGPITSSTPVQRVEPTVIAAAPRPVAVVTTSASSPSRPVVNTTKPKPSTGIILSTRNEPIGLNAGDFLSHARNAKASAMGDEEALAQIRKGHDTMCVMLSSRSKNLDSVRSVWASGDVKTSLDSAVSMNDLSIVVDVLNIINLKPSLWKLDLCTSILPQIEELLQSRYESYVQTGCMSLKLILKRFWPLISDTLNAPPSVGVDITREERHQKCKACYKQLKNLSNVVKNRAEQVGRHGSTFRELQLLMAPLDY", "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": "MSGDILQTPDAPKPQGALDNYFKITARGSTVRQEVLAGLTTFLAMVYSVIVVPGMLGKAGFPPAAVFVATCLVAGFGSLLMGLWANLPMAIGCAISLTAFTAFSLVLGQQISVPVALGAVFLMGVIFTAISVTGVRTWILRNLPMGIAHGTGIGIGLFLLLIAANGVGMVIKNPIEGLPVALGAFTSFPVMMSLLGLAVIFGLEKCRVPGGILLVIIAISIIGLIFDPAVKYHGLVAMPSLTGEDGKSLIFSLDIMGALQPTVLPSVLALVMTAVFDATGTIRAVAGQANLLDKDNQIINGGKALTSDSVSSIFSGLVGAAPAAVYIESAAGTAAGGKTGLTATVVGALFLLILFLSPLSFLIPGYATAPALMYVGLLMLSNVSKLDFNDFIDAMAGLVCAVFIVLTCNIVTGIMLGFVTLVVGRVFAREWQKLNIGTVIITAALVAFYAGGWAI", "text": "FUNCTION: High-affinity transporter for guanine and hypoxanthine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily."}
+{"protein": "MKTINSVDTKEFLNHQVANLNVFTVKIHQIHWYMRGHNFFTLHEKMDDLYSEFGEQMDEVAERLLAIGGSPFSTLKEFLENASVEEAPYTKPKTMDQLMEDLVGTLELLRDEYQQGIELTDKEGDNVTNDMLIAFKASIDKHIWMFKAFLGKAPLE", "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. Does not bind to DNA (By similarity). Dps is important for full resistance to heat and cold shocks and is essential for full virulence of this bacterium. It seems to play a direct or indirect role on the production and/or stability of listeriolysin O. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Dps family."}
+{"protein": "MAQCVQTTTILEQKEEKTVTLLVPQAGKRKFEIVYFNIITFAYWHIAGLYGLYLCFTSTKWATVLFSFFLFVVAEVGVTAGSHRLWSHKTYKAKLPLQILLMVMNSLAFQNTVIDWVRDHRLHHKYSDTDADPHNASRGFFYSHVGWLLVRKHPDVKKRGKEIDISDIYNNPVLRFQKKYAIPFIGAVCFVLPTLIPVYGWGETWTNAWHVAMLRYIMNLNVTFLVNSAAHIYGKRPYDKKILPSQNIAVSIATFGEGFHNYHHVFPWDYRAAELGNNSLNFPTKFIDFFAWIGWAYDLKTVSKEMIKQRSKRTGDGTNLWGLEDVDTPEDLKNTKGE", "text": "FUNCTION: Catalyzes the formation of delta(11) fatty acyl precursors in the pheromone gland, and has high activity towards palmitic acid and stearic acid. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
+{"protein": "MAGSALAVRARFGVWGMKVLQTRGFVSDSSDSMDTGAGSIREAGGAFGKREKAEEDRYFREKTKEQLAALRKHHEDEIDHHSKEIERLQKQIERHKKKIQQLKNNH", "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": "MGGVLSYFRGLLGSREMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVEQVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSADRDRIGISKDELLYMLREEELAGAILVVLANKQDMDGCMTVAEVHHALGLENLKNRTFQIFKTSATKGEGLDQAMDWLSNTLQSRK", "text": "FUNCTION: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
+{"protein": "MAASTRALFLSCFHGSGGGGGTSEVSRRLVLRPRYPSMPRRPRSAAVAGEGGEGGGGGGDGDLEAAAVGAEEEEKVAVFEVSGMTCAACAGSVEKAVKRLQGIHDAAVDVLGGRAQVVFYPAFVSEEKIRETIQDVGFEAKLIDEEVKEKNILVCRLHIKGMTCTSCASTVESILQVVPGVQRASVALATEEAEIRYDRRIVTASQLTHAVEETGFEAILITTGDDQSRIDLKVDGTLNERSIMIVKSSVQALPGVEDIKVDPELHKITISYKPDQTGPRDLIEVIESAASGDLTVSIYPEADGRQQHRHGEIKRYRQSFLWSLVFTIPVFLTSMVFMYIPGLKDGLEKKVINMMSIGELLRWILSTPVQFVIGRRFYTGAYKALSHGSSNMDVLIALGTNTAYFYSVYSILRAASSHNYMATDFFETSSMLISFILLGKYLEILAKGKTSEAIAKLMDLAPETATMLIYDHEGNVVGEKEIDSRLIQKNDVIKVVPGGKVASDGFVIWGQSHVNESMITGESRPVAKRKGDTVIGGTVNENGVLHVRATFVGSESALAQIVRLVESAQMAKAPVQKFADQISRVFVPLVIILSLLTWLAWFLAGRLHGYPNSWIPSSMDSFQLALQFGISVMVIACPCALGLATPTAVMVATGVGASQGVLIKGGQALESAQKVDCIVFDKTGTLTIGKPVVVNTRLLKNMVLREFYAYVAAAEVNSEHPLGKAVVEHAKKFHSEESHVWTEARDFISVTGHGVKAKISGRAVMVGNKSFMLTSGIDIPVEALEILTEEEEKAQTAIIVAMDQEVVGIISVSDPIKPNAREVISYLKSMKVESIMVTGDNWGTANAISKEVGIENTVAEAKPEQKAEKVKELQSAGRTVAMVGDGINDSPALVSADVGLAIGAGTDVAIEAADIVLMKSNLEDVITAIDLSRKTFFRIRMNYVWALGYNIIGIPIAAGVLFPSTRFRLPPWVAGAAMAASSVSVVCWSLLLRYYKSPKLGR", "text": "FUNCTION: Copper (Cu) transporter that plays an essential role in promoting translocation of Cu from roots to shoots. Involved in loading Cu to the xylem of the roots and other organs, including panicles. 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": "MADQLTEEQVTEFKEAFSLFDKDGDGCITTRELGTVMRSLGQNPTEAELRDMMSEIDRDGNGTVDFPEFLGMMARKMKDTDNEEEIREAFRVFDKDGNGFVSAAELRHVMTRLGEKLSDEEVDEMIRAADTDGDGQVNYEEFVRVLVSK", "text": "FUNCTION: May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates. SIMILARITY: Belongs to the calmodulin family."}
+{"protein": "MSGSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPNNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDSYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLINAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQRFWENSMLTDPGNVQKVVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLLNMLRLGKSEPWTLALENVVGAKNMNVRPLLDYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGNKAYEWNDNEIYLFRSSVAYAMRKYFLEVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVVLIFTGIRDRKKKNKARNEENPYASIDISKGENNPGFQNTDDVQTSF", "text": "FUNCTION: Essential counter-regulatory carboxypeptidase of the renin- angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity. SUBCELLULAR LOCATION: [Processed angiotensin-converting enzyme 2]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cytoplasm Cell projection, cilium Apical cell membrane Note=Detected in both cell membrane and cytoplasm in neurons. SIMILARITY: Belongs to the peptidase M2 family."}
+{"protein": "MEPHLLGLLLGLLLSGTRVLAGYPIWWSLALGQQYTSLASQPLLCGSIPGLVPKQLRFCRNYIEIMPSVAEGVKLGIQECQHQFRGRRWNCTTIDDSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGTSTICGCDSHHKGPPGEGWKWGGCSEDADFGVLVSREFADARENRPDARSAMNKHNNEAGRTTILDHMHLKCKCHGLSGSCEVKTCWWAQPDFRAIGDFLKDKYDSASEMVVEKHRESRGWVETLRAKYALFKPPTERDLVYYENSPNFCEPNPETGSFGTRDRTCNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCVFHWCCYVSCQECIRIYDVHTCK", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Required for normal gastrulation, formation of the primitive streak, and for the formation of the mesoderm during early embryogenesis (PubMed:10431240). Required for normal formation of the apical ectodermal ridge and for normal embryonic limb development (PubMed:12569130). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MKRYILATAIASLVAAPAMALAAGSNILSVHILDQQTGKPAPGVEVVLEQKKDNGWTQLNTGHTDQDGRIKALWPEKAAAPGDYRVIFKTGQYFESKKLDTFFPEIPVEFHISKTNEHYHVPLLLSQYGYSTYRGS", "text": "FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily."}
+{"protein": "MDAVNENGKRAMKDDSHGNSTSPKRRKSRHISALILARGGSKGIPLKNIKMLAGVPLIGWVIRAAVDSNVFNSVWVSTDHEEIAKVALAWGAKVHKRSPEVSQDSSSSLDTIREFSRQHREVDVICNIQATSPCLHPKHLTEAVELITKQGYDSVFSVVRRHNFRWKEVEKGGDCSTEPMNLNPACRPRRQDWSGELCENGSFYFAKKELIEQGLLQGGKKTYYEMKPEYSVDIDVDIDWPVAEQRVLRFGYFGKDKPEVVRLLLCNVSGCLTDGQIYTSASGEEMVSINIRDQIGISMLKKEGVKVILLETYPIAKALAVRLSERMGCPLLHHMDDKLKEVERIMVEEKLEWKEVAYLGNDEADVKCLELAGLSGVPVDAPTVALNHTKYTCHNAAGHGAVREFAEHILLLKKKAKSQMEQDRICRDAF", "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. Also has activity towards N-glycolylneuraminic acid (Neu5Gc). Has weak activity towards 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CMP-NeuNAc synthase family."}
+{"protein": "MKAARFVMRSARSLSSAGLVPREVEHFSRYSPSPLSMKQLLDFGSENACERTSSAFLRQELPVRLANILKEIDILPDRLVNTSSVQLVKSWYIQSLMELVEFHERSPDDQKVLSDFVDTLITVRNRHHNVVPTMAQGIIEYKDSCTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDSQTGNPSHIGSIDPNCNVAAVVQDAFECSRMLCDQYYLTSPELKLTQVNGKFPGEPIHIVYVPSHLHHMLFELFKNAMRATVEHQENEPSLTPVEVTVVLGKEDLTIKISDRGGGVPLRITDRLFSYMYSTAPTPVMDNSRNAPLAGFGYGLPISRLYAKYFQGDLHLYSLSGYGTDAIIYLKALSSESVEKLPVFNKSAFKHYQMSIEADDWCIPSKEPKNLAKEKVAV", "text": "FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the PDK/BCKDK protein kinase family."}
+{"protein": "MGRAPCCEKVGIKKGRWTAEEDRTLSDYIQSNGEGSWRSLPKNAGLKRCGKSCRLRWINYLRSDIKRGNITPEEEDVIVKLHSTLGTRWSTIASNLPGRTDNEIKNYWNSHLSRKLHGYFRKPTVANTVENAPPPPKRRPGRTSRSAMKPKFILNPKNHKTPNSFKANKSDIVLPTTTIENGEGDKEDALMVLSSSSLSGAEEPGLGPCGYGDDGDCNPSINGDDGALCLNDDIFDSCFLLDDSHAVHVSSCESNNVKNSEPYGGMSVGHKNIETMADDFVDWDFVWREGQTLWDEKEDLDSVLSRLLDGEEMESEIRQRDSNDFGEPLDIDEENKMAAWLLS", "text": "FUNCTION: Modulates overall growth by reducing the proliferation activity of meristematic cells and delaying development (PubMed:18359753). Flavonol-specific transcription activator involved in the regulation of several genes of flavonoid biosynthesis. Activates the expression of CHS, CHI, F3H and FLS1 (PubMed:17419845, PubMed:20731781). Confers tolerance to UV-B (PubMed:19895401). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSAALEDIKLEDIPVDDIDFSDLEKQYSVNDTVSFDQYIVVCGAPVIPEGKVAVLKKALTGLFSKAGKVVDIEFPIEDGKTKGFLFVECASPADGNKIIKAFHTKRLDLKHRLFIYTMRDVEKYNDKNFPTEFVEPEIPDFFPTSTLKSWLSDEDGRDQFVLQANEMTTVLWNSAIEDEESVVESRKNWSTNYIRFSPKGTYLFSYHPQGVVMWGGPHFDRLRRFYHPNVRTSSVSPSEKFLVTYSPDPIVVDEEDADCPFTKKNEGHQLCIWDIDSGLLQSTFPVVKSSYLQWPLVRWSYNDQYCARMVGETLVVHDVKKGFAVMDNKTLKVPGIRDFSFAPTGVKIAPFRANDKESVILAYWTPETNNMSCKATIVDVERSRVLKTVNLVQVSNVTLHWQSDSEFLCFNVERHTKSKKTQFSNLEICKLTEKDIPGDKIELKDCVVDFAWEPHGNRFGVIAVRETGDDNIAIPKNVATFFAPEKRDVKDKSTGVKKWLEVASITDKFSNTISWSPAGRYVVVATLVKPNVRRSDFVFYDMDFATDKNMNVTKDVHASLKEVATNSFPSATDMAWDPSGRFLAVWSSSLKHKMENGYKVFNVAGTIVKEEPLNSFKNFAWRPRPASLLTNAEKKKIRKNLKEWTAQFAEQDAMEADAATRDMILRQREMLKDWTEYRAEIGARFEEEFGYKTFNMIPLSNSEDDFTSVEEVKEEVLEESEEKVVE", "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": "MTFNKIFKYLISLLFLSILFHTIIHKNNLVFSKTMHKKVAFFSFSIFFVWIRHLKRYNSMLEKATFFVLQTSYTNELKGLYIAGNSYPYYQDKKKLVFNSFQKPFKNHQSTKIPRE", "text": "FUNCTION: Putative control of replication message."}
+{"protein": "MDERFNKWLLTPVLTLLFVVIMYQYVSPSCTSSCTNFGEQLRSGEARPPAVPSPARRAQAPLDEWERRPQLPPPPRGPPEGSRGVAAPEDEDEDPGDPEEEEEEEEEEPDPEAPENGSLPRFVPRFNFTLKDLTRFVDFNIKGRDVIVFLHIQKTGGTTFGRHLVKNIRLEQPCSCKAGQKKCTCHRPGKKETWLFSRFSTGWSCGLHADWTELTNCVPAIMEKKDCPRNHSHTRNFYYITMLRDPVSRYLSEWKHVQRGATWKTSLHMCDGRSPTPDELPTCYPGDDWSGVSLREFMDCSYNLANNRQVRMLADLSLVGCYNLTFMNESERNTILLQSAKNNLKNMAFFGLTEFQRKTQFLFERTFNLKFISPFTQFNITRASNVDINDGARQHIEELNFLDMQLYEYAKDLFQQRYHHTKQLEHQRDRQKRREERRLQREHRAHRWPKEDRAMEGTVTEDYNSQVVRW", "text": "FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 6 family."}
+{"protein": "MLKKFDKKDEESGGGSNPLQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAVERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVSKMISKFTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTNNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLEKALQQYTLEPSEKPFDLKSVPLATTPMTEQRPESTSTAAVKQPEKVAATRQEIFQEQLAAVPEFQGLGPLFKSSPEPVALTESETEYVIRCTKHTFSDHLVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLSYVPVRSLPYNQPGTCYTLVALPKEDPTAVACTFSCVMKFTVKDCDPNTGEIDEEGYEDEYVLEDLEVTVADHIQKVMKVNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPENKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSSEELPVDIILASVG", "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. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (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 (By similarity). About 70% of the COPG1-containing coatomers are found in the cis-Golgi apparatus. SIMILARITY: Belongs to the COPG family."}
+{"protein": "MRPEPGGCCCRRPMRANGCVKNGEVRNGYLRSSTATIAAAGQIHHITENGGLYKRPFNEAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRHWRIEKCHHATEREEQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGAKVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQEAAAEVLKTYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAALTYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSMKCIMGQDGTSLGKECIQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRHRPLPLLDRPFDETTYEETED", "text": "FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate (By similarity). Plays an important role in de novo sphyngolipid biosynthesis which is crucial for adipogenesis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MGCFRQTRDDEDDKLRKEANKKIEKQLAKDKLLYRGTHRLLLLGAGESGKSTIVKQMRILHVNGFSPEERKQKIEDIKRNVRDAILTITGAMSTLNPPVQLEHPQNKAKVDYIQDKASQAEFDYPPIFYEYTEILWKDKGVQAAFERSNEYQLIDCAQYFLDRVHIIRQAEYTPSEQDILRCRVLTSGIFETKFSVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVTACSGYNMVLREDATQNRLKESLDLFKSIWNNRWLRTISVILFLNKQDLLAEKVKAGKSKIEDYFPEYARYQVPPDASSEPGEDTEVVRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFDDCRDIIQRMHLRQYELL", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta- adrenergic stimuli. SIMILARITY: Belongs to the G-alpha family. G(s) subfamily."}
+{"protein": "MESPIQIFRGEPGPTCAPSACLLPNSSSWFPNWAESDSNGSVGSEDQQLEPAHISPAIPVIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSAVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLASSVGISAIVLGGTKVREDVDVIECSLQFPDDEYSWWDLFMKICVFVFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITKLVLVVVAVFIICWTPIHIFILVEALGSTSHSTAVLSSYYFCIALGYTNSSLNPVLYAFLDENFKRCFRDFCFPIKMRMERQSTNRVRNTVQDPASMRDVGGMNKPV", "text": "FUNCTION: G-protein coupled opioid receptor that functions as receptor for endogenous alpha-neoendorphins and dynorphins, but has low affinity for beta-endorphins. Also functions as receptor for various synthetic opioids and for the psychoactive diterpene salvinorin A. 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. Plays a role in mediating reduced physical activity upon treatment with synthetic opioids. Plays a role in the regulation of salivation in response to synthetic opioids. May play a role in arousal and regulation of autonomic and neuroendocrine functions. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MAAVQALPLSIDQNTEASGSQSHTNTRSPVTENTMGSVSSLISGRTYHDKQCRASEFSNKCRKPTNMPNCFKQQEGLLKTNYSSQDFLFNGLPTKKPSTTTSGNNGNYVYVNEDFKEEWHDARVPISPSSDAEDIREERSINGNIRGPPPKLIPISGKLEKNVEKTLIKPTAFKPVVPKKRNPSLQYLVQRNGGPGLSESQSSLNLLFNGNSAGIPEKHNSLSCRNIAHSGTMSDSGRTSLSSLPTSNTNCSHQLDSVSVSMGHINLDNHSNLNGYSDRASRGRTRPSNSDSGRSSSSKSTGSPILNDEILIRELEEKLKDREMELQQLKENLDENEAAICQVYEEKQKRCEQEMEELRQSCALKMKQAAQKAQRLQQVLQLQIFQLQQEKKKLQEDFSQLLQERELLEKRCASFEREQTEFGPRLEETKWEVCQKSGEISLLKQQLKDSQAELAQKSNEILLLRSQFREARCDLQISEEQVQELQDTAHTKTLEMEVCENELQRKKNEAELLREKVSKLDQEVASLREAAVASLRHGLCFCHEKEDPFLLYESDEAKAQRQNADNLQGLQQYVERLREALASERSRYQEQAEHFEDERRKWQEEKEKVIRYQKQLQHNYIQMYQQNRELERDIKQLTVELDAREFNEFDLHGAEIHFEEITATEI", "text": "FUNCTION: Negative regulator of katanin-mediated microtubule severing and release from the centrosome. Required for central spindle formation and the completion of cytokinesis. Negative regulator of the Wnt signaling pathway. Represses beta-catenin-mediated transcriptional activation by promoting the nuclear exclusion of beta-catenin. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the LZTS2 family."}
+{"protein": "MFIESFKVESPNVKYTEGEIHSVYNYETTELVHESRNGTYQWIVKPKTVKYEFKTDTHVPKLGVMLVGWGGNNGSTLTGGVIANREGISWATKDKVQQANYFGSLTQASSIRVGSFNGEEIYAPFKSLLPMVNPDDVVFGGWDISNMNLADAMGRAKVLDIDLQKQLRPYMEHMVPLPGIYDPDFIAANQGSRANNVIKGTKKEQVQQIIKDMRDFKEQNKVDKVVVLWTANTERYSNVVVGLNDTAESLMASVERNEAEISPSTLYAIACVFENVPFINGSPQNTFVPGLIDLAIQRNSLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQTFRSKEISKSNVVDDMVASNGILYEPGEHPDHIVVIKYVPYVGDSKRAMDEYTSEIFMGGKSTIVLHNTCEDSLLAAPIILDLVLLAELSTRIQLKAEGEGKFHSFHPVATILSYLTKAPLVPPGTPVVNALSKQRAMLENILRACVGLAPENNMILEYK", "text": "FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1- phosphate in a NAD-dependent manner. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family."}
+{"protein": "MVSTATFFFFVYLTLFVVIGFFSSLFIIPLLGISFVFAIGVVSFGFCSNMSFKMAQLIYVRADAFLKKVLDKMALQTQPAQLQEPQEPLSTLRPVSNPTIPSPLRQTARPSKFVTEEDVIFEPVSAQSAIARSLETAANKAGNKFQLS", "text": "FUNCTION: Involved in spore wall assembly. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OSW5 family."}
+{"protein": "MTPTVLLLILCFGVASGAQAHDPKLDAEWKDWKTKYAKSYSPKEEALRRAVWEENMRMIKLHNKENSLGKNNFTMKMNKFGDQTSEEFRKSIDNIPIPAAMTDPHAQNHVSIGLPDYKDWREEGYVTPVRNQGKCGSCWAFAAAGAIEGQMFWKTGNLTPLSVQNLLDCSKTVGNKGCQSGTAHQAFEYVLKNKGLEAEATYPYEGKDGPCRYRSENASANITDYVNLPPNELYLWVAVASIGPVSAAIDASHDSFRFYNGGIYYEPNCSSYFVNHAVLVVGYGSEGDVKDGNNYWLIKNSWGEEWGMNGYMQIAKDHNNHCGIASLASYPNIF", "text": "SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the peptidase C1 family."}
+{"protein": "MAVPGCNKDSVRAGCKKCGYPGHLTFECRNFLRVDPKRDIVLDVSSTSSEDSDEENEELNKLQALQEKRINEEEEKKKEKSKEKIKLKKKRKRSYSSSSTEEDTSKQKKQKYQKKEKKKEKKSKSKKGKHHKKEKKKRKKEKHSSTPNSSEFSRK", "text": "FUNCTION: Possible splicing regulator involved in the control of cellular survival."}
+{"protein": "SLLFLAAVGSCADDRNPLEECFRETDYEEFLEIAKNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIKKFDLRLNEFSQENENAWYFLQNIKKRVREVNKDPGVLEYPVKPSEVGKSAGQLYEESLRKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARVIEIQQDVKEVTVTYQTSQKETLSVTADYVIVCTTSRAARRITFEPPLPPKKAHALLSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAICRPSMIQRWSLDNYAMGGITTFTPYHFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLRAATDVNRASENK", "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). This enyzme shows activity on L-Leu (PubMed:29024770). This enzyme inhibits platelet aggregation in human platelet rich plasma induced by ADP (IC(50)=3.2 mg/mL), and shows antibacterial activities on both Gram-positive and Gram-negative bacteria (P.aeruginosa, V.cholerae, S.aureus, E.faecalis and E.coli) (PubMed:29024770). These two effects are due to hydrogen peroxide, since they are inhibited by catalase (PubMed:29024770). It also induces edema in mouse paw pads but does not show hemolytic activity (PubMed:29024770). This protein may also have activities in hemorrhage, and apoptosis (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
+{"protein": "MNLPEHGGNLIELSKKAGCNPKEILDFSANINPLGFPEWLRPFLHSKIEDLISYPDPNYTSLKKKIHSKYGICTEQIVLGNGASELILQIPFVVQADYALIAVPCYSGYKEAISLLKIPCIEVTLKEEKQFRLDINELRDVLKSKPDQKALVFLGHPNNPTGVTLDKIEVLKIVQEFQNSVFVIDESFIHFCTNESSFLKDKTENMILIQSMTKILALPGLRIGICYASPLICSNISKRLPTWNVNSIAASVYEKAISDEDYIENSKQNIKIWKEKLIYDLSNLEFLNLFSSEANFILIKILDNKNIFDLTQELLIKYKIAVRNCENFSGLSKNFIRIAVRTPEENKKIIDAFSNIFYGTRQRLKSRKKTPSIMFQGTASNVGKSILTAALCRILSQDGIKVAPFKSQNMALNSFVTLNGEEIGRAQALQAQAAKILPDIRMNPILLKPSNEKDSQVIINGKPLNSMNFKDYDQYKPIAFEEVKKSYDSLASEYNVIIIEGAGSASEVNLKKNDIVNMKMAEYAKADVLLVGNIDHGGLFGSLLGTMETLTEWERKLVFGFIINRFRGAKELLKTGINYIEEYTNKPILGIVPYIKNLKLPEEDSLEFKSGALDDTSKLEERLDVVLIDIPRISNHTDIDALRAEPDVRVRIVRTVEDLGEPDVLILPGSKNVISDLNHLYDVGLVNKIFALSRNQKTDIVGICGGYQMLGKNIFDPYRIESDQGSIQGISLLQIETILEKNKSLKRVFATHIPTKTEVEGYEIHHGKTKSIGNTRVILLNEKAEELGHSDPTGRIWGTYIHGIFDKDEFRRKYLDQIRIRKGKSPLVKVQVSYNLEKSLDRLARYVRQSLNINLIYRKLGLG", "text": "FUNCTION: Catalyzes two activities which are involved in the adenosylcobalamin biosynthesis: 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, and 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 (By similarity). SIMILARITY: In the C-terminal section; belongs to the CobB/CobQ family. CobQ subfamily. SIMILARITY: In the N-terminal section; belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "FRNVESKSCCPNTTGRNIYNTCRLGGGSRERCASLSGCKIISASTCPSDYPKFYCTLGCQSSKCASITTPPNSEVDAEAVRCKAACSNLCDFGVTTNQEIQDD", "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": "MDHHKQLTLQTTLESCNNLYNLLFNSIGSIKPSQQQQQQQQNQKNTNSVTSNTNIINDQEIFKLNKFHLYGENNIDELYNSIELQLQTIKFTCQQYRQWDSTERDSIKFFNTQKLYNQSQQRGNLVSKTLFDCSLLGKIYLNQQKEQQQQQKQKNKQQQQQPQPLVEDLSKNISKTVEVKRKLGLLAGKLQEMTNELNNKYSTFSVLDDLLGLLKSNTEIDYNSDSYVSCNISSSTFLLDIDIYHNGEIKEVKLVHILTTTGEVEPAEQQFNDELTNSLKTDMKEFIKKVQRICDLDLLFRKYKHFDLQKAFSILQSDFLNISINSNIKYIDNKEIEMNKGFGEIKLDCCGVLIKYFQSYIEKISKMNEPYSIMIEMESSAVTNNGSLIDQSEYSRLSLKTLLQKQQHTQPSAQTDYSEQQQQQSISTQLTSIEFNEKDCLDCEPLSSMLESDSIFSPVRLVCKLNKPILITNQQLSKILNLSKIHRSSQQPSQQQPSQQQQQQQQQQQQKKLNSVDESMNENGDSNIIENINELIKKYSIQNLLISSSSSSSSSNDSNISVNVDNSFDCEVYGMKQRYYYTGEFELGIEISRIPIYHPSQVYPTIQLLRQQIVFNILFKSCFQNLNISKSDDHHNIIDNNNDVKIFEITSNPPNSINIIFLHPIDNSFNSIDIFIKNNGDLEAFYYDNTTNIQPNIQKSTLFTKMLIKSLSISVSLACFFKNK", "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": "MRLFSGMNNQYTRREVFCRNTCHDLKHFWEREIGKQTYYRESEERRLGRSALRKLREEWKQRLETKLRLRNNPEDTEKRTNVG", "text": "SIMILARITY: Belongs to the FAM240 family."}
+{"protein": "MTLGTKLSVDQEYLKSFSEKHQEPAWLKNLRLQALEQAEDLPMPKPDKTKITNWNFTNFAKHTVDNEPLSSLEDLTDEVKALIDIENEDKTLYVQRDQTPAHLSLSQELKDKGVIFTDILTAAREHSDLVEKYFMKDGVKVDEHKLTALHAALVNGGAFLYVPKNVQVETPVQAVYVHESNDTALFNHVLIVAEDHSSVTYVENYISTVNPKDAVFNIISEVITGDNASVTYGAVDNLSSGVTTYVNRRGAARGRDSKIEWALGLMNDGDTISENTTNLYGDGTYGDTKTVVVGRGEQTENFTTQIIHFGKASEGYILKHGVMKDSASSIFNGIGKIEHGASKANAEQESRVLMLSEKARGDANPILLIDEDDVTAGHAASVGRVDPIQLYYLMSRGIPKEEAERLVIYGFLAPVVNELPIEGVKKQLVSVIERKVK", "text": "FUNCTION: The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation (By similarity). SIMILARITY: Belongs to the UPF0051 (ycf24) family."}
+{"protein": "MSDVFNSPQARSKISAAFGIKPTAGQDVEELLIPKVWVPPEDPLASPSRLAKFLRENGYKILQPRSLPENEEYETDQILPDLAWMRQIEGPVLKPTLSLPIGDQEYFPKYYPTHRPSKEKPNAYPPDIALLKQMIYLFLQVPEATDNLKDEVTLLTQNIRDKAYGSGTYMGQATRLVAMKEVATGRNPNKDPLKLGYTFESIAQLLDITLPVGPPGEDDKPWVPLTRVPSRMLVLTGDVDGEFEVEDYLPKINLKSSSGLPYVGRTKGETIGEMIAISNQFLRELSALLKQGAGTKGSNKKKLLSMLSDYWYLSCGLLFPKAERYDKSTCCTKTRNKWSAQSSTHLMISMITWPVMSNSPNNVLNIEGCPSLYKFNPFRGGLNRIVEWIMAPDEPKALVYADNIYIVHSNTWYSIDLEKGEANCTRQHMQAAMYYILTRGWSDNGDPMFNQTWATFAMNIAPALVVDSSCLIMNLQIKTYGQGSGNAATFINNHLLSTLVLDQWNLMKQPSPDSEEFKSIEDKLGINFKIERSIDDIRGKLRQLVPLAQPGYLSGGVEPEQPSPTVELDLLGWSATYSKDLGIYVPVLDKERLFCSAAYPKGVENKSLKSKVGIEQAYKVVRYEALRLVGGWNYPLLNKACKNNASAARRHLEAKGFPLDEFLAEWSELSEFGEAFEGFNIKLTVTPESLAELNRPVPPKPPNVNRPVNTGGLKAVSNALKTGRYRNEAGLSGLVLLATARSRLQDAVKAMAEAEKLHKSKPDDPDADWFERSETLSDLLEKADIASKVAHSALVETSDALEAVQSTSVYTPKYPEVKNPQTASHPVVGLHLPAKRATGVQAALLGAGTSRPMGMEAPTRSKNAVKMAKRRQRQKESRQ", "text": "FUNCTION: RNA-dependent RNA polymerase which is found both free and covalently attached to the genomic RNA. May also contain guanylyl and methyl transferase activities (By similarity). SUBCELLULAR LOCATION: Virion Note=Minor amounts are incorporated in the virion."}
+{"protein": "MEPAFGEVNQLGGVFVNGRPLPNAIRLRIVELAQLGIRPCDISRQLRVSHGCVSKILARYNETGSILPGAIGGSKPRVTTPTVVKHIRTYKQRDPGIFAWEIRDRLLADGVCDKYNVPSVSSISRILRNKIGNLAQQGHYDSYKQHQPAPQPALPYNHIYSYPSPITAAAAKVPTPPGVPAIPGSVAMPRTWPSSHSVTDILGIRSITDQVNDSSPYHSPKVEEWSSLGRNNFPAAAPHAVNGLEKGALEQEAKYGQAPNGLPAVSSFVSASSMAPYPTPAQVSPYMTYSAAPSGYVAGHGWQHAGGTPLSPHNCDIPASLAFKGMQAAREGSHSVTASAL", "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": "MIDRYLTPEMKVLWSEANKYRAWLKVELSALQAQARHGEVPAEAHAALVQKSEADPLDDAFAQQVAEIEAVTRHDIVAFTRALTERYGEEARFIHHGLTSTDVVDTAQNLLLDEAMGLIITDVQTLREVCRMQAAAHKHTPVVGRTHGIHAEPMTFGLKFLNWMATLDRDLERLQAARGRVQVVMLSGSVGTYAHVSPKIEEEVAESWGWHAAPVTNQTLARDRHAEVLAALAILGTTLEKIAVEIRHLQRSEVREAMEPFGKGQTGSSSMPHKKNPILTENVTGFARLLRGFLATGLENVALWHERDISHSSAERVILPDATASASYATRRLTGVLRDLVVFPERMLKNLDDLGGLVFSQRVLHALIDDKGMMREAAYGIVQRNALKSWETGEGLRDLLKADPENPLSDAELDAAFDLQWYLRHVDDIYARFGM", "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": "MKSSESAAATASERRAETFQHKLEQFNPGIVWLDPQGHVSAFNDVALHILGPAGEQSLGVAQDHLFGIDVVQLHPEKSRDKLRFLLQSRDAGGCPVRSPPPVAMMINIPDRILMIKVSKMTGAAGTCGSCMIFYDVTDLTTEPSSQPAGASVPAPRRLFKIPVYRKSRVILIDLKDIVRFQGDGHYTTIVTKDERYLSNLSLADLELRLDSSVYLRVHRSHIVSLPYAVELVKLDESVNLVMDDAEQTQVPVSRSRTAQLKELLGVV", "text": "FUNCTION: One-component, b-type heme-containing aerobic sensor and transcriptional regulator that responds to CO by activating the expression of the oxidation operon cox. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MGRFIFVSFGLLVVFLSLSGTGADFFCPSGWGSNNGHCYQAFNQRMTWEDAERFCSAQAKGGHLVSIETRAEADFVAHVVAERIETSFPHVWIGLRDEGKEQQCSSEWSDGSSVSYENWIEAESKTCLGLELDSNYHKWVNVYCGQRNPFVCEA", "text": "FUNCTION: Inhibits thrombin-induced fibrinogen clotting and factor Xa- induced prothrombin activation. Binds to thrombin and prothrombin exosites. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
+{"protein": "MNKEILAVVEAVSNEKALPREKIFEALESALATATKKKYEQEIDVRVQIDRKSGDFDTFRRWLVVDEVTQPTKEITLEAARYEDESLNLGDYVEDQIESVTFDRITTQTAKQVIVQKVREAERAMVVDQFREHEGEIITGVVKKVNRDNISLDLGNNAEAVILREDMLPRENFRPGDRVRGVLYSVRPEARGAQLFVTRSKPEMLIELFRIEVPEIGEEVIEIKAAARDPGSRAKIAVKTNDKRIDPVGACVGMRGARVQAVSTELGGERIDIVLWDDNPAQFVINAMAPADVASIVVDEDKHTMDIAVEAGNLAQAIGRNGQNVRLASQLSGWELNVMTVDDLQAKHQAEAHAAIDTFTKYLDIDEDFATVLVEEGFSTLEELAYVPMKELLEIEGLDEPTVEALRERAKNALATIAQAQEESLGDNKPADDLLNLEGVDRDLAFKLAARGVCTLEDLAEQGIDDLADIEGLTDEKAGALIMAARNICWFGDEA", "text": "FUNCTION: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis (PubMed:32871103). Participates in both transcription termination and antitermination. Involved in a variety of cellular termination and antitermination processes, such as Rho- dependent transcriptional termination and intrinsic termination (PubMed:31020314). Domain AR2 interacts with a large number of other proteins and may serve as a platform to recruit these factors for transcriptional regulation (PubMed:31127279). Involved in phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription. FUNCTION: Participates in both transcription termination and antitermination. SUBCELLULAR LOCATION: Cytoplasm Note=Colocalizes with nucleoids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NusA family."}
+{"protein": "MEVKVLSSKLVKPAYNGGVAAAPDVEYIPLSIFDKVTYKMQMAIIYAFPPPAPSTAAIEKGLAAVLAQYRAFAGQLGESPDGEAAVVLNDRGARLVEAAVDADLVDMAPAKPTPELLRLHPDLEGELQEVVLLQLTRFRCGSLAVGFTSNHVVADGHATSNFLVAWGRATRGLPMGAPPVHHHAALFKPRPSPHVEHDHRNREYYLPAAGDDSHGHGDGGAADNIVIHKAHFTKDFIAGLRAAASEGRGRPFSRFETILAHLWRTMTRARGLSPDEASTIRLSVDGRHRLGAPAEYFGNLVLWAFPRATVGDLLTRPLKHAAQVIHDEVARVDGAYFRSFLDFALSGAGGDKEGLAPSAVLKDVLCPNAEVDSWLTFPFYELDFGTGSPTYFMPSYFPTEGMLFLVPSYLGDGSVDAFVPVFNHNLEAFKECCYSME", "text": "FUNCTION: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to putrescine, to produce coumaroyl putrescine. Can use feruloyl-CoA and caffeoyl-CoA as acyl donors. SIMILARITY: Belongs to the plant acyltransferase family."}
+{"protein": "MVRGPKKHLKRVAAPHHWLLDKLSGTYAPKPSPGPHKARECLPLIVFLRNRLKYALNGREVKAILMQRLIQVDGKVRTDSTFPTGFMDVISVEKTGEHFRLVYDIKGRFTVHRITAEEAKYKLCKVKRVQLGAKGVPFLVTHDGRTIRYPDPLIKVNDTIKLNLETNKIESFIKFDTSAQVMVTGGRNMGRVGTIVHREHHLGSFEIIHVKDALDREFATRLSNVFVIGEAGKSWISLPKGKGVKLSITEERDRRRALKGLA", "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 eS4 family."}
+{"protein": "MAVFVVLLALVAGVLGNEFSILKSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVNKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLSSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLIRKTRTILEAKQAKNPASPYNLAYKYNFEYSVVFNMVLWIMIALALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD", "text": "FUNCTION: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system. May mediate renin-dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (By similarity). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity). FUNCTION: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (PubMed:12045255, PubMed:29127204, PubMed:30374053, PubMed:32276428). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (PubMed:12045255). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (PubMed:12045255). Through its function in V-type ATPase (v- ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Lysosome membrane; Single- pass type I membrane protein Cytoplasmic vesicle, autophagosome membrane; Single-pass type I membrane protein Cell projection, dendritic spine membrane; Single-pass type I membrane protein Cell projection, axon Endosome membrane; Single-pass type I membrane protein Cytoplasmic vesicle, clathrin-coated vesicle membrane; Single-pass type I membrane protein Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Cytoplasmic vesicle, autophagosome membrane; Single-pass type I membrane protein Cell projection, dendritic spine membrane; Single-pass type I membrane protein Cell projection, axon Endosome membrane; Single-pass type I membrane protein Cytoplasmic vesicle, clathrin-coated vesicle membrane; Single-pass type I membrane protein Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type I membrane protein."}
+{"protein": "MFLRSLNLCTILLFLAISSQVSQSLHFELQSGRTKCISEDIKSNSMTVGKYTVVNPNEAHPSPQSHKISIRVTSSYGNTYHHAEDVESGQFAFTAVESGDYMACYTAVDHKPEVTLSIDFDWRTGVQSKSWSSVAKKSQVEVMEFDVKRLIETVNSIHEEMFYLREREEEMQNLNRATNSKMAWLSFLSLFVCLGVAGMQFVHLKTFFEKKKVI", "text": "FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side (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 Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein Note=Cycles between the endoplasmic reticulum and Golgi via COPI and COPII dependent pathways. SIMILARITY: Belongs to the EMP24/GP25L family."}
+{"protein": "MSSTESPVPAAAAPAEAVPASTPAPAAEQPAVGNGEQRNNADAANNTSLYVGELDPSVTEAMLFEIFSMIGTVASIRVCRDAVTRRSLGYAYVNFLNAADGERAMEQLNYSLIRNRPCRIMWSQRDPALRRTGQGNIFIKNLDAGIDNKALHDTFAAFGNILSCKVATNETGSLGYGFVHYETAEAAEAAIKHVNGMLLNDKKVYVGHHIPRKERQAKIEETRANFTNVYAKNVDPEVTDDEFEKLFTKFGKITSCVLQRDEDGKSKGFGFVNFEDHNEAQKAVDELHDSDFKGQKLFVARAQKKSEREEELRRSYEAAKNEKLAKFQGVNLYLKNIPESYDDERLREEFAPFGAITSCKIMRAPSGVSRGFGFVCYSAPEEANKAVSEMNGKMLDNRPLYVALAQRKDVRRQQLEAQIMQRNQLRLQQQAAAQGMGYPGPGMYYPQPGAFPGQPGGMVPRPRYAPAGMMPQGMPMAPYGQPGQFPAGMMPQGYRPARPPRGAPNAAGGPAPPAGARPPTGVNGAPRPAGQPVPGQPMPRGPAARPAGRPEADQPGALTAAALAKASPEEQKQMLGEAIYPKVAASQPELAGKLTGMILELPVTELLHLLEESEALDAKVNEALEVLKEYQQNDSAGAEAEANAEAPKTEA", "text": "FUNCTION: RNA-binding protein involved in the formation of polar- growing hyphae which is essential for infection by the plant pathogen (PubMed:15643068). Component of endosomal mRNA transport that regulates polarity of the infectious hyphae by transporting a broad spectrum of cargo mRNAs from the nucleus to cell poles (PubMed:19494833, PubMed:25985087, PubMed:31338952). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Endosome Cytoplasm Note=Shuttles with endosomes along microtubules. SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family."}
+{"protein": "MSNLNGFIVVDKPKGPTSHQIDSWIRDITGEPRVGHIGTLDPGVSGVLVMALGKATKLIDIVHRESKEYVSVLRTYDKYDHDSIKSVFKEFTGKIYQIPPVRSAVSRELRIREIYNLELLEMDEKFVLFKVCCESGTYIRTLCTDIGYVLGSGGQMAELRRTRTGPFDESMCHTLQEVSDAFKLKSMGNEKLFKNIFIPMDFIFIKYPKVIVKETALKNIAHGSDIYPAGIHAITGSPKKGDVVAVYTEKNELVATGTMMVNADEIYDLKVIDIDNVLIETGDNDGKDSLVRKDNRWKDIPVQKPERKLHGNLQGSQEWKDTGNRGNPKRGGTGSKGFSSGFRKRKAKR", "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": "MAMNVLQSPSRPGLGKVSGFFWHNPGLGLFLLLLGPLMWFGIVYFGSLLTLLWQGFYTFDDFTMSVTPELTLANIRALFNPANYDIILRTLTMAVAVTIASAILAFPMAWYMARYTSGKMKAFFYIAVMLPMWASYIVKAYAWTLLLAKDGVAQWFLQHLGLEPLLTAFLTLPAVGGNTLSTSGLGRFLVFLYIWLPFMILPVQAALERLPPSLLQASADLGARPRQTFRYVVLPLAIPGIAAGSIFTFSLTLGDFIVPQLVGPPGYFIGNMVYSQQGAIGNMPMAAAFTLVPIILIALYLAFVKRLGAFDAL", "text": "FUNCTION: Probably part of the ABC transporter complex YdcSTUV. 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. CysTW subfamily."}
+{"protein": "MSLAGGRAPRKTAGNRLSGLLEAEEEDEFYQTTYGGFTEESGDDEYQGDQSDTEDEVDSDFDIDEGDEPSSDGEAEEPRRKRRVVTKAYKEPLKSLRPRKVSTPAGSSQKAREEKALLPLELQDDGSDSRKSMRQSTAEHTRQTFLRVQERQGQSRRRKGPHCERPLTQEELLREAKITEELNLRSLETYERLEADKKKQVHKKRKCPGPIITYHSVTVPLVGEPGPKEENVDIEGLDPAPSASALTPHAGTGPVNPPARCSRTFITFSDDATFEEWFPQGRPPKVPVREVCPVTHRPALYRDPVTDIPYATARAFKIIREAYKKYITAHGLPPTASALGPGPPPPEPLPGSGPRALRQKIVIK", "text": "FUNCTION: Deposition-and-exchange histone chaperone specific for H2AZ1, specifically chaperones H2AZ1 and deposits it into nucleosomes. As component of the SRCAP complex, mediates the ATP-dependent exchange of histone H2AZ1/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the VPS72/YL1 family."}
+{"protein": "MASISTTTWLYRGQVCTDSGKSSNCIVQRRVKCGFPLKTLHAGITSRDRSLRHCIKCKKEDGDGDVSEGSKKSEEGFEYVTVERHPYHSYMDSTSGKLEPASGARASIPGEDYWPEGTSSRVRAARAPQPAGESSSFPSYGKNPGSRRKKNRKATEENVTVETNDEVSDSEDSSEEEENDSSDGFVTYKNEFEREEEETGFELDKKLGRPHPFIDPTKKKQIEKTLTSDESWWNWRKPEKEQWSRWQRRRPDVETVFLKAMAETGQVKLYGEEPTLTETSLYRARRHLFKEERLQAERERLAKEGPMAFYSEWVKAWKRDTSREAVQKHFEETGEDENTQLIEMFSHQTDREYRIMMGTDIRIKRDPLAMRMREDQIKQIWGGDPVYPTINYIQDPNAVMDFRGPDFHEPTPNMLSYLKENGKVISREMHEALLTKEKTEQLEVPDMDDAMAQAVDIGENDDDEDDADVEKDDEKVPRNWSVLKETPELRTAKPKPKKEGRMSLDEAVDDAENLTDFLMDFEEETDP", "text": "FUNCTION: Involved in plastid gene expression (PubMed:16326926). Required in the nucleus for the initiation of photomorphogenesis mediated by phytochromes (PHYs) (e.g. PHYA and PHYB) by mediating PHYs localization to photobodies, especially in response to red and far-red light, and implicating phytochrome nuclear bodies as sites of proteolysis for PHYs and PIFs proteins (e.g. PIF1 and PIF3). Acts downstream of PHYs and upstream of DET1 (PubMed:20603003, PubMed:22895253). SUBCELLULAR LOCATION: Plastid, chloroplast Nucleus Note=Localizes to subnuclear domains in the nucleolus and in the nucleoplasm, and in chloroplasts."}
+{"protein": "MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYARKVTELPKGAVQQKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGRQIITYPPFEDHCYYHGRIENDADSTASISACNGLKGHFKLQGETYLIEPLKLPDSEAHAVYKYENVEKEDEAPKMCGVTETNWESYEPIEKASQSNLTPEQQKFSPRYIELAVVADHGMFTKYNSNLNTIRTRVHEMVNTLNGFFRSVNVDASLANLEVWSKKDLIKVEKDSSKTLTSFGEWRERDLLPRISHDHAQLLTTIVFDQQTIGLAYTAGMCDPRQSVAVVMDHSKKNLRVAVTMAHELGHNLGMDHDDTCTCGAKSCIMASTISKGLSFEFSKCSQNQYQTYLTDHNPQCILNKPLTTVSGNELLEAGEECDCGAPENPCCDAATCKLRPRAQCAEGLCCDQCRFKGAGKICRRARGDNPDDRCTGQSADCPRNRFHA", "text": "FUNCTION: [Disintegrin insularin]: Inhibits ADP-induced platelet aggregation (IC(50)=0.8 uM for native protein) (PubMed:21073888). Interestingly, inhibits the adhesion of HUVECs to immobilized fibrinogen at very low concentrations (IC(50)=36 nM) (PubMed:21073888). FUNCTION: [Snake venom metalloproteinase insularinase-A]: Non- hemorrhagic proteinase that activates prothrombin (F2) calcium- independently. Activates factor X (F10) and hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrin and fibrinogen without affecting the gamma chain. It induces neither detachment nor apoptosis of human endothelial cells and is also not able to trigger an endothelial pro-inflammatory cell response. Nitric oxide and prostacyclin levels released by endothelial cells are significantly increased after treatment with insularinase A. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily."}
+{"protein": "MWPDNRIARDAHYLYRYDRHGRLTEKTDLIPEGVIRTDDERTHRYHYDSQHRLVHYTRTQYAEPLVESRYLYDPLGRRVAKRVWRRERDLTGWMSLSRKPQVTWYGWDGDRLTTIQNDRTRIQTIYQPGSFTPLIRVETATGELAKTQRRSLADTLQQSGGEDGGSVVFPPVLVQMLDRLESEILADRVSEESRRWLASCGLTVEQMQNQMDPVYTPARKIHLYHCDHRGLPLALVSTEGATEWCAEYDEWGNLLNEENPHQLQQLIRLPGQQYDEESGLYYNRHRYYDPLQGRYITQDPIGLKGGWNFYQYPLNPVQYIDSMGLASKYGHLNNGGYGARPNKPPTPDPSKLPDIAKQLRLPYPIDQASSAPNVFKTFFRALSPYDYTLYCRKWVKPNLTCTPQDDSQYPGMDTKTASDYLPQTNWPTTQLPPGYTCAEPYLFPDINKPDGPATAGIDDLGEILAKMKQRTSRGIRK", "text": "SIMILARITY: Belongs to the RHS family."}
+{"protein": "MILLSLYLCLAAMLHQSEGEASPKLPGLMTSNPDQQTEITDKHNNLRRIVEPTASNMLKMTWSNKIAQNAQRSANQCTLEHTSKEERTIDGVECGENLFFSSAPYTWSYAIQNWFDERKYFRFNYGPTAQNVMIGHYTQVVWYRSYELGCAIAYCPDQPTYKYYQVCQYCPGGNIRSRKYTPYSIGPPCGDCPDACDNGLCTNPCKQNDVYNNCPDLKKQVGCGHPIMKDCMATCKCLTEIK", "text": "FUNCTION: Alters a variety of ion channel activities, including voltage-gated potassium channels (Kv) (PubMed:8071987), voltage-gated calcium channels (L-, N-, and P-type) (Cav) (PubMed:8817251) and ryanodine receptors (RyR) (PubMed:7647234). Is toxic to mice (causes lethargy, partial paralysis of rear limbs and lowering of body temperature). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
+{"protein": "MAPKSKKVAPSPFAQPKAAKTTKNPLFVSRPRSFGIGQDIQPKRDLSRFVKWPEYIRLQRRRKILNLRLKVPPAIAQFQKTLDKNTATQVFKLLNKYRPETAAEKKQRLVAEAEAVANGKSAQDVSKKPYNVKYGLNHVVALIEAKKAKLVLIASDVDPIELVVFLPALCKKMGVPYAIVKNKARLGTVIHQKTAAVLAVTEVREEDKNELASIVSAVDANFSAKYDESRRKWGGGIMGGKTQALLAKRAKAAAATVRL", "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 eL8 family."}
+{"protein": "MKLLFFTALVLVVISLIEVEAENERACIPLEKECTKTPGNCCSGLKCDCYRRFEQGVAKGIQCWCIEKDVTYKGV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 06 (U6-Lctx) subfamily."}
+{"protein": "MKTLLIIDANLGQARAYMAKTLLGAAARKAKLEIIDNPNDAEMAIVLGDSIPNDSALNGKNVWLGDISRAVAHPELFLSEAKGHAKPYTAPVAATAPVAASGPKRVVAVTACPTGVAHTFMAAEAIETEAKKRGWWVKVETRGSVGAGNAITPEEVAAADLVIVAADIEVDLAKFAGKPMYRTSTGLALKKTAQELDKAVAEATPYEPAGKAQTATTESKKESAGAYRHLLTGVSYMLPMVVAGGLCIALSFAFGIEAFKEPGTLAAALMQIGGGSAFALMVPVLAGYIAFSIADRPGLTPGLIGGMLAVSTGSGFIGGIIAGFLAGYIAKLISTQLKLPQSMEALKPILIIPLISSLVVGLAMIYLIGKPVAGILEGLTHWLQTMGTANAVLLGAILGGMMCTDMGGPVNKAAYAFGVGLLSTQTYGPMAAIMAAGMVPPLAMGLATMVARRKFDKAQQEGGKAALVLGLCFISEGAIPFAARDPMRVLPCCIVGGALTGAISMAIGAKLMAPHGGLFVLLIPGAITPVLGYLVAIIAGTLVAGLAYAFLKRPEVDAVAKAA", "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 FruAB PTS system is involved in fructose transport. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MAAAEEGCSVGAEADRELEELLESALDDFDKAKPSPAPPSTTTAPDASGPQKRSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDMTSQQEFTSCLKETLSGLAKNATDLQNSSMSEEELTKAMEGLGMDEGDGEGNILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHRESLPPEQFEKYQEQHSVMCKICEQFEAETPTDSETTQKARFEMVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDALNLSGPPGASGEQCLIM", "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 membrane-associated to the outer surface of peroxisomes. SIMILARITY: Belongs to the peroxin-19 family."}
+{"protein": "MQMKYLIPIFFLVLIVADHCHAFIGMIPGLIGGLISAFKGRRKRDITAQIEQYRNIQKREAAELEELLANLPVY", "text": "FUNCTION: Antimicrobial peptide. Is able to kill Mycobacterium abscessus subsp. massiliense in a dose-dependent manner (By similarity). Has antifungal activity against Candida spp. and one Cryptococcus neoformans strains with MICs values ranging from 12.5 to 200 uM (PubMed:27917162). Also shows an inhibitory activity on C.albicans biofilms at high concentrations (PubMed:27917162). Shows low cytotoxic activity and has weak hemolytic activity on human erythrocytes (PubMed:27917162). Shows anti-inflammatory activities, since it decreases release of pro-inflammatory cytokines, and increases release of anti-inflammatory cytokines (By similarity). Acts by blocking the Toll-like receptor 4 (TLR4) (By similarity). In addition, decreases the expression of costimulatory molecules such as CD80 and CD86 in LPS-stimulated cells (By similarity). In vivo, does not induce immune cell migration (By similarity). Helical wheel projections predict an amphipathic peptide with distinct hydrophobic and hydrophilic faces (Probable). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family."}
+{"protein": "MSSPAPSTSHNAANSTQAFSLKTRRPIDEDDLLTAEDREAKSTVEKLDCATRRRACKNCTCGRAELERQLEAGGSQVMGAMPPGGCGNCAKGDAFRCAGCPYLGMPAFDNAVDGKVKLDLTDDI", "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 (PubMed:25040552). 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 (By similarity). 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": "MQLQVMNSPFNQEQAELLNRLLPTLTESQKIWLSGYLSAQSVSAQEAAGTPAAAVSAEAPAPAVSKEVTVLYGSQTGNAQGLAENAGKQLEQSGFQVTVSSMSDFKPNQLKKVTNLLIVVSTHGEGEPPDNALSFHEFLHGRRAPKLEDLRFSVLALGDSSYEFFCQTGKEFDQRLEELGGKRISPRVDCDLDYDEPAAEWLEGVLKGLNEAGGGSAAPAPAAASQTGESSYSRTNPFRAEVLENLNLNGRGSNKETRHVELSLEGSGLTYEPGDSLGVYPENDPELVELLLKEMNWDPEEIVTLNKQGDVRPLKEALISHYEITVLTKPLLEQAAQLTGNDELRELLAPGNEENVKAYIEGRDLLDLVRDYGPFSVSAQEFVSILRKMPARLYSIASSLSANPDEVHLTIGAVRYDAHGRERKGVCSILCAERLQPGDTLPVYVQHNQNFKLPKDPETPIIMVGPGTGVAPFRSFMQEREETGAEGKAWMFFGDQHFVTDFLYQTEWQNWLKDGVLTKMDVAFSRDTEEKVYVQHRMLEHSAELFEWLQEGAAVYICGDEKHMAHDVHNTLLEIIEKEGNMSREEAEAYLADMQQQKRYQRDVY", "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 (Probable)."}
+{"protein": "MAKLAEEMNPEGSRYQLLLSCPSGLSPSQVSVDFSKSHDRIPRQDPGLEDSISQVWEQRSQGNSSLFNGQKFRYGGYCLDDDDGSTNEVPHVCLRLGLTDYRTFVGTNLSSLWEKFLVTSEDDSVRCRHTSSPLGNGAVIETSDKKIIVLRRSNNVGEFPGHYVFPGGHPEPTAVGIDYHQLENNVQTGEVLNKKVTQEMFDSIICEVVEETGIPASSLSSPLFIGISRRELNVRPAMFFYLKCSHHSDDIQRLYSSAEDGFESTQLHTVSLDELKMMTSRMPGCHHGGFALYELMLQRLKNTKETSLIAT", "text": "FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. SIMILARITY: Belongs to the Nudix hydrolase family."}
+{"protein": "MDLHRAAFKMENSSYLPNPLASPALMVLASTAEASRDASIPCQQPRPFGVPVSVDKDVHIPFTNGSYTFASMYHRQGGVPGTFANRDFPPSLLHLHPQFAPPNLDCTPISMLNHSGVGAFRPFASTEDRESYQSAFTPAKRLKNCHDTESPHLRFSDADGKEYDFGTQLPSSSPGSLKVDDTGKKIFAVSGLISDREASSSPEDRNDRCKKKAAALFDSQAPICPICQVLLRPSELQEHMEQELEQLAQLPSSKNSLLKDAMAPGTPKSLLLSASIKREGESPTASPHSSATDDLHHSDRYQTFLRVRANRQTRLNARIGKMKRRKQDEGQREGSCMAEDDAVDIEHENNNRFEEYEWCGQKRIRATTLLEGGFRGSGFIMCSGKENPDSDADLDVDGDDTLEYGKPQYTEADVIPCTGEEPGEAKEREALRGAVLNGGPPSTRITPEFSKWASDEMPSTSNGESSKQEAMQKTCKNSDIEKITEDSAVTTFEALKARVRELERQLSRGDRYKCLICMDSYSMPLTSIQCWHVHCEECWLRTLGAKKLCPQCNTITAPGDLRRIYL", "text": "FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (By similarity). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7- mediated deubiquitination of CTNNB1 promoting Wnt signaling (PubMed:25266658, PubMed:33964137). Plays a critical role in the regulation of nuclear lamina (PubMed:33964137). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "IMYDCCSGSCSGYTGRC", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
+{"protein": "MKHMFKNILFHKKGKHDKNDAIKKAFSLFSVPSNENERIIKFWPLKFKEKDEETLYIIKLCDNMYSKKYVILVSHLISLLLMYSVCLIVGNINDLFSVLKLTYILLHTFTAINIILILTLHATHYVEMFKSIKGEIFIFYIMMIFVIWCSWLFILFNNIKDLLPIVVNVNNFLYATYANNKINIVLGFFAYLPIFYLITIIPCRICYSCAFDILFFIMKVAIFSVYYLITMKSYILTDNIFMIISALVGSLFIFVIRYIIEIQRRLSFHNWNKQTKQIIKLKKTLKEEKQKLSTTNIEEIYNLINDSIGNYYNENKKQKETDWSIVNNLEKILNILKEDNLFSPDLKTINKKNYNHIYGYIMDLKKQKEIINDKIGSKEEPEAESESECVDESKEGSQIESIFESISDVKQKKKSDLAYTSSYEEKENEILKYDFNMNMDKENISIDIWNTKFLDRKSPNYDAFIKIGYILLNKYYISNQNISVKILYSLLYEMKKGYNDVPYHNSIHAAMVTKHCSILITSLDTVNILKDNEMAAFLISALGHDIGHFGRTNMFLKNCSNFLRIIYNDKSILENYHCSYLFNILSKEEHNIFKKEDLKTLTNLRQLIIEVILATDMSKHIKILAQFRIKSIKIKSYIEKNIILCLKMIIKAADLSHNCVDWSEHYLWVKRLVNEFYSEGDDLLERGFELNPLFDRKAHNNFIQIQRTFLRELVLPLISSLKTLDTSTITQLMLSHVKRNYSKWTKIEKDETKKEKYLNELLTDVPNSWKIVYAPNLNIYKL", "text": "FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes (Probable). Probably by regulating cGMP levels, required for sporozoite motility and invasion of the mosquito salivary glands (PubMed:25784701). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Intracellular localization in blood stage forms and in sporozoites (PubMed:25784701). Partially, localizes to the endoplasmic reticulum in blood stage forms (PubMed:25784701). SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family."}
+{"protein": "MAVSARSARSPPDSDKVQKDKAGQTSGRRQGSRMGKLLGFEWTDVSSWGKLVTLLNRPTDPASLAVFRFLFGLMMVLDIPQERGLSSLDRRYLDGLEVCRFPLLDALQPLPLDWMYLVYTIMFLGALGMMLGLRYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANRYWSVDGLLSARKRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKFVLSEEMTSLLVVHWCGLLLDLSAGFLLFFDASRSIGLLFVSYFHCMNSQLFSIGMFPYVMLASSPLFCSPEWPRKLVAHCPKRLQELLPLRTAPQPSASCVYKRSRAKGGQKPGLRHRLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQATWSPFQRTPWLQPLLMDLSPWRTKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLQEGEKMQLPAGEYHKVYTMSPSPSCYMYIYVNTTELALEQDLAYLQELKEKVENGSETEPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNAPFHERLLRFLLRKLYVFRRSFLMTCISLRNLVLGRPSLEQLAQEVTYANLRPFEPVGEPSPSNTDSSNPNPSEPNADAVHSEF", "text": "FUNCTION: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the vitamin K-dependent gamma-carboxylase family."}
+{"protein": "MSNENDDLSPQRRAPRLNERILSSISRRSVAAHPWHDLEIGPEAPSVFNVVIEISKGSKVKYELDKKTGLIKVDRILYSSVVYPQNYGFIPRTLCEDNDPMDVLVLMQEPVLPGCFLRARAIGLMPMIDQGEKDDKIIAVCADDPEYRHYTDIKQLPPHRLAEIRRFFEDYKKNENKDVAVDDFLPPNSAVNAIQYSMDLYAEYILHSLRK", "text": "FUNCTION: Catalyzes the irreversible hydrolysis of pyrophosphate (PPi) to phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase family."}
+{"protein": "MNNSSELIAVINGFRNSGRFCDIDIVINDERINAHRLILSGASEYFSILFSSDFIDSNKYEVNLSHLDYQSVNDLIDYIYGIPLSLTNDIVKYILSTADFLQIGSAITECENYILKNLCSRNCIDFYIYADKYNNKKIETASFNTILLNILRLINDENFKYLTEESMIKFLSDDMLNIKNEDFAPLILIKWLESTQQPCTVELLRCLRISLLSPQVIKSLYSHRLVGSIYECITFLNNISFLDESFPRYHSIELISIGISNSHDKISINCYNRKKNTWDIISSRRYRCSFAVAVLDNIIYMMGGYDQSPYRSSKVIAYNTCTNSWIYDIPELKYPRSNCGGVADDEYIYCIGGIRDQDSSLISSIDRWKPSKPYWQTYAKIREPKCDMGVAMLNGLIYVIGGVVKGDTCTDTLESLSQDGWMMHQRLPIKMSNMSTIVHAGKIYISGGYNNSSVVNGISNLVLSYNPIYDEWTKLSSLNIPRINPALWSVHNKLYVGGGISDDIQTNTSETYDKEKDCWTLDNGHMLPRNYIMYKCEPIKHKYPLEKTQYTNDFLKYLESFIGS", "text": "FUNCTION: Probable substrate-specific adapter of CUL3-containing E3 ubiquitin-protein ligases which mediate the ubiquitination and subsequent proteasomal degradation of host target proteins. SUBCELLULAR LOCATION: Host cytoplasm."}
+{"protein": "MDEAEYGRFVDWDKMEAGGQEQSPKVLSCTDFQELKQMARQGHWAKSHTLRAKVYQKLIKEIPCRTVTPDASVYRDIVGKIVGKRSASSLPLPEFVDDRQIPSYSLNSEGTGAVRKIISCISNQFPDISFCPALPSLVALLLHYSQDEAECFENVSRILACNDPNRRLVDQTFLAFESSCMTFGDLAGKYCQGPHKLMVAVSEDVLELYSDWQRWIFGELPFAYITRVFDVFLVEGYKVLFRVALALLKFFHKVRGGQPMESNNVKRDLQMFVRDLNKCVTPEKLLEKAFAIRLFSRKEIQLLQMANEKALQQKGITVKQKRQNVHLAVHAENFTSEIVSVKEMRDIWSWIPERFALSQPLLLFTNREHGNSLSRFYLHCEGHEPTLLLIKTTNQEVCGAFLSTDWSERKRSGNKLSFFGTGECFVFRLQPEVERYEWVVIKHPELGKVNSSSADKEANSSQSDKDGIDPSSRLSPFLATRHFNLPSKTASMFMAGSIDCIIIGGGDGQALYLDPDLNYGRTSHCNTFNNQPLCSETFQISIIEVWGFKDNMNNDGAHSALH", "text": "FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). Involved in neuronal projections development, probably through a negative modulation of ARF6 function. Involved in the regulation of synaptic vesicle trafficking. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cytoplasm Cytoplasmic vesicle membrane Presynapse Note=Mainly cytoplasmatic with partial expression at the plasma membrane (By similarity). Associates with certain types of membrane phosphoinositides, preferentially those phosphorylated at the D5 position of the inositol ring such as phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By similarity)."}
+{"protein": "MAKAPSWAGVGALAYKAPEALWPAEAVMDGTMEDSEAVQRATALIEQRLAQEEENEKLRGDARQKLPMDLLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLVQLWQADTRHALEHPEPGAEHNGLEGPNDSGRETPQPVPAQ", "text": "FUNCTION: Functions as a negative regulator of myocyte differentiation. May interact with both sarcoplasmic structural proteins and nuclear proteins to regulate gene expression during muscle development and in response to muscle stress. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band Cytoplasm, cytosol. Nucleus. Nucleus, PML body. Note=In the sarcoplasm of differentiated striated muscle cells, where it is cytosolic and enriched in the I band. In nucleus and PML bodies of proliferating and undifferentiated myoblasts. Associates with the euchromatin in the nucleus of myocytes upon muscle stress."}
+{"protein": "MGSGWLLRSIICLNGTKKNKSNRGNVHSETSNRVKPVESSSAASTKLTVEVAVIRIQKAFRAFKARKRLCSLKSARRFNSLIQGHTVMNQTSTALNVIHSWYDIQNQIRARRLYMVTQGRLQHKRLENRLKLEIKLHELEVEWCGGSETMEEILAKIQQKEEATVKRERAMAYAFSHQWRANATQYLGQASFNLGKESWGWSWKERWIAARPWEIRAQCYVVKPIKPSKKPEKSSPNNVITKTSAKPDEVGNSKKPGSG", "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 Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the IQD family."}
+{"protein": "MGGSREFRAEEHSNQFHSIIAMAIWLGAIHFNVALVLCSLIFLPPSLSLMVLGLLSLFIFIPIDHRSKYGRKLARYICKHACNYFPVSLYVEDYEAFQPNRAYVFGYEPHSVLPIGVVALCDLTGFMPIPNIKVLASSAIFYTPFLRHIWTWLGLTAASRKNFTSLLDSGYSCVLVPGGVQETFHMQHDAENVFLSRRRGFVRIAMEQGSPLVPVFCFGQARVYKWWKPDCDLYLKLSRAIRFTPICFWGVFGSPLPCRQPMHVVVGKPIEVTKTLKPTDEEIAKFHGQYVEALRDLFERHKSRVGYDLELKIL", "text": "FUNCTION: Involved in triacylglycerol (TAG) synthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA (PubMed:23770095, PubMed:24663078). Can use oleoyl-CoA, linoleoyl-CoA and linolenoyl-CoA as substrates. Has substrate preference for linolenoyl-CoA or oleoyl-CoA compared to linoleoyl-CoA (PubMed:23770095). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Lipid droplet. SIMILARITY: Belongs to the diacylglycerol acyltransferase family."}
+{"protein": "MPKYYCEYCDIYLTHSSPVGRRQHNQGRKHISAKIEYFQNLLREEGITPQNFLGFLGSQAYNNILSNPMMNNFMHGNYNGYMKYSPMRNYHHSNRNPNYQHSVGMHNNKYSRAGYVPPGANKYPNNNFHNNKRISNTPKPYNNYTNKPITNSPYKNDKQDYRNNNENSNNFSNYQMNKDNSNFVNKNSEQPN", "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": "MPNDLVVVKANSLIEANYRLSIDEIRILALTIGTMDPKSNQKIFDFTVADFVREFPEISQDNAYKQIQAAIKRIYDRSVKTEDKDRVTEFRWVSSRTYFKKEGRFRIAMTDEVMPYLTQLKGQFTQYQLKHIAYFNSVHSIRIYELITQYRSVGSREITVEKLKEWLQVENKYPRFNSLNQRVLEPAITEINEKSDLVVEVEQIKRGRTIHSLNFVIGSKKRTAQKIEEVAKRPVFPHKNKYGKFVKLDKQNPKMSNHEYGLWARDCLKILEDHYTDITKVTNEDLRNYWVFLAGNDSNRSKLGSKSDFLNELKKRGYKLVDCELVKI", "text": "SIMILARITY: Belongs to the initiator RepB protein family."}
+{"protein": "MTSNNTAHRSATKRLFKTCALAAGLGLMSLPAFAGDSALYGPTAPKGSTFVRVYNASSAEISASVGNTNLNEVAPLGSTAFSFMPQGDYTAKLGSQSVPVKLASDHYYTLVNNASGKPQLVEEPPFKNKQKSLVRVQNLSDKSLTLKTADGKTEVVNTVAAKGTGEREINPVKVSLALYDGDKKVTDVKPVALERGEAAVLYITGSGSSLSPVWVKPPVATR", "text": "FUNCTION: Together with AlgI and AlgJ, 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: Periplasm. SIMILARITY: Belongs to the AlgF family."}
+{"protein": "MEDMRIATLTSGGDCPGLNAVIRGIVRTASNEFGSTVVGYQDGWEGLLGDRRVQLYDDEDIDRILLRGGTILGTGRLHPDKFKAGIDQIKANLEDAGIDALIPIGGEGTLKGAKWLSDNGIPVVGVPKTIDNDVNGTDFTFGFDTAVAVATDAVDRLHTTAESHNRVMIVEVMGRHVGWIALHAGMAGGAHYTVIPEVPFDIAEICKAMERRFQMGEKYGIIVVAEGALPREGTMELREGHIDQFGHKTFTGIGQQIADEIHVRLGHDVRTTVLGHIQRGGTPTAFDRVLATRYGVRAARACHEGSFDKVVALKGESIEMITFEEAVGTLKEVPFERWVTAQAMFG", "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": "MEVRGGVGQGSAARHPPAPEPSRAAARVQAGDALPLPIRHTNLIFSALFAASLAYLMRRWREKIRSSTPLHAVGLAEMLAIFGLVASLIYLLSFFGIAFVQSIVSSGDDDEDFLVGSGSSGSAAAPSRQHAQAPAPCELLGSPAAAPEKMPEDDEEIVASVVAGKVPSYALEARLGDCRRAAGIRREALRRITGRDIEGLPLDGFDYASILGQCCELPVGYVQLPVGVAGPLLLDGRRFYLPMATTEGCLVASTNRGCKAIAESGGATSVVLRDAMTRAPVARFPTARRAAELKAFLEDPANFDTLSVVFNRSSRFARLQGVQCAMAGRNLYMRFSCSTGDAMGMNMVSKGVQNVLDFLQDDFHDMDVISISGNFCSDKKPSAVNWIEGRGKSVVCEAVIGEEVVKKVLKTDVQSLVELNTIKNLAGSAVAGALGGFNAHASNIVTAIFIATGQDPAQNVESSHCITMLEPVNAGRDLHISVTMPSIEVGTVGGGTQLASQSACLDLLGVRGASRDRPGSNARLLATVVAGGVLAGELSLLSALAAGQLVKSHMKYNRSSKDVSSTTATEKTRQREVDV", "text": "FUNCTION: Catalyzes the synthesis of mevalonate. The specific precursor of all isoprenoid compounds present in plants. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HMG-CoA reductase family."}
+{"protein": "QGGWPRNPIPP", "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": "MTGIFAEQTVEVVKSAIETADGALDFYNKYLDQVIPWKTFDETIKELSRFKQEYSQEASVLVGDIKVLLMDSQDKYFEATQTVYEWCGVVTQLLSAYILLFDEYNEKKASAQKDILIRILDDGVNKLNEAQKSLLGSSQSFNNASGKLLALDSQLTNDFSEKSSYFQSQVDRIRKEAYAGAAAGIVAGPFGLIISYSIAAGVIEGKLIPELNDRLKAVQNFFTSLSVTVKQANKDIDAAKLKLATEIAAIGEIKTETETTRFYVDYDDLMLSLLKGAAKKMINTCNEYQQRHGKKTLLEVPDI", "text": "FUNCTION: Toxin, which has some hemolytic activity towards mammalian cells. Acts by forming a pore-like structure upon contact with mammalian cells (By similarity). SUBCELLULAR LOCATION: Secreted Periplasm Host cell membrane; Single-pass membrane protein Note=Exported from the cell by outer membrane vesicles. Also found in the periplasmic space (By similarity). SIMILARITY: Belongs to the hemolysin E family."}
+{"protein": "MAAAASTLASLSATAAAAAGKRLLLSSPSRSLSLSLASRGRIAVMPHLRAGILSAAPRRAVSASAPAAATIAVGDKLPDATLSYFDSPDGELKTVTVRDLTAGKKVVLFAVPGAFTPTCTQKHVPGFVAKAGELRAKGVDAVACVSVNDAFVMRAWKESLGVGDEVLLLSDGNGELARAMGVELDLSDKPAGLGVRSRRYALLAEDGVVKVLNLEEGGAFTTSSAEEMLKAL", "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": "MDKVVKFAEPGRAFAKDSIRLVKRCTKPDRKEFQKIAIATAVGFAIMGFIGFFVKLIHIPINNIIVGS", "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": "MTALRPLSGRSRSLRCSSEKMEGTGSWDVLEWTKLDSASWSGSYSNLDCLLESERIIFEACGVILINTDEAGTLLLSNFRILFLSEGTRKLVPLGTIPFVAIEKFNKLAPKVQSNKYHNNENAPTRLLQVTGKDMRIVVYGFRPGTKQRHTVVDTLLRCNKPERVWDLYAFTCGPSQFGNTNPKERLLNEYFRLLGKSSQRASMNMIEDGSFTLSNDLWRITNLNSNYDLCQSYPFALMVPKSISDEELLQTSTFRARCRLPVISWCHPGSGAVIARSSQPLVGLMMNMRSNSDEKLVASFCTQLAGHKGARRKLYIVDARPRKNALANGAKGGGSESSSNYLQSEIVFLGIDNIHAMRESFSRLRDYLDMHGTTSSDGTSSFLRHGGWTWGGGNLSSMSASVSVLGDSGWLSHIQSILAGVAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFSGFQALVEKDWLSFGHPFSDRVGMPNVSESGNFELPIQSSSARSFPSSPVRQSPGSAAAQSSSSSYGLNNYSPIFLQWLDCISQLMRMYPSAFEFSPTFLVDFIDCLLSCRFGNFLCNSEKERQQCGISETCGCIWAYLADLRSSSGTSHVHCNPFYDPSRYDGPLLPPAAALAPTLWPQFHLRWACPVEPNVTETEDQCRAMTVKYSEMKKEKEEAERKVDELSSAMESLNEELLNERDISRAARESAKRATKERAVISRAVQSLGCKVKFTRNGDCTVEVEDGPQKCSHSIPQKQSEDNTTDVSESISSVTEQNVCEAVCPLRTREGTCRWPDAGCARIGNQFLGLKTNFEAFDNLCVYDSYFTAE", "text": "FUNCTION: Phosphatase with phosphoinositide 3'-phosphatase activity that can use phosphatidylinositol-3-phosphate (PtdIns3P) and phosphatidylinositol-3,5-diphosphate (PtdIns3,5P(2)) as substrates and produces phosphatidylinositol-5-phosphate (PtdIns5P); participates in pathway(s) that transfer gene regulatory signals to the nucleus. SUBCELLULAR LOCATION: Cytoplasm Note=Highly concentrated at the peripheral lobes of the epidermal cells. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily."}
+{"protein": "MSTEGGFGGTSSSDAQQSLQSFWPRVMEEIRNLTVKDFRVQELPLARIKKIMKLDEDVKMISAEAPVLFAKAAQIFITELTLRAWIHTEDNKRRTLQRNDIAMAITKFDQFDFLIDIVPRDELKPPKRQEEVRQSVTPAEPVQYYFTLAQQPTAVQVQGQQQGQQTTSSTTTIQPGQIIIAQPQQGQTTPVTMQVGEGQQVQIVQAQPQGQAQQTQSGTGQTMQVMQQIITNTGEIQQIPVQLNAGQLQYIRLAQPVSGTQVVQGQIQTLATNAQQITQTEVQQGQQQFSQFTDGQQLYQIQQVTMPAGQDLAQPMFIQSANQPSDGQTPQVTGD", "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 NFYC/HAP5 subunit family."}
+{"protein": "MGPRSGLLGLFALFVAGKCSYSPEPDQQRRLPPGWVSLGRADPEEELSLTFALRQQNVKRLSELVQAVSDPGSPRYGKYLTLEDVAELVRPSPLTLHTVQKWLLAAGARNCHSVTTQDFLTCWLSVRQAELLLSGAEFHHYVGGPAETHAVRSLHPYRLPKALAPHVDFVGGLHRFPPTSTLRQHPEPQVPGTVGLHLGVTPSVIRKRYNLTAQDVGSGTTNNSQACAQFLEQYFHDSDLAEFMRLFGGDFAHQASVARVVGQQGRGRAGIEASLDVEYLMSAGANISTWVYSSPGRHESQEPFLQWLLLLSNESALPYVHTVSYGDDEDSLSSTYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPSFPASSPYVTTVGGTSFQNPFRVTDEVVDYISGGGFSNVFPRPSYQEEAVTRYLSSSPHLPPSSYFNASGRAYPDVAALSDGYWVVSNHVPIPWVSGTSASTPVFGGLLSLINEHRILRGLPPLGFLNPRLYQKHGAGLFDVTRGCHESCLNEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLMNP", "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": "DKGPAMKYRTDNTPEPISSHVSHYGSDSSQATQSPAIKGSAVNFNSHSMTPFGGPSGMTPFGGASSSFSAVPSPYPSTLTGGGTVFVALYDYEARTTDDLSFKGGERFQIINNTEGDWWEARSIATGKTGYIPSNYVAPADSIEAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEVRGDNVKHYKIRKLDNGGYYITTRAQFESLQKLVKHSREHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKLGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMTKGSLLDFLKEGEGKFLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLEDYFTAAEPSGY", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily."}
+{"protein": "MYVGRFIVVAPDRAAYRVSSRSFPNRRIVDRDGTLTVGPTEDAPETDNPYISYNCLRTVGDDYAVVGNGTQVDPIAEKLSLGYPPRDALAESLLALDYEKDDYDTPRIAGVVGDESYIGTVRRDALIVEAVEEPTLVATYEKSEPEPTSLGADDPSELAAELYDRDLEHPVCAAGVVADGDSFEVGYYNGE", "text": "FUNCTION: Catalyzes the cyclization of 5-formylamidoimidazole-4- carboxamide ribonucleotide to IMP. SIMILARITY: Belongs to the archaeal IMP cyclohydrolase family."}
+{"protein": "MAFSLEEAAGRIKDCWDNQEVPALSTCSNANIFRRINAILDDSLDFSKVCTTPINRGIHDQLPDFQDSEETVTSRMLFPTSAQESPRGLPDANGLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTQSVLSMLQNPLGNVLGKAPLSFLSLDPLGSDLDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSMTGNGPRDPLKMGVGSRMDQEQAALAAVAPSPTSAPKRWPGASVWPSWDLLGAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGNMPKGYVYLVFELEKSVRALLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVWSPSQRLDPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVTAAFVEIKTTKFTKKVQIDPYLEDSLCLICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKN", "text": "FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the 3'-UTR of mRNAs. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses. Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation. Induces the assembly of stress granules in the absence of stress (By similarity). Required for cell cycle progression, specifically for prophase entry (By similarity). SUBCELLULAR LOCATION: Cytoplasm Synapse Cytoplasm, P-body Cytoplasmic granule Membrane Postsynaptic density Note=Localizes in synaptosomes at dendritic synapses of neurons. Strongly enriched in postsynaptic density (PSD) fractions. Transported into dendrites in a microtubule-dependent fashion and colocalizes in mRNA-containing particles with TACC3, dynein and kinesin. Membrane- associated. Colocalizes at excitatory synapses with members of the polyadenylation and translation complex factors (CPSF, APLP1, TACC3, AURKA, SYP, etc.) including CPE-containing RNAs. In P-bodies and stress granules (By similarity). Recruited to stress granules (SGs) upon arsenite treatment (By similarity). SIMILARITY: Belongs to the RRM CPEB family."}
+{"protein": "MSTETWNLFVAWAQFLLLLRMLPQCDSAKPCPSVCRCDAGFIYCNDRDLTSIPSGIPDDATTLYLQNNQINNAGIPSDLKGLDKVERIYLYRNSLDEFPINLPKNVKELHLQENNIRTITYDALLQIPFIEELHLDDNSVSAVSIEDGAFRDNIFLRLLFLSRNHLSTIPWGLPKTIEELRLDDNRISTISEISLQDLTNLKRLVLDGNLLNNNGLGERVFMNLINLTELSLVRNSLTSPPANLPGTSLRKLYLQENHMNYVPPNSFADLTQLYRLDMSNNNLTALPQGIFDDLDNLTQLFLRNNPWYCGCKMKWVRDWLQSLPSKVNVRGLMCQAPERVRGMTIKDLNKELFDCKDRIGSNTIHVTTTMLNSLLPAQGQWPVPVTKQPEIRPPDINKIFRTTPIPVKKIITIQVKSITTETIYISWKVALPMTALRLSWQLGHSPVFGSITETIVTGDRAEYLLTALEPESPYRICMVPMETGNIYLSDETPVCIETETAPLKMYNPTTTLNREQEKEPYKNSSLPLAAIIGGAVALVAITLLALVCWYVHRNGSLFSRNCAYNKGRRRKDDYAEAGTKKDNSILEIRETSFPMIPINSDPLSKEEFIIHTIFPPNGVSLYKNSHSESSSNRSYRDSGIPDSDHSHS", "text": "FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners (By similarity). Modulates cadherin-dependent cell-cell adhesion and cell sorting (PubMed:20027292, PubMed:19492039). Plays a role in the spatial organization of brain neurons. Plays a role in vascular development. Plays a role in cell-cell adhesion via its interaction with latrophilins that are expressed at the surface of adjacent cells. Mediates axon attraction towards cells expressing ntn1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with unc-5 family members. Plays a role in the regulation of the density of glutamaergic synapses (By similarity). Plays a role in signaling cascades downstream of fgfr1, and possibly also other fgfr family members (PubMed:14688794). Plays a role in embryonic morphogenesis, but not in embryonic patterning (PubMed:19492039). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Endoplasmic reticulum membrane Cell junction, focal adhesion Secreted Cell projection, axon Cell projection, growth cone membrane Note=Detected on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergic synapses. Proteolytic cleavage in the juxtamembrane region gives rise to a shedded ectodomain."}
+{"protein": "MLITFNFEVHQPHRLNKEINQNGNTLWEKYVDTKLNKEVFNKVANKCYIPTNELILELIDEYDFKVNYSITGVFVEQALEFNDYVLDLFKDLVKTGNVELIAETYHHSLTSLFETEDEFIEDIEMHRKMYKEIFGFKAKVFRNTELIYNNRIAKIAKDLGFKAIFTEGIEKILGWRSPNYLYQSPDGMKILLRNYRLSDDIGFRFSARDWDQYPLTADKYAIWLASTPGEVINIYMDYETFGEHHWKETGIFEFLRYLPIEIAKHEHLEVVNVSEVVDRLEPRGEIYVHEFATISWADTERDVSAWLGNKMQRISFEKLKDIGKFIKENSNKLKKLNKFDEIYKMYKVLQTSDNLYYQSIKGLSDMSVHNYFSHFDTPFDAYASYLNILYDFEYYIKELLAKSEFDKNNRRKDGQKQYEKDDEVKKESLINTNIIVAKDDKTESIYIEDEEGKKNKRYERDEGFIIA", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 57 family."}
+{"protein": "MMDISELLDGLNDKQRERVAAPLGNHLVLAGAGSGKTRVLTHRIAWLIAVENISEGSIMAVTFTNKAAAEMRHRIQSTLAKHAQHQLFGMWIGTFHSIAHRLLRAHHLDVGLPQDFQILDSEDQLRLIKRLLKLHNFDEKAFPPKQACWYINNKKDEGLRPNDIEDFNDRQEREWIKIYQIYQDTCDRAGLVDFAELLIRVYELFEKKPLILQRYQQRFQHILVDEFQDTNKIQYKWIKILAGKTGQVMIVGDDDQSIYGWRGAQIENIQKFLKDFKAETIRLEQNYRSTANILNSANELIANNSDRLGKNLWTEGEKGDPVGIYSAFNELDEAKFVASQIQDWVEHGGKLDDCAVLYRSNSQSRVIEEALIRCQIPYRIYGGMRFFERQEIKDALAYLRLINNRQDDAAFERVINTPTRGIGDRTLDILRNLTRERQITLWQAVQVATQENMLAGRASTALLRFQELINSLQLDTAEMPLFAQTDFVIKHSGLYEMYQQEKGEKGEVRIENLEELVTATREFIKPDNAEEMTELTAFLTHASLEAGEEQASPHQSCVEMMTLHSAKGLEFPRVFMVGVEEGLFPSFRSFEEPGRLEEERRLAYVGITRAKKKLTISYAESRRLYAKEERHLPSRFIAELPRECIQEIRLRGTVTRAMNLAKVGSLSNTSAVENEWKMGQKVKHEKFGFGTVINVEGSENNTRLQIAFQAQGIKWLIAHLAKLEKVR", "text": "FUNCTION: May process damage occurring in non-replicating regions of DNA to produce recombinational intermediates for sister strand recombinational exchange. SIMILARITY: Belongs to the helicase family. UvrD subfamily."}
+{"protein": "MGRVSWIIALYLTINVVIVVNGDRVTRNVEVTAEEEKIRDKLGYEAIRDIHRDMDDDHSGSIDRNESTGFMKEDMQMRGSERTRRENKFHGDDDAITVDDLWEAWFESIERTWTNERLVEWLINDVNLPSIVEAVKAKKIDGKILPRFASPNSDFLNKELGIKSSVYRQKLRLNSLDVVLFGYKDNNNRTKDILLAFLALLLTSLIFLYVRQKQKAQQKVNELSNKLTELKCMETEFEDVQKMLNDERSKRSISDGVVNHTEMENLRVQLEEAERRLEANSNGSQAPLALQPLLRRTCENEMAFLEKQRQDCFKEMKEAIEMVDRLQKKQGSVLSSLKLATGAASTSDQVDSKIFALKSRMEKIHTLTRETQERWLQIESLCGFPLLYLNETEHINRSIASSHFYNKSHEGSSSSGSISNAHSNPNAVNSNFVKKVSPPIPPSQQTANLRFVPTEQSDSIHSEDTSPIVEDVAISRSLTQDLAEADMQSIVSGSTNGSGSVAALKKRKGIFPKLFRRNTSKSSSLGGTSN", "text": "FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor which upon Ca(2+) depletion, activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, orai-1. Essential for Ca (2+) and IP3-dependent contractile activity of gonad sheath cells and spermatheca. Essential for fertility. Does not play a role in posterior body wall muscle contraction (pBoc) rhythmicity, intestinal cell oscillatory Ca(2+) signaling or intestinal ER Ca(2+) hemostasis. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Note=Localizes to intracellular puncta in the anterior intestine and reticular structure in the posterior intestine."}
+{"protein": "MGRFIFVSFGLLVVFISLSGTEAGFCCPLGWSSYDEHCYQVFQQKMNWEDAEKFCTQQHTGSHLVSYESSEEVDFVVSKTLPILKASFVWIGLSNVWNACRLQWSDGTELMYNAWTAESECIASKTTDNQWWSMDCSSKRYVVCKF", "text": "FUNCTION: Potent platelet activator that acts via GPIb (GP1BA/GP1BB) (PubMed:15175804). After activation by the toxin, the receptor is redistributed on platelet surface thanks to cytoskeletal translocation. The indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3) also induced by the toxin is downstream the cytoskeletal translocation of GPIb (PubMed:16102113). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
+{"protein": "MGSMNKEQAFELLDAFYEAGGNCIDTANSYQNEESEIWIGEWMKSRKLRDQIVIATKFTGDYKKYEVGGGKSANYCGNHKHSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSHGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERKKNGEGLRTVSGTSKQTDKEVKISEALAKVAEEHGTESVTAIAIAYVRSKAKNVFPLVGGRKIEHLKQNIEALSIKLTPEQIEYLESIIPFDVGFPTNFIGDDPAVTKKASLLTAMSAQISFD", "text": "SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily."}
+{"protein": "MKKQNNLRSLAAQAVEQVVEQGQSLSNVLPPLQQKVADKDKALLQELCFGVLRTLSQLEWLINKLMSRPMTGKQRTVHYLIMVGFYQLLYTRVPPHAALAETVEGAVSIKRPQLKGLINGVLRQFQRQQETLLNEFATSDARFLHPGWLVKRLQNAYPTQWQRIIEANNQRPPMWLRVNRTHHTRDGWLGLLEDAGMKGYPHPDYPDAVRLETPAPVHALPGFAEGWVTVQDASAQGCAVFLAPQNGEHILDLCSAPGGKTTHILEVAPEADVLAVDIDEQRLSRVYDNLKRLGMKATVKQGDGRYPAQWCGEQQFDRILLDAPCSATGVIRRHPDIKWLRRDRDIVELAQLQAEILDAVWPRLKPGGTLVYATCSVLPEENRDQIKTFLQRTPDAALSETGTPDQPGQQNLPGGEEGDGFFYAKLIKK", "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": "MEELVGLREGSSGNPVALRELWGPCPRLRRGIRGGLEWLKQKLFRVGEDWYFLMTLGVLMALISYAMNFALGRVVRAHKWLYREIGDSHLLRYLSWTVYPVALVSFSSGFSQSITPFSGGSGIPELKTILSGVVLENYLDIKNFGAKVVGLSCTLATGSTLFLGKVGPFVHLSVMIAAYLGRVRTKTIGEAENKSKQNEMLVAGAAVGVATVFAAPFSGVLFCIEVMSSHFSVWDYWRGFFAATCGAFMFRLLAVFNSEQETITSLYKTSFPVDVPFDLPEIFFFVLLGAICGVASCAYLYCQRTFLAFTKTNKLISKLMATSKPLYAALAATVLASITYPPGVGRFMASRLSMREHLDTLFDNHSWALLTRNSSPPWPAEPDPQHLWWEWYHPRFTIFGTLAFFLVMKFWMLILATTIPMPAGYFLPIFIIGAAIGRLLGEALSVAFPEGIVAGGVINPIMPGGYALAGAAAFSGAVTHSISTALLAFELTGQIVHALPVLMAVLAANAIAQSCQPSFYDGTIMVKKLPYLPWIRGRPINSHRVIVEHFMRRAISTLARDAALEQVVKVLTSTDEAEYPLVESTESQLLVGIVQRAQLVQALQAEAPARASGQQRCLQDILAGGCPTEPVTLTLSPETSLHQAHNLFELLNLRSLYVTSKGRAVGYVSWVELEKAISALTNPPPAK", "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. May be important in urinary concentrating mechanisms. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. CLCNKA subfamily."}
+{"protein": "MATREWFVMNAQQTKLALESPPLFAVKKDDDKDHTCDTGEEPYALVGSPVFNPLEDYKREVVSIIDEYFSSGDVEVAASDLMDLGLSEYHPYFVKRLVSMAMDRGNKEKEKASVLLSRLYALVVSPDQIRVGFIRLLESVGDLALDIPDAVNVLALFIARAIVDEILPPVFLARAKKTLPHSSQGFQVILVSENSYLSAPHHAELVETKWGGSTHITVEETKRKISEFLNEYVENGDTREACRCIRELGVSFFHHEIVKSGLVLVMESRTSEPLILKLLKEATEEGLISSSQMAKGFSRVADSLDDLSLDIPSAKTLFESIVPKAIIGGWLDEDSFKERSDQNGGSENLRRFKKDAETIIQEYFLSDDIPELIRSLEDLGLPEYNPVFLKKLITLAMDRKNKEKEMASVFLASLHMEMFSTEDFINGFIMLLESAEDTALDILAASDELALFLARAVIDDVLAPLNLEEISNSLPPKSTGSETIRSARSLISARHAGERLLRSWGGGTGWAVEDAKDKIWKLLEEYEVGGVISEACRCIRDLGMPFFNHEVVKKALVMAMEKKNDRMLNLLQECFAEGIITTNQMTKGFGRVKDSLDDLSLDIPNAEEKFNSYVAHAEENGWLHRDFGCSTDS", "text": "FUNCTION: Involved in target of rapamycin (TOR)-regulated translation control, especially under energy-deficient conditions. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol. SIMILARITY: Belongs to the PDCD4 family."}
+{"protein": "MKSVYHHFAIIFFLKLFLCNCILSIPKKTLGKGLFSLGLNEFKNNVDNNSLNILGELKNSKPFINKSFIQINEKKDNVLLLKLYKQNIASDKLSTYYGKIAIGENSENIFNVLFDTGSTEFWVPFKTCKFTKNNIHNKYERTQSFKYKYDDKGLPSVLEINYLSGKLVGFDGYDTVYLGPGFAIPHTNIAFATSIDIPVLEKFKWDGIIGLGFENEDSQKRGIKPFLDHLKDEKILTEKNYKNIFGYYITNTGGYITLGGIDNRFKRSPDEKIIWSPVSTEMGFWTIDILGIRKEKQPYMNERRDDEVIVKYEGFHDGSNKSIVDTGTFLIYAPKKTIENYLNDLTINSCEDKQKLPYIIFQIKSKEIESIKGLSVIELVLSPNDYVIEYIDEVNSTKECIIGIQSDEDNINGWTLGQVFLKSYYTIFDKDNLQIGFVRNKQTINDETYLNESFLRVSKKRNKKKSYNGPL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MADRGGPAEAPSPRGSPRPESRAPRTVGPGETPRTAALALRFDKPIKQAFYNTGAVLFVCLCCGAAVLVYFILEAFLRPLLWAVLCGTFLHPFKSSLTRLGRLWLRRLHRAHTPIVLAALLLPLCFADYGVEALGEQALRRRRLLLLLGAGGPLLYGLYCLGSYLGVQVLLAHAGALICRGLDYFSSLWIWTLVVGYVLMVSFKWNASTQRYLRAVSIPVWMILLFHIASLAGSWRIPVFLVIVFLMSVGTLYEKQNEKESAGAELPGQVISMAASTLANLAISITGYESSTEDQPSDPPTEPTDKGEPPPALSASSSSSSRSSPSSPSPTLGRQRPEMGTFLRKKKTSDIYFVSLVWAIIAVQLWLNLWIVQLLPVPVAVWIIKKLVIHFGVVGFLEKRCHAWWQVIECFLKERQEALAPWPIIGLGKFLLKVDSKLWHWLNKKMIIWLEKMLDKIISIFIIFLLVIGTLLLALLLTAKVHQESVHMIEVTSSLINETLANHPEWANWLPEAQVVQRALNSAANNVYQYGREWITHKLHKILGDKVNNTAVIEKQVLELWDRLYHSWFVKNVTHSGRHKGHKMHVSRQNSWLGDILDWQDIASFVHENIETFLSILESLWIVMSRNVSLLFTTVTTLLTILFYSGTALLNFVLSLIIFLTTLFYLLSSSDEYYKPVKWVISLTPLSQPGPSSNIIGQSVEEAIRGVFDASLKMAGFYGLYTWLTHTIFGINIVFIPSALAAILGAVPFLGTYWAAVPAVLDLWLTQGLGCKAILLLVFHLLPTYFVDTAIYSDISGGGHPYLTGLAVAGGAYYLGLEGAIIGPILLCILVVASNIYSAMLVSPTNSMPTPNQTPWPAQTQRTFRDISEDLKSSVD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family."}
+{"protein": "MNSNVENLPPHIIRRVYKEVSTLTSDPPEGIKIIPNEEDITDVQVNIEGPEGTPYAGGMFRMKLILGKDFPAAPPKGYFLTKIFHPNVSNNGEICVNVLKKDWKAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYASRARLMTDIHAQGTSLRGKDPTDPCSSASTPVVSGDGPMAKKHAGDRDKKLAAKKKTDKKRALRRL", "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": "MHKIFIIFGLLSLCAAHSLRDLSNKDEEDPPSSAPGVRKRRMMSEEDQKTVDYYMDKLNKLADEKHPEEIERHKNPELVAWDRKRDSVLNPEEQGKFFQGDIVLYPEQAKALYEQALTEGKTRVKRKFIGSNLRRWDASRPIIYAFDGSHTQREQRIIELALEHWHNITCLNFQRNDQANSGNRIVFTDVDGCASNVGRHPLGEEQLVSLAPECIRLGVIAHEVAHALGFWHEQSRPDRDQYVTVRWENIDKDSKGQFLKEDPDDVDNAGVPYDYGSIMHYRSKAFSKFDDLYTISTYVTDYQKTIGQRDQLSFNDIRLMNKIYCSAVCPSKLPCQRGGYTDPRRCDRCRCPDGFTGQYCEQVMPGYGATCGGKISLTRSTTRISSPGYPREFKEGQECSWLLVAPPGHIVEFQFIGEFEMYCKIRHSLCMDYVEVRNSTDFANTGMRYCCYGTPPTRIRSATTDMVVLFRSFYRGGKGFEARARAVPEAGNWNSWSPWTACSATCGACGSRMRTRTCPPGNACSGEPVETQICNTQACTGMCAQKREEEGQCGGFLSLLRGVRCRQEKTVMAPCENACCPGFTLQRGRCVR", "text": "FUNCTION: Metalloprotease which cleaves the carboxyl terminus of procollagens, such as sqt-3, to mature collagens (By similarity). Involved in cuticular collagen maturation (PubMed:15579684). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MGSPAHRPALLLLLPPLLLLLLLRVPPSRSFPGSGDSPLEDDEVGYSHPRYKDTPWCSPIKVKYGDVYCRAPQGGYYKTALGTRCDIRCQKGYELHGSSLLICQSNKRWSDKVICKQKRCPTLAMPANGGFKCVDGAYFNSRCEYYCSPGYTLKGERTVTCMDNKAWSGRPASCVDMEPPRIKCPSVKERIAEPNKLTVRVSWETPEGRDTADGILTDVILKGLPPGSNFPEGDHKIQYTVYDRAENKGTCKFRVKVRVKRCGKLNAPENGYMKCSSDGDNYGATCEFSCIGGYELQGSPARVCQSNLAWSGTEPTCAAMNVNVGVRTAAALLDQFYEKRRLLIVSTPTARNLLYRLQLGMLQQAQCGLDLRHITVVELVGVFPTLIGRIGAKIMPPALALQLRLLLRIPLYSFSMVLVDKHGMDKERYVSLVMPVALFNLIDTFPLRKEEMVLQAEMSQTCNT", "text": "FUNCTION: May be involved in phagocytosis during disk shedding, cell adhesion to cells other than the pigment epithelium or signal transduction. SUBCELLULAR LOCATION: Cell surface Note=Possibly surface of photoreceptor cell."}
+{"protein": "MELQEVLHMNGGEGDTSYAKNSFYNLFLIRVKPILEQCIQELLRANLPNINKCIKVADLGCASGPNTLLTVRDIVQSIDKVGQEKKNELERPTIQIFLNDLFQNDFNSVFKSLPSFYRKLEKENGCKIGSCLIGAMPGSFYGRLFPEESMHFLHSCYCLHWLSQVPSGLVTELGISANKGCIYSSKASRPPIQKAYLDQFTKDFTTFLRIHSEELISRGRMLLTWICKEDEFENPNSIDLLEMSINDLVIEGHLEEEKLDSFNVPIYAPSTEEVKCIVEEEGSFEILYLETFKVPYDAGFSIDDDYQGRSHSPVSCDEHARAAHVASVVRSIFEPIVASHFGEAILPDLSHRIAKNAAKVLRSGKGFYDSVIISLAKKPEKADM", "text": "FUNCTION: Involved in the biosynthesis of caffeine. Catalyzes the conversion of 7-methylxanthine to caffeine, likely via theobromine as an intermediate. SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family."}
+{"protein": "MAKEYKTITQIAGPLIFVEKTEPVGYNEIVNIKMGDGTVRRGQVLDSSADIVVVQVFEGTGGLDKDCGVIFTGETLKLPASVDLLGRILSGSGEPRDGGPRIVPDQLLDINGAAMNPYARLPPKDFIQTGISTIDGTNTLVRGQKLPIFSASGLPHNEIALQIARQASVPGSESAFAVVFAAMGITNEEAQYFMSDFEKTGALERAVVFLNLADDPAVERIVTPRMALTAAEYLAYEHGMHVLVILTDITNYAEALRQMGAARNEVPGRRGYPGYMYTDLATLYERAGIVKGAKGSVTQIPILSMPGDDITHPIPDLSGYITEGQIVVARELHRKGIYPPINVLPSLSRLMNSGIGAGKTREDHKAVSDQMYAGYAEGRDLRGLVAIVGKEALSERDTKFLEFADLFEDKFVRQGRNENRTIEDTLEIGWQILTHLPENQLGRIDNKYIQKYHPAHRKAK", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
+{"protein": "MMHAFHHLAVLLIGSLPASASTLPHPDGYRHVNGSCSKSVAVPAVWNGFGYLFNITVGTPPQELTMLSDWTWMSLFVRSGRCLNQYDPSLCLGTSGQTWFDERASTSFANTSLPQLSWPLTAFAPNFTVDYGTDDVCIGDLCSAGTVLQVSDFPYPGEGIPKVPFSGIFGMAPVTAGLNETFHPANYQAWKAGRLGSRVGWNSCAALASSDPCLGGEAKLVFGGTDSSLYDDDTLRIYEIQNPDWLSDAFYPLTPPRENYWTTPLTGSWILGTSEEESRNFAVPFSGSNGSNVTPLAVLDEGSEGLGAPLSLNAYNWLVDQVRGTLASNDTIEEIHAQGSSGFNTAEQNWYTVSCDDIDSYPELVYELNGHTNYTVPPQDYVTKLSDSSTCYLNINLWKYGRTEDGNAKVALLGLAFLKRLYVVLDFETQSFGLAPLSM", "text": "FUNCTION: Secreted aspartic protease; part of the gene cluster that mediates the biosynthesis of the mycotoxin lucilactaene and the lucilactaene-related compound NG-391 that act as cell cycle inhibitors with potent growth inhibitory activity against malarial parasites, moderate growth inhibitory activity against cancer cells, and no activity against bacteria and fungi (PubMed:32043422, PubMed:35484225). Within the cluster, LUC7 and LUC8 encode proteins which are not commonly involved in the biosynthesis of secondary metabolites and are not essential for lucilactaene biosynthesis (Probable). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "LAIPPFNYPVNLAVSKLAPALMAGNTVVLKPPSQGVVAGIHMIKCFQAAGLPAGTVNLVTGKGSEIGDFLTTHPAVNCISFTGGDTGIAISRKAGMVPLQMELGGKDACIVCSDADLDLAATHIIKGGFSYSGQRCTAVKVVLVMQDIADELVRKVHAGVQKLKVGRPEDNADITAVVSEGSANFIQGLVEDAKAKGATFLTDWKREGNLLWPVLLDNVTADMRIAWEEPFGP", "text": "FUNCTION: Important as a means of generating NADPH for biosynthetic reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
+{"protein": "MNSTCIEEQHDLDHYLFPIVYIFVIIVSIPANIGSLCVSFLQAKKESELGIYLFSLSLSDLLYALTLPLWIDYTWNKDNWTFSPALCKGSAFLMYMNFYSSTAFLTCIAVDRYLAVVYPLKFFFLRTRRFALMVSLSIWILETIFNAVMLWEDETVVEYCDAEKSNFTLCYDKYPLEKWQINLNLFRTCTGYAIPLVTILICNRKVYQAVRHNKATENKEKKRIIKLLVSITVTFVLCFTPFHVMLLIRCILEHAVNFEDHSNSGKRTYTMYRITVALTSLNCVADPILYCFVTETGRYDMWNILKFCTGRCNTSQRQRKRILSVSTKDTMELEVLE", "text": "FUNCTION: Receptor for the glycosphingolipid psychosine (PSY) and several related glycosphingolipids (PubMed:11309421). Plays a role in immune response by maintaining lysosome function and supporting phagocytosis-mediated intracellular bacteria clearance (PubMed:27287411). May have a role in activation-induced cell death or differentiation of T-cells (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MEDVNSDVNADQEVRKLQELVKMLEKQNEQLRSRSGAVQGAGSFGPGSPVRAGASTPSSGTASPRGFPLGLSAKSGSGAGSGPRRTSSEELRDATSLLAAGEGGLLDEVEPLRPEELERLSGWEEEEESWLYSSPKKKLTPMQKSVSPLVWCRQVLDYPSPDVECAKKSLIHKLDQTMSALKRQNLYNNPFNSVSYTSPYSPNASSPYSSGFNSPSSTPVRPPIVKQLILPGNSGNLKSSSDRNPPLSPQSSIDSELSASELDEDSIGSNYKLNDVTDVQILARMQEESLRQEYAATASRRSSGSSCNSTRRGTFSDQELDAQSLDDEDDNMHHAVYPAVNRFSPSPRNSPRPSPKQSPRNSPRSRSPARGIEYSRVSPQPMISRLQQPRLSLQGHPTDLQTTNVKNEEKLRRSLPNLSRTSNTQVDSVKSSRSDSNFQVPNGGIPRMQPQASAIPSPGKFRSPAAPSPLALRQPVKAFSNHGSGSPGSQETTQLMQTTSSPGPPMVQNTVPANPPSNINSTTLTRPAGTTVMRSGLPRPSAPSAGGIPVPRSKLAQPVRRSLPAPKTYGSMKDDSWKDGCY", "text": "FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Colocalizes with microtubules. Detected at the plus end of growing microtubules (By similarity). SIMILARITY: Belongs to the SLAIN motif-containing family."}
+{"protein": "MSLLEDIVDLLKCVLEYFGVPPDMLVPVWESTHCGQYRSLVRMIGTNLPLSPYPRLRFQIPLQTFNKHSHIDVSVDSPAIPTLADVLWLVEDEGDSHTKFRNAVPLRKKCVPHGYETPSLGSVSVKAQRGGGVLAQSTQPDALLKISALEEELQRLRAQIATIITAPAGPVVSPTDPGTPCSAPKPAPVLTSTPVCPPPPPPPPPPAMPTRTEVSMSEMIQQRQAAKKETLAQCGPSLTTAPSMLEVLRDLNQVKLRSVERSPGGTPIRRRRSKGVACSSDPAALIAEALKRKFAHRQRDDSFGKENHSAEPSPFSSPDTPRIFQHTRRSQGRIHL", "text": "FUNCTION: May play a role in mitochondrial aerobic respiration. Can also promote mitochondrial fission (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the MTFR1 family."}
+{"protein": "MGKISKAVRGVADIYNGASLIVRIIVGLIIGTVLALTMPHVTWIGEFGTLFVAALKAAAPILVFVLVASALAQGTSKLDRRFGTVLFLYLFTTFLAAVVAVLTSRLFPQTLSLGKAAKADVVPQGLSEVIQTLLTNIVANPIQAIIDGNYICILMWACLFGLAMKSIANESSKAFMANVADAVSQVIRWVINLAPFGIMGLVFTNVADNGLSAFTKYGSLLLLLVGTMLLMVLVFGPLVIFIFLRRNPYPLVYRCFKESGLTAFFTRSSAANIPVNMQLCEKLGLDKDMYSVSIPLGATINMNGAAITITIMAMAAANTLGIQISLPAAILLSVVSALGACGASGVAGGSLLLIPMACSLFGISNDIAMQVVGVGFIIGVIQDSVETCLNSASDVEFAATAEYHAWLKQGRQLPAFMYSKKERAKLGIEA", "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": "NLVQFKTLIMKIAGRSVVYKYFYYGCYCGWGGIGQPRDATDRCCFVHD", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that shows myotoxicity and induces paw edema in mice (PubMed:17451767). Exhibits indirect hemolytic activity (PubMed:17451767). Inhibits platelet aggregation induced by ADP and collagen (PubMed:17451767). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn- phosphoglycerides (PubMed:17451767). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
+{"protein": "MNGNLPHIQIQSPKNSLDHLNNGRQATHNFEHGKPGDREEANGHADAHSSSGRSRYLSSDTNLLRDGSSSLDPLSKHIMKRTRSEKTLSFLNPSRASSNTHLSREGTNRSSNVTRTVSGRKSNHGSSLTDTGESDQLSLKSFGAIRQPSQHRSSLFSRMLGSTSHIFGIREDMDNESSEEERDGIPRVEGNAADPFSWIPDGKNVWDSPPKYIRVLSHNKKEKSLDHLFLAQELYCKPTLAATHDRYYEPRATDFPNLAHESSEPSSSRHTADAQSITNASVHLHNSSSPLNRTPSVISDTLAVAITSNSSSNSSNNAIWAMKFSRDGRYLAVGGQDRILRIWAVLDSEHARSVASETCSSDPNNPKLNLKAPVFSEAPIREYAGHTADILDLSWSRNNFLLSSSMDKTARLWHPVRKDCLCCFEHSDFVTSIAFHPKDDRFFLSGSLDCKLRLWSIKEKAVSFWNELPELITAVAFSPDGGLAIAGTFVGLCLFYDTRGLRFRTQMSIRSSRGKNAKGSKVTGIQTRTQMIDNIAGDTEMLVTTNDSRIRIYNLRDKSLELKFKGHANAQSQNRAYFDDDGNYVICGSEDHQVFIWDLPPQHMHKTKKKKHEHFKASVRPITAAVFAPTKTKQLLTLSGDPVYLAAISARRSSVISNASIETGPSLRNLKSLSHSYLPIEIMKGHIIVCGDLDGRIRVFRQDSVFAARKLIEKKNIERKNSETLSNSSFFPQALKAHMNSISSPKRHFSLRHKKNASQITNNENNGNDDIKKGDEPEEEHVGLRKNSTQEKNANLDPNEALKRADMMMLQEGASSMVYYSLTNLDNPGATVNEAAKTAATIEQNEHEIQTSVDPISNVKAILPNADDVSSKNSSTEDQLECLRCGNSLFNVFSRSFVFEGAKFSIVCSHCNRKLLKSGSDDGSETHEMSTLP", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum Nucleus."}
+{"protein": "MPKHEFSVDMTCGGCAEAVSRVLNKLGGVEFNIDLPNKKVCIESEHSSDILLATLNKTGKAVSYLGPK", "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": "MFMLLVFGALLPEVPLSGQDKAPPQADGISATPLFNYASLRLPEEHIPFFLHNNRHIATVCRKDSHCPYKKYLENLKYCWGYEKSCRPEFRFGYPVCTYVDMGWTDTLESAQEIFWKQADFGYAAERLEELHVLCQPKEKNDSSLVCSRYLQYCRATNIYLDLRNIKRNHDRFKEDFVQSGEIGGYCKLDIRSLMSQGQRKSPLQSWFAELQSYTELNFRPVEDAQCDIVIEKPTYFMKLDAGVNMYHHFCDFINLYITQHVNNSFSTDVYVVMWDTSSYGYGDLFSDTWKAFTDYDVIHLKTYDAKRVCFKEAIFSLLPRMRYGLFYNTPLISGCQNTGLFRAFSQHVLHRLNITQEGPKGGKIRVTILARSTEYRKILNQNELVNALKTVSTFEVQIVDYKYKELGFLDQLRITHNTDIFIGMHGAGLTHLLFLPDWAAVFELYNCGDERCYLDLARLRGVHYITWRRQNKVFPQDKGHHPTLGEHPKFTNYSFDVEEFMYLVLQAADYVLQHPKWPFKKKHDEL", "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": "MGHLKLKSIEVDSTVKKLGDPLKFNLRFVCFEEIKCGVEFVVLYNMDVHSDENDQVLAEIEVAPIPKGKIEFSIDADAPDVNKIPLDEMFGLTSILIVGRYKGQQFIRIGYIVDVGYPGIPSTKLMKSDVEEPSEEIGDKEEEDEEDVEEELGSEEGSEESSCIVEDKDEDNEEAEPRTFMEAVEDVGNEGKERLFESEGREEEEDEKVGSDSYSEVNRELNKSVGEEAEGSDGGEDVVDYCGFRIDKKQIEMKLMDPPVINLFEIEWEEESPSEEVPRNNNESPAKKQKVE", "text": "FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ASF1 family."}
+{"protein": "MMAGMKIQLVCMLLLAFSSWSLCSDSEEEMKALEADFLTNMHTSKISKAHVPSWKMTLLNVCSLVNNLNSPAEETGEVHEEELVARRKLPTALDGFSLEAMLTIYQLHKICHSRAFQHWELIQEDILDTGNDKNGKEEVIKRKIPYILKRQLYENKPRRPYILKRDSYYY", "text": "FUNCTION: Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle. SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle. Note=Packaged within secretory vesicles. SIMILARITY: Belongs to the neurotensin family."}
+{"protein": "MGKKMEKKRAEMPPARAGILSFWDEEAPGIKIDPDYILYACFAVAVLLIIAHTMAAV", "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": "MSQEVIRGIALPPPAQPGDPLARVDTPSLVLDLAPFEANLRAMQAWADRHDVALRPHAKAHKCPEIALRQLALGARGICCQKVSEALPFVAAGIQDIHISNEVVGPAKLALLGQLARVAKISVCVDNAHNLSQVSQAMVQAGAQIDVLVEVDVGQGRCGVSDDALVLALAQQARDLPGVNFAGLQAYHGSVQHYRTREERAEVCRQAARIAASYAQLLRESGIACDTITGGGTGSAEFDAASGVYTELQAGSYAFMDGDYGANEWDGPLAFENSLFVLATVMSKPAPDRVILDAGLKSTTAECGPPAIFGEPGLTYTAINDEHGVVRVEPGAQAPDLGAVLRLVPSHVDPTFNLHDGLVVVRDGVVEDIWEISARGFSR", "text": "FUNCTION: Catalyzes the reversible cleavage of D-threonine or D- allothreonine into glycine and acetaldehyde. Can also cleave D-beta- phenylserine, D-beta-hydroxy-alpha-aminovaleric acid, D-beta-3,4- dihydroxyphenylserine and D-beta-3,4-methylenedioxyphenylserine into glycine and the corresponding aldehyde compounds. Inactive towards D- serine, beta-hydroxyaspartate and O-phospho-DL-threonine. SIMILARITY: Belongs to the DSD1 family."}
+{"protein": "MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (PubMed:12821780, PubMed:15053880, PubMed:15195100, PubMed:15632057, PubMed:16337594, PubMed:17290220, PubMed:19098711, PubMed:19219073, PubMed:19837670, PubMed:19965871, PubMed:20173098, PubMed:20385133, PubMed:20858735, PubMed:22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis (PubMed:30879903). Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis (PubMed:30879903). SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm Nucleus, nucleolus. Nucleus Note=Expressed predominantly in the nucleoplasm. Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins. Colocalizes with RASSF1 isoform A in the nucleus. SIMILARITY: Belongs to the MDM2/MDM4 family."}
+{"protein": "MKPSVILYKALPDDLLQRLQEHFTVHQVANLSPQTVEQNAAIFAEAEGLLGSNENVDAALLEKMPKLRATSTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTASIGPDWYGTDVHHKTLGIVGMGRIGMALAQRAHFGFNMPILYNARRHHKEAEERFNARYCDLDTLLQESDFVCLILPLTDETYHLFGAEQFGKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSMANVVAVPHIGSATHETRYGMAACAVDNLIDALQGKVEKNCVNPHVAD", "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": "MTEGDRELSALIQELWDNDTNRLRPGIDYRISLQGKAGDLAGVPDDSDGAGMPLFSFVDENIFKKETFLAFISLLDNYESDTGEPEIVTPEEEMENHRFLDSVIKTPTMKIAHKYLVEKRLSPEDTTGFKQQLYKIWFELYARKGSSKPDSSGFEHVFVGETRGGHTVIGFHNWIQLYLQEKLGHIDYKGYSVNANSPQPDENKHMLALQFSWKNGIKPKGSIFIGVSPEFEFSLYTLCFLMSPNERVKVSFNLYDVEIVCHHYNQKHIGTTYPVPVKYLNV", "text": "FUNCTION: Endoribonuclease that cleaves single-stranded RNAs at 5' of uridylates and releases a product with a 2',3'-cyclic phosphate at the 3'-end. The UU and GU sites are more efficiently cleaved than CU and AU sites. SIMILARITY: Belongs to the ENDOU family."}
+{"protein": "SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY", "text": "FUNCTION: Mixed specificity lectin with anti-HIV activity. Binds to HIV envelope glycoproteins, including exterior membrane glycoprotein gp120, and inhibits viral entry into cells. Binding to gp120 is dependent on gp120 being glycosylated, and is inhibited by mannose, glucose and N- acetylglucosamine. SIMILARITY: Belongs to the jacalin lectin family."}
+{"protein": "MFKNVFANLQKVGKSLMLPVSVLPIAGILLGIGSAHFNFLPDILSQIMAQTGGSVFSNMPLIFAIGVALGFTNNDGVAALAAVVSYGILIQTLTAVEPIVLHTTIEVIKNKHLSDTGILGGIIAGAISAYMFNKFYRIQLPEYLGFFAGKRFVPIISGLSAILIGVILSLIWPPIGHGIQIFSKWAAYQNPILAFALYGLVERALVPFGLHHIWNVPFQMQIGEYTNSIGQVFHGDIARYMAGDSTAGNLSGGFIFKMYGLPGAALAIWHTSKKENKTKIGSIMISAALTAFLTGITEPIEFSFIIVAPVLYVIHAILAGLSFPLCIFLDMRAGTSFSHGFIDFIVLSGNSHHILLFPIIGILYGLLYYILFYLFIINFNLDTPGRENIKNNILEKDNNEIAPYIITALGGKNNIKNLDACITRLRITVSDISKVKQKDLKNIGAAGIIISGSGIQVVFGTRSENIKTAMDECIKNI", "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. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MKDGKENSNATFGSFTTNLDHTKPCWYWDKKDLAHTPSQSDLDPATEARYRREGARFIFDVGTRLGLHYDTLATGITYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFAQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLRYAKQLKGDKNKVQKLVQMAWTFVNDSLCTMLSLQWEPEIIAVAVMYLAGRLCKFDIQEWTSKQSSRRWWEQFVQDVPVELLEDICHQILDLYSQGKQPIPQQPPMQDKEKPPPPPAAPPGQSGAQNPPAQPPSKKNSPQASPPAKIKRQHVSPKDEPKAPAEQVGSKIPRLESPMPPLPVSQPPERKTPSAIPAPPAEAEPAAASELDPAQGPAPPLPHGAPPPLPHRPPPTEFGGPCSDFLSSVKHKRRYLDDDRNL", "text": "FUNCTION: Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C- terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the cyclin family."}
+{"protein": "MGKKQTKPINAKSRSESNVVADPRFQSVHSDPRFSRLKRGNFKVKVDERFKSLKEDKDFKTTASVDRYGRPLNQDKATKEIDRLYELENEGSSSSSESSEITDNEEVASASSKSTKSEELTDEESEDEEVYDPARGEGIISTSESSDESDAESETEAQPEISELAGIEPEENIPRGSETNRLAVVNMDWDNLQAVDLFVALSSFCPPGGKLLKVSIYPSEFGKSRMAAEHVQGPPRDIFTPADNQPSSAELHEAQKFGFDNNESDQDEEDALIEEDLGNEFDMVKLRQYQLERLRYYYAVVECDSVRTAKVIYETCDGAEYETSANIYDLRFIPDDVTFDDDESREVCTKAPEKYEPRDFVTDALQHSKVKLSWDAEDPHRKDLIKKAFTSQDIEDLDFSAYIASSESEDEDVDVIRSRYQKLLSGDADDFQANSNPFEDDDKLEGANGEMEVTFTSGFDVDNNANSSEKDETTIEKYKRKAAERKQRRKELRQLKKTKDDEGEGSDVDLGFDDPFFKDKDASRNNKKNKKGKHTQIEDPTAASKEELENLVREDENDSEQLDHFDMKSILKAEKFKKNRKLKKKASNLEGLQEGFEADVSDPRFAALYTNHNFALDPTNPHFKRTKTVEKIMDESRKRRSNQLEQTQDGKPELKIKKRKAEKGDQRQELDRIVKSIKRSGK", "text": "FUNCTION: Involved 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 ESF1 family."}
+{"protein": "MDCRLGCGACCIAPSISSPIPGMPNGKPAGVRCVQLNEDNLCQLFGRPERPKVCHDFKACPVVCGKTNQQALANLTELERLT", "text": "SIMILARITY: Belongs to the UPF0153 family."}
+{"protein": "MTQTWPFLHNAQSFIQENWNASGFQKPTPVQEQAAQLIMDGKDVIAESPTGTGKTLAYALPVLERIKPEQKHPQAVILAPSRELVMQIFQVIQDWKAGSELRAASLIGGANVKKQVEKLKKHPHIIVGTPGRVFELIKAKKLKMHEVKTIVLDETDQLVLPEHRETMKQIIKTTLRDRQLLCFSATLKKETEDVLRELAQEPEVLKVQRSKAEAGKVKHQYLICDQRDKVKLLQKLSRLEGMQALVFVRDIGNLSVYAEKLAYHHVELGVLHSEAKKMERAKIIATFEDGEFPLLLATDIAARGLDIENLPYVIHADIPDEDGYVHRSGRTGRAGKEGNVLSLVTKLEESKLKKMAKKLGVELSEAVYAGGKLKTK", "text": "FUNCTION: A probable DEAD-box RNA helicase that plays a role in ribosomal 50S subunit assembly. May be a non-specific RNA helicase. SIMILARITY: Belongs to the DEAD box helicase family."}
+{"protein": "MAANDRAAAPGKSGGSSGADGLMRASLSAVAPGTALRDGLERILRGNTGGLIVLGSDKTVEAMCTGGFVLDVEFTATRLRELCKLDGGIVLSSDLSKILRAGVQLVPDPMIPTEETGTRHRTADRVSKQVGFPVVSVSQSMRLVALYVDGMRRVLEDSAAILSRANQALATLERYKLRLDEVAGTLSALEIEDLVTVRDVSAVAQRLEMVRRIATEIAEYVVELGTDGRLLALQLDELIAGVEPERELVVRDYVPEPTAKRSRTVDQALYELDALTHAELLELATVAKALGYTGSPEALDSAVSPRGFRLLAKVPRLPGAIIDRLVEHFGGLQKLLAASVDDLQTVDGVGEARARSVREGLSRLAESSILERYV", "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": "MGITKEEVNSYYQKAGIVLTDEEVDQIQLMDYGLGKERKVGLQLFVYVNTDRYCSKELVLFPGQTCPEHRHPPVDGQEGKQETFRCRYGKVYLYVEGEKTPLPKVLPPQEDREHYTVWHEIELEPGGQYTIPPNTKHWFQAGEEGAVVTEMSSTSTDKHDIFTDPRI", "text": "FUNCTION: Sugar isomerase that catalyzes the reversible isomerization of D-lyxose to D-xylulose. SIMILARITY: Belongs to the D-lyxose ketol-isomerase family."}
+{"protein": "MEQSNRQTAEPAIRSAETVDSTINSFQETDLKVQEKEDVAAAVQTESASIDSNEQGQSVSANTNTQSQAKKLSNNSHQEPMQMVSAANKERAVLETAQNQKNGNMINLTTDKAVYQAGEAVHLNLTLNNTTSLAQNITATAEVYSLENKLKTLQYTKYLLPNESYTTQKGEFVIPANSLANNRGYLLKVNISDSQNNILEQGNRAIAVEDDWRTFPRYAAIGGSQKDNNSVLTKNLPDYYRELEQMKNMNINSYFFYDVYKSATNPFPNVPKFDQSWNWWSHSQVETDAVKALVNRVHQTGAVAMLYNMILAQNANETAVLPDTEYIYNYETGGYGQNGQVMTYSIDDKPLQYYYNPLSKSWQNYISNAMAQAMKNGGFDGWQGDTIGDNRVLSHNQKDSRDIAHSFMLSDVYAEFLNKMKEKLPQYYLTLNDVNGENISKLANSKQDVIYNELWPFGTSALGNRPQESYGDLKARVDQVRQATGKSLIVGAYMEEPKFDDNRVPLNGAARDVLASATYQTDAVLLTTAAIAAAGGYHMSLAALANPNDGGGVGVLETAYYPTQSLKVSKELNRKNYHYQQFITAYENLLRDKVENDSAEPQTFTANGRQLSQDALGINGDQVWTYAKKGNDFRTIQLLNLMGITSDWKNEDGYENNKTPDEQTNLLVTYPLTGVSMAEADRIAKQVYLTSPDDWLQSSMISLATQIKTNENGDPVLYIQVPRLTLWDMIYINETIKPETPKVPEQPQHPARTLEPAIPQTPEAVSPLPVANKQAVDENKNEIVSALTGEENDLQLPTLSKRSLSISQAELPQTGDNNETRSNLLKVIGAGALLIGAAGLLSLIKGRKKD", "text": "FUNCTION: May play a role in sucrose-independent adherence to the pellicle-coated tooth surface. SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. SIMILARITY: Belongs to the glycosyl hydrolase 66 family."}
+{"protein": "MSSRRSVGDPEYLTRRIPQNPRYQHIKTRLDTGSSLTKYIEKLEEIKRNYRYRKDELFKRLKVTTFAQLVVQVASLSDETLEVTNEEIHKLEGGNSPASDADAELTAGTNGKGSPNGTPPSPVLFINNAGAGESYRSTLQSLISGVGELDIEKDTHKKADTQAKDTPYPDCPFLLLDVRDRDAYDQCHIVGAYSYPIAMLSRAMNPYTNSILEYKNAHGKIIILYDDDERLASQAATTMCERGFENLFMLSGGLKVLAQKVPEGLITGSLPISCQVAAPTGSARKKPVPKVPPTRAESKWRYSAEDLQKIKYYLEEEQLPSDTASRLSRGSSGRDSKATTARSSPSLPSTAGSRMLSRSSIQNRPWK", "text": "FUNCTION: Required during ciliogenesis for tubulin glutamylation in cilium. Probably acts by participating in the transport of tubulin polyglutamylases between the basal body and the cilium (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Note=Localizes mainly to the cilium basal body and in primary cilia. SIMILARITY: Belongs to the CEP41 family."}
+{"protein": "MSRQSLTKAHAKITELSWEPTFATPATRFGTDYTFEKAPKKDPLKQIMRSYFPMEEEKDNRVYGAMDGAIRGNMFRQVQERWLEWQKLFLSIIPFPEISAARAMPMAIDAVPNPEIHNGLAVQMIDEVRHSTIQMNLKKLYMNNYIDPAGFDITEKAFANNYAGTIGRQFGEGFITGDAITAANIYLTVVAETAFTNTLFVAMPDEAAANGDYLLPTVFHSVQSDESRHISNGYSILLMALADERNRPLLERDLRYAWWNNHCVVDAAIGTFIEYGTKDRRKDRESYAEMWRRWIYDDYYRSYLLPLEKYGLTIPHDLVEEAWNRIVDKHYVHEVARFFATGWPVNYWRIDAMTDTDFEWFEEKYPGWYNKFGKWWENYNRLAYPGKNKPIAFEDVDYEYPHRCWTCMVPCLIREDMVTDKVDGQWRTYCSETCAWTDKVAFRPEYEGRPTPNMGRLTGFREWETLHHGKDLADIITDLGYVRDDGKTLIPQPHLDLDPKKMWTLDDVRGIPFGSPNVALNEMSDDEREAHIAAYMANKNGAVTV", "text": "FUNCTION: Component of the propane 2-monooxygenase multicomponent enzyme system which is involved in the degradation of propane via the O2-dependent hydroxylation of propane (PubMed:14645271). Under acetone induction, also able to catalyze the oxidation of phenol to yield hydroquinone (PubMed:21183637). SIMILARITY: Belongs to the TmoA/XamoA family."}
+{"protein": "MVKLTSIAAGVAAIAATASATTTLAQSDERVNLVELGVYVSDIRAHLAQYYMFQAAHPTETYPVEVAEAVFNYGDFTTMLTGIAPDQVTRMITGVPWYSTRLKPAISKALSKDGIYTIAN", "text": "SIMILARITY: Belongs to the SRP1/TIP1 family. Seripauperin subfamily."}
+{"protein": "MHCIRPIKAGFNATGDIVYSSKKISKELASFAFPCRKCIPCRLNMAREKAIRAYHESQMWDDNIFLTLTYDDEHLKSDRLQWIDFDLFIKRLNEKLNRGLSKENRRPLPYMVTGEYGDKTKRPHWHVLIFNFRPDDAKKHYVTELGEQVYTSEFIRDLWTHGNIEFGSVTLDSASYVARYAAKKLAHGNDQDHDYHPIHNTSKKHAIGKKWIEKYHEQTFSRGYVVLPNGSQGPIPRYYQDWYKKNHPEKWMEYDAKVKLKSKELAEMQSRKDQLDDFANFINYRGGTNYPLSRTQVKLAILKSKFKQLQEKLKL", "text": "FUNCTION: Plays an essential role in viral DNA replication. Binds the origin of replication and cleaves the dsDNA replicative form I (RFI) and becomes covalently bound to it via phosphotyrosine bond, generating the dsDNA replicative form II (RFII). In turn, viral DNA replication initiates at the 3'-OH of the cleavage site. After one round of rolling circle synthesis, protein VP4 is linked to the newly synthesized ssDNA and joins the ends of the displaced strand to generate a circular single-stranded molecule ready to be packed into a virion. SIMILARITY: Belongs to the microviridae Rep protein family."}
+{"protein": "MATKVKSQAKLRFVSVEQVQSAIKEIGDLSREHTRLATEMNDKIGATSEHYAPKLKALKEEIEPLQKAVQEYCEANRDELTEFGKTKTANFVTGEVQWRQRPPSVAIRGAEAVMEFLQRMGFDRFIRTRQEINKEALLNEPEVAKGIAGVTIKQGLEDFVIKPFEQDAR", "text": "FUNCTION: Protects linear double-stranded DNA of Mu genome from exonuclease degradation. SIMILARITY: To phage Mu protein gam."}
+{"protein": "MSAILSADDLNDFISPGVACIKPIETLPTQPGPEQSQQPQSLEFEVILDGQQPTTGSSSNGTTPPAQISLTDCLACSGCVTSAEAVLVSLQSHNEVLTLLDAAPALRVIQDSDGKPVVSGLENPEAKLFVASVSPQTRASLAAACGGAVTEQQAGWMIEQLLMGPAGLAGGGKHGNGFTWVVDTNTAREACLMLGSDEVLGGGSWGGSDKPTSPILTSSCPGWVCYAEKTHPYVLPHLSRVKSPQALMGTLLKTTLSRVLGIAPDRVWHLAVMPCFDKKLEASREELTDTAWGSGGVPGRGVRDVDCVITSKEILMLAASKGVDFFGLAKSAPVKQPMFPDSDIHRFLFPAQRRKQLRDGGTSGGNLHYIIQDVLSKHAGSQIQMTRGRNADVVEFAVLSSSGETIFKAARYYGFRNIQNLVRKLKPAKASRMPGGKPFGSARRPAGKSATLEHSYVEVMACPGGCTNGGGQIKVDDQVVIDRKNFGEKPGPDEQKAWQAEVDEAYFSGDESDPAQGAGDDQSMELIAGISPSYIRDTLAHWADITGIQLDKLVYTSYREVVSDVGKPISDTERVVQLAGKIGGGW", "text": "FUNCTION: Component of the cytosolic Fe/S protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins. May play a role in the transfer of pre-assembled Fe/S clusters to target apoproteins (By similarity). SIMILARITY: Belongs to the NARF family."}
+{"protein": "MRLDLDFGRGLVAHVMLDNVSEEQYQQISDYFVPLVNKPKLKSRDAIGQAFVMATEVCPDANPSDLWHHVLYRIYIREKIGTDPSQSWVRTSGEAFEVALVERYNPVLARHGIRLTALFKGQKGLALTRMGVADRVGSRKVDVMIEKQGGGRSPDAEGFGVVGGIHAKVSLAERVSDDIPASRIMMGEGLLSVLSTLDVKSFPPPHGDLVNRGELGTPDRPSDKRNYIEGHGDFSACFSYNLRTSPSNATTPSGRHIYVSGFSGQDDEFTDYLVAQLA", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-ACCGGT-3' and cleaves after A-1. SIMILARITY: Belongs to the BsaWI type II restriction endonuclease family."}
+{"protein": "MKLTKFEIARILGARSLQISSGAYATIETKCDSSLKIAYEEIKQGKVPLKPIRPVKA", "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": "MATGTLPDAGQILNSLINSILLVDDDLAVHYANPAAQQLLAQSSRKLFGTPLPELLSYFSLNIGLMQESLAAGQGFTDNEVTLVIDGRSHILSLTAQRLPEGYILLEMAPMDNQRRLSQEQLQHAQQIAARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALMEYTKVIIEQADRLRNLVDRLLGPQHPGMHVTESIHKVAERVVKLVSMELPDNVKLVRDYDPSLPELPHDPDQIEQVLLNIVRNALQALGPEGGEITLRTRTAFQLTLHGVRYRLAARIDVEDNGPGIPSHLQDTLFYPMVSGREGGTGLGLSIARSLIDQHSGKIEFTSWPGHTEFSVYLPIRK", "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": "MTWSYPVDPYWMVALKALLVVVGLLTAFAFMTLIERRLLARFQVRMGPNRVGPFGLLQPLADAIKSIFKEDIVVAQADRFLFVLAPLISVVFALLAFGLIPFGPPGSFFGYQPWVINLDLGILYLFAVSELAVYGIFLSGWASGSKYSLLGSLRSSASLISYELGLGLALLAPVLLVGSLNLNDIVNWQKEHGWLFLYAFPAFLVYLIASMAEAARTPFDLPEAEQELVGGYHTEYSSIKWALFQMAEYIHFITASALIPTLFLGGWTMPVLEVPYLWMFLKIAFFLFFFIWIRATWFRLRYDQLLRFGWGFLFPLALLWFLVTALVVALDLPRTYLLYLSALSFLVLLGAVLYTPKPARKGGGA", "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 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 required for the synthesis of ATP. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
+{"protein": "MDATIAPHRIPPEMPQYGEENHIFELMQNMLEQLLIHQPEDPIPFMIQHLHRDNDNVPRIVILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSYTATEARRLYLQRKTVPSALLVQLIQERLAEEDCIKQGWILDGIPETREQALRIQTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEIQNRLMVPEDISELETAQKLLEYHRNIVRVIPSYPKILKVISADQPCVDVFYQALTYVQSNHRTNAPFTPRVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEKEMAVPDSLLMKVLSQRLDQQDCIQKGWVLHGVPRDLDQAHLLNRLGYNPNRVFFLNVPFDSIMERLTLRRIDPVTGERYHLMYKPPPTMEIQARLLQNPKDAEEQVKLKMDLFYRNSADLEQLYGSAITLNGDQDPYTVFEYIESGIINPLPKKIP", "text": "FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, cilium axoneme Note=Located in the proximal region of respiratory cilia. SIMILARITY: Belongs to the adenylate kinase family."}
+{"protein": "ALKDEFEEHAEKAKTLPENTSNENKLILYG", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ACBP family."}
+{"protein": "SDPAGGEFLAEGGGVR", "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": "MTEKYRPVRDIKPAPAAMQSTKQAGHPVFRSVVAFVSVLVLLVSGLGYLAVGKVDGVASGNLNLGGGRGIQDGNAADGATDILLVGSDSRSDAQGNTLTEEELAMLRAGDEENDNTDTIMVIRVPNDGSSATAVSIPRDTYIHDDDYGNMKINGVYGAYKDARRAELMEQGFTNESELETRAKDAGREGLIDAVSDLTGITVDHYAEVGLLGFVLLTDAVGGVEVCLNNAVDEPLSGANFPAGRQTLGGSDALSYVRQRHDLPRGDLDRIVRQQSYMASLVNQVLSSGTLTNPAKLSALADAVTRSVVIDEGWEIMSFATQLQNLAGGNVTFATIPVTSIDGTGDYGESVVTIDVNQVHAFFQEALGEAEPAPEDGSDDQSADQAPDLSEVEVHVLNASYVEGLANGIAAQLQELGYSIAETGNAAEGLYYESQILAAEEDSAKALAISEALGGLPIVANSSLDDNTVIVVSAGDYAGPTAEANAVTSSTVGQPGADVGEPIESPEFDAGGDGPRCVN", "text": "FUNCTION: Involved in cell wall biosynthesis. May be responsible for the transfer of arabinogalactan onto peptidoglycan. In vitro, has pyrophosphatase activity. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein Note=Localizes at regions of strong cell wall biosynthesis, such as the poles and the division plane. SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family."}
+{"protein": "MKLKSLLIACLLSSLSFSALADRIITDQLDRKVTIPDHINRAVVLQHQTLNIAVQLDATKQIVGVLSNWKKQLGKNYVRLAPELENMAMPGDLNSVNIESLLALKPDVVFVTNYAPSEMIKQISDVNIPVVAISLRTGEVGEKGKLNPTLTDEDKAYNDGLKQGIELIAEVFEKKQQGDELVKAAFANRKLLADRLGDVSADKRVRTYMANPDLGTYGSGKYTGLMMEHAGAYNVAAATIKGFKQVSLENVLEWNPAVILVQDRYPDVVPQILNDQGWANIQALKDKKVFLMPEYAKAWGYPMPEALALGEVWLAKALYPQRFQDVDLDKMVNDYYQKFYRTSYKPDNAAR", "text": "FUNCTION: Part of the ABC transporter complex MolBCA involved in molybdate import (PubMed:22078568, PubMed:24722984). Functions as a low-affinity molybdate transporter (PubMed:24722984). Binds to both molybdate and tungstate, but not to sulfate or phosphate (PubMed:22078568). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 8 family."}
+{"protein": "MKELLEKILRGIVKHPEEVVVMEFDEEGKKVYEIVVNEEDVGQVIGKDGRTIKSLKILLSALMGDSKEITIKVVR", "text": "FUNCTION: A probable RNA chaperone. Forms a complex with KhpB which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KhpA RNA-binding protein family."}
+{"protein": "MAAPAKGENLSLVVHGPGDIRLENYPIPELGPNDVLLKMHSVGICGSDVHYWEHGRIGDFVVKKPMVLGHEAAGTVTKVGELVKHLKPGDRVAIEPGVPREVDEYCKIGRYNLTPTIFFCATPPDDGNLCRFYKHNADFCYKLPDSVTFEEGALIEPLSVGIYACRRGSVSLGNKVLVCGAGPVGMVTLLVAKAMGAAQVVVTDLSASRLTKAKEVGADFTIQVGKETPQEIASKVESLLGSKPEVTIECTGAESSVQTGIYATHSGGTLVIVGMGAEMVNLPLVHAAIREVDIKGVFRYCNTWPMAISMLASKTLNVKPLVTHRFPLEKAVEAFETAKKGVGLKVMIKCDPNDQNP", "text": "FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)- dependent oxidation of various sugar alcohols (By similarity). Is active with D-sorbitol (D-glucitol) leading to the C2-oxidized product D-fructose (PubMed:6852349). 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 and protein tyrosine phosphorylation (PubMed:18799757). Has no activity on ethanol. Cannot use NADP(+) as the electron acceptor (PubMed:6852349). 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": "MANRGPSYGLSREVQQKIEKQYDADLEQILIQWITTQCREDVGQPQPGRENFQKWLKDGTVLCKLINSLYPEGQAPVKKIQASSMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDDGLFSGDPNWFPKKSKENPRNFSDNQLQEGKNVIGLQMGTNRGASQAGMTGYGMPRQIL", "text": "SIMILARITY: Belongs to the calponin family."}
+{"protein": "MKKSLLTIVLAFSFVLGGAALAPTVSEAHGYVASPGSRAFFGSSAGGNLNTNVGRAQWEPQSIEAPKNTFITGKLASAGVSGFEPLDEQTATRWHKTNITTGPLDITWNLTAQHRTASWDYYITKNGWNPNQPLDIKNFDKIASIDGKQEVPNKVVKQTINIPTDRKGYHVIYAVWGIGDTVNAFYQAIDVNIQ", "text": "FUNCTION: Involved in chitin degradation. Catalyzes the oxidative cleavage of glycosidic bonds in both alpha- and beta-chitin via a copper-dependent mechanism, leading to oxidized chitooligosaccharides with a dominance of even-numbered products. Acts synergistically with the chitinase EfChi18A, and combining the two enzymes leads to rapid and complete depolymerization of crystalline chitin, especially with beta-chitin as a substrate. Is likely involved in a chitin degradation pathway that allows E.faecalis V583 to grow on chitin as a carbon source. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MFQFHAGSWESWCCCCLIPADRPWDRGQHWQLEMADTRSVHETRFEAAVKVIQSLPKNGSFQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEMKKIIETMPMTEKVEELLRVIGPFYEIVEDKKSGRSSDITSVRLEKISKCLEDLGNVLTSTPNAKTVNGKAESSDSGAESEEEEAQEEVKGAEQSDNDKKMMKKSADHKNLEVIVTNGYDKDGFVQDIQNDIHASSSLNGRSTEEVKPIDENLGQTGKSAVCIHQDINDDHVEDVTGIQHLTSDSDSEVYCDSMEQFGQEESLDSFTSNNGPFQYYLGGHSSQPMENSGFREDIQVPPGNGNIGNMQVVAVEGKGEVKHGGEDGRNNSGAPHREKRGGETDEFSNVRRGRGHRMQHLSEGTKGRQVGSGGDGERWGSDRGSRGSLNEQIALVLMRLQEDMQNVLQRLQKLETLTALQAKSSTSTLQTAPQPTSQRPSWWPFEMSPGVLTFAIIWPFIAQWLVYLYYQRRRRKLN", "text": "FUNCTION: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters. SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATG37 family."}
+{"protein": "MTEPTWKTVASEKQQQRESKIPSEWQIPKSSHPAPEVTFVQDFPAKSGMFTNRELQLTAATASDVTAKISTGEWTAVEVTTAVCKRAAVAQQLLNCVTEICFDQAIARAKELDAYFEKEGKTVGPLHGLPISFKDQFNVKGFDSTIGYCSYASKPATADSTLVKLLVKAGAIIYVKSNVPITLMMGESFNNIFGRTLNPRNRELTTGGSSGGEAALVTFCASFLGVGTDIGGSLRIPCSFTGLYGLRPSHGRVSYQHVQNTLLGQEAVRSCAGPMCRAPEDIRLFMSSLAAQQPWLWDPQSLPLPWRAEEEVLPKKLCFGFALGDGHVGPKKLKQAGHAVINFNLTEGKEVNEIMNKMFTADGGAEFQRDTDATGEPLPPTVEYWLGHSSQIKASTVSETWKNQHKKALLAQKFLEKWQATKGRTGTSRPIDGLIMPSTPFPASRHGSGWPWHFGDLSALLDLTTGVFPVTRVNLEKDAVPPSWTPMSVKDKEAMDYYEKPENHENALVGLQLIGRRLEEEKVTAMLTLIRNVLEVDY", "text": "FUNCTION: Putative amidase; part of the gene cluster that mediates the biosynthesis of KK-1, a novel cyclic decapeptide compound with potent antifungal activity (PubMed:29686660). The nonribosomal peptide synthetase (NRPS) catalyzes the elongation and cyclization of the decapeptide chain composed of 1 pipecolic acid residue (Pip), 1 alanine residue (Ala), 1 aspartic acid residue (Asp), 1 isoleucine residue (Ile), 1 glycine residue (Gly), 1 tyrosine residue (Tyr) and 4 valine residues (Val) (PubMed:29686660). The Asp, Ile and 3 Val residues are N-methylated by the 5 methyltransferase domains from the NRPS (found in modules 3, 5, 6, 7 and 9), whereas the Tyr residue is O-methylated, probably by the cluster encoded O-methyltransferase OMT (PubMed:29686660). The other tailoring enzymes from the cluster may be involved in further modifications leading to the synthesis of KK-1 (Probable). SIMILARITY: Belongs to the amidase family."}
+{"protein": "MNSEKPDYNYLFKIVIIGDRKTGKTCLMNRFVENTWSEEYRQTNLLHFKVKTIYIDCKIIKLQIWDSQADENFRFNNNNLSNYRSASGFLVVYDCTNENSFSNLKHWIKDIKLYGRPNAINIVVSNKSDLVNEKVIDSDVAKSYCDSLEIPFIETSSKHSSNVEDCFVLLIKNVMKYLETEPTIPQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHQQSSKTKIGCLIQ", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MAEYSKVKSTKLMLKGIKNKSKKNKDKKRKREESDEDKLDIAGNWWSVKNFGEISGTVAIEMDKGAYIHALDNGLFTIGAPHKDDDDGPSPPEQFTAIKLSDSRVALKSGYGKYLGINSDGLVIGRSDAIGAREQWEPVFDTGKMALLASNSCFVGCNEEGDLVAQSKTAGEGEMIKIRSCAEREAKRDDDIPNEDKGNVKQCEINYVYV", "text": "FUNCTION: Binds to mRNA in a sequence-independent manner. May play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. May be involved in mRNA transport. May be involved in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B (By similarity). SUBCELLULAR LOCATION: Nucleus, Cajal body Nucleus, nucleolus Cytoplasm Cytoplasm, myofibril, sarcomere, Z line. SIMILARITY: Belongs to the FRG1 family."}
+{"protein": "MSSSEEVSWISWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPHYRQALDMILDLEPDEELEDNPNQSDLIEQAAEMLYGLIHARYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPMLPIGLSDIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPANQFVPRLYGFKIHPMAYQLQLQAASSFKSPVKAIR", "text": "FUNCTION: Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Participates in Wnt signaling (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the casein kinase 2 subunit beta family."}
+{"protein": "MKKKKTWKRFLHFSSAALAAGLIFTSAAPAEAAFWGASNELLHDPTMIKEGSSWYALGTGLTEERGLRVLKSSDAKNWTVQKSIFTTPLSWWSNYVPNYGQNQWAPDIQYYNGKYWLYYSVSSFGSNTSAIGLASSTSISSGGWKDEGLVIRSTSSNNYNAIDPELTFDKDGNPWLAFGSFWSGIKLTKLDKSTMKPTGSLYSIAARPNNGGALEAPTLTYQNGYYYLMVSFDKCCDGVNSTYKIAYGRSKSITGPYLDKSGKSMLEGGGTILDSGNDQWKGPGGQDIVNGNILVRHAYDANDNGIPKLLINDLNWSSGWPSY", "text": "FUNCTION: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays no activity against heavily substituted arabinans or a range of other polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p- nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is progressively reduced as alpha-(1->5)-chains become shorter or more highly substituted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 43 family."}
+{"protein": "MTLRPSLLPLHLLLLLLLSAAVCRAEAGLETESPVRTLQVETLVEPPEPCAEPAAFGDTLHIHYTGSLVDGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFPPSVPADAVVQYDVELIALIRANYWLKLVKGILPLVGMAMVPALLGLIGYHLYRKANRPKVSKKKLKEEKRNKSKKK", "text": "FUNCTION: PPIases accelerate the folding of proteins during protein synthesis. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FKBP-type PPIase family."}
+{"protein": "MAGQHPPAGEYGEEWARDLRVQFEGLLRDKRMNDLRNTSRQSSPSLGDQSPHMRSSPFPSDNRPSGSQGPALPSYAALRHLPKIPSPPAAGDRDSQKFRNLLISLSLTPTKYENPGLLDEALQTIPLDRIYGEAEEETQVLQAQAESMGDGRKPEWGYQDCVIRALLRWFKRSFFSWVNNPPCPSCLSPTIAQGMTAPTPEESACGALRVELYRCSAQHCGAYERFPRYGDVWRLLQTRRGRVGEWANCFSMLCRAVGGRVRWVWNAEDHVWTEVYSDHQKRWVHVDACEEAWDNPRLYAEGWGKKMSYCIAFSIDGATDVTRRYVRKNQHASERNRCPEEVLLYVMQEIKNMRRSNMNKDERFRLEKEDTREDKELRGYVVASIAQAVTDLVPGSPGGSNHTTASGSDTKLPAEQPGRQTGTSEWLTAQQQQSHSRYQQPRDPSHRRPLP", "text": "SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase family."}
+{"protein": "MKKQPKMTAIALILSGISGLAYGHGYVSAVENGVAEGRVTLCKFAANGTGEKNTHCGAIQYEPQSVEGPDGFPVTGPRDGKIASAESALAAALDEQTADRWVKRPIQAGPQTFEWTFTANHVTKDWKYYITKPNWNPNQPLSRDAFDLNPFCVVEGNMVQPPKRVNHECIVPEREGYQVILAVWDVGDTAASFYNVIDVKFDGNGPVLPDWNPAGQIIPSMDLSIGDTVYTRVFDNEGENPAYRTELKIDSETLTKANQWSYALATKINQTQKQQRAGQLNGDQFVPVYGTNPIYLKEGSGLKSVEIGYQIEAPQPEYSLTVSGLAKEYEIGEQPIQLDLTLEAQGEMSAELTVYNHHQKPLASWSQAMTDGELKSVTLELSEAKAGHHMLVSRIKDRDGNLQDQQTLDFMLVEPQTPPTPGDYDFVFPNGLKEYVAGTKVLASDGAIYQCKPWPYSGYCQQWTSNATQYQPGTGSHWEMAWDKH", "text": "FUNCTION: Probably interacts with GlcNAc residues. May promote attachment to both epithelial cell surfaces and chitin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the GbpA family."}
+{"protein": "MAEDAPVVQQTMLEPEVLLKKRKVNERTRKERVEQAIAKKEAQKKNRKETFKRAETFINNYRQRERERIRLNRSAKNKGDIFVPDETKLLFVIRIAGVKNMPPKIRKVLRLLRLSRINNAVFVRNNKAVAQMLRIVEPYVMYGIPNLHSVRELIYKRGFGKINGQRIALSDNALIEEALGKYDVISIEDIIHEIYNVGSHFKEVTKFLWPFTLTPVKHSLMEKKVKHFNEGRKAGYCGEEINELIKKQV", "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 universal ribosomal protein uL30 family."}
+{"protein": "MIETDRETFTALADDGPAIVRVAADLDIDVAPLTAYDALVADADDHAFLLESAEKTPASDPDGAFTPDTTTEETRHARYSFVGYDPAAVVTVDPDDTTITRLRDDPITDLLDAPDHATGDVLDRLRSVMPAVPRRNIPTEDRQLLDGGLVGFLAYDAVYDLWLDEVGVERPPTPLPDAEFAVTTRTLVFDRATDSVSLVCTPVADADTATDVYDALEAEAKRVQAVLRDATAPATAGIEVTTERAGDRDAYTDAVETAATAVRDGEVYQAVVSRTRELDGDIDPRALYDALRAVNPSPYMFLLAHGDHTVVGASPETLVAVHDDTVVTNPIAGTCQRGASPVADRRLAGEMLADEKERAEHTMLVDLARNDVRRVSAPGTVSVPEFMRVLKYSHVQHIESTVTGTLAADADAFDATRAAFPAGTLSGAPKVRAMEHIDAIEATPRGIYGGGVGYFSWTGDAELAITIRSGTITHTGDEDTLTVRAGAGVVADSDPDAEYEETEAKMDGVLAAVDRLRTTDDGEAVHR", "text": "SIMILARITY: Belongs to the anthranilate synthase component I family."}
+{"protein": "MMRKALLALCVATAFAVAQAQNVAYPNFPYCQCIKSPSPYSLEPVVKSNRTGQYCFTLRVTKPSPSATGYCATKADIKKIEINVNQVCDVFGNVVNATLNGVPTKVGPAFDTPPDGPNTSRILRFTQLNLGLDSDGAMLCITLGQNDKGKGCTTLEDLCAPPAGAPKGTCSLALFDSKPDCCPISRVSPPAPPPPPPPPPPEPVAVPITPPCKTCVYATITALPPLLFPFQLTPSICQSVADKIAGDLEMIVTSYSIGYSGATITCSGNVIKVCASFSLPPGAPYTGLQADISNALTFWLSLLAPSTGCPAYFANHQVTVTVGGDGDPNSVTCLEGTATTTCKPGNPDFPKCECETKPAATRFAALPTLTQEPGRPSNRTNSTLYCFTLQVVAPLNPNGLCGNTTTLLKAELWGNDIPTQRRKILALAFKAAGASSPLRYLSPSWGSAGEQTLKVSGLNWDASQADGAKICMELSNDTNLKTFCNTGQDTCWINLFSPDKQCCPLFAASLTP", "text": "FUNCTION: May be involved in conversion of asexual males and females to the sexual pathway. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
+{"protein": "MSLELEWMPIEDLKLPSNVIEIIKKRGIKKLNPPQTEAVKKGLLEGNRLLLTSPTGSGKTLIAEMGIISFLLKNGGKAIYVTPLRALTNEKYLTFKDWELIGFKVAMTSGDYDTDDAWLKNYDIIITTYEKLDSLWRHRPEWLNEVNYFVLDELHYLNDPERGPVVESVTIRAKRRNLLALSATISNYKQIAKWLGAEPVATNWRPVPLIEGVIYPERKKKEYNVIFKDNTTKKVHGDDAIIAYTLDSLSKNGQVLVFRNSRKMAESTALKIANYMNFVSLDENALSEILKQLDDIEEGGSDEKELLKSLISKGVAYHHAGLSKALRDLIEEGFRQRKIKVIVATPTLAAGVNLPARTVIIGDIYRFNKKIAGYYDEIPIMEYKQMSGRAGRPGFDQIGESIVVVRDKEDVDRVFKKYVLSDVEPIESKLGSERAFYTFLLGILSAEGNLSEKQLENFAYESLLAKQLVDVYFDRAIRWLLEHSFIKEEGNTFALTNFGKRVADLYINPFTADIIRKGLEGHKASCELAYLHLLAFTPDGPLVSVGRNEEEELIELLEDLDCELLIEEPYEEDEYSLYINALKVALIMKDWMDEVDEDTILSKYNIGSGDLRNMVETMDWLTYSAYHLSRELKLNEHADKLRILNLRVRDGIKEELLELVQISGVGRKRARLLYNNGIKELGDVVMNPDKVKNLLGQKLGEKVVQEAARLLNRFH", "text": "FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. A low processivity 3'- 5' helicase. Unwinds short dsDNA substrates with 3'-overhangs (25 bp dsDNA with 25 base overhang), less active on longer dsDNA substrates. Also unwinds the lagging strand of a stalled replication fork (but the leading strand was not tested). Binds ssDNA, but dsDNA about 35-fold less well. Able to displace streptavidin from biotinylated ssDNA, which is partially inhibited by DNA-binding proteins, suggesting it may play a role in stripping proteins from stalled replication forks. SIMILARITY: Belongs to the helicase family. Hel308 subfamily."}
+{"protein": "MLANENSLLTMFRELGSGKLPLQIEQFERGKTIFFPGDPAERVYLLVKGAVKLSRVYESGEEITVALLRENSVFGVLSLLTGQRSDRFYHAVAFTPVQLFSVPIEFMQKALIERPELANVMLQGLSSRILQTEMMIETLAHRDMGSRLVSFLLILCRDFGIPSPDGITIDLKLSHQAIAEAIGSTRVTVTRLLGDLRESKLIAIHKKRITVFNPVALSQQFS", "text": "FUNCTION: Required for full expression of proteins subject to ammonium repression. Transcriptional activator of genes subject to nitrogen control."}
+{"protein": "MMDPAAGSGPDGAAVMPPELPALPVAAEDPMALYRQVLRDFKELFFCLEPMEITRYVHRNEGRCLSLGPPKGWHVMLRTEDGIITAAKQAASKLICCREPLTPLGYAVILLPEPRRDHHDGMVATPYVVFMGRFSRVYAYDTREKYMVLVSHNLDELARYGVSRSEIAYRDVIHTTLRRMTVPVPRRYPKGARTMHVLFLNDTTPEGSYATAERILGCDVKLHTPGYGTVIMRLMKTVQQLHRIWPFCALTEVESRRWWWAVRANLATPWYVLGVTGRPRPGRSFVAEVLVLLDWFGAVYAIQMDDPNHYVRRVANTITEFFRMGLLKMVFRHRRFERERQRQTRMEHRHLCPHHHERAVDHKRDILFNEDAALPDERRERERRILQQQYDWLCLTERFDPHEGAWERLDPNTLVLHRYDTNSQSYVLDPDIVGVEAAEREAAGHQDDTGPRLHCLVTTRSSTREGAERVITALVHQSRLVTYSDPFPLKSLTGVREYIQI", "text": "SUBCELLULAR LOCATION: Virion tegument. SIMILARITY: Belongs to the herpesviridae US22 family."}
+{"protein": "MAMRQTPLTCSGHTRPVVDLAFSGVTPYGYFLISACKDGKPMLRQGDTGDWIGTFLGHKGAVWGATLNKDATKAATAAADFTAKVWDAVSGDELITLAHKHIVKSVDFTQDSNYLLTGGQDKLLRIYDLSKPEAEPDVVSGHTSGIKKALWSSDDKQILSADDKTVRLWDRSTMTEVKALNVAMSVSSMEYVPEGQILVITYGKTIAFHSAETLEQIKSFEAPATINSASLHPEKECLVAGGEDFKLYKYDYNTGEELESYKGHFGPIHCVRFSPDGELYASGSEDGTLRLWQTTVGKTYGLWKCVVPEEENAEAAKARTTLPGTAEEEIEEVASENSDSVYSSTPEVKA", "text": "FUNCTION: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre- mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP plays a role in the cellular distribution of the SMN complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localized predominantly in the cytoplasm but also found in the nucleus. SIMILARITY: Belongs to the WD repeat STRAP family."}
+{"protein": "MAARLIGFFLFQAVSWAYGAQPCIPKSFGYSSVVCVCNASYCDSLDPVTLPALGTFSRYESTRRGRRMELSVGAIQANRTGTGLLLTLQPEKKFQKVKGFGGAMTDATALNILALSPPTQKLLLRSYFSTNGIEYNIIRVPMASCDFSIRVYTYADTPNDFQLSNFSLPEEDTKLKIPLIHQALKMSSRPISLFASPWTSPTWLKTNGRVNGKGSLKGQPGDIFHQTWANYFVKFLDAYAKYGLRFWAVTAENEPTAGLFTGYPFQCLGFTPEHQRDFISRDLGPALANSSHDVKLLMLDDQRLLLPRWAEVVLSDPEAAKYVHGIAVHWYMDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVTGWTDWNLALNPEGGPNWVRNFVDSPIIVDIPKDAFYKQPMFYHLGHFSKFIPEGSQRVALVASESTDLETVALLRPDGSAVVVVLNRSSEDVPLTISDPDLGFLETVSPGYSIHTYLWRRQ", "text": "FUNCTION: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta- D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:24211208). Plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (By similarity). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol (PubMed:24211208). GlcCer containing mono-unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4-enine) (By similarity). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (By similarity). Can also hydrolyze cholesteryl 3-beta-D- glucoside producing glucose and cholesterol (By similarity). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D- galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers (By similarity). Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N- acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Peripheral membrane protein; Lumenal side Note=Interaction with saposin-C promotes membrane [?]association. Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2. SIMILARITY: Belongs to the glycosyl hydrolase 30 family."}
+{"protein": "MSQRFAPGQAPVQSRYQPPPPAPGMRPYPPPGASFPPRGFPLHPNTTQPVPGTANVAGVPGVPGVPGVPGPSLLQRAAQQPGFQSSLRGTGAGGGGVGSGGGSKRSNESRSLGGGGSKSDFATAKKKKKLAEKILPQKVRDLVPESQAYMDLLTFERKLDATIMRKRLDIQEALKRPMKQKRKLRIFISNTFYPSKEPTNDGEEGAVASWELRVEGRLLEDGKGDPNTKIKRKFSSFFKSLVIELDKELYGPDNHLVEWHRTHTTQETDGFQVKRPGDRNVRCTILLLLDYQPLQFKLDPRLARLLGVHTQTRPVIISALWQYIKTHKLQDAHEREYINCDKYLEQIFSCQRMKFAEIPQRLNPLLHPPDPIVINHFIESGAENKQTACYDIDVEVDDTLKNQMNSFLMSTASQQEIQGLDTKIHETVDTINQMKTNREFFLSFAKDPQMFIHRWIISETRDLKLMTDVAGNPEEERRAEFYYQPWTHEAVSRYFFTKVNQKRAELEQALGIRNG", "text": "FUNCTION: Involved in the recruitment and site-specific anchoring of the Brahma complex at specific promoter sites (PubMed:16083904, PubMed:24618901). The Brahma complex is a multiprotein complex which is the equivalent of the yeast SWI/SNF complex and acts by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA (PubMed:16083904, PubMed:24618901). This complex can both serve as a transcriptional coactivator or corepressor, depending on the context (PubMed:16083904). Participates in X-chromosomal dosage compensation (PubMed:16083904). Participates in neurogenesis (PubMed:16083904, PubMed:24618901)."}
+{"protein": "MPIRYISQKLAQQIDVELMSASGAFSLDQLMELAGLSCAQALAKSFPPTKHKHVMVACGPGNQGGDGLVAARHLHHFSYTPTVYLPKPSSKDFLQRLVKQCENLNIPILKDVDAFQTELAKSDVILDAIFGFSFQPPLRKPFDQVLKAIKGVSKKIPIVSVDIPSGWSVTDGPQPLWTEEDDKGGKEMIETFEPEVLVSLTAPKEGVKAFKGQHWLGGRFVPDELGKKHELNIPPYEGIDQVVELPRNH", "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": "MLVDMGEQYMLTTILSFLIVTTVVAYVSWLKTKGDDLKSSKGYFLAGRGLSGLVIGCSMVLTSLSTEQLIGVNAVSYKGNFSVIAWTVPTVIPLCFLALYIIGWL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family."}
+{"protein": "MWPRAPATPPPPPWPSKPSAASRSALRRLDLDDGRRQGTEGEENHAPLLCSPAMASSTAFAAAFALLLLASSAAAEGEAVLTLDAGNFTEVVGAHDFIVVEFYAPWCGHCNQLAPEYEAAAAALRSHDPPVVLAKVDASADLNRGLAGEHGVQGYPTIRILRDRGARSHNYAGPRDAAGIVAYLKRQAGPASVEIAASASPPAADSIANDGVVVVGVFPELSGSEFESFMAVAEKMRADYDFRHTTDAGVLPRGDRTVRGPLVRLFKPFDELFVDSQDFDRDALEKFIESSGFPTVVTFDTSPANQKYLLKYFDNAGTKAMLFLSFSDDRAEEFRTQFHEAANQYSANNISFLIGDVTASQGAFQYFGLKESEVPLVFILASKSKYIKPTVEPDQILPYLKEFTEGTLAPHVKSEPIPEVNDQPVKTVVADNLREVVFNSGKNVLLEFYAPWCGHCQKLAPILEEVAVSLKDDEDVVIAKMDGTANDVPSDFAVEGYPSMYFYSSGGNLLPYDGRTAEEIIDFITKNKGSRPGEATTTESVKDEL", "text": "FUNCTION: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. May play a role in storage protein biogenesis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the protein disulfide isomerase family."}
+{"protein": "MDEAKETVFTKPQNHSSTLEFYDFVTTLLEPLSRIGKTRKSKTSNLDPYELKRKILLDYFNKWRQHVGPDLYPLLRLMLPDLDRERGSYGFKEFGLGKLFIRAMHLSPTSEDAKSLKNWRGSESKHTGDFSTMLQDILQRRAYRTFPGAFTVGDVNALLDQLADASSEDTRVNILEQFYRSLSPLELRWLIPILLKVRKYGTSEKFILSVFHPDAARLYRLCSSLKRICWELYDPSRSLDETETDVEVFSCFQPQLANFKKKDLHQTLEAMGNKPFWIEEKLDGERIQLHMSSGKFQFYSRNARSYTYAYGSSYFDEQSRLTQYIIGAFDKRISQIILDGEMVTWDPVLETVIPYGSLRSIFEDSSSHSSYSPYYVVFDILYLNGKSLVKYSLESRRRILEKVIVRESHRMSILPYKVGSTIEDIEAELRNVIQEGSEGLVIKKPSGSYHLGERMDDWIKVKPYYLQGFGEDLDCLILGGYFGRGKQSGKINSFLCGLRMDYTPKDHSEKFQSFVRVGGGFTYFDRDIIRKETEGKWLPWSSDALEYMELAGTKQDFEKPDMWIHPKDSLVLQIKAAEVVVSNRFKTNYTLRFPRLEKVRLDRSWKDALTINEFFTLKNAVEKQDNVSFHVNKKRKVSQKREKQKKFLYDEPTFKKEASPHSDVLKNLHFVVLPPTELHETKAGLQQIIIENGGLIHQGVGNFGKERLFLVADRVSTRVSIERSKNMCTIIRSQWVMDSVNNQRLMPQWSYLLFSKDEKYSWKTALESLSAKSLSNLLVELKQLDLSKEYSKISDDTSILNLTISKEEASFVGAFPFLKFTVFLDLKGIENSELYDVRMGQYRLTKCILLWNGATIEKDISSKKLTHVVMFVEDSTRLEQLTKACELYQIEPKFVNFEWVVNEWKKASTNILG", "text": "FUNCTION: Involved in ds DNA break repair. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
+{"protein": "MASNSTKSFLADAGYGEQELDANSALMELDKGLRSGKLGEQCEAVVRFPRLFQKYPFPILINSAFLKLADVFRVGNNFLRLCVLKVTQQSEKHLEKILNVDEFVKRIFSVIHSNDPVARAITLRMLGSLASIIPERKNAHHSIRQSLDSHDNVEVEAAVFAAANFSAQSKDFAVGICNKISEMIQGLATPVDLKLKLIPILQHMHHDAILASSARQLLQQLVTSYPSTKMVIVSLHTFTLLAASSLVDTPKQIQLLLQYLKNDPRKAVKRLAIQDLKLLANKTPHTWSRENIQALCECALQTPYDSLKLGMLSVLSTLSGTIAIKHYFSIVPGNVSSSPRSSDLVKLAQECCYHNNRGIAAHGVRVLTNITVSCQEKDLLALEQDAVFGLESLLVLCSQDDSPGAQATLKIALNCMVKLAKGRPHLSQSVVETLLTQLHSAQDAARILMCHCLAAIAMQLPVLGDGMLGDLMELYKVIGRSATDKQQELLVSLATVIFVASQKALSVESKAVIKQQLESVSNGWTVYRIARQASRMGNHDMAKELYQSLLTQVASEHFYFWLNSLKEFSHAEQCLTGLQEENYSSALSCIAESLKFYHKGIASLTAASTPLNPLSFQCEFVKLRIDLLQAFSQLICTCNSLKTSPPPAIATTIAMTLGNDLQRCGRISNQMKQSMEEFRSLASRYGDLYQASFDADSATLRNVELQQQSCLLISHAIEALILDPESASFQEYGSTGTAHADSEYERRMMSVYNHVLEEVESLNRKYTPVSYMHTACLCNAIIALLKVPLSFQRYFFQKLQSTSIKLALSPSPRNPAEPIAVQNNQQLALKVEGVVQHGSKPGLFRKIQSVCLNVSSTLQSKSGQDYKIPIDNMTNEMEQRVEPHNDYFSTQFLLNFAILGTHNITVESSVKDANGIVWKTGPRTTIFVKSLEDPYSQQIRLQQQQAQQPLQQQQQRNAYTRF", "text": "FUNCTION: 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. 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 (Probable). Plays a role in DNA damage response (DDR) signaling during the S phase (PubMed:21659603). May be not involved in the recruitment of cytoplasmic dynein to the nuclear envelope by different components of the INT complex (PubMed:23904267). SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Localizes to sites of DNA damage in a H2AX-independent manner. SIMILARITY: Belongs to the Integrator subunit 7 family."}
+{"protein": "MKKELFSQQDIDDGLDLIIVSYFDRMYGDGKFLDAIDLLSRKWTLNVDGAYCHFPDMNSYDESEHFDGVEFAIGYPPSDAESVIVSEDICYQYVRLACEKYLKLHPEDAEKVKDLLTKLPA", "text": "FUNCTION: Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Protects cells against the tRNA endonuclease activity of cognate toxin CdiA-43969 but not other non-cognate toxins, inhibits the tRNase activity of the isolated CT fragment of CdiA-43969."}
+{"protein": "MFSHVICKFLLTLSFITIIYAAKSESTINKPEKCGLKASSSSTVRIHYRSRVWGQEEYFESTYIREAPLEVKLGNGNLLKGIEDGIHGMCTGEIRRLLIPPNQAYGAIGIPNLVPPNTAIVVDVEMVNVNSPFSLWFWISGLILFSAFLLFGRKPIKGDTSNIKKKE", "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: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily."}
+{"protein": "MSNKPFFYQDPFPLKKDDTEYYLLTSEHVSVAEFEGQEILKVAPEALTLLARQAFHDASFMLRPAHQQQVADILRDPQASENDKYVALQFLRNSDIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEAALARGVYNTYIEDNLRYSQNAALDMYKEVNTGTNLPAQIDLYSVDGDEYKFLCIAKGGGSANKTYLYQETKALLTPGKLKNYLVDKMRTLGTAACPPYHIAFVIGGTSAEANLKTVKLASAKYYDALPTEGNEHGQAFRDIELEKELLLEAQNLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSADRNIKAKINRDGIWIEKLERNPGKYIPEALRQAGEGEAVRVDLNRPMSEILQQLSQYPVSTRLSLNGTIIVGRDIAHAKLKERMDRGEGLPQYIKDHPIYYAGPAKTPEGYASGSLGPTTAGRMDSYVDQLQSQGGSMIMLAKGNRSQQVTDACKKHGGFYLGSIGGPAAVLAQGSIKRLECVEYPELGMEAIWKIEVEDFPAFILVDDKGNDFFQQIQSSQCGAALSNVAALRGGNMIRYFAGERRKRLIRSTPLCCYR", "text": "FUNCTION: Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate. SIMILARITY: Belongs to the class-I fumarase family."}
+{"protein": "WGEQEASILVPGDIVSIKLGDIVPADARIDQSGLTGESLPVTKNPGDEVFSGSTCKTGTLTLNKGIVGMTGDGVNDAPALKTLHGLQAPESTSLNLPNDKELSEIAEQAK", "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 (By similarity). 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": "MTKVAVEKEEPGVVYKVAGSLVIAENMSGTRMYELAKVGWNKLVGEIIRLEGNYAYIQVYEDTSGLSVGDPVIKTGNALSVELGPGILDNIYDGIQRPLERIANVCGDVYIYKGIDMTSLDHDKQWQFYADKKLKLNDIVTGGDIFGFVDENKLFKEHKIMAPPNAKGRLTYIAPDGSYTLKDKIFELEYQGKKYTYGLSHLWPVRDPRPVLEKVTGDTLLLTGQRVLDSLFPTVQGGTCAIPGAFGCGKTCVSQALSKYSNSEVIIYVGCGERGNEMAEILSDFPELTTKVDNEDVGIMQRTCLVANTSNMPVAAREASIYTGITLCEYFRDMGYNATMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGKVKCIGSPSRIGSITIVGAVSPPGGDFSDPVTTATMSIVQAFWGLDKKLAQRKHFPSVNWSTSFSKYVRQLEQYFDNFDQDFLSLRQKISDILQQESDLNDIVQLVGKDSLSEDQKVVMEVAKIIREDFLQQNAFSDYDYMCPLQKTVGMMRIICHFYAQCLRTLQEYDSRERKIGWGSIYNTLRPTINKITHMKFENPKNSDEYFKKYFKALEEEITVGLRNLMEK", "text": "FUNCTION: 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 (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 (PubMed:10915784). During the trophozoite stage, involved in the acidification of the extracellular space next to the cell membrane (PubMed:10915784). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Vacuole Vesicle. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
+{"protein": "MAVAGAVKTSGGVQFCSEFENDDSDFRRVVLLYVDGPFGVGKTVTAKTLMQMPNWRGCRLYLAEPMQAWRQWFGGADMIKEINEIQTLKASGKLECREASPVAVAEVQMTIAAPLRIMNHVIYNYLGSERCYSAAASGPDDVLFLVDRHPLAACLCFPVAQYLSGALEFGDLITLLSGIPDIPTHSNIVLMDLDICEQARRIIQRGRPGETVDWTYLCALRNSYICLMNTTTYLQRTSYPALLKEQEALTSATLLKFKRECLETATVPEINPSIDQTLFAILAFDQQNVHGERLKTVLSFVVQKLATVLKNLCIFYLPAHGLTPEACALKCLEFAETASSLTTKRAAIASLIDAVERYNADMGS", "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": "MATEHLPAERAQSPLSAPQRVEEPQKPNYALRLTLAGHSAAISSVKFSPNGEWLASSAADALIIIWGAYDGKCKKTLYGHSLEISDVAWSSDSSRLVSASDDKTLKLWDVRSGKCLKTLKGHSDFVFCCDFNPPSNLIVSGSFDESVKIWEVKTGKCLKTLSAHSDPISAVHFHCNGSLIVSGSYDGLCRIWDAASGQCLRTLADEGNPPVSFVKFSPNGKYILTATLDSTLKLWDYSRGRCLKTYTGHKNEKYCIFASFSVTGRKWVVSGSEDNMVYIWNLQTKEIVQRLQGHTDVVISAACHPTENIIASAALENDKTIKIWSSDY", "text": "FUNCTION: May function as a substrate receptor for CUL4-DDB1 ubiquitin E3 ligase complex. SIMILARITY: Belongs to the WD repeat WDR5/wds family."}
+{"protein": "MKTLRSTLLLLLFVPLIKPAPPAPQESPLTFDYAADHLEEAIFSQDYEDKYLDGKNIEEKQTMVRSVKRSLELQKDESVTPAPPKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADMPNLRRLDFTGNLIEDIEDGTFSKLALLEELSLAENQLLKLPVLPPKLTLFNAKYNKIKSRGIKANTFKKLNNLSFLYLDHNALESVPPNLPESLRVIHLQFNNITSITDDTFCKANDTRYIRDRIEEIRLEGNPIALGKHPNSFICLKRLPIGTYF", "text": "FUNCTION: Induces bone formation in conjunction with TGF-beta-1 or TGF- beta-2. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class III subfamily."}
+{"protein": "MYGGDEVSAIVVDLGSHTCKAGYAGEDAPKAVFPSVIGAVDGVEAMDVDVDSTKTNSNSEDSKTESEKEKSKRKLYVGSQAMSYRRDHMEVLSPIKDGIVSDWDLVDNIWEHAFKSCLMIDPTEHPMLLAEPPLNTQQQREKAAELMFEKYKVPALFMAKNPVLTSFATGRATSLVVDCGGGSTTISPVHDGYVLQKAVVSSPLGGEFLTDCLLKSLESKGIKIRPRYSFKRKEVRAGEFQVEDVDIPDTTESYKLFCQRMIVGDIKDSICRVPDTPYDDKSYSNIPTTSYELPDGQTLEIGADRFKVPDVMFNPSIVQTIPGMEKYAEMIPSVRGLPHMVMESINKCDVDIRRELYSSILLAGGTSSMQQLKERLEKDLIEESPHSARVKVLASGNTTERRFSVWIGGSILASLGSFQQMWFSKSEYEEHGASYIQRKCP", "text": "FUNCTION: Involved in several developmental processes including organization of plant organs, flowering time, anther development, flower senescence and fertility, probably by regulating the chromatin structure. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localized in the nucleus during the interphase, but is released into the cytoplasm during the mitotic phase (PubMed:12609034). SIMILARITY: Belongs to the actin family. ARP4 subfamily."}
+{"protein": "MVLCFPLLLLLLVLWGPVCPLHAWPKRLTKAHWFEIQHIQPSPLQCNRAMSGINNYAQHCKHQNTFLHDSFQNVAAVCDLLSIVCKNRRHNCHQSSKPVNMTDCRLTSGKYPQCRYSAAAQYKFFIVACDPPQKSDPPYKLVPVHLDSIL", "text": "FUNCTION: Ribonuclease which shows a preference for the pyrimidines uridine and cytosine. Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli. Causes loss of bacterial membrane integrity, and also promotes agglutination of Gram-negative bacteria. Probably contributes to urinary tract sterility. Bactericidal activity is independent of RNase activity. SUBCELLULAR LOCATION: Secreted Lysosome Cytoplasmic granule. SIMILARITY: Belongs to the pancreatic ribonuclease family."}
+{"protein": "MVLWGPVLGALLVVIAGYLCLPGMLRQRRPWEPPLDKGTVPWLGHAMAFRKNMFEFLKRMRTKHGDVFTVQLGGQYFTFVMDPLSFGSILKDTQRKLDFGQYAKKLVLKVFGYRSVQGDHEMIHSASTKHLRGDGLKDLNETMLDSLSFVMLTSKGWSLDASCWHEDSLFRFCYYILFTAGYLSLFGYTKDKEQDLLQAGELFMEFRKFDLLFPRFVYSLLWPREWLEVGRLQRLFHKMLSVSHSQEKEGISNWLGNMLQFLREQGVPSAMQDKFNFMMLWASQGNTGPTSFWALLYLLKHPEAIRAVREEATQVLGEARLETKQSFAFKLGALQHTPVLDSVVEETLRLRAAPTLLRLVHEDYTLKMSSGQEYLFRHGDILALFPYLSVHMDPDIHPEPTVFKYDRFLNPNGSRKVDFFKTGKKIHHYTMPWGSGVSICPGRFFALSEVKLFILLMVTHFDLELVDPDTPLPHVDPQRWGFGTMQPSHDVRFRYRLHPTE", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4- cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis (PubMed:10051404). Controls biliary balance of cholic acid and chenodeoxycholic acid, ultimately regulating the intestinal absorption of dietary lipids (By similarity). 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--hemoprotein reductase) (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Microsome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MSLKPFTYPFPETRFLHAGTNVYKFKIRYGNSIRGEEIEDKGVIIQELEDSIRAVLANMDSLQPFVTEHFIVFPYKSKWERVSHLKFKHGEIILTPYPFVFTLYIEMKCFAESLPSGKPTDDIPLELVLTAKEAEEATMRKRKLMEEPSTPSRPGPHRAKMETWSEASSTKKALKEHKRSWGEDSQQDTPASDSTAVTEQDPMLGHSLPGLVVPPLEHSNPPPLKEPAARGFLGFLSALFPFRYFFRKSTQ", "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. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane. SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass membrane protein Chromosome, telomere Note=In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. SIMILARITY: Belongs to the MAJIN family."}
+{"protein": "MSDLYIHELGDYLSDEFHGNDDGIVPDSAYEDGGQFPILVSNRKKRRNDDMGSGTNHLKSNTFIKREANMLGKNPWPEKDSGGSSVSRDTGTGKDVQDMTLEDTNTSDHGFNGGHVDVVENFSTGDPMLCDTSAATNDGVYNYSLNSIPDAENDLSFFDNGDKEKNDLFYGWGDIGNFEDVDNMLRSCDSTFGLDSLNNEGDLGWFSSAQPNEETAGAMTDDLKPDKMLENQRTAMLQVEDFLNNSEPNHAVEDEYGYTIEDDSAQGKSSQNVFDTSLQKKDILMLDVEANLEKKQTDHLHHLDGKSDGFSENSFTLQHSGISREIMDTNQYYPPSAFQQRDVPYSHFNCEQPSVQVSACESKSGIKSENKPSPSSASNESYTSNHAQSIESLQGPTVDDRFRKVFETRANLLPGQDMPPSFAANTKKSSKTDSMVFPDAAPIQKIGLENDHRKAATELETSNMQGSSCVSSVVDDISLEATSFRQLQQVIEQLDVRTKLCIRDSLYRLAKSAEQRHHGGNRPEKGAGSHLVTGEADKYAGFMDIETDTNPIDRSIAHLLFHRPSDSSLSSDNNVLSYKSHPMIPQPNSSPSLRIEKQEETTELRPEAEVVTSDNN", "text": "FUNCTION: Transcriptional coactivator necessary for expression of the clock genes PRR5 and TOC1 (PubMed:25012192, PubMed:25848708). Antagonizes REV8 function in the regulation of anthocyanin accumulation (PubMed:25848001). Involved in red light input to the clock (PubMed:25012192). Activates clock-controlled genes with afternoon peak (PubMed:23818596). Mediates light inhibition of hypocotyl elongation (PubMed:23818596). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MATMANHDRETTQPTCQNCATSTTPLWRRDEMGQVLCNACGLFLKLHGRPRPISLKTDVIKSRNRVKTMRPDLAKQKKQQQQQQQQQNLAATADMNGGVGMMDPNNPAAAARRASQKSINGHPVDDNSPVSRTGTPNVYNPHIPIDHSLEYQFQAQQIPGFGVPTASPGRAPSPMNGEHMPQTHEQLLAANASLKTRVSELEVIQELYRGRLHQLETEENIRQASEPGKLEAQLRAQIDAMGEAHQQLQKELEESHRRENMLKRRLDELEVELKDVKDALESQDNGRHKKIRLDENVKTEPYAEVVEPQQPEQQQPAPAEQPIPTPMAIDEATPAPAPAPEAAPEQAPAPAPEPVQEQAQEPEPAPVSEPTEASAPAPAPEADSVVPEPTPAAPESAPTEEPAAPETEASEPPTTAPVEEAPKAES", "text": "FUNCTION: Transcriptional regulator that functions in sexual development; disruption of asd-4 gene results in agenesis of ascus and ascospore with macroscopically normal fruiting body formation. The GATA-type zinc finger domain binds to DNA sequences from its own promoter region. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MPDPAAHLPFFYGSISRAEAEEHLKLAGMADGLFLLRQCLRSLGGYVLSLVHDVRFHHFPIERQLNGTYAIAGGKAHCGPAELCEFYSRDPDGLPCNLRKPCNRPSGLEPQPGVFDCLRDAMVRDYVRQTWKLEGEALEQAIISQAPQVEKLIATTAHERMPWYHSSLTREEAERKLYSGAQTDGKFLLRPRKEQGTYALSLIYGKTVYHYLISQDKAGKYCIPEGTKFDTLWQLVEYLKLKADGLIYCLKEACPNSSASNASGAAAPTLPAHPSTLTHPQRRIDTLNSDGYTPEPARITSPDKPRPMPMDTSVYESPYSDPEELKDKKLFLKRDNLLIADIELGCGNFGSVRQGVYRMRKKQIDVAIKVLKQGTEKADTEEMMREAQIMHQLDNPYIVRLIGVCQAEALMLVMEMAGGGPLHKFLVGKREEIPVSNVAELLHQVSMGMKYLEEKNFVHRDLAARNVLLVNRHYAKISDFGLSKALGADDSYYTARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEALSYGQKPYKKMKGPEVMAFIEQGKRMECPPECPPELYALMSDCWIYKWEDRPDFLTVEQRMRACYYSLASKVEGPPGSTQKAEAACA", "text": "FUNCTION: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B- lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD247/CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Note=In quiescent T-lymphocytes, it is cytoplasmic. Upon TCR activation, it is recruited at the plasma membrane by interacting with CD247/CD3Z. Colocalizes together with RHOH in the immunological synapse. RHOH is required for its proper localization to the cell membrane and cytoskeleton fractions in the thymocytes (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily."}
+{"protein": "MAVICNTCGLPEDLCACGDLAKDSTKIIIRLETRRFKKKGTMIEGLDPKLNNLENVAKELKNKYACGGTAKEGYVFLQGDHRDTIKDTLVGLGFPESSIELH", "text": "SIMILARITY: Belongs to the SUI1 family."}
+{"protein": "MAALLKRILRRRMAEKRSGRGRMAAARTTGAQSRKTAQRSGRSEADRRRRVHGQNFLVDRETVQRFVRFADPDPGEVVLEVGAGNGAITRELARLCRRVVAYEIDRHFADRLREATAEDPRIEVVAGDFLKTSQPKVPFSVVGNIPFGNTADIVDWCLNARRLRTTTLVTQLEYARKRTGGYRRWSRLTVATWPEVEWRMGERISRRWFRPVPAVDSAVLRLERRPVPLIPPGLMHDFRDLVETGFTGKGGSLDASLRRRFPARRVAAGFRRARLEQGVVVAYVTPGQWITLFEELHGR", "text": "FUNCTION: Probable RNA methylase. Confers resistance to carbomycin and several other macrolides, lincomycin and vernamycin B, but not to all macrolide-lincosamide-streptogramin B antibiotics. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family."}
+{"protein": "MATSALRGLAVAGGGESSESEDDGWEIGYLDRTSQKLKGQMLPIEEKKEKFKKALTTGDVSLVQELLDSGIISVDATFRYGWTPLMYAASVANAELVRVLLDRGANASFEKDKQTILITACSAHGSEEQILKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVASGAEVNTQDENGYTALTWAARQGHKSIVLKLLELGANKMLQTKDGKLPSEIAKRNKHHEIFNLLSFTLNPLEGKLQQLTKEETICKILTTDSDRENDHIFSSYAEFGDLEVFLHGLGLEHMTDLLKERDITLRQLLTMREDEFTKNGFASKDQQKILAALKELEVEEIQFGELSEEAKLEISGDEFLNFLLKLNKQCGHLITAVQNIITELPVNSQKIALEWASPQNFTSVCEELVNNVEDLSEEVCNLKDLIQKLQNERENDPTHIPLREEVSTWNSRILKRTAITVCGFGFLLFICKITFQRK", "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": "MLRSMLTASTTLNQLQQQIDTISSNLSNSNTTGYKAKDTNFSELVRQQFDQVDEKNEEVAKARKTPPGLRLGVGAMMSSRLVSDQGSIQKTDRDLDIAFTSPYQYLQVNVNGNRQYTRDGALYVTPSAANANQLQLVTGNGYPVLDENGNTVNIDSSMKNITINKNGTLTASDGNAVQRFNLGVVQVNNPQELKSEGNNLFSIDNAAAFEELNGANRQNIGMQQGSLEMSNVDISEQMTDLITSQRSYQLNSRTITMGDQMLGLINSVR", "text": "SIMILARITY: Belongs to the flagella basal body rod proteins family."}
+{"protein": "MRLTLLLAALLGYIYCQETFVGDQVLEIIPSHEEQIRTLLQLEAEEHLELDFWKSPTIPGETVHVRVPFASIQAVKVFLESQGIDYSIMIEDVQVLLDQEREEMLFNQQRERGGNFNFEAYHTLEEIYQEMDNLVAENPGLVSKVNLGSSFENRPMNVLKFSTGGDKPAIWLDAGIHAREWVTQATALWTANKIASDYGTDPAITSLLNTLDIFLLPVTNPDGYVFSQTTNRMWRKTRSKRSGSGCVGVDPNRNWDANFGGPGASSSPCSDSYHGPKPNSEVEVKSIVDFIKSHGKVKAFITLHSYSQLLMFPYGYKCTKPDDFNELDEVAQKAAQALKRLHGTSYKVGPICSVIYQASGGSIDWAYDLGIKYSFAFELRDTAFYGFLLPAKQILPTAEETWLGLKTIMEHVRDHPY", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M14 family."}
+{"protein": "MDPTAPLLTHGGEVEEDYAPARSWTDVKRVLSTESAKLWMIAAPVGFNIICQYGVSSVTNIFVGHIGEVELSAVSISLSVIGTFSFGFLLGMGSALETLCGQAYGAGQVNMLGVYMQRSWIILFVSCFFLLPIYIFATPVLRLLGQAEEIAVPAGQFTLLTIPQLFSLAFNFPTSKFLQAQSKVVAIAWIGFVALSLHVIMLWLFIIEFGWGTNGAALAFNITNWGTAIAQIVYVIGWCNEGWTGLSWLAFKEIWAFVRLSIASAVMLCLEIWYMMSIIVLTGRLDNAVIAVDSLSICMNINGLEAMLFIGINAAISVRVSNELGLGRPRAAKYSVYVTVFQSLLIGLVFMVAIIIARDHFAIIFTSSKVLQRAVSKLAYLLGITMVLNSVQPVVSGVAVGGGWQGLVAYINLGCYYIFGLPFGYLLGYIANFGVMGLWSGMIAGTALQTLLLLIVLYKTNWNKEVEETMERMKKWGGSETTSKDILA", "text": "FUNCTION: Multidrug and toxin efflux transporter involved in flavonoid metabolism. Required for proper reproductive development. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
+{"protein": "MKSCPKCGQQAQDDVQICTQCGHKFDSRQALYRKSTDEDIQTNNIKMRKMVPWAIGFFILILIIILFFLLRNFNSPEAQTKILVNAIENNDKQKVATLLSTKDNKVDSEEAKVYINYIKDEVGLKQFVSDLKNTVHKLNKSKTSVASYIQTRSGQNILRVSKNGTRYIFFDNMSFTAPTKQPIVKPKEKTKYEFKSGGKKKMVIAEANKVTPIGNFIPGTYRIPAMKSTENGDFAGYLKFDFRQSNSETVDVTEDFEEANITVTLKGDTKLNDSSKKVTINDREMAFSSSKTYGPYPQNKDITISASGKAKGKTFTTQTKTIKASDLKYNTEITLNFDSEDIEDYVEKKEKEENSLKNKLIEFFAGYSLANNAAFNQSDFDFVSSYIKKGSSFYDDVKKRVSKGSLMMISSPQIIDAEKHGDKITATVRLINENGKQVDKEYELEQGSQDRLQLIKTSEK", "text": "FUNCTION: Plays a major role in decreasing resistance to glycopeptide antibiotics. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TcaA family."}
+{"protein": "MAQKFTILFTILLVVIAAQDVMAQDATLTKLFQQYDPVCHKPCSTQDDCSGGTFCQACWRFAGTCGPYVGRAMAIGV", "text": "FUNCTION: May play a defensive role against insect attacks. SIMILARITY: To potato MCPI."}
+{"protein": "MHFLKKSIFLVLFLGLVSLSICEKEKREDQNEEEVDENEEASEEKRGLMSILGKVAGNVLGGLFKPKENVQKM", "text": "FUNCTION: Antimicrobial peptide with activity against both Gram- positive and Gram-negative bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Frenatin subfamily."}
+{"protein": "MVVGDISTGTDVAVVGAGPGGYVAAIRAGQLGLDVTLVEKDAYGGTCLNYGCIPSKAMITASGVAHEAGHAEEMGVYADPDVDVAEMVDWKDGVVDQLTGGVEKLCKANGVNLIEGRAEFAGSDKLRVVHGGDGQGSETIEYEHAIVSTGSRPIEVPGFDFGDDPVLDSRQALAMAELPSSMVIVGGGYIGMELSTVFAKLGVDVTVVEMLDGILPQYGDDIARPVRQRAEELGIDFHFGLAADSWTDTDDGIVVTAADEDGEETEFETEKVLVAVGRQPVTDTLNLDAVGLEPNDDGRLETDHEARTDVENVFAIGDVAPGPMLAHKASKEGEVAAEVIAGEPAALDYQAVPAAVFTDPEIGTVGLTEDDAAAQGFDPVVGTFPFNASGRALTTGHDDGFVEVVADEESGFLLGAQIVGPEASELVAELGLAIEMGATLEDVASTIHTHPTLSEATMEAAEHALGHAVHTLNR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MRPSIHRTAIAAVLATAFVAGTALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDLGAGK", "text": "FUNCTION: Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity. SIMILARITY: Belongs to the peptidase M20A family."}
+{"protein": "MAANSTRRPIIAFMSDLGTTDDSVAQCKGLMYSICPDVTVVDVCHSMTPWDVEEGARYIVDLPRFFPEGTVFATTTYPATGTTTRSVAVRIKQAAKGGARGQWAGSGAGFERAEGSYIYIAPNNGLLTTVLEEHGYLEAYEVTSPKVIPEQPEPTFYSREMVAIPSAHLAAGFPLSEVGRPLEDHEIVRFNRPAVEQDGEALVGVVSAIDHPFGNVWTNIHRTDLEKAGIGYGARLRLTLDGVLPFEAPLTPTFADAGEIGNIAIYLNSRGYLSIARNAASLAYPYHLKEGMSARVEAR", "text": "FUNCTION: Involved in the biosynthesis of fluorometabolites. Catalyzes the formation of a C-F bond by combining S-adenosyl-L-methionine (SAM) and fluoride to generate 5'-fluoro-5'-deoxyadenosine (5'-FDA) and L- methionine. It can also use 2'-deoxyadenosine in place of adenosine as substrate. SIMILARITY: Belongs to the SAM hydrolase / SAM-dependent halogenase family."}
+{"protein": "MLRLIALLVCVVYVYGDDVPYSSNQGKCGGHDYEKDGLCCASCHPGFYASRLCGPGSNTVCSPCEDGTFTASTNHAPACVSCRGPCTGHLSESQPCDRTHDRVCNCSTGNYCLLKGQNGCRICAPQTKCPAGYGVSGHTRAGDTLCEKCPPHTYSDSLSPTERCGTSFNYISVGFNLYPVNETSCTTTAGHNEVIKTKEFTVTLNYTDCDPVFHTEYYATSGKEGAGGFFTGTDIYQNTTKVCTLNVEIQCSEGDDIHTLQKTNGGSTMPHSETITVVGSCLSDVNVDIMYSDTNHPGEVDDFVEYHWGTRLRFFPLPKRCTPVS", "text": "FUNCTION: Binds to TNF-alpha and beta. Probably prevents TNF to reach cellular target and thereby deampening the potential antiviral effects of the cytokine."}
+{"protein": "MKISTLLCLLLIATTISPQVLAGPDAVSTPVTCCYNVVKQKIHVRKLKSYRRITSSQCPREAVIFRTILDKEICADPKEKWVKNSINHLDKTSQTFILEPSCLG", "text": "FUNCTION: Chemotactic factor that attracts eosinophils, monocytes, and lymphocytes but not neutrophils. Potent monocyte active chemokine that signals through CCR2. Involved in allergic inflammation and the host response to pathogens and may play a pivotal role during early stages of allergic lung inflammation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
+{"protein": "MRVIRQLHTSKRLLQSLVDKQKYQATTYARPNHLVLTRGKNAILYDDVNNKEYIDFTAGIAVTALGHANPEVAEIMYKQSKKLIHSSNLYYNEECLKLSENLVEATKSFGGQYDASRVFLCNSGTEANEAALKFAKRYGILKSPSKQGIIAFQNSFHGRTMGALSVTSNPKYREPFGSLIPGVEFLNINDELTKLDQQVSSLKEKTAGLIVEPIQGEGGVFPIPLDTLVGLKKICEDHDIIVIYDEIQCGLGRSGKLWAHSYLPKEAHPDIFTTAKALGNGFPIAATVTNDKVNDILKVGDHGTTYGGNPLGSAVGNYVVNVIAEQKFLDEVNKKGEIITNRLRKLQERFPEHIKDIRGKGLMIGCDFDEAPAKIVDAARDSGLLIITAGKTTVRFVPALTIEDNLLEKGLNIFEKAVEKVYS", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MLIKQFSRRPKNMKVQILLAFAALFVLAVGSYASESKKLDLRDASFSAMFSADYQLNPQERGCRYFLGECKKTSECCEHLACHDKHKWCAWDWTIGK", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 12 (Hntx-12) subfamily."}
+{"protein": "MEPNNSFRVDSEFRYTLFPIFYSIVFVLGVIANSYVLWVFARLYPSKKFNEIKIFMVNLTMADLLFLVTLPLWIVYYYNQGDWILPKFLCNLAGCFFFINTYCSVAFLAVITYNRFQAVTRPIKTAQATTRKRGILLSLIIWVSIVGAASYFFVLDSTNREPNKTGSANITRCFEHYEKGSIPVLTIHIFLVFSFFLVFLIILFCNLVIIRTLLTQQVQIQRNAEVKRRALWMVCTVLAVFIICFVPHHLVQLPWTLAELGFQDTDFHQAINDAHQVTLCLLSTNCVLDPIIYCFLTKKFRKHLTEKLYSMRESRKCSRATSETGTEVVMQLKDVPVKSLKY", "text": "FUNCTION: Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth-muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol-calcium second messenger system. May be involved in the morphological and physical modifications of the oviduct and uterus during the estrus cycle and early pregnancy (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MPSWREKHEKIVQSKILVIGAGGIGCELLKNLAVTGFRKVHVIDLDTIDISNLNRQFLFRKEHVSSSKAATATQVVKQFCPQIELTFDHDSIFEKKYNMEFFQAYDIVLNALDNRAARNYVNRMCHAANRPLIDSGSGGYFGQVSVIMRGKTECYECVDKPVQQTTYPGCTIRNTPSEHIHCTVWAKHVFNQLFGEVDIDDDVSPDMDAVDPDNTEAVTTEKEKEAMKEEPAPVGTRQWAESVDYDAAKVFDKLFLHDIEYLCKMEHLWKQRKRPSPLEFHTASSTGGEPQSLCDAQRDDTSIWTLSTCAKVFSTCIQELLEQIRAEPDVKLAFDKDHAIIMSFVAACANIRAKIFGIPMKSQFDIKAMAGNIIPAIASTNAIVAGIIVTEAVRVIEGSTVICNSSIATTQSNPRGRIFGGDATNPPNPRCFVCSEKREVFIYVNPDTMTVGGLCEKVLKQKLNMLAPDVMDSATSRIIVSSDGDTDDLLPKKLAEVSIEDGAILSCDDFQQEMEIKLFIKKGDRLAGDDFEVARSEKEPEPDDRKRKADGSEEPEAKRQKVEEKDDKNGNEAVAEITETMA", "text": "FUNCTION: The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable). SIMILARITY: Belongs to the ubiquitin-activating E1 family."}
+{"protein": "MEKPCTLLVHFDKGSPSMANEIKADLEGSDVAAKVDAMKRAIMLLLNGETLPHLFITVVRYVLPSEDHTIQKLLLLYLEIVDKRDVASGKVLPEMILICQNLRNNLQHPNEYIRGVTLRFLCRLNEPELLEPLIPSILANLDHRHHFIRRHALSAISAIYRLPHGDQLLPDAPEVVERALTGEQDASARRNGFLMLCACAQERAVAYLLTNAERVAEWPDLLQMAAVDLIRKVCRSPNRADKGRYIKIIISLLSAPNSAVVYESAGALVSLSSAPTAVRAAANTYCQLLSSQSDNNVKLIVLDRLHELRASHRDVMVDVVMDVLRALSSPNVDVRRKVLDLVLDLLTPRNVEEVVMYLKKEVVKTQAGDLEKGGEYRQMLVQAIHSCAVEYPEVAGSVVHLLMDFLGDTNVAAAVDVVLFVREIIETNPKLRVSMIQRLIDTFYQIRASRVCSCALWILGEYSLSLSEVESAISTIKQCLGDLPFYTVSEEGESTDASKPAQPVVNSVTVSSRRPVVLADGTYATQSAATETAISSPAVAPGSLSSTQNLRSLILSGDFFLAAVVACTLTKLVLRLEEVQPSKAEANKASTGALLIMVSILQLGQSSYLPHPIDNDSYDRIVLCVRLLCNTGDDVRKVWLQSCRQSFTKMLAEKQFRETEEMKAKAQISHAQPDDLIDFYHLKSRRGMSQLELEDAVQDDLKAATGEFTKDADDANRLNRILQLTGFSDPVYAEAYVTVHHYDIVLDVTVINRTKETLQNLCLELATMGDLKLVDRPQNYTLAPESSKQIRANIKVSSTETGVIFGNIVYETSNVMERSVVVLNDIHIDIMDYISPATCADVAFRNMWAEFEWENKVAVNTVIQDEKEFLDHIIKSTNMKCLTPPSALDGECGFIAANLYAKSVFGEDALVNISVEKQADGKLSGYIRIRSKTQGIALSLGDKITLKQKGGSS", "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 (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."}
+{"protein": "MASRLTPLTLLLLLLLAGDRVTSDMIVGPGNLQEGESEGDSQKGGILDGESIQGNEDSPTLPITNLTVVPATVTKPFSQPATEPVQSTIQPTAEPFCLAPVTSCSDSEIRSAEAVLGEALTDFSLRLYQDFSVLKKRETNFIFSPFSIASLLTQILLGAGGETRVSLEHLLSYPQNFSCVHHALRAFMSEGFTSFSQIFHSSDLTIKDTFAEASQRLYGSSPRPLGNDSTASLELINDWVAKKTNLRIRRLLDSLPEDTRLILLNAVALSAKWKIAFDKGRTSTKPFHLKSSAIKVPMMNSKKYPVASFTDRTLNRPGGRLQLSHNLSFVILVPQTVKHHLQDLEQALSTAVFKAVIKKLEMTKFHPTHLTMPRIKVQSSQDMLDYFDFIYDVNLCGLTEDPDVQVSGIRHQATLELTESGVDATAASVVSVARNLLLFEVQQPFLFLLWDQQHKFPVFMGRVYDPKG", "text": "FUNCTION: May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
+{"protein": "MTQQPSRAGTFGAILRVTSGNFLEQFDFFLFGFYATYIAKTFFPAESEFAALMLTFAVFGSGFLMRPIGAVVLGAYIDRIGRRKGLMITLAIMGCGTLLIALVPGYQTIGLLAPVLVLVGRLLQGFSAGVELGGVSVYLSEIATPGNKGFYTSWQSASQQVAIVVAALIGYGLNVTLGHDEISEWGWRIPFFIGCMIIPLIFVLRRSLQETEAFLQRKHRPDTREIFTTIAKNWRIITAGTLLVAMTTTTFYFITVYTPTYGRTVLNLSARDSLVVTMLVGISNFIWLPIGGAISDRIGRRPVLMGITLLALVTTLPVMNWLTAAPDFTRMTLVLLWFSFFFGMYNGAMVAALTEVMPVYVRTVGFSLAFSLATAIFGGLTPAISTALVQLTGDKSSPGWWLMCAALCGLAATTMLFARLSSGYQTVENKL", "text": "FUNCTION: Uptake of citrate across the boundary 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 major facilitator superfamily. Metabolite:H+ Symporter (MHS) family (TC 2.A.1.6) family."}
+{"protein": "MDAQSSAKVNSRKRRKEASSPNGATEEDGIPSKVQHCSVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYPIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEERSIDLIQTWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPRQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRHKAVTCDISEDEED", "text": "FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis. SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Endoplasmic reticulum Nucleus Note=It can interconvert between an inactive cytosolic form and an active membrane-bound form. SIMILARITY: Belongs to the cytidylyltransferase family."}
+{"protein": "MATVIPSPLSLGEDFYREAIEHCRSYNARLCAERSLRLPFLDSQTGVAQNNCYIWMEKTHRGPGLAPGQIYTYPARCWRKKRRLNILEDPRLRPCEYKIDCEAPLKKEGGLPEGPVLEALLCAETGEKKVELKEEETIMDCQKQQLLEFPHDLEVEDLEEDIPRRKNRAKGKAYGIGGLRKRQDNASLEDRDKPYVCDICGKRYKNRPGLSYHYTHTHLAEEEGEEHTERHALPFHRKNNHKQFYKELAWVPEAQRKHTAKKAPDGTVIPNGYCDFCLGGSKKTGCPEDLISCADCGRSGHPSCLQFTVNMTAAVRTYRWQCIECKSCSLCGTSENDGASWAGLTPQDQLLFCDDCDRGYHMYCLSPPMAEPPEGSWSCHLCLRHLKEKASAYITLT", "text": "FUNCTION: May have an important role in developing neurons by participating in regulation of cell survival, possibly as a neurospecific transcription factor. Belongs to 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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the requiem/DPF family."}
+{"protein": "MQNKIQVKSVEKRENALIFCAENSEIEVKGLSARNHVLVDSDNLSFLYILENESSFIYVSIPHTCWEAMHEAMNNDVVMFVRVNDIEMELEGLKEEVEYLVENIEGNANYGEELVTAVEKVFL", "text": "SIMILARITY: Belongs to the UPF0738 family."}
+{"protein": "MLDMGDRKEVKMIPKSSFSINSLVPEAVQNDNHHASHGHHNSHHPQHHHHHHHHHHHPPPPAPQPPPPPQQQQPPPPPPPAPQPPQARGAPAADDDKGPQQLLLPPPPPPPPTAALDGAKADGLGGKGEPGGGPGELAPVGPDEKEKGAGAGGEEKKGAGEGGKDGEGGKEGEKKNGKYEKPPFSYNALIMMAIRQSPEKRLTLNGIYEFIMKNFPYYRENKQGWQNSIRHNLSLNKCFVKVPRHYDDPGKGNYWMLDPSSDDVFIGGTTGKLRRRSTTSRAKLAFKRGARLTSTGLTFMDRAGSLYWPMSPFLSLHHPRASSTLSYNGTTSAYPSHPMPYSSVLTQNSLGNNHSFSTANGLSVDRLVNGEIPYATHHLTAAALAASVPCGLSVPCSGTYSLNPCSVNLLAGQTSYFFPHVPHPSMTSQSSTSMSARAASSSTSPQAPSTLPCESLRPSLPSFTTGLSGGLSDYFTHQNQGSSSNPLIH", "text": "FUNCTION: Transcription repression factor which plays an important role in the establishment of the regional subdivision of the developing brain and in the development of the telencephalon. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MGRGKVELKRIENKISRQVTFAKRRNGLLKKAYELSVLCDAEVALIIFSTRGRLFEFSTSSCMYKTLERYRSCNYNLNSCEASAALETELSNYQEYLKLKTRVEFLQTTQRNLLGEDLVPLSLKELEQLENQIEISLMNIRSSKNQQLLDQVFELKRKEQQLQDANKDLKRKIQETSGENMLHISCQDVGPSGHASEANQEFLHHAICDPSLHIGYQAYMDHLNQ", "text": "FUNCTION: Probable transcription factor. FUNCTION: Probable transcription factor. May be involved in the control of flowering time. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MVKLFIGNLPREATEQEIRSLFEQYGKVLECDIIKNYGFVHIEDKTAAEDAIRNLHHYKLHGVNINVEASKNKSKTSTKLHVGNISPTCTNKELRAKFEEYGPVIECDIVKDYAFVHMERAEDAVEAIRGLDNTEFQGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPIDRSGRVADLTEQYNEQYGAVRTPYTMSYGDSLYYNNAYGALDAYYKRCRAARSYEAVAAAAASVYNYAEQTLSQLPQVQNTAMASHLTSTSLDPYDRHLLPTSGAAATAAAAAAAAAAVTAASTSYYGRDRSPLRRATAPVPTVGEGYGYGHESELSQASAAARNSLYDMARYEREQYADRARYSAF", "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). 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. 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. 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": "MSDYPPPNYPPPNHPQYQQQQDETYHVRPDMERQQDFGYYEKPTPSQNFDDSFKVEKPKFNDWPFAIFFWLVVAGFIAVAGITLNALRSTYGFQGGSIYGSGNTFTLNTNTIILFAFIIVMAFILSAAIIVFARLAPKAFIVTGVILNVVLGIGTAIFYFVEKYYSAAIVFLIFALFGAWCYWSSRHRIPLSATILTIVIDVMKMYPSTLIASFIGLIFSAAFSALFSIVIVATYVKYDPNSNNEACSVGGGSCSKGKLIGVLVFVFFAGYYISEVIRNVIHVVIAGIYGTWYYLANSDQGAPKHPALSSLKRALTYCFGSITFGSLIVSLIQLLRQFISILRSNFAADGNGWGVCGMIILDFFVGFIDWLVRYLNKYAYCYVALYGKSYIKSAKDTFDLIRFKGMDALINDMFINTALNLYSLFVAYLVALLAYLYLKFTKPEYNSGGAFYAPVIAFAFLIAGQINRISLTVIESGTATFFVALAKDPEIFQMTNRNRFDDIFRNYPQVLEKITSDH", "text": "FUNCTION: Probably involved in transport through the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CTL (choline transporter-like) family."}
+{"protein": "MSSADWMAWIGRTEQVEDDICLAQAIAAAATLEPPSGAPTADSPLPPLWHWFYFLPRAPQSQLSSDGHPQRGGFIPPIPYPRRMFAGARIRFHHPLRIGQPARREGVIRNITQKSGRSGPLAFVTVGYQIYQHEMLCIEEEQDIVYREPGAPVPAPTPVELPPVHDAITRTVVPDPRLLFRFSALTFNAHRIHYDRPYAQHEEGYPGLVVHGPLVAVLLMELARHHTSRPIVGFSFRSQAPLFDLAPFRLLARPNGDRIDLEAQGPDGATALSATVELGG", "text": "FUNCTION: Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. Catalyzes the hydration of 3-methylfumaryl-CoA (mesaconyl-C4-CoA) to (3S)-citramalyl-CoA. SIMILARITY: Belongs to the HTD2 family."}
+{"protein": "MIRNIAIIGLGTMGPGMAARLARGGLQVVAYDVAPAAIERARSMLSVAETVLDALGIALPSAGVGTVRFTDDIGDAVSGADLVIENVPENISIKADVYRTIDGLIGQDTIVASDTSGIPITKLQAHISYPERMVGMHWSNPPHIIPMIEVIAGEKTAPQTVATIRDLIRSIGLLPVVVKKDVPGFVENRVLYALLREAVDLVERGVIDPEDLDTCVSWGIGYKIAVIGPMALLDMAGLDIYKSVSSFLNADLSNRDDVAPMVLEKTSASKFGIKSGEGMFCYTPEQTKALQAERARKLVAVRRILEGRE", "text": "FUNCTION: Involved in the degradation of pyridoxine (vitamin B(6)). Catalyzes the oxidation of 5-formyl-3-hydroxy-2-methylpyridine-4- carboxylate (FHMPC) by NAD(+) to 5-hydroxy-6-methylpyridine-3,4- dicarboxylate (HMPDC) (PubMed:19218190). Can also catalyze the reduction of FHMPC by NADH to 4-pyridoxic acid (PubMed:19218190). SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family."}
+{"protein": "MVQCRPPQEFSFGPRALKDALISCDLALKQLYTSAFSPSERLFLSEAYNPHRTLFSTLLIHSAFDWLLSRPEAPEDFETFHASLQLRKQSLARKHIYLQPIDLSEGLAGCPLLDHLRSCAEAFFLGLRVKCLPSVASASINCCSRPARDTDGLQLHTDGILSFLKNNKPGDALCVLGLTLADLYPHDAWTFTFGRFLPGHEVGVCSFARFSGEFLQAGSSIPDSALLEAAAGGPETLPQEGGQTLCYSALGMVQCCKVTCHELCHLLGLGSCRWLRCLLQGVLSLDEALRRPLDLCPICLRKLHHLLGFRLLERYKRLHTWTRVMLEMWSGQEAGEPSVSEDTLPFSADSGMGCESDTEPVTSPSEPVTPDAWSHTFPDGPEPVSEEGLSSLAASEVLLKLGGPVDALEEYRQWLDACIQALEREVAEEELVQVDAAVDALGRWEMFTGQLPVTKQYMPCVKDNVGLRRVLGDKFSSLRRRLSSRRLAKASSSQCHWGAEN", "text": "FUNCTION: Probable zinc metalloprotease. SIMILARITY: Belongs to the peptidase M54 family."}
+{"protein": "MRVLLTSFAHHTHYYGLVPLAWALLAAGHEVRVASQPALTDTITGSGLAAVPVGTDHLIHEYRVRMAGEPRPNHPAIAFDEARPEPLDWDHALGIEAILAPYFHLLANNDSMVDDLVDFARSWQPDLVLWEPTTYAGAVAAQVTGAAHARVLWGPDVMGSARRKFVALRDRQPPEHREDPTAEWLTWTLDRYGASFEEELLTGQFTIDPTPPSLRLDTGLPTVGMRYVPYNGTSVVPDWLSEPPARPRVCLTLGVSAREVLGGDGVSQGDILEALADLDIELVATLDASQRAEIRNYPKHTRFTDFVPMHALLPSCSAIIHHGGAGTYATAVINAVPQVMLAELWDAPVKARAVAEQGAGFFLPPAELTPQAVRDAVVRILDDPSVATAAHRLREETFGDPTPAGIVPELERLAAQHRRPPADARH", "text": "FUNCTION: Involved in the biosynthesis of the macrolide antibiotics methymycin, neomethymycin, narbomycin, and pikromycin. Catalyzes the attachment of dTDP-D-desosamine onto 12- and 14-membered macrolactone rings 10-deoxymethynolide and narbonolide to produce 10-deoxymethymycin (YC-17) and narbomycin. DesVII is unique among glycosyltransferases in that it requires an additional protein component, DesVIII, for its activity. DesVII can recognize and process not only cyclic substrates of different ring size, but also a variety of linear substrates albeit with reduced, but measurable activities (PubMed:18548476). Both L- sugars and D-sugars are recognized as substrates and variant substitutions at C-3 and C-4 are tolerated, but deoxygenation at C-6 is required (PubMed:16538696). SIMILARITY: Belongs to the glycosyltransferase 28 family."}
+{"protein": "MNSANPCCDPITCKPKKGEHCVSGPCCRNCKFLNPGTICKKGRGDNLNDYCTGVSSDCPRNPWKSEEED", "text": "FUNCTION: Extremely potent and selective inhibitor of integrin alpha- 5/beta-1 (ITGA5/ITGB1). Partially inhibits adhesion of cells expressing alpha-IIb/beta-3 (ITGA2B/ITGB3), alpha-V/beta-3 (ITGAV/ITGB3), and alpha-4/beta-1 (ITGA4/ITGB1) to appropriate ligands only at concentration higher than 500 nM. Weakly inhibits ADP-induced platelet aggregation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin subfamily."}
+{"protein": "MASGPSVFLLNVSGQIESAEFPEFDDLYCKYSFVYGHDWAPTSGVEEGISQITSKSQGGKQALVWNFPIEITFKSTNPFGWPQIVISVYGPDAFGNDVVRGYGAVHLPFTPGRHARTIPMFVPESSSRLQRFTSWFMGRRPEFTDPKVVAQGEGREVTRVRSQGCVTVSFNVVTKDLKKLGYNTGSGDFPNATTMSQP", "text": "FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. SIMILARITY: Belongs to the B9D family."}
+{"protein": "MSWKDTAEPLLVRMPAVQRPEGHVPFKRKLTWTGGVLLLYFFLTNVKLFGLDIDASQQVFGRFSSILASGQGSIMQLGIGPIVTASIVLQLLGGADLLGLNTQDDPRDQILYQGLQKLLVLVMICLTGLPMVFAGGFLPADTAVANSLGIGTAGVQWLIFAQMFVGGVLILFMDEVISKWGVGSGIGLFIVAGVSQRLVGGLLTAPFLGNSEGIIYTWYLFITGERGTGPVLAADGLQTVLLQGELLGLFTTVLIFAVVVYAESVRVEIPLSNARVKGARGRFPVKLIYASVLPMILVRALQANIQFLGRILNAQLGSMPAFLGTYANGQPTGGLFYFLAPIQSRGDWMWWLEGTAQPVWQILTRVGIDLFVMLVGGAVFAVFWVETTDMGPEATAKQIHNSGMQIPGFRQNVGVIEKVLERYIPQVTVIGGALVGLLAVMANMLGTIGGVSGTGLLLTVSITYKLYEEIAEEQLMEMHPMMRQMFG", "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": "MLILTRKVGESINIGDDITITILGVSGQQVRIGINAPKDVAVHREEIYQRIQAGLTAPDKRETP", "text": "FUNCTION: A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability (PubMed:17704818, PubMed:23635605). Post-transcriptionally represses the expression of genes controlled by GacA/GacS (PubMed:15601712, PubMed:23635605). Binds the 5' UTR of mRNA; the mRNA binds to the outside edge to each monomer and each dimer could bind the same mRNA twice (PubMed:17704818). Recognizes a (A/U)CANGGANG(U/A) consensus, binds to GGA (part of the Shine-Dalgarno sequence) in the 5' UTR loop, which prevents ribosome binding (PubMed:17704818, PubMed:24561806, PubMed:23635605). Overexpression represses target protein expression; mutating nucleotides in the 5' UTR abolishes repression in vivo (PubMed:17704818, PubMed:23635605). Binds specifically to small RNAs (sRNA) RsmX, RsmZ and RsmY; these sRNAs fold into secondary structures with multiple GGA sequences in loops to which the CsrA proteins bind (PubMed:15601712, PubMed:16286659, PubMed:24828038). Binding to RsmX, RsmY or RsmZ titrates the protein so that it can no longer bind mRNA and repress translation (PubMed:15601712, PubMed:24828038). RsmZ can bind up to 5 CsrA1 (rsmE) dimers; they bind cooperatively to GGA sequences in RsmZ in a defined order (PubMed:24828038, PubMed:24561806). Required for optimal expression and stability of sRNAs RsmX, RsmY and RsmZ (PubMed:15601712, PubMed:16286659). Four CsrA1 dimers maximally protect RsmZ from RNase activity (PubMed:24828038). Deletion of rsmX, rsmY or rsmZ alone has no detectable phenotype, but a double rsmY-rsmZ deletion has a marked decrease in production of secondary metabolites HCN, exoprotease AprA, antifungal agent 2,4-diacetylphloroglucinol and swarming motility, and protects cucumber plants from fungal infection less well than wild- type; the triple sRNA deletion has even stronger loss of these phenotypes (PubMed:16286659). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CsrA/RsmA family."}
+{"protein": "MEKKNIILNLIGLRCPEPIMVIRKTLRKMKKNEKILVLADDPSTKRDIPYFCYFMEHQLLDRFIHVKPYRYLLKKG", "text": "FUNCTION: Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sulfur carrier protein TusA family."}
+{"protein": "MAERERDREQHERLFKAASNPLRKKMAEKIGNRGITREELKKELGDVSDFEFKFNLDYLIAEGFVVEKDGKLYLTEDGVDLAYGG", "text": "SIMILARITY: To A.fulgidus AF_0255 and AF_1363."}
+{"protein": "MGSACIKVTKYFLFLFNLIFFILGAVILGFGVWILADKSSFISVLQTSSSSLRMGAYVFIGVGAVTMLMGFLGCIGAVNEVRCLLGLYFAFLLLILIAQVTAGALFYFNMGKLKQEMGGIVTELIRDYNSSREDSLQDAWDYVQAQVKCCGWVSFYNWTDNAELMNRPEVTYPCSCEVKGEEDNSLSVRKGFCEAPGNRTQSGNHPEDWPVYQEGCMEKVQAWLQENLGIILGVGVGVAIIELLGMVLSICLCRHVHSEDYSKVPKY", "text": "FUNCTION: Associates with CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MELRVSNTSCENGSLLHLYCSSQEVLCQIVNDLSPEVPSNATFHSWQERIRQNYGFYIGLGLAFLSSFLIGSSVILKKKGLLRLVATGATRAVDGGFGYLKDAMWWAGFLTMAAGEVANFGAYAFAPATVVTPLGALSVLISAILSSYFLRESLNLLGKLGCVICVAGSTVMVIHAPEEEKVTTIMEMASKMKDTGFIVFAVLLLVSCLILIFVIAPRYGQRNILIYIIICSVIGAFSVAAVKGLGITIKNFFQGLPVVRHPLPYILSLILALSLSTQVNFLNRALDIFNTSLVFPIYYVFFTTVVVTSSIILFKEWYSMSAVDIAGTLSGFVTIILGVFMLHAFKDLDISCASLPHMHKNPPPSPAPEPTVIRLEDKNVLVDNIELASTSSPEEKPKVFIIHS", "text": "FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Ba(2+), Mn(2+), Sr(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity). May be a receptor for ligands (trioxilins A3 and B3) from the hepoxilin pathway. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NIPA family."}
+{"protein": "MSRTLDLILLCRLVQDTAHLLMRITLQWDINEMSYFYSASTNGFYSTEFHGTNIPDDAVEISESEWETLINSQGVTKMITCGENGHPVIVDRPSPTPERLALINDEKKSALIAEATNVIAPLQDAVDLGMATDDETKLLLAWEKYRVLLMRVDIKNTEWPKKPEGNK", "text": "FUNCTION: Chaperone involved in tail fiber assembly. SIMILARITY: Belongs to the tfa family."}
+{"protein": "MNNPKYPKVNYIGNKEKIAEWICEQLPVDVRTIADVFSGGCSFSFEAKKRGYQVIANDILNINYQLALALIVNNQEILTACDVDFIFSNPPKSGFMTKNYSDVFFFKEECRELDAIRANILKLNNTYKQALAFALMRRAMIRKMPYSRFTISWEKVKQLRDEEYSYSKYGRRRAYHNQSFEFHFRENLNSYNQAVFNNGNIHQAYNEDVFELLDHIQADAVYLDPPYTGTMNNYFGFYGLLDSYMSGEIRQPFDNHFMDKNQAVELFEKLIEKLKPFKYWLLSYNNVSRPNREELTAMLSRNGRKVTVLETPHVYKVTGKENKQKHTELLFLVENR", "text": "FUNCTION: An alpha subtype methylase that recognizes the double- stranded sequence 5'-GGTGA-3', probably methylates A-5 on the top strand, and protects the DNA from cleavage by the HphI endonuclease. SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
+{"protein": "DPDSIPMIGLSNKQPFSVMMFFMCSYPTQPCQVGFSPAAFSSTPMGAGVKRRASEEEESDQPPKKLFPDGKLFKSNFVLLMDKTGAKIPCPEQPMHF", "text": "FUNCTION: Accessory subunit of the DNA polymerase that acts to increase the processivity of polymerization. SIMILARITY: Belongs to the herpesviridae polymerase accessory protein family."}
+{"protein": "MSFQLDQSTSVIKTAPPGRLEFKNEPIDIASSNIQDLAKMQTLDGYYQQTSLQLPQSQQYHRMYENVYNNQQILYAQTQNFQYPSTLLTNGSLAQTEWRGQQMDTSAYSNTGYSRSSTSQQPQYTQQVTENERIVYKPVDMPSPVDSGIGGDISILNPKEEFFTSADGGSMLERSSERTLSHRDSPLVIPKLYNNLGFQYVLEAPISTSVRRDDDRMTYVNKGQFYTVSLEYTPDLNKCLKSQTVKSQLMVVFREDKTYEEEIKTWQSWHARQHVSKQRILEIDSKNSSGMIGQIEEIGNNAVQFYWNPSDPSGVRISIAVQCLSTDFSTQKGVKGLPLHVQIDTYDGENDKVPFHRGYCQIKVFCDKGAERKLRDEDKRAQKRKVQEYTAGALPGGRKKSDGEYHDQCERSEFYHMRELDKPAALFIAPEEFEPRYVDSTSLSFDMSEIEPIPTKRPRTSERIMLYVRKRDEQIYQPLHVVPASLSGLALAIANKFGADPDKMSGVYKRCAKGITVKVDDEMLRLYCNEDTFIIDVEHATDGSTAATLIEVAPTNPNSYSNS", "text": "FUNCTION: Probable transcription factor (PubMed:12888489, PubMed:36688410). Binds a motif with the core sequence 5'-C[ACT][TG]G- 3' in regulatory elements of target genes (PubMed:12888489, PubMed:36688410). Many putative target genes show oscillating expression levels, perhaps as a result of rhythmic variation in accumulation of grh-1 (PubMed:36688410). Plays a role in proper cuticle formation and/or barrier function and is required repetitively during development, for successful completion of each molt (PubMed:36688410). Involved in modulating lifespan (PubMed:35013237). Plays a role in defense response to bacteria (PubMed:35013237). May act upstream of the p38 MAP kinase / pmk-1 pathway (PubMed:35013237). May act downstream of the insulin/IGF-1 receptor signaling (IIS) pathway (PubMed:35013237). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily."}
+{"protein": "MATIGSGSARVSDTTSTSSAYLMTTNPTATEGNRLLRGASANDASKVPVYHYPPEQDERSKKAPFIEDRLNEELTNPEYVNRLYERWYSEGLSSNEVALGLDQIDNQEVQETYQNLGLGYREYIDWRNSM", "text": "FUNCTION: Secreted effector that suppresses pattern-triggered immunity (PTI) in plant host. SUBCELLULAR LOCATION: Secreted Host cytoplasm Host nucleus. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MTDSQALVPGPSPPHSKAEICYGATFFNISSYGIMEKYETPTVIFGYALPLLELQIILIFVCIVLSHMFLRRIGIPRFVSNILAGLILGPQLLDLLEYSSDRLSLDIPGNVALEGVARLGLVMFTFLMGVKTNKRAVYQIGKRPIVIAVSSFFVTMISGLAFRNFRLDKVDPLYMPLRLAPTERSVIVSIQAVTLLPVITHLVYELKMSNSELGRIAISTAAVSDFLGFLTLVCISYVGTYRYVSPGIANRDIVALIILVLVILFIFKPMAQRIVDMTPEGKPVPKVYLYVTILTAIAASIYLSVFNQMYILGALLVGLAIPDGPPLGSALEARFESLVTNIFFPISIAVMAMKADVVRALYSFDDISFNILLLGLTVVVKWTASFVPCLIFCELPTRESVIIATIMNYKGFVDLCFFDVALRRRNLSRATYTVMIIYVLLNAGILPTIIKALYDPKRKYIGYVKRDIMHLKTNSDLKILTCLHKPDNISGAISLLELLSSPLNNDNKDRGVIAVTALHLVKLAGRTFPILIPHDKRSKARLLQNSYIQTMMLAFTEFQQENWESTTVSSFTAYSHENLMDQDICNLALDHLTSMIIVPSGRKWSPDGEYESDDIMIRRVNESLLDLAPCSVGILNYRGYNKGKKKTNSIINVGVIFIGGKDDREALSLAKWMGQNSRVCLTVIRFLSGQELDKSKNWDYLVDDEVLNDLKATYSLANNFNYMEKVVNGGPAVATTVRLVAEDHDLMIVGRDHEDYSLDLTGLAQWMELPELGVIGDLLASKDLRARVSVLVVQQQQQHG", "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": "MSTPTHNLPRTRVSAFCWVALERSTRIERPTSWSWKELSHYSLIVFHCIPDTTPKQIEECFKKFLRRPDIVIILINQVYADMIRPTVDAHNLAVPTVLEIPSKQHPYDSSRDSILKRAQRVITPPERHY", "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": "MEHDGTAALGWAARDASGHLSPFSFTRRVQEEDDVTIKVLYCGICHTDLHTIKNEWGNAMYPVVPGHEIVGVVAGVGAGVTRFKAGDTVGVGYFVDSCRACDSCGKGDENYCPTMVITSNGTDYGGATTQGGFSDVMVVRQDYVLRVPASLPPDGAAPLLCAGVTVYSPMVEYGLNAPGKHLGVVGLGGLGHLGVKFGKAFGMKVTVISSSPAKREEALERLGADAFLSSRDGEGMAAAAATMDGIIDTVSAGHPLVPLLSLLKPKGQMVVVGAPAAPLQLPAIAIIDGGKRVAGSGGGSVAECQAMLDFAGEHGIAADVEVVAMGDVNAALGRLERNDVRYRFVIDVAGTLHAAAAPS", "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": "MGPRNPSPDHLSESESEEEENISYLNESSGEEWDSSEEEDSMVPNLSPLESLAWQVKCLLKYSTTWKPLNPNSWLYHAKLLDPSTPVHILREIGLRLSHCSHCVPKLEPIPEWPPLASCGVPPFQKPLTSPSRLSRDHATLNGALQFATKQLSRTLSRATPIPEYLKQIPNSCVSGCCCGWLTKTVKETTRTEPINTTYSYTDFQKAVNKLLTASL", "text": "FUNCTION: Functions as a substrate recognition component for CUL4-DDB1 E3 ubiquitin-protein ligase complex, which mediates ubiquitination and proteasome-dependent degradation of nuclear proteins. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MPTRNLLLGSILLSLAVKGDPGPHRGARCGVSPLGSATELNYLSRIVGGRESKKGQHPWTVSLKRNGKHFCGGTLVSHCHVLTAAHCLLDRNVKLYMRVYIGEYDQILKEETEQMFRVIEIFKHPNFNQSQPMNYDVAVLLLDGSVTFDENIQPACLPNPDDVFEPGDLCVTLGWGHLTENGILPVVLQEVYLPIVDLSSCLHVMSALKGTVVSSYIVCAGFPEGGKDACQGDSGGPLLCQRRHGSWVLHGLTSWGMGCGRSWKNNVFLPHNRKGSPGIFTDIQKLLGWVSSQLNTAVPNKNQESCSMQDGVLSGKSGELIFLKNPMSVTRTMSGAPGFSLSLKTCTSCLNFTHLDIESDFACNLDYLAIYTDSHRLIGKFCGDIPPRSLLISFSSIKLNFFSDFHENRTGFVLYYSAVEPNTYPDSGCGSFAVLFEEGEIQSMNYPENYLSNSRCHWIIHGPSGSYIKLQFEDFALEPSDDCRSDYLAVYQDLAAEDKIETFCGFSLPAPVYSTTAVMHIKFSTDERDNDKGFRATFTFVSPNSLVEDSRQGNMPSTNKKETTAQDSICGVSQVPPIFIYNSIAKVEEAVPHSWPWHTSLQYAGEHVCDGAIIAENWILTTASCVLNRKFNDVWLVDPGIHDLLRPGHNQKGLVKQIIPHPSFSSQTNDFDIALVELDESLQFNSDIFPICLPGKTSELAPASLCVVSGWSLRGKEAEKSTKLQQREVPILTDDACSAHYIQNPGGITDRMLCAGIGTGQDNDSCSEQSGSPLVCLLEKKGIYTIFGIASWGVNCKENSKPGIYTKVSPFIDWIRQIMSDTGQIHSNLGDPKPHPMGNIEPEETAGRDIIQGGFPTNDASSNQNLYIASSCEDVVLLQSPGEIKMETKSQMYPNGFSCQWRIIAPKFQIIKLVMKQVHMSAENGKCCNSLIIYEGISKNKTLKVRFPTDEMVPGTVWSEGSSVTIESPPHPVDPEFGFCLVYSFHSRTQSQDHVVPDSDSSEP", "text": "FUNCTION: Converts the glycoprotein envelope surrounding the egg from an unfertilizable to a fertilizable form during its transit through the pars recta portion of the oviduct by selectively hydrolyzing the envelope glycoprotein gp43. The egg envelope is converted to a sperm- penetrable form, via an increase in sperm binding. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MHHQHGLFMLALLAFLLVMTVLGTDTGKKDKQEKKVKKSDCGDWQWSVCVPTSGDCGLGTREGTRSGKECKQTIKTQKCKIPCNWKKQFGAECKYQFQEWGDCDPETGLKTRNGNLKRALHNAECQKTVTLSKPCGKVTKPKLQESKKKKKEGKNKEKLLD", "text": "FUNCTION: Secreted growth factor that mediates its signal through cell- surface proteoglycan and non-proteoglycan receptors (By similarity). Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups (By similarity). Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration (By similarity). Has antibacterial activity against both Gram-positive and Gram-negative bacteria (PubMed:20308059). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pleiotrophin family."}
+{"protein": "MKEIVHEKIQNLDLKEYLINFIDEKNHFSFGILSFKHYVALSGNRSSHILTLAGGIELLILAFDIFDDLEDEDNIEIKWMKIDPSLALNAATTLYTLGLETICSISNSAEFHRLTLKYALNAMQGQHEDLRNSPETEEECIQMMKQKAGSLTAMSAVLAAMLANGEFNQTIEDYAYKIGIIKQLENDYYGLVNDQRSDIRKKRKTLIYLFLNRKFNEASEKILKLINSHTSYHSFISDSSKFDELLFEAGLNQYVSMLIKLYEEEITASMNQLNINIKL", "text": "FUNCTION: Part of a major quorum-sensing system that regulates the development of genetic competence (PubMed:22197102). Involved in the maturation of the competence pheromone ComX (PubMed:22197102, PubMed:25036949). Acts by catalyzing the transfer of a geranyl group on the ComX pheromone (PubMed:22197102, PubMed:25036949, PubMed:31670609). Cannot use farnesyl diphosphate (FPP) (PubMed:31670609). FUNCTION: Part of a major quorum-sensing system that regulates the development of genetic competence (By similarity). Involved in the maturation of the competence pheromone ComX (By similarity). Acts by catalyzing the transfer of a prenyl group on the ComX pheromone (By similarity). SUBCELLULAR LOCATION: Cell membrane. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MAEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFRPENELRDYFEQITGGRTVPRIFFGKTSIGGYSDLLEIDNMDALGDILSSIGVLRTC", "text": "FUNCTION: Has thioltransferase and dehydroascorbate reductase activities. SUBCELLULAR LOCATION: Virion. Note=Localizes to the virion core. SIMILARITY: Belongs to the glutaredoxin family."}
+{"protein": "MSRSGAIIIGLFFIASIFDVFRAEKEPPAEDSRLEDYLSSELETTAIPTVVNENSHSQDVVDSGFSKDLPKLTILYCVSCGYKQAFNQFYEFAKEKYPGLVIEGGNFSPDFWKGCLAQIVGVAKIGLIAIVITGSNPFEYIGFGYPQILQTAHYNRFSYSLLVFMIGNLFESTLSSTGAFEIFLGDKQIWSKISKERVPTQEEFLNLIDLQLKTIR", "text": "FUNCTION: Probably has thioredoxin reductase-like oxidoreductase activity. SUBCELLULAR LOCATION: Cytoplasm Perikaryon Cell projection, dendrite Cell projection, axon. SIMILARITY: Belongs to the SelWTH family. SELT subfamily."}
+{"protein": "MLFRYITFHREKVLYLTAACIFGVYISLHDACIPVVGKIGTNVTLNAVDVLPPRDQVRWSYGPGGQGYMLCIFTGTSTTTFNNTRFNFSCLSNYSLLLINVTTQYSTTYRTMTSLDHWLHQRHNHGSRWTLDTCYNLTVNENGTFPTTTTKKPTTTTRTTTTTTQRTTTTRTTTTAKKTTISTTHHKHPSPKKSTTPNSHVEHHVGFEATAAETPLQPSPQHQHLATHALWVLAVVIVIIIIIIFYFRIPQKLWLLWQHDKHGIVLIPQTDL", "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": "MNTGDKAKSQAVPASGDIDQQALFFHRYPRPGKLEIQPTKPLGNQRDLALAYSPGVAAPCLAIKDNPETAADFTARANLVAVVSNGTAVLGLGNIGPLASKPVMEGKAVLFKKFAGIDVFDIEIDAPTVDRMVDVISALEPTFGGINLEDIKAPECFEVERRLREKMEIPVFHDDQHGTAIIVAAAVLNGLELAGKDIAEAKIVASGAGAAALACLNLLVTLGARRENIWVHDIEGLVYKGREALMDEWKAVYAQESDNRVLADSIGGADVFLGLSAAGVLKPELLARMAEKPLIMALANPTPEIMPEVARAARPDAMICTGRSDFPNQVNNVLCFPHIFRGALDCGARTINEEMKMAAVRAIAGLAREEPSDVAARAYSGETPVFGPDYLIPSPFDQRLILRIAPAVAKAAAESGVATRPIQDFDAYLDKLNRFVFRSGFIMKPVFAAAKNAAKNRVIFAEGEDERVLRAAQVLLEEGTAKPILIGRPQIIETRLRRYGLRIRPDVDFEVVNPEGDPRYRDYVDDYFALVGRLGVIPEAARTIVRTNTTVIGALAVKRGEADALICGVEGRYSRHLRDVSQIIGKRSGVLDFSALSLLISQRGATFFTDTYVSFSPSAEEIAQTTVMAANEIRRFGITPRAALVSHSNFGSRDSESAFKMRTALQLVRELAPDLEVDGEMHGDSAISEVLRQRVMPDSTLNGEANLLVFPNLDAANITLGVVKTMTDSLHVGPILLGSALPAHILSPSVTSRGVVNMAALAVVESSHPV", "text": "FUNCTION: Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria. SIMILARITY: In the N-terminal section; belongs to the malic enzymes family. SIMILARITY: In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family."}
+{"protein": "MGFVLPASFPGASSITTGGSCLRSKQYAKNYYASSYVTTLWHKKGKIQKEYCAVIFSRHNLKQHYKVNEGGSTSKECEKKYVVNAISEQSFEYEPQARDPKNIWGSVNDALDTFYKFCRPYAIFSVVLGATFKSLVAVERLSDLSLAFFIGWLQVVVAVICIHIFDVGLNQLCDIEIDKINKPDLPLASGNLSFRNVVIITASSLILGLGFAWIVGSWPLFWTVFICCMFAAAYNVDLPLLRWKKYPVLTAISFIANVAVTRSLGFFLHMQTCVFKRPTTFPRPLIFCTAIVSIYAIVIALFKDIPDMEGDEKFGIQSLSLRLGPKRVFWICVSLLEMAYGVTILVGATSPILWSKIITVLGHAILASVLWYHAKSTDLTSNVVLQSFYMFIWKLHTAEYCLIPLFR", "text": "FUNCTION: Involved in the biosynthesis of sophoraflavanone G (SFG). Can use flavanones (naringenin, liquiritigenin and hesperetin) as substrates, but not flavonols or isoflavones. Shows a strict specificity for dimethylallyl diphosphate. SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family."}
+{"protein": "MPPRKKEYGIKRASGSLVHFRAPVSATTIRRHSAVVPSVLTFAVIVASGGLLLMIEKGMLNSVQTPPPRANGRKVEYRLRSSSDTAADVESQIVQEIRNRTIRSVCGQRNMPHSVWSLSPLQRKTLLQHILVNDEHRFLYCYVPKVACSNWKRVLKVLSGALANVDIKVKMDHRADLVFLSDLPPEEIRHRLRHYFKFMFVREPMARLLSAYRNKFGEIEAYQRKYGAEIIRRYRKGYAKDKKISGNDVTFTEFTRYLVDEDPERMNEHWMPIYNLCQPCAIEYDFIGSYERLESDASYILERVGAPQHVRFPERQTWYKPVTKETLHYYLCTVPQKFLKELLPKYILDFSLFGYPLPNTTTEYCRH", "text": "FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N- acetylgalactosamine (GalNAc) residue of dermatan sulfate. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 2 family."}
+{"protein": "MGFIVGVVIGLLVGIAIIIGFVKLENSRSKLRSELANTVAAFARMTVEDSRKLLPPEFYPSWVVFSERQKLTWLNHHLTKIWPYVDEAASELIKASVEPVLEQYRPAIVASLTFSKLTLGTVAPQFTGVSVIDGDKNGITLELDMQWDGNPNIVLGVKTLVGVSLPIQVKNIGFTGVFRLIFRPLVEDFPCFGAVSVSLREKKKLDFTLKVVGGDISAIPGLSEAIEETIRDAVEDSITWPVRKVIPIIPGDYSDLELKPVGMLEVKLVQAKNLTNKDLVGKSDPFAKMFIRPLREKTKRSKTINNDLNPIWNEHFEFVVEDASTQHLVVRIYDDEGVQASELIGCAQIRLCELEPGKVKDVWLKLVKDLEIQRDTKNRGEVHLELLYIPYGSGNGIVNPFVTSSMTSLERVLKNDTTDEENASSRKRKDVIVRGVLSVTVISAEEIPIQDLMGKADPYVVLSMKKSGAKSKTRVVNDSLNPVWNQTFDFVVEDGLHDMLVLEVWDHDTFGKDYIGRCILTLTRVIMEEEYKDWYPLDESKTGKLQLHLKWMAQSIYRDS", "text": "FUNCTION: May be involved in membrane trafficking. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the synaptotagmin family."}
+{"protein": "MELIEEIINLDEAIQGETRTEIIYTKSQTPSNIKIIVIAGNPGIESFYQEFVKVLNLSFNSKYDIYGVGHIGHCGKIENKTFSVEEQIKHKELFLEYLLKNKYGDKDRKDIKFILIGHSVGSYISLKVVSRFSEKFEFLSVVNLFPTFKNLYDGLSPFIKMVVMRESTRNGLSTFLHYIPSIVVSNVLKWILPSDESRIAVQSKINYYSALNILYMAYTETEDIKEIDDECHSVFNSRLNQLLFIYGQTDSYTPKSFYDEMKQLYPAGNIEYSSSYVPHAFVLHHSQEVALRVSEWLSLNILKN", "text": "FUNCTION: Probable serine lipid hydrolase associated with lipid droplets. Appears to lack cholesterol esterase activity. Appears to lack triglyceride lipase activity. SUBCELLULAR LOCATION: Lipid droplet. SIMILARITY: Belongs to the AB hydrolase superfamily. LDAH family."}
+{"protein": "MAPTIQTQAQREDGHRSSSHRTVPERSGVVCRVKYCNTLPDIPFDPKFITYPFDQNRFVQYKATSLEKQHKHDLLTEPDLGVTIDLINPDTYRIDPNVTLDIADEKLLEEEIQAPSSSKRSQQHAKVVPWMRKTEYISTEFNRYGVSNEKPEVKIGVSVKQQFTEEDIYKDRDSQISAIEKTFEDAQKPISQHYSKPRVTPVEVMPVFPDFKMWINPCAQVIFDSDPAPKDASGSAALDMMSQAMIRGMMDEEGNQFVAYFLPGEETMRKRKRDQEEGLDYMPEDIYDYKIAREYNWNVKNKASKGYEENYFFIFREGDGVYYNELETRVRLSKRRVKAGVQSGTNAVLVVKHRDMHEKELEAQEARRAQLENHEPEEEEEIEVDQETQGSDAEDGEKGSGSEKEGSGAEQSGSESEREEAEEEEKEDEEEKESSEEDRAARDKEEIFGSDDDDSDEDGPNESGQDGEDSGSDDEEEKGQGRRSRSASSSPFGSDHSQQENEDQSASDQGSGSSTGSDSD", "text": "FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II. PAF1C associates with RNA polymerase II, is involved in transcriptional elongation and in histone modifications including methylation on histone H3 'Lys-4' (H3K4me3) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PAF1 family."}
+{"protein": "MATPSMMPQWAYMHIAGQDASEYLSPGLVQFARATDTYFSLGNKFRNPTVAPTHDVTTDRSQRLTLRFVPVDREDTTYSYKARFTLAVGDNRVLDMASTYFDIRGVLDRGPSFKPYSGTAYNSLAPKGAPNSSQWLAKDTNAGDQALKTHTHGVAAMGGTDITAKGLQIGVDTTENKNEPIYANEIYQPEPQVGEENLQDVENFYGGRALKKETKMKPCYGSFARPTNEKGGQAKFLTDGDGQLTKNHDITMNFFDTPGGTVGQDTELEADIVMYAENVHLETPDTHVVYKPGTSDESSEANLVQQSMPNRPNYIGFRDNFVGLMYYNSTGNMGVLAGQASQLNAVVDLQDRNTELSYQLLLDSLGDRTRYFSMWNSAVDSYDPDVRIIENHGVEDELPNYCFPLDGAGTNATYQGVKVKNGQDGDVNADWEKDPNLASRNQICKGNIFAMEINLQANLWKSFLYSNVALYLPDSYKYTPANVTLPANTNTYEYMNGRVVAPSLVDAYINIGARWSLDPMDNVNPFNHHRNAGLRYRSMLLGNGRYVPFHIQVPQKFFAIKNLLLLPGSYTYEWNFRKDVNMILQSSLGNDLRVDGASVRFDSVNLYATFFPMAHNTASTLEAMLRNDTNDQSFNDYLSAANMLYPIPAKATNVPISIPSRNWAAFRGWSFTRLKTKETPSLGSGFDPYFVYSGSIPYLDGTFYLNHTFKKVSIMFDSSVSWPGNDRLLTPNEFEIKRSVDGEGYNVAQCNMTKDWFLVQMLSHYNIGYQGFHVPEGYKDRMYSFFRNFQPMSRQVVDEINYKDYKAVTLPFQHNNSGFTGYLAPTMRQGQPYPANFPYPLIGQTAVPSVTQKKFLCDRVMWRIPFSSNFMSMGALTDLGQNMLYANSAHALDMTFEVDPMDEPTLLYLLFEVFDVVRVHQPHRGVIEAVYLRTPFSAGNATT", "text": "FUNCTION: Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. SUBCELLULAR LOCATION: Virion Host nucleus Note=Forms the capsid icosahedric shell. Present in 720 copies per virion, assembled in 240 trimers. SIMILARITY: Belongs to the adenoviridae hexon protein family."}
+{"protein": "MRAKLLGIVLTTPIAISSFASTETLSFTPDNINADISLGTLSGKTKERVYLAEEGGRKVSQLDWKFNNAAIIKGAINWDLMPQISIGAAGWTTLGSRGGNMVDQDWMDSSNPGTWTDESRHPDTQLNYANEFDLNIKGWLLNEPNYRLGLMAGYQESRYSFTARGGSYIYSSEEGFRDDIGSFPNGERAIGYKQRFKMPYIGLTGSYRYEDFELGGTFKYSGWVESSDNDEHYDPGKRITYRSKVKDQNYYSVAVNAGYYVTPNAKVYVEGAWNRVTNKKGNTSLYDHNNNTSDYSKNGAGIENYNFITTAGLKYTF", "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. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A26 family."}
+{"protein": "MSKLGEVSLEEDLEKLLSHYPQHAEEIQRAYEFAKEKHGEQKRKTGEPYIIHPLNVALKLAELGMDHETIIAALLHDTLEDTDTTYEEIKERFGERVAKLVEGVTKIGKIKYKSEQAENYRKLILATAEDPRVILLKLSDRLDNVKTLWVFREEKRKKIAKETMEIYAPLAHRLGVWSIKNELEDWAFKYLYPEEYEKVRNFVKESRKNLEEYLRKYVIPKVRKELEKYGIEAEIKYRSKHYYSIWEKTRRKGIRLEDVHDILGVRIIVNTVPECYTVLGIIHSLFRPVPGKFKDYISLPKPNLYQSLHTTVIADKGKLVEFQIRTWEMHERAEKGIASHWAYKEGKNPSDAGVYSWLRELVESIQGSTNPSEVLENLKSNLFFEEVFVFTPKGDLVVLPKGSTPVDLAYKIHTEVGNHCAGAKSNGRIVPLNYELKSGDVVEIITNPNKSPSYEWLSFVKTSRARNKIKQFLKKQERERYLSEGKRILERIREKLGLSHEDLINKIRERVRFDTEEELLLALGKRKISSANLIKLIFPKKKEEKEERRGSSTVFLEDLSNIKHEVAKCCKPIPGDEILGVITRTKGLVLHEKSCSNLKNVLRLNPEKVKEVQLQASGYFQTDIRVVASDRIGLLSDITKVISESGSNIVSSMTNTREGKAVMDFTVEVKNKEHLEKIMKKIKSVEGVKICKRLYH", "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 degradation of ppGpp into GDP. It may also be capable of catalyzing the synthesis of ppGpp (By similarity). SIMILARITY: Belongs to the RelA/SpoT family."}
+{"protein": "MSSTLIVQLDMRTLCQEADVTADCVIEIVEHGIVEPSGRTPEDWLFDDQAPLLTRRAAKLHQELELEWEGVALALELLQEVQQLRSENSMLRQRLGRFTQM", "text": "FUNCTION: Interacts with CbpA and inhibits both the DnaJ-like co- chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. SIMILARITY: Belongs to the CbpM family."}
+{"protein": "MHTKVLQQGLWALLLWPHLFTVSVPLDCRDDQASLARCPSISQEKLLDRVIHHAELIYRVSEESCSLFEEMFIPLPLRLQSNQGGYACITKALPIPSSKSEIQQLSDKWLLHSVLMLVQSWIEPLVYLQMTLDRYDHAPDMLLNKTKWVSEKLISLEQGVVVLIKKMLDEGAMTTTYSEQGAFQYDVQLEMLEYVMRDYTLLTCLKKDAHKMETFLKLLKCRQTDKYNCA", "text": "FUNCTION: Selectively regulates proliferation and morphogenesis of neural-crest derived pigment cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
+{"protein": "MSSSSSPFFHPPPQQVMDDTTQQSPSYSQNSNSPSQHTFESMEPAAGGSTSMRYSPSGSSEADNPTLGLFSAQASYPYSLRKRRPCLTKDEDLCFPITAATADETPQPTMKKFKLECLSPGEARDFSIEDESGTNLEAKMETTECEPEEEEAVEEEDQQDHINRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELYCNLYDYRIPLFHPSHAKFEFREQSRWRDGNPWKESHRQLHHGVHVMKEPRVNLRSVNYRCFDQIEKAQSFLEEDEYREKLIFLHTGVHEPIDTILINTDVQIIGASDSRDITSSVVLEGSKNTALTFTDGSANAYFGFITVRFRADPVCRQQPQIAQQAQQMNHFYSILVTDKDAMPYIERCDITSKVGNGAAVCVKKSAAPKFKYCTVLDCENVGIYITDNATGHYEHCEIARNTLAGVWVKNHANPYFRKCTIHSGKDVGVFTFEHGQGYFEKCNIHSNRISGIEVKNSANPVVIRCEVHHGYTGGIYVHERGRGQFMENRIYANAYAGIWITSHSDPTIRKNEIFTGQQGGVYIFGEGRGLIEQNNIYGNALAGIQIRSQSDPIVRLNKIHDGLHGGIYVHEKGRGLIEENEVYGNTLAGIWVTTGSSPILRKNRIHSGKQVGVYFYDQGHGLLEENDIFNHLYSGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAMAGVWIKTDSEPTLRRNKIYDGRDGGVCIFNRGKGLLEDNEIFRNAQAGVLISTESNPTLRRNRVFDGKSAGIEITNGATATLEENQLFRNKYGGLCVATGVTPVQRGNRIYDNHDTISRAIKTGLCLFKVSSNNSFPMHNFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLERHCHLQNVPRDNDTVYDSATPISTETGTEI", "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 including blmp-1 (PubMed:17336909, PubMed:23431138, PubMed:24613396, PubMed:24968003). Heterochronic protein which is required for the timing of gonad development and epidermal seam cell differentiation (PubMed:17336909). Regulates tail-spike cell death through inhibition of the apoptosis regulator ced-9 (PubMed:23431138). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MGVCGSLFLPWKCLVVVSLRLLFLVPTGVPVRSGDATFPKAMDNVTVRQGESATLRCTIDNRVTRVAWLNRSTILYAGNDKWCLDPRVVLLSNTQTQYSIEIQNVDVYDEGPYTCSVQTDNHPKTSRVHLIVQVSPKIVEISSDISINEGNNISLTCIATGRPEPTVTWRHISPKAVGFVSEDEYLEIQGITREQSGYYECSASNDVAAPVVRRVKVTVNYPPYISEAKGTGVPVGQKGTLQCEASAVPSAEFQWYKDDKRLVEGKKGVKVENRPFLSKLIFFNVSEHDYGNYTCVASNKLGHTNASITLFGPGAVSEVSNGTSSRRAGCLWLLPLLVLHLLLKF", "text": "FUNCTION: Neural cell adhesion molecule. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family."}
+{"protein": "MMTDLKQSHSVRLNDGPFMPVLGFGTYAPDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKGSS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MKPKNWLILKRKVRFGDCDSAGVIHFHNLLRWAHESWEESIDIYGIPHQDIFPDSNSHKNQIICPIVNCEANFLSPIKIGDLLSIKIFPKKINNHLFQVNTFFLKDEINVAEGKIIHCSLDVDSKLKVKLPDQLERWIEASNINTNLKEC", "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": "MSSSMLNFTASRIVSLPLLSSPPSRVHLPLCFFSPISLTQRFSAKLTFSSQATTMGEVVDAGMDAVQRRLMFEDECILVDENDKVVGHESKYNCHLMEKIESENLLHRAFSVFLFNSKYELLLQQRSATKVTFPLVWTNTCCSHPLYRESELIDENCLGVRNAAQRKLLDELGIPAEDLPVDQFIPLSRILYKAPSDGKWGEHELDYLLFIIRDVNLDPNPDEVAEVKYMNRDDLKELLRKADAEEEGVKLSPWFRLVVDNFLFKWWDHVEKGSLKDAADMKTIHKL", "text": "FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). SIMILARITY: Belongs to the IPP isomerase type 1 family."}
+{"protein": "MSILALVEDRPTPREVYNWRVYLLAAVASFTSCMIGYDSAFIGTTLSLQSFQNEFNWESLNTDLISANIVSLYQAGAFFGALFAYPIGHFWGRRWGLMFSALIFFLGAGMMLGANGDRGLGLIYGGRVLAGIGVGAGSNICPIYISEMAPPAIRGRLVGVYELGWQIGGVVGFWINYGVDETLAPSHKQWIIPFAVQLIPAGLLIIGALLIRESPRWLFLRGNREKGIETLAWIRNLPADHIYMVEEINMIEQSLEQQRVKIGLGFWKPFKAAWTNKRILYRLFLGSMLFLWQNGSGINAINYYSPRVFKSIGVSGGNTSLLTTGIFGVVKAVITFVWLLYLIDHFGRRNLLLVGAAGGSVCLWIVGGYIKIAKPENNPEGTQLDSGGIAAIFFFYLWTAFYTPSWNGTPWVINSEMFDPTVRSLAQACAAASNWLWNFLISRFTPQMFTSMGYGVYFFFASLMILSIVFVFFLIPETKGVPLESMETLFDKKPVWHAHSQLIRELRENEEAFRADMGASGKGGVTKEYVEEA", "text": "FUNCTION: Integral membrane transporter that imports quinic acid to be catabolized as a carbon source. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell membrane. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
+{"protein": "MMEDDGQPRTLYVGNLSRDVTEVLILQLFSQIGPCKSCKMITEHTSNDPYCFVEFYEHRDAAAALAAMNGRKILGKEVKVNWATTPSSQKKDTSNHFHVFVGDLSPEITTEDIKSAFAPFGKISDARVVKDMATGKSKGYGFVSFYNKLDAENAIVHMGGQWLGGRQIRTNWATRKPPAPKSTQENNTKQLRFEDVVNQSSPKNCTVYCGGIASGLTDQLMRQTFSPFGQIMEIRVFPEKGYSFVRFSTHESAAHAIVSVNGTTIEGHVVKCYWGKESPDMTKNFQQVDYSQWGQWSQVYGNPQQYGQYMANGWQVPPYGVYGQPWNQQGFGVDQSPSAAWMGGFGAQPPQGQAPPPVIPPPNQAGYGMASYQTQ", "text": "FUNCTION: RNA-binding protein involved in alternative pre-RNA splicing and in cytoplasmic stress granules formation (PubMed:1326761, PubMed:8576255, PubMed:17488725, PubMed:10613902). Shows a preference for uridine-rich RNAs (PubMed:8576255). Activates splicing of alternative exons with weak 5' splice sites followed by a U-rich stretch on its own pre-mRNA and on TIA1 mRNA (By similarity). Promotes the inclusion of TIA1 exon 5 to give rise to the long isoform (isoform a) of TIA1 (PubMed:17488725). Acts downstream of the stress-induced phosphorylation of EIF2S1/EIF2A to promote the recruitment of untranslated mRNAs to cytoplasmic stress granules (SG) (PubMed:10613902). Possesses nucleolytic activity against cytotoxic lymphocyte target cells (PubMed:1326761). May be involved in apoptosis (PubMed:1326761). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytolytic granule Cytoplasm, Stress granule Note=Nuclear import seems to be coupled to RNA polymerase II transcription and may be dependent on RNA-binding (By similarity). Accumulates in cytoplasmic stress granules (SG) following cellular damage (PubMed:10613902)."}
+{"protein": "MTTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLDCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSPPPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNITAGNRAQIQTVIDANIFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQEAKRNGTGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGTEDEDSSIAPQVDLNQQQYIFQQCEAPMEGFQL", "text": "FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the importin alpha family."}
+{"protein": "MSRVIVKGLPIYLKEDRLRDLIEKRLTQKHQSTDVQSYLSDVKLMKNRDGESRRFAFIGFRDEEDAFDCVNYFNGTFVDTSKIEVSMAKSFADPRVPQPMREKRREALKRLREREELLLADKKDSQKKQKSDSNNDGGKKHDIDAEIAKNKQLQEFINTMKPSSQVTSWETVQSSKTQGEDEEAADDEVGEMSSNPLLSQALALKGNSRDADEDTDMFKLPGNESDDEYVSLNGGSNNANTDEPEPQMMSLDTFDTAGPTSTDDMAKDEAVSDLDWLKNRRVRIKDGADTPVSKQQQQPDTEQQQPEETEVETSQESEEEKSLKKIRETGRLFLRNILYTATEDDFRKLFSPYGELEEVHIAVDTRTGQSKGFAYVLFKNADNAATAFVELDKQIFQGRLLHILPADAKKSHKLDEFDLKNLPLKKQRELKRKANSAQQTFSWNSLYMNQDAVLSSVADKLGMKKSELIDAENSSSAVKQALAEASVIGDVRKFFETRGVDLTKFAQLKNSERDDRVILVKNFPYGTTREEIAELFLPFGKLQRLLLPPSGTIAILQFRDVPAARAAFSKISYKRFKDGIIYLEKGPSDCFTRDAQGDELVESETDIQKATAKEAKISGADLLEAQSLPAADKDDHDDDDDDDDVQAGPTVSIFIKNLNFSTTSQQLTEKFKPFNGFVVAQVKTKPDPKQPGKTLSMGFGFAEFKTKEQANAVISAMEGTILDGHKLQLKLSHRQGTSTTNASSKKKKKNQGKIIVKNLPFEATRKDVFELFSSFGQLKSVRVPKKFDKSARGFAFVEFLLPKEAENAMDQLQGVHLLGRRLVMEFVEQDPEDVEQQIEKMTRKVKKQVNTTKIANMRNSGKRKIDLDEDDENDGLQG", "text": "FUNCTION: Involved in pre-rRNA processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RRM MRD1 family."}
+{"protein": "MPENRSYNDELNFLDKIDANTWRIKKGFVPNMKVDGFFYVNDLLEKLMFDELRQHSRAAGFGGFLPAMKQIANVAALPGIVQKSVGLPDVHAGYGFAIGNLAAFDMSNPEAVVSPGGVGFDINCGVRLLRTNLDERDVQPVKDELAQAMFDHIPVGVGSKGVIPMGARDLEEALEMGVDWSLREGYAWAEDKEHCEEYGRMLNADQSAVGSKAKKRGLPQLGTLGAGNHYAEIQVVDEIFDDYASQRMGIDHKGQVVVMIHSGSRGFGHQVATDALVAMEKAMKRDKVLTNDRQLACARIHSPEGQEYLKGMACAANFAWVNRSSMTFLSRQAFAKVFNTTPDDLDMQLIYDVSHNIAKMEEHISFQLSTTLLVHRKGSTRAFPPHHPLIPVDYQLSGQPVLIGGTMGTCSYVLTGTEKGMEQTFGTTCHGAGRAWSRAKSRRNLDYQEVLDRLAELGISIRVASPKLVMEEAPESYKNVTDVVNTCHAVGISKKAIKLRPIAVIKG", "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": "MTQTTHHTPDTARQADPFPVKGMDAVVFAVGNAKQAAHYYSTAFGMQLVAYSGPENGSRETASYVLTNGSARFVLTSVIKPATPWGHFLADHVAEHGDGVVDLAIEVPDARAAHAYAIEHGARSVAEPYELKDEHGTVVLAAIATYGKTRHTLVDRTGYDGPYLPGYVAAAPIVEPPAHRTFQAIDHCVGNVELGRMNEWVGFYNKVMGFTNMKEFVGDDIATEYSALMSKVVADGTLKVKFPINEPALAKKKSQIDEYLEFYGGAGVQHIALNTGDIVETVRTMRAAGVQFLDTPDSYYDTLGEWVGDTRVPVDTLRELKILADRDEDGYLLQIFTKPVQDRPTVFFEIIERHGSMGFGKGNFKALFEAIEREQEKRGNL", "text": "SIMILARITY: Belongs to the 4HPPD family."}
+{"protein": "MSSKKAKTKNEASSSRGGIGGESIVADCGRNKSTCGYCKSSTRFSISHGLWTERLTVNDYQALLDSGWRRSGCYLYKPEMEKTCCPSYTIRLKASDFVPSKEQQRVRRRIERFLDGELDAKPSEQTEDQDVSFSREVSVSVKKSLGAAKREKNNELEPIMKDLSEQIDNAVQKCIQSGEFPSNVQIPKASVKKVFSAKRKKLAEGSEDLLYTSNIAFPIVAAMKHTQTLEKGKNVEENRLSPEAVSEKLLSAMNKVGEFTGFSVKVSKGHINFLSATQVTSSDRNEGEESLCATTIKSSSNKLHARKRKLEMHLKRSSFEPEEYELYKRYQMKVHNDKPESISETSYKRFLVDTPLTEVPSSGYDDEEKIPLCGFGSFHQQYRVDDRLIAVGVIDILPKCLSSKYLFWDPDFASLSLGNYSALQEIDWVKQNQAHCSTLEYYYLGYYIHSCNKMRYKAAYRPSELLCPLRYQWVPFEVAKPLLDKKPYSVLSNISKVSSSSSSPQASETLLESTSEHEDMEQGDTNDDDDEMYNSDEDSDSDSSSSRNRSDITNILISLNGPRLRYKDIPRFKNPVVQKQLESMLVSYRKVVGAELSEIMVYELR", "text": "FUNCTION: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Component of the N-end rule pathway with ATE1 and PRT6 (PubMed:19255443, PubMed:19620738, PubMed:22020282). The N-end rule pathway regulates seed after-ripening, seedling sugar sensitivity, seedling lipid breakdown, and abscisic acid (ABA) sensitivity of germination (PubMed:19255443). The end-rule pathway regulates various aspects of leaf and shoot development (PubMed:19620738). Involved in the oxygen-dependent N-arginylation of RAP2-12, an activator of hypoxic gene expression. This N-terminal modification leads to ubiquitination by PRT6 and subsequent degradation of RAP2-12 under aerobic conditions (PubMed:22020282). Involved in disease resistance (PubMed:27173012). The end-rule pathway plays a role in regulating the timing and amplitude of the immune response following infection with the bacterial pathogen Pseudomonas syringae pv tomato (PubMed:27173012). Regulates the biosynthesis of plant-defense metabolites such as glucosinolates, and the biosynthesis and response to the phytohormone jasmonate (JA), which plays a key role in plant immunity (PubMed:27173012). SIMILARITY: Belongs to the R-transferase family."}
+{"protein": "MLRRKPTRLELKLDDIEEFENIRKDLETRKKQKEDVEVVGGSDGEGAIGLSSDPKSREQMIIDRIGYKPQPKPNNRSSQFGSLEF", "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. May recruit the E2 ubiquitin-conjugating enzymes to the complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CDC26 family."}
+{"protein": "MTMRAARLSGSTGLTAALVAVLLVLTGCASLPESSAPQALGTIDREPTSEGPTPPIAGRDPDLLLRDFLQATADPTNRHLAARQYMTPAASAQWDDSTSTTIVEKPDTLLESRDGDRATYRIRAQRMAELSADGAYRAVNEPTLENKIEMVKVDGEWRIAELPDGVVMDITAFTKSYRRYVLYFADPSGNTAVPDLRWLSVPKNQLTQRLLSLLSEGPHGAIGAVVRNQLAAPVALRGPITKANGDPDDVGVGLGGVRLDFAGAAALSQRDKELLAGQVVLTLAQADIPGPYMLLADGRPLDERYATNGWSAADVEYLSPSVQAQNRIGLHALRDGALTQVTDNGVVETPGYFGSVNNLQSAALSPDGQLVAAVADAGRPAPEPPRTLMVGTYGGPAFPVAEGGSITRPSWTGDGSAAWAVIDGDRVIRAVNDRATGTVSVQGVDISGLTADPAGPALRLPITELRISRTGVRAALIADGKVYVAVVERRPDGGYALTAPVPVAVGLSTKATSLSWIGGDTLLIAREGNIDPVSTVLIDGSEWTPVTSQNLTPPVRVITAAPGAQYVADSRGVLELTSNTTSELHYWTEMPGLVGTDAAPVLPG", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the LpqB lipoprotein family."}
+{"protein": "MMFSGFNADYEASSFRCSSASPAGDSLSYYHSPADSFSSMGSPVNTQDFCADLSVSSANFIPTVTATSTSPDLQWLVQPTLVSSVAPSQTRAPHPYGLPTQSAGAYARAEMVKTVSGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDKKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEASTPESEEAFTLPLLNDPEPKPSLEPVKSISNVELKAEPFDDFLFPASSRPSGSETSRSVPNVDLSGSFYAADWEPLHSNSLGMGPMVTELEPLCTPVVTCTPLLRLPELTHAAGPVSSQRRQGSRHPDVPLPELVHYREEKHVFPQRFPST", "text": "SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the bZIP family. Fos subfamily."}
+{"protein": "MKLTDADNAADGIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI", "text": "FUNCTION: Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits."}
+{"protein": "MSKNKDQRTAKTLERTWDTLNHLLFISSCLYKLNLKSVAQITLSILAMIISTSLIIVAIIFIASANHKITSTTTIIQDATNQIKNTTPTYLTQNPQLGISPSNPSDITSLITTILDSTTPGVKSTLQSTTVGTKNTTTTQAQPNKPTTKQRQNKPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKRTTTKPTKKPTPKTTKKGPKPQTTKSKEAPTTKPTEEPTINTTKTNIITTLLTSNTTRNPELTSQMETFHSTSSEGNPSPSQVSITSEYPSQPSSPPNTPR", "text": "FUNCTION: [Isoform Secreted glycoprotein G]: Helps the virus escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fc-gamma receptors. FUNCTION: [Isoform Membrane-bound glycoprotein G]: Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities. SUBCELLULAR LOCATION: [Isoform Secreted glycoprotein G]: Secreted Note=The protein is shed from infected cells before the appearance of progeny virus. The initiation at the downstream methionine removes a portion of the transmembrane domain. The remaining hydrophobic portion of the sG protein is essential for translocating it into the lumen of the ER during translation and would likely maintain its membrane association until a proteolytic event releases the mature sG protein into the medium. SUBCELLULAR LOCATION: [Isoform Membrane-bound glycoprotein G]: Virion membrane; Single-pass type II membrane protein Host cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the pneumoviruses glycoprotein G family."}
+{"protein": "MSVDVAIIMGSQSDWETMRHAAHTLEALGISFDARIVSAHRTPDRLVAFAKGAKAEGFKVIIAGAGGAAHLPGMAAAMTPLPVFGVPVQSKALSGQDSLLSIVQMPAGIPVGTLAIGRAGAVNAALLAAAVLALYDEALAARLDEWRKAQTESVAERPSNEA", "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": "GLAYDISDDQQDITRMGINPIMMSAGELESGNAGEPAKMCCLFINDLDAGAGRIGVCTGIFR", "text": "FUNCTION: Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the RuBisCO activase family."}
+{"protein": "MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSEMVLVGLLRGSFMFMADLCREVQVPHEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILGLREPKSLAICTLLDKPSRREVDVPVEFVGFSIPDEFVVGYGIDYAQRYRHLPYVGKVVLLDE", "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": "MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDSYLESYISTIGVDFKIRTVEQDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLNEIDRYASENVNKLLVGNKCDLAENRVVSYEAGKALADEIGIPFLETSAKDATNVEKAFMTMAGEIKNRMASQPATNASKPATVQMRGQPVAQQSSCCS", "text": "FUNCTION: Possesses GTPase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MTSNNLPTVLESIVEGRRGHLEEIRARIAHVDVDALPKSTRSLFDSLNQGRGGARFIMECKSASPSLGMIREHYQPGEIARVYSRYASGISVLCEPDRFGGDYDHLATVAATSHLPVLCKDFIIDPVQVHAARYFGADAILLMLSVLDDEEYAALAAEAARFDLDILTEVIDEEEVARAIKLGAKIFGVNHRNLHDLSIDLDRSRRLSKLIPADAVLVSESGVRDTETVRQLGGHSNAFLVGSQLTSQENVDLAARELVYGPNKVCGLTSPSAAQTARAAGAVYGGLIFEEASPRNVSRETLQKIIAAEPNLRYVAVSRRTSGYKDLLVDGIFAVQIHAPLQDSVEAEKALIAAVREEVGPQVQVWRAISMSSPLGAEVAAAVEGDVDKLILDAHEGGSGEVFDWATVPAAVKAKSLLAGGISPDNAAQALAVGCAGLDINSGVEYPAGAGTWAGAKDAGALLKIFATISTFHY", "text": "FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain (By similarity). SIMILARITY: In the N-terminal section; belongs to the TrpC family. SIMILARITY: In the C-terminal section; belongs to the TrpF family."}
+{"protein": "MEAPPVTMMPVTGGTINMMEYLLQGSVLDHSLESLIHRLRGLCDNMEPETFLDHEMVFLLKGQQASPFVLRARRSMDRAGAPWHLRYLGQPEMGDKNRHALVRNCVDIATSENLTDFLMEMGFRMDHEFVAKGHLFRKGIMKIMVYKIFRILVPGNTDSTEALSLSYLVELSVVAPAGQDMVSDDMKNFAEQLKPLVHLEKIDPKRLM", "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 18 family."}
+{"protein": "MKTNNTFLSYFVCGFLLMGVGLGQNQTSEIKVGVVLDLNTTFSKICLTSIKMAVSDFYADHPNYLTRLTLHVRDSMEDTVQASAAALDLIKTEQVSAIIGPINSMQADFMIKLANKTQVPTITFSATSPLLTSIKSPYFVRATIDDSSQVRAIASIFKFFRWRRVVAIYVDNEFGEGFMPFLFDALQDVEVKRSVIPPEAIDDEIQKELRKLMERQARVFVVHMESSLALRVFQIARDIGMMEEGYVWLMTNGMTHMMRHINNGRSLNTIEGVLGVRSHVPKSKELGDFRLRWKRTFEKENPSMRDDLNVFALWAYDSITALAKAVEKANTKSLWYDNGSTLSKNRTDLGNVGVSLYGPSLQKAFSEVRFNGLAGEFKLIDGQLQSPKFEIINFVGNEERIIGFWTPRDGLMDATSSNKKTLGPVIWPGKSKIVPKGWEIPGKKLRVGVPMKKGFFDFVKVTINPITNKKTPTGYAIEIFEAALKELPYLVIPEYVSFESPNNYNNLVYQVYDKTWDAVVGDITITANRSLYADFTLPFTESGVSMMVPVRDNENKDTWVFLEPWSLELWVTTGCFFVFIGFVVWLFEHRVNTDFRGPPQYQIGTSLWFSFSTMVFAHRENVVSNLARFVVVVWCFVVLVLTQSYTASLTSFLTVQSLQPTVTNVNDLIKNRDCVGYQGGAFVKDILLGLGFHEDQLKPFDSAKDADDLLSKGKSKGIAAAFDEVAYLKAILSQSCSKYVMVEPTFKTGGFGFAFPKNSPLTGEFSRAILNLTQNNVTQQIEDRWFPKKNDCPDPMTALSSNRLNLSSFLGLFLIAGTAISFSLLVFVALFLYEHRHTLGDDSEDSLWRKLKFLFKIFDEKDMNSHTFKNSAIHNISSPMTHKTPSPSTVQITPWPQSPSQNREFELRRVSFSPSEERFTTQPIIHHEDGESDIECRVEQ", "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": "MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASS", "text": "FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression (PubMed:17101132, PubMed:31409757, PubMed:19941817). Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis (PubMed:17586473, PubMed:19414596, PubMed:31409757, PubMed:19941817, PubMed:26522158). Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (PubMed:31409757). Phosphorylates RPS6KB1 (By similarity). Acts as an essential activator of the NLRP3 inflammasome assembly independently of its kinase activity (PubMed:26642356, PubMed:36442502). Acts by unlocking NLRP3 following NLRP3 tranlocation into the microtubule organizing center (MTOC), relieving NLRP3 autoinhibition and promoting formation of the NLRP3:PYCARD complex, and activation of CASP1 (PubMed:26642356, PubMed:31189953, PubMed:36442502). Serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division: interaction with NEK9 prevents interaction with NLRP3 and activation of the inflammasome during mitosis (PubMed:26642356, PubMed:31189953). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Present at centrosome throughout the cell cycle (PubMed:17586473). Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody (PubMed:17586473). Interaction with ANKS3 prevents its translocation to the nucleus (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily."}
+{"protein": "MMDSRILEHPHAQFGGSLGSMVGMGFPYHLGHHHVYDISGHQLQSAAAVPFSIDGLLNGSCSGSVANSNPLLGSGCGVNGDSQYKLGDGGDPDKESPGCKRRRTRTNFTGWQLEELEKASNESHYPDVFMREALALRLDLVESRVQVWFQNRRAKWRKKENTKKGPGRPAHNSHPTTCSGEPMDPEEIARRELERLEKKKRKQERKLLKSQNKLLAGELFHTPGSDSDSGVSQSTDSESTPHTGPQHSAHRQQTEHICEQHARHQRASTVNETAEPMDSTRNSGLCPANGITRASTLQKLNPFSVESLLADSSPRRKTILDFSQLPPQRPLVGKGHFLLYPITQPLGFIVPQTAMKQSHDSGNSGHHCSTTDTSTSNQKNVNHLCRDNTGASDELQRETKNSSIQSPSTSSEKCFSESNSPQKESENDSESTVTNSSQKESISANLSEYSDRKSRSSADTNTDGEDVDMD", "text": "FUNCTION: Transcription factor involved in somitogenesis and neurogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Unc-4 subfamily."}
+{"protein": "MEPPFFLLLLLLVVSSSSPSAALLSAKGVNNEVQALIVIKNLLKDPHGVLKSWDQNSVDPCSWAMITCSPDFLVTGLEAPSQHLSGLLSPSIGNLTNLETVLLQNNNITGPIPAEIGRLENLKTLDLSSNSFYGEIPSSVGHLESLQYLRLNNNTLSGPFPSASANLSHLVFLDLSYNNLSGPIPESLARTYNIVGNPLICDANREQDCYGTAPMPMSYSLNGSRGGALPPAARDRGHKFAVAFGSTAGCMGLLLLAAGFLFWWRHRRNRQILFDVDEQQIENVNLGNVKRFSFRELQAATEGFSGKNILGKGGFGNVYRGQLPDGTLVAVKRLKDGNAAGGEAQFQTEVEMISLALHRNLLRLYGFCMTATERLLVYPFMSNGSVASRLKAKPALEWGTRRRIAVGAARGLVYLHEQCDPKIIHRDVKAANVLLDEACEAVVGDFGLAKLLDHRESHVTTAVRGTVGHIAPEYLSTGQSSDRTDVFGFGILLLELVTGQTALEFGKSSNHKGAMLDWVKKMQSEKKVEVLVDKGLGGGYDRVEVEEMVQVALLCTQYLPAHRPRMSDVVRMLEGDGLADRWEKASGHSTAAADSLSHSHRTSDPAPPAADFAAAFGRCFSDLTDDSSLLVQAVELSGPR", "text": "FUNCTION: LRR receptor kinase that may be involved in defense response. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Localizes in the plasma membrane. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MHYSPLTVLALLGGTLLLYCSGLVIYRLVFDPLSKFPGPKLSAATFWYEFYYDVIKKGQFTFKIGEWHKQYGPIIRINPYEIHIDDPEGDFYHTVFSGTGVRDKHFWYASQFGTPESGLGTINHHLHRHRRRALNPSFSKASIVRLTPVIWSKIEKLCSRFDELRGTDQPVNVRLAYTCLTTDVITSYAFNRCWNHLDKPDFSPVWCKTLVNGSKMTRWTKQFPWMLETMKKMPQALVGFFDPGMLLVFDVMNKIHHQILDILNGKQEVEDSATDGLSKSPIPNRTIFHELLKSDLPDYDKTIHHLGQEGQNIIGAGADTTSNALTVITYHLLSNPRVLGKLKEELERAMPDRYGAWDLKVAEGLPYLGGVIQEGLRLAYGASSRLTRVAPEEDLNFDGWFIQKGTPISMTALYMHHNEKIFPNSHTFLPERWTDAPDGGRSLDRYLVSFSKGSRQCIGINLAKVELFLTLATVFRRFEMDLHDTVFERDVQLKHDFFLPQPSMQSNGVRVIFK", "text": "FUNCTION: Cytochrome P450 monooxygenase that hydroxylates polyporic acid produced by the nonribosomal peptide synthetase acyN to produce the less toxic metabolite ascocorynin (PubMed:35477441). The hydrophobic substrate polyporic acid might approach the active site from the membrane and, after hydroxylation into ascocorynin, leaves into the cytoplasm (Probable). MO6277 appears vital to avoid high-level accumulation of polyporic acid in the fungal membrane (PubMed:35477441). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MKFSSALVLSAVAATALAESITTTITATKNGHVYTKTVTQDATFVWGGEDSYASSTSAAESSAAETSAAETSAAATTSAAATTSAAETSSAAETSSADEGSGSSITTTITATKNGHVYTKTVTQDATFVWTGEGSSNTWSPSSTSTSSEAATSSASTTATTTAETSSSATSSSTAELSSYTGAADAITAGTGLMGAALAAVMLL", "text": "FUNCTION: Involved in the uptake of non-siderophore and siderophore sources of iron. Has a role in the retention of iron in the cell wall and periplasmic space. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Lipid-anchor, GPI-anchor."}
+{"protein": "MHMRLFSKFKLHGSSAASEEVFGGKFSYTSAVADFYIELGDAHKIWKPRDVVTGEVVLTLRKPLRGVSLRMSLEGNLRVQTGSGATSRLKFQRTLFSKSSMIYGVEQPEDAEQEGHGLTRGDHRFPFRMRVPSKNIYTSIAFEKGSISYAVGCVLETRSGAQRLSSCSRQISVLVPVDVSLLPKLRPKTVVLQSPQLLRSAKANYPEHDTASSLTKRTTASANSNSSVTTVCSSKTVTISVDLPESGYVIGDTIRIKVHIQHYKEYRNSAGLIATLVRICRVHSTGTDDPMETFRKDICQCVAPLYVEPETHTCSVGMNLNVPLDAFPTLVVPNQGFTFQYYIEVLANLSSKNIVYTESNRVIGGSGMADIPMPGSKLHPVKKISMLPLKLQGPLGKQDTNIDESLIFFQDMVNVDKLKRLRNVTGTSIEVVIGTHRNNSVQQARQSCPGSPVGGSDSTMMSEQSAAGTSLPSSVLDIYDQLANRLSSSVGDQLLRYGMSPDSGPHSANDELPRYTPNVDYMVTEDKRELEQRKLKELESEPSVEEEQ", "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": "MKKIIKLSLLSLSIAGLASCSTLGLGGSDDAKASAKDTAAAQTATTEQAAAVSKPTAKVSLNKLGQDKIKATVYTAYNNNPQGSVRLQWQAPEGSKCHDTSFPITKYAEKNDKTWATVTVKQGNNFCSGKWTANVVYDKEVIASDSINI", "text": "SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor."}
+{"protein": "MAERGGAGGGPGGSGGGSSQRGSGVAQSPQQQPQQQPPQPQQPTPPKLAQATSSSSSTSAAAASSSSSSTSTSMAVAVASGSAPPGGPGPGRTPAPVQMNLYATWEVDRSSSSCVPRLFSLTLKKLVMLKEMDKDLNSVVIAVKLQGSKRILRSNEIILPASGLVETELQLTFSLQYPHFLKRDANKLQIMLQRRKRYKNRTILGYKTLAVGLINMAEVMQHPNEGALVLGLHSNVKDVSVPVAEIKIYSLSSQPIDHEGIKSKLSDRSPDIDNYSEEEEESFSSEQEGSDDPLHGQDLFYEDEDLRKVKKTRRKLTSTSAITRQPNIKQKFVALLKRFKVSDEVGFGLEHVSREQIREVEEDLDELYDSLEMYNPSDSGPEMEETESILSTPKPKLKPFFEGMSQSSSQTEIGSLNSKGSLGKDTTSPMELAALEKVKSTWIKNQDDSLTETDTLEITDQDMFGDVSTSLVVPEKVKTPMKSSKADLQGSASPSKVEGTHTPRQKRSTPLKERQLSKPLSERTNSSDSERSPDLGHSTQIPRKVVYDQLNQILVSDAALPENVILVNTTDWQGQYVAELLQDQRKPVVCTCSTVEVQAVLSALLTRIQRYCNCNSSMPRPVKVAAVGSQSYLSSILRFFVKSLASKTPDWLGYMRFLIIPLGSHPVAKYLGSVDSRYSSTFLDSAWRDLFSRSEPPVSEPLDVVGRVMQYVNGATTTHQLPVAEAMLTCRHKFPDEDSYQKFIPFIGVVKVGLVEDSPSTAGDGDDSPVVSLTVPSTSPPSSSGLSRDATATPPSSPSMSSALAIVGSPNSPYGDVIGLQVDYWLGHPGERRREGDKRDASSKNTLKSVFRSVQVSRLPHAGEAQLSGTMAMTVVTKEKNKKVPTIFLSKKPREKEVDSKSQVIEGISRLICSAKQQQTMLRVSIDGVEWSDIKFFQLAAQWPTHVKHFPVGLFSGSKTT", "text": "FUNCTION: Coat protein that is involved in the localization of trans- Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster- containing cytoplasmic domain of these molecules with the adapter- protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits (By similarity). Required for normal ER Ca2+ handling in lymphocytes. Together with WDR37, it plays an essential role in lymphocyte development, quiescence and survival. Required for stabilizing peripheral lymphocyte populations (PubMed:33630350). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network Note=Localizes in the perinuclear region, probably the TGN. SIMILARITY: Belongs to the PACS family."}
+{"protein": "MAAARPALTDSLSFCLAQLTAAAGEGPGGGKDPATNETALGRVLLALRTRHIKAAEGIERFRARGGLRPLVALLRRTAAAGPAPSQAASGSAPPSVASAGSSPGPAPAAESPLTLSAPMRLRKTLDLALSILANCCTEGACRSEVRRIGGILPLVTILQCVRIDSIQNRTARALGNLAMEPESCGDIHSAGAVPFLVESLTACQDSQCLQSIVRALRNLADSPQHRLALAQQGAVRPLAELLATAPDPALTSALVRALLELSRGCSRACAEQLSLGGGLGPLVSLASHPKRAIREAAILILANLCAQGLVRPALGNAGGVEVLLGELRRRRGPSGSSSASQQPLVRAVCLLCREAINRARLRDAGGLELLMGLLQDPGASAWHPRVVAALVGFLYDTGALGKLQALGLVPLLARQLCGEAGEEEEEGVEAASWDFPEERTSGQPEGGSFRSLRLWLISEGYAAGPGDISPDWSPERCPMPEPSESVSPTPGQTSMSTPRTLRKLGRVPAATTEEPWGQEGPALLLLSRFSQAPDPSGALVTGPALCGLLAYVTGAPGPPNPRALRILARLTCNPACLEAFVRSYGAALLRAWLVLGVSPDDWPVPHARPVHRSQHRELGEMLLQNLTVQAESPFGVGALTHLLLSGSPEDRVACALTVPFICRKPTLWRRLLLDQGGLRLLLTALTQPAPHPLFLFFAADSLSCLQGLVSPSASPVPLPDLPLELDSPSPCLYKPLLGPAPAPAPDLHFVLDSGLQLPAQRAASAAASPFFRALLSGSFAEAQMNLVPLRGLSPSAAWPVLHHLHGCRGCGAALGPIPPPGQPLLGSKAEEALEAAGRFLLPALEEELEEAVGRIHLSPQGGPESVGEVFRLGRPRLAAHCARWTLEPGQCPRKRALALTGLVEAAGEEAGPLTEALLAVVMGVES", "text": "FUNCTION: Involved in fetal development, T-cell function and adrenal gland growth homeostasis (By similarity). Negatively regulates adrenal cells survival. Plays a role in steroidogenesis, modulates steroidogenic enzymes expression and cortisol production (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MMRRVYSPVFCSVAAARFAATSAAKKYDLFGYEVDTNTAPWIEKIKKCKYYDEAGEVLVNMNVSNCPPDIATYNATLQCIYQSPSKQSTPVDNESKFCAMMDLLEEMQHRNRLKPNEESWTWVMKECVKSGQFRLGYCIQQVMETECKGCPADLVKANEANAQKAKTEGKEHPGHLSQQAGLFDVKVE", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(o) ATP synthase) 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:19436713, PubMed:29247468). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(o) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:19436713, PubMed:29247468, PubMed:29440423). 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) (PubMed:19436713, PubMed:29440423). 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 (Probable). Contrary to the procyclic, insect form that requires F(1)F(o) ATP synthase for ATP synthesis, the bloodstream form relies on ATP hydrolysis by F(1)F(o) ATP synthase to maintain its mitochondrial membrane potential (PubMed:29247468). SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side."}
+{"protein": "MRKGLRATAARCGLGLGYLLQMLVLPALALLSASGTGSAAQDDEFFHELPETFPSDPPEPLPHFLIEPEEAYIVKNKPVNLYCKASPATQIYFKCNSEWVHQKDHVVDERVDETSGLIVREVSIEISRQQVEELFGPEDYWCQCVAWSSAGTTKSRKAYVRIAYLRKTFEQEPLGKEVSLEQEVLLQCRPPEGIPVAEVEWLKNEDIIDPAEDRNFYITIDHNLIIKQARLSDTANYTCVAKNIVAKRKSTTATVIVYVNGGWSTWTEWSVCNSRCGRGYQKRTRTCTNPAPLNGGAFCEGQSVQKIACTTLCPVDGRWTSWSKWSTCGTECTHWRRRECTAPAPKNGGKDCDGLVLQSKNCTDGLCMQAAPDSDDVALYVGIVIAVTVCLAITVVVALFVYRKNHRDFESDIIDSSALNGGFQPVNIKAARQDLLAVPPDLTSAAAMYRGPVYALHDVSDKIPMTNSPILDPLPNLKIKVYNSSGAVTPQDDLAEFSSKLSPQMTQSLLENEALNLKNQSLARQTDPSCTAFGTFNSLGGHLIIPNSGVSLLIPAGAIPQGRVYEMYVTVHRKENMRPPMEDSQTLLTPVVSCGPPGALLTRPVILTLHHCADPSTEDWKIQLKNQAVQGQWEDVVVVGEENFTTPCYIQLDAEACHILTENLSTYALVGQSTTKAAAKRLKLAIFGPLCCSSLEYSIRVYCLDDTQDALKEVLQLERQMGGQLLEEPKALHFKGSIHNLRLSIHDIAHSLWKSKLLAKYQEIPFYHIWSGSQRNLHCTFTLERLSLNTVELVCKLCVRQVEGEGQIFQLNCTVSEEPTGIDLPLLDPASTITTVTGPSAFSIPLPIRQKLCSSLDAPQTRGHDWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEAQNFPDGNLSMLAAVLEEMGRHETVVSLAAEGQY", "text": "FUNCTION: Receptor for netrin required for axon guidance (PubMed:22685302, PubMed:10399920). Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (PubMed:10399920, PubMed:22685302). NTN1/Netrin-1 binding might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Axon repulsion in growth cones may also be caused by its association with DCC that may trigger signaling for repulsion (PubMed:10399920). Might also collaborate with DSCAM in NTN1-mediated axon repulsion independently of DCC (PubMed:22685302). Also involved in corticospinal tract axon guidance independently of DCC (PubMed:9126743, PubMed:9389662, PubMed:12451134). Involved in dorsal root ganglion axon projection towards the spinal cord (By similarity). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell surface Synapse, synaptosome Cell projection, dendrite Cell projection, axon Cell projection, growth cone Cell projection, lamellipodium Cell projection, filopodium. SIMILARITY: Belongs to the unc-5 family."}
+{"protein": "AELPQGLWVRPRLG", "text": "FUNCTION: Myoactive. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pyrokinin family."}
+{"protein": "MAKIGVENSLTDVQQALQQQGHEVITINSEHDAQGCDCCVVTGQDSNMMGIADTSIKGSVINAHGLTTDEICQQVESRI", "text": "SIMILARITY: Belongs to the UPF0180 family."}
+{"protein": "MVVLVTRSLLPALFFASRAPFAAATTSARFQRGLATMAAEAFTKHEVIPDVLASNPPSKVVSVKFNSGVEANLGNVLTPTQVKDTPEVKWDAEPGALYTLIKTDPDAPSRKEPTYREWHHWLVVNIPGNDIAKGDTLSEYIGAGPPPKTGLHRYVYLIYKQSGRIEDAEHGRLTNTSGDKRGGWKAADFVAKHKLGAPVFGNLFQAEYDDYVPILNKQLGA", "text": "SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family."}
+{"protein": "MATKIDKEACRAAYNLVRDDGSAVIWVTFRYDGATIVPGDQGADYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGEDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIRSELKKAGGANYDAQSE", "text": "FUNCTION: Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Nucleus. SIMILARITY: Belongs to the actin-binding proteins ADF family. Coactosin subfamily."}
+{"protein": "MDPKTSVVPPALHLVDPQIQLTIIRMEDAVVHGQSNAVPKVYPIILRLGSQLSLSMARRNLDSLEARAFQSTPIVVKMTKLATTEELPDEFVVVTAK", "text": "SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane; Peripheral membrane protein. Host cytoplasm. Note=Binds non-covalently to intracellular lipid bilayers."}
+{"protein": "MLSKNLYSNKRLLTSTNTLVRFASTRSTGVENSGAGPTSFKTMKVIDPQHSDKPNVLILGSGWGAISFLKHIDTKKYNVSIISPRSYFLFTPLLPSAPVGTVDEKSIIEPIVNFALKKKGNVTYYEAEATSINPDRNTVTIKSLSAVSQLYQPENHLGLHQAEPAEIKYDYLISAVGAEPNTFGIPGVTDYGHFLKEIPNSLEIRRTFAANLEKANLLPKGDPERRRLLSIVVVGGGPTGVEAAGELQDYVHQDLRKFLPALAEEVQIHLVEALPIVLNMFEKKLSSYAQSHLENTSIKVHLRTAVAKVEEKQLLAKTKHEDGKITEETIPYGTLIWATGNKARPVITDLFKKIPEQNSSKRGLAVNDFLQVKGSNNIFAIGDNAFAGLPPTAQVAHQEAEYLAKNFDKMAQIPNFQKNLSSRKDKIDLLFEENNFKPFKYNDLGALAYLGSERAIATIRSGKRTFYTGGGLMTFYLWRILYLSMILSARSRLKVFFDWIKLAFFKRDFFKGL", "text": "FUNCTION: Catalyzes the oxidation of NADH generated inside the Mitochondrion. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=Bound to the mitochondrial inner membrane facing the matrix site. SIMILARITY: Belongs to the NADH dehydrogenase family."}
+{"protein": "MKISSGAINFSTIPNQVKKLITSIREHTKNGFASKITSVKNTHASLNEKLKTGKSSSIEFALPQKIKDFFQPKDKNTLNKTLITVKNIKDTNNAGKKNISAEDVSKMNAAFMRKHIANQTCDYNYRVTGAAPLPGGVSVSANNRPTVSEGRTPPVSPSLSLQATSSPSSPAEWAKKLTDALLRQKAGETLTAADRDFSNADFRNITFSKILPTSFMKRDGDIIKGFNFSNSKFTYSDISHLHFDECRFTYSTLSDVVCSNTKFSNSDMNELTLQYSITTRQQPSFINTTLKNTFIRHKANLSGVILNEPDNSSPPSVSGGGNFIRLGDIWLQMPLLWSENAVDGFLNHEHNNGKSILMTIDSLPDKYSQEKVRAMEDLVKSLRGGRLTEACIRPVESSLVSVLAHPPYTQSALISEWLGPVQERFFAHQCQTYNDVPLPAPDTYYQQRILPVLLDSFDRNSAAMTTHSGLFNQVILHCMTGVDCTDGTRQKAAALYEQYLAHPAVSPHIHNGLFGNYDGSPDWTTRAADNFLLLSSQDSDTAMMLSTDTLLTMLNPTPDTAWDNFYLLRAGENVSTAQISPVELFRHDFPVFLAAFNQQATQRRFGELIDIILSTEEHGELNQQFIAATNQKHSTVKLIDDASVSRLATIFDPLLPEGKLSPAHYQHILSAYHLTDATPQKQAETLFCLSTAFARYSSSAIFGTEHDSPPALRGYAEALMQKAWELSPAIFPSSEQFTEWSDRFHGLHGAFTCTSVVADSMQRHARKYFPSVLSSILPLAWA", "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": "MSEKHIDEFSGVETTGHEWDGIRELNNPMPRWWVWTFYATIVWALGYAIAYPAIPMITDATKGMLGFSSRAELQQNLDQAKASQTTLHDLIAAKTVHEIDSDSALREFAIAGGASAFKVNCATCHGSGASGGPGFPNLNDDDWLWGGDLDAIQATIAHGIRFDGDTDTHASEMPPFAEVLDPLQTRQVAAYVWGLTNTPSDPGLAEAGKQVFVDNCAACHGDDAKGKAEMGAPDLADAIWLKARGEDAIIRQVAAPKHGVMPAWAGRLGDTTVKELTIFVHSLGGGT", "text": "FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. FixP subunit is required for transferring electrons from donor cytochrome c via its heme groups to FixO subunit. From there, electrons are shuttled to the catalytic binuclear center of FixN subunit where oxygen reduction takes place. The complex also functions as a proton pump (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CcoP / FixP family."}
+{"protein": "CKCPSCNFNDVTENCKCCIFRQP", "text": "FUNCTION: Upon intracranial injection in mice, as25a (the toxin without the two 4-hydroxyprolines) provokes paralysis of the hind limbs and death with a dose of 240 pmol. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MKLEFSIYRYNPDVDNAPRMQDYTLEGEEGRDMMLLDALIQLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALTQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA", "text": "FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family."}
+{"protein": "MASHIIGNRNSTPEASKSSLRPPSSSRNLATHQLRASADMSGFPSPLSSRSIRPASEVYFNQQAQTPGNAEDPLDRAAQQWLADIDQYETTLEEMAAATLDQDFKDELSAIEQWFRVLSEAERTAALYALLQQTTQVQIRFFIQVLQQMAKSHPMSGLLSPANFGEKGIDAMSNRLNDAMSKLNVDSSRNSLGRPPPSPGAKRNSGLDSSTINAMFPDAAAAIAKKKAEFTQQTGNAPPSNRNSAVFNERTSFVAPTISAPDNSADNLSQPPVSPWAQRGASEPQPPIARPKSSSGQQPMGQFNQSGLRSPLPTSQTATIPAPEIEAPLLSPYNVNASWASMTNTPMTATFGSQLGAPHQQGSDMVANATAMKLAALSTVNNRIALDDARKYRRARSNDGQGKNASNNTGAQSIQGGLASPGLPVAGQLLNAQQFAALQAQQQAAMAGHRSRPTSPGIAMQGGALGPMGFTSPQNNGFLTAYDPNNPLIGNGLGALGMGQFGLSGHEGYLSDHSEINRGRSPRGRRGSSKPPEDPTDPNLLKDIPSWLRSLRLHKYTDNLKDLKWTELIELNDKQLEERGVNALGARNKMLKVFEQVKEAKAEGKLDNATA", "text": "FUNCTION: RNA-binding protein involved in post-transcriptional regulation through transcript degradation. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, P-body. SIMILARITY: Belongs to the VTS1 family."}
+{"protein": "MDEFEMIKRNTSEIISEEELREVLKKDEKSAYIGFEPSGKIHLGHYLQIKKMIDLQNAGFDIIILLADLHAYLNQKGELDEIRKIGDYNKKVFEAMGLKAKYVYGSEFQLDKDYTLNVYRLALKTTLKRARRSMELIAREDENPKVAEVIYPIMQVNDIHYLGVDVAVGGMEQRKIHMLARELLPKKVVCIHNPVLTGLDGEGKMSSSKGNFIAVDDSPEEIRAKIKKAYCPAGVVEGNPIMEIAKYFLEYPLTIKRPEKFGGDLTVNSYEELESLFKNKELHPMDLKNAVAEELIKILEPIRKRL", "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": "MADLEAVLADVSYLMAMEKSKATPAARASKRIVLPEPSIRSVMQKYLAERNEITFDKIFNQKIGFLLFKDFCLNEINEAVPQVKFYEEIKEYEKLDNEEDRLCRSRQIYDAYIMKELLSCSHPFSKQAVEHVQSHLSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWKNVELNIHLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDCDQELYKNFPLVISERWQQEVTETVYEAVNADTDKIEARKRAKNKQLGHEEDYALGKDCIMHGYMLKLGNPFLTQWQRRYFYLFPNRLEWRGEGESRQNLLTMEQILSVEETQIKDKKCILFRIKGGKQFVLQCESDPEFVQWKKELNETFKEAQRLLRRAPKFLNKPRSGTVELPKPSLCHRNSNGL", "text": "FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors. SUBCELLULAR LOCATION: Postsynapse Presynapse. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily."}
+{"protein": "MKSSVAQVRGSNYDKVDTRSSSERSSSPEDSNEERSPSPRDRGYSNRSRDYSDRDRYEDRSRSGRYDRSDESRRRERERSTSPRDRGYTDRRRGYSDRDGYGNDRSRNGRYDRSEDNREREKRQNYQDRDYEKRSPPARRRSPPARRSEEQTEEQNQTEPPVKKKKEELDPILTRTGGAYIPPARLRMMQEQITDKSSMAYQRMSWEALKKSINGLVNKVNVSNIGNIIQELLQENIVRGRGLLARSVLQAQSASPIFTHVYAALVSIINSKFPHIGELILKRLILNFRKGYRRNDKQLCLTSSKFVAHLINQNVAHEVLALEMLTLLLERPNDDSVEVAIGFLKESGLKLTQVTPRGINAIFERLRNILHESEIDKRVQYMIEVMFAVRKDGFKDHPVIPEGLDLVEEEDQFTHMLPLEDDYNQEDVLNVFKMDPDFLENEEKYKAIKKEILDEGDSDSEGDANEGSEDESEEEEEDGQEAGTEGEKMTIHDKTEVNLVAFRRTIYLAIQSSLDFEECAHKLIKMDFPESQTKELCNMILDCCAQQRTYEKFFGLLAGRFCLLKKEYLEAFENIFKEQFETIHRLETNKLRNVAKMFAHLLYTDSLPWSVLECMNLSEETTTSSSRIFVKIFFQELCEYMGLPKLNARLKDVTLQPFFQGLLPMDNPKNTRFAINFFTSIGLGGLTDELREHLKNAPKMIMTQKQNVESSDSSSDSSSGSESSSDSDSSSSSSSESSSSSSDSDSSRRKKHSQKKKKSREAHKAASKKQAPDDRRKEAPKHKHQKEKYDDKQSRKSKRDSKN", "text": "FUNCTION: Required for pre-mRNA splicing as component of the spliceosome. Promotes exon-junction complex (EJC) assembly. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Note=Concentrates around speckles, which are sites of pre-mRNA synthesis and processing, where it colocalizes with EJC core proteins. SIMILARITY: Belongs to the CWC22 family."}
+{"protein": "MISNGLILAAAEGANPLIPNPWEILVVVVGFALLMFIVIKFIVPTLEKSYQDRVEAIEGGLAKAEKAQAEANAMMADYESQLADARTEANRIREDARTEAAEIVAEARERATAEATRVFEQAQAQIAAERQQAAAQLKREVGSLATTLAGKIVGESLEDDARSQRVVDRFLADLDRHQSAGVAE", "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 (By similarity). 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": "MKTGMFTCGHQRLPIEHAFRDASELGYDGIEIWGGRPHAFAPDLKAGGIKQIKALAQTYQMPIIGYTPETNGYPYNMMLGDEHMRRESLDMIKLAIDMAKEMNAGYTLISAAHAGYLTPPNVIWGRLAENLSELCEYAENIGMDLILEPLTPYESNVVCNANDVLHALALVPSPRLFSMVDICAPYVQAEPVMSYFDKLGDKLRHLHIVDSDGASDTHYIPGEGKMPLRELMRDIIDRGYEGYSTVELVTMYMNEPRLYARQALERFRALLPEDER", "text": "FUNCTION: Catalyzes the reversible interconversion of fructoselysine with its C-3 epimer, psicoselysine. May allow S.flexneri to utilize psicoselysine for growth. SIMILARITY: Belongs to the FrlC family."}
+{"protein": "MISGDTILFALMVVTCVNWARYFTALRTLIYIMREAHPLLYQQVDGGGFFTTHGNMTKQVRLFSYIKSKEYHHHHDEVFTSKCDRVRQLFILSSALLGVTLLSSFIV", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the universal stress protein B family."}
+{"protein": "WASQVSENRPVCKAIIQGKQFEGLVDTGADVSIIALNQWPKNWPKQKAVTGLVGIGTASEVYQSTEILHCLGPDNQESTVQPMITSIPLNLWGRDLLQQWGAEITMPAPLYSPTSQKIMTKMGYILGKGLGKNEDGIKIPVEAKINQKREGIGYPF", "text": "FUNCTION: Retroviral proteases have roles in the 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. SIMILARITY: Belongs to the peptidase A2 family. HERV class-II K(HML-2) subfamily."}
+{"protein": "MNGLPSAEAPGGAGCALAGLPPLPRGLSGLLNASGGSWRELERVYSQRSRIHDELSRAARAPDGPRHAAGAANAGPAAGPRRPVNLDSALAALRKEMVGLRQLDMSLLCQLWGLYESIQDYKHLCQDLSFCQDLSSSLHSDSSYPPDAGLSDDEEPPDASLPPDPPPLTVPQTHNARDQWLQDAFHISL", "text": "FUNCTION: Negatively regulates TGF-beta-induced signaling; in cooperation with SKI prevents the translocation of SMAD2 from the nucleus to the cytoplasm in response to TGF-beta. Acts as an adapter that mediates the specific recognition of LIMK1 by CDC42BPA and CDC42BPB in the lamellipodia. LRAP25-mediated CDC42BPA/CDC42BPB targeting to LIMK1 and the lamellipodium results in LIMK1 activation and the subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm Cell projection, lamellipodium Note=Co-localizes with CDC42BPA, CDC42BPB and LIMK1 in the lamellipodium. SIMILARITY: Belongs to the FAM89 family."}
+{"protein": "MNLGIVSLFREHVDSIPNILPHQLATLDFLLRSILDENNSVLLFHIMGSGKTIIALLFALIVSKFKKVYILVPNINILKIFTYNMGIAVNLINSDYVLENIHIYSTTSFYSLNYNDNVINYNGLAKYNNAIFIIDEAHNIFGNNTGELMTVIKNKNKVPFLLLSGSPITNTPITLSNIISIMSDEGINFSDIIIQGKKVFQILLNENGVSVLKRILRDKISYYELQDTELPSIVFHGRRFLDTRIVYCHMSKLQERDYINVRKLCNNEMFEKNMNNVSLAVLGPLNLINNLDILFQDQDKELYPNLKISNGVLYGDELVSLNISSKFKYFIARIQSLTGKHFIYFSNSTYGGLIIKYIMLSNGYSEHNGSQGTNPKTIGGRLKTFAIVTSKMKSSLEELLAVYNSPANNDGSRIMFLFSSNIMSESYTLKEVMHIWFMTIPDTFSQYNQILGRSIRKFSYTNIAEPVNVYLLAAIYADFDDDITSLDNYSIDEINVLPFDIKKLLYLKFKTKETKRIYSILKDISVNYTLPPHPQIVDVVLGELTRQFFYHHSRVRADDPELFAAIDRVLCSPDSTRRYLDEITRGHFFVCNRVFEKALLYRHGEDIIVVPFKLSHDQFLWAINFRKEYNVGAPL", "text": "FUNCTION: Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa (RAP94) to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters (By similarity). 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 helicase family. VETF subfamily."}
+{"protein": "MNTPQISLYEPGTILTVGSHHAKIIKYLTSGGFAQVYTAEISPPDPYSNANIACLKRVIVPHKQGLNTLRAEVDAMKLLRNNKHVVSYIDSHAARSVNGIAYEVFVLMEFCERGGLIDFMNTRLQNRLQESEILEIMSQTVQGITAMHALQPPLIHRDIKIENVLISHDGLYKVCDFGSVSGVIRPPRNTQEFNYVQHDILTNTTAQYRSPEMIDLYRGLPIDEKSDIWALGVFLYKICYYTTPFEKSGEAGILHARYQYPSFPQYSDRLKNLIRLMLMEAPSQRPNICQVLEEVSRLQNKPCPIRNFYLLRAMNQNANTQLAGEPSSTTYVPTQKFIPVQSLQSINQPPNMMPVTHVSTTPNLGTFPISINDNNKTEVTAHAGLQVGSHSNLTSPLMKTKSVPLSDEFASLYYKELHPFQKSQTFKSVESFQSPQRKSMPPLSLTPVNNDIFDRVSAINRPNNYVDSETQTIDNMAVPNLKLSPTITSKSLSSTKEIAAPDNINGSKIVRSLSSKLKKVITGESRGNSPIKSRQNTGDSIRSAFGKLRHGFTGNSVNNSRSASFDNNNVNGNGNNTNRRLVSSSTSSFPKFNSDTKRKEESDKNQRLEKRRSMPPSILSDFDQHERNNSRTGSRDYYRSHSPVKKTQASAKTTSKPTLIPDNGNVNINQEKKESIQRRVHNLLKSSDDPVTYKSASGYGKYTDIGTETSNRHSSVRITPITEEKFKKTLKDGVLDIKTKSNGKDKSRPPRPPPKPLHLRTEIQKIRNFSRLQSKKLPIERISSEATETIVDVNVDDLEADFRKRFPSKV", "text": "FUNCTION: Protein kinase involved in the regulation of actin cytoskeleton organization and endocytosis (PubMed:9885245, PubMed:10087264, PubMed:11694597, PubMed:11739778). Phosphorylates PAN1 which disrupts the interaction between PAN1 and END3, and between PAN1 and SLA1 (PubMed:9885245, PubMed:11739778, PubMed:13679512). Phosphorylates SCD5 (PubMed:12956961, PubMed:13679512). Preferentially, phosphorylates substrates on threonine residues in a [L/I/V/M]-x-x- [Q/N/T/S]-x-T-G motif (PubMed:9885245, PubMed:11739778, PubMed:12956961, PubMed:13679512). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch Note=Cortical actin patches. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MSEYLEYQNAIEGKTMANKKTFKQAPLPFIGQKRMFLKHVEIVLNKHIDGEGEGWTIVDVFGGSGLLSHTAKQLKPKATVIYNDFDGYAERLNHIDDINRLRQIIFNCLHGIIPKNGRLSKEIKEEIINKINDFKGYKDLNCLASWLLFSGQQVGSVEALFAKDFWNCVRQSDYPTAEGYLDGIEVISESFHKLIPRYQNQDKVLLLLDPPYLCTRQESYKQATYFDLIDFLRLINLTKPPYIFFSSTKSEFIRYLNYMQESKTDNWRAFENYKRIVVKASASKDGIYEDNMIYKF", "text": "SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
+{"protein": "MADLSAQDKLKQICDALREETLKPAEEEAGSIVHNAREQAKRIVEEAKEEAQRIIRSAEETADQTLKKGEAALVQAGKRSLENLKQAVETKIFRESLGEWLDHVATDPEVSAKLVQALVQAVDAQGISGNLSAYIGKHVSARAVNEALGKEITSKLKEKGVSVGNFSGGAQLKVEERNWVLDMSSEVLLDLLTRFLQKDFREMIFQSC", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase E subunit family. SIMILARITY: Belongs to the V-ATPase E subunit family."}
+{"protein": "MAAWAERLSGVRGVLLDISGVLYDSGTGGGAAIAGSVEAVARLKRSPLKVRFCTNESQKSRRELVGVLQRLGFDISEGEVTAPAPATCQILKERGLRPHLLIHEGVRSEFDDIDMSNPNCVVIADAGEGFSYQNMNRAFQVLMELENPVLISLGKGRYYKETSGLMLDVGGYMKALEYACGIEAEVVGKPSPEFFRSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRTGKFRPGDEHHPEVRADGYVDNLAEAVDLLLQHMDK", "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": "MWRNASMNHSKRNDANDFDSMDEWLRQFFEDPFAWYDETLPIDLYETSQQYIIEADLTFLQPTQVTVTLSGCEFILTVKSSGQTFEKQMMLPFYFNDKNIQVECENQILTVAVNKETEDGSSFSLQFPLS", "text": "FUNCTION: Involved in spore outer coat assembly. May be part of a cross-linked insoluble skeleton that surrounds the spore, serves as a matrix for the assembly of additional outer coat material, and confers structural stability to the final structure."}
+{"protein": "MFQPCCSKSTMSRSGVAVNDSALQAFNELKLGKKVTFIIYKINDAKTEIVVEEEGTTDSYDTFLGKLPENDCRYAVYDFEYEISSGEGKRSKLVFFTWSPDTAPVRSKMIYASSKDSLRRALTGISTEIQGTDFSEVAYESVLERVSRGAGSH", "text": "FUNCTION: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Nucleus matrix Note=Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton. SIMILARITY: Belongs to the actin-binding proteins ADF family."}
+{"protein": "MFSLQDLCRKHLFILPDVFGEHVLQRLGLYWRCHGSLQRVGDDHILIRRDLILSTNEALRMAGEEGNNEVVKLLLLWKGNLHYAIIGALQGDQYDLIHKYENQIGDFHLILPLIQDAKTFEKCHALERFCGVSCLLEHATKYNMLPILQTYQEELSMRAYLRETLFELACLWQRYDVLKWIEQTMHVYDLKIMFNIAISKRDLTMYSLGYILLFDRENTEATLLTQHLEKTAAKGLLYFVLETLKYGGNIDIVLTQAVKYNHRKLLDYFLRQLPRKHIEKLLLLAVQEKASKKTLNLLLSHLNYSVKRIKKLLRYVIEYESTLVIKILLKKRVNLIDAMLEKMVRYFSATKVRTIMDELLISPERVIKMAIQKMRTDIVIHTSYVWEDDLERLTRLKNMVYTIKYEHGKKMLIKVMHGIYKNLLYDEREKVMFHLAKLYVAQNAATQFRDICKDCYKLDVARFKPRFKQLMLDCLEIVTKKSCYSILEILEKHIISLFTMKVMTEEEKNLCLEILYK", "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 505 family."}
+{"protein": "MALSELEKKRQENIRRNQELLKKLDLDSISDSIKKEVDNKSFSSPSSQKRRKTTKKPVIKKEISEPSRRSRRIAGIKSELEDPKQAARIREEEELKQHRKQELERLKRTRLFGDFKLIDLITNKKGDMIFEKNVMDRKLSHIGLDSKVEEKKNEEDKEDEEEAINIDENNRVLQLVQSLGDKFSAGDFYEEIRNSQTNGNSKDKSLDAKRKEFDNLNIYPRFDPLDIKICHNRITSMFFHPSTTNRIVVGGDTTGNVGIWLVDEQNNDTKEEEEDDDDDEPSISILQLHGRNVSKIMTPTFSPEKIYTSSYDGSIRVLDLNKLTSTELLYLNEPGAREDIALGVSDINQCQDSSVIFMTTLDGEFYQHDTRTPFNTRQRHHLATKDLLRLHDKKIGGFAVNPNTNYQIATASLDRTLRIWDLRNVNKSVYSEFENQKSPHMYGNYNSRLSVSCVDWNQENRLVCNGYDDNICLFDYSGGSKLDNELPVITEWKSDFVPSTKSSEESELLPNNLTPFTKIKHNCQTGRWVSILKSHWQTNPADGVQKFIIANMNRGLDIYNQDGQILAHLNEQVGAVPAVCTLHPSQNWAVGGSASGKVYLFE", "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": "MWLSPSLLLLILPGYSIAAKITGPTTVNGSEQGSLTVQCAYGSGWETYLKWRCQGADWNYCNILVKTNGSEQEVKKNRVSIRDNQKNHVFTVTMENLKRDDADSYWCGTERPGIDLGVKVQVTINPGTQTAVSEWTTTTASLAFTAAATQKTSSPLTRSPLKSTHFLFLFLLELPLLLSMLGTVLWVNRPQRRS", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Cell surface localization requires the ITAM-bearing Fc receptor FCER1G to overcome ER retention. SIMILARITY: Belongs to the CD300 family."}
+{"protein": "MVMPLVLSLALTPPPLCHATLVDPRTTLQCHVRSYTFRATKPPIVNENGDPVTCQGDVRVSSCWGRCDSSEIGDYKMPFKISNHPVCTYTGRVSRTVRLSQCAGYPDPTVQVFDATGCACQFCNSETQLCEKLNG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family."}
+{"protein": "MANTIKASVVQASTAAYSLPDTLDKLEKLTRLAKERDGAQLAVFPEAFIGGYPKMSTFGLVVGDRQPEGRDEFVRYAKAAIEIPSPAITRIEQISRETNVFIVVGVIERDAGTLYCTAVFVDPEKGYVDKHRKLVPTAMERVIWGQGDGSTLPVLDKSFESASAPGSTVNTKLSATICWENYMPLLRTYYYSQGTQIYCAPTVDARPAWQHTMTHIALEGRCFVLSACQFAQEKDYPPDHAVANASARDPNNVMIAGGSVIISPLGKVLAGPLLDAEGVISAELDLDDVLRGKFDLDVTGHYARNDVFEFKLREPPATSS", "text": "FUNCTION: Nitrilase that hydrolyzes preferentially fumaronitrile, while 3-phenylpropionitrile, beta-cyano-L-alanine and 4-cyanopyridine are transformed at much lower rates. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family."}
+{"protein": "MRILCDACENAAAIIFCAADEAALCRPCDEKVHMCNKLASRHVRVGLAEPSNAPCCDICENAPAFFYCEIDGSSLCLQCDMVVHVGGKRTHGRFLLLRQRIEFPGDKPKENNTRDNLQNQRVSTNGNGEANGKIDDEMIDLNANPQRVHEPSSNNNGIDVNNENNHEPAGLVPVGPFKRESEK", "text": "FUNCTION: Acts as negative regulator of seedling photomorphogenesis. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKKIWLALAGMVLAFSASAAQISDGKQYITLDKPVAGEPQVLEFFSFYCPHCYQFEEVLHVSDNVKKKLPKGTKMTKYHVEFLGPLGKELTQAWAVAMALGVEDKVTVPLFEAVQKTQTVQSAADIRKVFVDAGVKGEDYDAAWNSFVVKSLVAQQEKAAADLQLQGVPAMFVNGKYQINPQGMDTSSMDVFVQQYADTVKYLVDKK", "text": "FUNCTION: Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily."}
+{"protein": "MGLPRGSFFWLLLLLTAACSGLLFALYFSAVQRYPGPAAGARDTTSFEAFFQSKASNSWTGKGQACRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPALWDRLSQHKAPYGWRGLSHQVIASTLSLLNGSESAKLFAPPRDTPPKCIRCAVVGNGGILNGSRQGPNIDAHDYVFRLNGAVIKGFERDVGTKTSFYGFTVNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVPEGLDKGDRPHAYFGPEASASKFKLLHPDFISYLTERFLKSKLINTHFGDLYMPSTGALMLLTALHTCDQVSAYGFITSNYWKFSDHYFERKMKPLIFYANHDLSLEAALWRDLHKAGILQLYQR", "text": "FUNCTION: Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins (PubMed:10742600, PubMed:29251719). Shows a preference for N-acetylgalactosamine (GalNAc) residues already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage (PubMed:10742600). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
+{"protein": "MSEMEVMASIMRDHILALLKEGKRVDGRSLEDYRDLEIKINVIEKAEGSAWVKLGNTQVLVGIKVDMGEPFPDLPEKGVITTNVELVPLASPSFEPGPPDERAIELARVVDRGIRESGAVELEKLVIVPGKLVRVVFIDVHVLDHDGNLLDASGIGAIAALMSAKMPKVVYDEESGEVQILDEYEPLPVSKMPIPVTIAKVGGNLLVDPNLDEELVMDGRITITTDENGMISSVQKSEGGSFKLEEVMYAIDLALTKAAEIREKVLEAVGAE", "text": "FUNCTION: Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase PH family. Rrp42 subfamily."}
+{"protein": "MEKFGMNFGGGPSKKDLLETIETQKKQLLQYQARLKDVVRAYKSLLKEKEALEASIKVLSVSHEADVGLSGVQPPGLTFPDSVDDRCSTHSEDSTGTATSLDTAASLTSVKGEFGVEDDRAARGPLPPKSEEASGSESGVSSSSGDGPSAGSEMDKRVHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDANKKAEEERGRLEGDLKVLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAADQVEGFELQTKQLTREVEELKGELQTIRDEKNRPDPRLQELQQEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALESQISEVSELLGTYEKAKQKDQLAIQKLKERLLQLDLENKTLALAASSRSSLDIHGDESSLDINVLKDKMEKLKKLLQVAARKSQVTLDVEKLCDPEIMANSEAADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGSLGKELEAAQEQLAELKDKYISLRLSCEELESQHQQEAEDWKQELARLQQLHRQELERSQLDFRDRTLKLEEELHKQRDRALAVLAEKDLELEQLRSVALSSGLPGRRSPVGGVGGGGLGDPADTASSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEVEAHQLQERLLEEGERHREEVGALQSHIEKNMRDQSREGANLEYLKNIIYRFLTLPDSLGRQQTLTAILTILHFSPEEKQVLMRLPSGGSWWPSGKR", "text": "FUNCTION: Probably involved in maintaining Golgi structure. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein."}
+{"protein": "MRFLRFLKIFFTVIRFGLDEMMLSRVNDRRVRLLLRITTIGRKFDAPPGVRLRLALESLGPIFVKFGQVLSTRRDLLPVDIADELAKLQDQVPPFESAVAIRLVENALGAPVDVLFDDFERVPVASASIAQVHFATVKAGQHAGKAVAVKVLRPNMLPVIDSDLALLRDIAVWAERLWADGKRLKPREVVAEFDKYLHDELDLMREAANGSQLRRNFAGLDLLLVPEMYWEFCTPTVLVMERMVGVPISQVETLRAAGVDIPKLAREGVEIFFTQVFRDGFFHADMHPGNIQVSLDPAHFGRYIALDFGIIGALSDFDKNYLAQNFLAFFKRDYHRVATLHLESGWVPPTTRVEELESAIRAVCEPYFDRALKDISLGQVLMRLFSTSRRFNVEIQPQLVLLQKTMLNVEGLGRSLDPELDLWKTAKPYLERWMNEQIGLRGWYERLKIEAPQWSKTLPQLPRLIHHALAERHDNKRGANDDMIRQILLEQKRTNRLLQGLLLFGVAVGVGAVLARAFLALAYGG", "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; Single-pass membrane protein. SIMILARITY: Belongs to the ABC1 family. UbiB subfamily."}
+{"protein": "NKPSLSIVNPLDVLRQRLLLEIARRQMKENTRQVELNRAILKNV", "text": "FUNCTION: Regulation of fluid secretion. Stimulates primary urine secretion by Malpighian tubules and causes a dose-dependent stimulation of cAMP levels in the tubules. May act as clearance peptide in that it may remove metabolic waste from the hemolymph. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sauvagine/corticotropin-releasing factor/urotensin I family."}
+{"protein": "MTAYPQFDVILKALNLSSVGVIITDPEQKDNPIIFVNTGFENITGYAKEEALGSNCHFLQGDDTDKEEVAKIRHAINEKSTANVLLKNYRKDGTSFMNELTIEPIYDDHEHLYFVGIQKDVTTEHDYQLELEKSLTEIEKLSTPIVPIKENICVLPLIGSLTHDRFQHMSEYVSEYMDHGKEDYLIMDLSGLAEFNEDAVMNLVKFHGFMKLTGVELIITGISPKFAMTLIRYEENLASLTTYSTIKEALQFY", "text": "FUNCTION: Exhibits the same spectroscopical features and blue-light induced photochemistry as plants phototropins, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct. Positive regulator in the activation of the general stress transcription factor sigma-B (By similarity)."}
+{"protein": "MGCFESKPDQQVQPVTVRSPTDIFWLVLYVVFWIALIVIAVFSFIYGNPLRIINGYDSFGNTCGVRSNDKFSNFPLSGMNTEDKPYLFFLDIKELRHTLKICVKECPQRELLNAAELYRYYEDRKTKLCRYDFNMSMLQTQEANQGAKYFDFNGPCPPFPVYQSAPVLHRCIPTGVNAPLQQVKKMYALINSWEATQQVFSDLYKAWPTIVLICALSLVFSIVMIALLHWLATIVSWLICIIVVVASVGITGVLWWSYYKAKHTLDTDQQLSYLEELVRNEATIYVLAIAATCIMIILLVVIYYLREKLTGLAALFEEAGKCMLQLPGLAGPPLLAFLALSVFLAFWVVVVVCLATANYPGVKPLLPLAQLEDSASIANDPKLKPELAGKNDTSFKSFKLVEYHDVNVLRHMLWIYIIGLIWTSEFIFACQQLAIAGAVAFWYFRKPTDSPVLLAIAKLVKYHLGSVAKGSLIITIFKIPRLILTYLYAKLKRHQQEGSECASCCLRCCICSFWLLEKFIRYLNHNAYTVIAIEGVNFCPAAKIAWNALVTNALQVATINGIGDFVLFLGKLAVASICGLISILLLRDNPDLHFYMAPVIIITVFAFFIAHIILSLYEMVVDTLFLCVCEDRTINGNSGRWKESNLARLLGEAPEEDAVEAPMQEVQLTPITKQPFSAQFLQAEMENSKA", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CTL (choline transporter-like) family."}
+{"protein": "MVQDTEVVEAGTSKETETTVDVEKEIQECMGAGKKDLLCNDYSEAVNCFQEACTLLSGKHGQMAEECCEAYYYYGVSLLELARLENGVLGNALKGVPEEDADGDSDQEQEQFEKPDLPETEREKLREEVEAAMATEDEDTQEERGCPRRVEKKKEDDKPKESEKSAEKSDEKEKEEKQAKVESSTVKDVKDEKSSDKPVESSNTEEPGTSGTSASSSKENESEEDPDDISNMQLAWEMLELAKVLYKKHDKSKTNKQMVAQCHLKLGELGLEVENHPQAIGDFLECLVIQKDLLPETDRKLAETYYNLGLAYSFEKRYDNALEHYQSALDVLEARVDMLNELIESNEGNKEKEKEIISECKEVGELKELIPDINSKIEDVILAKKQMQKLDGSPFRQASEGESSSGLGASTSDDKPCSTIPIRKVAPTSVPVAKDSPSDITHLVRRKRPSPDEDNQPAESKENESKKAKQEETEEATNGHSAVKKDTDVTDKNGTNGHSKTPKKDAAKRR", "text": "FUNCTION: May function as a nucleosome assembly factor during rapid embryonic cell divisions. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NASP family."}
+{"protein": "MVITLVGEKLAKPGVEFIYYGPAEPCKSCRLARVCTGNLEPGRRYKIIKVRNMEYPCLLHEGKVRVVEVVEPAIDVIIEPRYAVAGSKITLKFVECDDPEKVDLVRPEGLFEGDVVKILEIIGDIECNGRKYKIAKVIRENTQK", "text": "SIMILARITY: Belongs to the UPF0179 family."}
+{"protein": "MERQQQQQQQLRNLRDFLLVYNRMTELCFQRCVPSLHHRALDAEEEACLHSCAGKLIHSNHRLMAAYVQLMPALVQRRIADYEAASAVPGVAAEQPGVSPSGS", "text": "FUNCTION: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the small Tim family."}
+{"protein": "MNIMEISKFQSLGDKIRTMLEDHGYLSENNDYEPNPIDGNISISYAYPIKAFEKFLGYYDVENRVAYNPSISMRTDFSYCIAACRYNKNGNEDTVILDGVTDEKYLRKAKFALDYFRKEFRIKGSFDFYIRRYRRYTKAKGLSESSAVAAAVSRALIKNVFGEGPALDDVFVSKYARLVSGSGTRAAHSGISIWLSYPGINLRECAAFRVADDPHDVYYGIFPKYTDIATDSAHSVAVKSIFYASWLEDKYANIKRLIEHNFDIDELLISGENDMLKLNAILFSGGLIIQTGESLRILRAIQDFKKNGDLFFTADTGPSIMVLSRDKSLIEELRQSVEDPYIEGTYNFNRHTRDLNNFTKEANEYFLENKIE", "text": "FUNCTION: Catalyzes the ATP-independent decarboxylation of (R)- mevalonate 3,5-bisphosphate to isopentenyl 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 mevalonate 3,5-bisphosphate decarboxylase family."}
+{"protein": "GLWQKIKDKASELVSGIVEGVK", "text": "FUNCTION: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. FUNCTION: Antibacterial peptide with narrow spectrum of activity. Inhibits the formation of NO by neuronal nitric oxide synthase. 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": "MTDDTAAPPPRGPARDWKSSPLVSGLLLGLFSLVSALMLALASDATRGPIAARSAEDLLASLAQVLPAALHDNDPTADIRTLADADEGAVRVYVATRGGAVTAVTFELTGYGYGGAIRVLMAVAADGTILGARVLSHTETPGLGDKIEIGKDDWIEGFAGRSLTDPGPAGWKVRRDGGVFDQFSGATITPRAVVGTIHRGLTLFDRHRAELLAPLPLRS", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cellular chromatophore membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RnfG family."}
+{"protein": "IEVLLGSDDGGLAFVPGNFSISAGEKITFKNNAGFPHNVVFDEDEIPAGVDASKISMPEEDLLNAPGETYSVTLSEKGTYSFYCSPHQGAGMVGKVTVN", "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 (By similarity). SIMILARITY: Belongs to the plastocyanin family."}
+{"protein": "GIFTLIKGAAKLIGKTVAKEAGKTGLELMACKITNQC", "text": "FUNCTION: Has antibacterial activity against E.coli and S.aureus strains. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Esculentin subfamily."}
+{"protein": "MDKVWWHTAWGLLCLLQLSLAQQQIDLNITCRYAGVFHVEKNGRYSISRTEAADLCEAFNTTLPTMAQMELALRKGFETCRYGFIEGHVVIPRIHPNAICAANNTGVYILLASNTSHYDTYCFNASAPLEEDCTSVTDLPNSFDGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNIIDEDVSSGSTIEKSTPEGYILHTDLPTSQPTGDRDDAFFIGSTLATIATTPWVSAHTKQNQERTQWNPIHSNPEVLLQTTTRMTDIDRNSTSAHGENWTQEPQPPFNNHEYQDEEETPHATSTTWADPNSTTEEAATQKEKWFENEWQGKNPPTPSEDSHVTEGTTASAHNNHPSQRMTTQSQEDVSWTDFFDPISHPMGQGHQTESKGHSSGNQDSGVTTTSGPARRPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGTVEDRKPSELNGEASKSQEMVHLVNKEPTETPDQFMTADETRNLQSVDMKIGV", "text": "FUNCTION: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, microvillus Secreted Note=Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli."}
+{"protein": "MFTKSVEVLDTTLRDGAQTANISFTLNDKIRIALLLDELGVDYIEGGWPSSNPKDEEFFKEIKKYKLTKARIAAFGSTRKKESTAKEDQSLNSIIKADVDVGVLFGKSWSLHVTDVLKISLEENLDIIYDSVNYLKSHGLRVVYDAEHFYQGYKENREYALKAVKTAEEAGADVIVLCDTNGGTLPHEVYNITKDVVNHVKVKIGLHMHNDSGGAVANTVMGVVAGARHVQGTINGIGERTGNADLIQVIPNIMLKLGLNSLKGNESLKKLKEVSRVVYEIIGVHPNPYQPYVGDFAFTHKAGVHADAVMKVTRAYEHIDPTLVGNNRRFVISEVAGSSNVIYYLEKLGIKVDKKDPRVRNAVQRIKELENRGYSFDLAPASAVLVALRDLGMYRDLIKVEYWKVMNEKELAIAIVKVNGQLEVAEGVGPVHSVDIALRKALQKVYPQINKVKLTDYRVILPGEIKNTESVVRVTIEFTDGEKNWRTEGVSTSVIEASVIALIDGLDYYLQTEKLIKSEVINN", "text": "FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate. Makes part of a pathway for isoleucine biosynthesis, i.e. the citramalate-dependent pathway. Also displays a low alpha-isopropylmalate synthase activity, using 2-oxoisovalerate as substrate, but is unable to use 2-oxoglutarate. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family."}
+{"protein": "MLLGSLWGRCHPGRCALFLILALLLDAVGLVLLLLGILAPLSSWDFFIYTGALILALSLLLWIIWYSLNIEVSPEKLDL", "text": "FUNCTION: May play a role in inducing apoptosis during endoplasmic reticulum (ER) stress and in the inhibition of proliferation and tumorigenicity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
+{"protein": "MAGKLQAHNIRIRTFIHATEDPEKVLEALETLFPEEISPKDVEFEVIETEGYFGNPILVVDAEIKHSRNIRKFLENLRGLLSKEDRKYLWEHAEEKVDETGTFYIRFDKQKAYLGEVKVSEGEDVIHVRIKVKAFPMKKEAVVKAVREWLEGED", "text": "FUNCTION: In vitro, binds efficiently double-stranded RNAs in a non- sequence specific manner."}
+{"protein": "MIRWGLIGASTIAREWVIGAIRAAGGEVVSVMSSSAERGEAYAAENGIAKAVTSVDDLVGDPDVDAVYISTTNELHHGQALAAIRAGKHVLCEKPLAMNLNDGCEMVLKACEAGVVLGTNHHLRNAATHRAMREAIAAGRIGRPIAARVFHAVYLPPHLQGWRLDKPEAGGGVILDITVHDADTLRFVLNDDPIEAVAISHSAGMGKEGLEDGVMGVLRFRSGVIAQFHDAFTTKFAETGLEVHGTAGSLIGRNVMTQRPVGTVVLRNEEGESELPLDHRNLYETAIAAFHSAIGGNGRPSASGEDGVWSLATGLAVVKAAATGGAVEIETGL", "text": "FUNCTION: Catalyzes the NADPH-specific reduction of 1,5-anhydro-D- fructose to 1,5-anhydro-D-mannitol. SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
+{"protein": "MIETILPAGVESAELLEYPEDLKAHPAEEHLIAKSVEKRRRDFIGARHCARLALAELGEPPVAIGKGERGAPIWPRGVVGSLTHCDGYRAAAVAHKMRFRSIGIDAEPHATLPEGVLDSVSLPPEREWLKTTDSALHLDRLLFCAKEATYKAWWPLTARWLGFEEAHITFEIEDGSADSGNGTFHSELLVPGQTNDGGTPLLSFDGRWLIADGFILTAIAYA", "text": "FUNCTION: Catalyzes the transfer of the 4'-phosphopantetheine moiety from coenzyme A to a serine residue in the acyl-carrier domain of carboxylic acid reductase Car, thus converting apo-Car to fully active holo-Car. Is probably also responsible for the activation of other proteins with phosphopantetheine attachment sites. SIMILARITY: Belongs to the P-Pant transferase superfamily."}
+{"protein": "MSNMEKHLFNLKFAAKELNRSSKKCDKEEKAEKAKIKKAIQKGNMEVARIHAENAIRQKNQGVNFLRMSARVDAVAARVQTAVTMGKVTKSMAGVVKSMDATLKSMNLEKISALMDKFEHQFETLDVQTQQMEDTMSSTTTLTTPQNQVDMLLQEMADEAGLDLNMELPQGQTGSVGTSVASAEQDELSQRLARLRDQV", "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. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Endosome Late endosome membrane; Peripheral membrane protein Note=Localizes to the midbody of dividing cells, colocalizing with CEP55 and CHMP5. Localized at the periphery of the Fleming body (By similarity). SIMILARITY: Belongs to the SNF7 family."}
+{"protein": "MASSGFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE", "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: Vacuole membrane; Multi-pass membrane protein. Note=Tonoplast. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family."}
+{"protein": "MQGLLLSLSLLASAAVGVLASDDLKIDVTLPVECDRVTKKGDKINVHYKGTLKSNGEKFDSSYDRQSPFSFKLGAGMVIKGWDEGLVDMCIGEKRTLTIGPSYGYGDRNVGPIPAGSTLVFETELVGIEGVPKPESIVTKSATDAPESTASAKVVEKVASVAKQAAEVVETIIADTDDTQEHNEL", "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": "MEVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIVTMNGNDFQTGGIGNLPVRNWTFDFGLLGTTLLNLDANYVENARTTIEYFIDFIDNVCMDEIARESQRNGVAPQSEALRKLSGIKFKRINFDNSSEYIENWNLQNRRQRTGFVFHKPNIFPYSASFTLNRSQPMHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANIQQFEHIVQLRRALTTATITLLPDAERFSFPRVINSADGATTWFFNPVILRPNNVEVEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLMRPPNMTPAVNALFPQAQPFQHHATVGLTLRIESAVCESVLADANETLLANVTAVRQEYAIPVGPVFPPGMNWTELITNYSPSREDNLQRVFTVASIRSMLIK", "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": "MPLKPEEHEDILNKLLDPELAQSERTEALQQLRVNYGSFVSEYNDLTKSHEKLAAEKDDLIVSNSKLFRQIGLTDKQEEDHKKADISETITIEDLEAK", "text": "FUNCTION: Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid. The scaffolding protein is found within the capsid as a serie of concentric shells. During DNA packaging, the scaffolding protein molecules are released from the procapsid. SUBCELLULAR LOCATION: Note=Present in about 147 copies in the prohead but not present in mature virions. SIMILARITY: Belongs to the phi29likevirus scaffolding protein family."}
+{"protein": "MEEKGEISPSGVVTVKGDEALVPRTEFQQNPSFLQFVSPTTVVTPLPPPPAPSSAPVPTTVTPGSATASTGSDPTKKKRGRPRKYAPDGSLNPRFLRPTLSPTPISSSIPLSGDYQWKRGKAQQQHQPLEFVKKSHKFEYGSPAPTPPLPGLSCYVGANFTTHQFTVNGGEDVTMKVMPYSQQGSRAICILSATGSISNVTLGQPTNAGGTLTYEGRFEILSLSGSFMPTENGGTKGRAGGMSISLAGPNGNIFGGGLAGMLIAAGPVQVVMGSFIVMHQAEQNQKKKPRVMEAFAPPQPQAPPQLQQQQPPTFTITTVNSTSPSVNTVEEQKPQAYGGGIVRPMAQMPSSFQNDNSTMNNFTPAYHGYGNMNTGTTHKEEHEDEDGGDDDDDSGDTRSQSHSG", "text": "FUNCTION: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKKLTAAAIATMGFATFTMAHQADAAETTNTQQAHTLMSTQSQDVSYGTYYTIDSNGDYHHTPDGNWNQAMFDNKEYSYTFVDAQGHTHYFYNCYPKNANANGSGQTYVNPATAGDNNDYTASQSQQHINQYGYQSNVGPDASYYSHSNNNQAYNSHDGNGKVNYPNGTSNQNGGSASKATASGHAKDASWLTSRKQLQPYGQYHGGGAHYGVDYAMPENSPVYSLTDGTVVQAGWSNYGGGNQVTIKEANSNNYQWYMHNNRLTVSAGDKVKAGDQIAYSGSTGNSTAPHVHFQRMSGGIGNQYAVDPTSYLQSR", "text": "FUNCTION: Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M23B family."}
+{"protein": "MLVRTLYISSSVGSSNMLCNHGLKVIGKYSAIHEATRKIIVRSYSKETIKKHNKQAILNTAPIEFIANNSPLVGISDVNTIKEAAKRTLRCTDDVTDDQTDEIHPHLPFNVKPVDGKARAALKKEKNSMSLDIKKTMEAYVQLTKPRLTILVMLSAICSYALSPYPATVTELLCLTVGTTMCSGAANAINMGREPDYDRQMIRTQARPVVRGAVTPKQAFSFAFGMGTLGTSILYLGVNPTVAALGLSNIALYSWIYTSLKRKHIINTWVGALVGAIPPLMGWAAASPLTHPGSWCLAGLLYAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNPLLNARVALRYSLLMFPLCFGLSYFNITDWYYQIDSGLVNAWLCLWSFKFYMQQRLNYSSKIKNDRVKFNEGLATANVYARKAFFASVLHLPAVLILAILHKKNRWDWLFEDSENPKLK", "text": "FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family."}
+{"protein": "MTFSEILDRVGSMGRFQFLHVAILGLPILNMANHNLLQIFTAATPVHHCRLPPNASAGPWVIPMGPNGKPERCLRFVHPSNASLPNDTQRSMEPCLDGWVYNSTKDSIVTEWNLVCNSNKLKEMAQSIFMAGILIGGLVLGDLSDRFGRRPILTCSYLLLAASGSGAAFSPTFPVYVVFRFLCGCGISGITLSTVILNVEWVPTRMRAIMSTALGYCYTVGQFILPGLAYAIPQWRWLQLTVSIPFFIFFLSSWWTPESIRWLVLTGKSSKALKILRRVAAFNGKKEEGERLSLEELKLNLQKEISLAKAKYTAADLFRIPMLRRMTFCLSLAWFATGFAYYSLAMGVEEFGVNLYILQIIFGGVDIPAKFITILSLSYLGRHTTQAAALLLAGGAILALTFVPLDLQTVRTVLAVFGKGCLSSSFSCLFLYTSELYPTVIRQTGMGVSNLWTRVGSMLSPLVKITGEVQPFIPNIIYGITALLGGSAALFLPETLNQPLPETIEDLENWSLRAKEPKQEPEVEKASQRIPLQPYGPDLGSS", "text": "FUNCTION: Functions as an organic anion/dicarboxylate exchanger that couples organic anion uptake indirectly to the sodium gradient. Transports organic anions such as estrone 3-sulfate (E1S) and urate in exchange for dicarboxylates such as glutarate or ketoglutarate (2- oxoglutarate) (PubMed:15846473). Plays an important role in the excretion of endogenous and exogenous organic anions, especially from the kidney and the brain. Responsible for the transport of prostaglandin E2 (PGE2) and prostaglandin F2(alpha) (PGF2(alpha)) in the basolateral side of the renal tubule. May be involved in the basolateral transport of steviol, a metabolite of the popular sugar substitute stevioside. May participate in the detoxification/ renal excretion of drugs and xenobiotics, such as the histamine H(2)-receptor antagonists fexofenadine and cimetidine, the antibiotic benzylpenicillin (PCG), the anionic herbicide 2,4-dichloro- phenoxyacetate (2,4-D), the diagnostic agent p-aminohippurate (PAH), the antiviral acyclovir (ACV), and the mycotoxin ochratoxin (OTA), by transporting these exogenous organic anions across the cell membrane in exchange for dicarboxylates such as 2-oxoglutarate (PubMed:15846473) (By similarity). Contributes to the renal uptake of potent uremic toxins (indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2- furanpropionate (CMPF)), pravastatin, PCG, E1S and dehydroepiandrosterone sulfate (DHEAS), and is partly involved in the renal uptake of temocaprilat (an angiotensin-converting enzyme (ACE) inhibitor) (By similarity). May contribute to the release of cortisol in the adrenals (By similarity). Involved in one of the detoxification systems on the choroid plexus (CP), removes substrates such as E1S or taurocholate (TC), PCG, 2,4-D and PAH, from the cerebrospinal fluid (CSF) to the blood for eventual excretion in urine and bile (By similarity). Also contributes to the uptake of several other organic compounds such as the prostanoids prostaglandin E(2) and prostaglandin F(2-alpha), L-carnitine, and the therapeutic drugs allopurinol, 6- mercaptopurine (6-MP) and 5-fluorouracil (5-FU) (By similarity). Mediates the transport of PAH, PCG, and the statins pravastatin and pitavastatin, from the cerebrum into the blood circulation across the blood-brain barrier (BBB). In summary, plays a role in the efflux of drugs and xenobiotics, helping reduce their undesired toxicological effects on the body (By similarity). SUBCELLULAR LOCATION: Basolateral cell membrane; Multi- pass membrane protein Note=Localizes on the brush border membrane of the choroid epithelial cells. Localizes to the basolateral membrane of the proximal tubular cells. Localized on the abluminal and possibly, luminal membrane of the brain capillary endothelial cells (BCEC). SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family."}
+{"protein": "MALKLIHKEFLELARDPQPHCSAGPVWDDMLHWQATITRPNDSSYLGGVFFLKFPSDYLFKPPKIKFTNGIYHQR", "text": "SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "MEMKVLILVGVRLLFLPTTVCQSGMKHVSDNSALTAESFNGNEHSFEEFPLSDIEGWTGATTTIKAKCPEESITTLHVNNATMGYLRSSLSTKVIPAIYILVFVIGVPANIVTLWKLSSRTKSICLVIFHTNLAIADLLFCVTLPFKIAYHLNGNDWVFGEVMCRVTTVAFYGNMYCAILILTCMGINRYLATVHPFTYRKLPKRNFTLLMCGVVWVMVVLYMLPLAILKQEYHLVQPGITTCHDVHDTCESPLPFQFYYFVSLAFFGFLIPFVVSVFCYTTLIHKLNAQDRKWLRYIKAVLLILVIFTICFAPTNIILIIHHANYYYSNTDSLYFMYLIALCLGSLNSCLDPFLYFIMSKIVDQLTS", "text": "FUNCTION: 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": "MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMSSAGMAGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANSLGIPVPAAAGAQQ", "text": "FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (By similarity). May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (By similarity). During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage (By similarity). Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation (By similarity). Can also negatively regulate apoptosis (PubMed:12191471). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed:12191471). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed:12191471). Phosphorylates YY1, protecting YY1 from cleavage by CASP7 during apoptosis (By similarity). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV (By similarity). Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB (By similarity). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (By similarity). Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 (By similarity). Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (By similarity). Acts as an ectokinase that phosphorylates several extracellular proteins (By similarity). During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV (By similarity). Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (By similarity). Plays an important role in the circadian clock function by phosphorylating BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (PubMed:19330005). Phosphorylates FMR1, promoting FMR1-dependent formation of a membraneless compartment (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily."}
+{"protein": "MAKERCQKRSFQDTLEDIKNRMKEKRNKNLAGIGKRKSFIVAPGQVPTNTATLLRYYQDNNRLLVLALENEKSKVREAQDVILQLRKECYYLTCQLYALKEKLTSRQSEETTQNWKGRPSDVVSSIDNTTRDLSGKSLQQIAVEETDCPYQTTEPSPAVTPETQGCDFDSGKVESTDEVLPRTISIRRHLRKDFSNISHSTTLEDCKASPRVAQSLEVKGSRCREVTVTLHRLENVCLWNKDQISLCSRLINPAKITETEVILSSKPEQIESKHKRARKRRAEQRRTKQRCKSKSSLRSKGNKNKDKQGLPPTTLDGGIGSCDAYDFNLKGTVHPTPFRQKMNNGCNKETDSSNSEVSDLECSTSEDESDDLYLPPSKRLRDYRESERAVTRPRSKRGLQYPDGKERKEVLPSTAPTGIPPETQESPRCSLKDVTNILQCPRVKIRKPSLPPKRREDSPAVALTKRRCSTIKSYKEPTLASKLRRGDPFTDLCFLNSPIFKQKRGMRCPKRRTKQTQ", "text": "FUNCTION: Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the STAG2 subunit of cohesin complex at the centromere, ensuring cohesin persistence at centromere until cohesin cleavage by ESPL1/separase at anaphase. Essential for proper chromosome segregation during mitosis and this function requires interaction with PPP2R1A. Its phosphorylated form is necessary for chromosome congression and for the proper attachment of spindle microtubule to the kinetochore. Necessary for kinetochore localization of PLK1 and CENPF. May play a role in the tension sensing mechanism of the spindle-assembly checkpoint by regulating PLK1 kinetochore affinity. Involved in centromeric enrichment of AUKRB in prometaphase. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Chromosome, centromere, kinetochore Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to the inner centromere throughout prophase until metaphase and disappears at anaphase. Centromeric localization requires the presence of BUB1 and the interaction with PPP2R1A. Colocalizes with NEK2 at the kinetochore. Colocalizes with and SS18L1 at the kinetochore. Phosphorylation by AUKRB and the presence of BUB1 are required for localization to the kinetochore. Isoform 1 primarily localizes to kinetochores during G2 phase and mitotic prophase, metaphase, and anaphase and does not appear to be associated with kinetochores during late mitosis. Isoform 3 is found at the centrosome in interphase and at spindle poles in mitosis and its spindle pole localization is PLK1 dependent. Isoform 3 does not localize to kinetochores during any stages of the cell cycle. SIMILARITY: Belongs to the shugoshin family."}
+{"protein": "MKYSCCALVLAVLGTELLGSLCSTVRSPRFRGRIQQERKNIRPNIILVLTDDQDVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNRFRTNKKAKIWRDTFLVERGKFLRKKEESSKNIQQSNHLPKYERVKELCQQARYQTACEQPGQKWQCIEDTSGKLRIHKCKGPSDLLTVRQSTRNLYARGFHDKDKECSCRESGYRASRSQRKSQRQFLRNQGTPKYKPRFVHTRQTRSLSVEFEGEIYDINLEEEEELQVLQPRNIAKRHDEGHKGPRDLQASSGGNRGRMLADSSNAVGPPTTVRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSKQSYYNKEKGVKKQEKLKSHLHPFKEAAQEVDSKLQLFKENNRRRKKERKEKRRQRKGEECSLPGLTCFTHDNNHWQTAPFWNLGSFCACTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTVERGILNQLHVQLMELRSCQGYKQCNPRPKNLDVGNKDGGSYDLHRGQLWDGWEG", "text": "FUNCTION: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity (PubMed:12368295, PubMed:12686563). It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin (PubMed:12368295, PubMed:12686563). Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation (PubMed:12686563). SUBCELLULAR LOCATION: Endoplasmic reticulum Golgi apparatus, Golgi stack Cell surface. SUBCELLULAR LOCATION: [Extracellular sulfatase Sulf-2 secreted form]: Secreted. SIMILARITY: Belongs to the sulfatase family."}
+{"protein": "MCTKMEQPFYHDDSYAAAGYGRTPGGLSLHDYKLLKPSLALNLSDPYRNLKAPGARGPGPEGNGGGSYFSSQGSDTGASLKLASSELERLIVPNSNGVITTTPTPPGQYFYPRGGGSGGGAGGAGGGVTEEQEGFADGFVKALDDLHKMNHVTPPNVSLGASGGPPAGPGGVYAGPEPPPVYTNLSSYSPASAPSGGAGAAVGTGSSYPTATISYLPHAPPFAGGHPAQLGLGRGASAFKEEPQTVPEARSRDATPPVSPINMEDQERIKVERKRLRNRLAATKCRKRKLERIARLEDKVKTLKAENAGLSSTAGLLREQVAQLKQKVMTHVSNGCQLLLGVKGHAF", "text": "FUNCTION: Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[GC]TCA-3' (By similarity). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to an AP-1 consensus sequence and its transcriptional activity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Jun subfamily."}
+{"protein": "MNLSQDGIKLHRGNFTAIGRQIQPYLEEGKCFRMVLKPWREKRSLSQNALSHMWYSEISEYLISRGKTFATPAWVKDALKHTYLGYETKDLVDVVTGDITTIQSLRHTSDLDTGEMYVFLCKVEAWAMNIGCHLTIPQSCEFQLLRDKQEA", "text": "SIMILARITY: To equivalent protein in phage 82."}
+{"protein": "MHHHHQQPSYGSGYPGQAYRQQQNPYPQYGHPSPQPYPPQNGYSHPSSGYPPSPAPPNGGQMYHGRQPSYPPNQYPPAHGGPTAPPTNPQAFGHGAPQGYNFQYSRCTGKRKALLIGINYFGQKGQLRGCINDVKNMSTYLNQNFGYAREDMVILTDDQQNPMSQPTKANILRAMHWLVKDAQPNDSLFFHYSGHGGQTPDLDGDEDDGYDEVIYPVDFRVAGHIVDDEMHRIMVKPLQPGVRLTAIFDSCHSGSALDLPYIYSTQGILKEPNLAKEAGQGLLGVISSYARGDMGGMMSTAVGFLKKAAKGDEAYQRTKQTKTSPADVIMWSGSKDDQTSQDAQIAGQATGAMSWAFITAMRKNPQQSYVQLLNSIRDELSTRYTQKPQLSSSHPLDVNLLYVM", "text": "FUNCTION: Involved in cell death (apoptosis). SIMILARITY: Belongs to the peptidase C14B family."}
+{"protein": "MGSKKLTVGSDSHRLSKSSFSSNKSSHSATKDQPIDTDDIDEDDESGHNIILNIISQLRPGCDLTRITLPTFILEKKSMLERVTNQLQFPEFLLQAHSEKDPLKRFLYVMKWYLAGWHIAPKAVKKPLNPVLGEYFTAYWDLPNKQQAYYISEQTSHHPPECAYFYMIPESSIRVDGVVIPKSRFLGNSSAAMMDGSTVLQFLDIKDGNGKPEKYVLTQPNVYVRGILFGKMRIELGDHMIIKSPNFQADIEFKTKGYVFGTYDAIEGTVKDYDGNAYYEISGKWNDVMYLKDLKQPRSSPKVFLDTHKESPLRPKVRPLSEQGEYESRKLWKKVTDALAVRNHPVATEEKFQIEDHQRQLAKKRIEDGVEFHPKLFRRSKPGEDLDYCIYKNIPVDEDPEKQIRSILQIAPILPGQQFTDKFFIPAFEKIKSQKKMIENEKQNPAKQ", "text": "FUNCTION: Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide- coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:15173322, PubMed:16156791, PubMed:23934110, PubMed:26206936). Catalyzes the lipid countertransport between the endoplasmic reticulum (ER) and the plasma membrane (PM). Specifically exchanges phosphatidylserine (PS) with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the PM in exchange for PI4P, which is delivered to the ER-localized PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P gradient at the ER/PM interface, SAC1 drives PS transport (PubMed:23934110, PubMed:26206936). Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206936). Also binds phosphatidic acid (PA) (PubMed:16156791). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Endoplasmic reticulum membrane Note=Localizes to the cortical endoplasmic reticulum at the endoplasmic reticulum-plasma membrane contact sites. SIMILARITY: Belongs to the OSBP family."}
+{"protein": "MKIWTSEHVFDHPWETVTTAAMQKYPNPMNPSVVGVDVLDRHIDPSGKLHSHRLLSTEWGLPSIVKSLIGAARTKTYVQEHSVVDPVEKTMELKSTNISFTNMVSVDERLIYKPHPQDPDKTILTQEAIITVKGVSLSSYLEGLMASTISSNASKGREAMEWVIHKLNAEIEELTASARGTIRTPMAAAAFAEK", "text": "SIMILARITY: Belongs to the slowmo family."}
+{"protein": "MWPVLWTVVRTYAPYVTFPVAFVVGAVGYHLEWFIRGKDPQPVEEEKSISERREDRKLDELLGKDHTQVVSLKDKLEFAPKAVLNRNRPEKN", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMIM12 family."}
+{"protein": "MNKTQSPSLNTNSHWYVIDAKNQTLGRISTHISNILRGKNKPSYTPYLDTGDYVIVINSAHVSVSGNKTNQKLYRRHSGQPGGLKVETFDQLQTRLPNRIIEKSVKGMLPKGPLGRKLFTKLKVYSGPIHPHVAQKPQEYIV", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL13 family."}
+{"protein": "MASQQFPPQNQETQPGKEHAMDPRPEAIIQSYKPANKLKDKVAIVTGGDSGIGRAVCLCFALEGATVAFTYVKGQEEKDAEETLRALRDIRARTGAKDPMAIPADLGYDDNCRKVVDEVAGAYGGAIDILVNNAAEQYERPSITDITEDDLERVFRTNIFSYFFMSKHAVKRMRDRRGGAGAGGCSIINTSSINAYKGNKTLLDYTATKGAIVAFTRALALQLAEEGIRVNGVAPGPIWTPLIPASFAEEKVRQFGSQVPMGRAGQPSEVAPSFVFLASDDASYMSGQMLHVNGGVIVNG", "text": "FUNCTION: May act as a short alcohol-polyol-sugar dehydrogenase possibly related to carbohydrate metabolism and the acquisition of desiccation tolerance. May also be involved in signal transduction (By similarity). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MSSFINHHFYPSVCTSKHALPINPTSPFYLGIPNFRQKSRFMHLTPRCFSRQIDPLDKQKKRSFSVKECAISLALAAALISGVPSLSWERHAEALTSPVLPDLAVLISGPPIKDPEALLRYALPIDNKAIREVQKPLEDITESLRVLGLKALDSVERNLKQASRALKNGKSLIIAGLAESKKDRGVELLDKLEAGMGELQQIVENRNREGVAPKQRELLQYVGSVEEDMVDGFPYEVPEEYQTMPLLKGRAVVEMKVKVKDNPNVDNCVFRIVLDGYNAPVTAGNFLDLVERHFYDGMEIQRRDGFVVQTGDPEGPAEGFIDPSTEKPRTIPLEIMVEGEKVPVYGSTLEELGLYKAQTKLPFNAFGTMAMAREEFENNSGSSQIFWLLKESELTPSNANILDGRYAVFGYVTDNQDYLADLKVGDVIESVQAVSGVDNLVNPTYKIAG", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Has a regulatory effect on thylakoid protein phosphorylation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. Note=Can interact with the inner surface of the stroma-exposed thylakoid regions."}
+{"protein": "MNSKLAVALLATFLLSLTLCEAAVLTRIGTELRCQCIKTHSTPFHPKFIKELRVIESGPHCANSEIIVKLVDGRELCLDPKEKWVQKVVQIFLKRAEQQES", "text": "FUNCTION: Chemotactic factor that mediates inflammatory response by attracting neutrophils, basophils, and T-cells to clear pathogens and protect the host from infection. Also plays an important role in neutrophil activation. Released in response to an inflammatory stimulus, exerts its effect by binding to the G-protein-coupled receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes and endothelial cells. G-protein heterotrimer (alpha, beta, gamma subunits) constitutively binds to CXCR1/CXCR2 receptor and activation by IL8 leads to beta and gamma subunits release from Galpha (GNAI2 in neutrophils) and activation of several downstream signaling pathways including PI3K and MAPK pathways. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family."}
+{"protein": "MSGRRVYSTSVTGSREIKSQQSEVTRILDGKRIQYQLVDISQDNALRDEMRALAGNPKATPPQIVNGDQYCGDYELFVEAVEQNTLQEFLKLA", "text": "FUNCTION: Could act as a modulator of glutaredoxin biological activity (By similarity). May play a role in cytoskeleton organization (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell projection, ruffle membrane Nucleus. SIMILARITY: Belongs to the SH3BGR family."}
+{"protein": "MGRTREAGCVAAGVVIGAGACYCVYRLAWGRDENEKIWDEDEESTDTSEIGVETVKGAKTSVGAGSGVKLQGDSKVKPEVNLGLEDCPGVKEKAHSGSHRGGGLEAKAKALFNTLKEQASAKAGKGARMGTITGNRTLAPSLPCPGGRGGGCHPTRSGSRAGGRASGKSKGKARSKSTRAPATTWPVRRGKFNFPYKIDDILSAPDLQKVLNILERTNDPFIQEVALVTLGNNAAYSFNQNAIRELGGVPIIAKLIKTKDPIIREKTYNALNNLSVNAENQGKIKTYISQVCDDTMVCRLDSAVQMAGLRLLTNMTVTNHYQHLLSYSFPDFFALLFLGNHFTKIQIMKLIINFTENPAMTRELVSCKVPSELISLFNKEWDREILLNILTLFENINDNIKNEGLASSRKEFSRSSLFFLFKESGVCVKKIKALANHNDLVVKVKVLKVLTKL", "text": "FUNCTION: Regulates mitochondrial transport during axon regeneration. Increases the proportion of motile mitochondria by recruiting stationary mitochondria into the motile pool. Enhances mitochondria movement and neurite growth in both adult axons and embryonic neurons. Promotes neuronal survival and axon regeneration after nerve injury. May link mitochondria to the Trak1-kinesin motor complex via its interaction with MIRO1. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion outer membrane; Single- pass membrane protein. SIMILARITY: Belongs to the eutherian X-chromosome-specific Armcx family."}
+{"protein": "MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG", "text": "FUNCTION: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis (PubMed:7901002, PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134, PubMed:28813412). Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane (PubMed:14665625, PubMed:16888141, PubMed:19571812). STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion (PubMed:14665625, PubMed:16888141, PubMed:19571812). Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm (By similarity). Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein Cell membrane Synapse, synaptosome Note=Colocalizes with KCNB1 at the cell membrane (PubMed:17301173). Colocalizes with PLCL1 at the cell membrane (PubMed:22673903). SIMILARITY: Belongs to the syntaxin family."}
+{"protein": "MDYYRKYAAVILATLSVFLHILHSFPDGEFTMQGCPECKLKENKYFSKLGAPIFQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNAKVENHTECHCSTCYYHKS", "text": "FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family."}
+{"protein": "MGPKFGTSGLRGLATELVGSVSALYATAFSRMLLDRGRVAPGATVLVGRDFRDSSSEIAAICMAALARAGMVPVDCGGLPTPALALYGRKLGAASLMITGSHIPADRNGIKFYLPDGEINKADEQAITALAEQLSADADATRVECGRGADHSSEATDFYIQRYETLLPKSGLKGLKIGLYQHSSVARDILTTILEGHGANVVPVGRSEVFIPVDTEAISAATCKMLAAWAKEFAFDAIVSSDADADRPLLTDETGTPLRGDLLGLICARLLEAKLIATPITSNSGIEAASGVEVVRTRVGSPYVIAAMTEAVARGKQRVMGFEANGGVMLGSNFSFGGASLPALPTRDCVLPIIAALHMAVEAKTPLSGIVAMHRLPVALSGRIENYPFDRSDALVAFLKASKANVSHLFSRIGRVAGTDDVDGLRLTFEGGRILHIRPSGNAPELRCYVEADDPDAAEHLLAQGLAVLNSSMV", "text": "SIMILARITY: Belongs to the phosphohexose mutase family."}
+{"protein": "MNTSQTAAGNRITFTSQPLPNGTISIAGNPGAVISTAQLPNTTTIKTIQAGIGGQHQGLQQVHHVQQQQQSQQQQQQQQQTQSAGQPLLNSMLPAGVVVGMRQQAPSQQQQKNVPTNPLSRVVINSHMAGVRPQSPSITLSTLNTGQTPALLVKTDNGFQLLRVGTTTGPPTVTQTITNTSNNSNTTSTTNHPTTTQIRLQTVPAAASMTNTTATSNIIVNSVASSGYANSSQPPHLTQLNAQAPQLPQITQIQTIPAQQSQQQQVNNVSSAGGTATAVSSTTAATTTQQGNTKEKCRKFLANLIELSTREPKPVEKNVRTLIQELVNANVEPEEFCDRLERLLNASPQPCLIGFLKKSLPLLRQALYTKELVIEGIKPPPQHVLGLAGLSQQLPKIQAQIRPIGPSQTTTIGQTQVRMITPNALGTPRPTIGHTTISKQPPNIRLPTAPRLVNTGGIRTQIPSLQVPGQANIVQIRGPQHAQLQRTGSVQIRATTRPPNSVPTANKLTAVKVGQTQIKAITPSLHPPSLAAISGGPPPTPTLSVLSTLNSASTTTLPIPSLPTVHLPPEALRAREQMQNSLNHNSNHFDAKLVEIKAPSLHPPHMERINASLTPIGAKTMARPPPAINKAIGKKKRDAMEMDAKLNTSSGGAASAANSFFQQSSMSSMYGDDDINDVAAMGGVNLAEESQRILGCTENIGTQIRSCKDEVFLNLPSLQARIRAITSEAGLDEPSQDVAVLISHACQERLKNIVEKLAVIAEHRIDVIKLDPRYEPAKDVRGQIKFLEELDKAEQKRHEELEREMLLRAAKSRSRVEDPEQAKMKARAKEMQRAEMEELRQRDANLTALQAIGPRKKLKLDGETVSSGAGSSGGGVLSSSGSAPTTLRPRIKRVNLRDMLFYMEQEREFCRSSMLFKTYLK", "text": "FUNCTION: TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. May function as a coactivator by serving as a site of protein-protein contact between activators like Sp1 (or btd) and TFIID complex. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF4 family."}
+{"protein": "MSSPSKRREMDLMKLMMSDYKVEMINDGMQEFFVEFSGPKDSIYEGGVWKIRVELPDAYPYKSPSVGFITKIYHPNVDEMSGSVCLDVINQTWSPMFDLVNVFETFLPQLLLYPNPSDPLNGEAAALMMRDRPTYEQRVKEYCEKYAKPRADTEEMSSDDEMSEDEYASDGDDEDDVAIAGKLDP", "text": "FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNANSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPLPWMDEDELRYREEVPCYCGKQGCIETFISGTGFAMDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHVVNILDPDVIVLGGGMSNVDRLYQTVGQLIKQFVFGGECETPVRKAKHGDSSGVRGAAWLWPQE", "text": "FUNCTION: Catalyzes the phosphorylation of fructose to fructose-6-P. Has also low level glucokinase activity in vitro. Is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L- threonine. SIMILARITY: Belongs to the ROK (NagC/XylR) family."}
+{"protein": "MPGIKVHPNESFDEAYRKFKKQVDRNLVVTEVRARRFFEPMTEIRKKQKISARKKMLKRLYMLRRYESRL", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family. SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family."}
+{"protein": "MTMTVEKRIEADVTVSHEGVERAYVTFLAGNKDYWMLVVGLAKGLRKVKSAYPLVVATLPDVPEEHRQILVDQGCIIRDIEPVYPPENTTGYSMAYYVINYSKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTPRGYLYAVKDCFCEVSWSKTPQYKIGYCQQSPEKVTWPVESLGAPPPVYFNAGMLVFGPNLVTYEDLLRVVQITTPTYFAEQDFLNIYFRDIYKPIPSTYNLVMAMLWRHPEHIDLDQISVVHYCANGSKPWKFDEAEEHMDREDIKMLVKKWWEIYEDSSLDYKNFVETESKLNPVTATLASKKLVGDVLTSLAPSAA", "text": "FUNCTION: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. May promote plant stress tolerance (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyltransferase 8 family. Galactosyltransferase subfamily."}
+{"protein": "MCTTTDVVVLSSSPDQIRSCSLANPKCGAEKAFVLSPVSSSPSSLPSSSDLFQPPTRSRFFKPGGGNEGSSRTAREESETGTKQNDLAASRKKAAVRGGRQKRTKEQPPNESQTLFDNPEPPIPKHNGCTSKKGTGSRKKRIDAASKCTKSGSKKITGKVTKPGITETTKFENKTKIVTSDVSPGKSPANKLELEKDGLQIEVAMKRRLDWTPTKDTGKQAVALDDTGDNKTRFGELLSEYGFLKAAAVSQTDSKLSDGAPTKCRRLELVDTHNPSTSKRTSPDADSDRSNVRSTRSSRAPAAEGKSKKRSRKITTLTGRVTALYTKDCTDHLDAANTMIRASEDVSSKLLSKSLDLDSCVLAPGDAVDYLQDQDLIFGTCSQLEREDSPTMLRDMQKEICASKNSMIENRKPSSTTRAGSGLYSHTTVSRFQTQRDLWSVAARDMDGSLAEIEVLDMVDITDVSELPPKPNGELPDRSEKNDEDTVSQGESSRPIEITDDFGVEVDVRMEYLATSETKPEETAYAASEIRPMPRFADWKDSDLSRQVRLYGFKPMKNRRKMIEVLERCWKAQHSSTRTGVQYAPGKPDDGSTGKAGTIGSQMNKQSSKMDAAEKMRRESACLKEKAKSSTALEDKLSHATDRSSQMLTKSSFAHMEEIEDSEDEVIPSPSQLQSLYKRHISESRSSHPLPVSDTPSTPSSRTRTNADSDTKPSPSDSATESSLPDLASQITKAVRLQPRSFSVDCKRPSWHEKILMYDPIILEDFATWLNIEGLGLVHEDREVSAEFVRQWCESNGICCGFRKNSRRSER", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX4 family."}
+{"protein": "MKWLFWASPPQDDSNSNSGAASQVKCRNNENVDVPAPSNAAPPSDRTISKVQSSSRDWNSIVNATDWKQFTEPRTIIPTALVTGGILLCVHIHRKYLRRIPEAGHISPSFFRRRSLLGKVTSVGDGDNFRMYHTPGGKLGGWEWWRKVPTGKNELKNRTIHVRLAGVDAPELPHFGRPAQPFSQEAHSWLTNYILGRRVRAHLYRPDQYGRVVATVYVRRWLFFRQDVGLQMLKHGLATVYEAKTGVEFGGVELERQYREAEACAKKKGKGMWKALKGGTKGEWESPREYKTRMAAEEGQKKNARGITRKK", "text": "SUBCELLULAR LOCATION: Mitochondrion. Membrane; Single- pass membrane protein. SIMILARITY: Belongs to the LCL3 family."}
+{"protein": "MQEAALGMMGATVGGDGDTAVVAEQNRQLKGEIATHPMYEQLLAAHVACLRVATPIDQLPIIEAQLSQSHHLLRSYASTAVGYHHDRHELDNFLAQYVMVLCSFKEQLQQHVRVHAVEAVMACREIENNLHSLTGATLGEGSGATMSEDEDDLPMDFSSDNSGVDFSGGHDMTGFGPLLPTESERSLMERVRQELKLELKQGFKSRIEDVREEIMRKRRAGKLPGDTTTVLKNWWQQHCKWPYPTEDDKAKLVEETGLQLKQINNWFINQRKRNWHNNSHSLTSLKSKRKH", "text": "FUNCTION: May be involved in secondary cell wall biosynthesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/KNOX homeobox family."}
+{"protein": "MTLPVLIIGAGLSGLTTARLLTNAHIPCIVFEASPPSRTQGYAISLRDWGFNALLRALGNLPLSSLTRAVAPDRHIGGWGWLDQSWRNNQTGEIIMMPPKESKEKPTILRANRNALRQWIADAGVGEDEEIDVRYGHRLVGVQLLREGGDGNVVTAEFANGATYTGSLLIAADGVHSTVRTLILPAVKPEILPVLVYHGDFKLSREEYECVIRPHAGESTIVAGVGDGFNTPLTVCDVTSTTVHMDWTYSRPSIGDNDPLYNPNITSEEAKVIPEALIEEINAKKLGEPWSLFLNGEAMRRHRVFNWLTRCVSMERSDVNSCTGKGVVFVGDSWHAMPIFGGEGGNHAIFDGIELAKMLEVAWGRSKEDVQAAIGKYYDKSWRRCNDAVRRSKQRFYQLHRPISEWIEIAEKQKMRA", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment (PubMed:18978088, PubMed:21866960). Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:18978088). Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone (PubMed:18978088). Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC (PubMed:18978088). Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster (PubMed:18978088). Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin (PubMed:18978088). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
+{"protein": "MFNKILVVCVGNVCRSPTAERLLKRFHPSLTVASAGLGALVGKGADPAAASVASAHDLSLENHCARQISARLCREYDLILTMEKRHIAALCDIAPEMRSKVMLFGHWDSEREIPDPYRKSRDAFEAVYTLLERSARQWAQALNAEQGKP", "text": "FUNCTION: Dephosphorylates Wzc. Required for the extracellular polysaccharide colanic acid synthesis. Probably involved in the export of colanic acid from the cell to medium. Involved in protection of cells against contact-dependent growth inhibition (CDI). SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein phosphatase family."}
+{"protein": "METLHHPLVKMEDDYALSSDSEPNSSCMASTWDWKNNDERYSLSQTPSPQSLSPAVSYESPYSSSSHTQGLEEMPFSYSLLQYPSLCHGDNGDLTKKDHGHKPSMTVQRRRKASEREKLRMRAIAEALHTLRNNLPPMYSQGRQPLTKIQTLKCTINYISELTNLLQCSKRV", "text": "FUNCTION: Involved in specifying the paraxial, but not dorsal, mesoderm. May regulate the expression of T-box transcription factors required for mesoderm formation and differentiation, such as brachyury T, wnt8, vegt and eomes (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MILTKNSNEKKPLKKGLFIVFEGIDGAGKTSILKQLLEVLKEPKLVNKIFLTREPGGKNNNAAEMIREFFLKNLEVFDPLTLAYLYASSRAEHVKKTINPHLEKDHIVISDRFVHSSYIYQGIVQNQSLDVIYQINQQAIGELEIDYVFYFDVNVNNALNRMKNRFDNTNAFDSQNKQFYEKLLKQYPSVFKVYNQPKKIIFIDANKNENEVLCEVKEQLLKIFKEHKYI", "text": "FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. SIMILARITY: Belongs to the thymidylate kinase family. SIMILARITY: Belongs to the thymidylate kinase family."}
+{"protein": "MESVSCSAAAVRTGDMESQRDLSLVPERLQRREQERQLEVERRKQKRQNQEVEKENSHFFVATFVRERAAVEELLERAESVERLEEAASRLQGLQKLINDSVFFLAAYDLRQGQEALARLQAALAERRRGLQPKKRFAFKTRGKDAASSTKVDAAPGIPPAVESIQDSPLPKKAEGDLGPSWVCGFSNLESQVLEKRASELHQRDVLLTELSNCTVRLYGNPNTLRLTKAHSCKLLCGPVSTSVFLEDCSDCVLAVACQQLRIHSTKDTRIFLQVTSRAIVEDCSGIQFAPYTWSYPEIDKDFESSGLDRSKNNWNDVDDFNWLARDMASPNWSILPEEERNIQWD", "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": "MSQEIYDYANQLERAVRALPEYQKVLEVKEAIQADASASELFDEFVAMQEKIQEMMQSGQMPTAEEQTSIQELSQKIEANDQLKAYFEAQQALSVYMSDIERIVFAPLKDLVK", "text": "SIMILARITY: Belongs to the UPF0342 family."}
+{"protein": "MSYTEKPDEITKDEWMEKLNNLHVQRADMNRLIMNYLVTEGFKEAAEKFRMESGIEPSVDLETLDERIKIREMILKGQIQEAIALINSLHPELLDTNRYLYFHLQQQHLIELIRQRETEAALEFAQTQLAEQGEESRECLTEMERTLALLAFDNPEDSPFGDLLNMMQRQKVWSEVNQAVLDYENRESTPKLAKLLKLLLWAQNELDQKKVKYPKMTDLSKGVIEEPK", "text": "FUNCTION: 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. Acts as a positive regulator of Wnt signaling pathway by promoting beta-catenin (CTNNB1) nuclear accumulation. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes in the cytoplasm in the absence of Wnt stimulation and in the nucleus in the presence of Wnt stimulation. SIMILARITY: Belongs to the GID8 family."}
+{"protein": "MKFTFHKVTLKKRFPLAISRGVRYNSENLFVCYEKDGHIGWGEAAPGNSEGAATAEAVQEALENFIATGIEGFSIQELYDRAREMKIPPCAYVALDTAFWDWTAKKAQLPLRQLLGFSKPHTPTSVTIGINPPEVIKERVPLLLEGTTVQSLKIKLGSPEGIDADKTMFEQVVESTKKYPVKLRVDANGGWDVNQAQHMMQWLADRKVDYIEQPLKEGDEAGLKTLFKSRPLPIYVDESCRFSQNIPSFAAHVDGVNMKLMKCGGITEALRIIGTARAHGLKTMIGCMSESSVAIAAAAAMTGGIDHIDLDSHYNLAPDPAHGAPLINGVTLPPEIPGHGAYLKEEFYA", "text": "FUNCTION: Catalyzes the epimerization a variety of hydrophobic dipeptides. Epimerase activity is highest with L-Ala-L-Tyr, and lower with L-Ala-L-Met, L-Ala-L-Phe, L-Tyr-L-Ala, L-Tyr-L-Met and L-Tyr-L-Trp (in vitro). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family."}
+{"protein": "MTDASHPTAADDLGALSTLFRSEQGGHERVLLCQDRESGLKAVIALHSTALGPALGGTRFHAYASDEEAVLDALNLARGMSYKNALAGLPHGGGKAVIIGSPAPVSEGGLKSEALLRAYGRFVASLDGRYVTACDVGTYVADMDVVARECRWTTGRSPENGGAGDSSVLTAFGVFQGMRASAQALWGEPTLRGRTVGVAGVGKVGHHLVDHLVEDGARVVVTDVRPESVERVRARHPRVVAVPDTESLIRADLDVYAPCALGGALNDDTVPALTARVVCGAANNQLAHPGVEKDLAGRGILYAPDYVVNAGGVIQVADELLGFDFDRAKAKAAQIFDTTLAIFDRARTDGVPPAVAADRIAEQRMAEARTV", "text": "FUNCTION: Oxidative deamination of branched-chain amino acids. The catabolism of valine is the major source of fatty acid precursors for macrolide biosynthesis and a vital source of antibiotic precursors. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
+{"protein": "MRGPSGALWLLLALRTVLGGMEVRWCATSDPEQHKCGNMSEAFREAGIQPSLLCVRGTSADHCVQLIAAQEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVRRSSHVTIDTLKGVKSCHTGINRTVGWNVPVGYLVESGRLSVMGCDVLKAVSDYFGGSCVPGAGETSYSESLCRLCRGDSSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDGGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQKDLLFKDSTSELVPIATQTYEAWLGHEYLHAMKGLLCDPNRLPPYLRWCVLSTPEIQKCGDMAVAFRRQRLKPEIQCVSAKSPQHCMERIQAEQVDAVTLSGEDIYTAGKTYGLVPAAGEHYAPEDSSNSYYVVAVVRRDSSHAFTLDELRGKRSCHAGFGSPAGWDVPVGALIQRGFIRPKDCDVLTAVSEFFNASCVPVNNPKNYPSSLCALCVGDEQGRNKCVGNSQERYYGYRGAFRCLVENAGDVAFVRHTTVFDNTNGHNSEPWAAELRSEDYELLCPNGARAEVSQFAACNLAQIPPHAVMVRPDTNIFTVYGLLDKAQDLFGDDHNKNGFKMFDSSNYHGQDLLFKDATVRAVPVGEKTTYRGWLGLDYVAALEGMSSQQCSGAAAPAPGAPLLPLLLPALAARLLPPAL", "text": "FUNCTION: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the transferrin family."}
+{"protein": "MSKIFVNPSAIRAGLADLEMAEETIDLINRTIEDNQAHLQGVPIEVEALPEDMKKLQISDHQQGQPSGGATGQDGSEEEDFYMTESENPYIPFQSYLDAVGIQLVRKMKTGEGFLKIWSQAAEEIVSYVAINFPLPADKESAEKSTQTVGEPLKSNSASNTPNKRSKPSTSTDLKAQEASGPHGIDWAASNDEDDASVEAEIAHQIAESFSKKYKFPSRSSGIFLWNFEQLKMNLDDIVGGAKEIPGVIRMAKEGNKLPLRCILGGVALTHSKRFQVLVNSEKLGRIMQEDLNKYLAN", "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 P3]: Host nucleus. 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": "MSSKRAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD", "text": "FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity). In myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cell cortex Note=Colocalizes with F-actin, MYH9 and PIEZO1 at the actomyosin cortex in myoblasts."}
+{"protein": "MRMSEYFRILQGLPDGSFTREQAEAVAAQYRNVFIEDDQGTHFRLVVRQDGTLIWRSWNFEDCAGYWMNQYIRDFGILK", "text": "SIMILARITY: Belongs to the UPF0401 family."}
+{"protein": "MQEFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGIKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEELLNQPPEEQI", "text": "FUNCTION: Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Has peroxidase activity using thioredoxin or glutathione as a reducing power (PubMed:20572871, PubMed:22659048). Involved in peroxisome formation (PubMed:22659048). SUBCELLULAR LOCATION: Peroxisome matrix Mitochondrion outer membrane; Peripheral membrane protein. SIMILARITY: Belongs to the glutathione peroxidase family."}
+{"protein": "MADLEEQLSDEEKVRIAAKFIIHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNLDQFTPVKIEGYEDQVLITEHGDLGNGKFLDPKNRICFKFDHLRKEATDPRPYEAENAVESWRTSVETALRAYVKEHYPNGVCTVYGKKIDGQQTIIACIESHQFQAKNFWNGRWRSEWKFTITPSTAQVVGILKIQVHYYEDGNVQLVSHKDIQDSLTVSNEVQTAKEFIKIVEAAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA", "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": "MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQQLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADLKSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLNMAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAVGGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS", "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: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGC family."}
+{"protein": "MLDINALKEIPPATAVGAAVAVGALYFFCQCFYNLYLHPLRKIPGPKLAAIGPYLEFYHEVLRDGQYLWEIEKMHQKYGPIVRVNAREVHVKDTSYYNTIYTAGARKTNKDPATVGAFDVPTATAATVDHDLHRARRGYLNPYFSKRAVAGLEPTIHERITKLLSRFDQHRKDDQVLSLDGAFSALTADVITARFYGEHKDYLDVPDFHFVVRDGFQGLSRVYHLGRFLPSVVGALKGLPKFLIRIIFPPIAELLTMREEIEAGGIDEFTKSKSSGIKSSVLVGALSDPHIPPQERTVARMLDEGTVFLFAGTETTSRTLGITMFYLLSNPDILNKLREELKSLPPSDDNMHSLGQLENLPYLTGVVHEGLRLSFGPISRSSRVATHEALQYKEHTIPAGTPVSQSTYFVHTDTEIFPDPWEFKPERWIKAAEDGVALKKYITNFSQGSRQCIGYSMSFAEMFLTLSRIIPAFDLELYDTTKADIDMTHARIVGYPKKVPGKTESLGELRVKVIKKL", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the production of the antimicrobial trichothecene harzianum A (HA) that plays a role in Botrytis cinerea antagonistic activity and plant defense priming (PubMed:21642405, PubMed:29623313). The biosynthesis of harzianum A begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 (PubMed:21642405). Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4. TRI4 controls the addition of 3 oxygens at C-2, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichodiol (PubMed:21642405). Isotrichodiol then undergoes a non-enzymatic isomerization and cyclization to form 12,13- epoxytrichothec-9-ene (EPT) which is further converted to trichodermol by the cytochrome P450 monooxygenase TRI11 via C-4 hydroxylation (PubMed:21642405). The last step of HA synthesis is esterification of an octatriendioyl moiety to the C-4 oxygen of trichodermol. The octatriendioyl moiety is probably produced by the polyketide synthase TRI17 and the esterification performed by the trichothecene O- acetyltransferase TRI3 (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MASETKAPSEEPTSSSNKDESARFECNICLDAAKDAVVSLCGHLFCWPCLSQWLDTRPNNQVCPVCKSAIDGNKVVPIYGRGGDSSDPRKKVPPRPKGQRSEPPPQSFAGFNWGGDGGMMGGGGPNVHFSFGIGTVNGLFPLMFMLPFIQGIFPLSFVASFFGNGNQGAAAAGGGNGGGNDGNDGTHAHTHGHTHGPRGHGESAAPGSRMAQEEEYLSNIFKYIGFFMLFWLLFV", "text": "FUNCTION: E3 ubiquitin ligase that plays a role in the maintenance of muscle cell boundaries and muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix (PubMed:15210732). Ubiquitinates the LIM domain protein unc-95, thereby regulating its dislocalization from muscle dense bodies and weakening the link between the muscle cells and the hypodermis (PubMed:20385102, PubMed:15210732). Regulation of unc-95 dissociation from muscle dense bodies by ubiquitination plays an important role in ecdysis during molting (PubMed:20385102). Plays a role in the cessation of distal tip cell migration at the end of larval morphogenesis (PubMed:22285439). Acts as a negative regulator of autophagy (PubMed:23093945). SUBCELLULAR LOCATION: Cell junction Cell junction, focal adhesion Cell membrane Note=Colocalizes with deb-1/vinculin in muscle dense bodies. SIMILARITY: Belongs to the RNF5 family."}
+{"protein": "MSQYVSSMIKYAQSGDSFNILIKDNAKKITEKQFSLAYVECPRFRREGDEPFAFEAQEFSRRLVVGRPASVSTLYVIPTSKREYGRIRTSEFDLAESLLREGLAKLRPEATRNEGTSENSYFVSLEEAQDHAQQYKLGIWGPSDDVVVTEKANPANPAKFLKAHKGKKLNGIVETIRNGDQVRVRLFLSPKQHQLVTISLAGVRCPRSTFTATSPEQTSSEQEPCGDEAKQFVVTRLLQRNVVIELLDLAPNGVSFLGNVLHPAGNIATFLLSSGLGRVADNHISALGPETMQSLRTIERKAKISRLGIWKNISVSIPDINSLSLKDYSAVVSRVISTDTLEVRKDNGVECRIQLSSIRHPRPSNEKEAPYQLEAREFLRKKIIGKRVQVSLDFIRPGQNDLPAINNCTVKLSDGTNVALMVVKSGYATVIRYRMDSVDRSPIYDFLIEAEKAAQEGRKGMWSGKKPAYENIVNASESSLRSRQYLSSLQRTRKLSVIIENVISGSRFRCFCPKENCYFMFACAGIRTPRTARNDQEKGEPFAEESLSLAKSLLQHDAQVEILSVDNNGCFLGDIYVNHDTNFALKLLSQGLAWCQGYASQSNVQYSQYHDTEAAAKEQKVGMWHDYVPPEKKAASTEKESENTVKEPIYLDIVLSDIAEDGKFSFQIIGTGIQQLETLMSDLGSLKKSFKPSEKINVGMNVAAISALDNAMYRGRVLRCDRENQAADVLLYDYGSVEQIPFKNISSLPDTYTKLKPQAQLARLSYVQLPPPSSDYYEDARLVFRELAMNKGLVAKVDGHEGNVYSVTLYNPSDGSDFSDCINAQLVALGMASVIPKKKTSHFEKDTASLNILEEHQQEARLNHIGFWVYGDPLEYED", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
+{"protein": "MNSFRESDEEDNNPFSGTNHLYASGIGAVPEGDDDFLSAEVDTADETVQETREQMMSRLFGECEGPRESSAGGWTSGSMGSIGAPDGHSDEVTEFGIDTVLVEGEVRTPGRARVPASYPDAEGSLGALRIVDAGQYKDTFGNYAIGYTIAYEGRQVTRRYSEFDSLRQALARLLPTVIIPPIPSKHPLIRYFLNPLNAENDIRIIEKRRRLLSRFLNNCHDITDIREHTVFQKFLNPEYIWSEVLLTPPVSILPTNNLLAPPLNPTKPSPLHLLLPTPPRRTTSYGSPKTNNPEYDIRFTELESLLLRYHKCLQPVLASSRQKKIHFKQLASSLADLGAYYNAFSLEDNVINLPHQMDQIRDLSRAIEKIGQAVDVNYVSSELLVENIMILLEEPIGEMLQFVQEGREVLRFRMQKQQQFHIIDTTIKKRRGRIEELRNFQAQLARLEAALKQNAEESPTIARAVQRLDAQHLHKQRKSPSGELQWTGLFKSRSGSVRTHDSLTTRPVTGDVDVDLLSDEERAREIARLEGDLEKLNECYKLIQRDMLQVNESMARSFDWFIMYLHDTWALVLRNYTRTLLNWLKDCLTAWKNARVTIDTIAV", "text": "FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy. SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein Endomembrane system; Peripheral membrane protein Note=Endosome and other perivacuolar punctate structures. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "MKINLFFVFLFELLHFVAAYSCEGDESAAIEAMNVLQVPYEKYNTDPVCAFDNSTVVELSDKTWDHVIESGKWFVQLTAEGCANCTLGELLFNDLSHAFHEKYPDVHFARVYLSSSLELSVRLLISRIPSYYFIDNQNFYRVSPQVLPKNKAIALYEKDGFKSMKKEQGFFSVNGPLKSFYWVFGKALALYGHLSQKYTPLGMNVAIFGISAYIMYRSSKKAKQKQAAAAAAAAAKKK", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein."}
+{"protein": "MVGAKAGPSPGTSLGLAQQHSGGSSVLVKSPFCQVCCCGPAPCASCCHSRWPSLTASTCSRLFYILLHVGASAICCLLLSRTVVERVWGKTHRIQMPSGLCAHLFGLSDCPVLSGSGAVYRVCAGTATFHLLQAVLLVHLHSPTSPRAQLHNSFWLLKLLFLLGLCAIAFCIPDEHLFPAWHYIGICGGFAFILLQLVLITAFAHSWNKNWQTGAAQDCSWFLAVLLATLGFYSMAGVGAVLLFHYYTHPAGCLLNKMLLSLHLCFCGLISFLSIAPCIRLKQPRSGLLQASVISCYIMYLTFSALSSRPPERVILQGQNHTLCLPGLSKMEPQTPDISLAMLSASIMYACVLFACNEASYLAEVFGPLWIVKVYSYEFQKPSLCFCCPETVEADKGQRGGAARPADQETPPAPPVQVQHLSYNYSAFHFVFFLASLYVMVTLTNWFSYEGAELEKTFIKGSWATFWVKVASCWACVLLYLGLLLAPLCWPPTQKPQPLILRRRRHRIISPDNKYPPV", "text": "FUNCTION: Incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TDE1 family."}
+{"protein": "MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSGGGRGSSRRLDCKVIRLAECVSVAPVTVETPPEPGATAFRLDTAQRSHLLAADAPSSAAWVQTLCRNAFPKGSWTLAPTDNPPKLSALEMLENSLYSPTWEGSQFWVTVQRTEAAERCGLHGSYVLRVEAERLTLLTVGAQSQILEPLLSWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTAQGNDIFQAVETAIHRQKAQGKAGQGHDVLRADSHEGEVAEGKLPSPPGPQELLDSPPALYAEPLDSLRIAPCPSQDSLYSDPLDSTSAQAGEGVQRKKPLYWDLYEHAQQQLLKAKLTDPKEDPIYDEPEGLAPVPPQGLYDLPREPKDAWWCQARVKEEGYELPYNPATDDYAVPPPRSTKPLLAPKPQGPAFPEPGTATGSGIKSHNSALYSQVQKSGASGSWDCGLSRVGTDKTGVKSEGST", "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. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, perinuclear region. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. SIMILARITY: Belongs to the DOK family. Type A subfamily."}
+{"protein": "RDAQAEVQMTNAGVQLAGGSALCRHRPQQSIKRLVIRGRGIQLNDESVSSSLGLRPDGVFQIAGCGRSSFTPRQAVLTLESSSSQPRSGGIGTLQFVEEFTPSVYFNPFSGSPGQYPDEFIPNFDAISESVDGYD", "text": "SIMILARITY: Belongs to the adenoviridae pVIII family."}
+{"protein": "MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGILQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLLQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIYQWCGSKSNRFERLKATQVSKGIRDNERSGRAQVSVFEEGAEPEAMLQVLGPKPTLPEATEDTVKEDAANRKLAKLYKVSNGAGPMVVSLVADENPFAQGALRSEDCFILDHGKDGKIFVWKGKQANMEERKAALKTASDFISKMDYPKQTQVSVLPEGGETPLFRQFFKNWRDPDQTEGLGLAYLSSHIAHVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRVEGSNKVPVDPATYGQFYGGDSYIILYNYRHGSRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIVYKGGTSREGGQTAPASTRLFQVRASSSGATRAVEIIPKAGALNSNDAFVLKTPSAAYLWVGAGASEAEKTGAQELLRVLRAQPVQVAEGSEPDSFWEALGGKATYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGEFMQEDLATDDVMLLDTWDQVFVWVGKDSQDEEKTEALTSAKRYIDTDPAHRDRRTPITVVKQGFEPPSFVGWFLGWDDSYWSVDPLDRALAELAA", "text": "FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (By similarity). Plays a role in ciliogenesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the villin/gelsolin family."}
+{"protein": "MTQFSALALLLIVFVAASFAQSYDDVSAEKRAMRNALVRFGRASGGMRNALVRFGKRSPLDEEDFAPESPLQGKRNGAPQPFVRFGRSGQLDHMHDLLSTLQKLKFANNK", "text": "FUNCTION: [NGAPQPFVRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. FUNCTION: [AMRNALVRF-amide]: Potent inhibitor of the activity of the dissected pharyngeal myogenic muscle system (PubMed:16187307). Acts as a ligand for the npr-22 receptor in vitro (PubMed:16377032). FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. FUNCTION: [ASGGMRNALVRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
+{"protein": "MSIVGLVSVVCPSGGIKKRYFSKGLDNFQGFRSSECLGIQLQVPVPFYSGIRQSPRATSLQVVCKDCPRPELEGAVNFLEAAQLSASFRSSPRPEKGLEVVVVGAGLAGLSTAKYLADAGHKPILLESRDVLGGKIAAWKDKDGDWYETGLHIFFGAYPNVQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPEVLPAPLNGIWAILRNNEMLTWPEKVRFAIGLLPAMVGGQAYVEAQDGLTVTEWMRRQGVPDRVNDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVDHIQSLGGRAQLNSRLQKIELNPDGTVKHFVLGNGNIITGDAYVVAAPVDILKLLLPQEWREIPYFQKLDKLVGVPVINVHIWFDRKLKNTYDHLLFTRSPLLSVYADMSVTCKEYYDPNRSMLELVFAPAEEWISRSDSEIIERTMKELAKLFPDEIAADQSKAKILKYHVVKTPRSVYKTIPDCEPCRPLQRSPIEGFYLAGDYTNQKYLASMEGAVLSGKLCAQSIVQDYELLVRRSKKASTAEMTVV", "text": "FUNCTION: 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 with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis. SUBCELLULAR LOCATION: Plastid, chloroplast Plastid, chromoplast Membrane; Peripheral membrane protein Note=Exists as an inactive soluble form and an active membrane-bound form. SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family."}
+{"protein": "MALPFRKDLEKYKDLDEDELLGNLSETELKQLETVLDDLDPENALLPAGFRQKNQTSKSTTGPFDREHLLSYLEKEALEHKDREDYVPYTGEKKGKIFIPKQKPVQTFTEEKVSLDPELEEALTSASDTELCDLAAILGMHNLITNTKFCNIMGSSNGVDQEHFSNVVKGEKILPVFDEPPNPTNVEESLKRTKENDAHLVEVNLNNIKNIPIPTLKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDNQRQQLGTAVELEMAKMLEENTNILKFGYQFTQQGPRTRAANAITKNNDLVRKRRVEGDHQ", "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": "MVVVSDSRVRMPRYGGVSVKRKTLNVRVTTMDAELEFAIQSTTTGKQLFDQVVKTIGLREVWFFGLQYTDSKGDSTWIKLYKKVMNQDVKKENPLQFRFRAKFYPEDVAEELIQDITLRLFYLQVKNAILTDEIYCPPETSVLLASYAVQARHGDHNKTTHTAGFLANDRLLPQRVIDQHKMSKDEWEQSIMTWWQEHRSMLREDAMMEYLKIAQDLEMYGVNYFEIRNKKGTDLWLGVDALGLNIYEQDDRLTPKIGFPWSEIRNISFSEKKFIIKPIDKKAPDFMFFAPRVRINKRILALCMGNHELYMRRRKPDTIDVQQMKAQAREEKNAKQQEREKLQLALAARERAEKKQQEYEDRLKQMQEEMERSQRDLLEAQEMIRRLEEQLKQLQAAKDELELRQKELQSMLQRLEEAKNMEAVEKIKLEEEIMAKQMEVQRIQDEVNAKDEETKRLQDEVEEARRKQAEAAAALLAASTTPQHHHVAEDENENEEELTNGDAGGDVSRDLDTDEHIKDPIEDRRTLAERNERLHDQLKALKQDLAQSRDETKETANDKIHRENVRQGRDKYKTLREIRKGNTKRRVDQFENM", "text": "FUNCTION: Involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Cell junction, adherens junction Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton."}
+{"protein": "MSETINTAAQFPSFEKPTVQFNEKGWGPCELPDTFKDVPYQPFSKNDRLGKICDWTSTSNNDKKYQNKYASTFGTGNQYAYYHEEDETTFHLVDTARVQKPPHQRGRFRNMRNSRSGRGRNARGGLNTHGHGMTTLNSKNVKARDPRRGVGKRFGNRGPPPKMRESSVAVRADWASIEEMDFPRLMKLSLPNIKEGEDITTCGTLEYYDKTYDRINVKNEKPLQKIDRIVHTVTTTDDPVIRRLSKTIGNVFATDAILATIMCSTRSNYSWDIVIEKVGEKIFMDKRDHTEFDLLTVNETSVEPPTDDDSSCNSPRNLAIEATFINHNFSQQVLKTGDQEAKYKFEEPNPFISEDEDIQVASVGYRYKKWELGSDIVLVARCEHDGVLQTPSGEPQFLSIKALNEWDSKLANGVEWRQKLDTQRGAVLANELRNNACKLAKWTVQAVLAGSDQLKLGYVSRINPRDHSRHVILGTQQFKPHEFATQINLSMDNAWGILRCIIDLVMKQKDGKYLIMKDPNKPIIRLYDIPDNTFDSDDSDDGEGDDGEGFQQVYNYANNSNKI", "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": "MADGNTPHVAIIPSPGIGHLIPLVELAKRLLDNHGFTVTFIIPGDSPPSKAQRSVLNSLPSSIASVFLPPADLSDVPSTARIETRISLTVTRSNPALRELFGSLSAEKRLPAVLVVDLFGTDAFDVAAEFHVSPYIFYASNANVLTFLLHLPKLDETVSCEFRELTEPVIIPGCVPITGKDFVDPCQDRKDESYKWLLHNVKRFKEAEGILVNSFVDLEPNTIKIVQEPAPDKPPVYLIGPLVNSGSHDADVNDEYKCLNWLDNQPFGSVLYVSFGSGGTLTFEQFIELALGLAESGKRFLWVIRSPSGIASSSYFNPQSRNDPFSFLPQGFLDRTKEKGLVVGSWAPQAQILTHTSIGGFLTHCGWNSSLESIVNGVPLIAWPLYAEQKMNALLLVDVGAALRARLGEDGVVGREEVARVVKGLIEGEEGNAVRKKMKELKEGSVRVLRDDGFSTKSLNEVSLKWKAHQRKIDQEQESFL", "text": "FUNCTION: Possesses low quercetin 3-O-glucosyltransferase activity in vitro. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MGFPIPDPYVWDPSFRTFYSIIDDEHKTLFNGIFHLAIDDNADNLGELRRCTGKHFLNEQVLMQASQYQFYDEHKKEHETFIHALDNWKGDVKWAKSWLVNHIKTIDFKYKGKI", "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. SIMILARITY: Belongs to the hemerythrin family."}
+{"protein": "MLLLALLAFLLVSRTIARPSYSMVDDTTPEPEEPPAKYQISKADVFPVLPGEPLDLRCPLADGPLVTWTKDGAKLEVNNRTLIVRTYLQIKESTTRDSGLYACSVLKNSHFFHVNVTEASSSGDDEDDNDGSEDFTNDNNNIRAPYWTNTEKMEKKLHAVSAANTVKLRCPAREPHPSNEWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGIYTCIVENEHGSINHTYHLDVIERSSHRPILQAGLPANTTAVVGGDAEFVCKVYSDAQPHIRWVRYIEKNGSRFGVDGLPYFKVLKAAGVNVTDEEIEVLYVRNVSFEDAGEYTCIAGNSIGISQHSAWLTVHPAPVNPLEDNPVPYYMEIGIYSTGIFIIFCMVVVCVVCRMRQGAKKKKNFTGPPVHKLTKRIPLHRQVTVSADSSSSMNSTTPLVRITTRLLNSTDAMPLANVSEYELPHDPMWEFSRDKLTLGKPLGEGCFGQVVMAEALGIDKERPKESVTVAVKMLKDNATEKDLADLVSEMEMMKMIGKHKNIINLLGACTQGGTLYVIVEYAAKGNLRQYLRARRPLEMEYSFDVTRVPDEQMTFKDLVSCTYQIARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDVNNIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAIPSHRPTFKQLVEDLDRILTLTTNEEYLDLSAPLEQYSPSFPDSSCSASSSSGDDSVFSPDPMPHDPCLPKFQHVNGVVKT", "text": "FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus Cytoplasmic vesicle Note=Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily."}
+{"protein": "MDINASRALANVYDLPDDFFPKIDDLVRDAKDALEPYWKSDSIKKHVLIATHFVDLIEDFWQTTQGMHEIAESLRAVIPPTTAPVPTGYLIQHEEAEEIPLGDLFKHQEERIVSFQPDYPITARIHAHLKAYAKINEESLDRARRLLWWHYNCLLWGEANVTNYISRLRTWLSTPEKYRGRDAPTIEAITRPIQVAQGGRKTSSGTRKPRGLEPRRRKVKTTVVYGRRRSKSRERRAPSPQRAGSPLPRSSSSHHRSPSPRK", "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": "MSNAQPHFAPSHLQNGTPNSVHSGVNRPTTEHWAEQRTRSADSTKRRTRKSATGQQHSEPRTARTTSRGQYVDFGGQNLKVITPTLFINYSFLTKLYLNANKLTYLHQAIGQLRNLTHLDLSLNNLHSLPPEIGMLVNLKQLLVFDNQLTDLPEELGSLYQLELLGIEGNPIPDDIKQIMMEQGTVELIKHFRETAAGPEAPPERDWIVLDEITDPAQETVTALSYNILCDKYCTQSQYGYTPSSALAWETRRELILGELKQRNADIVCLQEIDQDSFNEYFREKLAHYDYKGVFWPKSRARTMAEREAKLVDGCAIFYKNSKYVLLDKQLIDFANTAINRPDMKGEHDIFNRVMPRDDIGVVAFLENRATGSRFIVGNVHVFWNPAFTDVKLVQVAILMEGISKFATKWSKFPPCKDKVVYRFTNGDDEDGKEADTTQEPGPSKEYGAGADIPVILCGDFNSMPSSGVYDLITQGTIAHSHQDLGSRKYGNFTRDGISHPFSLKSSYSAIGEMTFTNYVPHFQGVLDYIWYSTNTLQVVGLLGDIDKEYLRRVPGFPNYHFPSDHVALYAQYIVKGRKEKKVSEVDFGPSRDRERR", "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": "MRFLDGHTPAYDLTYNDVFVVPGRSDVASRFDVDLSTVDGSGTTIPVVVANMTAVAGRRMAETVARRGGIVVLPQDLPITAVSETVDFVKSRDLVVDTPVTLSPEDSVSDANALLHKRAHGAAVVVFEGRPIGLVTEANCAGVDRFARVRDIALSDFVTAPVGTDPREVFDLLEHAPIDVAVMTAPDGTLAGVLTRTGAIRAGIYTPAVDAKGRLRIAAAVGINGDVGAKAQALAEAGADLLVIDTAHGHQAKMLDAIKAVASLDLGLPLVAGNVVSAEGTRDLIEAGASIVKVGVGPGAMCTTRMMTGVGRPQFSAVVECAAAARQLGGHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLLFDRDDRPYKESYGMASKRAVAARTAGDSSFDRARKGLFEEGISTSRMSLDPARGGVEDLLDHITSGVRSTCTYVGAANLPELHEKVVLGVQSAAGFAEGHPLPAGW", "text": "FUNCTION: Involved in the purine-salvage pathway (PubMed:35338694). Catalyzes the NADPH-dependent conversion of GMP to IMP (PubMed:35338694). Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP (PubMed:35338694). SIMILARITY: Belongs to the IMPDH/GMPR family. GuaB1 subfamily."}
+{"protein": "MSLLSDLVNLNLTDATGKIIAEYIWIGGSGMDIRSKARTLPGPVTDPSKLPKWNYDGSSTGQAAGEDSEVILYPQAIFKDPFRKGNNILVMCDAYTPAGDPIPTNKRHNAAKIFSHPDVAKEEPWYGIEQEYTLMQKDVNWPIGWPVGGYPGPQGPYYCGVGADKAIGRDIVDAHYKACLYAGIGISGINGEVMPGQWEFQVGPVEGISSGDQVWVARYLLERITEISGVIVSFDPKPVPGDWNGAGAHCNYSTKTMRNDGGLEVIKKAIGKLQLKHKEHIAAYGEGNERRLTGKHETADINTFSWGVANRGASVRVGRDTEKEGKGYFEDRRPASNMDPYVVTSMIAETTILG", "text": "FUNCTION: Low-affinity glutamine synthetase (PubMed:14757761). May contribute to the homeostatic control of glutamine synthesis in roots. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family."}
+{"protein": "MKLFKNLTVQVITAVIIGVIVGLVWPDVGKEMKPLGDTFINAVKMVIAPIIFFTIVLGIAKMGDMKKVGKVGGKAFIYFEVVTTLALIIGLFVVNIMKPGAGLDYSKLEKGDVSQYTQNGGQGIDWIEFITHIVPSNMVDAFAKGDILQVLFFSILFGVGLAALGEKGKSVIDFFDKVSHVFFKIIGYIMRAAPIGAFGAMAYTIGHFGLDSIKPLASLMMSVYITMFLFVFVALNIICKLYGFSLWNYLRFIKDELLIVLGTSSSESVLPRMMDKMERYGCSKSVVGLVIPTGYSFNLDGTSIYLSMATVFLAQVFGVDLSIGQQITIILVLMLTSKGAAGVTGSGFIVLASTLSALQVIPLEGLALLLGVDRFMSEGRAIVNLIGNGIATIIVAKSENEFDEAKSIEAVEGMKKMKTAV", "text": "FUNCTION: Responsible for the transport of succinate and fumarate, but not malate, across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family."}
+{"protein": "MQDNALTIALSKGRIFEETLPLLAAAGIVPTEEPEKSRKLIIGTNHENIRLVIVRATDVPTYVRYGAADFGIAGKDVLIEHGGTGLYRPLDLEIAKCRMMVAVRKGFDYEAASQPGCRLKIATKYPEIAASHFAGKGVHVDIIKLYGSMELAPLVGLSDAIVDLVSTGNTLKANGLEAVEHIVDISSRLVVNKAALKTKYALLEPIIQAFGGAVKAK", "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. Short subfamily. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short subfamily."}
+{"protein": "MIKLLVLWLLILTIFLKSPTVEGDVSFRLSGATTTSYGVFIKNLREALPYERKVYNIPLLRSSISGSGRYTLLHLTNYADETISVAVDVTNVYIMGYLAGDVSYFFNEASATEAAKFVFKDAKKKVTLPYSGNYERLQTAAGKIRENIPLGLPALDSAITTLYYYTASSAASALLVLIQSTAESARYKFIEQQIGKRVDKTFLPSLATISLENNWSALSKQIQIASTNNGQFESPVVLIDGNNQRVSITNASARVVTSNIALLLNRNNIAAIGEDISMTLIGFEHGLYGI", "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": "MMTMWCLTLFVLWMLRVVGMHVLRYGYTGIFDDTSHMTLTVVGIFDGQHFFTYHVNSSDKASSRANGTISWMANVSAAYPTYLDGERAKGDLIFNQTEQNLLELEIALGYRSQSVLTWTHECNTTENGSFVAGYEGFGWDGETLMELKDNLTLWTGPNYEISWLKQNKTYIDGKIKNISEGDTTIQRNYLKGNCTQWSVIYSGFQTPVTHPVVKGGVRNQNDNRAEAFCTSYGFFPGEINITFIHYGNKAPDDSEPQCNPLLPTFDGTFHQGCYVAIFCNQNYTCRVTHGNWTVEIPISVTSPDDSSSGEVPDHPTANKRYNTMTISSVLLALLLCALLFAFLHYFTTLKQYLRNLAFAWRYRKVRSS", "text": "FUNCTION: Plays a role in the protection against host NK cell cytotoxicity by interacting with and modulating the activity of the host inhibitory leukocyte Ig-like receptor 1/LILRB1, which is expressed on monocytes, dendritic cells, as well as subsets of T and NK cells. UL18 exerts an inhibitory effect on LIR-1+ NK cells, while it stimulates LIR-1- NK cell (By similarity). SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein."}
+{"protein": "MASGQQERSELDRMAREGETVVPGGTGGKTLEAQEHLAEGRSRGGQTRKEQLGEEGYREMGHKGGETRKEQLGEEGYREMGHKGGETRKEQLGEEGYREMGHKGGETRKEQMGEEGYREMGRKGGLSTMNESGGERAAREGIDIDESKFKTKS", "text": "FUNCTION: Lea proteins are late embryonic proteins abundant in higher plant seed embryos. SIMILARITY: Belongs to the small hydrophilic plant seed protein family."}
+{"protein": "MKVLFAKTFVKDLKHVPGHIRKRIKLIIEECQNSNSLNDLKLDIKKIKGYHNYYRIRVGNYRIGIEVNGDTIIFRRVLHRKSIYDYFP", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity (By similarity). Is very toxic upon expression in E.coli. Its toxic activity is probably neutralized by the cognate antitoxin RelB3. SIMILARITY: Belongs to the RelE toxin family."}
+{"protein": "MAVALILLLIAIGSVLFHLFSPWWWTPIATNWGYIDDTINITFWITGFVFTAVILFMAYCVFRFHHKEGRQAAYNPENKKLEWWLSVGTGVGVAAMLAPGLVVWHQFVTVPADATEVEIMGQQWQWSFRLPGKDGRLGTSDVRNISPENPMGLNRDDPHGQDDVVIENGDLHLPIGKPVKVLLRSVDVLHDFYVPEFRAKMDMVPGMVTYFWIRPIRTGTFDVLCAELCGAAHYQMRAKVIVEAESDYHAWLEQQKTFAGLSGRNAVVRAKYNSGDD", "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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
+{"protein": "MLKNINPTQTQAWKALTAHFESAQDMDLKALFAQDSERFAKYSARFGQDILVDYSKNLVNAETMQHLFALAKETDLQSAITAMFKGEAINQTEDRAVLHTALRNRSNSPVLVNGEDVMPAVNAVLAKMKAFSERVIGGEWKGFTGKAITDVVNIGIGGSDLGPYMVTEALVPYKNHLTMHFVSNVDGTHMAETLKNVDPETTLFLVASKTFTTQETMTNAHTARDWFLKAAGDEAHVAKHFAALSTNGKAVAEFGIDTDNMFEFWDWVGGRYSLWSAIGLSIILSIGYDNFVELLAGAHEMDQHFVNTPFESNIPVILALIGIWYNNFHGAESEAILPYDQYLHRFAAYFQQGNMESNGKYVDRNGNPVTYQTGPIIWGEPGTNGQHAFYQLIHQGTKLIPCDFIAPAVSHNLVGDHHQKLMSNFFAQTEALAFGKSAQAVQAELEKAGKSAAEIAALVPFKVFEGNRPTNSILVKQITPRTLGNLIAMYEHKIFVQGVIWNIFSFDQWGVELGKQLANQILPELADSAAVTSHDSSTNGLINAFKAFRA", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family. SIMILARITY: Belongs to the GPI family."}
+{"protein": "MESGHRFDAQTLHSFIQAVFRQMGSEEQEAKLVADHLIAANLAGHDSHGIGMIPSYVRSWSQGHLQINHHAKTVKEAGAAVTLDGDRAFGQVAAHEAMALGIEKAHQHGIAAVALHNSHHIGRIGYWAEQCAAAGFVSIHFVSVVGIPMVAPFHGRDSRFGTNPFCVVFPRKDNFPLLLDYATSAIAFGKTRVAWHKGVPVPPGCLIDVNGVPTTNPAVMQESPLGSLLTFAEHKGYALAAMCEILGGALSGGKTTHQETLQTSPDAILNCMTTIIINPELFGAPDCNAQTEAFAEWVKASPHDDDKPILLPGEWEVNTRRERQKQGIPLDAGSWQAICDAARQIGMPEETLQAFCQQLAS", "text": "FUNCTION: Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family."}
+{"protein": "MPNRRARKKRRTEDFSSSSASENDSDSESVTSVQEEQPDAPETYTIDGLDTQEVSDSTQVRLQQLNADRLASIEQSLSGNLKLDINAVRQIDDVREQLQNEYLKKLLVTYSEDLDALRQKTDFKENSLKTLARLLKESGNIFDDGTLKSLVE", "text": "FUNCTION: Required for efficient biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RSA3 family."}
+{"protein": "MNNPYENWINFFQEALNTNIPSIEKIEELVYLGIGGSGIPGRILEILELPVKYQLFRGYKVKVNEKSTVIAVSYSGNTTETIFALLTSLKKTRKAIVITSGGKIEEIASKHNLPVIKLPKGLQTRFVFPYIFTYLIRIINEGLGTNYNVNELVEGIKDYSKLNEISGILASQIIGKIPIIYSSTFLPIAERFKQEINENAKYPAFYNELPEANHNEIELYSYPSPYTFYPIVIVSDKLDEESANLINAYKIYPLYQSILKNIASLTLLAGLTSVKLAMLLGVKPEQLNIIPKIREKTFKLFEGDINADQNL", "text": "FUNCTION: Involved in the synthesis of UDP-N-acetylgalactosamine (UDP- GalNAc). Catalyzes the conversion of glucosamine-6-phosphate (GlcN-6-P) to galactosamine-6-phosphate (GalN-6-P). SIMILARITY: Belongs to the PGI/PMI family."}
+{"protein": "MRVLVLGAGQLARMMSLAGAPLNIETIAFDVGSENIVHPLTQTVLGHGLEQAIEQVDVITAEFEHIPHPILDLCARSGKLYPSAEAIKAGGDRRLEKALLDRAQVANARYTMIRSRDDLTSAIAEIGLPMVLKSALGGYDGKGQWRLKEPTQIESVWQELAQYLAANPEQAIVAEEFVAFDREVSLVGARNLVGDVVVYPLAENVHTQGVLSLSTAIDAPALQTQAKAMFKAVAEQLNYVGVLALEFFEVQGQLLVNEIAPRVHNSGHWTQQGAETCQFENHLRAVCGLPLGSTKLVRETAMINILGEDQLPAEVLALEGCHVHWYGKAKRSGRKMGHINVTADYSGELQRKLCQLATVLDEKAFPAVHAVAKEIQP", "text": "FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). SIMILARITY: Belongs to the PurK/PurT family."}
+{"protein": "MKLKRILLSVALLCGIGTTAMADKGMWLLNELNQQNYERMKELGFKLSPEQLYSLGQPSVASAVVIFGGGCTGITVSNEGLIFTNHHCGFGAIQSQSTVDHDYLRDGFRSNNHVEELPIPGLSVRYLREIVDVTPRIEAAVKGAKSEMERMQIIEELSQKINAEYTKGSTVVGEVTPYYAGNKYYVVVYNVFQDVRLVMAPPSSVGKFGGDTDNWMWTRHTGDFSVFRVYADANNNPALYSQNNKPYKPISYAPVSLNGYREGDYAMTIGFPGSTNRYLTSWGVEDVVNNENSPRIEVRGIKQAIWKEAMEADQATRIKYASKYAQSSNYWKNSIGMNRGLKNLDVVNRKRAEEKAFEAWIAKNNSQSTYGHILPGLKADYAKSAAISKDINYLYETLWGGTEIVRLARDVNSVGRIQAADMPKYKGRLEELYKDYLPSLDVKVLPAMLDIVRQRVSADCQPDIFKFIDKKFKGSTEKYAQYVFEKSIVPYADKVKDFLNLPADKQKKILDKDPAVALFNSVLPAIMQAQDKSEEMMLNIEKGKREYFAASRIMDPNRQMPSDANFTMRMSYGSIKGYAPKDGAWYNYYTTEQGVFEKQDPTSSEFAVQPEILSLLRSKDFGQYGVGDHLRLCFLSDNDITGGNSGSPVFNGNGELIGLAFDGNWEAMSGDIEFEPDLQRTISVDIRYVLFMIDKWAKMPHLIKELNLVKGDQRDLMPAGKGGNCSHKKAQTCAKKECSKGKKCAEKSATCISAMKDGKPCKTEKACAAGQKSAEKKANCCSTMKDGKPCTGDKDCAKSGKACCGKNKEAAAKKASKK", "text": "FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Most efficiently cleaves the synthetic substrate Met- Leu-methylcoumaryl-7-amide (Met-Leu-MCA), and slowly hydrolyzes Leu- Gln-, Lys-Ala-, Leu-Arg, and Ala-Asn-MCA. Is likely involved in amino acid metabolism and bacterial growth/survival of asaccharolytic P.endodontalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources. SIMILARITY: Belongs to the peptidase S46 family."}
+{"protein": "MDSDTLSGLLENVAKKFPDRRALSVSGKFNLTHARLHDLIERAASRLVSDAGIKPGDVVALTFPNTVEFVIMFLAVIRARATAAPLNAAYTAEEFEFYLSDSDSKLLLTSKEGNAPAQEAASKLKISHVTATLLDAGSDLVLSVADSDSVVDSATELVNHPDDGALFLHTSGTTSRPKGVPLTQLNLASSVKNIKAVYKLTESDSTVIVLPLFHVHGLLAGLLSSLGAGAAVTLPAAGRFSATTFWPDMKKYNATWYTAVPTIHQIILDRHASHPETEYPKLRFIRSCSASLAPVILSRLEEAFGAPVLEAYAMTEATHLMSSNPLPEEGPHKPGSVGKPVGQEMAILNEKGEIQEPNNKGEVCIRGPNVTKGYKNNPEANKAGFEFGWFHTGDIGYFDTDGYLHLVGRIKELINRGGEKISPIEVDAVLLTHPDVSQGVAFGVPDEKYGEEINCAVIPREGTTVTEEDIKAFCKKNLAAFKVPKRVFITDNLPKTASGKIQRRIVAQHFLEKP", "text": "FUNCTION: Oxalyl-CoA synthetase acting exclusively against oxalate (PubMed:22447686, PubMed:27326693). Follows a two-step reaction mechanism, wherein oxalate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield oxalyl-CoA (By similarity). No activity with malonate, succinate, malate, acetate, formate, lactate, glycolate, glyoxylate or glutarate (PubMed:22447686). Required for oxalate degradation, normal seed development and defense against oxalate-producing fungal pathogens (PubMed:22447686). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MTIAKSVLLFILAAVAEIGGAWLVWQAVREGRAWWWAGLGIIALGLYGFVATLQPDAHFGRILAAYGGVFVAGSLVWGMVFDGFRPDRWDVIGSVICLVGVAVIMFAPRGTTS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0060 family."}
+{"protein": "MRFLAATFLLLALSTAAQAEPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVTFTSNIQSKSSKAVVHGILMGVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYPSIKLVVEWQLQDDKNQSLFCWEIPVQIVSHL", "text": "FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment. Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. May bind and mobilize cholesterol that is associated with membranes. NPC2 binds cholesterol with a 1:1 stoichiometry. Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (By similarity). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport (By similarity). FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment (PubMed:17018531, PubMed:11125141, PubMed:18772377, PubMed:29580834, PubMed:15937921). Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1 (PubMed:17018531, PubMed:18772377, PubMed:27238017). May bind and mobilize cholesterol that is associated with membranes (PubMed:18823126). NPC2 binds cholesterol with a 1:1 stoichiometry (PubMed:17018531). Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (PubMed:17018531). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport (By similarity). SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum Lysosome Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum Lysosome Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum Lysosome Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. SIMILARITY: Belongs to the NPC2 family."}
+{"protein": "MSNLRLLISDSYDPWFNLAVEECIFREMTTQKILFLWRNAETVVIGQSQNPWKECNTRRMEQDGIRLARRSSGGGAVFHDLGNSCFTFMAGKPGYDKTVSTGIILQALAQLGITATASGRNDLVIDTAEGVRKISGSAYRETQDRGFHHGTLLLNADLNRLADYLNPDPKKLQAKGITSVRSRVANLAEFKADISHHQVCDAITQAFFDHYGEMAKAEIISPDVYPDLPDFAAQFAKQSSWQWNFGKAPAFSHLLNERFVWGGVDIFFDVEKGAICRAQIFTDSLSPAPLQRLAEMLVGCTYRSEALANCCDALIVQYPEQAAELTELRQWLLETIK", "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": "MSTQYIDETAFVQAEQGKTNLMFSDEKQQARFELGVSMVIYKWDALDVAVENSWGGPDSAEKRDWITGIVVDLFKNEKVVDAALIEETLLYAMIDEFETNVEDDSALPIAVEVINIYNDCFNLNYNKVEKLYLEWQEKQRTKKSKRVVHIEGDDDEDDEDVEDYDDEDEDEEMDEVVPDLVSSKPEPIVDEDGFELVQPKGRRKH", "text": "FUNCTION: Required for 20S pre-rRNA processing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TSR2 family."}
+{"protein": "MLTDPIADMLTRIRNATRVYKESTDVPASRFKEEILRILAREGFIKGYERVDVDGKPYLRVYLKYGPRRQGPDPRPEQVIHHIRRISKPGRRVYVGVKEIPRVRRGLGIAILSTSKGVLTDREARKLGVGGELICEVW", "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. 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 central domain. 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 uS8 family."}
+{"protein": "MKNKYYPLRSSMDEMSAKNDNEIDLEKGPLPEYNSEDGSTLPPYSDLNNPKQMGQNITKLFNWNKSTTPPDYDENRLHITDEGNNPPNTHRENHSSGTADNSSPFLIKLLISFTPIVLLNAPAVCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWTKAVKVTVIFLAQCVKVTVIFLAKCVKVTVIFLAKCVKVTAISLAKCIKVTAIFLAQCVKVTAVGLYNSREKWVVIIWLLWVVICYTLFLRSKFGNLNLNKALICSTCSISAALLLFLLYVRLPFWTLKHMFSGLFQVLGVQSCVVIVTKGLTYLFDKHIDATGYEIEASSLFVIGNFLFFYEMECPGALKRMPKFIRNGIASFLEGIGNIGNAIGRIGNAIGRIGNAFRGANDNNDIPLGEMEVESEV", "text": "FUNCTION: [Isoform 2]: Forms toxic aggregates that disrupt spore maturation. FUNCTION: [Isoform 1]: Localizes isoform 2 to the vacuole thereby facilitating its degradation. 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. 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": "MTVITIAKRGLPKLTTSTSSTTTASSSSTITSVASSSSSLPLLSNSTSSSIIPSITPPSRNGNPYILDSGDMPNGTVFIVVGGIAGVIFLAILLWWVITTYSSHRLTRSVQDYESKMFSTQHTQFYGDSPYMDYPAKENFQDQVHISESDISPGNKDESVKDALVSHTNNEKPFLSNFERPLFSLASESNRNSLFISPTGDILYKTRLSKLYQESPRLLQKPVIMTSDNVSTNSLVSTISSSSASSLDNGNEKEVGEDIRKPAKIASSPSRKLLNSPESDGSVNRNHSKGNLLVVQSKRKPTPSTYLEHMLEGKEQDE", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PRM5 family."}
+{"protein": "MDATVILPILKKKLAFLSGGKDRRSGLILTIPLCSDQTSMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQWNVVKTVVLMLQNVVPAEVSLVCVVKPDEFWDKKVTHFCFWKEKDRLGFEVILVSGNKLTRYIEPNQLTEEFGGSLTYDHMDWLNKRLVFEKFTKESTSLLDELAVINNGSDKGSQNEKERSVDFNYLPSVDPETVLQTGHELLSELQQRRFNGSDGGVSWSPMDDELLAQPQVMKLLDSLREQYTRYQEVCRQRSKRTQLDEIQQKVMQVVSWLEGPGSEQLRTQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLVELKTLQQRLSDVCYRQASQLEFRQNLLQIALEFHSVSQDLSQQLDGLLGMLCADVAPTDGATIQQTLKLLEEKLKSVDTGLQGLREKGQGLLDQITNQASWAYGKDVSTENKDNVDHIQGVMEDMQLRKQRCEDMVDVRRLKMLQMVQLFKCEEDAAQAVDWLNELLDALLKTHIRLGDDSQETKILLEKHRKFVDVAQSTYDYGRQLLQATVVLCQSLRCTSRSSGDTLPKLNRVWKQFTITSEERVQRLEMALAFHSNAEKILQECPDLGETVMDFEQFDEVEAVGKSLLDRLTVPD", "text": "FUNCTION: May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels trpc4 and trpc5. Binds phospholipids (By similarity). SIMILARITY: Belongs to the SOLO family."}
+{"protein": "MTSNRSNLLFSLVLFHFLFVPTQLQALNTDGVLLLTFKYSILTDPLSVLRNWNYDDATPCLWTGVTCTELGKPNTPDMFRVTSLVLPNKHLLGSITPDLFSIPYLRILDLSSNFFNGSLPDSVFNATELQSISLGSNNLSGDLPKSVNSVTNLQLLNLSANAFTGEIPLNISLLKNLTVVSLSKNTFSGDIPSGFEAAQILDLSSNLLNGSLPKDLGGKSLHYLNLSHNKVLGEISPNFAEKFPANATVDLSFNNLTGPIPSSLSLLNQKAESFSGNQELCGKPLKILCSIPSTLSNPPNISETTSPAIAVKPRSTAPINPLTEKPNQTGKSKLKPSTIAAITVADIVGLAFIGLLVLYVYQVRKRRRYPESSKFSFFKFCLEKNEAKKSKPSTTEVTVPESPEAKTTCGSCIILTGGRYDETSTSESDVENQQTVQAFTRTDGGQLKQSSQTQLVTVDGETRLDLDTLLKASAYILGTTGTGIVYKAVLENGTAFAVRRIETESCAAAKPKEFEREVRAIAKLRHPNLVRIRGFCWGDDEKLLISDYVPNGSLLCFFTATKASSSSSSSSSLQNPLTFEARLKIARGMARGLSYINEKKQVHGNIKPNNILLNAENEPIITDLGLDRLMTPARESHTTGPTSSSPYQPPEWSTSLKPNPKWDVYSFGVILLELLTSKVFSVDHDIDQFSNLSDSAAEENGRFLRLIDGAIRSDVARHEDAAMACFRLGIECVSSLPQKRPSMKELVQVLEKICVLV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily."}
+{"protein": "MDKFWWHAAWGLCLLPLSLAHEQIDLNITCRYAGVFHVEKNGRYSISRTEAADLCQAFNSTLPTMDQMVMALSKGFETCRYGFIEGHVVIPRIQPNAICAANHTGVYILTSNTSHYDTYCFNASAPLEEDCTSVTDLPNSFEGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNTTDDDVSSGSSSEKSTSGGYVFHTYLPTIHSTADQDDPYFIGSTMATRDQDSSMDPRGNSLTVTDGSKLTEHSSGNQDSGLNSTSRPGGKPRVPEWLIVLASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGKVEDRKPSELNGEASKSQEMVHLVNKEPSETPDQFMTADETRNLQNVDMKIGV", "text": "FUNCTION: Cell-surface receptor that plays a role in cell-cell interactions, as well as cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, microvillus Secreted Note=Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli."}
+{"protein": "HVVAAITALKERGGSSHQALKKYKAAN", "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": "MSGADRIPAAGAAPDSASGRAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLREEPGAFNWSMYSQYACLIEGKGESWQEKERQLRARVKRVLPIDVHQPQPLGTGSPAPLPADTLVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLMVVPVSEEEVREALVRSGYEVRDLRTYIMPAHLQTGVDDVKGIFFAWAQKVGL", "text": "FUNCTION: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor (PubMed:13863458). Other substrates include phenylethanolamine, octopamine and normetanephrine (PubMed:13863458). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family."}
+{"protein": "MSSGLSLERACAVALGIVASASLVAAGPCDIYSSGGTPCVAAHSTTRALYSAYTGALYQVKRGSDGSTTDIAPLSAGGVADAAIQDSFCANTTCLITIIYDQSGRGNHLTQAPPGGFNGPESNGYDNLASAVGAPVTLNGKKAYGVFMSPGTGYRNNAASGTATGDKAEGMYAVLDGTHYNSACCFDYGNAEVSNTDTGNGHMEAIYYGDNTVWGSGAGSGPWIMADLENGLFSGLSSTNNAGDPSISYRFVTAVVKGEANQWSIRGANAASGSLSTYYSGARPSASGYNPMSKEGAIILGIGGDNSNGAQGTFYEGVMTSGYPSDATENSVQADIVAAKYAIASLTSGPALTVGSSISLQVTTAGYTTRYLAHDGSTVNTQVVSSSSTTALRQQASWTVRTGLANSACLSFESVDTPGSYIRHYNFALLLNANDGTKQFYEDATFCPQAGLNGQGNSIRSWSYPTRYFRHYENVLYVASNGGVQTFDATTSFNDDVSWVVSTGFA", "text": "FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L- arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 54 family."}
+{"protein": "MFRMLSSSFEDDPFFSESILAHRENMRQMMRSFTEPFGRDLLSISDGRGRVHNRRGHNDGEDSLTHTDVSSLQTVDQMVSNMRNYMQKLERNFGQLSVDPNGHSFCSSSVMTYSKIGDEPPKVFQASTQTRRAPGGIKETRKAMRDSDSGLEKMAIGHHIHDRAHVIKKSKNKKTGDEEVNQEFINMNESDAHAFDEEWQSEVLKYKPGRHNLENTRMRSVGHENPGSRELKRREKPQQSPAIEHGRRSDVLGDKLHIKGSSVKSNKK", "text": "FUNCTION: Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Note=Shuttles between the cytoplasm and nucleus. SIMILARITY: Belongs to the MLF family."}
+{"protein": "MKWDEIGKNIAKEIEKEILPYFGRKDKSYVVGTSPSGDETEIFDKISEDIALKYLKSLNVNIVSEELGVIDNSSEWTVVIDPIDGSFNFINGIPFFAFCFGVFKNNEPYYGLTYEFLTKSFYEAYKGKGAYLNGRKIKVKDFNPNNIVISYYPSKKIDLEKLRNKVKRVRIFGAFGLEMCYVAKGTLDAVFDVRPKVRAVDIASSYIICKEAGALITDENGDELKFDLNATDRLNIIVANSKEMLDIILDLL", "text": "FUNCTION: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1- phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate. SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase class 4 family."}
+{"protein": "MGDYVPGFEQRESDNRSFGHSRLPTLGAIPIKNEKGQTVMQKVKVSRYVAGKAPEYARNYDSDSSESDRETDRDDDRRRRRRRESSDEEDRRRHRRHEDYGRRRQVEKPEVLGKVEDESSENEQESEEDEEKQEERRERARMRRLELHENNREKDEEQEDSAESDEEDFERRRQMLRDRAIKREEEIKREIKEELEEDDVEEEEEEESSEEEDSDEDDDPVPRLKPIFTRKKDRITLQEAEKEKEKEILKKIEDEKRAEERKRESAKLVEKVLQEEEAAEKRKTEDRVDLSSVLTDDETENMAYEAWKLREMKRLKRNRDEREEAAREKAELDKIHAMSEEERLKYLRLNPKVITNKQDKGKYKFLQKYFHRGAFFLDEEDEVLKRNFAEATNDDQFDKTILPKVMQVKNFGKASRTKYTHLTEEDTTDHQGVWASTNQLNSQFSTKRAGGSRPVFERPATKKRKN", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MFAP1 family."}
+{"protein": "MSSQRRNYRFILVVTLFVLASLAVSGRLVYLQVHDHEFLADQGDLRSIRDLPIPVTRGMITDRNGEPLAVSTEVASIWCNPREMAAHLDEVPRLAGALHRPAAALLAQLQANPNKRFLYLERGLSPIEASEVMALGITGVHQIKEYKRFYPSSELTAQLIGLVNIDGRGQEGTELGFNDWLSGKDGVREVAINPRGSLVNSIKVLKTPKASQDVALSIDLRLQFIAYKALEKAVLKFGAHSGSAVLVNPKSGQILAMANFPSYNPNNRASFAPAFMRNRTLTDTFEPGSVIKPFSMSAALASGKFDENSQVSVAPGWMTIDGHTIHDVARRDVLTMTGVLINSSNIGMSKVALQIGPKPILEQLGRVGFGAPLSLGFPGENPGYLPFHEKWSNIATASMSFGYSLAVNTAELAQAYSVFANDGKLVPLSLLRDNPQNQVRQAMDPQIARRIRAMLQTVVEDPKGVVRARVPGYHVAGKSGTARKASGRGYADKSYRSLFVGMAPASDPQLVLAVMIDSPTRIGYFGGLVSAPTFSDIMAGSLRALAIPPDNLQDSPAVADRQHHG", "text": "FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:9045804). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily."}
+{"protein": "MAQTVQNVTLSLTLPITCHICLGKVRQPVVCTNNHVFCSICIDLWLKNNSQCPACRVPITPENPCKEIIGGTSESEPMLSHTVRKHLRKTRLELLHREYEDEIDCLQKEVEELKSKNLSLESQIKTILDPLALMQGSQNEDKHPLADNPSKMDPDSVVEWKKKLRTANEIYEKVKDDVDKLKEANKKLKLENGGLLRENLRLKAEVDNRSPQKFGRFTVAALQSKVEQYERETNRLKKALERSDKYIEELESQVAHLKHSEEAKEDVDALCQRAPSADSKGPNGSDELGPPKNQSDSARKQAGSASASHLASPSSSRLADSGSVRQESTSRTEPNCPQNKDRYPKPTEPRLGARETPMDTYLEREWGSKPSDCAPYKEDELYGIPASCTPLSLSCLQLNTPENRENPVIKAGSSKKHANHLRKLVFDDFCDSPNACNNNSSEDDRRENEKKSDCFASSKTGFWDCCSTSYAQSLEFDGSEGNAIANSVGEIPSKLSEKSGSCLSKRLSCIRSLEMNRTRTSSEASMDAAYLDKISELDSMMSESDNSKSPCNNGFKSVEVEGPSKSPQGREFLEEPDKLQEGSKLNLSKPALTADGLESGGEWKPSSFFLLSPADHEMSEDFSLHSTSHSGTSEVKPPNCLFQTEFSQGALLSSSQGLFEDQRFGSSLFKISSEMQSLHSPLQSPWSAAFVPEKRSKNGNQSTKRKIQSSLANASPSKATKS", "text": "FUNCTION: E3 ubiquitin ligase essential for DNA replication origin activation during S phase. Acts as a replication origin selector which selects the origins to be fired and catalyzes the multi-mono- ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S- phase. SUBCELLULAR LOCATION: Chromosome Note=Association to chromatin is cell cycle-regulated, absent from mitotic chromosomes, is associated with chromatin from G1 and partially released from chromatin from mid S-phase."}
+{"protein": "METLNIFLVIFSLLGTIIIASSSDESSERKKRDLDTIDDTNNDFLTADKRRPGWGKRSFDDDILNNLDKRRPGWGKRSDMLFDSEEIEKRRPGWGKRSSSLYDDEKRKPGWGKRSSALLDDLSLYNSIVKRRPGWGKRSDTFKVDIRRPGWGKRTPGWGKRSGPNMCMDFQDEILQLYKLLNEAEKLHSECEALNI", "text": "FUNCTION: RPGW-amide, KPGW-amide and TPGW-amide tetrapeptides are involved in control of muscle contraction and may function as neurotransmitters. These peptides increase tension of the pedal retractor muscle and, in conjunction with FMRF-amide, increase peak tension of the anterior byssus retractor muscle (ABRM)."}
+{"protein": "MGGSSSKESPRGGGSGRRYERSVSGSSSYSSAWDQSSYYQTPNHPSASPVSSYNSGRQTPKNLERKYSRIADNYRSIDEVTAALSHAGLESSNLIVGIDVTKSNEWTGARSFGRKSLHFIGTTPNPYQQAISIIGKTLSVFDEDNLIPCYGFGDATTHDQDVFSFNPNDTYCNGFEEVLMCYREIVPQLRLSGPTSFAPIIERAMTIVEESGGQYHVLLIIADGQVTRSVDTDNGGFSPQEQQTIDAIVRASEYPLSIVLVGVGDGPWDTMRQFDDNIPARAFDNFQFVNFTDIMSKNIDPARKEAEFALSALMEIPSQYKATLELGLLGQRTGHCPDRIALPPPTYATQSMRNSPRTSRSTSFQNKPYDNGVSSTPPSTTHNESQQQFCPVCLVSAKNMAFNCGHQTCAGCGEDLHVCPICRSSISVRIKLY", "text": "FUNCTION: Together with RGLG1, mediates the ubiquitination and subsequent proteasomal degradation of the target protein PP2CA. Functions as positive regulator of abscisic acid (ABA) signaling through ABA-dependent degradation of PP2CA, a major inhibitor of ABA signaling. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
+{"protein": "MSKMKMLPVQLSLNSLNPGIWSDVLWRCPPAPSSQLAELKTQLPPSLPSDPRLWSREDVLVFLRFCVREFDLPKLDFDLFQMNGKALCLLTRADFGHRCPGAGDVLHNVLQMLIIESHMMQWHLPNSPVTPTSRYPLSPHSHPPTPTWPPLNAPPENSPFHSSAHSLAGHHFMAPNSVTLSPPPSVDSQASSPPQAPYQNGGATGAAPGSAGGSAPAAGGATNTSNPTSSSASSTGSNGSQPNIMPMKGISSASSNHSDSEEEYSETSGGVSKMPPAPLSYSTASPPGTPILKDIKPNWTQQLTNSFVNSWSQQQQQQQQQQAAAVAAVAAQAQQHQLQQQQQQQQLPQKLTLDNTAGPVVTPAGGSISAPTTPSYMYKAKREFFPENSEPNTNGRLLWDFLQQLLNDRNQKYSDLIAWKCRDTGVFKIVDPAGLAKLWGIQKNHLSMNYDKMSRALRYYYRVNILRKVQGERHCYQFLRNPTELKNIKNISLLRQSTPANGNGGSPSMPQGSSQAPGSPAGQNWNPQQQSQQQQQSPQRPASRNGPMSLPAVAAVAAAAAAAYGPPPTSPLFMHAINGAFHYLSAAAAGPPPNSPALNTPSAVGGPDKFQFHPLKLENGSGSGSESAGEDLKPTDLSVSSKSTATSNEDCYPLIRNADGLTTIKLIRYNEHQVAASPAGQSPKHDDQQAGASNASSSPRPMDQASEQAQPVPMESDCNGGESEDSFRHMQQ", "text": "FUNCTION: Ets-related protein that functions as a negative regulator of photoreceptor development acting antagonistically to pnt and the proneural signal mediated by RAS (PubMed:1505027, PubMed:1495974, PubMed:8033205). It acts upstream of SINA to inhibit R7 development (PubMed:1505027, PubMed:1495974). SUBCELLULAR LOCATION: Nucleus Note=In undifferentiated cells during the early stages of eye development. SIMILARITY: Belongs to the ETS family."}
+{"protein": "MAEPIPSSSLSPKSLQSPNPMEPSPASSTPLPSSSSQQQQLMTAPISNSVNSAASPAMTVTTTEGIVIQNNSQPNISSPNPTSSNPPIGAQIPSPSPLSHPSSSLDQQTQTQQLVQQTQQLPQQQQQIMQQISSSPIPQLSPQQQQILQQQHMTSQQIPMSSYQIAQSLQRSPSLSRLSQIQQQQQQQQHQGQYGNVLRQQAGLYGTMNFGGSGSVQQSQQNQQMVNPNMSRAALVGQSGHLPMLNGAAGAAQMNIQPQLLAASPRQKSGMVQGSQFHPGSSGQQLQGMQAMGMMGSLNLTSQMRGNPALYAQQRINPGQMRQQLSQQNALTSPQVQNLQRTSSLAFMNPQLSGLAQNGQAGMMQNSLSQQQWLKQMSGITSPNSFRLQPSQRQALLLQQQQQQLSSPQLHQSSMSLNQQQISQIIQQQQQQSQLGQSQMNQSHSQQQLQQMQQQLQQQPQQQMQQQQQQQQQMQINQQQPSPRMLSHAGQKSVSLTGSQPEATQSGTTTPGGSSSQGTEATNQLLGKRKIQDLVSQVDVHAKLDPDVEDLLLEVADDFIDSVTSFACSLAKHRKSSVLEPKDILLHLEKNLHLTIPGFSSEDKRQTKTVPTDLHKKRLAMVRALLESSKPETNASNSKETMRQAMVNPNGPNHLLRPSQSSEQLVSQTSGPHILQHMTRY", "text": "FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Required for the expression of a subset of ethylene- responsive genes (By similarity). Involved in the negative regulation of cytokinin sensitivity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF12 family."}
+{"protein": "LLTLAVLLMVSADMAFAGFGCPGDQYECNRHCRSIGCRAGYCDAVTLWLRCTCTGCSGKK", "text": "FUNCTION: Antibacterial peptide mostly active against Gram-positive bacteria (PubMed:20605792). It acts by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20605792). It does not disrupt cell membranes (PubMed:20605792). Is noticeably more potent than Cg-Defh1 (PubMed:20605792). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the invertebrate defensin family."}
+{"protein": "MKLAYWMYAGPAHIGTLRVASSFRNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASVVDRHVLARGSRDKVVSNISRKGEEQRPDLIVLTPTCTSSILQEDLQNFVDRASLYSESDVILADVNHYRVNELQASDKTLEQIVRYYLDRARKEGIFNRSLTDVPSANIIGILTLGFHNQHDCRELKRLLGELGVSINQIIPEGEFLNNLKDLPRAWFNIVPYREIGLMAASFLEKEYGMPYISTTPIGISNTADFVMQVEKLMNFWATVLLGKKFHYDQYVENQTKFVSQAAWFSKSIDCQNLAGKEAVVFGDATHAASITKILSGEMGIRVSCSGTYCKHDAGWFNEQVQGLCDEVIITEDHTEVGDTIARIEPSAIFGTQMERHIGKRIDIPCGVISSPVHIQNFPLGYRPFMGYEGTNQISDLIYNSFNLGMEDHLLDVFGGHDTKGISTKSLSTGGKSIDWTPEAESELKRIPGFVRGKVKKNTEVFARQNNILKITVDVMYAAKERRSIESLA", "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": "MAALQEKKSCSQRMEEFRHYCWNPDTGQMLGRTLSRWVWISLYYVAFYVVMTGLFALCIYVLMQTIDPYTPDYQDQLKSPGVTLRPDVYGEKGLEIHYNISDNRTWTSLTHTLRSFLAGYSPAAQVDNINCTSKTYFFQESFGAPNHTKFSCKFTADMLENCSGLTDPSFGFKEGKPCFIIKMNRIVRFLPSNSTPPRVDCTFLDMPHQALTPLQVEYYPPNGTFSLHYFPYYGKKAQPHYSNPLVAAKLLNVPTNTEVVVLCKILADHVTFDNPHDPYEGKVEFKLKIQK", "text": "FUNCTION: The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells (PubMed:7485470, PubMed:10722662, PubMed:11909858). Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (PubMed:7485470, PubMed:10722662, PubMed:11909858). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2) (By similarity). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein Cell membrane; Single-pass type II membrane protein Note=Localized in the apical canalicular membrane of parietal cells. SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family."}
+{"protein": "MAKLTAVPLSALVDEPVHIQVTGLAPFQVVCLQASLKDEKGNLFSSQAFYRASEVGEVDLEHDPSLGGDYMGVHPMGLFWSLKPEKLLGRLIKRDVMNSPYQIHIKACHPYFPLQDIVVSPPLDSLTLERWYVAPGVKRIQVKESRIRGALFLPPGEGPFPGVIDLFGGAGGLMEFRASLLASRGFATLALAYWNYDDLPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQIRATVLINGPNFVSQSPHVYHGQVYPPVPSNEEFVVTNALGLVEFYRTFQETADKDSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHANQAIAQLMKNGKKNWTLLSYPGAGHLIEPPYTPLCQASRMPILIPSLSWGGEVIPHAAAQEHSWKEIQKFLKQHLLPDLSSQL", "text": "FUNCTION: Catalyzes the amidation of bile acids (BAs) with the amino acid taurine (PubMed:9215542). Selective for taurine conjugation of cholyl CoA and only taurine-conjugated BAs are found in bile (PubMed:9215542). Amidation of BAs in the liver with taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (By similarity). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption (By similarity). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (By similarity). In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome. SIMILARITY: Belongs to the C/M/P thioester hydrolase family."}
+{"protein": "MALRIWASSTANALRLSSATRPHFSPLSRCFSSVLDGLKYANSHEWVKHEGSVATIGITDHAQDHLGEVVFVDLPEAGGSVTKATGFGAVESVKATSDVNSPISGEIVEVNSKLSETPGLINSSPYEDGWMIKVKPSNPSELDSLMGAKEYTKFCEEEDSAH", "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. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvH family."}
+{"protein": "MAFPYQCLVARSESSADGAAWTLFGASGSKIVVQSSNGVASVWSRQAVQVLDPKDDDTQEPPGKRIKLSTPKEQKFNFSSLVLSNNGHYLVGVTGEDKCVRVFQIDAQSGLQQLSERCMSRRPSAITLTSDDSTILCADKFGDVYALPLLPSPEDEQVEAPAPALPLEEKDFTPSATVFTVHSGRNRRTLEEQLKQKAKGPAKPKEAITFRHDLLLGHVSMLTDLAFAKIGNKSYIITADRDEHIRISRGVPQAHIIEGFCFGHEEFVSRLCVTRSGLLVSGGGDAHLLVWDWRNFLLNEKLPLRDTVIKHLRSRPDLSSSFKDDASFKTAVSGIWEVPGIKETSEVLVACEGLPGLFNFNVGTGAVNGDSLSLMGNPLDVAFVQTSPNSWTTIVSIDNVHKAGSTSELRENADGARLQYFSKQVDGAWREDAEMGALVSSFALGGTDGPDLTTADDKAVRDILYHVENLRKRPGAED", "text": "FUNCTION: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat TRM82 family."}
+{"protein": "MNETQIQRETRQVVEDVLEKTNLKQGALFVLGLSSSEVLGGQIGKESSQEIGELIVETILGILSSRGIHLAVQGCEHVNRALVVERQVAEQFGLEIVSVHPTLHAGGSGQLAAFKFMQDPVEVEFIKAHAGLDIGDTAIGMHVKHVQVPIRPILREIGHAHVTALASRPKLIGGARAHYPQDAIRKS", "text": "SIMILARITY: Belongs to the UPF0340 family."}
+{"protein": "MFHILRLESTVDLSEPLKDNGIIVFQSDKLDLEPSPNLGPTGIDNTNVNLINAKGDVLLHIGIRRRENAFVFNSIPYGESRGPEERIPLEGTFGDRRDPSITVFDHPDRYQIMIDYKTVYYYKKRLEGRCEKVSYKINEGQTPPFSDVLGVTVLYFANVMPRAN", "text": "FUNCTION: Binds lactose. May play a role in fruiting body formation (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted, cell wall."}
+{"protein": "MGRFIFVSFGLLVVFLSLSGTGADCPPDWSSYEGNCYLVVKEKKTWAEAQKFCTEQRKECHLVSFHSAEEVDFVVSKTFPILSYDLVWIGLNNIWNDCMLEWSDGTKLTYKAWSGIPECIISKTSDNQWLSRACSRTQPFVCKFQA", "text": "FUNCTION: Is a potent glycoprotein Ibalpha (GP1BA) antagonist. Concentration-dependently inhibits botrocetin-, ristocetin- and low dose thrombin-induced platelet aggregation. Inhibits platelet adhesion only through inhibiting the vWF interaction with GP1BA, but has minimal effect on other platelet receptors, such as alpha-IIb/beta-3 (ITGA2B/ITGB3) or alpha-2/beta-1 (ITGA2/ITGB1). Causes an instant severe thrombocytopenia in rats and is not lethal to mice. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
+{"protein": "MHARLLGLSALLQAAEQSARLYTVAYYFTTGRLLWGWLALAVLLPGFLVQALSYLWFRADGHPGHCSLMMLHLLQLGVWKRHWDAALTSLQKELEAPHRGWLQLQEADLSALRLLEALLQTGPHLLLQTYVFLASDFTDIVPGVSTLFSWSSLSWALVSYTRFMGFMKPGHLAMPWAALFCQQLWRMGMLGTRVLSLVLFYKAYHFWVFVVAGAHWLVMTFWLVAQQSDIIDSTCHWRLFNLLVGAVYILCYLSFWDSPSRNRMVTFYMVMLLENIILLLLATDFLQGASWTSLQTIAGVLSGFLIGSVSLVIYYSLLHPKSTDIWQGCLRKSCGIAGGDKTERRDSPRATDLAGKRTESSGSCQGASYEPTILGKPPTPEQVPPEAGLGTQVAVEDSFLSHHHWLWVKLALKTGNVSKINAAFGDNSPAYCPPAWGLSQQDYLQRKALSAQQELPSSSRDPSTLENSSAFEGVPKAEADPLETSSYVSFASDQQDEAPTQNPAATQGEGTPKEGADAVSGTQGKGTGGQQRGGEGQQSSTLYFSATAEVATSSQQEGSPATLQTAHSGRRLGKSSPAQPASPHPVGLAPFPDTMADISPILGTGPCRGFCPSAGFPGRTLSISELEEPLEPKRELSHHAAVGVWVSLPQLRTAHEPCLTSTPKSESIQTDCSCREQMKQEPSFFI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the XK family."}
+{"protein": "MVSIRPDEISSILKQQITDYDQSVSVSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASDLDEATQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVKGLIDEVPVEDVTKFAAELREYLKLNKAEFIEEILKEKKLNEGLETTLTEVIKEVKSSMLATV", "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: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
+{"protein": "MEQWRQCGRWLIDCKVLPPNHRVVWPSAVVFDLAQALRDGVLLCQLLHNLSPGSIDLKDINFRPQMSQFLCLKNIRTFLKVCHDKFGLRNSELFDPFDLFDVRDFGKVISAVSRLSLHSIAQSKGIRPFPSEETAENDDDVYRSLEELADEHDLGEDIYDCVPCEDEGDDIYEDIIKVEVQQPMKMGMTEDDKRSCCLLEIQETEAKYYRTLEDIEKNYMGPLRLVLSPADMAAVFINLEDLIKVHHSFLRAIDVSMMAGGSTLAKVFLEFKERLLIYGEYCSHMEHAQSTLNQLLASREDFRQKVEECTLRVQDGKFKLQDLLVVPMQRVLKYHLLLKELLSHSADRPERQQLKEALEAMQDLAMYINEVKRDKETLKKISEFQCSIENLQVKLEEFGRPKIDGELKVRSIVNHTKQDRYLFLFDKVVIVCKRKGYSYELKEVIELLFHKMTDDPMHNKDIKKWSYGFYLIHLQGKQGFQFFCKTEDMKRKWMEQFEMAMSNIKPDKANANHHSFQMYTFDKTTNCKACKMFLRGTFYQGYLCTRCGVGAHKECLEVIPPCKMSSPADVDAPGAGPGPKMVAVQNYHGNPAPPGKPVLTFQTGDVIELLRGDPDSPWWEGRLVQTRKSGYFPSSSVKPCPVDGRPPTGRPPSREIDYTAYPWFAGNMERQQTDNLLKSHASGTYLIRERPAEAERFAISIKFNDEVKHIKVVEKDSWIHITEAKKFESLLELVEYYQCHSLKESFKQLDTTLKFPYKSRERTTSRASSRSPASCASYNFSFLSPQGLSFAPQAPSAPFWSVFTPRVIGTAVARYNFAARDMRELSLREGDVVKIYSRIGGDQGWWKGETNGRIGWFPSTYVEEEGVQ", "text": "FUNCTION: Guanine nucleotide exchange factor for the Rho family of Ras- related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly."}
+{"protein": "MSVRPFESPPPYRPDEFKPNHYAPSNDMYGGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTGLFGGSLNYPYSGFGYGGGYGGGYGGYGYGYGGYTDPRAAKGFLLAMAAFCFIASLVIFVTSVIRSGMSRTRRYYLIVIIVSAILGIMVFIATIVYIMGVNPTAQASGSMYGSQIYMICNQFYTPGGTGLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKNVSAGTQDMPPPPSDYAERVDSPMAYSSNGKVNGKRSYPESFYKSTPLVPEVAQEIPLTLSVDDFRQPRYSSNGNLETPSKRAPTKGKAGKGKRTDPDHYETDYTTGGESCEELEEDWVREYPPITSDQQRQLYKRNFDAGLQEYKSLQAELDDVNKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKRNYCKQLKSKLSHIKRMVGDYDRRKP", "text": "FUNCTION: May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell junction, tight junction. SIMILARITY: Belongs to the ELL/occludin family."}
+{"protein": "MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQARAVGSTHMNEVSSRSHAIFVITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNAAGGPATQPTAGGGSGSGSASGSASSGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKKGMLGKRPRRKSSRRKKAVSAPAGYPEGSVIEAWVAEEEDDNNNNHHPPQPILEAALEKNMENYLQDQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEDLRREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMLLRDEETMELRGTYSSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHEEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWRFQPLVPAGVNNSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAIFEMEFSHDQEQDPRVLHMERLMRLDSFLERPSTTKVRKSRSWCQSPQRMPPPSTAHASMTSVPLHPATVVDHD", "text": "FUNCTION: Microtubule-based anterograde translocator for membranous organelles. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin II subfamily."}
+{"protein": "MRIEKCWFCSSNIYQGHGTIYVRNDAKVFRFCRPKCRKLFARRVNPRKVKWTKISRKMANKELCNDAILTFEHRLNEPRMYDRAEAERTLSSIPRILEIRKRREDFFIKDRILTGQEMNKESDLKYIERHANLLEEEVAGEKQVAKAKKREAQTN", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family."}
+{"protein": "MNTVLFSPYTTRGLTLKNRIVMSPMCMYSCDTKDGTVRTWHKIHYPARAIGQVGLIIVEATGVTPQGRISEHDLGIWDDDHIHGLHELVGLVKEHGAAIGIQLAHAGRKSEVPGEIIAPSAIPFNESSPTPKEMTKADIEKTVQAFQDGARRAKKAGFDVIEIHAAHGYLINEFLSPLSNRRQDEYGGSPENRYHFLGEVIDAVREVWDGPLFVRISASDYHPDGLTVKDYVPYVKRMKEQGVDLVDVSSGAVVPARIDVYPGYQVPFAEFIRREAGIPTGAVGLITSGWQAEEVLHNGRADLVFLGRELLRNPYWPYAAAKELGVKIEAPVQYERGWRF", "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": "MSSSFKFNYNMGDSRILVVINQRCLALPSMMSADGTCCNGDENRVIDTFSKLGFQDFVYRNMTTADLKDIVTLLTRHNHRTYSCVVVVILTDGAAVGEIKTADGSYKLRDFMTLFDVDKLRDKPKMFVVQTNRGAKIRRNHCKHASCQCLMYSSSERGGLRRIYSVIGWLCKVFGRSSSSPQFASQQLACLNYTLPVRETIVIYSYVDAFVLYGDTDVGSPVIYELCTALDKFGKSCNILTAITMMQHKVAKYVPAALPVVHMNCTRLMHYGDAPNDVTPSKATITTMIDGCSVILEEEGELSDDDGELRTASK", "text": "FUNCTION: May be involved in viral replication. SIMILARITY: Belongs to the peptidase C14A family."}
+{"protein": "MDLMSFKEREISKKDCVELFEDTENFFDILKLADSIRKDIVGDTVTFVKNTNIETTNVCTMGCKFCAFSVSKNSPEAFKLDADEIAKKAVIAKKSGLTEVTIHGGIHPDVDTHFQVETINKVNSATSKLGGIYTHAYSPQEILNGAENAGLSIKEALKMLNEAGLRTIPGTAAEILDDEVRSDICPLKMSTKKWIDIMKTAHKTGIKTTSTIIYGHVEEYKHIVDHLSILKELQEETGGITEFIPMSFLHENTPLYKSGRVTDGASGLYELKLYAIARILFKESIKNIQAPRVKIGTKLSQLILKSGANDLGGTLVEDKVSKAAGSIYEDASVDLMKNAITSIGRIPKERTTLYEIIE", "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": "MKTLSPAVITLLWRQDAAEFYFSRLSHLPWAMLLHSGYADHPYSRFDIVVAEPICTLTTFGKETVVSESEKRTTTTDDPLQVLQQVLDRADIRPTHNEDLPFQGGALGLFGYDLGRRFESLPEIAEQDIVLPDMAVGIYDWALIVDHQRHTVSLLSHNDVNARRAWLESQQFSPQEDFTLTSDWQSNMTREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLNQANRAPFSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRLPDPQEDSKQAVKLANSAKDRAENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITAQLPEQLHASDLLRAAFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIFCSAGGGIVADSQEEAEYQETFDKVNRILKQLEK", "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. PabB, in the absence of PabA, can catalyze the formation of ADC in the presence of exogenous ammonia. SIMILARITY: Belongs to the anthranilate synthase component I family."}
+{"protein": "DPYAFGL", "text": "FUNCTION: May act as a neurotransmitter or neuromodulator. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the allatostatin family."}
+{"protein": "MSKNWFPLLCASVLVVYVSIASSSTGTASGAVTPTSPTENTTGPLIENTTLRTHEVFKINMSKFPYRVCSMAQGTDLLRFEQNINCDSFKPTKEDFEEGIMVVYKRDIRPYTFKVHMYQKILTFRQSYSFIRENHLLGFSQEHLAVPMWEVHYINKLNRCYNSVVRNVAGATYVNYHRDSYVNETMLLVEDDFSNTHSSRFVTVKELWHKPGSTWLYTTSCNVNCMVTVTTARSKYPYDFFVTSDGKVVDISPFYNGSNNKHFGENRDKFSVRKNYSMIAYYGRDNAPEVAHPLVGFFERPDVLMSWDIVEEANNTCEYTFWEQSERTIRSEADDTYHYTSSSMTATFLTSKEELNESDPSFQCIKDKANEQLQLIFNTSYNETYVQSGNVSMYETTGGLIVFWLPVKEKSILEMEELAVAYNNTNSSTRRKRSTDSASDSNKTSEEVLKSIVYAQLQYTYDTLRNYINRALRQIAEAWCKDQKRTLEVFKELSKINPSAMLSAIYDKPIAARFVGDVISLAKCVEVDQNSVKVLRDMRTKESGVCYSRPVVLYTFKNSSHVQYGQLGEYNEILLGRHRTEACEYPSLKIYIAGNSSYEYVDYLYKRMIPLDSISTVDTMISLDIDPLENTDFKALELYSEDELRSSNVFDLEDIMREFNTYKQRMIHVEGKVFDKVPGYLRGLDDMMSGLGSAGKALGVAIGAVGGAVASFVEGVVGFIKNPFGSFTVILFLLAVLGVIYLIYMRQKRAYEKPFEHFFPYVVPPTTVKEAPPSYEQSQYENIKEKAASATKEFSLEEAYQMLLALQKLDQEKRRKAEADDEDFASNGQSAGFLDRLRNRRRGGYQKIQNEYEV", "text": "FUNCTION: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. 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 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). SIMILARITY: Belongs to the herpesviridae glycoprotein B family."}
+{"protein": "MAQMLLHGTLHATIFEAASLSNPHRASGSAPKFIRKFVEGIEDTVGVGKGATKVYSTIDLEKARVGRTRMITNEPINPRWYESFHIYCAHMASNVIFTVKIDNPIGATNIGRAYLPVQELLNGEEIDRWLDICDNNREPVGESKIHVKLQYFDVSKDRNWARGVRSTKYPGVPYTFFSQRQGCKVTLYQDAHVPDNFIPKIPLADGKNYEPHRCWEDIFDAISNAQHLIYITGWSVYTEITLVRDSNRPKPGGDVTLGELLKKKASEGVRVLMLVWDDRTSVGLLKRDGLMATHDEETENYFHGSDVNCVLCPRNPDDSGSIVQDLSISTMFTHHQKIVVVDHELPNQGSQQRRIVSFVGGLDLCDGRYDTQYHSLFRTLDSTHHDDFHQPNFATASIKKGGPREPWHDIHSRLEGPIAWDVLYNFEQRWRKQGGKDLLLQLRDLSDTIIPPSPVMFPEDRETWNVQLFRSIDGGAAFGFPDTPEEAAKAGLVSGKDQIIDRSIQDAYIHAIRRAKNFIYIENQYFLGSSYAWKPEGIKPEDIGALHLIPKELALKVVSKIEAGERFTVYVVVPMWPEGVPESGSVQAILDWQRRTMEMMYTDITEALQAKGIEANPKDYLTFFCLGNREVKQAGEYQPEEQPEADTDYSRAQEARRFMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAMGGYQPYHLATRQPARGQIHGFRMALWYEHLGMLDDVFQRPESLECVQKVNRIAEKYWDMYSSDDLQQDLPGHLLSYPIGVASDGVVTELPGMEYFPDTRARVLGAKSDYMPPILTS", "text": "FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily."}
+{"protein": "MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN", "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. Negatively regulates the kinase activity of PDPK1. SIMILARITY: Belongs to the 14-3-3 family."}
+{"protein": "MTNYFDSPFKGKLLSEQVKNPNIKVGRYSYYSGYYHGHSFDDCARYLFPDRDDVDKLIIGSFCSIGSGASFIMAGNQGHRYDWASSFPFFYMQEEPAFSSALDAFQKAGNTVIGNDVWIGSEAMVMPGIKIGHGAVIGSRSLVTKDVEPYAIVGGNPAKKIKKRFTDEEISLLLEMEWWNWSLEKIKAAMPMLCSSNIVGLHKYWLEFAV", "text": "FUNCTION: This enzyme is an effector of chloramphenicol resistance in bacteria. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
+{"protein": "MLFLAPGYIFPNVATPVTVAIDFAQAVKQGAYNVLDLKASPIPNPELFQPPSRIIRGPLNYLLSLPGKDIRGKLIDALNEWFRVPEDKLNIIKEIVVILHTASLLIDDIQDSSELRRGNPVAHRIFGVAQTINSANYAYFLAQAKLADLNDSRAFDIFTKGLLKLHRGQGMELYWRDNLICPTEEEYVEMVSCKTGGLFYLAVQLMQLNSEVTVNFSNFINLLGIIFQIRDDYMNLQSGTMTKTKGFSEDLTEGKFGYPIIHSIHAAPNDSQLIQILKLKTKDEVIKQYAVRYIESTGSFVYCREKLDMYLEEANETFRGLEMLLGPSKGIRAILDFLRTR", "text": "FUNCTION: Geranylgeranyl pyrophosphate synthase; 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). SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MASKRKSTTPCMVRTSQVVEQDVLEEADRAKDKGLGVPPSDVSKERWAAEPEPSSKESEVVEVRSVGESQSKKLQGGYECKYCPYSTQNLNEFTEHVDMQHPNVILNPLYVCAECNFTTKKYDSLSDHNSKFHPGETNFKLKLIKRNNQTVLEQSIEATNHVVSITASAPGSSDNDPGVSVGKTATVKTGKQKADAKKVPKKPDEAAPDNHMEGTARLVTDTAEILSRLGSVELLHDSLGHVMPSVQLPPNINLVPKVPVPLNTTKYNSALDTNATMINSFNKFPYPTQAELSWLTAASKHPEEHIRIWFATQRLKHGISWSPEEVEEARKKMFNGTIQSVPPTITVLPAQLTPTKVSQPILQTALPCQILGQPSLVLTQVTSGSTAVSCSPITLAVAGVTNHGQKRPLVTPQAAPEPKRPHIAQVPEPPPKVANTPLTPASDRKKTKLQIAHLKASFLQSQFPDDAEVYRLIEVTGLARSEIKKWFSDHRYRCQRGIVHITSESLAKDQMAITGTRHGRTYHVYPDFAAQKFKEKSQGQLKTLEDSFLKSSFPTQAEVERLRVETKLSRREIDSWFSERRKLRDSMEQAVLDSMGSGKKGSDVVAPNGALSRLDQLSGAQLAGPLPSPSSAVVQNQEQVHLLRSTFARTQWPTPQEYDQLAAKTGLVRTEIVRWFKENRCLLKTGTLSWLEQYQRHHLSDDHGHDVASRRATKHVAESPKNGSEVAHQYAKDPKALGEEESEKLVPRVKLVGDPSKDCLAGKPSEATSDRSEGSRDGQGSEENEESGIVDFVEVTVGEEDAISEKWGSWSQRVAEGTVERADSDSDSTPAEAGQA", "text": "FUNCTION: Acts as a transcriptional repressor. Represses the promoter activity of the CDC25C gene stimulated by NFYA. May play a role in retinal development where it regulates the composition of bipolar cell populations, by promoting differentiation of bipolar OFF-type cells. In the brain, may promote maintenance and suppress differentiation of neural progenitor cells in the developing cortex. SUBCELLULAR LOCATION: Nucleus Note=Colocalizes with EFNB1 intracellular domain in the nucleus. SIMILARITY: Belongs to the ZHX family."}
+{"protein": "MLIKINSNDIWLPIHFYDETFNFQLVLSIVELFSYLICAYILTLNIYIILKIKMFHRNLYILAIPLFGIWFELIIGKLITIAYRLKILNPGFELGVHIEIWTSDPTRKLKVESVNGLELLIFGGFLQWHYMFTIIFGVLAIAVERVVASVLIENYESNTQLFIPLFLTVISQFLSISTSLALLFQKVGPFLAQLPWIICCPFSAMAYFFVKKCNESFEREIRNPRRRRHFSVSQQFQVKENLRALYLGTRLVFVVLSCIALCGIGITALFYDLIPPFCCHFVENFLFLHPYLSCLTAIFSVPQWKNEFREVSVLGRCLKIGRLKIESENAMEIQDSTKKMGTETDLYFQQLADSWI", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nematode receptor-like protein sre family."}
+{"protein": "MSLSSAFRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKKGGVASGMKHVETNTYDVKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVLQDTLGRRSMIKPAVSDEIMDQQQKSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTTGLGKIFSTGKIAKIFQDKFDVSLLHTKPEVAAQERMVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVRVSMGKEPRHFMAIFKGKLVIYEGGTSRKGNEEPDPPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNADTVAEGQEPPEFWDLLGGKTAYANDKRLQQETLDVQVRLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRDPDTPILIIKQGFEPPTFTGWFLAWDPHIWSEGKSYEQLKNELGDATAIVRITADMKNATLYLNPSDGEPKYYPVEVLLKGQNQELPEDVDPAKKENYLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF", "text": "FUNCTION: Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1- mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis (PubMed:15247299, PubMed:18160648). In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, lamellipodium Cell junction, focal adhesion Cell projection, neuron projection Cell projection, axon Note=In podocytes, present in the F- actin-enriched cell periphery that generates lamellipodia and focal adhesions. SIMILARITY: Belongs to the villin/gelsolin family."}
+{"protein": "MQSHIGQWTSTAKGHLSRDENGDEKTDYSRWRLVDRQGRQTWRYLESDEENEKSPQTVPEKYFLGLDTGLPDLPKAETPLQAAQDGVSFLSQLQLSSGQWASECTGPMFILPCVIIAWYVTNTPIPPAYAIEIRRYLFARQRVEDGGWGWHVEARSSAIGTALNYVVLRLLGASKDDHRLIQARKLLHSYGGATYAPGIAKFWLCVLGVMKWECVNPFLPEFWLLPDSDPTAPSKWYIHTRTNFTSLSYIWSKQWSFAGDEVTKQLQTELYPEPYSAIDFAAHRTSLAEVDNNYPKWWLVNLMNWLTVAVYIPYMRKKATVESAEQRVWELIQAEDKNSEFIGLSPISKAANMIACYIHDGKDSESVRSHGETIFQYFWMNGEGMACNLSDGIQVWDTSLAVQAIAAAGGAGNPRFQSTVIKAHEFLEDHQLLDDVQDQEMCCRGHRKGGWPFSTKYQGYMISECTGEGLRSILQLQKTFQLDLKKRIPADRLHNAVDCLLNLQNDTGGFGVYEKRQGSLKLAWLEMGEFSGKTMVTYDYVECTTAVVSALASFSEFYPDYRKEEVQTARTRGLEFIKSSQKPYGGWHGAWGVCFTYAGMFALESLALAGETYSNSEPSRKGCTFLVSKQRDDGGWGESYLSFQKEEYIEHEDAQVVQTAWACLGLMHAEYPDKTPVKRGLKLIMSRQQSKGHWLQEQYEGGVGDGVISYSNYKLYWPVRALAEYVRRFGNEEM", "text": "FUNCTION: Terpene cyclase/mutase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids nectripenoids A and B, as well as cochliquninone D and isocochliquninone E (PubMed:29797385). The pathway probably begins with the HR-PKS ntnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS ntnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of nectripenoids (Probable). The FAD-dependent monooxygenase ntnJ then performs an oxidative decarboxylation at C11 of the ntnH/ntnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation (Probable). The membrane-bound polyprenyl transferase ntnF then introduces a farnesyl group before the FAD- dependent monooxygenase ntnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by ntnA (Probable). The terpene cyclase/mutase ntnI then initiates the sequential tricyclic ring formation through protonation of the terminal epoxide and catalyzes the regioselective and stereoselective 6/6/6-tricyclic ring formation (Probable). The cytochrome P450 monooxygenase ntnM may then hydroxylate C1' (Probable). SIMILARITY: Belongs to the terpene cyclase/mutase family."}
+{"protein": "MLECFESSPVAVAVGVSLLVLLLLCGIGCAWHWNRRESTPFTLPKFMQRRSSRQKDVTKTVSSSAYVISPSMKASVESKGHKSTAKRNKMHGNYENVEVCPPCTEGTTEKALYENTQPSNLEEHVYGNQTDPLYYNFQKPSPPPPQDDDIYILPDCD", "text": "FUNCTION: Negatively regulates B-cell proliferation following stimulation through the B-cell receptor. May play an important role in maintenance of marginal zone (MZ) B-cells. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GAPT family."}
+{"protein": "MTQTANAAKKTTSTKASAAKEAKVKVTAEEKAVTEVKKPAAKKKSALAFPFTAIVGQEEMKLSLILNIIDPRIGGVLVMGHRGTGKSTTVRALAEVLPLIPRVKGDIYNRTVEQYIEMEAAGKGAPAIKPEDVETELIPVPVVDLPLGATEDRVCGTIDIEKALTSGVKAFEPGLLAQSNRGFLYIDEVNLLDDHLVDVLLDVAASGKNVVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGLHARITTINDVAKRVQIVKLRREFDEDPEAFMKKVSREQQKLRKKIVAAQQLLPQVTMDDAVLTDIAKLCMNLGIDGHRGELTITRTAHAYAAWEGDKKVTMKHVREIAGLCLRHRLRKDPLETVDAGEKIDRELAKVLGEAEAAA", "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": "MPPSGPRAALFLLPSLLLLRAVLAVPLERGAPKEENPATESPDTGLYYHRYLQEVINVLETDGHFREKLQAANAEDIKSGKLSRELDFVSHHVRTKLDELKRQEVSRLRMLLKAKMDAQQEPNIQLDHLNLLKQFEHLDPQNQHTFEARDLELLIQTATRDLAQYDAAHHEEFKRYEMLKEHERRRYLESLGEEQRKEAERKLEEQQRRHREHPKVNVPGSQAQLKEVWEELDGLDPNRFNPKTFFILHDINSDGVLDEQELEALFTKELEKVYDPKNEDDDMREMEEERLRMREHVMKNVDTNQDRLVTLEEFLASTQRKEFGDTGEGWEQGKAGVPLPMAPVLTLQTVEMHPAYTEEELRRFEEELAAREAELNAKAQRLSQETEALGRSQGRLEAQKRELQQAVLQMEQRKQQQQSHNNPAPGPEGQLKFHPDTDDVPVPAPAGDQKDVDASEKKVPEQTPEPPQLDSQHL", "text": "FUNCTION: Major calcium-binding protein of the Golgi which may have a role in calcium homeostasis (PubMed:7890746). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates alpha subunits of guanine nucleotide-binding proteins (G proteins) (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein; Lumenal side Cytoplasm Secreted Note=A small fraction of the protein may be cytoplasmic. SIMILARITY: Belongs to the nucleobindin family."}
+{"protein": "MAEEKKLKLSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHAQEFIPFRFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLKSAKPGQEEDGPLKGKGQGAAAADGKGKEKKAPPLLEGAPFRLKPRSIHELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVQNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKHCAPVLAKLRPPPDNQDAYRGEFGSLGPLLCSHVVKARAQAALQAQQVNRTTLTITQPRPTLTLSQAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSASSTQQVLSLSTSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATTAPPSTAPAGPGSVQKYIVVSLPPTGEGKGGPPSHPSPVPPSSSSPSPLGGSALCGGKQETGDSPPPAPGTPKANGSQPTGPSSPQPAL", "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. The TFIID complex structure can be divided into 3 modules TFIID- A, TFIID-B, and TFIID-C. TAF6 homodimer connects TFIID modules, forming a rigid core. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF6 family."}
+{"protein": "MSTQVSASSLAQIPQPKNRPVANFHPNIWGDQFITYTPEDKVTRACKEEQIEDLKKEVKRKLTAAAVANPSQLLNFIDAVQRLGVAYHFEQEIEEALQHICNSFHDCNDMDGDLYNIALGFRLLRQQGYTISCDIFNKFTDERGRFKEALISDVRGMLGLYEAAHLRVHGEDILAKALAFTTTHLKAMVESLGYHLAEQVAHALNRPIRKGLERLEARWYISVYQDEAFHDKTLLELAKLDFNLVQSLHKEELSNLARWWKELDFATKLPFARDRLVEGYFWMHGVYFEPQYLRGRRILTKVIAMTSILDDIHDAYGTPEELKLFIEAIERWDINSINQLPEYMKLCYVALLDVYKEIEEEMEKEGNQYRVHYAKEVMKNQVRAYFAEAKWLHEEHVPAFEEYMRVALASSGYCLLATTSFVGMGEIATKEAFDWVTSDPKIMSSSNFITRLMDDIKSHKFEQKRGHVTSAVECYMKQYGVSEEQVYSEFQKQIENAWLDINQECLKPTAVSMPLLARLLNFTRTMDVIYKEQDSYTHVGKVMRDNIASVFINAVI", "text": "FUNCTION: Involved in the biosynthesis of valencene, a major volatile emitted from flowers of grapevine. Can use farnesyl diphosphate as substrate, but not geranyl diphosphate or geranylgeranyl diphosphate. Produces mainly (+)-valencene and (-)-7-epi-alpha-selinene along with five minor products. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes close to lipid bodies in maturing microspores. SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily."}
+{"protein": "MSRRRAHDTEDEGYDHRRNKRRRVSENQEIEDRLESLILRVGERSTSSVESNLEGLVSVLEADLGTFRLKILRILSDCAVRMPEKCTVYTTLVGLLNAKNYKFGGEFVDHMVKTFKESLKMCRWDAARYSLRFLADLVNCHVISATSLLQLLDTMIDVSNEDTVPQVRRDWFVFAVLSTLPWVGRDLYEKKESALESLLLRIEVYLNKRSKKHHNALRVWSSDAPHPQEEYLDCLWAQIRKLRQDNWAEKHIPRPYLVFDSILCEALQHNLPTIVPPPHHDNFEYPMPWVVYRMFDYTDCPDGPNLPGAHSIERFLIEEHLHHIIETYHHERKDCAAQLLSFPYKHKIPLEYCIVEVVFAELFHMPTPRYLDICYGSILIELCKLQPATLPQVLAQATEILFMRIDSMNTSCFDRFVNWFSYHLSNFKFTWSWDEWDSWLLLDGEHPRPKFIQEVLQKCLRLSYHQRITEMMPTTYAKLIPLTPVPNYKYANEEAASLPGTTVAHQLVVAIRQKCTPEEVVNILKDIPNSGYSGEEMSDGSFNALKIDVFVQTLLNLGSKSFSHSFAAISKFHSVFRALAETEEAQICILHNIFELWSSHQQMMVVLIDKLLKLQIVDCSAVATWIFSKEMTGEFTKLYLWEILHLTIKKMNKHVIKLNSELSEAKDKLAKADSSSSDSEDDSSHKRKKPITHADKPSEEVVERMEEKLEAANVNQKRLFLIVFQRFIMILSEHLLRSDTDGRDPDTDWYRWTIGRLQQVFLMHHEQVQKYSSTLETLLFTSDLDTHILEVFQQFVALRA", "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": "MLRATAPCWFPPGYPEAKKVAEEAALEAPEFPLPSHQPAQSFGLPVPQMHNQASAFVDIQAEPQNRGPAVHPAWPKMVTEACYFPAQRGSACCLPAAPRLTERPSGVRISAPRKRKTIAQSSSPCLVTGCTDAKRTRVASSSQRSSGSKVGRQPGKTRNRSGMACKTTTTISSKRIVRRPSLPSLKKPIILRRSGCQVPTVLRRGYLQLFTEECLKFCASKQEAEEKALNEEKVAYDCSPNKNRYLNVVLNTLKRLKGLTPSSMPGLSRAALYSRLQEFLLSQDQLKENGYPFPHPERPGGAVLFTGQGKGPGDSSCRVCCRCGTEYLVSSSGRCVRDQLCYYHWGRVRSSQVAGGRVSQYTCCAAAPGSVGCQVAKQHVRDGRKDSLDGFVETFKKELSRDAYPGIYALDCEMCYTTHGLELTRVTVVDADMRVVYDTFVKPDNEIVDYNTRFSGVTEADVAKTSITLPQVQAILLSFFSAQTILIGHSLESDLLALKLIHSTVLDTAVLFPHYLGFPYKRSLRNLAADYLGQIIQDSQDGHNSSEDANACLQLVMWKVRQRAQIQPRHRSASPAALACPWPQAPSTTAISPESSPCPPRRKAKETGAVDGRRGQKAKSNPNRPLPVPRNPCRGPSGLSPSLCPSQTSVLPLIASRSTEPPLPVPRVPAAPPRACPHPSAHPRPLSLHH", "text": "SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the REXO1/REXO3 family."}
+{"protein": "MTKLSAQVKGSLNITTPGVQIWRIEAMQMVPVPSNSFGSFFDGDCYVIQAIHKTGSNLSYDIHYWIGQASSQDEQGAAAIYTTQMDDFLKGRAVQHREVQGNESDTFRGYFKKGIVIRKGGVASGMKQVETNSYDIQRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERLRGMNLAKEIRDQERGGRTYVGVVDGEDEKASPQLMEIMNHVLGQRKELKAAVADTVVEPALKAALKLYHVSDSEGKVVVREIATQPLTQDLLSHEDCYILDQGGLKIYVWKGKNANAQEKKEAMNQALNFIKAKQYPPSTQVELQNDGAESAVFQQLFQKWTVPNRTTGLGKTHTVGSVAKVEQVKFDAMSMHVQPQVAAQQKMVDDGSGEVQMWRIENLELVPVNTKWLGHFFGGDCYLLLYTYFINEKPHYLLYIWQGSQASQDEITASAYQAVILDQEYNNEPVQIRVPMGKEPPHLMSIFKGCMVVYQGGTSRANSVEPVPSTRLFQVRGTSANNTKAFEVSPRAASLNSNDVFILKTQSCCYLWCGKGCSGDEREMAKMVADTVSRTEKQVVVEGQEPANFWLALGGKAPYASTKRLQEENLVITPRLFECSNQTGRFLATEIPDFNQDDLEEDDVFLLDVWDQVFFWIGKNANEDEKKAAATTVQEYLKTHPGGRDLETPIIVVKQGHEPPTFTGWFLAWDPFKWNNSKSYEDLKAELGNSGDWSQITAELTSSKPEAFNANSNLSSGPLPIFPLEQLVNKPTEELPEGVDPSRREEHLSIEDFTRALGMTPSAFWALPRWKQQNLKKEKGLF", "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": "VRTPVTVQTKVDNIKXY", "text": "FUNCTION: Hydrolysis of carbamoyl and sulfocarbamoyl esters of paralytic shellfish toxins. Ester hydrolysis is unaffected by the presence or absence of a hydroxyl moiety at the N-1 postion of the substrate toxin but is significantly affected by the stereochemistry of sulfate esters at C-11 of the substrate toxin."}
+{"protein": "MFLRTVRSQAVRAAALHHTVAPALCMRPVLRTQTVAFSSTPVTLGKKKKGGKEPKAAAKAAAEEAVDEDLFMIEWNKFEDLSAKSVAAFAAKAKEIKAGNNSPDLINNIEVKISKDEVYQIKDIASVALKGGRTLSISVYDPSHTKQVTASILASDLNMNPQPQANSPQILNIPLPPPSAESRAEQQKELKALYNAFKADKKLTSGLAAIRDAFKKDHKKMADQKSIGKDVVKREDKKFEELQKAWTSKIEKEFKTVSDEIAKK", "text": "FUNCTION: Necessary for protein synthesis in mitochondria. Functions as a ribosome recycling factor in mitochondria (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RRF family."}
+{"protein": "MELRHLRYFVAVAQALNFTRAAEKLHTSQPSLSSQIRDLENCVGVPLLVRDKRKVALTAAGECFLQDALAILEQAENAKLRARKIVQEDRQLTIGFVPSAEVNLLPKVLPMFRLRQPDTLIELVSLITTQQEEKIRRGELDVGLMRHPVYSPEIDYLELFDEPLVVVLPVDHPLAHEKEITAAQLDGVNFVSTDPVYSGSLAPIVKAWFAQENSQPNIVQVATNILVTMNLVGMGLGVTLIPGYMNNFNTGQVVFRPIAGNVPSIALLMAWKKGEMKPALRDFIAIVQERLASVTA", "text": "FUNCTION: Transcriptional activator of the hca operon for 3- phenylpropionic acid catabolism. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MSSDRTSVVVSKRDAGGFEYPFAASCHPGREVTEQRTLAWVRRLRLVPDGRSLSRLKATNFSHLAAWLLPSASTQTLQLASDFTAVLFLLDDAYDEGQLSTDPESVEWLNEKYLGELFGYTEADMSDPLTRGMLDVRERIRRSHPHFFLNRWLSHFQYYYEANLWEANNRKQMRVPHLEEYLMMRRYSGAVYTYCDLLELLLERPLPLEVVQHPLIQTVRDICNDILCWTNDYFSLGKELTNGETHNLIVVLRNECVSTLEEAIDRLKDMHDRRVAEYQGVKEKVLALWADDEIRLYLDAVEAMIAGNQRWALEAGRYSGLESLIVRAG", "text": "FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene eremophilene via a 1,10- cyclization, which requires the abstraction of the pyrophosphate from FPP to yield the (E,E)-germacradienyl cation. The only accepted substrate is farnesyl diphosphate (FPP). SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILPFYIPTPMEFTGEIGSYTGVKLEVEKKEANKVILKNGEAVLIPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGNDPPVSKHISPYTPRTRIAIEVEKAFDECMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEPYKTHGDDFLIPETILFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADTATKEVDVPICYSDPETVHSYANHVRTEILHHNMVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIVRNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNDTQTGSQTSSLTDLVPTRLHSFLNHNLSKLKILNRAQQTVKNILSNDCLNQLKHYVKHTGKNEILKLLQE", "text": "FUNCTION: [p8]: Component of the core shell. FUNCTION: [Polyprotein pp62]: Essential for the correct assembly and maturation of the core of the virion. FUNCTION: [p15]: Component of the core shell (By similarity). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (By similarity). FUNCTION: [p35]: Component of the core shell (By similarity). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (By similarity). SUBCELLULAR LOCATION: [p35]: Virion Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. SUBCELLULAR LOCATION: [Polyprotein pp62]: Host cytoplasm, host perinuclear region Note=Found in perinuclear cytoplasmic viral factories during assembly. SUBCELLULAR LOCATION: [p15]: Virion Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. SIMILARITY: Belongs to the asfivirus polyprotein pp62 family."}
+{"protein": "MELFKYMETYDYEQVLFCQDKESGLKAIIAIHDTTLGPALGGTRMWMYNSEEEALEDALRLARGMTYKNAAAGLNLGGGKTVIIGDPRKDKNEAMFRAFGRFIQGLNGRYITAEDVGTTVADMDIIYQETDYVTGISPEFGSSGNPSPATAYGVYRGMKAAAKEAFGSDSLEGKVVAVQGVGNVAYHLCRHLHEEGAKLIVTDINKEVVARAVEEFGAKAVDPNDIYGVECDIFAPCALGGIINDQTIPQLKAKVIAGSADNQLKEPRHGDIIHEMGIVYAPDYVINAGGVINVADELYGYNRERAMKKIEQIYDNIEKVFAIAKRDNIPTYVAADRMAEERIETMRKARSPFLQNGHHILSRRRAR", "text": "FUNCTION: Catalyzes the reversible deamination of L-leucine to 4- methyl-2-oxopentanoate. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
+{"protein": "MGSLDSNYDTESPASVGQFNPLDPEEFRKQAHCIVDFIADYYKNIESYPVLSQVDPGYRHSRLGKNAPYRSEPFESILKDVQKDIIPGMTHWMSPNFFAHFPATVSSAAFVGEMLCTCFNSVGFNWLASPAATELEMVVIDWLANMLKLPKSFMFSGTGGGVLQGTTSEAILCTLIAASPMHFEIVGVKTSTSFVVYGSDQTHSTYAKACKLAGILPCNIRSIPTTADSNFSVSPLLLRRAIEADKAAGMVPLYICATVGTTSTTAIDPLSSLADVANDYGVWFHVDAAYAGSACICPEFRHYLDGIERADSLSLSPHKWLLSYLDCCCLWVKSPSLLVKALSTDPEYLKNQPSESKSVVDYKDWQVGTGRRFKALRLWFVMRSYGVANLQSHIRTDVQMAKMFEGFVKSDPRFEILVPRVFSLVCFRLNPISGSDPTGTEALNRKLLDWVNSTGRVYMTHTKVGGIYMLRFAVGATLTEKRHVSSAWKLIKEGADVLLKED", "text": "FUNCTION: Involved in the biosynthesis of tryptamine. Supplies tryptamine for the indole moiety of camptothecin (CPT), an anti-cancer monoterpene alkaloid. Represents a key step in monoterpene indole alkaloid biosynthesis. Is specific for tryptophan, and inactive against tyrosine, phenylalanine and 3,4-dihydroxyphenylalanine (dopa). SIMILARITY: Belongs to the group II decarboxylase family."}
+{"protein": "MAFATGITTSSNPTFLGLKISNTSLRSVVSCNSISFPSLSYVNLNLNRRNRLSVRSASVPAAPAMEGLKPAISLSENALKHLSKMRSERGEDLCLRIGVKQGGCSGMSYTMDFENRANARPDDSTIEYQGFTIVCDPKSMLFLFGMQLDYSDALIGGGFSFSNPNATQTCGCGKSFAAEM", "text": "FUNCTION: Involved in the assembly of chloroplastic iron-sulfur proteins. Is able to transfer iron-sulfur clusters to apo-ferredoxin. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the HesB/IscA family. Ycf83 subfamily."}
+{"protein": "MSSILLRSYRHHAKVWTRPSSKSSFIRSLASRSNPTSSFEHVRRVFDDDKYYQDFNNGTLSRKIFSGPRTGLFKNEKLTTPQGLIDFSGQCLTEAQTLVDTMIREAETSDQGKIHYIRRLDQLSDILCRVIDVAEFIRVAHPNSKWTHAAQQTHELMFEYMNQLNTNVQLHTILGNILADKSITSKLSSEEIMVGEYLKQDFERSGIYMEPHTRENFVALTQEISVLGSHFNNGIHELKDYWCEISQQEYEAIDNADLKREIRRFQQKSPRSSRNSVYIPLAGSLPYSILQRCSMESVRRKVWIALHNASEEQISTLNLFLKYRATLSKMLGYESFAHYQLEHKMAKNPENVLTFLENLQRKMVDGENSGLISELESLYAMSNHWKPGASKSDIIHAIQPWDRDYLLHKLQEEKKETQLDDNISEYLSVGTIMSGLSQLFHSIYSIELLPEPSASGETWASQVRKIKVFDNETQSTLGFLYLDFWSPNVLPSHFTIVCSRQLNKDLGEKVEVMKPLVQLDETESHQLPVISLVCNFHQGNSFIGRFAGLETSKPTLLTLDQVDTIFHEMGHAMHSMIGRTKLQNLSGTRCSTDFVELPSVLMESFSKDPRVLGRIARHYSTNELLPHDILAKHQHYRNVLENSETYMQSKMAMLDQVLHGKSIVKQLEMARDDIDSTTMYHSLEKELKVFSDQWSTWHGKFPHLFSYGAVYFSYLFDRAIAEKIWKSLFQNDPWSREAGTTYKEAILKWGGTRDPWHCLADALSNQELSKGDEKAMRIIGGETKDL", "text": "FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase M3 family."}
+{"protein": "MAVDKEVQLHAQAWDHALSYIKPTALDAAVELEIPDILEDHGGPMSLSELSAATGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTRENLGLYMLMQATPATRSPAGLSGEALKTGTPLYLKSIRGEDSWNDPAYGFHMRAFTNAMTAHSRLTAAAIVTNYPTAFDGVRSVVDVGGRHGMAIGRLVEAFPWVRGITFDLPEIVADAPPLKGVDFVGGDMFKSVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPTSTGKVMIVDAIINEEGEGDEFSGARLSLDMIMMATTTQGKERSYKEWVHLLNKAGFSKHSVKNIKTIEFVIDAYP", "text": "FUNCTION: Flavonoid 6-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:22923679). Catalyzes S-adenosylmethionine-dependent regioselective 6-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and ladanein (LAD), and, with a lower efficiency, chrysoeriol (CHRYS) and cirsioliol (CIRL) (PubMed:22923679). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
+{"protein": "MQMPAMMSLLLVSVGLMEALQAQSHPITRRDLFSQEIQLDMALASFDDQYAGCAAAMTAALPDLNHTEFQANQVYADSWTLASSQWQERQARWPEWSLSPTRPSPPPLGFRDEHGVALLAYTANSPLHKEFNAAVREAGRSRAHYLHHFSFKTLHFLLTEALQLLGSGQRPPRCHQVFRGVHGLRFRPAGPRATVRLGGFASASLKHVAAQQFGEDTFFGIWTCLGAPIKGYSFFPGEEEVLIPPFETFQVINASRLAQGPARIYLRALGKHSTYNCEYIKDKKCKSGPCHLDNSAMGQSPLSAVWSLLLLLWFLVVRAFPDGPGLL", "text": "FUNCTION: Has ADP-ribosyltransferase activity toward GLP1R. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family."}
+{"protein": "MRAQEDLEGRTQHETTRDPSTPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGHDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKAILALERWKCPPEEEIYGNWSLPLNTSHIWHPRIREVQGAIMVSSVVEVVIGLLGLPGALLNYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIILFSQYLRNLTFLLPVYRWGKGLTLLRIQIFKMFPIMLAIMTVWLLCYVLTLTDVLPTDPKAYGFQARTDARGDIMAIAPWIRIPYPCQWGLPTVTAAAVLGMFSATLAGIIESIGDYYACARLAGAPPPPVHAINRGIFTEGICCIIAGLLGTGNGSTSSSPNIGVLGITKVGSRRVVQYGAAIMLVLGTIGKFTALFASLPDPILGGMFCTLFGMITAVGLSNLQFVDMNSSRNLFVLGFSMFFGLTLPNYLESNPGAINTGILEVDQILIVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSDMSSSLKSYDFPIGMGIVKRITFLKYIPICPVFKGFSSSSKDQIAIPEDTPENTETASVCTKV", "text": "FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate. FUNCTION: [Isoform 2]: Inactive transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family."}
+{"protein": "MSKKFIITWDAMQSYCRELAEKQMPAEQWKGIWAVSRGGLVPGAILARELGIRHVDTICISSYDHDHQRDMTVVKAPEGDGEGFLIVEDLVDSGDTARKLREMYPKAKLIAVCAKPAGVELLDDYVVDIAQDTWIEQPWDMSIQFVEPVNRKQK", "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": "MAKLTGMFSAAILLSMAICSTAIIYRGEHMSMYLNASSEFAVYPTDQSLVLVGHLLFLDGQRLPTTNYSGLIELIHYNYSSVCYTVIQTISYESCPRVANNAFRSCLHKTSKHYHDYFRVNASVETNVLLNITKPQPTDSGAYILRVKLDHAPTADVFGVSAFVYDLKSKTVPDPMPTTQTVEPTTSYVSTPTYDYTDDVTTETESTSTSTQQAMTSTQTPSATWGTQLTTELPTNETVVIGQEALLCHWFQPSTRVPTLYLHLLGRTGNLPEDVLLVEDSEFLRTTSPAHRPSASPADGDDFKQTNSTSLKARNKIVAMVVIPTACVLMLLLVVVGAIINGAVRKHLLSCASRRIYRSGQGGASAAERRRLTCGPTLAASSESLADDTTSSPPTPKPSKKTKLETDPLMEQLNRKLEAIKEES", "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": "MGSISEMVFETCPSPNPIHVMLVSFQGQGHVNPLLRLGKLIASKGLLVTFVTTELWGKKMRQANKIVDGELKPVGSGSIRFEFFDEEWAEDDDRRADFSLYIAHLESVGIREVSKLVRRYEEANEPVSCLINNPFIPWVCHVAEEFNIPCAVLWVQSCACFSAYYHYQDGSVSFPTETEPELDVKLPCVPVLKNDEIPSFLHPSSRFTGFRQAILGQFKNLSKSFCVLIDSFDSLEQEVIDYMSSLCPVKTVGPLFKVARTVTSDVSGDICKSTDKCLEWLDSRPKSSVVYISFGTVAYLKQEQIEEIAHGVLKSGLSFLWVIRPPPHDLKVETHVLPQELKESSAKGKGMIVDWCPQEQVLSHPSVACFVTHCGWNSTMESLSSGVPVVCCPQWGDQVTDAVYLIDVFKTGVRLGRGATEERVVPREEVAEKLLEATVGEKAEELRKNALKWKAEAEAAVAPGGSSDKNFREFVEKLGAGVTKTKDNGY", "text": "FUNCTION: UDP-glucosyltransferase that forms glucose esters with phenylpropanoids (PubMed:11042211, PubMed:11187886). Glucosylates 4- coumarate, ferulate, caffeate, sinapate and cinnamate (PubMed:11042211, PubMed:11187886). Can glucosylate the phytotoxic xenobiotic compound 2,4,5-trichlorophenol (TCP) (PubMed:12721858). SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MLRNTSRVLMSHFARANIPTPVNQPMLNYEVGSTHRKLLKEACAKFRNTTIDIPCVVGGKEIRTGDVQKQLICSDHNKVLATFHQANAELLKLAVENSMESKAQWESLPFEARSAVFLKAADLLNTKYRYDVLASTMLGQGKTVWQAEIDAAAEGIDFLRFNVKYAQEIYQQQPPANSAGCWNILTYQPLEGYVVAISPFNFTAIGLNLSSAPALMGNVVLWKPASTAVLSNWIVYKALLEAGLPAGVIQFLPGSGRLVGEHLFNNRNFSGLHFTGSTGVFNDIYKKTADNLVAGVYKGYPRIVGETGGKDFHFLHNSGDVENFVNNTLRGAFEYQGQKCSACSRAYIPQSLWPQIKDRLVTGVKSMKMGQSDDFSSFVSAVIDKNSFNNIQSYIEHAKASPDAEIIVGGKCDSSVGWFVEPTIILAKDPHYKSMEEEIFGPVLTIYVYEDSKFEETLKICDETSPYALTGSIFSTCRYAIETAHKYLKNAAGNFYINDKCTGAVVGQQPFGGSRASGTNDKAGSSLNLLRWISARTIKENFVPLTSFTYPYMIDPEN", "text": "FUNCTION: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
+{"protein": "MLACVTMKMLRHAKCFQRLAIFGSVRALHKDNRTATPQNFSNYESMKQDFKLGIPEYFNFAKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVAPKCENLHSKLIVSENSREGWGNLKEMMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWKTI", "text": "FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism (By similarity). Capable of activating medium-chain fatty acids with a preference for isobutyrate among fatty acids with 2-6 carbon atoms (By similarity). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion matrix. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MLLPVVARAAVPAIESAIAATPGLVSRIAAAIGSKVSPSAILAAVKSNPVVAGLTLAQIGSTGYDAYQQLLENHPEVAEMLKDLSFKADEIQPDFIGNLGQYREELELVEDAARFVGGMSNLIRLRQALELDIKYYGLKMQLNDMGYRS", "text": "FUNCTION: Assembles to form an icosahedral capsid with a T=13 symmetry. Drives the penetration of the inner capsid (core) into the cytoplasm. SUBCELLULAR LOCATION: Virion. Note=Outer capsid protein (600 copies)."}
+{"protein": "MSEGAAAASPPGAASAAAASAEEGTAAAAAAAAAGGGPDGGGEGAAEPPRELRCSDCIVWNRQQTWLCVVPLFIGFIGLGLSLMLLKWIVVGSVKEYVPTDLVDSKGMGQDPFFLSKPSSFPKAMETTTTTTSTTSPATPSAGGAASSRTPNRISTRLTTITRAPTRFPGHRVPIRASPRSTTARNTAAPATVPSTTAPFFSSSTLGSRPPVPGTPSTQAMPSWPTAAYATSSYLHDSTPSWTLSPFQDAASSSSSSSSSATTTTPETSTSPKFHTTTYSTERSEHFKPCRDKDLAYCLNDGECFVIETLTGSHKHCRCKEGYQGVRCDQFLPKTDSILSDPTDHLGIEFMESEEVYQRQVLSISCIIFGIVIVGMFCAAFYFKSKKQAKQIQEQLKVPQNGKSYSLKASSTMAKSENLVKSHVQLQNYSKVERHPVTALEKMMESSFVGPQSFPEVPSPDRGSQSVKHHRSLSSCCSPGQRSGMLHRNAFRRTPPSPRSRLGGIVGPAYQQLEESRIPDQDTIPCQGIEVRKTISHLPIQLWCVERPLDLKYSSSGLKTQRNTSINMQLPSRETNPYFNSLEQKDLVGYSSTRASSVPIIPSVGLEETCLQMPGISEVKSIKWCKNSYSADVVNVSIPVSDCLIAEQQEVKILLETVQEQIRILTDARRSEDYELASVETEDSASENTAFLPLSPTAKSEREAQFVLRNEIQRDSALTK", "text": "FUNCTION: Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors. May be a survival factor for oligodendrocytes. SUBCELLULAR LOCATION: [Pro-neuregulin-3, membrane-bound isoform]: Cell membrane; Single-pass type I membrane protein Note=Does not seem to be active. SUBCELLULAR LOCATION: [Neuregulin-3]: Secreted. SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I membrane protein. Note=Isoform 3 is also proteolytically released as a soluble form. SIMILARITY: Belongs to the neuregulin family."}
+{"protein": "YCQKWMWTCDSARKCCEGLVCRLWCKKII", "text": "FUNCTION: Potent and specific blocker of Kv4.2/KCND2 (IC(50)=5 nM) and Kv4.3/KCND3 (IC(50)=28 nM) potassium channels (PubMed:10051143). Acts by altering the gating properties of these channels (PubMed:10051143). Also shows moderate inhibition on human voltage-gated sodium channel Nav1.7/SCN9A activation (IC(50)=423 nM) (PubMed:25026046). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 30 (phrixotoxin) family."}
+{"protein": "MALSVPPIAGAIIGYFTNDLAITMLFRPYKPIKIGQRTLPFTPGLIPANQERLARRISDAIMGSLLTPEELQKLTRRLLQTERVQAAIQWLLKMALDQVQSETEQKSAQVLAHILHDLLGSAIPRLIRVWARREDFLEAQLNQIFDQVLLELKLSEEQAGRIADWLLQVVLPPDRLRQTLIDFLTDRNIQVIDEDLREKTSGTYWVVANLFGVRNTLIRLRDFCIEEREACNVRLAELMDALGVRQRLIEGLQDLSLQNLPVATVRQLRKVFRQNVRIYIQSQGLELVKGLSDSLNWEHVSLSILNRLRSSTAVTASLEVVSQELALVLERYLERDLEIIVEKAIPILNLDEVIVERVKATTPQELEAAIQGIVKSELQAIVTLGGVLGLLIGIAQSVLLLVQGGL", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0754 family."}
+{"protein": "MHSGILIRGRILGSRTANRDNNSPQHILGVGIQKADGFGGTTQDVEQVKIPDQLVQSGVVNQINSLIGKLCEVPINVRSWSMNGKNGTSYTLSFESGIQEIEELIYVR", "text": "FUNCTION: Binds to DNA in a highly cooperative manner without pronounced sequence specificity. During synthesis of the single- stranded (progeny) viral DNA, prevents the conversion into the double- stranded replicative form. G5P is displaced by the capsid protein G8P during phage assembly on the inner bacterial membrane (By similarity). SIMILARITY: Belongs to the inovirus G5P protein family."}
+{"protein": "IVGGDECNINEHRFLVALYDPDGFFC", "text": "FUNCTION: Thrombin-like snake venom serine protease that cleaves alpha- chain of fibrinogen (FGA) releases only fibrinopeptide A. Shows coagulant, esterase and amidase activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
+{"protein": "MFDFDATLPLMALQFVLLAIILNAIFYKPLNKALDERADYIRQNETGGQQQLAEAKELAAKYEQQLAQARKESQDIVAQAQAEAKQLATEAVAEAQKEAIAKKEAAAQEIEQQRQEALKTLEQQVDTLSRQILEKLLGPELVK", "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": "MAFAPMGPEASFFDVLDRHRESLLAALRRGGREPPTGGSRLASSSEVLASIENIIQDIITSLARNEAPAFTIDNRSSWENIKFEDSVGLQMVSHCTTRKIKSDSPKSAQKFSLILKILSMIYKLVQSNTYATKRDIYYTDSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGNLRYIEEDGTKVNCTCGATAVAVPSNIQGIRNLVTDAKFVLIVEKDATFQRLLDDNFCNKLSPCIMITGKGVPDLNTRLLVKKLWDTFHVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRLNVPKDSLIPLTKRDQMKLDSILRRPYVTCQPFWRKEMEIMADSKMKAEIQALTFLSSDYLSRVYLPNKLKFGGWI", "text": "FUNCTION: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with TOP6BL, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. Essential for the phosphorylation of SMC3, HORMAD1 and HORMAD2. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TOP6A family."}
+{"protein": "MLCSLLLCECLLLVAGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGISGEKDVSPDLSCADEISECYHKLDSLTYKIDECEKKKREDYESQSNPVFRRYLNKILIEAGKLGLPDENKGDMHYDAEIILKRETLLEIQKFLNGEDWKPGALDDALSDILINFKFHDFETWKWRFEDSFGVDPYNVLMVLLCLLCIVVLVATELWTYVRWYTQLRRVLIISFLFSLGWNWMYLYKLAFAQHQAEVAKMEPLNNVCAKKMDWTGSIWEWFRSSWTYKDDPCQKYYELLLVNPIWLVPPTKALAVTFTTFVTEPLKHIGKGTGEFIKALMKEIPALLHLPVLIIMALAILSFCYGAGKSVHVLRHIGGPESEPPQALRPRDRRRQEEIDYRPDGGAGDADFHYRGQMGPTEQGPYAKTYEGRREILRERDVDLRFQTGNKSPEVLRAFDVPDAEAREHPTVVPSHKSPVLDTKPKETGGILGEGTPKESSTESSQSAKPVSGQDTSGNTEGSPAAEKAQLKSEAAGSPDQGSTYSPARGVAGPRGQDPVSSPCG", "text": "FUNCTION: Seems to act as a chloride ion channel (PubMed:30157172). Plays a role in retina development (PubMed:30157172). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Nucleus membrane; Multi- pass membrane protein Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. SIMILARITY: Belongs to the chloride channel MCLC family."}
+{"protein": "MSDSPIGSSQQVEPEHRTPDLMDIDPLIANLKALHEETRSDDDDDGQPSTSAKRKDSRADGIVIHQKKYSDPGRFLWIWLLGVRVPALSIDGEPHLPIEILDDMLTKKDKKDQMSFQNLLRYKNVYIRMASPSQFRAVMEKSKECENLNITSLSLMSRSDIERIMGELRLESMLTLAEHDNWDISDRVHVVHVNFIDYCSEWLESDDLEEDVMQSGTHGYWYKNRRNMRCIECQHCEGKFTPTDFIMHHHYPIKPSGFVHTGCNSFQWIRLIEVFDKSNENLEAWNKFVLNSHRAGKREYDEAAPHQAPPKRPAMETPVPVAADNGWEADEEEEGEEIVDRDADIEKCKLRNKKKMENLHIADFLGPSGSKGLKPRNKFEAVIIEQLNKMDDAALEALFLKSPEEYNLWVKESDFTHKVVTQQQEWKAKMKDPNFKSRASANFDVSKGEFDNMRHFDNASKATRQEIQQLAEQFANLDRDAKLLTPMEFVLREHALLKNVSADAIRVLCNRPPLPPLPPPPPPPKPKPAPVQPISLGNINFVALAQQLIASGIKLPLPIVTPPVVSTPAPVITPIPAALPISPNSDFLKQQLSTAMSSPALLSLYPKLTAGAYEQLAQFIKTTTVKN", "text": "FUNCTION: Probable component of transcriptional regulatory complex with SMAD protein daf-3 (PubMed:14681186). Required to regulate entry into a developmentally arrested larval state known as dauer, in response to harsh environmental conditions (PubMed:14681186). Involved in larvae undergoing cell-cycle arrest during the dauer stage (PubMed:14681186). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SKI family."}
+{"protein": "MLPRRLLAAWLAGTRGGGLLALLANQCRFVTGLRVRRAQQIAQLYGRLYSESSRRVLLGRLWRRLHGRPGHASALMAALAGVFVWDEERIQEEELQRSINEMKRLEEMSNMFQSSGVQHHPPEPKAQTEGNEDSEGKEQRWEMVMDKKHFKLWRRPITGTHLYQYRVFGTYTDVTPRQFFNVQLDTEYRKKWDALVIKLEVIERDVVSGSEVLHWVTHFPYPMYSRDYVYVRRYSVDQENNMMVLVSRAVEHPSVPESPEFVRVRSYESQMVIRPHKSFDENGFDYLLTYSDNPQTVFPRYCVSWMVSSGMPDFLEKLHMATLKAKNMEIKVKDYISAKPLEMSSEAKATSQSSERKNEGSCGPARIEYA", "text": "FUNCTION: May play a protective role in mucosal tissues by preventing exaggerated allergic responses. SUBCELLULAR LOCATION: Mitochondrion."}
+{"protein": "MTDSVIRIKRYHYIHILDNNTNVTRTISGPVVYTRKEHETCLFDPCPCVSVPPRHYCVVKNPCVRGEAGEVVLESSGQVKLRLGDSEIRFEGEPFPLYPGEELDCRDGKGVQKLQLIPPNTGLHVRCVRDFKDADRRVGAGTEWMVAGPQTYIPRVEVVVVEEVKATVIYPNTALLVQANVNFTDRCGVPRVAGEKWLVRALGAYLKSVEETVLGLIQGTMLSDLKALRLSAVRSFTDVYGKARRAGEQWQVTLKDAPVHIVDAYETKVADVAAVSLSAKEYVIIHHPVDDTGHNRFGETLVRRGECTFFLQPGETMPRGVEQVLVVGKEEALLLEAVCEYRDGGEKRQPGSRWMVHGPLEYIPANEVKLLEHRRMMALDKNEGIYIMNTTTGEVRAVIGKPYMLDVNEVLWEKHLPLAVEELLESPNGSIQTSERNPGFVSHREKYRIVRFNVQHNAAVQIYDYRKKQPRIVLGPNLVMLAPHEEFTVLSLSGGTPKVPNSLQSLQLFLGPRFSSDTIVVETSDHARLRLRLSYNWYFDIDRANPSRRTFSVPDFIGDCCKTIASRVRGAVAAEDFDSFHRNSAKIIRTAVFGVDEAGETKKNLRFTANDFVVTNIDVQSSEPTDEKTRDSLQKSVQLAIEITTKSQEAAARHGNELKDQEAKGQLERQKLLDKIEVENARTKWLELQAKSEAVQASGQSVAEAKARAEALFIEVRSEMQQAEMRAKAYRISAEAELQKLQQRQALELEYTQRQNEIDVSKARAAAEAEAEKVKRMVDCIGRDTLVAIARAGPETQVKLLSSLGLKGYLITDGNSPVNLFGTAQGMIGEPKK", "text": "FUNCTION: Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MVTRETKLTSEREVESSMAQARHNGGGGGENHPFTSLGRQSSIYSLTLDEFQHALCENGKNFGSMNMDEFLVSIWNAEENNNNQQQAAAAAGSHSVPANHNGFNNNNNNGGEGGVGVFSGGSRGNEDANNKRGIANESSLPRQGSLTLPAPLCRKTVDEVWSEIHRGGGSGNGGDSNGRSSSSNGQNNAQNGGETAARQPTFGEMTLEDFLVKAGVVREHPTNPKPNPNPNQNQNPSSVIPAAAQQQLYGVFQGTGDPSFPGQAMGVGDPSGYAKRTGGGGYQQAPPVQAGVCYGGGVGFGAGGQQMGMVGPLSPVSSDGLGHGQVDNIGGQYGVDMGGLRGRKRVVDGPVEKVVERRQRRMIKNRESAARSRARKQAYTVELEAELNQLKEENAQLKHALAELERKRKQQYFESLKSRAQPKLPKSNGRLRTLMRNPSCPL", "text": "FUNCTION: Participates in ABA-regulated gene expression during seed development and subsequent vegetative stage by acting as the major mediator of ABA repression of growth. Binds to the embryo specification element and the ABA-responsive element (ABRE) of the Dc3 gene promoter and to the ABRE of the Em1 and Em6 genes promoters. Can also trans- activate its own promoter, suggesting that it is autoregulated. Plays a role in sugar-mediated senescence. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. ABI5 subfamily."}
+{"protein": "MTKKILLLLCKGFEVMEFTPFVDVMGWAREDDNNEDKADIQVVTCGLYNKMVTSTFGVKVQVDVLLGEVVKSLDEFDALAIPGGFENYSFYEEAYSEDVSQLIRDFDSKGKHIASVCVAALALGKSGILKGRNATTYRNSLREHSVRQQQLRDFGANVIADQSIVIDKNVITSYNPQTAPYVAFELLSRLSDENKAKKVKTLMGF", "text": "FUNCTION: Protects cells against oxidative stress and cell death. SIMILARITY: Belongs to the peptidase C56 family."}
+{"protein": "MEDINFASLAPRHGSRPFMGTWNEIGTSQLNGGAFSWSSLWSGIKNFGSSIKSFGNKAWNSNTGQMLRDKLKDQNFQQKVVDGLASGINGVVDIANQALQNQINQRLENSRQPPVALQQRPPPKVEEVEVEEKLPPLEVAPPLPSKGEKRPRPDLEETLVVESREPPSYEQALKEGASPYPMTKPIGSMARPVYGKESKPVTLELPPPVPTVPPMPAPTLGTAVSRPTAPTVAVATPARRPRGANWQSTLNSIVGLGVKSLKRRRCY", "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": "MAASALSTCLWMLVLGTCVSLVVGTDCGKECALCVYRLLGQQSTLSSLTCSLECDGGLDSQKLRLCQDVLLEEENQSPLASQQDQERVDAMMADEEDATSPEHQMAKKYGGFMKRYGGFMSRRSSASSLEEAGNQDEEQSIRTEILKILNAATEHGGEGDGQEAEAVKRYGGFMRRADRGAAQGNLVEAVLGRVLKKRYGGFMRRVGRPEWLVDSSKKVGVLKENGSELQKRHGGFMD", "text": "FUNCTION: Met-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. Enkephalin peptides found in Meiacanthus fangblennies induce physiological effects via their interaction with delta-type opioid receptors (OPRD1) (tested on M.grammistes). Therefore, finding a proenkephalin sequence in M.atrodorsalis venom suggests that this protein act in the same manner (Probable). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the opioid neuropeptide precursor family."}
+{"protein": "MSYKIMAINAGSSSLKFQLLEMPQGDMLCQGLIERIGMADAQVTIKTHSQKWQETVPVADHRDAVTLLLEKLLGYQIINSLRDIDGVGHRVAHGGEFFKDSTLVTDETLAQIERLAELAPLHNPVNALGIHVFRQLLPDAPSVAVFDTAFHQTLDEPAYIYPLPWHYYAELGIRRYGFHGTSHKYVSGVLAEKLGVPLSALRVICCHLGNGSSICAIKNGRSVNTSMGFTPQSGVMMGTRSGDIDPSILPWIAQRESKTPQQLNQLLNNESGLLGVSGVSSDYRDVEQAANTGNRQAKLALTLFAERIRATIGSYIMQMGGLDALVFTGGIGENSARARSAVCHNLQFLGLAVDEEKNQRNATFIQTENALVKVAVINTNEELMIAQDVMRIALPATEGLCVPA", "text": "FUNCTION: Works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of propionate and 1,2-propanediol (1,2-PD). Ectopic expression partially complements a cobB deletion allowing some growth on propionate (PubMed:12700259). Restores growth to an eutQ deletion on ethanolamine and tetrathionate under anoxic conditions (PubMed:26448059). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetokinase family. PduW subfamily."}
+{"protein": "MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGSSRESRGGWDSRDDFNSGFRDDFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE", "text": "FUNCTION: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region."}
+{"protein": "MLGLHVGTLISLFLCILLEPVEGSLMQPCQPINQTVSLEKEGCPTCLVIQTPICSGHCVTKEPVFKSPFSTVYQHVCTYRDVRYETIRLPDCPPWVDPHVTYPVALSCDCSLCNMDTSDCTIESLQPDFCITQRVLTDGDMW", "text": "FUNCTION: Involved in gametogenesis and steroidogenesis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family."}
+{"protein": "MPFNGYQTYYRIVGDRQSNKTPLVLLHGGPGSTHNYFEGFDDLAAQTGRPIVMYDQLGCGRSSIPDDDQLWQAAMWVAELRALRTYLDLPEIHLLGQSWGGMLAIIYGCDYRPQGIKSLILASTLSSARLWAQEQHRMIRLMSPVDQSAIATAERLQDFTGAAYLTANQHFMTQHASGPITADDPEFLRRSKRVGTTAYNVAWGPNEYNPTGTLADYEYTDRLQYLQMPTLVTSGTDDLCTPLVAKTMVDQLPHATWTLFPRSRHMAFIDENTAYMTRLRHWLAAHD", "text": "FUNCTION: Releases the N-terminal proline from various substrates. SUBCELLULAR LOCATION: Cell envelope. SIMILARITY: Belongs to the peptidase S33 family."}
+{"protein": "YPAKPEAPGEDASPEELSRYYASLRHYLNLVTRQRY", "text": "FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility. FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
+{"protein": "MRKRARIIYNPTSGKELFKRVLPDALIKLEKAGYETSAYATEKIGDATFEAERALESEYDLLIAAGGDGTLNEVVNGIAEQPNRPKLGVIPMGTVNDFGRALHLPSDIMGAIDVIIDGHTTKVDIGKMNNRYFINLAAGGKLTQVSYETPSKLKSIVGPFAYYIKGFEMLPQMKAVDVRIEYDDNIFQGEALLFLLGLTNSMAGFEKLVPDAKLDDGYFTLIIVEKANLAELGHIMTLASRGEHTKHPKVIYAKAKSINISSFTDMQLNVDGEYGGKLPANFLNLEQHIEIFTPKDVFNEELLENDTITDITPDKQ", "text": "FUNCTION: Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway. SIMILARITY: Belongs to the diacylglycerol/lipid kinase family."}
+{"protein": "MNNTLNQHYEEKVRPCIDLIDSLRSLGVEKDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLELKMKRKKEGEEWHGKISYQDHEEEIEDPSDVEKKIREAQDEMAGVGVGISDDLISLEIGSPDVPDLTLIDLPGIARVAVKGQPENIGEQIKRLIRKFIMKQETISLVVVPCNVDIATTEALKMAQEVDPEGERTLGILTKPDLVDKGTEETVVDIVHNEVIHLTKGYMIVKCRGQKEIMERVSLTEATEREKAFFKEHAHLSTLYDEGHATIPKLAEKLTLELVHHIEKSLPRLEEQIEAKLSETHAELERYGTGPPEDSAERLYFLIDKVTAFTQDAINLSTGEEMKSGVRLNVFSTLRKEFGKWKLHLERSGEIFNQRIEGEVDDYEKTYRGRELPGFINYKTFEVMVKDQIKQLEGPAVKKLKEISDAVRKVFLLLAQSSFTGFPNLLKSAKTKIEAIKQVNESTAESMLRTQFKMELIVYTQDSTYSHSLCERKREEDEDQPLTEIRSTIFSTDNHATLQEMMLHLKSYYWISSQRLADQIPMVIRYLVLQEFASQLQREMLQTLQEKDNIEQLLKEDIDIGSKRAALQSKLKRLMKARSYLVEF", "text": "FUNCTION: Does not inhibit strain RB-1 of the fish pathogen, infectious hematopoietic necrosis virus (IHNV). SUBCELLULAR LOCATION: Cytoplasm Note=Exhibits cytoplasmic staining in a large globular pattern surrounding the nucleus. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
+{"protein": "MDNNNACVLVDGHSAELKLRSSTIGPNVLGIGSLYEQTKMFTYDPGFTSTASCESSITFIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTAAQKKDFDYRVVHHTMVHEQMSRFFTGFRRDAHPMAVMCGCVGALSAFYHDSTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFAVPCEEYVVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANERALNMLTEIGTVDRIPEYIARAKDKNDPFRLMGFGHRVYKNYDPRAKIMQKTAHEVLGELGIKDDPLLDIAIELERIALTDDYFIEKKLYPNVDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPDQRIGRPRQLYTGAPLREYVPLSKR", "text": "FUNCTION: The exact function of the plasmid-encoded citrate synthase is not clear, it could help nodulation by allowing the bacteria to use citrate as a chelator of iron and calcium. SIMILARITY: Belongs to the citrate synthase family."}
+{"protein": "MNTPPFVCWIFCKVIDNFGDIGVSLRLARVLHRELGWQVHLWTDDVSALRALCPDLPDVPCVHQDIHVRTWHSDAADIDTAPVPDAVIETFACDLPENVLHIIRRHKPLWLNWEYLSAEESNERLHLMPSPQEGVQKYFWFMGFSEKSGGLIRERDYRDAVRFDTEALRQRLMLPEKNAPEWLLFGYRSDVWAKWLEMWQQAGSPMTLLLAGAQIIDSLKQSGIIPQNALQNDGDVFQTASVRLVKIPFVPQQDFDQLLHLADCAVIRGEDSFVRAQLAGKPFFWHIYPQDEHVHLDKLHAFWDKAHGFYTPETASAHRCLSDDLNGGEALSATQRLECWQILQQHQNGWRQGAGAWSRYLFGQPSASEKLAAFVSKHQKIR", "text": "FUNCTION: Protein-arginine rhamnosyltransferase that catalyzes the transfer of a single rhamnose to elongation factor P (EF-P) on 'Lys- 32', a modification required for EF-P-dependent rescue of polyproline stalled ribosomes. SIMILARITY: Belongs to the glycosyltransferase 104 family."}
+{"protein": "MIKLSNFVKKNQNVENYFISKEFIPFTTDKASFINLPNHNRHIGFWLSNKFIYSSEKHSEQVAIGLIYDNSYPIVKYDENLKRNIWKYLTGTELINLYNQYKQNYFTKMKKALFLSEPKKVKANNNNNNLTNWSVEKEEQLINDLESLN", "text": "SIMILARITY: Belongs to the plectrovirus ORF4 family."}
+{"protein": "MCSPLPLLILRLLLLTHPSLGRHLRHRESRKIHSVVVSTWNYTDANLQAWSVLKQGPRRTRQAVIQGCLACQNLRCGRLLGGSYGPDERGNLSLEAAIMDGRNQKFGAVAGMEGIRNAILVAEAVLQHTHHSLLVGKGATDFARVMGYKEEHAVNLNTKNVIGNWTFARCQPNFWRDVVPPPRTQCGPYSPLPQYLLQRPMRQEYPITQGEHDQLAFLALDSEGLIHVASYSSGARFRLRGRVGDSAVPGAGIYADNEVGGAIASGDGDVLMHHLPAFLAVEAMRAGQSPAKAAAKVIQRVLKHNTEFNGAVIAVNRWGTYAAACAGMDEFHFVVSGGKGFLRMARVERVKCQDRKDVVDGGPKGFFTRKPMKNRKIE", "text": "SIMILARITY: Belongs to the Ntn-hydrolase family."}
+{"protein": "MAAPKGNRFWEARSSHGRNPKFESPEALWAACCEYFEWVEANPLWEMKAFSYQGEVIQEPIAKMRAMTITGLTLFIDVTLETWRTYRLREDLSEVVTRAEQVIYDQKFSGAAADLLNANIIARDLGLKEQSQVEDVTPDKGDRDKRRSRIKELFNRGTGRDS", "text": "FUNCTION: The terminase small subunit binds to the packaging initiation site and regulates the ATPase activity of the terminase large subunit. 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 full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by neck proteins. SIMILARITY: Belongs to the P22likvirus small terminase family."}
+{"protein": "MKFTQRLSLRVRLTLIFLILASVTWLLSSFVAWKQTTDNVDELFDTQLMLFAKRLSTLDLNEINAADRMAQTPNKLKHGHVDDDALTFAIFTHDGRMVLNDGDNGEDIPYSYQREGFADGQLVGDKDQWRFVWMTSPDGKYRIVVGQEWEYREDMALAIVAGQLIPWLVALPVMLIIMMVLLGRELAPLNKLALALRMRDPDSEKPLNATGVPSEVRPLVESLNQLFARTHAMMVRERRFTSDAAHELRSPLTALKVQTEVAQLSDDDPQARKKALLQLHSGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSSVMDIYHTAQQAKIDVRLTLNVQGIKRTGQPLLLSLLVRNLLDNAVRYSPQGSVVDVTLNADNFIVRDNGPGVTPEALARIGERFYRPPGQTATGSGLGLSIVQRIAKLHGMNVEFGNAEQGGFEAKVSW", "text": "FUNCTION: Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MRPALFLCPVLISVLFLLSSLSLISGCNKALCASDVSKCLLQGLCQCRPQEGNCSCCKECMLCLSSLWEECCDCVGMCNPRSYNDSPATSKSTVEELYRPIPSLFRALTEGDAPINMMVVSFPVAEELSHHENLVSFLETLDSQSQNISLPTSSAQDDALCTVVYFDDCVSIRQCKQYCESMGGSKYRWFHNACCECIGPECLDYGSKTVKCMNCLI", "text": "FUNCTION: Involved in dorsal-ventral patterning. Appears to function predominantly as a ventralizing factor, through its actions as a BMP signaling agonist, acting through both chd-dependent and chd- independent mechanisms. May also antagonize BMP signaling, probably via formation of ternary complexes with chd and BMPs, resulting in dorsalization (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the twisted gastrulation protein family."}
+{"protein": "MAKYYLIHGVVEDKPEKIVKILSDGYLFASSYSTQQGFSGIPLDYVYFSRLGDVNVFMGGFKFILSTKILYKRSFRYALNWVGSDINRTTKINYRYDNVDKVLDEINTHITNGTYSLSPSIDTLHEIILKKKVNLHRYLVAVSDGNYLTPEITDYLKTNYPNVKILTEIPSSADKLSEILEK", "text": "SIMILARITY: Belongs to the mimivirus L28/L54 family."}
+{"protein": "MALPVSLLMALVVLSCHSSCSLGCDLPHTHSLGNTRVLMLLGQMRRISPFSCLKDRNDFGFPQEVFDGNQFRKPQAISAVHETIQQIFHLFSTDGSSAAWDESLLDKLYTGLYQQLTELEACLSQEVGVEETPLMNEDSLLAVRRYFQRIALYLQEKKYSPCAWEIVRAEIMRSFSSSTNLPQS", "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": "MSKAPVVFAIVVVLFFVELNAGGLPKSFLEALKMAKGDKVAESFIYKNRNDCMTNCKLLPTCPRLAPECCPTKTPECPK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-10 family."}
+{"protein": "MIRIDATPYPYQFHPRSTALVVIDMQRDFIEEGGFGSALGNDVRPLAAIVPTVAALLQLAREAGMLVVHTRESHLPDLSDCPRSKRLRGNPTLGIGDVGPMGRILVQGEPGNQILPQLAPVEGELVIDKPGKGAFYATDLHAQLQERRITHLLVAGVTTEVCVQTSMREANDRGYECLVIEDACASYFPDFHRITLEMLTAQGGIVGWRTPLAQLQAGVAAYTGENP", "text": "FUNCTION: Involved in the degradation of triuret (carbonyldiurea), an impurity in agricultural urea fertilizer, and an intermediate of uric acid oxidation endogenously found in human urine and in prokaryotic metabolism. Catalyzes the hydrolysis of triuret to 1-carboxybiuret and ammonia. The product, carboxybiuret, channels into biuret metabolism and is spontaneously decarboxylated to biuret. Extremely specific for triuret with four, three and two orders of magnitude less activity with biuret, 1-nitrobiuret and formylurea, respectively. No activity with tetrauret, pentauret or nonplanar compounds methylene diurea or succinamide. SIMILARITY: Belongs to the isochorismatase family."}
+{"protein": "MTAIRPGSVTFENVTKKFGNFTALPNLSLTVEPGTLVTLLGPSGCGKTTTLRLLAGLEHPTSGRILVGGKDVTNLPANERDVSMVFQSYALFPHMTSLENVAYGLESSGFKKNEARERAEEGLKLVGLGGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTADYVTHDQDEALAVSDTIIVMKEGGIAQKGSPRDLYEAPASAFIADFMGEANVVPCEVISAENGEAVIRVAGLTHRVPARNAQPRPAQLAIRPNAVTLQPQAGGGFSGTVAHSAYLGDHIEYEIETEHGKLFIVDPAVEQSLPLQTDVSIQFKTRGLAIINQ", "text": "FUNCTION: Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Fe(3+) ion importer (TC 3.A.1.10) family."}
+{"protein": "MSNSLSSQIFTRKMLICAFTGFNSGLPLFVLSQMLPVWLTDKHLSIELIGAVTGVMLPYGLKFLWAPLLDRYFPSFLGRRRSWMLLSQVALLILLYIISLFDPLTQLGTVANIALLIAFFSATQDIVLDAYRREILSDHELGLGNTIHINAYRIAGLIPGGLSLYLAAIYPWETVFLWTALCMLAGIFMTLFLAKEPKIDMQQTNQPFYQAFWIPLQEFFQRKGVIQAIGFLLFLFLYKFGDSFATTLQTKFIYDMGFSKEDIAIVVKSTALWSSILSGLAGGMIMLKLGINRALWLFGLVQMVTIGGFIWLAAFGHFDVITSAELWKLGVVIAAEYIGVGLGTAAFVAFMARESNPLYTATQLALFTSLSALPSKVLGILSGYVVGAVGYYQYFWFCLFLAIPGMLCLFWVAPLKQENNKTSSV", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: To E.coli AmpG and yeast YBR220c."}
+{"protein": "MASALAASTAVCSSPLASASASASSARRLRAVPPSRGIRYQALRADSGFAGNRRGGGRGASVVCAVQGQDTSIQVPEVTKSTWQSLVMESELPVLVGYWATWCGPCKMIDPVVGKLSKEYEGKLKCYKLNTDENPDIASQYGVRSIPTMMIFKNGEKKDAVIGAVPESTLIASIEKFVER", "text": "FUNCTION: Probable thiol-disulfide oxidoreductase that may be involved in the redox regulation of chloroplastic enzymes. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily."}
+{"protein": "MYVRHLGLRDFRSWAHADLELQPGRTVFIGSNGFGKTNLLEALWYSSTLGSHRVGTDAPLIRAGADRAVVSTIVVNDGRECAVDLEIAAGRANKARLNRSPVRSTREVLGVLRAVLFAPEDLALVRGDPSERRRYLDDLATLRRPAIAAVRADYDKVLRQRTALLKSLSGARHRGDRGALDTLDVWDSRLAEYGAQLMAARIDLVNQLAPEVEKAYQLLAPGSRAASIGYRSSLGAAASAEVNAGDRDYLEAALLAGLAAHRDAELERGMCLVGPHRDDLELWLGEQVAKGFASHGESWSLALSLRLAAFELLRADESDPVLLLDDVFAELDAARRRALAAVAESAEQVLVTAAVLEDIPTGWQARRLFVELRDTDAGRVSELRP", "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": "MSNKVHVGSLEMEEGLSKTKWMVLEPSEKIKKIPKRLWNVGKEDPRRVIHALKVGLSLTLVSLLYLMEPLFKGIGSNAIWAVMTVVVVLEFSAGATLCKGLNRGLGTLIAGSLAFFIEFVANDSGKVLRAIFIGTAVFIIGAAATYIRFIPYIKKNYDYGVVIFLLTFNLITVSSYRVDSVINIAHDRFYTIAVGCGICLFMSLLVFPIWSGEDLHKTTVGKLQGLSRSIEACVDEYFEEKEKEKTDSKDRIYEGYQAVLDSKSTDETLALYANWEPRHTLRCHRFPCQQYVKVGAVLRQFGYTVVALHGCLQTEIQTPRSVRALFKDPCVRLAGEVCKALTELADSISNHRHCSPEILSDHLHVALQDLNSAIKSQPKLFLGSNLHRHNNKHQNGSISNNKHHQRNSSNSGKDLNGDVSLQNTETGTRKITETGSRQGQNGAVSLSSFRTDTSALMEYRRSFKNSNSEMSAAGERRMLRPQLSKIAVMTSLEFSEALPFAAFASLLVEMVARLDNVIEEVEELGRIASFKEYDNKRDQTADDVRCENPANVTISVGAAE", "text": "FUNCTION: Malate-sensitive anion transporter permeable to chloride, nitrate, sulfate and malate. Involved in dark-, CO(2)-, abscisic acid- and water-deficient-induced stomatal closure. Belongs to the R- type anion channels. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=PubMed:20626656 indicates also a not confirmed endomembrane localization. SIMILARITY: Belongs to the aromatic acid exporter (TC 2.A.85) family."}
+{"protein": "MSFRGGGRGGFNRGGGGGGFNRGGGSNNHFRGGGGGGGGGGNFRGGGRGGFGRGGGRGGFNKFQDQGPPERVVLLGEFMHPCEDDIVCKCTTEENKVPYFNAPVYLENKEQIGKVDEIFGQLRDFYFSVKLSENMKASSFKKLQKFYIDPYKLLPLQRFLPRPPGEKGPPRGGGGGGGGGRGGRGGGRGGGGRGGGRGGGFRGGRGGGGGFRGGRGGGGGFRGRGH", "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": "MSMHFRNKAWIILAILCFSSLIHSTEAVVTYDHKALIINGQRRILISGSIHYPRSTPEMWPDLIKKAKEGGLDVIQTYVFWNGHEPSPGNYYFQDRYDLVKFTKLVHQAGLYLDLRIGPYVCAEWNFGGFPVWLKYVPGMVFRTDNEPFKIAMQKFTKKIVDMMKEEKLFETQGGPIILSQIENEYGPMQWEMGAAGKAYSKWTAEMALGLSTGVPWIMCKQEDAPYPIIDTCNGFYCEGFKPNSDNKPKLWTENWTGWFTEFGGAIPNRPVEDIAFSVARFIQNGGSFMNYYMYYGGTNFDRTAGVFIATSYDYDAPIDEYGLLREPKYSHLKELHKVIKLCEPALVSVDPTITSLGDKQEIHVFKSKTSCAAFLSNYDTSSAARVMFRGFPYDLPPWSVSILPDCKTEYYNTAKIRAPTILMKMIPTSTKFSWESYNEGSPSSNEAGTFVKDGLVEQISMTRDKTDYFWYFTDITIGSDESFLKTGDNPLLTIFSAGHALHVFVNGLLAGTSYGALSNSKLTFSQNIKLSVGINKLALLSTAVGLPNAGVHYETWNTGILGPVTLKGVNSGTWDMSKWKWSYKIGLRGEAMSLHTLAGSSAVKWWIKGFVVKKQPLTWYKSSFDTPRGNEPLALDMNTMGKGQVWVNGHNIGRHWPAYTARGNCGRCNYAGIYNEKKCLSHCGEPSQRWYHVPRSWLKPFGNLLVIFEEWGGDPSGISLVKRTAK", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
+{"protein": "MISLTPSLFLNKTVVPGCSTRLSLRQPRTIITPPASLRVFSSLGSNQDPTGSVLIETTATSSSSLETSAADIVPKSTVSGGVQDVYGEDAATEDMPITPWSLSVASGYTLLRDPHHNKGLAFSHRERDAHYLRGLLPPTVISQDLQVKKIMHTLRQYQVPLQKYMAMMDLQETNERLFYKLLIDHVEELLPVIYTPTVGEACQKYGSIFLRPQGLFISLKEKGKIHEVLRNWPEKNIQVIVVTDGERILGLGDLGCQGMGIPVGKLSLYTALGGVRPSACLPVTIDVGTNNEKLLNDEFYIGLRQRRATGEEYSELMHEFMTAVKQNYGEKVVIQFEDFANHNAFDLLAKYGTTHLVFNDDIQGTASVVLAGLIAALRFVGGSLSDHRFLFLGAGEAGTGIAELIALEISKKSHIPLEEARKNIWLVDSKGLIVSSRKESIQHFKKPWAHDHEPIRELVDAVKAIKPTVLIGTSGVGQTFTQDVVETMAKLNEKPIILSLSNPTSQSECTAEEAYTWSQGRAIFASGSPFAPVEYEGKTFVPGQANNAYIFPGFGLGLIMSGTIRVHDDMLLAASEALAEELMEEHYEKGMIYPPFRNIRKISARIAAKVAAKAYELGLATRLPQPKELEQCAESSMYSPSYRSYR", "text": "FUNCTION: The chloroplastic ME isoform decarboxylates malate shuttled from neighboring mesophyll cells. The CO(2) released is then refixed by ribulose-bisphosphate carboxylase. This pathway eliminates the photorespiratory loss of CO(2) that occurs in most plants (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the malic enzymes family."}
+{"protein": "MRKFDLSLRSSRSSYFATFRHQLTILSKTDALDEEKWLNMLGTFVKDWFRYESHFVHGRDSLVDILKERGLLSESDAVQPLIGKKS", "text": "FUNCTION: Plays a central role in the packaging of viral DNA into phage procapsid, which occurs in the late stage of infection. The protein C can interact with the replicative complex composed of the protein A, the host rep and the viral DNA after the completion of one round of DNA synthesis. When protein C is bound to the replicative form, the complex becomes accessible to procapsid and serves as a DNA packaging apparatus. FUNCTION: C protein is one of the proteins involved in the production and packaging of viral single-stranded DNA. SIMILARITY: Belongs to the microviridae C protein family."}
+{"protein": "MQDPNADTEWNDILRKKGILPPKETPVEEEEDEQLHLQSQSVVKTYEDMTLEELEENEDEFSEEDEHAMEMYRLKRLAEWKANQMKNVFGELKEISGQDYVQEVNKAGEGIWVVLHLYKQGIPLCSLINQHLAQLARKFPQSKFLKSISSTCIPNYPDRNLPTLFVYRDGEMKAQFIGPLVFGGMNLTCDELEWRLSESGAVKTDLEENPRKQIQDQLMTSIRCSANTHRDGEEDSDED", "text": "FUNCTION: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (PubMed:26059764). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Endoplasmic reticulum. SIMILARITY: Belongs to the phosducin family."}
+{"protein": "MTKLCLLLLPLVFLVSYSFAEEEITISISPNANPVQKPIGHQISLVCSIKKTDSNGEKPGMIWKKHGGLDRTGNVEVKKLDDYTLGLIIRNSSVEDSGVYYCQAQVGSKVYMNKMDVIVFEDIVFRDKQLHFGQVLATASVNISCEVSAKKDSVITYWTRHGKQILEGGKHKFYSRGSILEIQNYQPEQDAGQYTCEVFHVSSGSSNTKTVTLGTTGEKNYVACQQMCNSFCTDVHNKVFTNN", "text": "FUNCTION: Probably not involved in maintaining the position of ASI and ASH head neuron cell bodies and ventral nerve cord axons of PVQ, PVP, RMEV, AVK and HSN neurons. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSTATTTVTTSDQASHPTKIYCSGLQCGRETSSQMKCPVCLKQGIVSIFCDTSCYENNYKAHKALHNAKDGLEGAYDPFPKFKYSGKVKASYPLTPRRYVPEDIPKPDWAANGLPVSEQRNDRLNNIPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKEGDIVNLDVSLYYQGYHADLNETYYVGENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEHGVEILTARNKKSPGGPRQRIK", "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). Plays the major role in N- terminal methionine removal. Less efficient when the second residue is Val. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily."}
+{"protein": "MFVDKTLLITGGTGSFGNAVLSRFLKNDIIKDIKEIRIFSRDEKKQEDMRIALNNPKIKFYIGDVRNYNSIDDAMKGVDYVFHAAALKQVPTCEFYPMEAINTNILGAENVLRAATINKVAKVIVLSTDKAVYPINAMGLSKALMEKLAIAKARMNVRDKTVFCVTRYGNVMASRGSVIPLFINQIKQNKDLTITEPSMTRFLMSLVDSVDLVLYAFEYGHQGDIFVQKSPASTIEVLAKALQGIFNSKNKIRFIGTRHGEKHYESLVSSEEMAKAEDLGNYYRIPMDGRDLNYAKYFVEGEKKIALLEDYTSHNTKRLNLEEVKELLLNLDYVQEELKNA", "text": "FUNCTION: Epimerizes UDP-galactose to UDP-glucose. SIMILARITY: Belongs to the polysaccharide synthase family."}
+{"protein": "MDEQAGPGVFFSNNHPGAGGAKGLGPLAEAAAAGDGAAAAGAARAQYSLPGILHFLQHEWARFEVERAQWEVERAELQAQIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDMKPPSYDSDEGNETEVQPQQNSQFMWKQGRQLLRQYLQEVGYTDTILDVKSKRVRALLGFSSDVTDREDDKNQDSVINGTEAEVKETAMIGKSELTDSASVLDNFKFLENAAADFSDEDEDEDIDGREKSVIDTSTIVRKKPLPDTSEDRDTKEALKEFDFLVASEEGDNESRSAGDGTDWEKEDQCLTPERWNVDQGVITRLKEQYKKERKGKKGVKRPNRSKLQDMLANLRDVDELPSLQPSVGSPSRPSSSRLPEQDISRADEVEALTFPPSSGKSFIMGADEALESELGLGELAGLTVANEADSLAYDIANNKDALRKTWNPKFTLRSHFDGIRALAFHPIEPVLITASEDHTLKMWNLQKTAPAKKSTSLDVEPIYTFRAHKGPVLCVVMSSNGEQCYSGGTDGLIQSWSTTNPNVDPYDSYDPSVLRGPLLGHTDAVWGLAYSAAHQRLLSCSADGTLRLWTTTEVAPALTVFNDNQELGIPASVDLVSSDPSHMVASFSKGYTSIFNMETQQRILTLESNVDSTASSSCQINRVISHPTLPISITAHEDRHIKFYDNNTGKLIHSMVAHLEAVTSLAVDPNGLYLMSGSHDCSIRLWNLESKTCIQEFTAHRKKFEESIHDVAFHPSKCYIASAGADALAKVFV", "text": "FUNCTION: Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Cell projection, dendritic spine Note=CTTNBP2-binding may regulate dendritic spine distribution. SIMILARITY: Belongs to the WD repeat striatin family."}
+{"protein": "MTEGKSSDKPAKRLLALNPKEDAEFQKKVQQVKKRPQTGQTLSPGVLYVGHLPRGLFEPQLKSYFEQFGKVLRLRVSRSKKTGGSKGYGFVEFECDEVAKIVAETMNNYLMGERIIKCHVIPPEKVHEKLFVGSIAGFKKPKYPAVTRYNKTHTEDDVKKVGTKLLSKESKLRKRLAAKGIDYDFPGFAAQIPAKKAPSEANVSVCSEDVTPVCTPSLLERRKSLRVEDDDVDDEIVIKVKPLPENSDDVEESEEESAEEDEGEEEEAA", "text": "FUNCTION: Plays an essential role in early embryonic development. SUBCELLULAR LOCATION: Nucleus, nucleolus."}
+{"protein": "MKVLDQSLLWMLLPFFHLIASAAEHEEVAKHAIKLHRGKGATATQRKQWALDSCRRLTGLLRQKNVVLNKLKNAIRAVEKDTSLSGEEKLFQVHTFEIFQKELNESENSIFQAIYGLQRALQGDYRDVVNMKESSKQRLEALREAAIKEETEYVELLAAEKHQVEALKNMQHQNKSLSMLDEILEDVRKAADRLEEEIEEHAFDDNKSVKGVNFEAVLRVEEEEASSKQNMTKREVEDGLGLSMLIDSQNNQYILTKPRDSTIPRADHHFIKDIVTIGMLSLPCGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKLRKVWRISLQGPCYMTLLMIAFGLWWGHLLRIRPTQSVFISTCLSLSSTPLVSRFLVGSARGDKEAGDIDYSTVLLGMLVMQDVQLGLFIAVMPTLIQAGAGASSSVVMEVLRILFLIGQILFSLAAVFLLCLVMKTYLIGPYYRKLHLESKGNKEILVLGVSAFTFLMLTVTELLDVSMELGCFLAGALVSSQGHMVTEEIMTYIEPIRDFLAIIFFASIGLHVFPTFVIYELTVLVFLTLSVVIMKFVLAVLVLSLILPRSSQYIKWIVSAGLAQVSEFSFVLGSRARRAGILSREVYLLILSVTTLSLLLAPVLWKAAITKCVPRPERRSSL", "text": "FUNCTION: Probable 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": "MEKYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDLLFGTIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFYGQEVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAYGIDGKVNYALEGSIFVSGSAIQWLRDGLRMINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAFLAGLAVGFWESKDDIAKNWKLEEKFDPKMDEGEREKLYRGWKKAVEATQVFKTE", "text": "FUNCTION: Key enzsyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate (By similarity). 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": "MPTRRGCSGPCHFLASAFVLLLLPALNQSVVLPSTVPRAVQESKPLEPGPRTLSPLPPGPTAAQPRGQAQSEGAGPRGAESRNGSIPGAASEADGPEGKAGESSLGGSLAVSPNPSDKPMTQRALTVLVVVSAAVLVYFVVRTVRMRRRNRKTRRYGVLDTNIENMELTPLEQDDEDDDNTLFDANHPRR", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the FAM174 family."}
+{"protein": "MHLQRNFFILIFFFISFLLWKTWQQKEFSSDVHKIINKYENVNLVNNNINKLASNIIIKTDVLKIQVNLYGGDIEKAELLHFKSKLNSSQSLVLLDTNENFVYQAQCGITGKDGADNLQKHIRPLYIAKRKYYELSRHNKKIEVPLQWISKDGIIYKKIFVLKSGEYDVSVKYKINNITNKHLKVSMFGQLKQTINLPEDKNTYTNNFALQTFRGAAYSSDNDKYVKYSFDSIVNKEKKNIVVTHSGWVAMLQKYFATSWIPDNSYLNTMYIGSSGDNLAEIGYYSRPIDIFPHSTISLSSKLWIGPEIQNKMAVIASNLDLTVDYGWLWFLSQPLFKLLNFLYNICGNWGVSIILITFIIKGITFPLTKSQFKTMAKIRKLQPKINYIKKKFKNNNQKISEEIMSLYKTEKVNPLGGCFPLFIQMPIFLALYYMLISSVELRHAPFFLWIHDLSDQDPFYVLPILMGVTMFFIQRVTPSNVTDPVQKKIMNYIPILFTVFFLWFPSGLVLYYLISNLVTIIQQKIIIKALNKTLK", "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": "MAAILARKSLSALRSRQLVLAGHTIEGTNGYNRTLLGTRSFATKHSFSTDKDDEEREQLAKELSKDWNSVFERSINTLFLTEMVRGLMLTLKYFFEKKVTINYPFEKGPLSPRFRGEHALRRYATGEERCIACKLCEAICPAQAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAENLRSESLYR", "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). May donate electrons to ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 23 kDa subunit family."}
+{"protein": "MSWVQVNLLVRSLSRGWGGLCRPALSGTPFAQVSLQALRGLHCSAATHKDEPWLVPRPPEPQRKPIKVPAMHEDLFKPSGNRERDKASFLNAVRSFGAHNVRKRGHVDFIYLALRKMPEFGVERDLSVYNLLLDVFPKEVFRPRNVIQRIFVHYPRQQECGVAVLEQMERHGVMPSAETEFLLIQIFGRKSYPMLKFLRMKLWFTRFKNINPYPVPRDLPQDPLDLAKLGLRHMEPDLSAKVTVYQMSLPSDSTGMEDPTQPHIVGIQSPDQQAALARHNPSRPVFVEGPFPLWLRNKCVYYHILRADLPPPEEEKVEEIPEEWELYYPQKLDLEYSRSGWDDYEFDVDEVTEGPVFAMCMAGAHDQATLIKWIQGLQETNPTLAQIPVVFRLARSTGELLTTSRLEGQSPPHSPPKGPEEDDETIQAEQQQGQS", "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 (PubMed:10465784). 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 (PubMed:14633973). Required for normal embryonic development (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion. SIMILARITY: Belongs to the ECSIT family."}
+{"protein": "MGNCLYPVADDNSTKLAIKEDLLIDFPEDYYPDYNETDVEAAAPCHSCSLLNYSSLPFFILVSILGILASGTILYALLRPLFRWQLYQDRSTLVQLAVGSALFSIVVPILARGLSGALITSLCHLAHLVAYGSAFAQALLIGYHACLGPQLGAGQVPGLRLGVTVGLWGVAALLSLPVVLGSDTSQGLCTVTFSGEWETLRYIHAAACFAIFVLLPLGLLGTKGLKTVLGRAPCPWVDVLWVWFIFWWPQGMTLGLDSLVRSKAIVVSTCPAQQALDMLLDVAEALAILHCVATPLLLAWVCYQATHTSPPSLPLPTTQTSHLDTLGSKS", "text": "FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Has a promiscuous chemokine- binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1 and TARC. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels (By similarity). SUBCELLULAR LOCATION: Early endosome Recycling endosome Membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via caveolae. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Atypical chemokine receptor subfamily."}
+{"protein": "MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYREQAERLIGEVKKMFNSMSSEDGELINPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGLRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIRSVLSLYRASLIAFPGEKVMEEAEIFSAKYLEEALQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFGRHRHVEYYTLASCIAFEPQHSGFRLGFAKTCHIITILDDMYDTFGTVDELELFTAAMKRWNPSAADCLPEYMKGMYMIVYDTVNEICQEAEKAQGRNTLDYARQAWDEYLDSYMQEAKWIVTGYLPTFAEYYENGKVSSGHRTAALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGVTEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYEYKYRDGYSVANIETKSLVKRTVIDPVTL", "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 (1S,5S)-beta-pinene (PubMed:21385377). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
+{"protein": "MKHLTEMVRQHKAGKTNGIYAVCSAHPLVLEAAIRYASANQTPLLIEATSNQVDQFGGYTGMTPADFRGFVCQLADSLNFPQDALILGGDHLGPNRWQNLPAAQAMANADDLIKSYVAAGFKKIHLDCSMSCQDDPIPLTDDIVAERAARLAKVAEETCLEHFGEADLEYVIGTEVPVPGGAHETLSELAVTTPDAARATLEAHRHAFEKQGLNAIWPRIIALVVQPGVEFDHTNVIDYQPAKATXLSQMXENYETLIFEAHSTDYQTPQSLRQLVIDHFAILKVGPALTFALREALFSLAAIEEELVPAKACSGLRQVLENVMLDRPEYWQSHYHGDGNARRLARGYSYSDRVRYYWPDSQIDDAFAHLVRNLADSPIPLPLISQYLPLQYVKVRSGELQPTPRELIINHIQDILAQYHTACEGQ", "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": "MARQKMFYNKLLGMLSVGFGFAWALENITIYEFDFGKGILDQSYGGVFSNNGPSQVQLRDAVLMNGTVVYDSNGAWDSSALEEWLQGQKKVSIEKIFENIGPSAVYPSISPGVVIASPSQTHPDYFYQWIRDSALTINSIVSHSAGPAIETLLQYLNVSFHLQRSNNTLGAGIGYTNDTVALGDPKWNVDNTAFTEDWGRPQNDGPALRSIAILKIIDYIKQSGTDLGAKYPFQSTADIFDDIVRWDLRFIIDHWNSSGFDLWEEVNGMHFFTLLVQLSAVDKSLSYFNASERSSPFVEELRQTRRDISKFLVDPANGFINGKYNYIVGTPMIADTLRSGLDISTLLAANTVHDAPSASHLPFDINDPAVLNTLHHLMLHMRSIYPINDSSKNATGIALGRYPEDVYDGYGFGEGNPWVLATCTASTTLYQLIYRHISEQHDLVVPMNNDCSNAFWSELVFSNLTTLGNDEGYLILEFNTPAFNQTIQKIFQLADSFLVKLKAHVGTDGELSEQFNKYTGFMQGAQHLTWSYTSFWDAYQIRQEVLQSL", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 15 family."}
+{"protein": "MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQTTETVGLVVGDVSDPFFGAMVKAVEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDADLASLMKQMPGMVLINRILPGFENRCIALDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIAANDRLVTFGEPDESGGEQAMTELLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLPEITNVFSPTLVRRHSVSTPSLEASHHATSD", "text": "FUNCTION: Repressor of the galactose operon. Binds galactose as an inducer."}
+{"protein": "MSAKSRRPGTGSSQTPNECVQVVVRCRPMSNRERSERSPEVVNVYPNRGVVELQNVVDGNKEQRKVFTYDAAYDASATQTTLYHEVVFPLVSSVLEGFNGCIFAYGQTGTGKTFTMEGVRGNDELMGIIPRTFEQIWLHINRTENFQFLVDVSYLEIYMEELRDLLKPNSKHLEVRERGSGVYVPNLHAINCKSVEDMIKVMQVGNKNRTVGFTNMNEHSSRSHAIFMIKIEMCDTETNTIKVGKLNLIDLAGSERQSKTGASAERLKEASKINLALSSLGNVISALAESSPHVPYRDSKLTRLLQDSLGGNSKTIMIANIGPSNYNYNETLTTLRYASRAKSIQNQPIKNEDPQDAKLKEYQEEIERLKRLIGPQQQQRSEKQVTAKKQRVKKPKKETVTKEMSDSLQVSTIEQPVEDDSDPEGAESESDKENEAEVAKSNEELERERVENSKLAAKLAELEGQLVRGGKNLLDTYSERQIELEKKLVEIAERKKREIEIQQQLELQEETTLEIRERNVSLEQEVELKKRKLSKCYAKYLALQQELNDCKSDHNQDLRELEMAQNELVKELKRQLLIIDNFVPIEVKQRLYTQAKYDEEQEEWKFSSMSLPTPPGGDGKFSSKRPVSHPQRRRPTSEYALQEAKSNSPSSLRFKSENIVNYELEMPCRTTQEYRTPKVSASLQAVLAQAMQTGGDDIDIVDSHTNSLRSRLENIINANANGGAGPGAGVAVGSSIPNVRNIKSSRGLPSAASNLDSNRRPPTGRLPAKKPASAYPKARGLVNK", "text": "FUNCTION: Plus-end directed microtubule motor that may be used for anterograde axonal transport and could conceivably move cargos in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin II subfamily."}
+{"protein": "MGNGMCSRKQKRIFQTLLLLTVVFGFLYGAMLYYELQTQLRKAEAVALKYQQHQESLSAQLQVVYEHRSRLEKSLQKERLEHKKAKEDFLVYKLEAQETLNKGRQDSNSRYSALNVQHQMLKSQHEELKKQHSDLEEEHRKQGEDFSRTFNDHKQKYLQLQQEKEQELSKLKETVYNLREENRQLRKAHQDIHTQLQDVKQQHKNLLSEHEQLVVTLEDHKSALAAAQTQVAEYKQLKDTLNRIPSLRKPDPAEQQNVTQVAHSPQGYNTAREKPTREVQEVSRNNDVWQNHEAVPGRAEDTKLYAPTHKEAEFQAPPEPIQQEVERREPEEHQVEEEHRKALEEEEMEQVGQAEHLEEEHDPSPEEQDREWKEQHEQREAANLLEGHARAEVYPSAKPMIKFQSPYEEQLEQQRLAVQQVEEAQQLREHQEALHQQRLQGHLLRQQEQQQQQVAREMALQRQAELEEGRPQHQEQLRQQAHYDAMDNDIVQGAEDQGIQGEEGAYERDNQHQDEAEGDPGNRHEPREQGPREADPESEADRAAVEDINPADDPNNQGEDEFEEAEQVREENLPDENEEQKQSNQKQENTEVEEHLVMAGNPDQQEDNVDEQYQEEAEEEVQEDLTEEKKRELEHNAEETYGENDENTDDKNNDGEEQEVRDDNRPKGREEHYEEEEEEEEDGAAVAEKSHRRAEM", "text": "FUNCTION: Plays a role in endosome to Golgi protein trafficking; mediates protein transport along the late endosome-bypass pathway from the early endosome to the Golgi. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single- pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein. Membrane; Lipid-anchor Note=Localizes to cis and medial Golgi cisternae. Probably cycles between early Golgi and distal compartments like endosome. SIMILARITY: Belongs to the GOLIM4 family."}
+{"protein": "MPRVTISITAPGTPSDGELLTLELPPGSTVKDLKGFIEAETNLPAASQGIYLNGQPVSQETQTLENVGIRDGEMLAVIVRQNRQQPQQPAASRPAPVGQSDPEAVRQQVLRNPQVQAELRQRDPELLAIMNDADRWREAFASRQNSAQNAERERQNQIALLNEDPFNVEAQRKIEDIIRQERVVENLEKAYNENPEVFVRVHMLYINTEVNGVPVKAFVDSGAQATIMSPDCAERCGIMRLMDTRYAGMARGVGTARILGRVHHAEIKIGGAVMPCAFTVMEGKDVDLLFGLDMLKRYKAKIDLEKNALCFESIEVPFLHESEIPRNLDEAEMNEPTVAGPNGTEIGARSGAVRPAGGSAAVEPSTQAGPSAAGPSSASTPAPAPAQTAPAPSAPGPSTASSFPEEHINQLMSMFGVARQEAIQALEIASGNVDEAASVFLG", "text": "FUNCTION: Probable aspartic protease. May be involved in the regulation of exocytosis. Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DDI1 family."}
+{"protein": "MLRNSNKLIKSVIKNESTLLKCKNNNQRVVNYSSSSTSITSGNGIYSQIKKIEEFVSKKPSVTKVSSSSATINFNTSKSGSTNTTAVDYSKSVKIKDQKQIVLVKIGGGVIESDISSLIGSLNFLKKIGLFPIVVHGGGPQLNAELAAAGEPAEYVEGLRVTPPSVLAIAQRVFLRENLKIVEALESSGTKARPVTQGVYQATPLDPKLYGFVGNVTKIHTDALASCITNDYVPVISSLAMTPEGQVLNINADVAALELAKSINPLKILFINTTAGMKDGDGKVMQHIKLDEQYADLMKQPWVKHGTKLKLKEFKSCLDVLPPSTSITITSPDLLMKELFAKDGSGTTVERGEVMHSHESPSFDETKFFALIEKSTGTKGGRIDYQQLKTDLSKGVVKAFVNSHYTAGILVRPLSSGSSVSYVDQFFFFNNSIQSTEDSESVFKKMFENSSYIWKESSNNQLNNEWFKKIATGFITGATNNIFWTNIDTNKIENSIKECLSQSSTYLSGITKAASSKSASEKLLQDKNHKFRVGLIGARGFTGGNLVRLIDGHPNLELAIASSSTNFGKPITTEFPQLKSNLKFDNVKPENIDIFTRDHGIDGWFMALPDKISSPYIQTLENSSESPVLVDLSSDHRFNEKWTYGQPETNRAAIKESKLIANPGCYATGMFLTLKPFVNDLVTPPSCFGISGYSGAGSKPSEKNDPTRLSDNILPYKLVQHTHELEVSHQLGSPIYFMPHVGQFFQGITLTISMELKYPMTKEQVVERYQKFYQNEPLIKIDKDGIPEVKSNSGKHTVTIGGFAVNGNHLVVVTTLDNLLKGAATQALQNMNICLGLDELASIKNEL", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: In the N-terminal section; belongs to the acetylglutamate kinase family. SIMILARITY: In the C-terminal section; belongs to the NAGSA dehydrogenase family."}
+{"protein": "MSMSANTMIFMILGASIVMAIACLMDMNALLDRFHNYILPHLRGEDRVCHCNCGRHHIHYVIPYDGDQSVVDASENYFVTDNVTKQEIDLMLGLLLGFCISWFLVWMDGVLHCAVRAWRAGRRYDGSWTWLPKLCSLRELGRRPHRPFEEPTGNMVHVKQKLYHNGHPSPRHL", "text": "SUBCELLULAR LOCATION: Synapse Cell membrane; Multi-pass membrane protein."}
+{"protein": "MIPMKRERMLTIRVTDDEHARLLERCEGKQLAVWMRRVCLGEPVARSGKLPTLAPPLLRQLAAIGNNLNQTARKVNSGQWSSGDRVQVVAALMAIGDELRRLRLAVREQGARDDS", "text": "FUNCTION: Required for efficient mobilization of ColE1 plasmid and is thus essential to promote the specific transfer of the plasmid during conjugation. Probably functions by inducing DNA bending, helping the MbeA relaxase to melt the DNA around the nic site and cleave the phosphodiester bond. Binds specifically double-stranded DNA (dsDNA) containing the ColE1 oriT but does not recognize the inverted repeat (IR). SIMILARITY: To E.coli MbaC and MbkC."}
+{"protein": "MAKMMGPRFKMCRRLGLNVVGHPKAMKRAGRGTSRADKKLSDYGIQLLEKQRLRAYYGVMERQFTRYVDQAFNSKEQPGEALLMILESRLDNMVYRMGFASSIRQARQMVNHGHFLVNGKKVNIPSFRLNIGDEVVLREKSRKTEMFVNNFKDSIGSEVPYVSKEEDNFKGIFTRKPKREEIPITIQEQLIVEFYSK", "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. SIMILARITY: Belongs to the universal ribosomal protein uS4 family."}
+{"protein": "MIKKASLLTACSVTAFSAWAQDTSPDTLVVTAIRFEQPRSTVLAPTTVVTRQDIDRWQSTSVNDVLRRLPGVDITQNGGSGQLSSIFIRGTNASHVLVLIDGVRLNLAGVSGSADLSQFPIALVQRIEYIRGPRSAVYGSDAIGGVVNIITTRDEPGTEISAGWGSNSYQNYDVSTQQQLGDKTRVTLLGDYAHTHGYDVVAYGNTGTQAQTDNDGFLSKTLYGALEHNFTDAWSGFVRGYGYDNRTNYDAYYSPGSPLLDTRKLYSQSWDAGLRYNGELIKSQLITSYSHSKDYNYDPHYGRYDSSATLDEMKQYTVQWANNVIVGHGSIGAGVDWQKQTTTPGTGYVEDGYDQRNTGIYLTGLQQVGDFTFEGAARSDDNSQFGRHGTWQTSAGWEFIEGYRFIASYGTSYKAPNLGQLYGFYGNPNLDPEKSKQWEGAFEGLTAGVNWRISGYRNDVSDLIYYDDHTLKYYNEGKARIKGVEATANFDTGPLTHTVSYDYVDARNAITDTPLLRRAKQQVKYQLDWQLYDFDWGITYQYLGTRYDKDYSSYPYQTVKMGGVSLWDLAVAYPVTSHLTVRGKIANLFDKDYETVYGYQTAGREYTLSGSYTF", "text": "FUNCTION: Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily."}
+{"protein": "MGNKKKTRKTVPKEFISLFRVHSGRDAPRRDTREVQKSKKHGFRFTSLPDLPVASNALQELLLEYGLLNDIKWDSKGLKASKNKKTKLKPINSFIAFRSFYSRTISNPEHQRELSSKLADVWTQESNQEVWKQYTQSYNNYLLLPDAKLNFVDWLCEALDYTIDNTTPQIEDISLTSYNQLLSGTIEDVYIMK", "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. Transcriptional activator that induces the transcription of alpha- specific mating genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MATALPHA1 family."}
+{"protein": "MLSAAAAAAVIPKLRFATRPQLRRPAARTYWPRPLSSSSHVTPAAAGAGELEPPDLTRLANAARISLSPQEAEDFEPKIRQVVDWFGQLQAVDLESIEPSLRAGTTADSSLREDKPETFDNRDAIVEAIPSYDDPYIKVPRVLNKE", "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 GatC family."}
+{"protein": "MALAYDPLFITSDKSLSAFDVASSPPQPMNLTQDELKRIAAYKAVEFVESGMVLGLGTGSTAKHAVDRIGELLRQGKLENIVGIPTSKKTQEQALSLGIPLSDLDAHPVIDLSIDGADEVDPFLNLVKGRGGSLLREKMIEGASKKFVVIVDDSKMVKHIGGSKLALPVEIVPFCWKFTAEKLRSLLEGYGCEANLRLGEKGKAFVTDNGNYIVDMHVEEDMGDLGAVSDAILRLPGVVEHGMFLDMASTVIIAGELGVKIKNKH", "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": "VVSCADITALAARQGLFTSDQDLYTDSRMGQLNVLTGTQGEIR", "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. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
+{"protein": "MSLSQNAIFKSQTGEENLMSSNHRDSESITDVCSNEDLPEVELVNLLEEQLPQYKLRVDSLFLYENQDWSQSSHQQQDASETLSPVLAEETFRYMILGTDRVEQMTKTYNDIDMVTHLLAERDRDLELAARIGQALLKRNHVLSEQNESLEEQLGQAFDQVNQLQHELSKKEELLRIVSIASEESETDSSCSTPLRFNESFSLSQGLLQLDMMHEKLKELEEENMALRSKACHIKTETFTYEEKEQKLINDCVNELRETNAQMSRMTEELSGKSDELLRYQEEISSLLSQIVDLQHKLKEHVIEKEELRLHLQASKDAQRQLTMELHELQDRNMECLGMLHESQEEIKELRNKAGPSAHLCFSQAYGVFAGESLAAEIEGTMRKKLSLDEESVFKQKAQQKRVFDTVKVANDTRGRSVTFPVLLPIPGSNRSSVIMTAKPFESGVQQTEDKTLPNQGSSTEVPGNSHPRDPPGLPEDSDLATALHRLSLRRQNYLSEKQFFAEEWERKLQILAEQEEEVSSCEALTENLASFCTDQSETTELGSAGCLRGFMPEKLQIVKPLEGSQTLHHWQQLAQPNLGTILDPRPGVITKGFTQMPKDAVYHISDLEEDEEVGITFQVQQPLQLEQKPAPPPPVTGIFLPPMTSAGGPVSVATSNPGKCLSFTNSTFTFTTCRILHPSDITQVTPSSGFPSLSCGSSAGSASNTAVNSPAASYRLSIGESITNRRDSTITFSSTRSLAKLLQERGISAKVYHSPASENPLLQLRPKALATPSTPPNSPSQSPCSSPVPFEPRVHVSENFLASRPAETFLQEMYGLRPSRAPPDVGQLKMNLVDRLKRLGIARVVKTPVPRENGKSREAEMGLQKPDSAVYLNSGGSLLGGLRRNQSLPVMMGSFGAPVCTTSPKMGILKED", "text": "FUNCTION: May regulate endosome-to-lysosome trafficking of membrane cargo, including EGFR. SUBCELLULAR LOCATION: Cytoplasm. Early endosome. Mitochondrion. Note=Colocalizes with MGARP at the mitochondria. Translocates from the cytoplasm to the mitochondria in a MGARP-dependent manner. SIMILARITY: Belongs to the milton family."}
+{"protein": "NLYQFGKMIFKMTGKSALLSYSDYGCYCGWGGKGKPLDATDRCCFVHDCCYGRVNGCNPKLSTYSYSFQNGDIVCGDDNACLRAVCECDRVAAICFGENLNTYDRKYKDYPSSQCTETEQC", "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": "MSTATASPAVKLNSGYEIPLVGFGCWKLTNDVASDQIYRAIKSGYRLFDGAEDYANEQEVGEGIKRAIKEGIVKREELFITSKLWNSFHDKKNVEVALMKTLSDLNLDYVDLFYIHFPIAQKPVPIEKKYPPGFYCGDGDKWSIEEVPLLDTWRALEKLVDQGLAKSIGISNFSAQLIYDLIRGCTIKPVALQIEHHPYLTQPKLVEYVQLHDIQITGYSSFGPQSFLEMDLKRALDTPVLLEEPTVKSIADKHGKSPAQVLLRYQTQRGIAVIPRSNSPDRMAQNLSVIDFELTQDDLQAIAELDCNLRFNEPWDFSNIPVFV", "text": "FUNCTION: Reduces D-xylose into xylitol. Preferentially utilizes NADH as a cosubstrate. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MADEATRRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDFLKYEFDIEFEIPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEVPDLIQKGVIQHKEKCNQ", "text": "FUNCTION: E1-like enzyme which specifically catalyzes the second step in ufmylation. Accepts the ubiquitin-like modifier UFM1 from the E1 enzyme UBA5 and forms an intermediate with UFM1 via a thioester linkage. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UFC1 subfamily."}
+{"protein": "MTTKEAIADMALEAQEEDDAGPPDGGFRAWLVVLGGFLAYFVTFGMLNSFGTFQEYYGEKLLPGRSTSEISWIGSLQLFLLFIGGLFFGPVFDAKGSKVLFIPGTLLLSLSQMMVSLCKEYYQFILAQSLLFGIAVAMLFYPTISAISHWFHHRRGLAMGIVLTGSSLGGIAWPLILERLFAVVGFPWGLRIVGFISFALLAPACFMVIPRLPPRKSGGLSKADLSEGLKDRRYWLTVVGMLFVIWGMFIPFYYIPLFAMDHGVNSSFANSLISILNAGSFVGRIVSGALADKLGR", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds (PubMed:32077283). Directly involved in the secretion of pyranterreones (PubMed:32077283). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
+{"protein": "MKFGWIKTTGTDSEERMDSVKDALESSIPGIIAEKDEISSVRELGNIKIVSDSLDADVVLINKGEDLEILKSAKLSGKETAVYVVINTKDDEVYATEVSKLDFVDYIVLEGSDWTIIPLENIIADLFGEEIKIVSVVTSVKDAEAAYEILEKGVDGVVLIPNDINEVKDFSKLIERMNSESVKLDYATVTKIEPVGSGDRVCIDTCSMMEMGEGMLIGSYSRGMFLVHSETVENPYVATRPFRVNAGPVHAYILCPENKTKYLSDLKAGDKVLVVNKNGETRESIIGRVKIEKRPLFLVEAEYNGENLRTILQNAETIRLVGEDGKPVSVVDLKVGTKVLIKPDENARHFGMAIKETIIEK", "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": "MVHVSSFKNDHPLDKRREVAERIRSKYLDRIPVIVEKAPRSDAPDIDKKKYLVPADITVGKFVYEIRKHMTKVSAEKAIYLFVNNTIPPTAALISQIYERYKDEDGFLYITYSGENTFGSDL", "text": "FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation. Participates in membrane fusion events that take place in the secretory pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor. SIMILARITY: Belongs to the ATG8 family."}
+{"protein": "MHTPIISETVQPKTAGLIVLGKASAETRGLSQGVEPDIGQTYFEESRINQD", "text": "FUNCTION: Shows weak antimicrobial activity against its phylogenetic relative Caulobacter crescentus. Does not show activity against other bacteria tested (E.coli, Vibrio sp, Burkhoderia thailandensis, and Salmonella newport)."}
+{"protein": "MACCSTSFCGFPTCSTGGTCGSNFCQPTCCQTSCCQPTSIQTSCCQPTSIQTSCCQPTSIQTSCCQPISIQTSCCQPTCLQTSGCETGCGIGGSIGYGQVGSSGAVSSRTKWCRPDCRVEGTSLPPCCVVSCTSPSCCQLYYAQASCCRPSYCGQSCCRPACCCQPTCIEPVCEPTCCEPTC", "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": "EDTGTFEEGHGGVR", "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. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MAESGGGGGCCPPMDLMRSETMQLVQLIVPMESAHLTVSYLGDLGLVQFKDLNSEKSPFQRTYAAQIKRCGEMARKIRFFRDQMSKAGVPAKEMQGKENDIDLDDVEVKLGELEAELVEINANNDKLQRSYNELMEYKLVLQKAGEFFSSAHRSAADQQRETESQQAGEDLLESPLLQEEKSIDSTKQVKLGFLTGLVPREKSMVFERILFRATRGNIFIRQTVIEEPVIDPNSGEKAEKNVFVVFYSGERAKSKILKICEAFGANRYPFSEDLGRQAQMITEVSGRLSELKTTIDAGLGQRNILLQTIGDKFELWNLKVRKEKAIYHTLNMLSLDVTKKCLVAEGWSPVFASREIQDALQRAAVDSNSQVGSIFQVLRTKESPPTYFRTNKFTSAIQEIVDAYGVAKYQEANPGVFTIVTFPFLFAVMFGDWGHGICILLATMYLILKEKKLASQKLGDIMEMAFGGRYVILMMSLFSIYTGLIYNEFFSIPFPLFAPSAYDCRDVSCSEATTIGLIKVRDTYPFGLDPVWHGSRSELPFLNSLKMKMSILLGVSQMNLGIIMSYFNARFFKSSVNIWFQFIPQMIFLNSLFGYLSVLIIIKWCTGSQADLYHVMIYMFLSPMDELGENQLFPHQKTLQLVLLFLALVSVPCMLLPKPFILKKQHEARHQGQAYAPLDETDESLHVETNGGGSHGHEEFEFSEIFVHQLIHTIEFVLGAVSNTASYLRLWALSLAHSELSSVFYEKVLLLAWGYNNPLILIVGVLVFIFATVGVLLVMETLSAFLHALRLHWVEFQNKFYEGDGYKFAPFTFIFTANEDE", "text": "FUNCTION: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase. Involved in vacuolar nutrient storage (e.g. accumulation and storage of nitrate) and in tolerance to some toxic ions (e.g. zinc ions sequestration in vacuoles). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family."}
+{"protein": "RPFRKHGAVPLSTYMRIYKKGDIVDIKGMGTIQ", "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": "NKASVVANQLIPINTALTLIMMKAEVVTPMGIPAEEIPKLVGMQVNRAVPLGTTLMPDMVKNYE", "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": "MFLFLPIPLNVQDIWKVNSKYKHVLLTCPVCQNKTVRVYRLVKSLALIVLPVLPVYTSKVLRCSHCGWYEPVDSAMIDQRRRREDLPTPERPEASAQQHAFFPGSSSQQTDIPNVRPQPHIPPPRKSDEAPPPYSYK", "text": "SIMILARITY: Belongs to the UPF0768 family."}
+{"protein": "MRCSAISPGSGTIINAISTGKGSAFGIDLKIKANVELKNDGKSKINGILLDNPSLKPNLVERCVKNVLEHFEVDYSAKISTSSELPLKSGLSSSSAASNAAVLATFGALGEKIDSELILDLAIKSSFEEQLTITGAYDDATASYFGGITVCNNLERKILKKDVFKEELDVIILMPNFKKNLNVKRMKLISDYVELAFEKCMNADYYKALFLNGILYSSALNFPSYISVDALEAGAVTAGLSGTGPSYIALSYQENTEKVKNAFKKYGTVIISKPDNFGSKIIY", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily."}
+{"protein": "MASISSLGAGSGMDLGSLLDKLQAAEKKRLEPLAQQQTSYKAKLTGFGTLKGSLEKLKSASEELKKFDKLNTTKTNGDHKTFTPSTDSKASPGNYEIEVQQLAKAQSLQSTEVSGVKKLLGEQGKGTRTIIITQPGEKEPMKISLKDDETSLVEIRDAINKKEGNVNASIIKADENGTEEEGKSYLILTSKKAGTRSIMTIKVEGDDELGKLLNYTSDGKGGGSGAMTQKVGAANAKLTVNGIPIERQTNEIKDAPEGIILNLKKVSETEEVIVKVNGEDKKIPRPKTEILVVSRDIEPMKEAIKKWVDSYNELQTTFDSLAKFKPVGKGEAASKDNGALLGDGTLKGIQSQLRHQLFAAQDVADIATLNKLGIKQKLDGTLEISDEKLEKNLKEKSADVKAFFMGDGAKPGSTQTYNLLKETLDGHEGTIATATEGINKRLKTLERQVEQTNRNIDATMERYKRQFTELDKLVNSLNNTSSSLFQLLR", "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": "MEEWDVPQMKKEVESLKYQLAFKREMSSKTIPELLKWIEDGIPKDPFLNPDLMKNNPWVEKAKCTIL", "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; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the G protein gamma family."}
+{"protein": "MSFQIETVPTKPYEDQKPGTSGLRKKTKVFKDEPNYTENFIQSIMEAIPEGSKGATLVVGGDGRYYNDVILHKIAAIGAANGIKKLVIGQHGLLSTPAASHIMRTYEEKCTGGIILTASHNPGGPENDMGIKYNLSNGGPAPESVTNAIWEISKKLTSYKIIKDFPELDLGTIGKNKKYGPLLVDIIDITKDYVNFLKEIFDFDLIKKFIDNQRSTKNWKLLFDSMNGVTGPYGKAIFVDEFGLPADEVLQNWHPSPDFGGMHPDPNLTYASSLVKRVDREKIEFGAASDGDGDRNMIYGYGPSFVSPGDSVAIIAEYAAEIPYFAKQGIYGLARSFPTSGAIDRVAKAHGLNCYEVPTGWKFFCALFDAKKLSICGEESFGTGSNHVREKDGVWAIMAWLNILAIYNKHHPENEASIKTIQNEFWAKYGRTFFTRYDFEKVETEKANKIVDQLRAYVTKSGVVNSAFPADESLKVTDCGDFSYTDLDGSVSDHQGLYVKLSNGARFVLRLSGTGSSGATIRLYIEKYCDDKSQYQKTAEEYLKPIINSVIKFLNFKQVLGTEEPTVRT", "text": "FUNCTION: Major phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6- phosphate (PubMed:5784209). Constitutes about 80-90% of the phosphoglucomutase activity in the cell (PubMed:14264884, PubMed:5231755). Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1- phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source because glucose 1-phosphate is the starting point for the synthesis of UDP- glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (PubMed:14264884). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphohexose mutase family."}
+{"protein": "MGDRGVRLGLLMPMLALLSWAASLGVAEETPSRIPADKLLVITVATKENDGFHRFMNSAKYFNYTVKVLGQGQEWRGGDGMNSIGGGQKVRLMKEAMEHYAGQDDLVILFTECFDVIFAGGPEELLKKFQKTNHKIVFAADALLWPDKRLADKYPGVHIGKRYLNSGGFIGYAPYISRLVQQWNLQDNDDDQLFYTKVYIDPLKREALNITLDHRCKIFQALNGATDEVVLKFENGKSRVKNTFYETLPVAINGNGPSKILLNYFGNYVPNSWTQENGCALCDFDASDLSTVDVYPKVTLGVFIEQPTPFQPRFLDLLLTLDYPKEALRLFVHNKEVYHEKDIKAFVDKAKHDISSIKIVGPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTRHGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGIWNVPYMANVYLIQGKTLRSEMSERNYFVRDKLDPDMSLCRNARDMGVFMYISNRHEFGRLISTANYNTSHLNNDLWQIFENPVDWKEKYINRDYSKIFTENIVEQPCPDVFWFPIFSERACDELVEEMEHYGKWSGGKHHDSRISGGYENVPTDDIHMKQIDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQRSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEGLPVKNGTRYIAVSFIDP", "text": "FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side."}
+{"protein": "MEVGLSPSACLRRIKLMEQAGVIRGYTALVDPTQSESTIAVIINITLERQTEEYLDKFEAAVRKHPEIRECYLMTGGSDYMLRVDVENAGAFERIHKEVLSTLPGVLRIHSSFSIRNVLAGRLKAKR", "text": "FUNCTION: Not known, symbiotically active."}
+{"protein": "MERYMSLKKKISYSELIGSAKANELQTQLQAYVPGKDPNIVVEHEPSKNAAKELIRGDYRWGHQGDDKSETFQLTYSFLESEPDNMPWHITGFSAFNEEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGFFDASLTGSYAFAYLPSPESKQSGTWYNLKSRTFSENDIGVNGYGRQTFTHEIGHTLGLEHPAAYNASDKERPTYKKSATYFEDSRAYTVMSYFGEKNTRTDFKGIYSSAPLLNDISAIQEVYGANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGLKGNVSIARGVTIENAIGGSGNDILIGNDAENILKGGAGDDIIYGGLGADQLWGGEGKDTFVYLSAKESPPLERDWIHDFVSGEDKIDVSLFDLGEAGKGGVKFVREFTGAVGEAVLRYDTVNKVNDFAINLGDKFSYDDFWVKIVGEPILESDFILA", "text": "FUNCTION: Involved in the inhibition of insect antibacterial peptides. Reduces the antibacterial activity of G.mellonella hemolymph by 50%. Reduces the antibacterial activity of cecropin A by 80% and cecropin B by 75%. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M10B family."}
+{"protein": "NTVSSFQDILMRMSKMQLGSSSEDLNGMIIRLESLKLYRDSLGEAVMRMGDLHSLQSRNEKWREQLSQKFEEIRWLIEEVRHRLKNTENSFEQITFMQALQLLLEVEQEIRT", "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. SIMILARITY: Belongs to the influenza viruses NEP family."}
+{"protein": "MKKVTAMLFSMAVGLNAVSMAAKAKASEEQETDVLLIGGGIMSATLGTYLRELEPEWSMTMVERLEGVAQESSNGWNNAGTGHSALMELNYTPQNADGSISIEKAVAINEAFQISRQFWAHQVERGVLRTPRSFINTVPHMSFVWGEDNVNFLRARYAALQQSSLFRGMRYSEDHAQIKEWAPLVMEGRDPQQKVAATRTEIGTDVNYGEITRQLIASLQKKSNFSLQLSSEVRALKRNDDNTWTVTVADLKNGTAQNIRAKFVFIGAGGAALKLLQESGIPEAKDYAGFPVGGQFLVSENPDVVNHHLAKVYGKASVGAPPMSVPHIDTRVLDGKRVVLFGPFATFSTKFLKNGSLWDLMSSTTTSNVMPMMHVGLDNFDLVKYLVSQVMLSEEDRFEALKEYYPQAKKEDWRLWQAGQRVQIIKRDAEKGGVLRLGTEVVSDQQGTIAALLGASPGASTAAPIMLNLLEKVFGDRVSSPQWQATLKAIVPSYGRKLNGDVAATERELQYTSEVLGLNYDKPQAADSTPKPQLKPQPVQKEVADIAL", "text": "SIMILARITY: Belongs to the MQO family. SIMILARITY: Belongs to the MQO family."}
+{"protein": "MYEIKQPFHSGYLQVSEIHQIYWEESGNPDGVPVIFLHGGPGAGASPECRGFFNPDVFRIVIIDQRGCGRSRPYACAEDNTTWDLVADIEKVREMLGIGKWLVFGGSWGSTLSLAYAQTHPERVKGLVLRGIFLCRPSETVWLNEAGGVSRIYPEQWQKFVAPIAENRRNQLIEAYHGLLFHQDEEVCLSAAKAWADWESYLIRFEPEEVDEDAYASLAIARLENHYFVNGGWLQGDRAILNNIGKIQHIPTIIVQGRYDLCTPMQSAWALSKAFPEAELRVVQAGHRAFDPPLVDALVQAVEDILPHLL", "text": "FUNCTION: Specifically catalyzes the removal of N-terminal proline residues from peptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S33 family."}
+{"protein": "MGCGTSKVLPEPPKDVQLDLVKKVEPFSGTKNDVYKHFITEVDSVGPLKAGFPATSQYAPPCPGVPNTGHTAPPSEPPRRARVAKYRAKFDPRVTAKYDIKALIGRGSFSRVVRVEHRATRQPYAIKMIETKYREGREVCESELRVLRRVRHANIIQLVEVFETQERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVRYLHALGITHRDLKPENLLYYHPGTDSKIIITDFGLASARKKGDDCLMKTTCGTPEYIAPEVLVRKPYTNSVDMWALGVIAYILLSGTMPFEDDNRTRLYRQILRGKYSYLGEPWPSVSNLAKDFIDRLLTVDPGARMTALQALRHPWVVSMAASSSMKNLHRSISQNLLKRASSRCQSTKSSQSTRSSRSTRSNKSRRVRERELRELNLRYQQQYNG", "text": "FUNCTION: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing. SUBCELLULAR LOCATION: Golgi apparatus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus speckle Endoplasmic reticulum membrane; Lipid-anchor Cell membrane; Lipid-anchor Cytoplasm Note=Localized in the brefeldin A- sensitive Golgi compartment, at centrosomes, in the nucleus with a somewhat speckle-like presence, membrane-associated to the endoplasmic reticulum (ER) and the plasma membrane (PM), and more diffusely in the cytoplasm. Found to concentrate in splicing factor compartments (SFCs) within the nucleus of interphase cells. The acylation-negative form may be only cytoplasmic and nuclear. Acylation seems to allow the sequestering to the intracellular membranes. Myristoylation may mediate targeting to the intracellular non-Golgi membranes and palmitoylation may mediate the targeting to the Golgi membranes. Dual acylation is required to stabilize the interaction with Golgi membranes (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
+{"protein": "MPTKTSQHAFAGSERWVVPRYSSKPGTLIRLGSVLTDPEDLESSLNLDSIPPIPPHLLRDATPEVRMSVQTELSKSDSTLAKAAPALEGILTLGGGVEASRSQGVSSSLNISGTVKATVFRADKSYMDVLLKDKNVISYAKRGLGKPMFVVVGVATAGRVEMKETRHVTRKAGVSGKVGVEVIGEGEVGLERERSDKSCNEVRGEGGLDFAYRVREFGYSRVRGTVKDKGDWTGKVLFAGGKGPVVEKGGEVVPVFKEFKEGEVKLRATGSFDVAAKA", "text": "FUNCTION: [Gasdermin-like protein het-Q1, N-terminal]: Pore-forming protein that causes membrane permeabilization and cell death (PubMed:35135876). Released upon cleavage and maturation by het-Q2 and binds to membrane inner leaflet lipids (PubMed:35135876). Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering cell death (By similarity). FUNCTION: [Gasdermin-like protein het-Q1]: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition) (PubMed:35135876). In P.anserina, the het-q locus exists as 2 incompatible alleles, het-Q1 (this entry) and het-Q2 (AC P0DW09) (PubMed:35135876). This form constitutes the precursor of the pore-forming protein: during the allorecognition process, it is cleaved by het-Q2, releasing the N- terminal moiety (Gasdermin-like protein het-Q1, N-terminal) that binds to membranes and forms pores, triggering cell death (PubMed:35135876). SUBCELLULAR LOCATION: [Gasdermin-like protein het-Q1, N-terminal]: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the gasdermin family."}
+{"protein": "MFTLKKSLLLLFFLGVINVSLCEEERDADEEERRDDPEERDVEVEKRFFPLALLCKVFKKC", "text": "FUNCTION: Antimicrobial peptide. Has low activity against the Gram- positive bacterium S.aureus (MIC>100 uM) and the Gram-negative bacterium E.coli (MIC=25 uM). Lacks hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
+{"protein": "MNKVFPFVVIVATVLILVFDTTDAKGEKKCSNSEECVKFCSEYSDVHPACIGDHCECIRWEGGISI", "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": "MKDERRPICEVVAESIERLIIDGVLKVGQPLPSERRLCEKLGFSRSALREGLTVLRGRGIIETAQGRDSRVARLNRVQDTSPLIHLFSTQPRTLYDLLDVRALLEGESARLAATLGTQADFVVITRCYEKMLAASENNKEISLIEHAQLDHAFHLAICQASHNQVLVFTLQSLTDLMFNSVFASVNNLYHRPQQKKQIDRQHARIYNAVLQRLPHVAQRAARDHVRTVKKNLHDIELEGHHLIRSAVPLEMNLS", "text": "FUNCTION: Transcriptional activator of the glcDEFGB operon which is associated with glycolate utilization, and encodes malate synthase G and the genes needed for glycolate oxidase activity (PubMed:8606183, PubMed:9880556). Also negatively regulates the transcription of its own gene (PubMed:9880556). Glycolate acts as an effector, but GlcC can also use acetate as an alternative effector (PubMed:9880556). FUNCTION: Transcriptional activator of the glcDEFGB operon which is associated with glycolate utilization, and encodes malate synthase G and the genes needed for glycolate oxidase activity. Also negatively regulates the transcription of its own gene. Glycolate acts as an effector, but GlcC can also use acetate as an alternative effector."}
+{"protein": "MKLLGLLLLVFTFMALAFADEKDCIARGQKCVGENKPCCKGTTCMYYANRCVGV", "text": "FUNCTION: Binds reversibly and blocks P/Q-type voltage-gated calcium channels (Cav). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Ptu1-like knottin family."}
+{"protein": "MRYIVSPQLVLQVGKGQEVERALYLTPYDYIDEKSPIYYFLRSHLNIQRPEIVKRHILLTLRMTQLKGYLGNLLDIKDDIIIYSHKNNLEYSYVDNTIFNPFVYTQKKTLLKNDSFLYNVYSGACDFLVIWVARACDTSIPEFGSYEDVDNNIIKFETMLMEVFPQLDLDITVESKFNNIFRTNLKLTGLKKIIQRVQDLDINYKSLLSRYDEHFINMTGNHFILNDEQLNLSIWDLDSTLALSSDGDTVMINNVKLFTDLVSDIDTQMERIKGDITYKVHLATPINSRIKLDIETSFIFIETATNNILLSSDKKISIILAKNHISIKVKNHIPNIEKYFTFLVIAINAMFNSVQKSSDFTKVETVYWSRICQNTKNKNRKPIIINYLDPGMKKISNNFYRSDEKEVFINDNGIMFTCIDPLGKYNKVGFLNIFHDMRKYCIPCCFLHDQSHRSTFSSCVHQIDVEKKIVSPYILNFGKVVTESKMSFLPIIFDAFLNDGMTANMEQDNKRLKETSGYHIVRCCAGDDIVRLRTISDIIQFVNEDKNILIVNDMIYFPMNATDIGKKIHILIQEIVHEVMIVKKKESSDKIDFFPPNYKLLKDLFPKQTIQTPIHSDAGMVLTTDGFYIDGKLFNEDLSSKYVTFTKNVIASDAVTKYFSPLFKYVISEAKDRFIKTWMINIMIHMNVDPNNIIPTLEKYYPNSGRAQIN", "text": "FUNCTION: Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa RAP94/OPG109 to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters. 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 (By similarity). SIMILARITY: Belongs to the poxviridae VETF large subunit family."}
+{"protein": "MVNLSRSVALISVFLLPLLSFSFSVDNPTDRRVLVLLDDLSLKSSHSIFFNTLKSRGFDLDFKLAEDSKLALQRYGQYLYDGLIIFAPSTERFGGSLDSKSIADFVDSGRDLILSADTAASDLIRGIATECGVDFDEDSSAMVIDHTSFSVSDVDGDHTLIAADDLVKSDVILGKTKIEAPVLFRGVAHSLNPTNNLVLKVLSASPSAYSANPSSKLSSPPQLTGSSISLVSVMQARNNARVVISGSVQLFSDRLIRSGVQKAGSPNQYEKSGNEQFVTELSKWVFHERGHLKAGNLVHHRVGETDEPAIYRIKDDLEFSVEIYEWSGKSWEPYVANDVQVQFYMMSPYVLKTLSTDKKGLFHTSFKVPDVYGVFQFKVEYEKLGYTTLSLSKQIPVRPYRHNEYERFIPTAYPYYGACFTTMAGFFVFSFVYLYHK", "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:15860005). 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). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the DDOST 48 kDa subunit family."}
+{"protein": "MKRTRRALPANYDPVYPYDAPGSSTQPPFFNNKQGLTESPPGTLAVNVSPPLTFSTLGAIKLSTGPGLTLNEGKLQASLGPGLITNTEGQITVENVNKVLSFTSPLHKNENTVSLALGDGLEDENGTLKVTFPTPPPPLQFSPPLTKTGGTVSLPLQDSMQVTNGKLGVKPTTYAPPLKKTDQQVSLQVGSGLTVINEQLQAVQPPATTYNEPLSKTDNSVSLQVGAGLAVQSGALVATPPPPLTFTSPLEKNENTVSLQVGAGLSVQNNALVATPPPPLTFAYPLVKNDNHVALSAGSGLRISGGSLTVATGPGLSHQNGTIGAVVGAGLKFENNAILAKLGNGLTIRDGAIEATQPPAAPITLWTGPGPSINGFINDTPVIRCFICLTRDSNLVTVNASFVGEGGYRIVSPTQSQFSLIMEFDQFGQLMSTGNINSTTTWGEKPWGNNTVQPRPSHTWKLCMPNREVYSTPAATISRCGLDSIAVDGAPSRSIDCMLIINKPKGVATYTLTFRFLNFNRLSGGTLFKTDVLTFTYVGENQ", "text": "FUNCTION: Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface (By similarity). SUBCELLULAR LOCATION: Virion Host nucleus Note=Anchored to the pentons, protrudes from the virion surface. SIMILARITY: Belongs to the adenoviridae fiber family."}
+{"protein": "MASKAFELQMMGYGLTTAEIHYHMPDHPGLLQLYVWQEYDLAPKFPTLKGFLDFWAKELDGVLHSVRVAHNRLISPREWRVVNGVFTLQ", "text": "FUNCTION: Probably necessary for the cotranslation of trpF. It may also function as a subunit or stabilizer of phosphoribosylanthranilate isomerase (trpF)."}
+{"protein": "MSEDRDLLAVGHTAFDYIIHLDEFPEPNTSTAIKRMRNLHGGAAANVALVGSRLGLRTSLVSAVGGDFEGSEYRELLESSGIDIESMILVADESTPTAFVMTDSDHNQISYFYWGAARYFKDAETPADAIKSARAVHLATGDPSFNCRCGEFARSLGKIISFDPGQDLHMYSRSQLERAVGVCDILFGNHHEIDRICSKLSVDIHGLREMGPGVVVKTYGKEGSIIYSDDVIKIDAIPREAVDPTGAGDSYRAGFMRAYLRGADLKTCGRFASAVASFIVEDEGTQTNIPDTGEAVKRFTAQWGYEPPI", "text": "FUNCTION: Catalyzes the phosphorylation of a wide range of nucleosides to yield nucleoside monophosphates, using ATP, ITP or GTP as phosphate donor. SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
+{"protein": "MFGLGGQPQLSSQQKLSAAEAELDLVTDMFNKLVDNCHKKCIEQIYNDGQLNKNESTCIDRCVAKYFETNVKVGENMQQLGQAFSPGKF", "text": "FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of 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": "MVSQNPNRQKVELNRTSLFWGLLLIFVLAILFSSYIFN", "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, cyanelle thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbL family."}
+{"protein": "MRLVQLSRHSIAFPSPEGALREPNGLLALGGDLSPARLLMAYQRGIFPWFSPGDPILWWSPDPRAVLWPESLHISRSMKRFHKRSPYRVTMNYAFGQVIEGCASDREEGTWITRGVVEAYHRLHELGHAHSIEVWREDELVGGMYGVAQGTLFCGESMFSRMENASKTALLVFCEEFIGHGGKLIDCQVLNDHTASLGACEIPRRDYLNYLNQMRLGRLPNNFWVPRCLFSPQE", "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. 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. 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. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the L/F-transferase family. SIMILARITY: Belongs to the L/F-transferase family."}
+{"protein": "MYAEERAYGSFDDVMEVYQQIVTESIQLKRLHFGSGCLIEFLGDSGTCETFCGGWISMICWTSDTNSMGSLTVDIGIDDGKYKTYNARGFLLCSKSITSISQNTEGRDRILTVSQENNKLQITFVTLTKVFKEHDIRNLGDPKCIEKFEKECRALDRKKHDDEHRKRSGKQKEKRKVEDTDKKKDDDRRKQEERKRNDEDKQPDKKEESDELPKEKRQKYHDMKRNLEEQSHEDGITLTSTTLVNGAVEGALPPCISIDNHEDQQHDELDKRAYAQGTNREGLSNEDNYGNFRLNKSLEQLRAKLVASSGDIVERSLLKLKECLDNVKDNLIKNECADVTGPSKCLSKTKHIEPKKQIVFSDCVRPVPVCEIKPFIDVRLFETARSPRRLRQRTRTIVGSTDGAIEQQRVISGQNRGRARGRGRGRAPRRRNSNINNSRTQTTIVIDDSSEAENFENEGSFNEDLLATTILETL", "text": "FUNCTION: May be involved in DNA replication. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae U79/UL112 family."}
+{"protein": "MTPTANLLLPAPPFVPISDVRRLQLPPRVRHQPRPCWKGVEWGSIQTRMVSSFVAVGSRTRRRNVICASLFGVGAPEALVIGVVALLVFGPKGLAEVARNLGKTLRAFQPTIRELQDVSREFRSTLEREIGIDEVSQSTNYRPTTMNNNQQPAADPNVKPEPAPYTSEELMKVTEEQIAASAAAAWNPQQPATSQQQEEAPTTPRSEDAPTSGGSDGPAAPARAVSDSDPNQVNKSQKAEGER", "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 the thylakoid membrane. Involved in delta pH-dependent protein transport required for chloroplast development, especially thylakoid membrane formation. TATC and TATB mediate precursor recognition, whereas TATA facilitates translocation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein Note=The C-terminus is located in the stroma. SIMILARITY: Belongs to the TatB family."}
+{"protein": "MVLADLGNQLSSALRSLNETTIVNEDTINQLLKEVGNALSKSDVSMSLIIQMRKNIKDKIKLDQMAAGLNKRKIIKQVVFDELIRLLDPGVPLWKPTKGKSNIVMFVGLQGAGKTTSVTKLAYFYKKKGFSTAIVCADTFRAGAFDQVRHNAAKAKIHYYGSETEKDPVVVARTGVDIFKKDGTEIIIVDTSGRHKQDSELFEEMKQIETAVKPDNCIFVMDSSIGQAAYEQATAFRSSVKVGSIIITKMDGNSMGGGAISAVAATNTPIIFIGTGEHLTDLELFDPSTFVSKLLGYGDMKGMLEKIKEVIPEDSTSLKEIAQGKFTLRSMQQQFQQIMQLGPIDKLVQMIPGMNQLPQLQGNEGGLKLKAYINILDSLSEKELDGKKPITQKRIITIAQGSGRHPNEVVELLEQHKTFEKLIGKGGPGGGLGSLMAGKGGPKNMEQAMKQMNANGGMQGLMNSLKGMGGMGDLAKMFGGGGGGGGGMPSMGDLAKMMGGMGGGGRGGGGMPNMGDLAKMMGGMGGGAGKGGQNGFPNLDLD", "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). As part of the SRP complex, associates with the SRP receptor (SR) component srpra to target secretory proteins to the endoplasmic reticulum membrane. Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes. Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit srpra. 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). SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily."}
+{"protein": "MGDGQAGSVININGSASGQQAPTSNSPTLTRKSSSSELPPELRILCFDLTHYNQTTQFLLSCAGVFILYILYGYLQELIFTVEGFKPFGWFLTLVQFGYYIGFGLVERRLEAYRSGRRSLWNVEPAPRCIPMKTYLVLAALTLGTMGLSNSSLGYLNYPTQVIFKCCKLIPVLVGSILIQGKRYGPLDFAAASCMCIGLAWFTLADSQMTPNFNLLGVAMISGALLCDAAIGNVQEKAMKEHKAPSSEVVFYSYGLGFVYLFVIMLVTGNFFSGFAFCLEHPLQTFGYGFLFSLSGYLGIQFVLALVRSSGAPIAATVTTARKAVTIAFSFVLFSKPFTVQYLWSGLIVVLGIYLNVYSKKNKLTFADIRSRFKQFGFRLARSPSRKFLVEV", "text": "FUNCTION: Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. Essential for viability. Involved in glycosaminoglycan synthesis and the subsequent signaling. May be involved in hh and dpp signaling by controlling the sulfation of heparan sulfate (HS) (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily."}
+{"protein": "MNIKDEHIDSVCSLLDQLVGNVSFKNLFTGYGLFHKEETMFAIWQNKKLYLRGEGVLAIQLTKLGCEPFTTNELNKRFVLSQYYALSDQILRSNRLCRKLIILSIKQILEQKLECTLRKLNRLKDLPNLTIKHERALIKVGITNVAMLREIGAENALVELKKSGSGATLDFYWKLVCALQNKNSQMLSQAEKERLLKKLNEVWRKNGLKGYRKLDDE", "text": "FUNCTION: Required for DNA transformation (PubMed:1653215, PubMed:18761017). Positively regulates genes required for DNA transformation (late competence-specific genes) in association with CRP (PubMed:18761017). Required for expression of the dprABC operon (PubMed:9244270). SIMILARITY: Belongs to the TfoX family."}
+{"protein": "MAERRRHKKRIQEVGEPSKEEKAVAKYLRFNCPTKSTNMMGHRVDYFIASKAVECLLDSKWAKAKKGEDALFTTRESVVDYCNRLLKKQFFHRALKVMKMKYDKDVKKEKDKGKSESGKEDDKKSKKESVKEEKTKKEKEKKKDGEKEDSKKEETPGTPKKKETKKKFKLEPHDDQVFLDGNEVFVWIYDPVHIKTFVMGLILVIAVIAATLFPLWPAEMRVGVYYLSVGAGCFVASILLLAIARCILFLIIWLITGGRHHFWFLPNLTADVGFIDSFRPLYTHEYKGPKADLKKDEKSETKKQQKSDSEEKSDSEKKEDEEGKGAPADHGPEGSGGERHSDTDSDRREDDRSQHSSGNGNDFEMITKEELEQQTDGDCDEEDDDKDGEVPKSAHEKS", "text": "FUNCTION: Mediates post-translational transport of precursor polypeptides across endoplasmic reticulum (ER). Proposed to act as a targeting receptor for small presecretory proteins containing short and apolar signal peptides. Targets and properly positions newly synthesized presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SEC62 family."}
+{"protein": "MGNTCRGSIGGKTFQGYTQPEDSSCSTNHNPSSGNSYSSSDNFSPTSNAQQNSNHKKEHSLSLVSPRKASMNRSGSNQAYYVMGHMTPNIRDLYTLGRKLGQGQFGTTYLCTENSTGAEYACKSISKRKLISKEDVEDVRREIQIMHHLSGHRNIVTIKGAYEDPLYVHIVMEICSGGELFDRIIQRGHYSERKAAELTKIIVGVVEACHSLGVMHRDLKPENFLLVNKDNDFSLKAIDFGLSVFFKPGQIFTDVVGSPYYVAPEVLLKHYGPEADVWTAGVILYILLSGVPPFWAETQQGIFDAVLKGHIDFDSDPWPLISESAKDLIRKMLCMQPSERLTAHEVLCHPWICENGVAPDRALDPAVLSRLKQFSAMNKLKKMALRVIAESLSEEEIAGLREMFKAMDTDSSGAITFDELKAGLRKYGSTLKDTEIRELMDAADVDNSGTIDYGEFIAATVHLNKLEREEHLMAAFQYFDKDGSGYITVDEVQQACIEHNMTDVYFEDIIREVDQDNDGRIDYGEFVAMMQKGNPCIGRRTMRNSLNLSMRDAPGAQ", "text": "FUNCTION: Regulates the production of reactive oxygen species (ROS) by NADPH oxidase. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily."}
+{"protein": "EGSGGSGSSGHFTTGSNVHMSSVTNTSNGGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTASGTATGTASGTATGTANGTGTGKGTDTHTAGSGSGSGTGTGTGTGTTTTTTTGNNSSSSTPPVTLTESLLNK", "text": "FUNCTION: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. 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 through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, perinuclear region Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity)."}
+{"protein": "MAILSYISATSTTPPIPQDQSPNSRLPTKIILPNKKPEKWSTGVAPGEYGGPPTTTKLRKYWGGEKEDPITSTDLIWNRDFMDQMKKLFDDPNDSSLDPSPSKEKSSGFLSFSRVMSLDSMDVDLSKELASSSKSVVKNRLDTSKSEAKKQMSKAIVSPKWKLAPTRREQEKWDRATKAATGGSDVMFRELRRPRGDPEVQAAKDREQYFKLKNKIQVLTLGIGGVGLVSAYISYTPEIALSFGAGLLGSLAYMRMLGNSVDAMADGARGVAKGAANQPRLLVPVVLVMIFNRWNAILVPEYGFMHLELIPMLVGFFTYKIATFFQAIEEAISITTQKPESISPDTQASD", "text": "FUNCTION: Facilitates the assembly of the membrane proton channel of the chloroplastic F-type ATPase. Specifically required for the efficient assembly and integration of the CF(0) subunit c into the chloroplastic ATPase complex in the thylakoid membrane. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein."}
+{"protein": "MEPATLTRSSSLTRFPYRRGLSTLRLARVNSFSILPPKTLLRQKPLRISASLNLPPRSIRLRAVEDHHHDHHHDDEQDHHNHHHHHHQHGCCSVELKAESKPQKMLFGFAKAIGWVRLANYLREHLHLCCSAAAMFLAAAVCPYLAPEPYIKSLQNAFMIVGFPLVGVSASLDALMDIAGGKVNIHVLMALAAFASVFMGNALEGGLLLAMFNLAHIAEEFFTSRSMVDVKELKESNPDSALLIEVHNGNVPNISDLSYKSVPVHSVEVGSYVLVGTGEIVPVDCEVYQGSATITIEHLTGEVKPLEAKAGDRVPGGARNLDGRMIVKATKAWNDSTLNKIVQLTEEAHSNKPKLQRWLDEFGENYSKVVVVLSLAIAFLGPFLFKWPFLSTAACRGSVYRALGLMVAASPCALAVAPLAYATAISSCARKGILLKGAQVLDALASCHTIAFDKTGTLTTGGLTCKAIEPIYGHQGGTNSSVITCCIPNCEKEALAVAAAMEKGTTHPIGRAVVDHSVGKDLPSIFVESFEYFPGRGLTATVNGVKTVAEESRLRKASLGSIEFITSLFKSEDESKQIKDAVNASSYGKDFVHAALSVDQKVTLIHLEDQPRPGVSGVIAELKSWARLRVMMLTGDHDSSAWRVANAVGITEVYCNLKPEDKLNHVKNIAREAGGGLIMVGEGINDAPALAAATVGIVLAQRASATAIAVADILLLRDNITGVPFCVAKSRQTTSLVKQNVALALTSIFLAALPSVLGFVPLWLTVLLHEGGTLLVCLNSVRGLNDPSWSWKQDIVHLINKLRSQEPTSSSSNSLSSAH", "text": "FUNCTION: Involved in cadmium/zinc transport. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily."}
+{"protein": "MGASCSSCCGGKSRDGLYDNVLADSEREAVADLLQYLENRGETDFFSGEPLRALSTLVYSENIDLQRSASLTFAEITERDVRAVDRDTLEPILFLLQNSDIEVQRAASAALGNLAVNTDNKVLIVQLGGLAPLIRQMMSPNVEVQCNAVGCITNLATHEDNKAKIARSGALGPLTRLAKSRDMRVQRNATGALLNMTHSDENRQQLVNAGAIPVLVQLLSSTDVDVQYYCTTALSNIAVDANNRRKLAQTEPRLVQSLVNLMDSSSPKVQCQAALALRNLASDEKYQLEIVRASGLGPLLRLLQSSYLPLILSAVACIRNISIHPMNESPIIEAGFLKPLVDLLGSTDNEEIQCHAISTLRNLAASSDRNKALVLEAGAVQKCKQLVLEVPVTVQSEMTAAIAVLALSDELKTNLLELGVFEVLIPLTKSPSIEVQGNSAAALGNLSSKVGDYSVFIHNWNEPSDGIHGYLSRFLASGDATFQHIAIWTLLQLLESEDKKLIGLIGKSNDIVDMIRQIANRQIESDNELEDDDEGEVVSLAQRCLELLGQGNAKAHIEG", "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": "MKIAITITVLMLSICCSSASSDICPGFLQVLEALLLGSESNYEAALKPFNPASDLQNAGTQLKRLVDTLPQETRINIVKLTEKILTSPLCEQDLRV", "text": "FUNCTION: Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the secretoglobin family."}
+{"protein": "RLCLSDYSIFSETIEICPEGHNYCFKKFPKGITRLPWVIRGCAATCPKPEAQVYVDCCARDKCNR", "text": "FUNCTION: Has anticoagulant activity, since it is able to inhibit the activation of coagulation factor X (F10) by coagulation factor VIIa (F7) (IC(50)=123.8 nM) (PubMed:27173146). Also shows weak irreversible neurotoxicity (PubMed:27173146). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Orphan group I sub-subfamily."}
+{"protein": "MTPGEVRRLYFIIRTFLSYGLDELIPKMRITLPLRLWRYSLFWMPNRHKDKLLGERLRLALQELGPVWIKFGQMLSTRRDLFPPHIADQLALLQDKVAPFDGKLAKQQIEAAMGGLPVEAWFDDFEIKPLASASIAQVHTARLKSNGKEVVIKVIRPDILPVIKADLKLIYRLARWVPRLLPDGRRLRPTEVVREYEKTLIDELNLLRESANAIQLRRNFEDSPMLYIPEVYPDYCSEGMMVMERIYGIPVSDVAALEKNGTNMKLLAERGVQVFFTQVFRDSFFHADMHPGNIFVSYEHPENPKYIGIDCGIVGSLNKEDKRYLAENFIAFFNRDYRKVAELHVDSGWVPPDTNVEEFEFAIRTVCEPIFEKPLAEISFGHVLLNLFNTARRFNMEVQPQLVLLQKTLLYVEGVGRQLYPQLDLWKTAKPFLESWIKDQVGIPALVRAFKEKAPFWVEKMPELPELVYDSLRQGKYLQHSVDKIARELQSNHVRQGQSRYFLGIGATLVLSGTFLLVSRPEWGLMPGWLMAGGLIAWFVGWRKTR", "text": "FUNCTION: Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. 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. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC1 family. UbiB subfamily."}
+{"protein": "MVEEGVRVVRCGGSRLNFRRAVFSVDSKYIFCVSGDFVKVYSTTTEECVHILHGHTDLVSGILVNPSNHLQLYSCSFDGTIKLWDYVDGILIKTFTIGPKLHAFFIPLHAEDSVFLTISKEEPDIFQLVSVKLPKSTSQDVEARQLTFVLDYINRSPKCIAFGNEGEYVAAVRDFYLSVYFFKKKKTCNFTLPSTKNKKNAKNKFTCVACHPKEDCIASGHMDGKIRLWRNFHSDQKYTYTCLHWHHDMVMDLAFTVTGTSLLSGGRECVLVEWRDGSEKNKEFLPRLGSSIEHISVSPAGDLFCTSHSDNKITVIHRNLDASAVIQGLVKDRSISTGLMVDPRTKALVLNGKPGHLQFYSLQGDKQLYNLDIIQQEYINDEGLTQTELTKAAFGCSGTWLATVEQRQENENELELQMKLWNYSKKTQGFVLNTKIAMPHDDHITALCFNNAESYEKPILVTASRDGHFKVWILTDDSDIYKKAIAWTCDFVGSYHKYQATNCCFSEDGSLLAVSFEEIVTIWDSQTWELKCTFCQRAGKIRHLCFGRLTCSKYLLGTTDNGILCCWNLLSCSIQWSAKLNVRVMEPDPYSDHVAAVAQSSAGSDLFVFKPSEPRPLYIQKNVSREEVQWGVFVPRDVPESFTSETHQWLNRSQFYFLTKSQSLLTFSTKSPEEKLTPTSKQLLAEESLPTTPFSFILGKHRQQQGAKLTETSENELVQLPLTENIPAITELLHTPAHVLPSASFLCSLFVNSLLLSKETKSAEEVPDDVDMEGNKESDDSDEEYDLTEKDKETNNNTDLGEDAIHQLSKSEEKELRKFRKVDYSWLTAL", "text": "FUNCTION: Ribosome biogenesis factor. 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. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. SUBCELLULAR LOCATION: Nucleus, nucleolus."}
+{"protein": "MPDSDNESGGPSNAGEYASAREQDRFLPIANVSRIMKRALPANAKISKDAKETVQECVSEFISFITGEASDKCQREKRKTINGDDLLWAMTTLGFEDYIDPLKLYLHKFRELEGEKAIGAAGSGGGGAASSGGSGSGSGSHHHQDASRNNGGYGMYGGGGGMIMMMGQPMYGSPPASSAGYAQPPPPHHHHHQMVMGGKGAYGHGGGGGGGPSPSSGYGRQDRL", "text": "FUNCTION: Component of the NF-Y/HAP transcription factor complex. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NFYB/HAP3 subunit family."}
+{"protein": "MDLYISNYTSDDDMAILRRRWIELLPLVVGDIVHVENPEGYSYLLDPIIPGPGYVVTWYHQLHCLFFLMSEYDRLLRHGPNGKERSIPAGSSSIHTRHCFEILRHSILCHLDMTLEGGSAPFFNGTTGFGHAHVCQNRQEAIDWMEKNRANDNRMIIRA", "text": "FUNCTION: UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats (PubMed:32929037). The role of vicYa within the pathway has still to be determined (PubMed:32929037). The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster- specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable). SIMILARITY: Belongs to the ustYa family."}
+{"protein": "MSQDTVEIRVEFGGGTELLLAPPHEKKHTLTIPRTDTAGNETNVSFLIGHIRKNLITEREELFVDGDSVRPGILVLINNGDWELEGEGDYVLQDGDEVVFISTLHGG", "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 the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. 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": "MKVQILFALMMVLVTLCLGQKMQRGVIEDVCNNCETNCQLIKDYYGRSFCQDSLCQDSYRFCTNLEFTMDKCKDENSNTHAGCVTALLSTS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the teretoxin C (TC) superfamily."}
+{"protein": "MTQNHNIPTAIQIQNPINNNVSVTISDQLPKPSANNPNLLSVDTRPTHRKGHHHKHSLSHQYFLPPKNRQPLEIPASYPIPTFKETFAILTFPQKLKLTSSILFFLVAVGVLLSGDATILLTLSCSLIVEGVLIIINVWRETLDSFLVWRHTCLRYPFGMQQMELLVDFSFSILLIFLGMNLLKEPAEHAIEDWGNLHHAGDHEEETVHIHLTISLFASAIISGFALLLDHPSAHIRELNSRFFHGLTLVPSLILVLLLSLGYQVGSFLSHLLSLTIAVTALVNGFSIAKSLALMLLLTYSNKEKVFECVSLIKEDTRIDQLNYAAIWQPHYNTCIANIGLTVSGGEREQAAVREDIIRIIQKTVGSIFGAGVQPKWEISVDIQRA", "text": "FUNCTION: Probable transporter involved in the regulation of zinc homeostasis. SUBCELLULAR LOCATION: Cytoplasm Nucleus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily."}
+{"protein": "MALALKQRPSRFRPTTTTYEDNYGYTMNFYQPMLDYLDAKAKGLEVKKPHLPWVSERGLKQYRPSNAVRQYNADEIVRLSRTCAARADEILLNFRAQKRSPFSVQKLVDASRVTKHLEPDTVVERSRQRRRRRQEELEDLIKRDTLKILQRIRKIELDNELDKMSDDFKRSIRGKSASAIAQALLSESEKNIKTAKKEEEDYIAQTLVRSSRAVSRARSRSSSPLDGQYRAHALHIELMDDRLVDKLDHRVSSSLHNVKRQLSTLNQRTVEFYADSSKQTSIEIEQLNARVIEAETRLKTEVTRIKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKRIISKLEARIRDLELELEEEKRRHAETIKILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQEGVSQQTTTRVRRFQRELEAAEDRADTAESSLNIIRAKHRTFVTTSTVPGSQVYIQETTRTITE", "text": "FUNCTION: Paramyosin is a major structural component of many thick filaments isolated from invertebrate muscles. SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. SIMILARITY: Belongs to the paramyosin family."}
+{"protein": "MIKFLLFLAIAAATVISNAELAVPTASISAHVLDISGGSPAGGIQILAFILLNNGWTNIGSQFTQDNGRVDWVSPDFTLIPGTYRLVYITEPYYTAKNVESFYPYVEVVFNIRNATQHYHVPLTLSPWGYSTYRGS", "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": "MAIKGPRKHLKRLAAPANWQLPRKERTFTVRPSPGPHSMDKSLPLLLIVRDTLKCADNAREAKKIIQMGKILIDGVKRKEYKHPVGLMDVLSIPELNENYLVLFDENGRISLKKTEKTGVKLCKIVNKTVIKGGHIQLNLHDGRNQIVKVANALKAEEDIYKTGDSVLVSLPEQAVVGHVEFNEGKLAYITGGKHVGEFAKVVEVEKRTLYSDIVTLENKDGEKFKTIKPYVFIVGQDEPVISM", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family."}
+{"protein": "MPQLDKFTYFTQFFWSCLFLFTFYIAICNDGDGLLGISRILKLRNQLLSHRTNNIRSKDPNSLEDILRKGFSTGLSYMYSSLFEDSQWCKAVDLLGKRRKITLISCFGEISGSRGMERNIFYLISKSSYSTSSNPGWGITCRNDIMLIHVPHGQGSIGF", "text": "FUNCTION: This is one of the chains of the nonenzymatic component (CF(0) subunit) of the mitochondrial ATPase complex. SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase protein YMF19 family."}
+{"protein": "MPGLTIGDTIPDLEVDTTQGKIKLHHFCSDSWTILFSHPGDFTPVCTTELGKMAQYASEFNKRGVMLLGMSCDDLESHKEWIKDIEAHTPGAKVNYPIISDPKREIIKQLNMVDPDEKDSNGNLPSRALHIVGPDKKIKLSFLYPAQTGRNMDEVLRVVESLQKASKYKIATPANWKPGEPVVISPDVTNDQAKEMFPQGFKTADLPSKKEYLRFTNV", "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": "MAVPPRPLQLLGILFIISLNSVRLIQAGAYYGIKPLPPQIPPQIPPQIPQYQPLGQQVPHMPLGKDGLSMGKEMPHMQYGKEYPHLPQYMKEIPPVPRMGKEVVPKKGKGEVPLASLRGEQGPRGEPGPRGPPGPPGLPGHGMPGIKGKPGPQGYPGIGKPGMPGMPGKPGAMGMPGAKGEIGPKGEIGPMGIPGPQGPPGPHGLPGIGKPGGPGLPGQPGAKGERGPKGPPGPPGLQGPKGEKGFGMPGLPGLKGPPGMHGPPGPVGLPGVGKPGVTGFPGPQGPLGKPGPPGEPGPQGLIGVPGVQGPPGMPGVGKPGQDGIPGQPGFPGGKGEQGLPGLPGPPGLPGVGKPGFPGPKGDRGIGGVPGVLGPRGEKGPIGAPGMGGPPGEPGLPGIPGPMGPPGAIGFPGPKGEGGVVGPQGPPGPKGEPGLQGFPGKPGFLGEVGPPGMRGLPGPIGPKGEGGHKGLPGLPGVPGLLGPKGEPGIPGDQGLQGPPGIPGIVGPSGPIGPPGIPGPKGEPGLPGPPGFPGVGKPGVAGLHGPPGKPGALGPQGQPGLPGPPGPPGPPGPPAVMPTPSPQGEYLPDMGLGIDGVKPPHAYAGKKGKHGGPAYEMPAFTAELTVPFPPVGAPVKFDKLLYNGRQNYNPQTGIFTCEVPGVYYFAYHVHCKGGNVWVALFKNNEPMMYTYDEYKKGFLDQASGSAVLLLRPGDQVFLQMPSEQAAGLYAGQYVHSSFSGYLLYPM", "text": "FUNCTION: Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also a component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis. FUNCTION: Vastatin, the C-terminal fragment comprising the NC1 domain, inhibits aortic endothelial cell proliferation and causes cell apoptosis. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane."}
+{"protein": "MYGQQNNYGAPPPQQWGQAPPQGYQPGYQNGPPAVNYGAHPSQQQQWGAPPGPPQHQPYGAPPVNQYGAPPQHQQGYGGHSPQPPFGAPSPAPAGYGAPPTAPQGQYGAPSPYPQQPPQQGFGGPQQGYGSQPQGQSPMMYLGVPIPAPPPAVPVSTLAGYDARFDAERIRKATKGFGTDERTIIDTLSPLDAFQMDVLSRTYEQTVGRSLKSTLEKELSSWLEYTLVLLSLGPLGGDVYLLHRACNGMGTHEDLLNEVLLGRTNQEIFLLKEAYRRTYNQDLVQIVQGELSMKTERMFNMALSGQRDESPYLNHQLVQQDVETLYRAGPGKIGTDEIAICGILISRSKEHLKAIAQAFPARHRVSLSQMIHSEFSGHMRDALFFIARGVEADGDGVVRDCELLHAAMAGMGTKDERMIYRLVRNHWNRPRFNAIKNQYQVLYRNSLRRAVEGETTGKYEKALVGIIEQN", "text": "FUNCTION: Does not appear to play a major role in virulence (PubMed:31140968). May play a role in titan cell formation (PubMed:31140968). SIMILARITY: Belongs to the annexin family."}
+{"protein": "MAHSKEIPSFRWTQSLRRGLSQVHPTVKTDVLKDAKLIADSIDFNQVSQVQRALRKNKRGEEDLNKLRDLNKEVDRLMSMKSIQKNTIFKIGDLGRDELMELASDLEKLKNKIKRTESGPQGLYMGNLSQLQLTKRSEILKTLGFQQQRGAGNGVVRIWDVSDPSKLNNQFGSMPALTIACMTVQGGETMNSVVQALTSLGLLYTVKYPNLNDLDKLTLEHECLQIVTKDESSINISGYNFSLSAAVKAGASILDGGNMLETIRVTPDNFSSLIKSTLQVKRKEGMFIDEKPGNRNPYENLLYKLCLSGDGWPYIGSRSQILGRSWDNTSVDLTKKPQVGPRQPEKNGQNLRLANLTEMQEAVIKEAVKKLDPTNTLWLDIEGPPTDPVELALYQPANKHYIHCFRKPHDEKGFKNGSRHSHGILMQDIEDAMPGVLSYVIGLLPQDMVITTQGSDDIRKLLDIHGRKDLKLVDVKLTSDQARLYDQQIWEKFGHLCKHHNGVVVNKKKREKDSPFKLSSGEPHCALLDCIMYQSVMDGKMVDEEPVALLPLSLLFLPKAAFAL", "text": "FUNCTION: Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in other negative strain RNA viruses. Through the interaction with host IKBKE, strongly inhibits the phosphorylation and nuclear translocation of host IRF3, a protein involved in interferon activation pathway, leading to the inhibition of interferon-beta and IRF3-dependent promoters activation. Encodes also a functional 3'-5' exoribonuclease that degrades preferentially dsRNA substrates and thereby participates in the suppression of interferon induction. SUBCELLULAR LOCATION: Virion Host cytoplasm. SIMILARITY: Belongs to the arenaviridae nucleocapsid protein family."}
+{"protein": "MEPEEGTPLWRLQKLPPEQGAGLLHKIIDGFCGRAYPAHQDYHSVWNSAEWKHVLEDVTTFFKAVVGKNFSEEETLQQLNQLNSCHQEAVLKCLKSRRNEIKQALLGEIVDISCAQLQDFDWQLKLALSSDKIATLQMPLLNLHLDVKEDDKVKPYTVEMSKEELQSLISSLEAANKVVLQLK", "text": "FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MSRSFRNGFRLLKLSQMDFERAWWDMANLFRAPRRVYRSITLRKQNINRYGREDFSFIVLFSCMIVISALLWALFYMNTPKGYVTTITFMLFVDFGAVGVIMATMYYFIAKRFLMKSNDTILSSTDYQLEWNYCFDVHCNSFFPSFVLLYVIQLFLLPVITRDNFISLFMGNTLYLVALCYYSYLTFIGYQILPFLKNTHALLLPIPMFFIMWALSLLGFNVPKHVVDVYFGKSA", "text": "FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the unc-50 family."}
+{"protein": "MEAPAQLLFLLLLWLPDTTGEIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWP", "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:20176268, PubMed:17576170). SUBCELLULAR LOCATION: Secreted Cell membrane."}
+{"protein": "MIKKIGVLTSGGDAPGMNAAIRGVVRSALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFVVVPEVEFSREDLVNEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIDLLLAGYGGRCVGIQNEQLVHHDIIDAIENMKRPFKGDWLDCAKKLY", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (PubMed:3158524, PubMed:2953977). In addition, is involved in the utilization of D-sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway, via the sedoheptulose bisphospate bypass pathway (PubMed:19756045). Catalyzes the phosphorylation of D- sedoheptulose 7-phosphate to D-sedoheptulose 1,7-bisphosphate (PubMed:19756045). 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: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub- subfamily."}
+{"protein": "SQPHTKPSVFVMKNGTNVACLVKEFYPKDIRINLVSSKKITEFDPAIVISPSGKYNAVKLGKYEDSNSVTCSVQHDNKTVHSTDFEVKTDSTDHVKPKETENTKQPSKSCHKPKAIVHTEKVNMMSLTVLGLRMLFAKTVAVNFLLTAKLFFL", "text": "FUNCTION: Constant region of T cell receptor (TR) delta chain that participates in the antigen recognition (PubMed:24600447). Gamma-delta TRs recognize a variety of self and foreign non-peptide antigens frequently expressed at the epithelial boundaries between the host and external environment, including endogenous lipids presented by MH-like protein CD1D and phosphoantigens presented by butyrophilin-like molecule BTN3A1. Upon antigen recognition induces rapid, innate-like immune responses involved in pathogen clearance and tissue repair (PubMed:28920588, PubMed:23348415). Binding of gamma-delta TR complex to antigen triggers phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the CD3 chains by the LCK and FYN kinases, allowing the recruitment, phosphorylation, and activation of ZAP70 that facilitates phosphorylation of the scaffolding proteins LCP2 and LAT. This lead to the formation of a supramolecular signalosome that recruits the phospholipase PLCG1, resulting in calcium mobilization and ERK activation, ultimately leading to T cell expansion and differentiation into effector cells (PubMed:25674089). Gamma-delta TRs are produced through somatic rearrangement of a limited repertoire of variable (V), diversity (D), and joining (J) genes. The potential diversity of gamma-delta TRs is conferred by the unique ability to rearrange (D) genes in tandem and to utilize all three reading frames. The combinatorial diversity is considerably increased by the sequence exonuclease trimming and random nucleotide (N) region additions which occur during the V-(D)-J rearrangements (PubMed:24387714). SUBCELLULAR LOCATION: Cell membrane."}
+{"protein": "MFGETGTGDALRPIFMDVVSVQSQVVYGHVGNNVALPTLRAHGLNVAAVPTVMFSNTPHYPTLHGGALPIDWFGGYLSDLSARGALQRLKAILVGYLGNPEQVAVLSRWINQVLAEHPDVQVIVDPVIGDHDTGIYVADGMVEAVRELLLPLAHGLTPNDFELGHLSGRSADSVEQVVAAARSLLTDRVQWMVVTSAAPGTWGHDDMKLLIVTRDDAQVLSHPRIPVSPKGTGDLFSAKLTARLLEGMPLAEAAASASDHVVTALEATRRAQSLELQLPSNPCITHRE", "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": "MMNLIPKTNFDFLKIRKYFYAVSAIILIAGLICILTRGLNMGIDFKGGTMVQVQFTESITIDQVRSAVEKYNPEIQSYVGKNTYMIKIKGSQENVNEVRSDVETSLTAAKLKFTVVATDFVGPTVGKDLGERALWALALSLVFMVLYIAFRFQNIIWGTAGVIALIHDAFFMVAAFAFLQKEFDLVIVAALLTAVGYSINDNIVIFDRMRENIKENPKESFYNIVNRSLNETLSRTVITGSTVLIVLVIIYFFGGEVLKNFSLIMLIGVIVGTYSTLFIATPIVYDWAKDSDNFAKTVGNQDVALAAEIKTAKKHNKKKHR", "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 inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily."}
+{"protein": "MSDDTKSPHEETHGLNRRGFLGASALTGAAALVGASALGSAVVGREARAAGKGERSKAEVAPGELDEYYGFWSGGHSGEVRVLGVPSMRELMRIPVFNVDSATGWGLTNESKRVLGDSARFLNGDCHHPHISMTDGKYDGKYLFINDKANSRVARIRLDVMKCDRIVTIPNVQAIHGLRLQKVPHTRYVFCNAEFIIPHPNDGSTFDLSGDNAFTLYNAIDAETMEVAWQVIVDGNLDNTDMDYSGRFAASTCYNSEKAVDLGGMMRNERDWVVVFDIPRIEAEIKAKRFVTLGDSKVPVVDGRRKDGKDSPVTRYIPVPKNPHGLNTSPDGKYFIANGKLSPTCTMIAIERLGDLFAGKLADPRDVVVGEPELGLGPLHTTFDGRGNAYTTLFIDSQLVKWNLADAVRAYKGEKVDYIRQKLDVQYQPGHNHATLCETSEADGKWIVVLSKFSKDRFLPTGPLHPENDQLIDISGEEMKLVHDGPTFAEPHDCILARRDQIKTRKIWDRKDPFFAETVKRAEKDGIDLMKDNKVIREGNKVRVYMVSMAPSFGLTEFKVKQGDEVTVTITNLDEIEDVTHGFVMVNHGVCMEISPQQTSSITFVADKPGVHWYYCSWFCHALHMEMCGRMLVEKA", "text": "FUNCTION: Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the NosZ family. SIMILARITY: In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family."}
+{"protein": "MMNRVIPLPDEQATLDLGERVAKACDGATVIYLYGDLGAGKTTFSRGFLQALGHQGNVKSPTYTLVEPYTLDNLMVYHFDLYRLADPEELEFMGIRDYFANDAICLVEWPQQGTGVLPDPDVEIHIDYQAQGREARVSAVSSAGELLLARLAG", "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 probably 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. Displays ATPase activity in vitro. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TsaE family."}
+{"protein": "MAESDDEYDRKRRDKFRGERDSYRPERRDDRRPMGGGAGNARDEWAERNPFRGSAAAGGGGGGGGVGGGGGARHRPDYSDYRGSGPRPRYGSPGREMPPAKRMRPDWGDGEMRANPRFGYDPYLVQAWNDHYQSLHSAYSHSGHAPSAREPPPSGISNSDTQTQPAMLTLKQFLDTQDENISDSEVMRKYTEYKTDFKRQQLNEFFVAHKDEEWFKNKYHPEDSVRRSDEQRGFLKRRTDVFLELLNNGTISNVKVDSSQADALVRVLDTCVIKLEGGTDEDLKILDEKPKDPAPVYERRSERSERSEATESVVVTKREPESPKHQTKSEKDDDDLPEVESPQRKNVRPVNSDDEDWDDDEEMPAAKSEQQSELAAEKPAKQLNDEESMQANIDKNQKKSKKRKRTSSDDESSSSSSSESDSDSDDEKLIEKYDVEEGLRADQKAEAEKDKEEEEERAATAAAKAKQLPPDSPTPDEDVDAAAVEEQKNEVVAIKTEVNDEESQKTEQPAAEEEKSEQPKDDPEASSKNGEENEEEKAEKSEADTATTKAAAAAADDDAMTETIDVDKLKDSLKPRALHRTSSIFLRNLAPSITKAEIETICTRFSGYLRVAIADPLVERRWYRRGWITFTRDVNIKEICWSLNNQRLRDCEMGAIVNRDLSRRVRPANGITAHKQIVRSDIKLCAKIAMNLDERFKLWSEVDNADNAELNPEELKEATNGSGSYGFNSKNPVLQNITDYLIEEASAEEEELLGLAGDSKDGEGEPIERDEPLIQVLDRLVLYLRVVHSVDYYNHCEYPYEDEMPNRCGIIHARGPAPMRVTSNDVQEYIKSYEGKLQQFLAKTVQLSDENIKELGAKNPEKEVEKFVQANTQELAKDKWLCPLSGKKFKGPEFIRKHIFNKHEEKVDEVRKEVQYFNNYLRDPKRPQLPEHPGSSKRTESESGRGSGGYRPPMYPPFSAMPYGFAPPMMGGGGRGGRNFPQARREMPVEHQRRLIGYHDLDAPVNSDMFD", "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 containing drosha and pasha (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARS2 family."}
+{"protein": "MSGLLTSASSSASKTLESAMGQSLTESANAQASKMKMDTQNSILDGKMDSASKSLNSGHNAAKAIQF", "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": "MQGKCWFLENKALKPFVCFYGGDQFLYIGDRIVSYFSTNDLYVALRGRIDKDLSLSRKVELYNGECVYLFCEHPAVGIVNTDFKLEIH", "text": "SIMILARITY: Belongs to the coronaviruses NS4b protein family."}
+{"protein": "MTEKFLFLYLSLLPMPLLSQAQWNENSLVSFSKIIASGNHLSNCWICHNFITRSSSYQYILVRNFSLNLTFGSGIPEGQHKSVPLQVSLANSAHQVPCLDLTPPFNQSSKTSFYFYNCSSLNQTCCPCPEGHCDRKNTSEEGFPSPTIHPMSFSPAGCHPNLTHWCPAKQMNDYRDKSPQNRCAAWEGKELITWRVLYSLPKAHTVPTWPKSTVPLGGPLSPACNQTIPAGWKSQLHKWFDSHIPRWACTPPGYVFLCGPQKNKLPFDGSPKITYSTPPVANLYTCINNIQHTGECAVGLLGPRGIGVTIYNTTQPRQKRALGLILAGMGAAIGMIAPWGGFTYHDVTLRNLSRQIDNIAKSTRDSISKLKASIDSLANVVMDNRLALDYLLAEQGGVCAVINKSCCVYVNNSGAIEEDIKKIYDEATWLHDFGKGGASARAIWEAVKSALPSLNWFVPLLGPATVILLLFLFGPCFFNLLIKCVSSRIKQFHMKSPQMERYQLSVIGGPSTYKHISPLDASGQRFRETMEEFSL", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the gamma type-C retroviral envelope protein family."}
+{"protein": "MSRFIVFAFIVAMCIAHSLAAPAPEALEASVIRQKRLTCDLLSFEAKGFAANHSLCAAHCLAIGRKGGACQNGVCVCRR", "text": "FUNCTION: Shows very strong activity against S.aureus. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the invertebrate defensin family. Type 1 subfamily."}
+{"protein": "MADDIDIEAMLEAPYKKDENKLNSANGHEERSKKRKKSKSRSRSHERKRSKSKERKRSRDRERKKSKSRERKRSRSKERRRSRSRSRDRRFRGRYRSPYSGPKFNSAIRGKIGLPHSIKLSRRRSRSKSPFRKDKSPVREPIDNLTPEERDARTVFCMQLAARIRPRDLEEFFSTVGKVRDVRMISDRNSRRSKGIAYVEFVDVSSVPLAIGLTGQRVLGVPIIVQASQAEKNRAAAMANNLQKGSAGPMRLYVGSLHFNITEDMLRGIFEPFGRIESIQLMMDSETGRSKGYGFITFSDSECAKKALEQLNGFELAGRPMKVGHVTERTDASSASSFLDSDELERTGIDLGTTGRLQLMARLAEGTGLQIPPAAQQALQMSGSLAFGAVAEFSFVIDLQTRLSQQTEASALAAAASVQPLATQCFQLSNMFNPQTEEEVGWDTEIKDDVIEECNKHGGVIHIYVDKNSAQGNVYVKCPSIAAAIAAVNALHGRWFAGKMITAAYVPLPTYHNLFPDSMTATQLLVPSRR", "text": "FUNCTION: RNA-binding protein that acts as a pre-mRNA splicing factor. Acts by promoting exon inclusion via regulation of exon cassette splicing (By similarity). Also acts as a transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1, independently of the pre-mRNA splicing factor activity (PubMed:11704680). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family."}
+{"protein": "MPSSAQNVGIKALEIYFPSRYVPQTELETFLGASAGKYTIGLGQQNMSFCDDREDLYSLALTAVSSLLRKYAIDPNTIGRLEVGTETLLDKAKSCKTVLMQLFGDNTDIEGVDTYNACYGGTNALFNAVNWIESSSWDGRDAIVVAGDIALYETPAARPTGGAGCVAMLIGPDAPLVLEPVRGSCMKHVYDFYKAYFKSEYPLVDGQFSNTCYLGALDACYQRYQAKQRARQAAKTNGTAISNGHQGSFLDTFDYFAFHAPNCKLVAKGYGRLLFNDFKLESGSFDEVPAQVREADFAASLTDKALEKLCVSLTKERFVQRVEPSLTAPTNCGNMYTASVYAGLISLISNVPSDRLQDKRIGMFSYGSGLASTLFSFRVKGDTTEMARKIGLQDRLSARTAVSPEFYDQMCKLREKAYQQRNYTPEGSVESLAPGTYFLVHVDDAYRRKYDMKPYLSMCEDRHEQAV", "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). Erg13A and erg13B condense 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 erg10B that catalyzes the formation of acetoacetyl- CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate- limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (PubMed:16110826, PubMed:22106303) (Probable). SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase family."}
+{"protein": "MLKGLYTATSAMIAQQRRTEMLSNNIANANTSGYKADQGSMRAFPEMLLSRIESKSPAGTSRTEIGSVNTGVYMQELKPLFTQGSLKSTDQPTDIALIENQVPMSAETNEKAALFYPVQTADGIRYSKSSTFSLNENNQLTINGRPILSTDRQPITVDNENFTVSENGTVTTNGRTAGQIDVRMAEDVRNLKRDGNDLYSTADGNDLPSAAGNNQVAYSLKQGVSELSNVDVTSAYTEMTEAYRSFEANQKVIQAYDKSMDKAANEIGKI", "text": "FUNCTION: Not required for motility. SIMILARITY: Belongs to the flagella basal body rod proteins family."}
+{"protein": "MTEIVADKTVEVVKNAIETADGALDLYNKYLDQVIPWQTFDETIKELSRFKQEYSQAASVLVGDIKTLLMDSQDKYFEATQTVYEWCGVATQLLAAYILLFDEYNEKKASAPH", "text": "SIMILARITY: Belongs to the hemolysin E family."}
+{"protein": "MRIERVDDTTVKLFITYSDIEARGFSREDLWTNRKRGEEFFWSMMDEINEEEDFVVEGPLWIQVHAFEKGVEVTISKSKNEDMMNMSDDDATDQFDEQVQELLAQTLEGEDQLEELFEQRTKEKEAQGSKRQKSSARKNTRTIIVKFNDLEDVINYAYHSNPITTEFEDLLYMVDGTYYYAVYFDSHVDQEVINDSYSQLLEFAYPTDRTEVYLNDYAKIIMSHNVTAQVRRYFPETTE", "text": "FUNCTION: Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. SIMILARITY: Belongs to the MecA family."}
+{"protein": "MLYALLLLFGGVSTVSSLRVAVVGEGVIGLSTATAILDLAEKRNIPAPEIHIFHHKPFEKILSRHIAGLFRIDSGSEIDRKYGYDTFEKLATLWREYGGLSGVQLVSGHILSDSKTKLDSQRESYGSLVYNYRDLAEPELFGPTSLFDLPRNTTTRGIHYTAYTSEGLRFCPFLKKELMTKGVRFTQRRIGNLEELGAEFDVVVNSAGLLGGVLAGDDAGNMKPIRGVLIRVDAPWQKHFLYRDFSTITIPVIDHVYMGTVKQEGAFGPNNVTSADIQDITSRYVALQPSFKRVHMLSSFVGYRPGRKQVRVEKQIRETNGSKKFTVVHNYGHSGNGFTLGYGSAVHAAHIVLDLPLDAYHGLVPEPLPINATISEWVKYLDD", "text": "FUNCTION: Selectively catalyzes the oxidative deamination of D- aspartate and its N-methylated derivative, N-methyl D-aspartate. Has no activity towards L-amino acids or N-methyl-L-aspartic acid. May play a role in the egg-laying events and maturation processes of the reproductive organs. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the DAMOX/DASOX family."}
+{"protein": "MGNLQQLALDADIAAVKQQEKLLRLPEFNEDIAWQLGSYIRQIAVQKNYPIAITVARFNQPLFYCAMPNSSPDNKNWLRRKAATVAHYYTSSYAVGLKLKKKGVTTLSGYGLDDKDYATHGGAFPITVEKAGIVGYIAVSGLDQRDDHALVVQALAVHLGLPAEKTALEYLTQDSLGKARLDETIV", "text": "SIMILARITY: Belongs to the UPF0303 family."}
+{"protein": "MPVKVYAEEMEGESMKKKKLSETPLPKIKKRKMKNGDTEDLDLEHMAESVNGEINNNNPTPKLKKKKKPAPISDLSETAEECDGEQPDPSTPTPKKVKKKKIKESKEDSDTQEEAEQSEPQTNGVKSVKKSKKNITSDDNEPAPKKRKTDTTEITTAKECEEKVLTKEEQDINQEKIDGDFSKFPLSKETIKNLQAKGVSYLFPIQSKTFHTAYSGKDVVVQARTGTGKTFSFAIPLVEKLNEDQQPLARGRAPRVIILTPTRELAIQITNEIRSITKKLKVSCFYGGTPYQQQVFAIKDGIDFLVGTPGRVRDLVQNYRLDLTTLKHVVLDEVDMMFDMGFSEQVEEILSVRYKADPEENPQTLLFSATCPDWMYNMAKKYMRKQFEKIDLIGHRSQKAATTVEHLAIECTRSQKAAVLGDLVQVYSGSHGKTIIFCDSKLEAHTLATSCGSLKQSAKSLHGDLQQKEREVVLKGFRQGTFEVLIATNVAARGLDIPEVDLVVLYSAPKEADAYVHRSGRTGRAGRTGVCISLYEPWERHYLRNVERSTGITFKRVGVPSLLNVAKSSSADAIKSLDTVPADVIEHFKEYAQELIEQKGALTAIAAALAHISGATSIKQRSLLNMEAGCDTITLKSSVPIHSLSYAWQSIKEQLGDDVDSKIHRMCLLKDSMGVCFDVRSENLESMQERWTDTKQWQFTVATELPAIQESERNFDGPRNRGFGGRGRRPFDRRNNSRNSNRGGGGRGRNRNGGFRRGR", "text": "FUNCTION: RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (By similarity). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (By similarity). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification (PubMed:12851405) (Probable). Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre- ribosomal complexes (By similarity). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (By similarity). Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Cytoplasm, cytosol Mitochondrion. SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily."}
+{"protein": "MHASLSSWLLAASLLTQPISVSGQGCPFAKRDGTVDSSLPQKRADAPETTTFGRCAVKSNQAGGGTRSHDWWPCQLRLDVLRQFQPSQNPLGGDFDYAEAFQSLDYEAVKKDIAALMTESQDWWPADFGNYGGLFVRMAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLTGNVALENMGFKTLGFGGGRADTWQSDEAVYWGAETTFVPQGNDVRYNNSVDINARADKLEKPLAATHMGLIYVNPEGPNGTPDPAASAKDIREAFGRMGMNDTETVALIAGGHAFGKTHGAVKGSNIGPAPEAADLGMQGLGWHNSVGDGNGPNQMTSGLEVIWTKTPTKWSNGYLESLINNNWTLVESPAGAHQWEAVNGTVDYPDPFDKTKFRKATMLTSDLALINDPEYLKISQRWLEHPEELADAFAKAWFKLLHRDLGPTTRYLGPEVPKESFIWQDPLPAREGDLIDDADVDKLKAAILSTDGLDVSKLASTAMACATTYRNSDKRGGCNGARIALEPQRNWVSNNPTQLSAVLDALKKVQSDFNGSNGNKKVSLADLIVLGGTAAVEKAAKDAGVDIKVPFSAGRVDATQEQTDVTQFSYLEPQADGFRNYGRGTARARTEEIMVDKASQLTLTPPELTVLVGGMRALGANYDGSDVGVFTANKGKLTPDFFVNLVDMNIAWTASGADGESWVGTDRKSRSEKYKGSRADLVFGSHAELRAIAEVYAENGNQEKFVKDFVAAWTKVMNLDRFDLKVKK", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
+{"protein": "MKKALITGITGQDGSYLAEFLLEKGYQVHGIKRRSSSFNTSRIDHIYQDPHEVNPHFFLHYGDLTDTSNLIRLVKEIQPDEIYNLGAQSHVAVSFESPEYTADVDAMGTLRLLEAVRINGLEHKTRFYQASTSELYGLVQEIPQRETTPFYPRSPYAVAKMYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIALGLEDCLYLGNMDSLRDWGHAKDYVRMQWMMLQQDQPEDFVIATGKQITVREFVRMSAKEAGIEIEFSGKGIDEIATISAISDEYATSAKVGDIIVRVDPRYFRPAEVETLLGDPSKAKEKLGWVPEITVEEMCAEMVAGDLQQAKQHALLKANGFDVSITLES", "text": "FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6- deoxy-D-mannose. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily."}
+{"protein": "MDIKRTILIAALAVVSYVMVLKWNDDYGQAALPTQNTAASTVAPGLPDGVPAGNNGASADVPSANAESSPAELAPVALSKDLIRVKTDVLELAIDPVGGDIVQLNLPKYPRRQDHPNIPFQLFDNGGERVYLAQSGLTGTDGPDARASGRPLYAAEQKSYQLADGQEQLVVDLKFSDNGVNYIKRFSFKRGEYDLNVSYLIDNQSGQAWNGNMFAQLKRDASGDPSSSTATGTATYLGAALWTASEPYKKVSMKDIDKGSLKENVSGGWVAWLQHYFVTAWIPAKSDNNVVQTRKDSQGNYIIGYTGPVISVPAGGKVETSALLYAGPKIQSKLKELSPGLELTVDYGFLWFIAQPIFWLLQHIHSLLGNWGWSIIVLTMLIKGLFFPLSAASYRSMARMRAVAPKLAALKERFGDDRQKMSQAMMELYKKEKINPLGGCLPILVQMPVFLALYWVLLESVEMRQAPWILWITDLSIKDPFFILPIIMGATMFIQQRLNPTPPDPMQAKVMKMMPIIFTFFFLWFPAGLVLYWVVNNCLSISQQWYITRRIEAATKKAAA", "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. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily."}
+{"protein": "MVKVGLVDDYRVDLEKLEAIVSRMQDVEIVFSTDSAKEAYRRVKNGDIDLLLADIEMPHMSGYELADLIKSHSLDVDVIFVTGHGGYAVHAFDLNVHDYIMKPYYADRLAASFDRYLKKKTETSLNGRILIKQKSEMHVLQKKDIIFAERTGRSTTIVTTAEEVQTYQTLNDIKGDLPEKDFLRSHRSFIINIHYIKHFSAYTKHSFTVSFEGTSKKAMITKQQLDYFQNYYF", "text": "FUNCTION: Member of the two-component regulatory system NatK/NatR that positively regulates the expression of the natAB operon. Acts by binding directly to the promoter of natAB. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MKSYEIALIGNPNVGKSTIFNALTGENVYIGNWPGVTVEKKEGEFEYNGEKFKVVDLPGVYSLTANSIDEIIARDYIINEKPDLVVNIVDATALERNLYLTLQLMEMGANLLLALNKMDLAKSLGIEIDVDKLEKILGVKVVPLSAAKKMGIEDLKKAISIAVKDKKTAEIKYPNFEPYIKKITSILQKDEDLKKYNLRYLAIKLLENDKYVEEIVKNSKVWNELKPVLDSIINELSKKYGEAELGIVEERYKVIDKIVKEVMKKTSGKLTTTEMLDDVLTDEKIGTLLIIPFLWMLFKFTFDVSKPFSAMIEYFFGFLSEVVKSSISNKFIASLLADGIISGVGAVLVFFPILAFLFFAISFLEDSGYMARIPFITDRIMNKFGLPGKAVISMVMGFGCNVPAIMATRTIEDEKDRILTILINPLLSCSARLPIYALFAGALFSKYQGVVILSMYALGVVLALITAFLFRKLIFKTSPSYLIVELPPYHIPHLNVVLKNTWERVYDFLRKAGTIIVFGVILVWVLSVYGPSGYLGEEVFENPQLIANSWVAVIGKTLAPLFSPMGWDWRACSALVFGIIAKEVVVGSLAMLYGTGEENLSSVIAHAFSPVSAYAFMAFSLIYLPCIATLAVIKQEIGWKWALFAVTYEMILAYVVALVISVIGNLLF", "text": "FUNCTION: Probable transporter of a GTP-driven Fe(2+) uptake system, might be able to transport Fe(2+) into or out of the cell (Probable). SUBCELLULAR LOCATION: Cell 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": "MGVTCVTQVPVLEGKSVQQTVELLSKKLELLGAEKHGAFGVDCETYHTAAAISSQGQTGKLMYVMHNSEYPLSCFALFENGPCLIADANFDTLMVKLKGFFQNAKANKIESRGTRYQYCDFLVKVGTVTMGPSARGISVEVEYCPCVIANDCWNLLMEFMQSFMGSHTPGIPSVFGTKHDSIYSPADTMVQYMELFNKIRKQQQVPVAGIR", "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": "MSFSKWGGKPSNSSEKQKASSTPTVEEINRGVGDIGLNSEQNEGWEVYARKPKNKGGSSAGKQWAPQNPSPKAWGNQNTKAWGHPDVGKKSGTRNNAGSGRGSGNNWSTPSDPQKLARPHLYDGGFPSSAPVPPALKNGWDWSSRVASAHPKDNSQVAAAADDDKASEHDAEDNELDFLDESDDDLHSDDFDSDVGEMSYETRKKNPWFNQLFHSLDSLTVTEINEPERQWHCPACKGGPGAIEWFTGLQSLMTHAKTKGLRVKIHRELAELLEEDLRQRGTSVVPPGEVYGRWGGMEFKDKEIVWPPMVIIMNTRLDKDENDKWIGMGNQELLEYFSSYAAVKARHSYGPQGHRGMSLLIFEASAVGYIEADRLSEHFSENGRNRDAWERRSARFYPGGKRLLYGYMADKKDIDNFNQHSAGKSKLKFEMRSYKEAVWNPAKQMREDNQQLIWFKNKAAKHQMQAKALEESLSLVSEKHRQTLEENKIVRLKTKMHHEQIKEEMEFQEQFFKDQIKIIHDARTAREDNFEKTQQEQREMVKQSNANTASVEDHRVRAEKVAKFIKLQDKEMEEFVEERENLMRTHDDRIAALRRKYWEEEVELERKFDLELSKLMEKYSPKQSDEVNSSGTM", "text": "FUNCTION: Required for post-transcriptional gene silencing and natural virus resistance. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). SIMILARITY: Belongs to the SGS3 family."}
+{"protein": "NPVVRITNGAIRGQN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
+{"protein": "MFDGARLAQGLPYYISQVVFYPFEIYNSMSIVDVISRQDELDSPKAKPHVNATVFDSWWFDAVSNNLTKESITVVFYNAGPESIGAPDLGGPLFVEISGTFDNGTKFTIGSTAPEGAVIESGTQGIRGDWMGSGCSFTGSDLHRPSPEYTVSIDNAGLGVFGKLTLQSVSPPHFAGGSNKPGVSPELIPNIYAAFAQPDAAAVVDFTINGKTLKFNGVGHHEKNWGTAALEASVKAWYWGHGRVGPYSLVWFDGVTPGGKEYFASLITENGKIVSQSCEPNSVVVRPWGENDEFPPVRGAAAPAGYTLRYALGHGMAFVANFTREVSQVEADTYKRMIGSFSGGMEGGEQYEGRALCDQFQF", "text": "FUNCTION: Quinolone epoxide rearrangement protein; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group (PubMed:25859931). The first stage is catalyzed by the nonribosomal pepdide synthetase penN that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (By similarity). 4'-methoxycyclopeptin is then converted to 4'- methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (By similarity). PenM also converts its first product methoxydehydrocyclopeptin to 4'- methoxycyclopenin (By similarity). The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL (By similarity). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD- dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene (PubMed:25859931). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2 (PubMed:25859931). The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD-dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group (PubMed:25859931). The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C (PubMed:25859931, PubMed:28114276). PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D (PubMed:28114276). Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone (PubMed:28114276). SIMILARITY: Belongs to the quinolone epoxide rearrangement protein penF family."}
+{"protein": "MPTIRGQSILIIGGSSGIGAAVAKYACGDGVKVSVASSNKGRVEKALKKIQALVPASEILGFTVDLSQYDLESRLEKLFKEVVDATGGPLDHVVMTAGTGNMVSLSEYTAKAFQESAPLHFIAPLMVGKVAPRFMNRHWKSSITFTSGAFGKKPAKGYCVIASAVGALDAATRALALELAPIRVNAVSPGPTVTEMFGPPSEALDKAVAAMGAQSLLGKLGRPEDVAEAYIYLMRDANTTGTIVDSNGGAFLQ", "text": "FUNCTION: Short-chain dehydrogenase/reductase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP) (PubMed:25015739). The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13 (PubMed:25015739). The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8 (PubMed:25015739). Of the CAC's other predicted gene products, the reducing PKS ATR6 might synthesize a polyketide chain (PubMed:25015739). This polyketide is probably transferred onto the atranone backbone by the polyketide transferase ATR5 (By similarity). Other predicted CAC products include 4 oxygenases (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9, and ATR10), and a methyltransferase (ATR12) (PubMed:25015739). These may all be involved in the various steps of atranone biosynthesis, although their specific roles must await experimental determination (PubMed:25015739). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MIINAKGPASFAEKYIVRSIWENKFPPGSILPAERELSELIGVTRTTLREVLQRLARDGWLKIQHGKPTQVNNFWETSGLNILETIADLNPDGFPLLVDQLMAARGNVSNIYFRASIRHNPEKVVEVLAGIHSLENDAEAYATFDYQLHHTLAFASGNPLYVLILNGFKGLYNRVGRYYFSSQEARELTMRFYLKLEKLAQDKNYSDVPALMRTNGIESGKMWQKLRDDLPAEMGHDKS", "text": "FUNCTION: Multifunctional regulator of fatty acid metabolism. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MASHSQVLVEEKSSVRILTFNRPKQLNALSFHMVSRLLQLFLAYEEDPSVKLVVLKGQGRAFSAGGDIPPIVRDILQGKLIRGAHYFKVGYTLNYVLSTYRKPQVSILNGIVMGGGAGLSTNGRFRIATENTVFAMPETALGLFPDVGASYFLSRLPGFFGEYVGLTGARLDGAEMLACGLATHFVPSISLTALEAELYKVGSSNQTFISTILDAYAEYPHLNQHSSYHRLDVIDRCFSKRTVEEIFSALEREVTQKPNDWLLATIQALEKASPSCLKISLRSIREGRLQGVGQCLIREYRMVCHVMKGDISKDFVEGCRAVLIDKDRNPKWQPRRLEDVTDSMVDQYFERVEDEEGWEDLKFPPRNNLPALAIAAKL", "text": "FUNCTION: Involved in valine catabolism. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
+{"protein": "MSFLIPNRGVGGTKIPLSIIVLVLCGFMFFILLYTERISLLSSSSSSSSSFFKLKSCPRKDVSSKPKEKIRKERSEILEVLDDRFEFDPEECNVAAGKWVYNSSIEPLYTDRSCPYIDRQFSCMKNGQPETDYLRWEWQPDDCTIPRFSPKLAMNKLRGKRLLFVGDSLQRSQWESFVCLVESIIPEGEKSMKRSQKYFVFKAKEYNATIEFYWAPYIVESNTDIPVISDPKKRIVKVDSVKDRAKFWEGADILVFNTYVWWMSGLRMKALWGSFGNGESGAEALDTQVAYRLGLKTWANWVDSTVDPNKTRVFFTTMSPTHTRSADWGKPNGTKCFNETKPIKDKKFWGTGSNKQMMKVVSSVIKHMTTHVTVINITQLSEYRIDAHTSVYTETGGKILTAEQRADPMHHADCIHWCLPGLPDTWNRILLAHL", "text": "FUNCTION: Involved in secondary cell wall cellulose deposition. Required for normal stem development (PubMed:20388664). 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: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily."}
+{"protein": "AVCVSLLGAANIPPQSLNLYQFKNMIECAGTRTWLAYVKYGCYCGPGGTGTPLDELDRCCQTHDHCYDNAKKFGNCIPYLKTYVYTCNKPDITCTGAKGSCGRNVCDCDRAAAICFAAAPYNLANFGIDKEKHCQ", "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. Very weakly suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
+{"protein": "MIKNHWMKKLKYLSLFFLLFAIYWFPDVILAYPEVYLKSLVGYERQVVATWIFLGNMSISLFLGILICYKLGYYKNTISIFKIKNLLFLLITTIILFVIYFFSYTYYNSHFITPGIAKTQAAFSIQIVFPFVQFITIAICAPIFEEASFRTTIYSFFKNDKIAYIVSCVGFAWMHTGPNPILIVYLPMSIVLTSIYHRRRVLGESILVHGVFNALLPIVIPLLQVITGLYYL", "text": "FUNCTION: The function of this protein is currently unknown, but it has been shown that it is not necessary for phage resistance. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0177 family."}
+{"protein": "MKIRHWSALSLFVLPALAQAEALTGEVHRQPLNIQAIVMFLLFVGGTLYITYWASKRTRSRQDYYTAGGRITGFQNGLAIAGDYMSAASFLGISALVYASGYDGLIYSIGFLIGWPIILFLIAERLRNLGRYTFADVASYRLQQRPIRTLSACGSLVVVALYLIAQMVGAGKLIQLLFGLNYHVAVVLVGILMVLYVLFGGMLATTWVQIIKAVMLLSGATFMAIMVMKSVNFNFNTLFSEAVKVHPKGLSIMSPGGLVSDPISALSLGLALMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFIGYFYILTFIIGFGAILLVGPNQTFKDAAGALLGGNNMAAVHLANAVGGSFFLGFISAVAFATILAVVAGLTLAGASAVSHDLYASVIKKGKANERDELRVSKITVIILGIVAIGLGILFEKQNIAFMVGLAFSIAASCNFPIIIISMYWDKLTTRGAMIGGWLGLSTAVILMILGPTIWVTILGHEKPIYPYEYPALFSMIAAFVGTWFFSITDNSETGKQERLLFKSQFVRSQTGLGASKGGAH", "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": "MKYTKQNFMMSVLGIIIYVTDLIVDIWVSVRFFHEGQYVFSALALSFMLFGTLVAQCFSYSWFKADLKKAGQESQHCFLLLHCLQGGVFTRYWFALKRGYHAAFKYDSNTSNFVEEQIDLHKEVIDRVTDLSMLRLFETYLEGCPQLILQLYILLEHGQANFSQYAAIMVSCCAISWSTVDYQVALRKSLPDKKLLNGLCPKITYLFYKLFTLLSWMLSVVLLLFLNVKIALFLLLFLWLLGIIWAFKNNTQFCTCISMEFLYRIVVGFILIFTFFNIKGQNTKCPMSCYYIVRVLGTLGILTVFWVCPLNIFNPDYFIPISITIVLTLLLGILFLIVYYGSFHPNRSAETKCDEIDGKPVLRECRMRYFLME", "text": "FUNCTION: [XK-related protein 9, processed form]: Phospholipid scramblase that promotes phosphatidylserine exposure on apoptotic cell surface. Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the XK family."}
+{"protein": "MSQVDINHARALVYQLLSSLFAREVDEQRLKELTSEAAQQFWEQLSLEANFTQSVDKIRSTLNGIKDDEALLELAADYCGLFLVGTKHSASPYASLYLSGEDEPLLFGEQHQQMSEFLHQSKLQVQSHFPEPADHLAVMLAYMAHLCCHSEDSVQLSFLQTCVDSWLAKFINQLTQCDKNGFYSAVATLTLAWVKQDIAQLEPA", "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": "MLPENLPTDPAAMTPAAVAAALRVDTKVGLSSNEVEERRQAFGINELPSEPPTPFWKLVLAQFEDTLVRILLLAATVSFAMAVVENNAADFVEPFIILLILILNATVGVWQENRAEGAIEALKSFVPKTAVVLRDGDIKTVNAEELVPGDVVEVAVGNRVPADMRVVELHSTTLRADQSILNGESVEAMKQIEAVKGRQERFPACMVYSGTAIVYGKALCVVVRTGASTEIGTIERDVREQEEVKTPLQVKLDEFGVLLSKVIGYICLVVFAVNLVRWYATHKPTKNETFFTRYIQPSVHCLKVAVALAVAAIPEGLPAVVTTCLALGTRRMAQHNALVRDLPSVETLGRCTVICSDKTGTLTTNMMSVLHAFTLKGDGSIKEYELKDSRFNIVSNSVTCEGRQVSSPLEQDGALTKLANIAVLCNDASLHHNAATVQVEKIGEATEAALLVMSEKFANIKGDSAVNAFRTLCEGKWKKNATLEFTRKRKSMSVHVTSTVTGSPASSTNNLFVKGAPEEVLRRSTHVMQDNGAVVQLSATHRKRIIEQLDKISGGANALRCIGFAFKPTKAVQHVRLNDPATFEDVESDLTFVGACGMLDPPREEVRDAIVKCRTAGIRVVVITGDRKETAEAICCKLGLLSSTADTTGLSYTGQELDAMTPAQKREAVLTAVLFSRTDPSHKMQLVQLLKDERLICAMTGDGVNDAPALKKADIGIAMGSGTEVAKSASKMVLADDNFATVVKAVQEGRAIYNNTKQFIRYLISSNIGEVVCILVTGLFGLPEALSPVQLLWVNLVTDGLPATALGFNAPDRDIMEQRPRRMEEPIVNGWLFMRYMVIGVYVGLATVGGFLWWFLRHGFSWHDLTTYTACSDMTNGTCLLLANPQTARAIALSILVVVEMLNALNALSENASLIVSRPSSNVWLLFAIFSSLSLHLIIMYVPFFAKLFNIVPLGVDPHVVQQAQPWSILTPTNFDDWKAVIVFSVPVIFLDELLKFITRRMEKAQEKKKD", "text": "FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. SUBCELLULAR LOCATION: Flagellar pocket. Cell membrane; Multi-pass membrane protein. Note=May be located in the flagellar pocket of the membrane. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family."}
+{"protein": "MAMISARRYFLLGLLVLTTSAYVTVGDEGDPCQVRSDIPGICLSSSACENIRGYLKSGTLSTSQVPSCGFGAREEIICCPTVACCATDRGREVQFHATSSERSSLPEPKREPTPEPEPLPPTTTEGKRERESRLDENQNFFDFNKLLSTTVKPQKTHESLKLPTQESMKTPTHESMKMPTHESMKLPTHEPMKLPIQSVGAWGIAPSKTQPIASTQRSFMEPEWGREPRIVNRPLTTPRSRPQRPNNSNFNTNPSPNNNNLIHLVNDRLREQGMQIEPAREVPMVLQTTPTPTPAPTPTQLIDPFEPYRFRGQDRDKDTQPQEPWNDVSNNLDADPAPSIFNPAETRPTTPNPNPSRVNLPEKERPSVAACEKIRSGGKPLTVHILDGERVDRGVYPHMAAIAYNSFGSAAFRCGGSLIASRFVLTAAHCVNSDDSTPSFVRLGALNIENPEPGYQDINVIDVQIHPDYSGSSKYYDIAILQLAEDAKESDVIRPACLYTDRSDPPANYKYFVAGWGVMNVTNRAVSKILLRAALDLVPADECNASFAEQPSANRTLRRGVIASQLCAADKNQRKDACQGDSGGPLILEIDDVDGTYSIVGVISSGFGCATKTPGLYTRVSSFLDYIEGIVWPSNRF", "text": "FUNCTION: Serine protease which, by converting prophenoloxidase 1 (PPO1) into its active form, plays an essential role in the melanization immune response to physical or septic wounding. May function in diverse PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A and Spn28D in the hemolymph, and Spn28D and Spn77BA in the trachea. Also required in the systematic wound response by mediating the redox-dependent activation of the JNK cytoprotective cascade in neuronal tissues after integument wounding. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily."}
+{"protein": "MAKKKTSSSMARSQLAALLISLCFLSLASNAVGWSRRGEREEEDERRRHGGEGGRPYHLGEESFRHWTRTRHGRFSVLERFPDEQVVGAAVGGYRVAVLEAAPRAFLQPSHYDADEVFYVKEGEGVIVLLREGRRESFCVREGDAMVIPAGAIVYSANTHSSKWFRVVMLLNPVSTPGHFEEYFPVGGDRPESFFSAFSDDVLQAAFNTRREELEKVFERQREGGEITTAPEEQIRELSKSCSRGGGGGSGSEWEIKPSSLTGKSPYFSNNHGKLFELTGDECRHLKKLDLQIGLANITRGSMIAPNYNTRATKLAVVLQGSGYFEMACPHVSGGGSSERREREREHGRRREEEQGEEEHGERGEKARRYHKVRAQVREESVIVIPASHPATIVASEGESLAVVCFFVGANHDEKVFLAGRNSPLRQLDDPAKKLVFGGSAAREADRVLAAQPEQILLRGPHGRGSVSDM", "text": "FUNCTION: Seed storage protein (Probable). Globulin-like protein that acts as zinc metalloprotease. Cleaves specifically between Leu-15 and Tyr-16 of insulin B chain, and Gln-1 and Leu-2 of neurotensin (NT) peptide in vitro. May play a role as an initiating endopeptidase in germinating seeds (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the 7S seed storage protein family."}
+{"protein": "MREPLLQLIVLSLIIIVVNTQFESGRLCFCKGFEAVEPCDCSKPQTIDKLNNHRIYEKVQKLLKKDFFRFYKVNMDKTCPFWADDRQCGTNQCGIAFCDDEVPAGLRRRNAVNMEAAAVKEEEDDDAEKCADAGNNIDPMDRTLHDDEKRQLDAMDHHDDGLEDKFCEIEDDESDGMHYVDLSKNPERYTGYAGKSPQRVWKSIYEENCFKPDPKFDKNFLTNPSNFGMCLEKRVFYRLISGLHSAITISIAAYNYKPPPPSLGQFGSQMGTWFRNTEMFAGRFGTKWSWEGPQRLRNVYFIYLLELRALLKAAPYLQNELFYTGNDVEDAETRKAVEDLLEEIRAYPNHFDESEMFTGVESHARALREEFRSHFVNISRIMDCVECDKCRLWGKVQTHGMGTALKILFSDLPHSHYKQDSSKFQLTRNEVVALLQSFGRYSSSILEVDNFREDMYPGESVMNTAADGPPRKSNKIDL", "text": "FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the EROs family."}
+{"protein": "MMLQHPGQVSASEVSATAIVPCLSPPGSLVFEDFANLTPFVKEELRFAIQNKHLCHRMSSALESVTVNNRPLEMSVTKSEAAPEEDERKRRRRERNKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDERNLFIQQIKEGTLQS", "text": "FUNCTION: This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters (PubMed:11916968). Represses transcription from promoters with ATF sites (PubMed:11916968). It may repress transcription by stabilizing the binding of inhibitory cofactors at the promoter (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. ATF subfamily."}
+{"protein": "MFRQSIRPLVSNRLTFIRYNSSPAYTAAVSLLKGDLKKAMIAKDEMKKTAIRNMLSAIKNKEIALKGKSADEYSLYDMYSKLISQRKDSINEFLANKRDDLVAKEQGEMDIIKKYMDQLPVSSELDIDQNVKKLLDALKTKAGEKKVQIKEIMGEIDWKSLPTEWKTSPTAIKNSIVKQFKEIFK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM41 family."}
+{"protein": "MIDVIIRHQASPLIESALVYQSITIIFGNAHLQSSFRKRNVILAAMMRTRIPGLVPRICQTPLPWKRPTQMTRVRYARWSTSHAVTWLETGHIDLKENEGLLFINNIFPSRLQWLLRGPLGGMRSYEAAVKRIDRPHLAASDTFQIIQRVVPKNLNVQVKEVVPRFREGGAFVKYTRPGDVNDADIEASIKENLKEHPIRPWFNPFQEVQVCRVIGRPWIEDLYRLPSPRLKVSFHPVSPEASAADLNTETLYTLFRPYGKIRDIETQPSDGKVTPRYAYVEFSRPKYAGMAKNCMHGFTIPEQEGGGKSGTRLKIKYERKIKLSMIKDWLLNHPRIVIPVLAALLAAITVTIFDPMRTFFIELKIKSTLQTEENGVMQWIRKQVNKANIIYFGRKGADPRGLTAIWEDRQEDITRLQSWLMENVETFIIIHGPRGSGKRELVLDRALVDYKYKIVIDCKQIQDARGDSAKIARAASQVGYRPVFSWMNSISSFIDLAAQGMIGTKAGFSETLDAQLSNIWQNTATALKKVTLEHRKKNDNDSHLTDEEYLEAHPELRPVVVIDNYLHNASESSVVYDKITEWAAGLTAGNIAHVIFLTTDVSYAKPLSKALPNSVFRTITLGDCSLEVGRKFVMSHLAYESKDGKTQPRRAEELEDLDACIEALGGRVTDLEFMAHRIEAGETPRGAVNRIIEQSASEILKMFLLTPETIEQSWTHEQAWYLIKRLAESKDGSLSYNEIVLSELFKENGEITLRALEHAELISIAAVNGCPQRIRPGKPVLRAVFKKVTENKALSSRMDLAIIAKKINKENKSIEKYEEELSLLGSLPRQPRELTDRIQWLLNKVYSSQNKIAKYEKESAYLQKILRSEH", "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": "AADCNGACSPFEMPPCRSTDCRCIPIALFGGFCINPTGLSSVAKMIDEHPNLCQSDDECLKKGSGNFCARYPNHYMDYGWCFDSDSEAL", "text": "FUNCTION: A1b binds to basic 7S globulin (BG) and stimulates its phosphorylation activity."}
+{"protein": "MTASAQPRGRRPGVGVGVVVTSCKHPRCVLLGKRKGSVGAGSFQLPGGHLEFGETWEECAQRETWEEAALHLKNVHFASVVNSFIEKENYHYVTILMKGEVDVTHDSEPKNVEPEKNESWEWVPWEELPPLDQLFWGLRCLKEQGYDPFKEDLNHLVGYKGNHL", "text": "FUNCTION: May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP (PubMed:26238318). Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives (PubMed:22556419, PubMed:26238318). Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides to prevent their incorporation into DNA, is unclear (PubMed:26238318, PubMed:22556419). Through the hydrolysis of thioguanosine triphosphates may participate in the catabolism of thiopurine drugs (PubMed:26238318, PubMed:25108385). May also have a role in DNA synthesis and cell cycle progression by stabilizing PCNA (PubMed:19419956). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). SIMILARITY: Belongs to the Nudix hydrolase family."}
+{"protein": "MKYGKVSFLALLCSLYVRGSLADPESEQEPLVFNPTEVKAPLVEQFQGAWSERWIPSHAKRFVNGIEEMSYVGEWTVEESSGPGALKGEAGLVMKDEAAHHAISYEFDEPINEPEKDLVVQYEVNPEEGLNCGGAYLKLLAEPTHGEMSNSIDYRIMFGPDKCGVNDRVHFIFKHKNPLTGEYSEKHLDSRPASLLKPGITNLYTLIVKPDQTFEVRINGDVVRQGSLFYDFIPPVLPPVEIYDPEDIKPADWVDEPEIPDPNAVKPDDWDEDAPRMIPDPDAVKPEDWLEDEPLYIPDPEAQKPEDWDDEEDGDWIPSEIINPKCIEGAGCGEWKPPMIRNPNYRGPWSPPMIPNPEFIGEWYPRKIPNPDYFDDDHPSHFGPLYGVGFELWTMQPNIRFSNIYVGHSIEDAERLGNETFLPKLKAERELLSKQESMEKQSMHVDEESNQILEKFLDVYDIIKAKLPPNVAEKVDYYVETIIETPEIGIAIVAVLGSLTAVILTCYFYFFASSSPASLSTGTTEAEKEQQEKFKQETETEKIDVSYAPETESPTAKNED", "text": "FUNCTION: Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the calreticulin family."}
+{"protein": "MRGLTLLSLAFLGVCSALTVPHSLVHPRDLEIRHGGIEGRITNGNLASEGQVPYIVGVSLNSNGNWWWCGGSIIGHTWVLTAAHCTAGADEASLYYGAVNYNEPAFRHTVSSENFIRYPHYVGLDHDLALIKTPHVDFYSLVNKIELPSLDDRYNSYENNWVQAAGWGAIYDGSNVVEDLRVVDLKVISVAECQAYYGTDTASENTICVETPDGKATCQGDSGGPLVTKEGDKLIGITSFVSAYGCQVGGPAGFTRVTKYLEWIKEETGIYY", "text": "FUNCTION: Its major function may be to aid in digestion. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MQKDSGPLVPLHYYGFGYAALVATGGIIGYAKAGSVPSLAAGLFFGGLAGLGAYQLSQDPRNVWVFLATSGTLAGIMGMRFYNSGKFMPAGLIAGASLLMVAPGVAKIQEITTMP", "text": "FUNCTION: Required for normal heme biosynthesis. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM14 family."}
+{"protein": "MEQILSMNGGSGEQSYANNSIGQSTCLSRSMPVLKQAVLDSCCTNLPETVTMADLGCSSGPNTFYAVSEITSIIYKRCCQLGRSAPEFRVFLNDLPGNDFNTVFQSLPAYQGKLREENGPGFGPLYVAGVPGSFYGRLFPLKTLHFVHSSSSLHWLSQVPPELTDKANPLINKWKIFISKTSPPAVISSYLTQFRKDFSLFLKLRSEEVAPEGRMVLTFRGRTTADPTSDESCLLWDYLGQAFQDLVAEGLVEEERLDTYNTPYYEPHPEEIQAEIEKEGSFTLDRLEVIALPWDSVNGGIKDDRATTAKRMAKAIRAVNESMFRSHFGEDILDPLFHRFIEIMAADTKEVEHVSLVISLIRKA", "text": "SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family."}
+{"protein": "MEAEPSQPPNGSWPLGQNGSDVETSMATSLTFSSYYQHSSPVAAMFIAAYVLIFLLCMVGNTLVCFIVLKNRHMRTVTNMFILNLAVSDLLVGIFCMPTTLVDNLITGWPFDNATCKMSGLVQGMSVSASVFTLVAIAVERFRCIVHPFREKLTLRKALFTIAVIWALALLIMCPSAVTLTVTREEHHFMLDARNRSYPLYSCWEAWPEKGMRKVYTAVLFAHIYLVPLALIVVMYVRIARKLCQAPGPARDTEEAVAEGGRTSRRRARVVHMLVMVALFFTLSWLPLWVLLLLIDYGELSELQLHLLSVYAFPLAHWLAFFHSSANPIIYGYFNENFRRGFQAAFRAQLCWPPWAAHKQAYSERPNRLLRRRVVVDVQPSDSGLPSESGPSSGVPGPGRLPLRNGRVAHQDGPGEGPGCNHMPLTIPAWNI", "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": "MKIVNITTQVESIELKTPFKTALRQTSHVEFVRVEVECDNGFVGIGEASATKVITGEDIYIILTSIASVEELFLNLTCEEALGALHTKCAIGSSAKASLDIAFVHLLSQEAKKPLYEYFGATDKSALKSDITISLNEADVMLNDAKKAFSNGMDILKIKVGSDILHAIDIVRKIAKELPECDILVDANQAWSFENTVLFIENMLNTPIKLIEQPVEAPNLDGLKKITELSHIPILADEAVFTLKDAKKVIEEKCADMINIKLMKCGGVSKAIEILEFARNREFKCMLGSMLEGPYSINMALHLAFAYRDVIEFVDLDSPLLYKEMPKELDFVFDGCEIKPL", "text": "FUNCTION: Catalyzes the epimerization of dipeptides with L-Glu in the second position. Has epimerase activity with L-Gly-L-Glu, L-Ala-L-Glu, L-Ser-L-Glu, L-Pro-L-Glu, L-Val-L-Glu, L-Met-L-Glu, L-Thr-L-Glu and L- Phe-L-Glu (in vitro). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family."}
+{"protein": "MSSAAENGEAAPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDAKRTGMQKVLYSTAMESIQGPGKSGDGIITENPDTMGGIPAKSHRGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQALKASPSKKRCNSIAALKATSQEIVSSISQEWKDEKRDLLTEGQSFSSLDEEALGSRHRPDLVPSTPSLFEAASLATTISSSSLYVNEHYPHDRPTLYSNSKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL", "text": "FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (By similarity). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of phospholipase PLD2. Together with PIP5K1A, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane Endomembrane system. Note=Associated with membranes."}
+{"protein": "MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP", "text": "FUNCTION: May be involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin- dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D- CDK4 complex. Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding (PubMed:11595739). Plays an important role in controlling cell cycle progression and DNA damage- induced G2 arrest (PubMed:9106657). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CDI family."}
+{"protein": "MNFHPCYPVDHGVPSWILVLLLSLGLCNLQARADRVLDPDFHENYFEQYMDHFNFESFGNKTFGQRFLVSDKFWKMGEGPIFFYTGNEGDIWSFANNSGFMVELAAQQEALLVFAEHRYYGKSLPFGVQSTQRGYTQLLTVEQALADFAVLLQALRQDLGVHDAPTIAFGGSYGGMLSAYMRMKYPHLVAGALAASAPVVAVAGLGDSYQFFRDVTADFYGQSPKCAQAVRDAFQQIKDLFLQGAYDTISQNFGTCQSLSSPKDLTQLFGFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCQRLLNEGQRIMGLRALAGLVYNSSGTEPCYDIYRLYQSCADPTGCGTGSDARAWDYQACTEINLTFDSNNVTDMFPEIPFSEELRQQYCLDTWGVWPRQDWLQTSFWGGDLKAASNIIFSNGDLDPWAGGGIQSNLSTSVIAVTIQGGAHHLDLRASNSEDPPSVVEVRKLESTLIREWVAAARLKQPAMPRWPGPKKQHPSR", "text": "FUNCTION: Plays an important role in the degradation of some oligopeptides. SUBCELLULAR LOCATION: Lysosome Cytoplasmic vesicle Secreted. SIMILARITY: Belongs to the peptidase S28 family."}
+{"protein": "MGQGLSQPAQAVEEPSPPAVEAAPSSSPSPAPAPSSLEALAAEAMSFDEDGNESIDVKVQKALDCPCVAELKNGPCGSQFVDAFSCFLKSTEEEKGSDCVKPFIALQDCIKINPEAFSKEILEEEENDEEAEKSNLKVRAPAWSRESKPKL", "text": "FUNCTION: Required for the import and folding of small cysteine- containing proteins in the mitochondrial intermembrane space. SUBCELLULAR LOCATION: Mitochondrion intermembrane space Peroxisome matrix."}
+{"protein": "MKAVHFGAGNIGRGFIGLQLVKSGYDVCFIDVNAEVVEALKTRGAYTVGYAAEEAAVEEVSRVTALNSQTEAERVVEAIATADVVTTAVGPTLLARIAPLLAEGLKQRTTTQNVFVIACENMIEGSSHLQQEVMHYLESTPGNVFFPNAAVDRIVPLQHHEDPLYVEVEPFFEWVIETKALPDDYPVFEGVTYVADITPFIERKLFTVNTGHAIASYLGALFGKETIAESLQDVRVRRGVQSALYETGWLLLEKYGFDPKDHSAYIQKNIKRFENPRIHDEIVRVARSPIRKLGPRDRLVKPARELMDRGIEANGLALGIAAALTYSDPNYSEYSELNTFIEQNGIQETVATYLGLEADERLSQLIVSQYEQMHPMSDSIA", "text": "SIMILARITY: Belongs to the mannitol dehydrogenase family."}
+{"protein": "MATFAVSGLNSISSISSFNNNFRSKNSNILLSRRRILLFSFRRRRRSFSVSSVASDQKQKTKDSSSDEGFTLDVFQPDSTSVLSSIKYHAEFTPSFSPEKFELPKAYYATAESVRDTLIINWNATYEFYEKMNVKQAYYLSMEFLQGRALLNAIGNLGLTGPYADALTKLGYSLEDVARQEPDAALGNGGLGRLASCFLDSMATLNYPAWGYGLRYQYGLFKQLITKDGQEEVAENWLEMGNPWEIVRNDISYPVKFYGKVIEGADGRKEWAGGEDITAVAYDVPIPGYKTKTTINLRLWTTKLAAEAFDLYAFNNGDHAKAYEAQKKAEKICYVLYPGDESLEGKTLRLKQQYTLCSASLQDIIARFEKRSGNAVNWDQFPEKVAVQMNDTHPTLCIPELLRILMDVKGLSWKQAWEITQRTVAYTNHTVLPEALEKWSFTLLGELLPRHVEIIAMIDEELLHTILAEYGTEDLDLLQEKLNQMRILDNVEIPSSVLELLIKAEESAADVEKAADEEQEEEGKDDSKDEETEAVKAETTNEEEETEVKKVEVEDSQAKIKRIFGPHPNKPQVVHMANLCVVSGHAVNGVAEIHSEIVKDEVFNEFYKLWPEKFQNKTNGVTPRRWLSFCNPELSEIITKWTGSDDWLVNTEKLAELRKFADNEELQSEWRKAKGNNKMKIVSLIKEKTGYVVSPDAMFDVQIKRIHEYKRQLLNIFGIVYRYKKMKEMSPEERKEKFVPRVCIFGGKAFATYVQAKRIVKFITDVGETVNHDPEIGDLLKVVFVPDYNVSVAEVLIPGSELSQHISTAGMEASGTSNMKFSMNGCLLIGTLDGANVEIREEVGEDNFFLFGAQAHEIAGLRKERAEGKFVPDPRFEEVKAFIRTGVFGTYNYEELMGSLEGNEGYGRADYFLVGKDFPDYIECQDKVDEAYRDQKKWTKMSILNTAGSFKFSSDRTIHQYARDIWRIEPVELP", "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. SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. SIMILARITY: Belongs to the glycogen phosphorylase family."}
+{"protein": "MNASSWSLRNLPWFRATLAQWRYALRNTIAMCLALTVAYYLNLDEPYWAMTSAAVVSFPTVGGVISKSLGRIAGSLLGAIAALLLAGHTLNEPWFFLLSMSAWLGFCTWACAHFTNNVAYAFQLAGYTAAIIAFPMVNITEASQLWDIAQARVCEVIVGILCGGMMMMILPSSSDATALLTALKNMHARLLEHASLLWQPETTDAIRAAHEGVIGQILTMNLLRIQAFWSHYRFRQQNARLNALLHQQLRMTSVISSLRRMLLNWPSPPGATREILEQLLTALASSQTDVYTVARIIAPLRPTNVADYRHVAFWQRLRYFCRLYLQSSQELHRLQSGVDDHTRLPRTSGLARHTDNAEAMWSGLRTFCTLMMIGAWSIASQWDAGANALTLAAISCVLYSAVAAPFKSLSLLMRTLVLLSLFSFVVKFGLMVQISDLWQFLLFLFPLLATMQLLKLQMPKFAALWGQLIVFMGSFIAVTNPPVYDFADFLNDNLAKIVGVALAWLAFAILRPGSDARKSRRHIRALRRDFVDQLSRHPTLSESEFESLTYHHVSQLSNSQDALARRWLLRWGVVLLNCSHVVWQLRDWESRSDPLSRVRDNCISLLRGVMSERGVQQKSLAATLEELQRICDSLARHHQPAARELAAIVWRLYCSLSQLEQAPPQGTLAS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic acid exporter ArAE (TC 2.A.85) family."}
+{"protein": "MQKLKQQVFEANMDLPHYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGNVVEGEYRPSSDTATHLELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGDAEPLHTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARSINPQLNHIDSFLMNKHFMRKHGPNAYYGQK", "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": "MAVPRWAVRDLTQISSARELSLRLEQARNDFRATVGSICYFNASARTPGQFDDEYIMTDQSLTYVYADGVTAQSCAMNRLLPSSSSNFGAAATAIPPWLLDPPRLNRLLREGTDEGGLVNYYEGPHKNAFFLAIMRSCIFVRPGADEINGVSYDFFARSGNYTEQAEEEEEEEEEEEEEEVLDREFQLGNLVSYPIIAWGSCPNSA", "text": "FUNCTION: Involved in tumor formation and increases auxin and cytokinin effects in host plants."}
+{"protein": "MNNLPLLNDLRVFMLVARRAGFAAVAEELGVSPAFVSKRIALLEQTLNVVLLHRTTRRVTITEEGERIYEWAQRILQDVGQMMDELSDVRQVPQGMLRIISSFGFGRQVVAPALLALAKAYPQLELRFDVEDRLVDLVNEGVDLDIRIGDDIAPNLIARKLATNYRILCASPEFIAQHGAPKHLTDLSALPCLVIKERDHPFGVWQLRNKEGPHAIKVTGPLSSNHGEIVHQWCLDGQGIALRSWWDVSENIASGHLVQVLPEYYQPANVWAVYVSRLATSAKVRITVEFLRQYFAEHYPNFSLEHA", "text": "FUNCTION: Transcriptional regulator required for the aerobic growth on D-malate as the sole carbon source. Induces the expression of dmlA in response to D-malate or L- or meso-tartrate. Negatively regulates its own expression. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MAGGGGYGGASGKVDYVFKVVLIGDSAVGKSQLLARFARDEFSMDSKATIGVEFQTRTLSIEQKSIKAQIWDTAGQERYRAVTSAYYRGAVGAMLVYDMTKRETFEHIPRWLEELRAHADKNIVIILIGNKSDLEDQRAVPTEDAKEFAEKEGLFFLETSALNATNVENSFNTLMTQIYNTVNKKNLASEGDSNNPGSLAGKKILIPGSGQEIPAKTSTCCTSS", "text": "FUNCTION: Regulator of membrane trafficking. May be required for secretion of cell wall components in cells. SUBCELLULAR LOCATION: Early endosome membrane Golgi apparatus, trans-Golgi network membrane; Lipid-anchor. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MILVLAESAIELVPREIWSHPAVASDARRRGKRPGEILLDRARHHPAMAGLEDGARRGRPDIVHQVLLVFQYSLLNRRGLGRVYIHTRGDYIIQVKPQTRIPKNYNNFVSLMEQLYALGRAPPHGDSLMELHRGSLAGLLEQLGGRWVVLHERGARRRFAELGAALLNSVVVVGGFPHGDFSNRWVLEKAEAVYSVGDEPLDAAQAVCRAVAAAEASAGLI", "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": "GACRWFLGGCKSTSDCCEHLSCKMGLDYCAWDGTF", "text": "FUNCTION: Selectively activates the mammalian capsaicin receptor TRPV1, a non-selective cation channel expressed by sensory neurons of the pain pathway. Is more potent than VaTx1, but less potent than VaTx3. Interacts with distinct regions of the channel than capsaicin, since it only acts on the extracellular face of the channel, and capsaicin binds to the cytosolic side. Also activates avian TRPV1, which is insensitive to capsaicin. Produce weak inhibition on potassium channels Kv2.1/KCNB1. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 62 (Vatx) subfamily."}
+{"protein": "MSKSTATAQNLSFVLEGIHQVKFEDRPIPELKDPHDVLVNVKFTGICGSDVHYWEHGSIGQFVVKGPMVLGHESSGVISKVGSAVTGLKVGDRVAMEPGIPCRRCEPCKAGKYNLCEKMAFAATPPYDGTLAKFYVLPEDFCYKLPDNISLQEGALMEPLGVAVHIVKQASVTPGQSVIVFGAGPVGLLCCAVAKAFGAAKIIAVDIQKARLDFAKKYAATSTFEPAKVSAVDNADRLRKENNLGVGADVVIDASGAEPSVHTGIHVLRPGGTYVQGGMGRSEIMFPIMAACTKELAIKGSFRYGSGDYNLAVGLVASGKVNVKDLITGVVEFHDAEQAFKEVKAGKGIKTLIAGIQD", "text": "FUNCTION: Xylitol dehydrogenase which catalyzes the conversion of xylitol to D-xylulose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway (By similarity). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MMISQFFVLSQRGDNIVFRDYRAEVPKGSTETFFRKVKFWKEDGNAEAPPIFNVDGVNYFHVKVVGLYFVATTRVNVSPSLVLELLQRIARVIKDYLGVLNEDSFRKNFVLVYELLDEVIDFGYVQTTSTEVLKSYIFNEPIVVSPARLQPIDPAAIFTQGAKRMPGTAVTKSVVANDPGGRRREEIFVDIIEKISVTFSSSGYILTSEIDGTIQMKSYLSGNPEIRLALNEDLNIGRGGRSVYDYRSSSGSGVILDDCNFHESVRLDSFDSDRTLSLVPPDGEFPVMNYRMTQEFKPPFHVNTLIEEAGRLKAEVIIKIRAEFPSDIIANTITVQMPLPNYTSRASFELEPGAAGQRTDFKESNKMLEWNLKKIVGGGEHTLRAKLTFSQEFHGNITKEAGPVSMTFTIPMYNVSKLQVKYLQIAKKSSSYNPYRWVRYVTQANSYVARI", "text": "FUNCTION: Subunit of novel type of clathrin- or non-clathrin-associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network Membrane, coated pit Note=Associated with the trans-Golgi network. SIMILARITY: Belongs to the adaptor complexes medium subunit family."}
+{"protein": "MTAICTDKTELNASWNTVSSAWLTRYPNPYSLHVVSADVLERYVDDEGRLYTERLLVKQGRLPRWASDLLNVNKSYILERSVIDPSKQELKSETFNLDHVKILRVIEYSRFIQSSENCSKTIVDTIAKFVSPLRFGLGRRVQKYSLKRFQEQLSSSRRGLLYVIQQKFQPS", "text": "FUNCTION: Required for maintenance of normal mitochondrial morphology as well as PCP1-dependent processing of MGM1. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Mitochondrion intermembrane space."}
+{"protein": "MDSELEDLCSYVNEKIGNIKKILSIRNLGQDPALKTTLSKIGDEIIAVNELLNKFELEIQYQEQTNSSLKELCESLREECEDVEHLKEHVPPHLPQVTATQSLVHKPEPDPKESDKAEEPGLPKKPPREQRVIKEMQFITMDEFSDVPAYMKSRLTYCQINDIIKEINKAVVSKYKIMHQPKASMSSVKRNLYQRFINEETKDTKGHHFIVEADIKEFTALKVDKRFYVIMHILRHCHRLSEVRGGGLTRYVIT", "text": "FUNCTION: Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. 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. 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. In the complex, it mediates the interaction with 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. Localizes to both the mitotic spindle and kinetochore- associated proteins. Associates with kinetochores following microtubule attachment from prometaphase, through mid-anaphase and then vanishes in telophase. SIMILARITY: Belongs to the SKA1 family."}
+{"protein": "MERAIQGNDTREQANGERWDGGSGGITSPFKLPDESPSWTEWRLYNDETNSNQDNPLGFKESWGFGKVVFKRYLRYDRTEASLHRVLGSWTGDSVNYAASRFLGANQVGCTYSIRFRGVSVTISGGSRTLQHLCEMAIRSKQELLQLTPVEVESNVSRGCPEGIETFKKESE", "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. Binds to short interfering RNAs (siRNAs) with high affinity. Acts as a molecular caliper to specifically select siRNAs based on the length of the duplex region of the RNA. SIMILARITY: Belongs to the tombusvirus protein p19 family."}
+{"protein": "MSDAYCTDCKKETELVVDHSAGDTLCSECGLVLESHSIDETSEWRTFANESSNSDPNRVGGPTNPLLADSALTTVIAKPNGSSGDFLSSSLGRWQNRNSNSDRGLIQAFKTIATMSERLGLVATIKDRANELYKRLEDQKSSRGRNQDALYAACLYIACRQEDKPRTIKEICVIANGATKKEIGRAKDYIVKTLGLEPGQSVDLGTIHAGDFMRRFCSNLAMSNHAVKAAQEAVQKSEEFDIRRSPISIAAVVIYIITQLSDDKKTLKDISHATGVAEGTIRNSYKDLYPHLSKIAPSWYAKEEDLKNLSSP", "text": "FUNCTION: General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II (By similarity). Interacts with TBP2 and is required for activated transcription and possibly basal transcription (PubMed:10634912). Plays important roles in pollen tube growth, guidance, and reception as well as endosperm development. Is partially functionally different from TFIIB2 and PBRP2 (PubMed:23547107). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIB family."}
+{"protein": "MRTVPLFAACLLLTLMAQAEPLPRAADHSDTKMKGDREDHVAVISFWEEESTSLQDAGAGAGRRCICTTRTCRFPYRRLGTCLFQNRVYTFCC", "text": "FUNCTION: Has antibiotic, anti-fungi and antiviral activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MSSGYKPDILWSPHHADRYVICDTELSLYRIGPSGSSETKAGALQLSEETAATLLAINSDTPFMKCVAWYPKHEPECLLAVGHTNGRVVLTSLGQSHNSKSKDLAGKEFVPKHARQCNTLAWNPVDSNWLAAGLDKHRADFSVLIWDISSKFSPEAVPAEKVRLSGDADSGLLVTKPLYELGQNDACLSLCWLPRDHQKLLLAGMHRNLAIFDLRNTSQKTFVNTKAIQGVTVDPHFQDRVASYFEGQVAIWDLRKFEKPVFTLNEQPKPLTKVAWCPTRMGLLATLTRDSNIIRLYDMQHTPMPFGDEVEPTIMERGVQPCSESIISSFAWHPSAQNRMVVVSPSRVMNDFTLFERISLAWSSTTSLMWACGRHLYECAEDSGQAAEAEKDIATKMRERAQSRYGHDTVQVWRNHVLAGGDDPQLRSLWYTLHFMKQYTENVEQKQQSNKQSLIYSGIKNIVKSSSGTTETRRCWSGSDRQTDVPRFHSEERSLALQLCGWISQGPDTDVEPFLKSLEQEGEWERAAAVALFNLDIRRAIQILNKGASSEKGDLNLNVVAMALSGYTDEKNSLWREMCSSLRLQLKKPYLCIMFAFLTSEPGAYDGVLYESRVAVRDRVAFACMFLNDAQLPRYIDKLTNEMKEAGNLEGILLTGLTKDGVDLMESYVDRTGDVQTASFCMLKGSPGEVLKDPRVQCWIENYRNLLDAWRFWHKRAEFDIHRSKLDPSSKPLAQVFVSCNFCGKSISYSCSAMPHQGRGFSQYGVSGSPTKSKVTSCPGCRKPLPRCALCLMNMGTPVSSCPGTGKADEKADLTRDKKLAQFNNWFTWCHNCRHGGHAGHMLSWFRDHSECPVSACTCKCMQLDTTGNLVPSDSV", "text": "FUNCTION: As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. SUBCELLULAR LOCATION: Lysosome membrane. SIMILARITY: Belongs to the WD repeat mio family."}
+{"protein": "MRLLGAAAVAALGRGRAPASLGWQRKQVNWKACRWSSSGVIPNEKIRNIGISAHIDSGKTTLTERVLYYTGRIAKMHEVKGKDGVGAVMDSMELERQRGITIQSAATYTMWKDVNINIIDTPGHVDFTIEVERALRVLDGAVLVLCAVGGVQCQTMTVNRQMKRYNVPFLTFINKLDRMGSNPARALQQMRSKLNHNAAFMQIPMGLEGNFKGIVDLIEERAIYFDGDFGQIVRYGEIPAELRAAATDHRQELIECVANSDEQLGEMFLEEKIPSISDLKLAIRRATLKRSFTPVFLGSALKNKGVQPLLDAVLEYLPNPSEVQNYAILNKEDDSKEKTKILMNSSRDNSHPFVGLAFKLEVGRFGQLTYVRSYQGELKKGDTIYNTRTRKKVRLQRLARMHADMMEDVEEVYAGDICALFGIDCASGDTFTDKANSGLSMESIHVPDPVISIAMKPSNKNDLEKFSKGIGRFTREDPTFKVYFDTENKETVISGMGELHLEIYAQRLEREYGCPCITGKPKVAFRETITAPVPFDFTHKKQSGGAGQYGKVIGVLEPLDPEDYTKLEFSDETFGSNIPKQFVPAVEKGFLDACEKGPLSGHKLSGLRFVLQDGAHHMVDSNEISFIRAGEGALKQALANATLCILEPIMAVEVVAPNEFQGQVIAGINRRHGVITGQDGVEDYFTLYADVPLNDMFGYSTELRSCTEGKGEYTMEYSRYQPCLPSTQEDVINKYLEATGQLPVKKGKAKN", "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. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
+{"protein": "MAEGSAVSDPQHAARLLRALSSFREEARFCDAHLVLDGEEIPVQKNILAAASPYIRTKLNYNPPKDDGSTYKIELEGISVMVMREILDYIFSGQIRLNEDTIQDVVQAADLLLLTDLKTLCCEFLEGCIAAENCIGIRDFALHYCLHHVHYLATEYLETHFRDVSSTEEFLELSPQKLKEVISLEKLNVGNERYVFEAVIRWIAHDVEMRKVHMKDVMSALWVSGLDSSYLREQMLNEPLVREIVKECSNIPLSQPQQGEAMLASFKPRGYSECIVTIGGEERVSRKPTAAMRCMCPLYDPNRQLWIELAPLSMPRINHGVLSAEGFLFVLGGQDENKQTLSSGEKYDPDANTWTALPPMHEARHNFGIVEIDGMLYILGGEDGDRELISMECYDIYSKTWTKQPDLTMVRKIGCYAAMKKKIYAMGGGSYGKLFESVECYDPRTQQWTAICPLKERRFGAVACGVAMELYVFGGVRSREDIQGSEMVTCKSEFYHDEFKRWIYLNDQNLCIPASSSFVYGAVPIGASIYVIGDLDTGTNYDYVREFKRSTGTWHHTKPLLPSDLRRTGCAALRIANCKLFRLQLQQGLFRIRVHSP", "text": "FUNCTION: Probable cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Controls degradation of TBCB (By similarity). Controls degradation of MAP1B and MAP1S, and is critical for neuronal maintenance and survival. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton."}
+{"protein": "MVQPADIDVPETPARPVLVVDFGAQYAQLIARRVREARVFSEVIPHTASIEEIRARQPVALVLSGGPASVYADGAPKLDPALLDLGVPVLGICYGFQAMAQALGGIVAHTGTREYGRTELKVLGGKLHSDLPEVQPVWMSHGDAVTAAPDGFDVVASSAGAPVAAFEAFDRRLAGVQYHPEVMHTPHGQQVLSRFLHDFAGLGAQWTPANIANALIEQVRTQIGDGHAICGLSGGVDSAVAAALVQRAIGDRLTCVFVDHGLLRAGERAQVQRDFVAATGANLVTVDAAETFLEALSGVSAPEGKRKIIGRQFIRAFEGAVRDVLDGKTAEFLVQGTLYPDVVESGGGSGTANIKSHHNVGGLPDDLKFTLVEPLRLLFKDEVRAVGRELGLPEEIVARQPFPGPGLGIRIVGEVTAKRLDTLRHADSIVREELTAAGLDNQIWQCPVVLLADVRSVGVQGDGRTYGHPIVLRPVSSEDAMTADWTRVPYEVLERISTRITNEVAEVNRVVLDITSKPPATIEWE", "text": "FUNCTION: Catalyzes the synthesis of GMP from XMP. FUNCTION: Catalyzes the synthesis of GMP from XMP. FUNCTION: Catalyzes the synthesis of GMP from XMP."}
+{"protein": "MWRCLRVASSSRRSESNGAFITSQLSRFFSAPPSAGDKSSYTIVDHTYDAVVVGAGGAGLRAAIGLSEHGFNTACITKLFPTRSHTVAAQGGINAALGNMSVDDWRWHMYDTVKGSDWLGDQDAIQYMCREAPKAVIELENYGLPFSRTEDGKIYQRAFGGQSLEFGIGGQAYRCACAADRTGHALLHTLYGQAMKHNTQFFVEYFALDLIMNSDGTCQGVIALNMEDGTLHRFHAGSTILATGGYGRAYFSATSAHTCTGDGNAMVARAGLPLQDLEFVQFHPTGIYGAGCLITEGARGEGGILRNSEGEKFMDRYAPTARDLASRDVVSRSMTMEIRQGRGAGPMKDYLYLYLNHLPPEVLKERLPGISETAAIFAGVDVTREPIPVLPTVHYNMGGIPTNYHGEVITLRGDDPDAVVPGLMAAGEAACASVHGANRLGANSLLDIVVFGRACANRVAEIQKPGEKLKPLEKDAGEKSIEWLDRIRNSNGSLPTSKIRLNMQRVMQNNAAVFRTQETLEEGCDLIDKTWDSFGDVKVTDRSMIWNSDLIETMELENLLVNACITMHSAEARKESRGAHAREDFTKRDDANWMKHTLGYWEEGNVKLEYRPVHMKTLDDEVDTFPPKPRVY", "text": "FUNCTION: Flavoprotein (FP) 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 FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily."}
+{"protein": "MAAALADMADLEELSRLSPLSPGSPGPAARGRAEPPEEEEEEDDEEAEAEAVAALLLNGGAGGGAGGGEAETMSEPSPESASQAGGDEDEDEEDDEDEGSSSGGAEEESSAESLVGSSSGGCSGDETRSLSPGAASSSSGDGDGKEGLEEPKGPRGGPGGPGSSGGGSSSSSVVSSGGDEGYGTGGGGSSATSGGRRGSLEMSSDGEPLSRMDSEDSISSTLMDIDSTISSGRSTPAMMNGQGSTTASSKHIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGVFVCLWKGCKVYNTPSTSQSWLQRHMLTHSGDKPFKCVVGGCNASFASQGGLARHVPTHFSQQNSSKVSSQPKAKEESPSKAGMNKRRKLKNKRRRSLPRPHDFFDAQTLDAIRHRAICFNLSAHIESLGKGHSVVFHSTVIAKRKEESGKIKLLLHWMPEDILPDVWVNESERHQLKTKVVHLSKLPKDTALLLDPNIYRTMPQKRLKRFDILNFPR", "text": "FUNCTION: Acts as an accessory subunit for the core Polycomb repressive complex 2 (PRC2), which mediates histone H3K27 (H3K27me3) trimethylation on chromatin leading to transcriptional repression of the affected target gene. Plays a role in nucleosome localization of the PRC2 complex. SUBCELLULAR LOCATION: Nucleus Note=Localizes to chromatin as part of the PRC2 complex. SIMILARITY: Belongs to the AEBP2/jing C2H2-type zinc-finger family."}
+{"protein": "MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFKEMEKKVDVTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMIRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCEKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLKRRMREASSRPKREYKPKPREPFDLGEPEQSNGGFPCTTAPKIAASSSFRSSDKPIRTPSRSMPPLDQPSCKALYDFEPENDGELGFHEGDVITLTNQIDENWYEGMLDGQSGFFPLSYVEVLVPLPQ", "text": "FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity). SUBCELLULAR LOCATION: Cytoplasm Early endosome membrane; Peripheral membrane protein Cell projection, podosome Note=Associated with postsynaptic endosomes in hippocampal neurons. SIMILARITY: Belongs to the endophilin family."}
+{"protein": "MNVSTPGFQRCATENEMIGRTAFLFQSNVYTNNIIAIITWTLTVVVLRKLYTKSIFPNSTLVLLVASLAVGSIHEFLYGFIQNWSLLRSLVYWDQPCKIMFNEYECYPFYTANIFIRLLMICTNCAITIDRLITLSNVGIKSTAQRGIVLFILSILVSVGVCMYMTSDGPNDNLQSNCFQRQGRNIDELTTQIMIYLYIIAICLSLNTIGWFISWRNLKKDKFNLAVQMSKQESINSSLVVTWYLVSQIIFLGLYSILIYAVIKLKDVIGPLLVTNVVLWCYTYTYACMFLPIIILTSTKIISLQRREKINGLTKENQNENQKSYFDKLDRSWSQGYGNRYAPNVPAPVVCINSS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nematode receptor-like protein sra family."}
+{"protein": "MRTVACAVLLACFMGCLAGAWAQSAGLEILPNSENQTKPIGRSMLLTCKPNVTNKNLISQLRWTDPSGREVPFKNPTLLKPHIFVDWLPPPGEKVLTLMIPELREADTGTYTCSALYSNTKQLSKSVHVRTIMPITWDDAPEEQYPTVNETFKIRCRVSANPPAIVNWMRDGHIVETGDRYVVEQDGLTILNVTEMDDGTYTCRAIVIATGEMALRPIRVEVHTPPQMSGALPPKLEAVEGTDFTAKCAASGKPVPRYTWIRVDTARDLTKDGDRVSADVLLGELRIREVRPEDAANYSCTAKNAAGTATATVEVTVVVRPRIGRFDNISVASGKDSEAVLECHATGSPLPAVTFRKLSNPNRYINGIQPTEDRITVDGVDSPDGRTRIGKLIISNVLRSDDGLYECIATNKGGEVKKNGHLMVEFKPSFADTPQKEVWGWEQHAVNLTCLAHSIPNATISWHFNGADLFRGREGQELQQTGYTLFGSGPRSTLQVIPFNRKMYGNYKCTATNKHGTAVHEIMLREARVPSAVLQVKMDVMTATTVTFKFFGPGNDGGLPTKNYAVQYKQDSQGWEDALNRTWPVDSPYILENLKPQTRYNFRFAAQNEVGFGPWSSQQTHTTPRISAPEEPRLLGLPLSATSGTENEVVVSPYPNRYELRWQVPADNGEPITHYSVKSCPVEKYDTEWRLLPYPCQEHKLEGQATTFQLESLQPDTHYKVEVRATNAIGNSVPGQIIVRTVKDPSQMPGVANVEDGSEGQMSSAAIVVLVVAALLLALLVVDLVCCLVWRGGLIAALCHRCCSAAKTDDSDAKIASLYSWRFPLPYCSNKEDPAMLAPAKMQQATVKIPVIEEKEPLRDGKEPVPIIKERVKRETAVDFDVKKSVSRTSFVGKDSAV", "text": "FUNCTION: Neuronal recognition molecule. Involved in a pathway recognition for axons during the development of nerve fascicles. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MSAVKSVSSFRLASLLRRENDPSAAMKLFRNPDPESTNPKRPFRYSLLCYDIIITKLGGSKMFDELDQVLLHLKTDTRIVPTEIIFCNVINFFGRGKLPSRALHMFDEMPQYRCQRTVKSLNSLLSALLKCGELEKMKERLSSIDEFGKPDACTYNILIHGCSQSGCFDDALKLFDEMVKKKVKPTGVTFGTLIHGLCKDSRVKEALKMKHDMLKVYGVRPTVHIYASLIKALCQIGELSFAFKLKDEAYEGKIKVDAAIYSTLISSLIKAGRSNEVSMILEEMSEKGCKPDTVTYNVLINGFCVENDSESANRVLDEMVEKGLKPDVISYNMILGVFFRIKKWEEATYLFEDMPRRGCSPDTLSYRIVFDGLCEGLQFEEAAVILDEMLFKGYKPRRDRLEGFLQKLCESGKLEILSKVISSLHRGIAGDADVWSVMIPTMCKEPVISDSIDLLLNTVKEDGPLSAMPQC", "text": "FUNCTION: Involved during embryo development. SIMILARITY: Belongs to the PPR family. P subfamily."}
+{"protein": "FQYVSTTTKVPPPDMTSFPYGTRRSPAKIWPTTKRPAITPANNPKHSKDPHKTGPEDTTVLIETKRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHETHRRPSPQRNTTNDIAHIQNEEIMSLQMKQLEHDHECESLQAHDTLRLTCPPDYTLTLRRSPDDIPLMTPNTITMIPNTLTGMQPLHTFNTFSGGQNSTNLPHGHSTTRV", "text": "FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Postsynaptic density membrane. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
+{"protein": "MSDSMLYQTLQTCLPKSRLITLWLAFTLAMLIQEPRRHAATVNAATAGGSMLGDVNISAILDSFSVSYDKRVRPNYGGPPVEVGVTMYVLSISSLSEVKMDFTLDFYFRQFWTDPRLAYRKRPGVETLSVGSEFIKNIWVPDTFFVNEKQSYFHIATTSNEFIRVHHSGSITRSIRLTITASCPMNLQYFPMDRQLCHIEIESFGYTMRDIRYKWNEGPNSVGVSSEVSLPQFKVLGHRQRAVEISLTTGNYSRLACEIQFVRSMGYYLIQIYIPSGLIVVISWVSFWLNRNATPARVALGVTTVLTMTTLMSSTNAALPKISYVKSIDVYLGTCFVMVFASLLEYATVGYMAKRIQMRKQRFMTIQKMAEQKKQQQLDGVQPPPNPNPNTMVDHGGHGHGHGHHSHGHPHVPKQTVSNRPIGFQTMQQQNIGGRGCSIVGPLFQEVRFKVHDPKAHSKGGTLENTVNGGRGGPPVGPHGPGPQGPPGGPPAGGGGGGAPPEGGDAEAAVPAHLLHPGKVKKDINKLLGITPSDIDKYSRIVFPVCFVCFNLMYWIIYLHVSDVVADDLVLLGEEK", "text": "FUNCTION: GABA, an inhibitory neurotransmitter, mediates neuronal inhibition by binding to the GABA 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."}
+{"protein": "MMMKSILITFIIASALLSSVFADIGGKRTLVVLDDLSIKKTHSTFFKNLENKGYKLQFEQSNTKVVLEKYGDFNFDNLILFSPTSESLSFSSADVTRFIDGGNNVLFAGSNVISENIRDIAAECGMEIEEDKTLIFDHFNYDKSQSDHSVLVADQFIDDSPIILQGLNKPILFKGIGHKIRNNPLNYAILTGSSTAFSAKAISGVSTKLMGKSCGLVSSLQARNNARVTFSGSLDLFSDKSFYSKIDNKESGNKEFVERLVSWTFQERGILRASELELVKISTESNSTVAPDVFTIKDEVKYSLKVEEFDGIKGKWVPYVGSLQLEVIMLDPYIRTFIKGDANGLYKIHFKLPDVYGVFTFEASIHKSGYSTLDHIYRKPILPFRHDSYERFIPAAFPYYATCFSMLIGTFIFSIIFLFNKDQLNK", "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. SIMILARITY: Belongs to the DDOST 48 kDa subunit family."}
+{"protein": "MSFSESRHNENCLIQEGALLFCEQAVVAPVSGDLVFRPLKIEVLSKLLAFIDGAGLVDTTYAESDKWVLLSPEFRAIWQDRKRCEYWFLQQIITPSPAFNKVLALLRKSESYWLVGYLLAQSTSGNTMRMLGEDYGVSYTHFRRLCSRALGGKAKSELRNWRMAQSLLNSVEGHENITQLAVNHGYSSPSHFSSEIKELIGVSPRKLSNIIQLADK", "text": "FUNCTION: Transcriptional regulator required for the expression of several genes encoding type III secretion system SPI1 effector proteins. The interaction with SicA is necessary for the activation of sigDE (sopB pipC), sicAsipBCDA, and sopE (By similarity). FUNCTION: Transcriptional regulator required for the expression of several genes encoding type III secretion system SPI1 effector proteins. The interaction with SicA is necessary for the activation of sigDE (sopB pipC), sicAsipBCDA, and sopE."}
+{"protein": "MASSAEAIVTHAERSISEDAIVAAARERADDIGAGAVTPAVGALLSVLARLTGGRAVVEVGTGAGVSGLWLLSGMRDDGVLTTIDVEPEHQRIAKQGFSEAGVGPGRTRLISGRAQEVLTRLADESYDLVFIDADPVDQPQFVVEGVRLLRSGGAIVVHRAALGGRAGDADARDAEVTAVREAARLIAEDERLTPVLIPLGDGLLAAVRD", "text": "SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family."}
+{"protein": "MEMYPRHRYSKHSVFKGFSDKVRKNDLDMNVVKELLSNGASLTIKDSSNKDPITVYFRRTIMNLEMIDERKYIVHSYLKNYKNFDYPFFRKLVLTNKHCLNNYYNISDSKYGTPLHILASNKKLITPNYMKLLVYNGNDINARGEDTQMRTPLHKYLCKFVYHNIEYGIRYYNEKIIDAFIELGADLTIPNDDGMIPVVYCIHSNAEYGYNNITNIKIIRKLLNLSRRASHNLFRDRVMHDYISNTYIDLECLDIIRSLDGFDINGYFEGRTPLHCAIQHNFTQIAKYLLDRGADIVVPNTLIIHQYIQ", "text": "SIMILARITY: Belongs to the orthopoxviruses VACWR203 protein family."}
+{"protein": "MRKALYSLLFYMCICLYIYTPVFMANLKEIEVGNYFICNLRDYPTGNCSVDHDYNKTIKLLCPIVNNKNNSNKTYDPSYCFKYDGIKDEFIINNKQAYIHNTLPGVILTNNIENDTYNLSIYPPFVVKEDVTIVCICDSEKGNEGITPYLKINIKKTHGLNNDLEGDYIKGCDYGNNQGKYKFLTKPVKYTSNPICEIDAYPGDVVGINCNSYTTKMQGARLEPEGCFAMVYFSILTMKFIKTNVNNIMPNAKYYPDLASHPGNQNSKIFLTSYLLIPNEVDRDILIYCNCSYNGNKGLAIYRIFSTKAS", "text": "FUNCTION: Involved in sporozoite infection of hepatocytes and replication therein. SUBCELLULAR LOCATION: Cell surface Cell membrane Note=Present on the surface of sporozoite."}
+{"protein": "MKMSAEQISEVLKEGELEKRSDNLLQFWKRKTCVLTTDSLNIYADTQKRTKSKELKLQSIKKVDCVERTGKFVYFTIVTTDNKEIDFRCSGDDNCWNAVITMALIDFQNRKAIQDFKTRQDDESGSPGQHESRMARAP", "text": "FUNCTION: Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the PHLDA2 family."}
+{"protein": "MPPLVFDIDHIKLLRKWGICGVLSGTLPTAAQQNVFLSVPLRLMLEDVLWLHLNNLADVKLIRQEGDEIMEGITLERGAKLSKIVNDRLNKSFEYQRKFKKDEHIAKLKKIGRINDKTTAEELQRLDKSSNNDQLIESSLFIDIANTSMILRDIRSDSDSLSRDDISDLLFKQYRQAGKMQTYFLYKALRDQGYVLSPGGRFGGKFIAYPGDPLRFHSHLTIQDAIDYHNEPIDLISMISGARLGTTVKKLWVIGGVAEETKETHFFSIEWAGFG", "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. It probably carries the active site for 3'-splice site cleavage. SUBCELLULAR LOCATION: Nucleus Endomembrane system; Peripheral membrane protein Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Note=The tRNA splicing endonuclease complex is predominantly associated with the outer membrane of mitochondria, suggesting that tRNA splicing mainly takes place on the mitochondrial surface. SIMILARITY: Belongs to the tRNA-intron endonuclease family."}
+{"protein": "MSSTTVKNLVNQPYKYGFVTNIEADAIPRGLSEDVVRLISAKKNEPEFMLDFRLRAYRHWLTMAEPTWPAVHYPPIDYQDIIYYSAPKQSKKKLESLDEVDPALLETFEKLGIPLSEQKRLSNVAVDAIFDSVSIGTTFKEKLAEDGVIFCSISEALQEHPDLVQKYLGSVVPTADNFFAALNSAVFSDGSFVFIPKGVKCPMELSTYFRINNGDTGQFERTLIIAEEGASVSYLEGCTAPMYDTNQLHAAVVELVALDNADIKYSTVQNWYAGDENGKGGIYNFVTKRGLCKGVNSKISWTQVETGSAITWKYPSCVLVGDNSVGEFYSIALTNNKQQADTGTKMIHIGKNTRSIIISKGISAGNSANSYRGLVKMGPKAQGARNYSQCDSMLIGDRAAANTFPYIQVDNNTAKVEHEASTSKIGEDQLFYFAQRGISEEDAVSMLVSGFCKDVLNELPMEFAAEADKLLSLKLEGTVG", "text": "SIMILARITY: Belongs to the UPF0051 (ycf24) family."}
+{"protein": "MVNKFLAGRLKKSKGKSFKGSSSKGNSKTVKSNNNDNVVVNAADLKWKPVEIPDTLDDFEGFYGLEEIDGVGVKIVGGQVQFVAHDDTKINGNEDNLDSKDKIEIDEDAPENDLVEFKNMDDMKDGELTDNSQSESEAEAESEAESEEEEEKTGDDEGEDGAEKVDNEVLKTNVFNTDIDLEDITPSDLPEWTEKVGELSFTTLHGLTKLGFNKPTLIQEEAIPMALKGEDIMGKASTGSGKTLAYGIPIIEKLMKSKSNTAPIGLIFTPTRELAKQVTDHLRKIASLIVDKSPHAILSLTGGLSIQKQERLLKYEGSGRIVVATPGRFLELIEKDKTLVERFSQISTLVLDEADRLLQDGHFDEFENILKYLGRESKNRKHNWQTMIFSATFATDLFDKLSHASWKNMKTPSKNENEMEIVLKHLMTKIHFKSKPILIDANPEDKVSSQIKESLIECAATERDLFCYYFVSMYPGKTLIFCNAIDSVKKLTAYLNNLNISCFQIHSSMTQKNRLRNLERYQQQSEKNKILGKPTVLVGSDVAARGLDIPGIQHVIHYHLPRTADVYIHRSGRTARANNEGVSVMICSPEEAMGPLRKLRKTLANKSGKDIIMGKKKWQKTVTMLPIDDTILSQLKERSRLASELADHDLASSSLQKDDTWMKKAAEDLGVDIDSDDEIKDTFLAKNINKKRNKTLGKDQKKVLVAQLNDLLKRPLRKDMRQRYLTGGLVNLADSLVKKRGHDHIIGHEKTDALETLKNKKRK", "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": "MPTRTISISEEAYEKLKSLKSSEKDSFSDVILRYYPKKRKLSEVLAEIGPNPELADAIEKVSGEMRAEKMREIDPES", "text": "FUNCTION: Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is VapC3 (Potential). SIMILARITY: Belongs to the UPF0330 family."}
+{"protein": "MADFYYLPGSSPCRSVIMTAKAVGVELNKKLLNLQAGEHLKPEFLKINPQHTIPTLVDNGFALWESRAIQVYLVEKYGKTDSLYPKCPKKRAVINQRLYFDMGTLYQSFANYYYPQVFAKAPADPEAFKKIEAAFEFLNTFLEGQDYAAGDSLTVADIALVASVSTFEVAGFEISKYANVNKWYENAKKVTPGWEENWAGCLEFKKYFE", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SIMILARITY: Belongs to the GST superfamily. Theta family."}
+{"protein": "MNKNMAGILSAAAVLTMLAGCTAYDRTKDQFVQPVVKDVKKGMSRAQVAQIAGKPSSEVSMIHARGTCQTYILGQRDGKAETYFVALDDTGHVINSGYQTCAEYDTDPQAAK", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Lipid-anchor. SUBCELLULAR LOCATION: Cell inner membrane; Lipid-anchor."}
+{"protein": "MYTPIPANTPAPTAPTSSMTSNSSSASNANTTSSSGINPRNRASGTPSNERARPASGISSFLNTFGIRQNSQTASSSAAPDQRLFGTTPSNSHMSVAMESIDTAPQQQEPRLHHPIQMPLSAQFHVHRNYQLPISISLTAPTTTDHQQSSAHNFEGNNVGNVQESLNQRQPNGTNNTTTSIISMAPAATTRNIVGGADGSTIVNNSQEMYKNLRHLIYAANQPNGTEILHLDLPATSAEESNNMFNVDEVTLKQRKDKHGLFSIRLTPFIDSSSTTNQGLFFEPIIRKAGPGSQLVIGRYTERVRDAISKIPEQYHPVVFKSKVVSRTHGCFKVDSQGNWYIKDVKSSSGTFLNHQRLSPASSLSKDTPLRDGDILQLGMDFRGGTEEIYRCVRMRIELNRSWKLKANSFNKEALQRLQNLQKLTTGIEEEDCSICLCKIKPCQAIFISPCAHSWHFRCVRRLVMLSYPQFVCPNCRSSCDLEASFESSDEEDESDVESEGDQLVDQLSVLMETSKDVDSHP", "text": "FUNCTION: E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugating enzymes. Involved in nutritional control of the cell cycle. Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DMA1 family."}
+{"protein": "MKTDILIIGGGGAAARAAIECRDKNVIIAVKGLFGKSGCTVMAEGGYNAVFNPKDSFKKHFYDTVKGGGFINNPKLVEILVKNAPKELLNLERFGALFDRTEDGFIAQRPFGGQSFNRTCYCGDRTGHEIMRGLMEYISKFERIKILEEVMAIKLIVKDNRCYGAIFLDLKTGNIFPIFAKATILATGGAGQLYPITSNPIQKTGDGFAIAYNEGAELIDMEMVQFHPTGMVGTGILVTEAVRGEGGILYNKYKERFMVRYDKERMELSTRDVVARAIYKEIQEGRGVNGGVYLDVSHLPNEVIEKKLETMLKQFLRVGIDIRKEPMIVSPTAHHFMGGLKINERCETNIIGLFACGEVTGGVHGANRLGGNALADTQVFGAIAGKSAKEFVENHDFNNIDAEEDVAKILEEINSLKGDLNVYNLIEDLRKVMWDYVSIIRNEDGLKKALEKIDEIERNIDNVKVNGIIDLQNYFELKNMVVVAKLVTKSALYRKESRGAHYREDFPETKEEWRGNIIIKGKKMWFEKLDYSVFQNFLE", "text": "SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily."}
+{"protein": "MKGFIFAGVLVSALICLAEGKPFDNLELVEDDMLMTKEQKEAYLAHQNGRVRRAALRDRYLWPQGKIPYTFSDDIDQAGRELAERAMNHWMSRTCLRFSPRRREHAYIEFQYDGRCRARVGYTGEARQKVSIGSALDPCPLGSVIHELGHGIGFFHEHSRPDRDEYVNINVNNMREGAESNFRKDNGYFVDSRGQDYDYGSIMHYSKYQGNNAFNAVVMEPIQRGAEIGQRDGLSAGDIRQTNLMYKCNAQGDSELQPVNDEDEDKDGGDSKKKPDPKGPKPGEIEE", "text": "FUNCTION: Metalloprotease. SUBCELLULAR LOCATION: Secreted Nematocyst."}
+{"protein": "MVCVPCILLPVLLALYIKFIQPIVFRFLPESWRTTFDALLYPTCPIQIPTASAEDATTVAAGKSVKVDGENVQKELDNYDNCTDSSKKNK", "text": "SIMILARITY: Belongs to the UPF0729 family."}
+{"protein": "MNTTLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALMAERVAFVVRKMTVEYYAPARLDDMLEIQTEITSMRGTSLVFTQRIVNAENTLLNEAEVLVVCVDPLKMKPRALPKSIVAEFKQ", "text": "FUNCTION: Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond (By similarity). FUNCTION: Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family."}
+{"protein": "MSDGITGALRNAASVVAPDAIRRRFGAKFAVAFIVVLVVIAGAGVFAFQSTETTVEHQTTRQLAESNQLEADAIGAWMEQQRTHARSVSQDEALRDDRRAAPYILLKDQLLPADVVSMHLVNETRGTVVASTELAIEGRSLAELDAPWTTAAVPEGPGNDSAVWATEQSYRSPVLNDEPVMAFASSVPKREGAHLVVVTRIQPQVDRLSDANSTRRTTILNTGDEPVLDSNSRFDAGALTDSIAAVRNDTTAATTTVSNGRVYALSATPHTDWVTVTSVDTGEAFAVRDTVGQTVTVLVVLAVISLAIVGIALGRHTVTPLKRLRNRAQDIESGTFDVDLSTRRIDEVGRLYGSFDDMRVSLQDRIQEAEAAVEEANAAKAEAEELRTDAEDAQAEAERAKATAEAASERLQERAADYSEVMQAVADGDLTERLDEDADEEAMRAVATEFNAMLDGLEATIAQVAGFADEVADETLQVATGAEEIETTSQTVSERIQEIADGAIQQHDDLERAAGEMDELSASIQEVAASSATVAETAADAVERGEAGRDAAESAIDDMAEIESLSADAVDQILALQERMSDIGDIIEFITDIAEQTNMLALNANIEAARADKDGDGFAVVANEVKDLAEETKQAAADIESEIQAVQAETDETVADIRATSEHIDDGVSTVERAAAAIEDTVDAIEDANHGIQEISDATEDQADATQSVVRRVDDVADISQHVTEDAEQVSAAAEEQSASVAEIARSADDLRDRADALATTVNQFETRADADEPDADTTVDASADDTGD", "text": "FUNCTION: Potentially involved in chemo- or phototactic signal transduction. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein family."}
+{"protein": "MSMTSDDIIYVVFALGLVVSFGLGAITAGVFR", "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": "MDDHLKLGDSGVVKNVARLGRRGQRARQAAEQTSLEEPRHVRKSSSSTSMGEGPPPKPARRQGGWAEETSGSAKSGRRPAMVQDVEDRRLRPQTPQGSDGEGDIPVIPDLDEVQEEDLNMQVAAPPSIQVNRVMTYRDLDNDLMKYSAFRTLDGEIDLKLLTKVLAPEQEVREEDVGWDWDHLFTEVSSELLTEWDQGEKEEQVCVMRTSLPKMG", "text": "FUNCTION: Component of IFT complex A (IFT-A) involved in retrograde ciliary transport along microtubules from the ciliary tip to the base. SIMILARITY: Belongs to the IFT43 family."}
+{"protein": "MDNLGHRENGRQRPDQYKGLHTQWMMPQTQRHLKDHQSMNLLALMNDRDNAIRERDHALAEKKAAIAERDMAFTQRDAAMAERNAAVVERDNALAALELARTNGLNMNNGNGFPQGSLSGSKNIHHHDQLSHAQSSPLQLADSPYDHAREMHISEAYPISTAPGSAGKAKRPKKNSSQASPLKRPSGVLRKTKKPSGDWKNVGMSGCGDDSAHASVMKNEWKDQNLGLNQVAFDDSTMPAPACSCTGKLRQCYKWGNGGWQSSCCTMNISMYPLPVMPNKRHARMGGRKMSGGAFTKLLSRLAAEGHDLSTPVDLKDHWAKHGTNRYITIR", "text": "FUNCTION: Transcriptional regulator that specifically binds to GA-rich elements (GAGA-repeats) present in regulatory sequences of genes involved in developmental processes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BBR/BPC family."}
+{"protein": "MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLPARTVETRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMNCKCVIS", "text": "FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Golgi apparatus membrane; Lipid-anchor Note=Shuttles between the plasma membrane and the Golgi apparatus. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MSCPVIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQGETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA", "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. 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. SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily."}
+{"protein": "MNRIGMITTIITTTITTGNGAG", "text": "FUNCTION: This protein is involved in control of the biosynthesis of threonine. SIMILARITY: Belongs to the thr operon leader peptide family."}
+{"protein": "MDCQEKLEVPVYTDVDKETFLRDIYPQRRPAVLKRVPIGPCVRTWTVCFLAEKGGDREVKVHVSPEPRMDFLHKNFVYRTLPFDEFIKRAAEAKHPEFFISEDESYYLRSLGEDARKEPADLRKQFPELAEDFHVPQFFEPEQFFSSVFRISSPGLQLWTHYDVMDNLLAQVTGKKRVVLYSPEDALHLYLTGDKSEVLDIDSPDLQLYPEFVKARRYECILEPGDLLFIPALWFHNTLALQFGVGVNVFWRHLPSESYDKKDPYGNKDPVAATRALQSLERTLGILDELPPDYRDFYARRMVLRIQSRAYIRKPINAAQENSDTT", "text": "FUNCTION: tRNA hydroxylase 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. Catalyzes the hydroxylation of 7-(a- amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW*). OHyW* being further transformed into hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a derivative of wybutosine found in higher eukaryotes. SIMILARITY: Belongs to the TYW5 family."}
+{"protein": "MAERVLTRVHSLRERLDETLVANRNEIVALLSRIIGKGKGICRNHQLIAEVEAIPEATRKKLLDGAFGEVLRSAQEAIVLPPWVALAVRPRPGVWEYIRVNVHALVVEELRVPEYLHFKEELVDGSTNGNFVLELDFDPFNASFPRPTLSKSIGNGVEFLNRHLSAKLFHDKESMHPLLEFLRVHCYKGKNMMLNDRIQNVNALQYVLRKAEEYLTTIAPETPYVKFEHKFQEIGLVRGWGDTAEGVLEMIQLLLVLLEAPVPCTLEKFLGKSLWLNVVIMSPHGYFAQDNVGYPDTGGQVVYILDQVRALESEMLLRIKQQGLDITPRILIVTRLLPDAVGTTCGQRLERVYGSEHADILRVPFRTEKGIVRQWISRFEVWPYLETYTEDVGVELIKELQGKPDLIIGNYSDGNIVASLLAHKFGVTQCTHAHALEKTKYPESDIYWKKMDEKYHFSSQFTADLIAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHELCIDPKFNIVSPGADMSIYFPYTEKEKRLTSFHPEIEELLYSPVENEEHLCVLKDRNKPIIFTMARLDRVKNITGLVEWYGKNTRLRELVNLVVVAGNLEKESKDNEEKAEMTKMHGLIETYKLNGQFRWISSQMNRVRNGELYRYIADTKGGLCAGPAIYEAFGLTVVESMTCGLPTFATCKGGPAEIIVHGKSGFHIDPYHGEQAAQLLVDFFEKTKADPSHWAKISLGGLQRIHEKYTWKIYSERLLTLTGVTAFWKHVSNLDRLESRRYIEMFYALKYRKLAESVPLAVE", "text": "FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways. SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose synthase subfamily."}
+{"protein": "MPTPRMSMRKLKEVLRLKWACGLTHRQISRAIGISVGAVSKFAAQASQAGLDWAAAEAMSDDELDARLRPAATNAAATTTRRIEPDYTALHRELRRKGVTLQLLWEEYAEANPGQRTYRYTQFCQKYKDWAKSIKRSMRQQHRAGEKLFADFAGPTVPVLASDGGVEFEAHVFVAVLGASNYTFACATRTETMADWIGSLCDALEFIGGVPELLVPDNPKALIARPDRYEPGLGTTTQDFVNHYGTAMLPARPRKPQDKAKVEVGVQIVERWVLARLRHYRFYSLAELNKAIAELIADLNQRPFKRLEGNRREWFERLDQPVLRPLPVRRYEIATFQKCRVNIDYHVDVGGHYYSVPHSLARQEVWARITRHGVEILHGGKRVAAHARSRLKGKHTTIAEHMPAAHRAHMEWTPGRLLNWGASVGPGAEAVVRHLLTNKPHPEMGYRACLGLLSLARKYGKHRLEAACQRALKIGSPTRRSVLSILEAGLDLQPSLPTTPAEWRSPEHENVRGPDYYH", "text": "FUNCTION: Required for the transposition of the insertion element. SIMILARITY: Belongs to the transposase IS21/IS408/IS1162 family."}
+{"protein": "MNPNMNMMPMSGPQMMQVMQSSPSGPPGPVQHQQQQPPQPLQQQQQAEKLDNISRVKSLLGPLRESMFLTIRSSAFALQQNNLADNLKRDTGAHHVPRFDKHLEDFYACCDQIEIHLKTAMQCLQQQNSSNHYLPGPVTPMRMETFMPDNAGPISYPTYLNTVRVHIQSAKDIHDTLISAAQNISQAD", "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). Required for female somatic sexual development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 29 family."}
+{"protein": "MAQDRKKVLVLGAGYAGLQTVTKLQKELSADAAEITLINKNEYHYESTWLHEASAGTINYEDLLYPVEKTVNKNKVNFVVAEVTKIDRNAKRVETDKGVYDFDILVVALGFVSETFGIDGMKEHAFQIENVLTSRKLSRHIEDKFANYAASKEKDDKDLSILVGGAGFTGIEFLGELTDRIPELCSKYGVDQSKVKLTCVEAAPKMLPMFSDDLVSYAVKYLEDRGVEFKIATPIVACNEKGFVVEVNGEKQQLEAGTSVWTAGVRGSHLMEESFEGVKRGRIINKQDLTIEGHNDIFVIGDCSAFIPADEERPLPTTAQIAMQQGEHTASNIKRLLNGESTQDFQYVNRGTVCSLGANDGVGIVYGRDIAGKKAAFLKKVIDTRAIYKLGGIGLAFKKGKF", "text": "FUNCTION: Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones, and contributes to the regeneration of NAD(+). SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the NADH dehydrogenase family."}
+{"protein": "MKKSTIWILGIIMGLSFLSLLYLQVSYIEEMVKMRKEQFNTSVRNALFQVSKDVEYDETQRWLLEDITEAERRALAQSSSTTEQKNGLIQQSERYRFKSPDGTLYSEFELKMITTEPSKVPKAMISERHGRNTIPQTSRSLTDAIKNRYMYQRFLLDDVALRMIYKASDKSIGERVNFKKLDNYLKSNFINNGVELLYHFSVIDKDGREVYRCSDYEDGGSEDSYTQPLFQNDPPAKMSIVKVHFPGKKDYIFDSVSFMIPSMIFTIVLLITFIFTIYIVFRQKKLTEMKNDFINNMTHEFKTPISTISLAAQMLKDPAVGKSPQMFQHISGVINDETKRLRFQVEKVLQMSMFDRQKATLKMKELDANELITGVINTFALKVERYNGKITSNLEATNPVIFADEMHITNVIFNLMDNAVKYKKPEEDLVLNVRTWNEPGKLMISIQDNGIGIKKENLKKVFDKFYRVHTGNLHDVKGFGLGLAYVKKIIQDHKGTIRAESELNVGTKFIIALPLLKND", "text": "FUNCTION: Member of the two-component regulatory system RprX/RprY. May activate RprY by phosphorylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MSQPPKILLLYAHPEPQDSVANRVLLQPAQQLANVTVHDLYAHYPDFFIDIHHEQQLLREHQVIVFQHPFYTYSCPALLKEWLDRVLSRGFANGIGGNALAGKYWRSVITTGEPEDAYHPDGNNRYPMEDLLRPFELTAAMCRMHWMHPMIVYWARRLQPDVLSSQARAYGEWLASPLPEEER", "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": "MSRRAGTPTAKKVTQLVNEEEHVEGFRQVREAHRRELIDDYVELISDLIREVGEARQVDMAARLGVSQPTVAKMLKRLATMGLIEMIPWRGVFLTAEGEKLAQESRERHQIVENFLLVLGVSPEIARRDAEGMEHHVSEETLDAFRLFTQKHGAK", "text": "FUNCTION: In the presence of manganese, represses expression of mntH and mntS. Up-regulates expression of mntP (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DtxR/MntR family."}
+{"protein": "MDLIPNLAVETWLLLAVSLILLYLYGTRTHGLFKKLGIPGPTPLPFLGNALSFRKGYWTFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGGLLLTEKPIVLKAESRDETVSGA", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins during embryogenesis (PubMed:9555064, PubMed:11093772, PubMed:14559847, PubMed:12865317, PubMed:17178770). 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:9555064, PubMed:11093772, PubMed:14559847, PubMed:12865317, PubMed:17178770). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes 3beta- hydroxyandrost-5-en-17-one (dehydroepiandrosterone, DHEA), a precursor in the biosynthesis of androgen and estrogen steroid hormones (PubMed:9555064, PubMed:17178770). Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1), particularly D- ring hydroxylated estrone at the C16-alpha position (PubMed:14559847, PubMed:12865317). Mainly hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in atRA clearance during fetal development (PubMed:11093772). Also involved in the oxidative metabolism of xenobiotics including anticonvulsants (PubMed:9555064). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MKTSIRYALLAAALTAATPALADITVYNGQHKEAAQAVADAFTRATGIKVKLNSAKGDQLAGQIKEEGSRSPADVFYSEQIPALATLSAANLLEPLPASTINETRGKGVPVAAKKDWVALSGRSRVVVYDTRKLSEKDLEKSVLNYATPKWKNRIGYAPTSGAFLEQVVAIVKLKGEAAALKWLKGLKEYGKPYAKNSVALQAVENGEIDAALINNYYWHAFAREKGVQNVHTRLNFVRHRDPGALITYSGAAVLKSSQNKDEAKKFVAFLASKEGQRALTAVRAEYPLNPHVVSTFNLEPIAKLEAPQVSATTVSEKEHATRLLEQAGMK", "text": "FUNCTION: This protein may be a central component in the iron- acquisition system. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
+{"protein": "MTRSYLPLNSLRAFEAAARHLSFTHAAIELNVTHSAISQHVKTLEQHLNCQLFVRVSRGLMLTTEGENLLPVLNDSFDRIAGMLDRFANHRAQEKLKIGVVGTFATGVLFSQLEDFRRGYPHIDLQLSTHNNRVDPAAEGLDYTIRYGGGAWHGTEAEFLCHAPLAPLCTPDIAASLHSPADILRFTLLRSYRRDEWTAWMQAAGEHPPSPTHRVMVFDSSVTMLEAAQAGVGIAIAPVDMFTHLLASERIVQPFATQIELGSYWLTRLQSRAETPAMREFSRWLVEKMKK", "text": "FUNCTION: This protein is a positive regulator of gene expression of cephalosporinase (AmpC). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MTTNNSNDNNKRYGIIKQQLQQQQQQHHQQHEQHSRLVEMTAGCGAGFMASLFTTPLDVIKTTLQVDNSSNKTIMSTVKSILDRKGGVKNLYLGLKPTLVGQIPSWAVYFSTYTFCKELFTKENDKHSLLEKESPLIFMTSAIIAGAATSICTSPIWLIKTRFITQEMVGRQKKYRGIVHSMVSIYHEEGFRGLYKGLGPSLLGVLHVGVQFPLYEKFKSILKEKNKNKELGIVEIMIASSVSKIIASVVAYPHEVLRARSQDSSPDSPNRTYRGNIIQMFKQIVREEGWRGLYRGMGVNLLRVTPSCVITFTSYEYIKKFLSQNQNHF", "text": "FUNCTION: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MNSTPDLISPQKSSENSNADLPSNSSQVMNMPEEKGVQDDFQAEADQVLTNPNTGKGAYVTVSICCVMVAFGGFVFGWDTGTISGFVAQTDFLRRFGMKHKDGSYYLSKVRTGLIVSIFNIGCAIGGIILAKLGDMYGRKMGLIVVVVIYIIGIIIQIASINKWYQYFIGRIISGLGVGGIAVLSPMLISEVAPKEMRGTLVSCYQLMITLGIFLGYCTNFGTKNYSNSVQWRVPLGLCFAWALFMIGGMTFVPESPRYLVEAGQIDEARASLSKVNKVAPDHPFIQQELEVIEASVEEARAAGSASWGELFTGKPAMFKRTMMGIMIQSLQQLTGDNYFFYYGTTVFNAVGMSDSFETSIVFGVVNFFSTCCSLYTVDRFGRRNCLLYGAIGMVCCYVVYASVGVTRLWPNGEGNGSSKGAGNCMIVFACFYIFCFATTWAPIAYVVISETFPLRVKSKAMSIATAANWLWGFLIGFFTPFITGAINFYYGYVFMGCMVFAYFYVFFFVPETKGLTLEEVNDMYAEGVLPWKSASWVPTSQRGANYDADALMHDDQPFYKKMFGKK", "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": "MSDSLVVCEVDPELTEKLRKFRFRKETDNAAIIMKVDKDRQMVVLEEEFQNISPEELKMELPERQPRFVVYSYKYVHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNRLVQTAELTKVFEIRTTDDLTEAWLQEKLSFFR", "text": "SIMILARITY: Belongs to the actin-binding proteins ADF family. GMF subfamily."}
+{"protein": "MAESELMHIHSLAEHYLQYVLQVPAFESAPSQACRVLQRVAFSVQKEVEKNLKSYLDDFHVESIDTARIIFNQVMEKEFEDGIINWGRIVTIFAFGGVLLKKLPQEQIALDVCAYKQVSSFVAEFIMNNTGEWIRQNGGWEDGFIKKFEPKSGWLTFLQMTGQIWEMLFLLK", "text": "FUNCTION: Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection. Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11 (PubMed:11888890). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Bcl-2 family."}
+{"protein": "MSFVPGQENAGSRSSSGNRAGNGILKKTTWADQTERGQNNGNRGRRNQPKQTATTQPNTGSVVPHYSWFSGITQFQKGKEFQFAGGQGVPIANGIPPSEQKGYWYRHNRRSFKTPDGQQKQLLPRWYFYYLGTGPHAGASFGDSIEGVFWVANSQADTNTSADIVERDPSSHEAIPTRFAPGTVLPQGFYVEGSGRSAPASRSGSRSQSRGPNNRARSSSNQRQPASTVKPDMAEEIAALVLAKLGKDAGQPKQVTKQSAKEVRQKILNKPRQKRTPNKQCPVQQCFGKRGPNQNFGGPEMLKLGTSDPQFPILAELAPTPGAFFFGSKLELVKKNSGGVDEPTKDVYELQYSGAVRFDSTLPGFETIMKVLNENLNAYQNQAGGADVVSPKPQRKRGTKQTAQKEELDSISVAKPKSAVQRNVSRELTPEDRSLLAQILDDGVVPDGLDDSNV", "text": "FUNCTION: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. SUBCELLULAR LOCATION: Virion Host endoplasmic reticulum-Golgi intermediate compartment Host Golgi apparatus Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family."}
+{"protein": "MANLPILLDYWPSMFGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPIHKKIPVLVHNGKPVCESLNVVQYVDEAWPEKNPFFPSDPYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISLITFSSWFQAYEKFGNFSIESESPKLIAWAKRCMEKESVSKSLPDSEKIVAYAAEYRKNNL", "text": "FUNCTION: Exhibits glutathione-dependent thiol transferase activities. Can use glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) as substrates. Involved in the regulation of far-red light influence on development (PubMed:17220357). Regulator of the interplay between light and JA signaling by increasing JAR1/FIN219 efficiency (PubMed:28223489). Maybe involved in gravitropic signal transduction (Probable). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. Tau family."}
+{"protein": "MMKLDEIIETLRQGKHVDEDSIYSLCVMAQELLMNESNVTHVDTPVTICGDIHGQLHDLLTLFAKSGGIEKNRYIFLGDFVDRGFYSLESFLLLVCYKLRYPDRIVLIRGNHETRQITKVYGFYDEVVRKYGNSNVWRYCCEVFDYLPLGAIVNNKVFCVHGGLSPDVLSINEIRTIDRKKEVPHEGAMCDLLWSDPEDVDTWSLSPRGAGFLFGQNEVDKFLHTNSVELIARAHQLVMEGYKEMFDGGLVTVWSAPNYCYRCGNVAAVLRIDDDMTKDYTIFEAVQARDSGGNVILPTKKPQMDYFL", "text": "FUNCTION: Forms the histone H2A phosphatase complex in association with the regulatory subunits PSY2 and PSY4, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily."}
+{"protein": "MQQEEIIEGYYGASKGLKKSGIYAKLDFLQSATGLILALFMIAHMFLVSSILISDEAMYKVAKFFEGSLFLKAGEPAIVSVVAAGIILILVAHAFLALRKFPINYRQYKVFKTHKHLMKHGDTSLWFIQALTGFAMFFLASIHLFVMLTEPESIGPHGSSYRFVTQNFWLLYIFLLFAVELHGSIGLYRLAIKWGWFKNVSIQGLRKVKWAMSVFFIVLGLCTYGAYIKKGLENKENGIKTMQEAIEADGKFHKE", "text": "FUNCTION: The fumarate reductase enzyme complex is required for fumarate respiration. This subunit anchors the complex in the membrane and binds a diheme cytochrome b. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the diheme cytochrome b FrdC family."}
+{"protein": "MLRRLVQQWSVAVFLLSYSVPSCGRSVEGPGRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPAANTKNHAVRFGSDDEGRYLTQETNKVEPYKEQPLKTPGKKKKGKPGKRKEQEKKKRRTRSAWPLSAGAGSGLAGDHLSDISEPEPELDSRRH", "text": "FUNCTION: Osteostatin is a potent inhibitor of osteoclastic bone resorption. FUNCTION: Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport. Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth. Required for skeletal homeostasis. Promotes mammary mesenchyme differentiation and bud outgrowth by modulating mesenchymal cell responsiveness to BMPs. Up-regulates BMPR1A expression in the mammary mesenchyme and this increases the sensitivity of these cells to BMPs and allows them to respond to BMP4 in a paracrine and/or autocrine fashion. BMP4 signaling in the mesenchyme, in turn, triggers epithelial outgrowth and augments MSX2 expression, which causes the mammary mesenchyme to inhibit hair follicle formation within the nipple sheath (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Secreted. SIMILARITY: Belongs to the parathyroid hormone family."}
+{"protein": "MASALEQFVNNVRQLSAQGQMTQLCELINKSGELLAKNLSHLDTVLGALDIQEHSLGVLAVLFVKFSMPNIPDFETLFSQVQLFISTCNGEHIRYATDTFAGLCHQLTNALVERKQPLRGISILKQAIDKMQMNTNQLTSVHADLCQLCLLAKCFKPAVPFLELDMMDICKENGAYDAKHFLCYYYYGGMIYTGLKNFERALYFFEQAITTPAMAVSHIMLEAYKKYILVSLILHGKVQQLPKYTSQIVGRFIKPLSNAYHELAQIYATNNPAELRALVNKHSETFTRDNNTGLVKQCLSSLYKKNIQRLTKTFLTLSLQDMASRVQLSGPQEAEKYVLHMIEDGEIYASINQKDGMVCFHDNPEKYNNPAMLHKIDQEMLKCIELDEKLKSMDQEITVNPQFVQKSMGTQEDDVGSKTSSYS", "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": "MEKATERQRILLRHLQPSSSSDASLSASACLSKDSAAYQYGDDVVIVAAQRTALCKAKRGSFKDTFPDELLASVLRALIEKTNVNPSEVGDIVVGTVLGPGSQRASECRMAAFYAGFPETVPIRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGLESMTTNPRGWKGSVNPNVKKFEQAHNCLLPMGITSENVAHRFNVSREEQDQAAVDSHRKAASATASGKFKDEITPVKTKIVDPKTGDEKPITVSVDDGIRPNTTLSGLAKLKPVFKEDGTTTAGNSSQLSDGAGAVLLMRRNVAMQKGLPILGVFRTFSAVGVDPAIMGVGPAVAIPAAVKAAGLELNDVDLFEINEAFASQFVYCRNKLGLDAEKINVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDCRFGVVSMCIGSGMGAAAVFERGGGVDELCDVRKV", "text": "FUNCTION: Involved in fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Implicated in jasmonic acid (JA) biosynthesis (By similarity). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
+{"protein": "MSISNWITTAYLITSTSFQPLYGSFSDALGRRNCLFFANGAFTIGCLACGFSKNIYMLSFMRALTGIGGGGLITLSTIVNSDVIPSSKRGIFQAFQNLLLGFGAICGASFGGTIASSIGWRWCFLIQVPISVISSILMNYYVPNQKEYNRQNSSIFQNPGKILRDIDVMGSILIITGLTLQLLYLSLGCSTSKLSWTSPSVLLLLVGSVIILLLFILHERKTSARAIIPMELVNSSYSVVVLSISILVGFASYAYLFTLPLFFQIVLGDSTAKAGLRLTIPSLFTPVGSLITGFSMSKYNCLRLLLYIGISLMFLGNFLFLFIEKTSPNWLIGLFLIPANLGQGITFPTTLFTFIFMFSKSDQATATSTLYLFRSIGSVWGVAISAGVIQLSFAGLLRSNLKGLLDENKIKKLIVQLSANSSYIGSLHGEVKNTVIKSFDEATKRAHLMSTLLSSLALILCILKDNLAKPKTRR", "text": "FUNCTION: Transporter required for vacuolar uptake of histidine, arginine and lysine and to a lesser extent tyrosine. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MMLQHPGQVSASEVSATAIVPCLSPPGSLVFEDFANLTPFVKEELRFAIQNKHLCHRMSSALESVTINNRPLEMSVTKSEVAPEEDERKRRRRERNKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDERNLFIQQIKEGTLQS", "text": "FUNCTION: This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Represses transcription from promoters with ATF sites (By similarity). It may repress transcription by stabilizing the binding of inhibitory cofactors at the promoter (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. ATF subfamily."}
+{"protein": "MKQRPTGPDTTPRNRRGFGRDTAVASVCGLVVALMVGASYAAVPFYNWFCRVTGFNGTTQVAAAAPQGGALKRTIAVRFDSNTNGLPWSFAPETTEIEIPIGQVTTVYYKVTNRAAHETTGQAAYNVAPLTVGAYFQKINCFCFTDQTLGPHETRELPVVFYVDPALATDSDNDTLNSITLSYTFYPLRSAAPKPLAASEAGPRQGAL", "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. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SIMILARITY: Belongs to the COX11/CtaG family."}
+{"protein": "NLVQFSNMIQCANHGSRPTRHYVDYGCYCGWGGSGTPVDELDRCCQTH", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits collagen- induced platelet aggregation. In terms of inhibition of platelet aggregation, superbin d is less potent as superbin a, b, and c. 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": "MAMTELLNAEDIKKAIGAFAAAESFDHKKFFQMVGLKKKSTEDVKKVFHILDKDKSGFIEEEELGFILKGFSPDARDLSVKETKTLMAAGDKDGDGKIGADEFSTLVSES", "text": "FUNCTION: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. SIMILARITY: Belongs to the parvalbumin family."}
+{"protein": "MASNATFEVEIYGNTTKFENSLKGVNTAMSGLRGEAKNLREALKLDPANTGKMAQLQKNLQTQLGLSRDKATKLKEELSTVDKGTSAGQKKWLQLTRDLGTVETQANRLEGEIKQVEGAISSGSWNIDAKMDTKGVNSGIDGMKSRFSGLREIAVGVFRQIGSSAVSAVGNGLKGWVSDAMDTQKAMISLQNTLKFKGNGQDFDYVSKSMQTLAKDTNANTEDTLKLSTTFIGLGDSAKTAVGKTEALVKANQAFGGTGEQLKGVVQAYGQMSASGKVSAENINQLTDNNTALGSALKSTVMEMNPALKQYGSFASASEKGAISVEMLDKAMQKLGGAGGGAVTTIGDAWDSFNETLSLALLPTLDALTPIISSIIDKMAGWGESAGKALDSIVKYVKELWGALEKNGALSSLSKIWDGLKSTFGSVLSIIGQLIESFAGIDLKTGESAGSVENVSKTIANLAKGLADVIKKIADFAKKFSESKGAIDTLKTSLVALTAGFVAFKIGSGIITAISAFKKLQTAIQAGTGVMGAFNAVMAINPFVALGIAIAAIVAGLVYFFTQTETGKKAWASFVDFLKSAWDGIVSFFSGIGQWFADIWNGAVDGAKGIWQGLVDWFSGIVQGVQNIWNGITTFFTTLWTTVVTGIQTAWAGVTGFFTGLWDGIVNVVTTVFTTISSLVTGAYNWFVTTFQPLISFYKSIFGLVGSVINLAFQLILAIIRGAYQLVIGAWSGISGFFGVIFNAVSSVVSTVFSAIGSFAGSAWNVLVGVWNAVAGFFGGIFNAVKGVVSSVFSAIGSFASSAWGVVSSIWSAVSGFFSGIFNAVSSVVSGVFSALGGFASNAWGAITGIFSGVADFFSGVFDGAKNIVSGVFEAFGNFASNAWNAITGVFNGIGSFFSDIFGGVKNTIDSVLGGVTDTINNIKGSIDWVASKVGGLFKGSMVVGLTDVNLSSSGYGLSTNSVSSDNRTYNTFNVQGGAGQDVSNLARAIRREFELGRA", "text": "FUNCTION: Probable tape measure protein. Serves as a base for tail tube protein polymerization and acts as a template for tail length determination. SUBCELLULAR LOCATION: Virion Note=Present inside the tail tube. SIMILARITY: Belongs to the skunalikevirus tape measure protein family."}
+{"protein": "MDLINFIKICHLLYDRKYVVGSGGNVSIRDGNHIYITPTGSILGFLNEEDVCIVDLNGNIIKGKPTSELNMHLKIYQNKDCVNAIVHTHSMYCTAFSALDKKLELFTPEAEIVVKKIAYVDYSPCGSLELAENVSSCVEDSIILKNHGIVTVGKDITEAYVKTEVLEEIAQLNYIINNLK", "text": "FUNCTION: Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde. SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily."}
+{"protein": "MTRPPLVRGIFSLGLSVAVLKGVEKTVRKHLERQGWIEPQKVDYELIFTIDRLKNLVDNKREALTAEQPDAGELSWRKVFNFISRQSSELDTRIYVLILLLSFLLPIAWTVLDGDRETTLEDKDNDCNVDLIENERRLKHYNDGERAVLQFGKNRSEPIILSYKDMNVLEGEHEFTSKEEHSNSHLTSKSENALNQVGSEDLLGCHLEKQLEEDKNEPNGEADGEDDNNREKDCSSSSEVESQSKCRKESTAEPDSLSRDTRTTSSLKSSTSFPISFKGSIDLKSLNQPSSLLHIQVSPTKSSNLDAQVNTEQAYSQPFRY", "text": "FUNCTION: Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13. SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass membrane protein."}
+{"protein": "MPDYSYRPTIGPTYVYHNKYYKNLGSVIKKPKRKKHLVEHEEEEKDPLDNYMVAEDPFLGPGKNQKLTLFKEIRNVKPDTMKLIVNWSGKEFLRETWTRFVEDSFPIVNDQEVMDVFLV", "text": "FUNCTION: Major component of the virus occlusion bodies, which are large proteinaceous structures (polyhedra), that protect the virus from the outside environment for extended periods until they are ingested by insect larvae. SIMILARITY: Belongs to the polyhedrin family."}
+{"protein": "MAAAFSSDGEAVLRRTLDPAAAAPRGDKDEFYEVDRAAAFVRDGGFRKVALQFPDALLADAAAVAARMEEVTGAEMYVLGDTTYGSCCVDEVAAEHVSAGAVVHYGPACLSPCRKLPVLHVFGRQPLDVGRCAEVFRELYPERQSRVVVLSDVVYAHAMGELEKQLCHEYPNIIFSEVVCGDAPSPTLPGEVRQFGRRFHMEAAEELQDCSMFYVGAEGLALTSFMLTWNRFPFSSFDPATGHGRRETLNVNRALMRRLYLVERARDAHVVGILVGTLGVAGYLDVLEHLHQLVRRAGKRSYTLSVGKPNPAKLANFLEVDIFVLVACAQNSLLDSSEFYRPIVTPYELELACNPAREWTGNYLTDFRDLLPGACAHIELPPAVPAAEAIPDVSLITGEMRATHLCDPLAPQPPSSTTLACRDQTRALAEMSPAATFLESRSWRGLEQQLGKTAVSKAVQGRRGIAIAYEDEGREQS", "text": "FUNCTION: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). 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). Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity). SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily."}
+{"protein": "MPKYTLHYFPLMGRAELCRFVLAAHGEEFTDRVVEMADWPNLKATMYSNAMPVLDIDGTKMSQSMCIARHLAREFGLDGKTSLEKYRVDEITETLQDIFNDVVKIKFAPEAAKEAVQQNYEKSCKRLAPFLEGLLVSNGGGDGFFVGNSMTLADLHCYVALEVPLKHTPELLKDCPKIVALRKRVAECPKIAAYLKKRPVRDF", "text": "FUNCTION: High activity toward 1-chloro-2,4-dinitrobenzene. Not very efficient at catalyzing the addition of GSH to enones and epoxides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Sigma family."}
+{"protein": "MSKKKGKTPQPAAKTMTASGPKMEAFTFGEPVPVLDRRDILDYVECISNGRWYEPPVSFTGLAKSLRAAVHHSSPIYVKRNILASTFIPHPWLSQQDFSRFVLDFLVFGNAFLEKRYSTTGKVIRLETSPAKYTRRGVEEDVYWWVPSFNEPTAFAPGSVFHLLEPDINQELYGLPEYLSALNSAWLNESATLFRRKYYENGAHAGYIMYVTDAVQDRNDIEMLRENMVKSKGRNNFKNLFLYAPQGKADGIKIIPLSEVATKDDFFNIKKASAADLLDAHRIPFQLMGGKPENVGSLGDIEKVAKVFVRNELIPLQDRIREINGWLGQEVIRFKNYSLDTDND", "text": "FUNCTION: Forms the portal vertex of the capsid (PubMed:8178458). 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": "MISAVLNLPSTPLLPLLWFTLIIPASLTNPKFVWRFSITETWSTGNQAHSQTQGTADCSPQGCQDALLLNFHLSSVGNYDHPVICFLYDQTEYNCKNYWQETNLGCPYNYCNMHEIGLMCANGICTPNDRPFVRNRTSGGYILTIKDPWDPRWAQGVKGGLYATSWSSYPTATLQIKRVYVQQVPAPKSKQVDPPKSVQALQNLTSVVKSHEQKIQKLLSPPNSPNNEDPFSWLTLIRQGLNLTQAAGVRNLSHCFLCAALGKAPLVAVPLPTAFNITTDSTSSSQATSLPQVPLYRNPQSQTLPFCYSTPNSSWCDRTQAPSRTQTAPVGGYFWCNQTLSKTLNHASITQSLCVPVSLVPSLTLYSEGELAELASQLSSSNNIQKQAVFLPLIIGVSLASSLVASGLGTGALTHSIQSTQTLSTQVQAAIEASAESLASLQRQITSVAQVAAQNRRALDLLTAEKGGTCLFLGEECCYYVNESGLVDTNVKTLNKIKKELQQFNAPLTPGPPVWLLPVVQQMLPFLIPILILCLMLCLAPILIKFLRARVQEITRVTFNQMLLHPYTQLPTSDPNYAP", "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. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=At the origin, this retroviral envelope protein was localized in the virion. SIMILARITY: Belongs to the gamma type-C retroviral envelope protein family. HERV class-I F(c)1 env subfamily."}
+{"protein": "MAGLPDKDKLIRNFSRCLNWEEKYLYVIELGAQLPPLTEQQRQPDNLISGCQSQVWIAMSTSTEGQVVFAGDSDAAIVKGLVVVVFILYQGLTPQQIIDLDVRPFFADLALSQHLTPSRSQGLEAMIRAIRAKAAVLKAG", "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": "MNNQNEDTEGGRNCCTCCLSFIFTAGLTSLFLWLSLRADKPKCSIQNFFIPALGKDPNSRDNTTLNFMVRCDNPNKDKGIYYDDVHLNFSTINTTKINSSALVLVGNYTVPKFYQGHKKKAKKWGQVKPLNNQTVLRAVLPNGSAVFRLDLKTQVRFKIVFWKTKRYGVEVGADVEVNGDGVKAQKKGIKMKKSDSSFPLRSSFPISVLMNLLVFFAIR", "text": "FUNCTION: Involved in disease resistance. Required for resistance conferred by multiple R genes recognizing different bacterial and oomycete pathogen isolates like avirulent P.syringae or H.parasitica (downy mildew). Required for the establishment of hypersensitive response (HR) and systemic acquired resistance (SAR) after infection with the bacterial pathogen P.syringae DC3000 carrying avrRpt2. Required for resistance to the soilborne fungus V.longisporum. Interaction with RIN4 is required for the activation of the R gene RPS2 and RPS2-mediated resistance. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor."}
+{"protein": "MGRIGILGAGLAGLAAATKLAEAGENVTVFEARNRPGGRVWSETLDTPKGSYVIERGAEFVLDGYTSMRRLLSQFGLSLVDTGMSYYVREPGDTTGITCDDIIRTGREALELASGSGLQGTAEELLAKLPDEPELVDALRARIEISTAVSASEVTARSLQHIASFEPKPSWRVAGGNQRLPDAMAAALGSAVRYGETVRAVENISDGGVLVTTDTDTSVFDTVVVALPLAVIRDSQLNLPTTEARDAALKHVLQGHAAKLHLPLETQPATSAVMSVEGRYWTWTATDESGAVAPVLNAFMGSPSAITRANLKQRPAEWVAKARALRTDLAIPQDAAALTTVWSEDQLAGGAYAAHAPGVTAAGTALLEKPVGDVFWAGEYSEPEFVGLMEGAIRSGERAAGRVMQRLETKSGNSDSERSKA", "text": "FUNCTION: Catalyzes the removal of methylamine from 4- methylaminobutanoate with the formation of succinate semialdehyde. Is involved in the catabolism of 4-methylaminobutanoate produced from nicotine. Has a very weak monoamine oxidase activity with 4- aminobutanoate. Cannot use spermidine, spermine, sarcosine, dimethylglycine, glycine, choline, betaine, alpha-methylamino isobutyrate, methylamine propionitrile and methylamino propylamine as substrate. SIMILARITY: Belongs to the flavin monoamine oxidase family."}
+{"protein": "SGSCTTKTCWTMLPKFRELGYILKEKYNEAVQVEPVRTHRNKRPVFLKIKKPLSYRKPMVTDLVYIEKSPNYCEEDPITGSVGTQGRMCNKTSSQNNSCDLMCCGRGYNTHQYSRVWQCNCKF", "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. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MSQANKIYFEDRSIVTPGDLIAEGEFQVPWSPYYYKVNGKYYSAITGLITVKDGSIFEVIPLESSRYYPKVGDTIIGLVEDIEIYGWVIDIKSFYSAYLPASSLLGRPISPGEDVRRYLDVGDYVIAKIEAFDRTISPVLTVKGKGLGRIPLGTVMDIMPVKVPRVIGKNRSMIEVLTSESGCEIFVAQNGRIHIKCANNLIEEALIEAINIIQSESHTKGLTERIRNFLKQKLGVIRNDSAPKTEANT", "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": "MALKSLVVLPLLVLVLLLVRVQPSLGKESAAAKFERQHMDSGNSPSSSSNYCNLMMCCRKMTQGKCKPVNTFVHESLADVKAVCSQKKVTCKNGQTNCYQSKSTMRITDCRETGSSKYPNCAYKTTQVEKHIIVACGGKPSVPVHFDASV", "text": "FUNCTION: This enzyme hydrolyzes both single- and double-stranded RNA. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pancreatic ribonuclease family."}
+{"protein": "MASVKRVVVAVMIVNVLALIFVGVAGSTRDVGSGGDDSEGARGREQQQVQQHEQNEDRSLFERGRAAVTGHPVRTAVGLAAAVVAVVSLLRLLKRRRRRAIQEESKESATAEEEEVAEEE", "text": "FUNCTION: Plays a role in the function of the cyst and parasitophorous vacuole membranes and therefore in host-parasite interactions. SUBCELLULAR LOCATION: Secreted. Parasitophorous vacuole lumen. Parasitophorous vacuole membrane. Cytoplasmic vesicle, secretory vesicle. Note=Located in dense granules of tachyzoites. Upon infection, secreted into the cyst and the parasitophorous vacuole (PV)."}
+{"protein": "MEVISTNTNGSTIFKNGAIPMNGYQNGTSKHQNGHQNGTSEHRNGHQNGISEHQNGHQNGTSEHQNGHQNGTISHDNGNELQLLGSSNSIKPGWFSEFSALWPGEAFSLKVEKLLFQGKSDYQDVMLFESATYGKVLTLDGAIQHTENGGFPYTEMIVHLPLGSIPNPKKVLIIGGGIGFTLFEMLRYPTIEKIDIVEIDDVVVDVSRKFFPYLAANFSDPRVTLVLGDGAAFVKAAQAGYYDAIIVDSSDPIGPAKDLFERPFFEAVAKALRPGGVVCTQAESIWLHMHIIKQIIANCRQVFKGSVNYAWTTVPTYPTGVIGYMLCSTEGPEVDFKNPVNPIDKETTQVKSKLAPLKFYNSDIHKAAFILPSFARSMIES", "text": "FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'- nitrosonornicotine (NNN) (PubMed:10598105, PubMed:31276744, PubMed:34095742). Methyltransferase that mediates the conversion of putrescine to N-methylputrescine (PubMed:10598105). Promotes leaves ripening (PubMed:34095742). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Putrescine methyltransferase family."}
+{"protein": "MKLLGWMHRKLRQNSNDVFKEFNNAAGGTCNCITGLAASDPATFLATANEYFTADNDFTNNHPSSPAADLFTFGGSGLLTIGTLGIAAVAVSADADEVDYDVDADADSDFDDNDDTAGDDEDQVDSAVTPTFTYAAPPPIEDATVVEKAAVAVVEAIAEKDDDTTTEDDLMVVSAELEKVLGGRNSGTAGDLVASARVSFAMGVDCPLQGFLFGSPVSDAESRLEQPRDSNGGRRTSLGELFMRTRFAEEKVALVAVEEGEDGGDIGAGGERDDRKAGKGGGGHKTTKKRSAKDEKVPRGDGAQASATVTKSKFHKILQIFHRKVYPESAALARNLTKKSRKRGSGAYHKPEPAASKLRCLKEQRAPGFGCCASRASFGGAASPIDGDDDDELNGSKSGHWIKTDAEYLVLEL", "text": "FUNCTION: Involved in the regulation of shoot gravitropism, and tassel and ear development through the regulation of polar auxin transport (PAT) and auxin signaling. Acts as negative regulator of basipetal PAT, but positive regulator of lateral auxin transport (PubMed:24089437). Involved in the regulation of shoot gravitropism and leaf angle through the regulation of cell development (PubMed:24987012). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Nucleus. SIMILARITY: Belongs to the LAZY family."}
+{"protein": "MIIDRVQVEAINSFSNLELLKEVYGLIWILPILTLLLGITIEVLVIVWLEREISASIQQRIGPEYAGPLGLLQAIADGTKLLFKEDILPSRGDIPLFSIGPSIAVISILLSFLVIPLGYRFVLADLSIGVFLWIAISSIAPIGLLMAGYSSNNKYSFLGGLRAAAQSISYEIPLTFCVLAISLLSNSLSTVDIVEAQSKYGFFGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKYGLFYLVSYLNLLVSSLFVTVLYLGGWNLSIPYISFFGFFQMNKMVGILEMTMSIFITLTKAYLFLFISITIRWTLPRMRMDQLLNLGWKFLLPISLGNLLLTTSFQLVSL", "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. 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. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family. SIMILARITY: Belongs to the complex I subunit 1 family."}
+{"protein": "MARRFQEELAAFLFEYDTPRMVLVRNKKVGVIFRLIQLVVLVYVIGWVFLYEKGYQTSSGLISSVSVKLKGLAVTQLPGLGPQVWDVADYVFPAQGDNSFVVMTNFIVTPKQTQGYCAEHPEGGICKEDSGCTPGKAKRKAQGIRTGKCVAFNDTVKTCEIFGWCPVEVDDDIPRPALLREAENFTLFIKNSISFPRFKVNRRNLVEEVNAAHMKTCLFHKTLHPLCPVFQLGYVVQESGQNFSTLAEKGGVVGITIDWHCDLDWHVRHCRPIYEFHGLYEEKNLSPGFNFRFARHFVENGTNYRHLFKVFGIRFDILVDGKAGKFDIIPTMTTIGSGIGIFGVATVLCDLLLLHILPKRHYYKQKKFKYAEDMGPGAAERDLAATSSTLGLQENMRTS", "text": "FUNCTION: Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the P2X receptor family."}
+{"protein": "MSEQLVTPENVTTKDGKINLLDLNRQQMREFFKDLGEKPFRADQVMKWMYHYCCDNFDEMTDINKVLRGKLKEVAEIRAPEVVEEQRSSDGTIKWAIAVGDQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIVGAAKVTGQRPITNVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDEIRDEIVPINKKYNIETFLAAVRRYLEKSNANQGRVTIEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFSKVLMSYGFTTIVRKTRGDDIDAACGQLAGDVIDRTKRTLRKRMQGEAIDIKAV", "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. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family."}
+{"protein": "MPFVGGAESGDPLGAGRPIGDDECEQYTSSVSLARMLYGGDLAEWVPRVHPKTTIERQQHGPVTFPNASAPTARCVTVVRAPMGSGKTTALIRWLREAIHSPDTSVLVVSCRRSFTQTLATRFAESGLVDFVTYFSSTNYIMNDRPFHRLIVQVESLHRVGPNLLNNYDVLVLDEVMSTLGQLYSPTMQQLGRVDALMLRLLRICPRIIAMDATANAQLVDFLCGLRGEKNVHVVVGEYAMPGFSARRCLFLPRLGTELLQAALRPPGPPSGPSPDASPEARGATFFGELEARLGGGDNICIFSSTVSFAEIVARFCRQFTDRVLLLHSLTPLGDVTTWGQYRVVIYTTVVTVGLSFDPLHFDGMFAYVKPMNYGPDMVSVYQSLGRVRTLRKGELLIYMDGSGARSEPVFTPMLLNHVVSSCGQWPAQFSQVTNLLCRRFKGRCDASACDTSLGRGSRIYNKFRYKHYFERCTLACLSDSLNILHMLLTLNCIRVRFWGHDDTLTPKDFCLFLRGVHFDALRAQRDLRELRCRDPEASLPAQAAETEEVGLFVEKYLRSDVAPAEIVALMRNLNSLMGRTRFIYLALLEACLRVPMATRSSAIFRRIYDHYATGVIPTINVTGELELVALPPTLNVTPVWELLCLCSTMAARLHWDSAAGGSGRTFGPDDVLDLLTPHYDRYMQLVFELGHCNVTDGLLLSEEAVKRVADALSGCPPRGSVSETDHAVALFKIIWGELFGVQMAKSTQTFPGAGRVKNLTKQTIVGLLDAHHIDHSACRTHRQLYALLMAHKREFAGARFKLRVPAWGRCLRTHSSSANPNADIILEAALSELPTEAWPMMQGAVNFSTL", "text": "FUNCTION: Functions as a docking protein to recruit essential components of the viral replication machinery to viral DNA origins. In the presence of the major DNA-binding protein, opens dsDNA leading to a conformational change in the origin that facilitates DNA unwinding and subsequent replication. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae OriBP family."}
+{"protein": "MTLTTEKQVKVVVDRDVVPTSFEKWAKPGHFSRSLAKGPKTTTWIWNLHADAHDFDSHTSSLEEVSRKIFSAHFGQLAIIFIWLSGMYFHGARFSNYVAWLSNPTGIKPSAQVVWPIVGQQILNADVGGGMQGIQITSGLFQLWRASGIVNELQLYVTALGGLGMAGLMIFAGWFHYHKAAPKLEWFQNVESMLNHHLAGLLGLGSLSWAGHQIHVSLPINKLLDAGVAPSSIPLPHEFILNRNLMAELYPSFQQGLVPFFTLNWKQYSDILTFKGGLSPVTGGLWLTDVAHHHLAIAVLFLVAGHMYRTNWGIGHSIKQILEAHKGPLTGEGHKGLYEILTTSWHANLAINLAMLGSLSIIVAHHMYAMPPYPYLATDYPTQLSLFTHHMWIGGFCIVGAGAHAAIYMVRDYSPTVNFNNVLDRMIRHRDAIISHLNWVCIFLGMHSFGLYIHNDTMRALGRAQDMFSDTAIQLQPVFAQWIQQIHTLAPGNTAVNALATASYAFGADTVTVGSKIAMMPIKLGTADFMVHHIHAFTIHVTTLILLKGVLYARNSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNALSIVIFHFSWKMQSDVWGTVTSNGAISHITGGNFAQSAITINGWLRDFLWAQASQVIQSYGSSLSAYGLMFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIAPRALSITQGRAVGVAHYLLGGIATTWAFFLARIIAVG", "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: Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family."}
+{"protein": "MTSAQNESQALGDLAARQLANATKTVPQLSTITPRWLLHLLNWVPVEAGIYRVNRVVNPEQVAIKAEAGAGSEEPVPQTYVDYETSPREYTLRSISTLVDIHTRVSDLYSSPHDQIAQQLRLTIETIKERQELELINSPEYGLLAQATGRQTIQTLAGAPTPDDLDALITKVWKTPSFFLTHPLGIAAFGREATYRGVPPPVVSLFGPTQFITWHGIRLPSDKVPVEDGKTKFILVRTGEERQGVVGLFQPGLVGEQAPGLSVRFTGINQSAIATYLVTLYTSLAVLTDDALAVLDDVAVDQFHEYK", "text": "FUNCTION: Shell component of a type 2A encapsulin nanocompartment. Forms encapsulin nanocompartments about 24 nm in diameter from 60 monomers. Probably encapsulates at least cysteine desulfurase (CyD) and allows passage of cysteine into its interior, probably involved in sulfur metabolism. SUBCELLULAR LOCATION: Encapsulin nanocompartment. SIMILARITY: Belongs to the encapsulin family. Family 2A subfamily."}
+{"protein": "MEQDSDLESGRATNQRPPRVRVRGAGVRGRGRVRRRALSEGQRRSPFRLDDLQLPDSLYVTRALQRDHALEMPRGQVDFSLIEAEERRAGPTDEWYFESVKTYRAKPGDDLQTLIKNYAKISLECGAVYEINSKIVVTGACYIIGNCAVLRANLPVGTAMFEVLNVDVIPSIGFMERIVFSNILFDCRSTTAVVCCISERNTLFHNCVFSGPHMLCLDIRAGAEVRGCHFVGAVCALRSKGLYSVRVRNSIFEKCAFGVVSGSKASISHSMFKDCACCIMFGGQGTIAHSHFMATTCTDTPMNLQLCTCEGNGSHVVPLGNIHFASNREAPWPTFNANVLVRVRLYMGRRRGVFHPKQSTFSMCVIAAPRGVVQRIYLFSVYDATCAILQLGEAGDAATERLCTRGMRHNTPSLRAAYVTDTRIDREINSQDTAEFFSSDEDNL", "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": "MQKRRIITVNPSASIEMSQYENNEVPYSSVGADEVPSSPPKATDKIRKVSMLPLVFLIFYEVSGGPFGVEDSVNAAGPLLALLGFVIFPFIWSIPEALITAEMGTMYPENGGYVVWVSSALGPFWGFQQGWMKWLSGVIDNALYPVLFLDYLKSGVPALGSGLPRVASILVLTILLTYLNYRGLTIVGWVAVLMGVFSILPFAVMGLISIPQLEPSRWLVMDLGNVNWNLYLNTLFWNLNYWDSISTLAGEVENPNHTLPKALFYGVILVACSYIFPLLAGIGAIPLEREKWTDGYFSDVAKALGGAWLRWWVQAAAATSNMGMFIAEMSSDSFQLLGMAERGMLPEFFAKRSRYGTPLLGILFSASGVVLLSWLSFQEIVAAENLLYCVGMILEFIAFVRMRMKHPAASRPYKIPIGTTGSILMCIPPTILICAVVALSSLKVAAVSIVMMIIGFLIHPLLNHMDRKRWVKFSISSDLPDLQQQTREYEETLIR", "text": "FUNCTION: Probable cell membrane polyamine/proton symporter involved in the polyamine uptake in cells. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Polyamine:cation symporter (PHS) (TC 2.A.3.12) family."}
+{"protein": "MNDTVTIRTRKFMTNRLLQRKQMVVDVLHPGKATVPKTEIREKLAKMYKTTPDVVFVFGFRTQFGGGKTTGFAMVYDSLDYAKKNEPKHRLATHGLYEKKKTSRKQRTERQNRMKKVRSIKKASVGAAGKKN", "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 processing of pre-rRNA and maturation of 40S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS24 family."}
+{"protein": "MMRDSLGPFRTFTLLTVGLLLSLFVIKTVKHRRRYHGLPTPPHNMLLGNLGVVLAEILASPEGFFHLFCVENIRRKYNMPSVFYLDLWPILPSIMVVAEPVVAKHMTQVQPLQRERFSPNLFSPLLTAEFILAMEQKNWKKENPALNAALTSTRVNEATSLLFPSLHSLRSRLHSISQSGKQYPIKDLLISYIIEVGGVIQLGGSFDLLAETSALDPIIKQSLDMMGWNPVKRYICSKEIKQRTDCLNRVLVATVQNTVQTGESGMMSQSPIYLAHVEQLASGRMDHAESIAYLVNTMKVIILASVVTAGAASYCYLFLHKYPDCLREMREEHDRVFSPDRTQTWELLQKEPHRINSLHFTLAVVKETLRLIGVGGVFKKLKTEEFLETEGNVYPVVCNVAFICHLAMGRRADLFPDPDAFRPHRFLPGANPPIPADSFRPFEKGQLSCPGQTLALKSLVLLLLTTSREFDLVPVFPKGAPRAAEYLGGEGYPEFHIGPHVNKGMPVMVHTRVDA", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems (PubMed:25831977). The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (PubMed:25831977). Condensation of indole-3- glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (PubMed:25831977). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (PubMed:25831977). Paspaline is subsequently converted to 13- desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ (PubMed:25831977). Paxilline is converted to beta-paxitriol via C- 10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD (PubMed:25831977). A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine (PubMed:25831977). 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 ptmE (PubMed:25831977). Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A (PubMed:25831977). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MAPLFLLLLLLLSPSPTSAHRFAYSAPNRPEVRTTTGSVRGLLIPAGPSGSTAAAFLGIPFAVPPLGPLRFRPPLPIPTPWTGIRDADSQPFACYQMVDTTFPGFQGSEMWNPNREMSEDCLYLNVWTQKGDPTEPPVLVWIYGGGFTGGSVSLDVYDGRYLAAAEEAVVVSMNYRVGSLGFLALAGHRDAPGNVGLWDQRLALQWVRDNAEAFGGDPDLITLFGESAGAASVGFHLLSPHSKGLFRRAVLQSGSPNGPWATIGAAEGRRRAAALGRAVGCPYGNETEFLGCLRGKEAADVLEGEGVVMPPQSVFRFAFVPVVDGDFVVDSPDVALWGDYGVKGGEGGHGVEGGDGGYGVKGGDGVKGGYGGGYGARGVREGDGDGGYGVKEGLREGYGVKEGYGVEGDGANAYGARVPPRPHRDETPPDAYGAKGSADAYGAKAAPRPHRDETSPDAYGAKMPPRPHRDEASPDTYGAKMPPRPHRDETSPDAYGAKMPPRPHRAGGEVEVLLGAVRVEGSYFLVYGVPGFGKDNESLISREEFLGGVRMGVPQATELAAEAVVLHYTDWLDADNPVKNREALDDIVGDHNVVCPLMAFAQRWAQRGGKVYAYLFDHRSSTLLWPSWMGVPHGYEIEFVFGLPLEPRNNYTREEVELSRRIMRYWGNFARTGDPNGGVGGPRWPPYTPSGQRYAHLNARPLSVGHGLRTQICAFWTRFLPKLLNATGPPEDAEREWRLEFHRWSSYMGRWRTQFEHYSRQQPCATL", "text": "FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. SUBCELLULAR LOCATION: Synapse. Secreted. Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
+{"protein": "MNTSCEPILKPTLNKYVVFPIVYEDIWKMYKKAVASFWTVEEVDLSKDFSDWLKLSDNEKNFIKHILAFFAASDGIVNENLAERFYSEVQISEARCFYGFQIAMENIHSEMYSLLIDTYILDSKEKNYLFNAIENMNCVKQKANWAKKWIESKNRTYGERLVAFAAVEGIFFSGSFAAIFWIKKRGLMPGLTFSNELISRDEGLHCDFACIMFKHLLNPPLNSVVRDIIIEAVNIEKNFLTEAIPVKLIGMNCDLMKQYIEFVADRLLLELGCDKYYCSKNPFDFMENISLEGKTNFFEKRVSEYQKMSVMSNKKDNVFSLDIDF", "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": "MEAVLNELVSVEDLKNFERKFQSEQAAGSVSKSTQFEYAWCLVRSKYNDDIRRGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS", "text": "FUNCTION: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering (PubMed:15979461). Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission (By similarity). May not be essential for the assembly of functional fission complexes and the subsequent membrane scission event (By similarity). Also mediates peroxisomal fission (By similarity). May act when the products of fission are directed toward mitochondrial homeostasis, mitophagy, or apoptosis (By similarity). Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FIS1 family."}
+{"protein": "MKLFVFFVAAVVLVAWPCHGAGYQRFPLRMKTGYGERSSEVKCASFRLAVEAHNIRAFKTIPEECVEPTKDYINGEQFRSDSKTVNQQAFFYASEREVHHNDIFIFGIDNTVLSNIPYYEKHGYGVEEFNETLYDEWVNKGDAPALPETLKNYNKLLSLGFKIVFLSGRYLDKMAVTEANLKKAGFHTWEQLILKDPHLITPNALSYKSAMRENLLRQGYRIVGIIGDQWSDLLGDHRGESRTFKLPNPMYYIE", "text": "FUNCTION: May function as somatic storage protein during early seedling development. SIMILARITY: Belongs to the APS1/VSP family."}
+{"protein": "MAWTSVLLMLLAYLTGCGPQPMVHQPPLASSSLGATIRLSCTLSNDHNIGIYSIYWYQQRPGHPPRFLLRYFSHSDKHQGPDIPPRFSGSKDTTRNLGYLSISELQPEDEAVYYCAVGLRSQEKKRMEREWEGEKSYTDLGS", "text": "FUNCTION: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B- cell differentiation. SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the immunoglobulin superfamily."}
+{"protein": "MTVDALTQPHHLLSLAWNDTQQHGSWFAPLVTTSAGLLCLLLYLCSSGRRSDLPVFNPKTWWELTTMRAKRDFDANAPSWIESWFSQNDKPIRFIVDSGYCTILPSSMADEFRKMKELCMYKFLGTDFHSHLPGFDGFKEVTRDAHLITKVVMNQFQTQAPKYVKPLANEASGIITDIFGDSNEWHTVPVYNQCLDLVTRTVTFIMVGSKLAHNEEWLDIAKHHAVTMAIQARQLRLWPVILRPLVHWLEPQGAKLRAQVRRARQLLDPIIQERRAERDACRAKGIEPPRYVDSIQWFEDTAKGKWYDAAGAQLAMDFAGIYGTSDLLIGGLVDIVRHPHLLEPLRDEIRTVIGQGGWTPASLYKLKLLDSCLKESQRVKPVECATMRSYALQDVTFSNGTFIPKGELVAVAADRMSNPEVWPEPAKYDPYRYMRLREDPAKAFSAQLENTNGDHIGFGWHPRACPGRFFASKEIKMMLAYLLIRYDWKVVPDEPLQYYRHSFSVRIHPTTKLMMRRRDEDIRLPGSL", "text": "FUNCTION: Dihydromonacolin L monooxygenase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)- hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) (PubMed:10334994, PubMed:12929390, PubMed:21495633). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units (PubMed:10334994, PubMed:10381407, PubMed:19900898, PubMed:22733743). Dihydromonacolin L acid is released from lovB by the thioesterase lovG (PubMed:23653178). Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid (PubMed:12929390, PubMed:21495633). The 2- methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit (PubMed:19530726, PubMed:21069965). Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin (PubMed:10334994, PubMed:17113998, PubMed:18988191, PubMed:19875080, PubMed:24727900). LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3- mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro (PubMed:19875080). LovD has much higher activity with LovF-bound 2- methylbutanoate than with free diketide substrates (PubMed:21069965). SUBCELLULAR LOCATION: Membrane; Single- pass membrane protein Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MSEQVRHVLTLQCPEGIGIVHAVTGFLVRHQRTIVELKQYDDMSAGRLFLRVDFAGDSAPDLLDALRSEFSEVAAKFDMDWQLRERGQKTKVLIMVSKFEHCLQDLLFRMHSGDLPIEVVGVASNHPDHRSLVEWYGIGFHHIPISKDTKPRAEAALLELIDQTGAELVVLARYMQVLSDHLASELTGKTINIHHSFLPSFKGAKPYHQAWERGVKTVGATAHYVNSELDEGPIIAQQVVEVDHTYGPQDLVAAGRDSECKALSNAVRWHCEGRVFLYGNRTVVLR", "text": "FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). SIMILARITY: Belongs to the PurU family."}
+{"protein": "MGNLLGGVSFREPTTVEDCDSTWQTDSEPEPEEPGPGGGSEGPGQESEQPAQPPEQAGGRPGASPAPDEDAEAAGAEQGGDSTEATAKPKRSFYAARDLYKYRHQYPNFKDIRYQNDLSNLRFYKNKIPFKPDGVYIEEVLSKWKGDYEKLEHNHTYIQWLFPLREQGLNFYAKELTTYEIEEFKKTKEAIRRFLLAYKMMLEFFGIKLTDKTGNVARAVNWQERFQHLNESQHNYLRITRILKSLGELGYESFKSPLVKFILHEALVENTIPNIKQSALEYFVYTIRDRRERRKLLRFAQKHYTPSENFIWGPPRKEQSEGSKAQKMSSPLASSHNSQTSMHKKAKDSKNSSSAVHLNSKTAEDKKVAPKEPVEETDRPSPEPSNEAAKPRNTEKDSNAENMNSQPEKTVTTPTEKKESVSPENNEEGGNDNQDNENPGNTNCHDVVLVQ", "text": "SIMILARITY: Belongs to the opioid growth factor receptor family."}
+{"protein": "MAQDAITAVINSADVQGKYLDTAALEKLKAYFSTGELRVRAATTISANAAAIVKEAVAKSLLYSDITRPGGNMYTTRRYAACIRDLDYYLRYATYAMLAGDPSILDERVLNGLKETYNSLGVPVGATVQAIQAIKEVTASLVGADAGKEMGIYLDYISSGLS", "text": "FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 to 653 nanometers. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=Forms the core of the phycobilisome. SIMILARITY: Belongs to the phycobiliprotein family."}
+{"protein": "MNKLTERVLCVGVSGLILFSVAALVQGTKKCYANPVRNRAASRVKPYADSFKEFTNIDEARAWGDKQFAKYKLSSSEKNALTIYTRNAARINGPLRANQGNTNGLPADIRKEVEQIDKSFTKMQTPENIILFRGDDPGYLGPDFENTILNRDGTINKAVFEQVKLRFKGKDRKEYGYISTSLVNGSAFAGRPIITKFKVLDGSKAGYIEPISTFKGQLEVLLPRSSTYTISDMQIAPNNKQIIITALLKR", "text": "FUNCTION: ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: To C.botulinum D and C phages exoenzyme C3, and to S.aureus EdiN."}
+{"protein": "MQNAPKCYLPNSRKGRDVNFHDRGPETLKCLYDESEDNNNFTMHSESIGPKSLDSLSPRRLSNYSSAVDPRTTSLEDVPRLILTRSNSQEQTPLRTHTPVEYMSDSIHKSLADLQLGGSSYSVAESPVPVLQSSAVSEADDMASAHSAHPSRKASRSLRLFESSTSNNLETGNSTNTALHNVSSPLESVSERLSKSGSPSVGAQHDLDEVISEKDTSLSRRSSRGRSSAPKRRKDSGSSKTTATYIPHNPSKKSSQHLPLLPDASFELERSVSRSYQSPASTPRSSVSSVSSSPPEDHPFFHWNVDYPVTVRLEPFKHQVGGHTAFFRFSKRAVCKPLTRNENTFYETIEACHPELLPFIPKYIGVLNVTHTITKTEENDSTTEYVNTESSSKTPAPHKHTFNSCYQKKDYGYIPEVSVEQNRHIFPEWMLPDKRSHSYGSPKSLHHKSSSAGERPVSPTFVADIPPKTPWGTTLINRKLREEVLREVFAPKHARRRLGTRFHSRSSHRPSVFRDNSVAFGQLDNGNTSSRARDKDADPNKSLSCSVEDKHYDLHSAVAEENEEVDEELLNVPSNNQGKSYRRFSSDAVWEEPESNEFPRVSGTMEDYDSRESTGHTIKELRSTPNSHGTVPDDSIFAMDNEENSELPPPLEPAEIGDPFRSVNDPRRVLSLPHMASADEDHRIPASDNQNNNNNDANALAENSESQHSTQIERYIVIEDLTSGMKRPCVLDVKMGTRQYGIMATEKKKASQTKKCAMTTSRVLGVRICGMQVWHPWLQSYTFEDKYVGRDIKAGEEFQHALMRYLGKTDDDEDNSHLLVHHIPTIIRKLEQLEQIVRFLKGSRLYASSLLFLYDGEPPPSDKSSKEKVKPREIDIRIVDFANCVFAEDKELLAKATCPPQHKDTYDRGYVRGLRTLRLYFLKIWKEAKGMQIAERGYEDSLSNAYDELGGLMSYSNDDDSCGETST", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family."}
+{"protein": "MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGSAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQTSASESLSNSGVSSGDIDSSQIITNPLPPVASPPPASKAKEVSDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSETGPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK", "text": "FUNCTION: Catalytic 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. As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes (By similarity). SUBCELLULAR LOCATION: Midbody Late endosome Cytoplasmic vesicle, autophagosome Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes (By similarity). Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (PubMed:24089209). SIMILARITY: Belongs to the PI3/PI4-kinase family."}
+{"protein": "MQKTSNTLALGSLTALFFLMGFITVLNDILIPHLKPIFDLTYFEASLIQFCFFGAYFIMGGVFGNVISKIGYPFGVVLGFVITASGCALFYPAAHFGSYGFFLGALFILASGIVCLQTAGNPFVTLLSKGKEARNLVLVQAFNSLGTTLGPIFGSLLIFSATKTSDNLSLIDKLADAKSVQMPYLGLAVFSLLLALVMYLLKLPDVEKEMPKETTQKSLFSHKHFVFGALGIFFYVGGEVAIGSFLVLSFEKLLNLDAQSSAHYLVYYWGGAMVGRFLGSALMNKIAPNKYLAFNALSSIILIALAILIGGKIALFALTFVGFFNSIMFPTIFSLATLNLGHLTSKASGVISMAIVGGALIPPIQGVVTDMLTATESNLLYAYSVPLLCYFYILFFALKGYKQEENS", "text": "FUNCTION: Intake of glucose and galactose. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. FHS transporter (TC 2.A.1.7) family."}
+{"protein": "MFSTTSIVLWFTILLPVTLPVSIDNRDLLLKRHVEPNDIQFFNQGVRSSLSYIYQKRDVSDSDNEQVLRKSKKKKKTTSTGTPGNENTTDFASAQEFEKWEGDREGWQISAGLYFDKAIASDSCDSDSEDEDEGRKKFWIFTDDAPVDNENLIVSSEDKLELNYISSGKNLEGLTKVIRKAKGNSTTYNQSKIKFNVDAQGEDQFESGFGSLIPYNSFYLYILLFCIIF", "text": "FUNCTION: Predicted GPI-anchored protein which may have a role during host infection. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor."}
+{"protein": "MEWSLTQNKLLAFHRLMRTDKPIGALLLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAGALFVYQQKLIANREREACFKAFMNNNYVGLVLFLGLAMSYWHF", "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. 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 (PubMed:4552989). Geranyldiphosphate (GPP), all-trans- farnesyldiphosphate (FPP) and all-trans-solanesyldiphosphate (SPP) are also accepted as side chain precursors (PubMed:8155731). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. SIMILARITY: Belongs to the UbiA prenyltransferase family."}
+{"protein": "MPVVKMLKQVASRTLGSPACGCQPPTLPRRFLGTSPRQIPADANFHSTSFSEANQPRVLITGGLGQLGVGLASLLRKRFGKDNVILSDIRKPPEHVFLSGPFIYSDILDYKNLREIVVNNRVTWLFHYSALLSAVGEANVSLARAVNITGLHNVLDVAAEHGLRLFVPSTIGAFGPTSPRNPTPDLCIQRPRTIYGVSKVHAELMGEYYYYRYGLDFRCLRYPGIISADSQPGGGTTDYAVQIFQDAVKNGRFECNLNPGTKLPMMYIDDCLRATLEVMEAPAEALSLRTYNVNAMSFTPAELAQEVLKHIPEFQITYNVDSVRQAIADSWPMNFDDSTARRDWGWKHDFDLPELVTTMLNFHGAHSRVAQAN", "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": "MTYLLNSPDDFADEAVRGLVAANPDLLTEVPGGVVRSTETPKGQPALVIGGGSGHYPAFAGWVGPGMGHGAPCGNIFSSPSASEVYSVVRNAENGGGVILGFGNYAGDVLHFGLAAEKLRHEGIDVRIVTVSDDIASNSPENHRDRRGVAGDLPVFKIAGAAIEAGADLDEAERVAWKANDATRSFGLAFEGCTLPGATEPLFHVEKGWMGVGLGIHGEPGVRDNRLGTAAEVADMLFDEVTAEEPPRGENGYDGRVAVILNGLGTVKYEELFVVYGRIAERLAQQGFTVVRPEVGEFVTSLDMAGVSLTMVFLDDELERLWTAPVETPAYRRGAMPAVDRTPRTTTWDAAETTIPEASEGSRECARNIVAVLETFQQVCADNEAELGRIDAVAGDGDHGQGMSFGSRGAAQAARDAVDRNAGARTTLLLAGQAWADAAGGTSGALWGAALTSAGGVFSDTDGADEQAAVDAICAGIDAILRLGGAQPGDKTMVDAAVPFRDALVKAFDTQAGPAITSAARVAREAAEKTADITARRGRARVLGEKSVGTPDPGALSFAMLMKALGEHLTR", "text": "FUNCTION: Kinase that has a preference for L-erythrulose, producing L- erythrulose-1P. Involved in the degradation pathway of L-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Is also able to phosphorylate D-erythrulose and dihydroxyacetone in vitro."}
+{"protein": "MYVSSLLFLYASESYESFIFHFQMCYNKAHNGFMPSIFQQLKGLGEGLQWKVGISLDHQEKQTSSHEKEMTSPNSATRLIPSDWRRELLAGTVSFFAAVYIIIVNSSILADAGIPQEAGIIATILASAIGCFIMGLWGNAPLVIVPGMGINAMFTYTLVQGMGLTWQQALAAVMMSGICFFAISMTSLVEKLRTAIPASLQEAISVGIGLMLVLIGLHKGGVIASDRSSVIAVQSFADPGVLVTLATLALTCILYIRKVPGNLLLAIIGGSALAYLFKAVPSKAATGVGGSSWSSYGDLFGQLSVKGASITTLVIAVFSLTLVIVFENVGLINAQLKMSGRTERFKRVTQATSLTVILSGIFGTSPTVSTVEAAAGISAGGRTGWASIATGTLFLLSFIAMPVITLVPDQAVAPILIFIGGLMMPAVRHISFERMEEGLPAFFIIAFIPLMHSIVDGIAIGFISYALFHIAVGKWREVKPLFYIISLLFVMHFVLQTM", "text": "FUNCTION: Transports adenine, guanine, hypoxanthine, xanthine, cytosine and uracil. Transport is probably proton-dependent. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily."}
+{"protein": "MEDIKDSKVKRFCSKNILIILGFSSVLAVIALIAVGLTHNKPLPENVKYGIVLDAGSSHTNLYIYKWPAEKENDTGVVQLLEECQVKGPGISKYAQKTDEIAAYLAECMKMSTERIPASKQHQTPVYLGATAGMRLLRMESKQSADEVLAAVSRSLKSYPFDFQGAKIITGQEEGAYGWITINYLLGRFTQEQSWLNFISDSQKQATFGALDLGGSSTQVTFVPLNQTLEAPETSLQFRLYGTDYTVYTHSFLCYGKDQALWQKLAQDIQVSSGGILKDPCFYPGYKKVVNVSELYGTPCTKRFEKKLPFNQFQVQGTGDYEQCHQSILKFFNNSHCPYSQCAFNGVFLPPLQGSFGAFSAFYFVMDFFKKMANDSVSSQEKMTEITKNFCSKPWEEVKASYPTVKEKYLSEYCFSGTYILSLLLQGYNFTGTSWDQIHFMGKIKDSNAGWTLGYMLNLTNMIPAEQPLSPPLPHSTYISLMVLFSLVLVAMVITGLFIFSKPSYFWKEAV", "text": "FUNCTION: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GDA1/CD39 NTPase family."}
+{"protein": "MMELITELFDEDTTLPITNLNPKKKIPQIFSVHVDDAIEQPGFRLCTYTSGGDTNRDLKMGDKMMHIVPFTLTAKGSIAKLKGLGPSPINYINSVFTVAMQTMRQYKIDACMLRILKSKTAGQARQIQVIADRLIRSRSGGRYVLLKELWDYDKKYAYILIHRKNVSLEDIPGVPEISTELFTKVESKVGDVYINKDTGAQVTKNEAIAASIAQENDKRTDQAVIVKVKISRRAIAQSQSLESSRFESELFQKYESTAANFNKPATAPLIPEAEEMKIGINSLASKTKAAKIIAEGTANELHYDYKFFSKSEVDEVSEKIKDVIFNAIKNEPTTSIKCLEKYAAAVNQFFEEYKDNWLDKHNKTRKGQPDEVWGEITKNAWNAAKTKFLKRMIYSFSGIGAGPMIDITIACDGSKYTPSQKRGIREYCGSGYTDINNLLLGRYNPERYDVMSEKEIESAINNLDSAFENGDRIPEGITVYRAQSMTAPIYEALVKNKVFYFRNFVSTSLTPIIFGRFGITHAGIGLLEPEARNELTVDKNEEGITINPNEIRAYKENPEYVKVQIGWAIDGAHKVNVVYPGSLGIATEAEVILPRGLMVKVNKITDASNNDGTTSNNTKLIQAEVMTTEELTESVIYDGDRLMETGEVVAMTGDIEIEDRVDFASFVSSNVKQKVESSLGIIASCIDITNMPYKFVQG", "text": "FUNCTION: ADP-ribosyltransferase that efficiently ADP-ribosylates one of the two alpha subunits of host RNA polymerase RPOA on an arginine located in the C-terminal region. ADP-ribosylation of RPOA alpha subunit enhances the transcription of viral early genes. Also ribosylates RPOA subunits beta, beta' and sigma 70 and performs an autoribosylation reaction. SUBCELLULAR LOCATION: Virion Note=About 25-50 copies per virion. This protein is injected into the bacterial cell along with the viral DNA. SIMILARITY: Belongs to the Tevenvirinae NAD(+)--arginine ADP- ribosyltransferase family."}
+{"protein": "MGASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLALGIGTLIYGHWSMMKWNRERRRLQIEDFEARIALLPLLQAETDRRTLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVAPLIGELYGLRTTEEALHASHGFMWYA", "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. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side Nucleus Note=Localizes mainly in the mitochondrion. May be translocated into the nucleus upon IFN/RA treatment. SIMILARITY: Belongs to the complex I NDUFA13 subunit family."}
+{"protein": "MAAAGAAVARSPGIGAGPALRARRSPPPRAARLPRLLVLLAAAAVGPGAGGAARLYRAGEDAVWVLDSGSVRGATANSSAAWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYPTFRYFKAFTKEFTTGENFKGPDRELRTVRQTMIDFLQNHTEGSRPPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTRALDGDKAFLEKLGVSSVPSCYLIYPNGSHGLINVVKPLRAFFSSYLKSLPDVRKKSLPLPEKPHKEENSEIVVWREFDKSKLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDLVNNKMRISGIFLTNHIKWVGCQGSRSELRGYPCSLWKLFHTLTVEASTHPDALVGTGFEDDPQAVLQTMRRYVHTFFGCKECGEHFEEMAKESMDSVKTPDQAILWLWKKHNMVNGRLAGHLSEDPRFPKLQWPTPDLCPACHEEIKGLASWDEGHVLTFLKQHYGRDNLLDTYSADQGDSSEGGTLARGEEEEKRLTPPEVSHGDRDTQSVRPPGALGPRPALPESLHHSLDGKLQSLDGPGAHKEVGGAAPFLGVDFSSLDMSLCVVLYVASSLFLMVMYFFFRVRSRRWKVKHHHPAV", "text": "FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosis. SUBCELLULAR LOCATION: Membrane; Single- pass membrane protein Secreted Cell membrane; Single-pass membrane protein Nucleus membrane; Single- pass membrane protein Note=Seems to be predominantly targeted to the nuclear and outer plasma membrane. SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family."}
+{"protein": "MIITQMWHFYVTRVVLLLLISILPGTTSQGESRRQEPGDFVKQDIGGLSPKHAPDIPDDSTDNITIFTRILDRLLDGYDNRLRPGLGDAVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQTWHDERLKFDGPMKILPLNNLLASKIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTLLYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAYTKAEVIYSWTLGKNKSVEVAQDGSRLNQYDLLGHVVGTEIIRSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRSWAWEGKKVPEALEMKKKTPAAPTKKNTTFNIVGTTYPINLAKDTEFSTISKSAAAPSASSTPTAIASPKATYVQDSPAETKTYNSVSKVDKISRIIFPVLFAIFNLVYWATYVNRESAIKGMIRKQ", "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. GABRA3 sub- subfamily."}
+{"protein": "MSFKDKDERISCLEAYVTLTSKSSRFTDETEILKMSQRHSGQAGTEAGNGADSPPIVNSKYSTFRDFCSTSSFQDSGYNELKSCSFDNIDKEYLGKKEKGPTLLYEHPETSGLGLTHPLESPTQKKKCILPRKEKDKTPELCETPKISGKKCLPRRRLNVSFALLKGDFESQNSSLESSISQVINLEKNIPSSASGFSRANNFSPLVTSTLKTEEVTSCSQKLRLNFSQQKTSTIDDSKDDCSLFEVECISPIQGNNFKDSITHDFSDSSLCINDENACPELLGSSVSGTTCGTDEDIFVTPISNLVANIRFNASQILSPSPEVRGSISTPEDSGFNSLSLEKSEDSLSDQEGSFQELLQKHKGTPKVGDTIRKTRHLGRSRRLSTLREQSSQSETEEEKQIVHPDSEKRAAAASAISEGQLSSDESGDLTFSLKNLSKTPALQLVHELFMKSKRKRLQENSGHEFLEQGDGEKIAVLQCILAGLIGKKMGIEKLDILTELKYRNLKHILAMVLESLTAESLCSVWKVSRNWREIVVQDKNANRRRKFYITQLKTDSEGAVLNVEDAATRLQLLNRSALRSVQAQARIPGSQREQGSTLSPWGEVLTPLASSSVTHLSSKQEEYVKVAKTLFTDEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECSRGAAKPRNRKDALPGSAQSKRNLKRL", "text": "FUNCTION: Required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. Acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation (PubMed:34052850, PubMed:34595750). Plays a vital role in modulating the ubiquitilation of CCNB1 and CDK1 during gametogenesis."}
+{"protein": "MEQQSYTIIDETGIHARPATMLVQTASKFDSDIQLEYNGKKVNLKSIMGVMSLGVGKDAEITIYADGSDEADAIQAITDVLSKEGLTE", "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": "MASAQSFYNQSSVLKINVMVVDDDHVFLDIMSRMLQHSKYRVIAVDDPKKALSTLKIQRDNIDLIITDYYMPGMNGLQLKKQITQEFGNLPVLVMSSDTNKEEESLSCGAMGFIPKPIHPTDLTKIYQFALSNKRNGKSTLSTEQNHKDADVSVPQQITLVPEQADVLKTKRKNCSFKSDSRTVNSTNGSCVSTDGSRKNRKRKPNGGPSDDGESMSQPAKKKKIQWTDSLHDLFLQAIRHIGLDKAVPKKILAFMSVPYLTRENVASHLQKYRIFLRRVAEQGLYSMLSDRGIDSMFRQTHIKEPYFNYYTPSTSWYDTRLNNRSFYSKPVHGFGQSKLLSTTREPVCFNQMPYNYMNRSSTYEPHRIGSGSNLTLPIQSNLSFPNQPSQNEERRSFFEPPVMANKIAQTSQVLGFGQLGPSAISGHNFNNNMTSRYGSLIPSQPGPSHFSYGMQSFLNNENVTYNPQPPANATTQPNLDELPQLENLNLYNDFGNTSELPYNISNFQFDDNKHQQGEADPTKFELPAAKFSTELNHEDDGDWTFVNINQGQSNGETSNTIASPETNTPILNINHNQNQGQDVPEFNDWSFLDPQELVDDDFMNSLFNNDMN", "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": "MQTTQRASSFAAAEDNIAMDKAVVYTRIPHLYLWLEILNILSSRPLTGYAQHTSLPEVVIPLRVTGNRPMWAMGWLTYSLHFGGQKHFIHIKAKKFLVSRLFSVFTYTKQGALHKDQPYVQNDCYYHGHMDGDPESMVAITTCYGGFQGILQINGTVYEIKPKNLSSTFEHLVHKMDSEETELLPMRCALTEEIARQMKLQQNENPTLMQSHYEGWWTHKSFLDLALVVERERIRYHNNNTSRVLVEVFTIINIINNIYETLDVELVLLGVEMWNERNHVQVRSIEELLDEFCMWKARSLNFRIPNDIAHIFVNHEFGIYLGLAYIGSVCVPSHNCGVDRLLGGNLFYFGRIIAHEMGHNLGMEHDSSSCTCGTKICLMAPADNGIPKFSNCSYSYYWATYATAKCMRKEKKSKGILRGKLCGDGVVDDGEQCDCGSAKSCADDPCCKPSCTLKDGAACAFGLCCLYCQIMPAGTVCRQEVNECDLPEWCNGHSHKCPNDVYLLDGSPCRDGGYCYEKRCNNRDEQCKQIFGKEARSADHSCYRELNTQGDRFGNCGVIRDAYLRCHDPDILCGRVQCENVAHIPFLRDHSTVHWTHLNGVTCWGTDYHFGMTIPDIGIVKDGTDCGPEHVCINKKCVSKSIWRSQCSPKTCNMKGVCNNLHHCHCNLGWDPPHCLKSGLGGSIDSGPPNYTENYTEKKHKKSIGLVILFWILFACFSVLFIVFLFFLRSYVELPMSEEPKVPTPENKEDTNEVMNTETE", "text": "FUNCTION: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MNDRFRRELQVIEEQGLTRKLRLFSTGNESEVVMNGKKFLLFSSNNYLGLATDSRLKKKATEGISKYGTGAGGSRLTTGNFDIHEQLESEIADFKKTEAAIVFSSGYLANVGVISSVMKAGDTIFSDAWNHASIIDGCRLSKAKTIVYEHADMVDLERKLRQSHGDGLKFIVTDGVFSMDGDIAPLPKIVELAKEYKAYIMIDDAHATGVLGNDGCGTADYFGLKDEIDFTVGTLSKAIGAEGGFVSTSSIAKNYLLNNARSFIFQTALSPSAIEAAREGISIIQNEPERRKQLLKNAQYLRLKLEESGFVMKEGETPIISLIIGGSHEAMQFSAKLLDEGVFIPAIRPPTVPKGSSRLRITVMATHTIEQLDMVISKIKKIGKEMGIV", "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 (By similarity). Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily."}
+{"protein": "MSKSKIGEDVYKKVDKVNAELFVLTYGSIVAQLCKDMNYEKVNEELDKMGYNIGIRLIEDFLAKTEWPRCADFRETGETVAKVGFKVFLNFSPIISSVSDDGNTFVLTLDDNPLAEFVELPADARQKLWYSNILCGVIRGALEMLQMDVDAVFLRDILRGDEHTEIRVHLKRILKEEIPPGDE", "text": "SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus, cis-Golgi network Endoplasmic reticulum. SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily."}
+{"protein": "MLLLLGLCLGLSQCVGSQEEAQSWGHSSEQDGLRVPRQVRLLQRLKTKPLMTEFSVKSTIISRYAFTTVSCRMLNRASEDQDVEFQMQIPAAAFITNFTMLIGEKVYQGEITEREKKSGDRVKEKRNKTTEENGEKGTEIFRASAVIPSKDKAAFFLSYEELLQRRLGKYEHSISVRPQQLSGRLSVDVNILESAGIASLEVLPLRNSRQRGSGRGEDDSGPPPSTVINQNETFANIIFKPTVVQQARIAQNGILGDFIIRYDVNREQSIGDIQVLNGYFVHYFAPKDLPPLPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDHFSIIGFSNRIKVWKDHFDISHSRQHQGWQSVHSPYVAHWRHRHQRGLAEGHQAPQQVRGPQWHWRPERVPHCLPDGWEAHGRGDAHPQDPQQHPRGRPRPSLHLHIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIGFYDEIRTPLLSDIRIDYPPSSVVQATKTLFPNYFNGSEIIIAGKLVDRKLDHLHVEVTASNSKKFVIPKTDVPVGPQKAGKDVTGSPRPGGDGERNPNHIERLWSYLTTKELLSSWLQSDDEPEKERLRQRAQALAVSYRFLTPFTSMKLRGPVPRTDGLKEAHGMSAAMGPEPVVQSVRGAGTQPGPLLKKPYQPRIKISKTSVDGDPHFVVDFPLSKLTVCFNIDGQPGDILRLVSDHMDSGVTVNGELIGAPPNGHKKQRTYFRTITILINKPERSYLEITPSRVILDGGDRLVLPCNQSVVVGSRGLEVSVSANANVTVTIQGSIAFVIPIHLYKKPAPFQRHHLGFYIANSEGLSSNCHGLLGQFLNQDARLTEDPAGPSQNLTHSLLLQVGEGPEAVLTVKGRQVPVVWKQRKIYNGEEQIDCWFARNNAAKLIDGEYKDYLASHPFDTGMTLGRGMSREL", "text": "FUNCTION: May act as a tumor suppressor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ITIH family."}
+{"protein": "MVHIFTSILLGLLLLATGTRAQFQFFEQMFGGGQQQQQHDSREQNVPSDSDWYQRTYDNARCSNYLCPGTLACVAVPHHCPCQHPAVEDKFELGDGSAICVSKGGFKFGEAARKVELARKGLL", "text": "FUNCTION: Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway. SIMILARITY: Belongs to the LCL2 family."}
+{"protein": "MSLTKKIKNEKSLKQEKQTDQLKSNLRNNNNNINNKSKPKDQNLNTLHYIKTHLKEELFFIFCVGGIYIFYLLYGLVQEQLNVTKFGTEKKVFGFTAFLLALQCFFNMVSAWLVSLVNKEQKDNTPFMKYGFVSMLLVISTFLSNQSIRYISYPTQVLAKSCKPIPVIFMGLLLFKKKYPFLKYIVVIVISLGISLFMLPKATSKKNIQFEGHDHLFGNFILFVSLMMDGVMGPFQDNLVRQYKPSATSMMLNTNIWNLGLFSIMAFARGEVSQAIDFILEYPEVIKLILAFCITSAIGQQFIFLTTNKFGSLNCSTITTTRKFFSILVSIFYFGHSLDNLQWAAICMVFGGLILDLYISYSNKKKGVVLSPIAAPVKHPTATTPLENKKSL", "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": "MLVLTQPFLLMPRKLWVSSALRSDDQKQPPFSSSSTHAETPEHAEEQYQQQQSPPRYTDQAGEESEDYESEEQLQQRILTAALQFVPDFGWSADAIAEGAKSLDMSAAAGGMFEDGGSELVLHFVTQCNLQLTELLEKEHKLVQLGTSEKKPTAQFLRDAVKARLRMHIPYIEQWPQALGMLLLPRNIPSSLKLLSAMVDDMWHYAGDQSTDVSWYTSRAVLTGIYNSTELVMLQDSSPDFEDTWKFLENRISEAMTMGNSMKQVASTGEAVIQGLMGAAVTLKNLTGLNQRR", "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. Binds a phospholipid of at least 10 carbons in each acyl group. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the COQ9 family."}
+{"protein": "MLRYPYFYRTYNRLFSHFVDSGASNLDVCPHTIHTAVALHTESKAVEGTALCGPQKVYSSEEKELEAMAKLHIPVMVDQVVHCLAPQKGQVFLDMTFGSGGHTRAILQKEPDVMVYALDRDPVAYAIAEQLSRLYPTQIQALLGQFSQAEALLMKAGVQPGTIDGILMDLGCSSMQLDAPERGFSLRKDGPLDMRMDGDRYPDTPTASDVVNALDQQALASILRAYGEEKHAKKIASAIIQARSTYPISRTQQLASIVAGAFPPSAVYARKDLLQRSTHIATKTFQALRIFVNNELNELYAGLRTAEKFLKTGGRLVALSFHSLEDRIVKRFLLGISMTERFNLSIRQKVKQTSQLDSDQETEERHSVRAPLKWELIHKKVLTPEDQDVQDNPRGRSAKLRAAIKL", "text": "FUNCTION: N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA. Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family."}
+{"protein": "MESLCGVLVFLLLAAGLPLQAAKRFRDVLGHEQYPDHMRENNQLRGWSSDENEWDEQLYPVWRRGEGRWKDSWEGGRVQAALTSDSPALVGSNITFVVNLVFPRCQKEDANGNIVYERNCRSDLELASDPYVYNWTTGADDEDWEDSTSQGQHLRFPDGKPFPRPHGRKKWNFVYVFHTLGQYFQKLGRCSARVSINTVNLTVGPQVMEVIVFRRHGRAYIPISKVKDVYVITDQIPIFVTMYQKNDRNSSDETFLRDLPIFFDVLIHDPSHFLNYSAISYKWNFGDNTGLFVSNNHTLNHTYVLNGTFNFNLTVQTAVPGPCPSPTPSPSSSTSPSPASSPSPTLSTPSPSLMPTGHKSMELSDISNENCRINRYGYFRATITIVDGILEVNIIQVADVPIPTPQPDNSLMDFIVTCKGATPTEACTIISDPTCQIAQNRVCSPVAVDELCLLSVRRAFNGSGTYCVNFTLGDDASLALTSALISIPGKDLGSPLRTVNGVLISIGCLAMFVTMVTILLYKKHKTYKPIGNCTRNVVKGKGLSVFLSHAKAPFSRGDREKDPLLQDKPWML", "text": "FUNCTION: Could be a melanogenic enzyme. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Melanosome membrane; Single- pass type I membrane protein Early endosome membrane; Single-pass type I membrane protein Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the PMEL/NMB family."}
+{"protein": "MADAGIPDEILYSDISDDEIIIDGDGDSSGDEDDDDGGLTRQAAARIVTDLGFEVLQPLQSGSEGRVFVARRPGEADTVVLKVGQKPSTLMEGMLLQRLSHDNVMRMKQMLARGPATCLVLPHFRCDLYSYLTMRDGPLDMRDAGCVIRAVLRGLAYLHGMRIMHRDVKAENIFLEDVDTVCLGDLGAARCNVAAPNFYGLAGTIETNAPEVLARDRYDTKVDVWGAGVVLFETLAYPKTITGGDEPAINGEMHLIDLIRALGVHPEEFPPDTRLRSEFVRYAGTHRQPYTQYARVARLGLPETGAFLIYKMLTFDPVRRPSADEILNFGMWTV", "text": "FUNCTION: Able to phosphorylate in vitro the major virion phosphoprotein phosphorylated in vivo. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MTKSEKIIELTNHYGAHNYLPLPIVISEAEGVWVKDPEGNKYMDMLSAYSAVNQGHRHPKIIQALKDQADKVTLVSRAFHSDNLGEWYEKICKLAGKDKALPMNTGAEAVETALKAARRWAYDVKGIEPNKAEIIAFNGNFHGRTMAPVSLSSEAEYQRGYGPLLDGFRKVDFGDVDALKAAINENTAAVLVEPIQGEAGINIPPEGYLKAIRELCDEHNVLFIADEIQAGLGRSGKLFATDWDNVKPDVYILGKALGGGVFPISVVLADKEVLDVFTPGSHGSTFGGNPLACAASIAALDVIVDEDLPGRSLELGDYFKEQLKQIDHPSIKEVRGRGLFIGVELNESARPYCEALKEEGLLCKETHDTVIRFAPPLIITKEELDLALEKIRHVFQ", "text": "FUNCTION: Catalyzes the interconversion of ornithine to glutamate semialdehyde. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. OAT subfamily."}
+{"protein": "MRLPIFLDTDPGIDDAVAIAAAIFTPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNVDIPLAQGAAVPLVRAPRDAASVHGESGMAGYDFVEHNRKPLGIPAFLAIRDALMRAPEPVTLVAIGPLTNIALLLSQCPECKPYIRRLVIMGGSAGRGNCTPNAEFNIAADPEAASCVFRSGIEIVMCGLDVTNQAILTPDYLATLPELNRTGKMLHALFSHYRSGSMQSGLRMHDLCAIAWLVRPELFTLKPCFVAVETQGEFTSGTTVVDIDGCLGKPANVKVALDLNVKGFQQWVAEVLALVP", "text": "FUNCTION: Hydrolyzes both purine and pyrimidine ribonucleosides with a broad-substrate specificity. SIMILARITY: Belongs to the IUNH family. RihC subfamily."}
+{"protein": "MANPGGGAVCNGKLHNHKKQSNGSQSRNCTKNGIVKEAQQNGKPHFYDKLIVESFEEAPLHVMVFTYMGYGIGTLFGYLRDFLRNWGIEKCNAAVERKEQKDFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGPLFDLMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAAKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDGTTQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKKSARPELYDETSFELED", "text": "FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. SPT complexes containing SPTLC3 generate shorter chain sphingoid bases compared to complexes containing SPTLC2. The SPTLC1- SPTLC3-SPTSSA isozyme uses C12-CoA, C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. On the other hand, the SPTLC1- SPTLC3-SPTSSB has the ability to use a broader range of acyl-CoAs without apparent preference. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MAEGLVLKGTMRAHTDMVTAIATPIDNSDTIVSASRDKSIIVWKLTKDDKSYGVRQRRLTGHSHFVEDVVLSSDGQFALSGSWDGELRLWDLAAGVSTRRFVGHTKDVLSVAFSLDNRQIVSASRDRTIKLWNTLGECKYTISEGGEGHRDWVSCVRFSPNTLQPTIVSASCDKTVKVWNLSNCKLRSTLAGHTGYVSTVAVSPDGSLCASGGKDGVVLLWDLAEGKKLYSLEANSVIHALCFTPNRYWLCAATEQGIKIWDLESKTVVEDLKVDLKAEAEKSDGSGTAATKRKVIYCTSLNWSADGSTLFSGYTDGVIRVWGIGRY", "text": "SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily."}
+{"protein": "MAANNFATKLSRNTNRITVILVYAFLEWLLMFFIFLNSFFTYFIVKFASFFGLKQVCLLCPKLDRIFERKPENRFTYKELLCQNHIAELASLSFCRTHGKLSESANLCSDCSNREEEQSNIGLGFCTCCQKSLADKPYPNYLLLKSSIWGKTLGDREDGGLILEMIDDDKFGDGFEIDRESYPLGFFRDKAEEGKKQDQQQNGEVISDVESYGLSLREVSEEDGLRSIISNNSPGNEAKSRVSEDEQRNDDTSNVATYGEDQISGRVEEKEEETGVADLLYDQFESKNFTGSQIEEEEEDREETTKELDPETPTSVSTLFNKKLHFLARNEYAAAEDAGDGNVLVSEMDGGDPLRTIERLRETVRAEQEALRDLYAELEEERSASAISANQTMAMITRLQEEKAKVQMEALQYQRMMEEQAEYDQEALQLLNHLMVKREKEKEQLQRELEVYRAKVLEYESKAKNKIIVVENDCEADDDDKEEENREEDNSSEMDVDLEKITLDCVQHMSMLGESLSEFEEERLVILDQLKVLEDRLVTMQDKESAEDPGEFSNSYEEASNGHGGLTMASMAKSLLPLLDAAENESEDGSQGLPESDEKNFGSDSEKLEIIKQVDSVYERLQELETDGEFLKNCMSSAKKGDKGTDILKDILQHLRDLRTIELTNTIENQTTQEE", "text": "FUNCTION: Membrane-anchored myosin receptors that define a distinct, plant-specific transport vesicle compartment. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
+{"protein": "MTILFLFLLLFLLMFIGVPIAVSLGLSGALTILLFSPDSVRSLAIKLFETSEHYTLLAIPFFLLSGAFMTTGGVARRLIDFANACVGHIRGGLAIAAVLACMLFAALSGSSPATVAAVGSIAIAGMVRSGYPQAFGAGIVCNAGTLGILIPPSIVMVVYAAATETSVGKLFIAGVVPGLLLGLILMVVIYIVARVKKLPAMPRVSLREWLASARKALWGLLLMVIILGGIYSGAFTPTEAAAVAAVYSAFVALFVYRDMRLSECPKVLLESGKLTIMLMFIIANAMLFAHVLTTEQIPQSIASWVTELGLSPWMFLLVVNIVLLIAGNFMEPSAIILILAPIFFPIAMELGIDPIHLGIIMVVNMEIGLITPPVGLNLFVTSAVTGMPLGATIRAALPWLMILLVFLIIVTYIPAVSLALPNWLGMS", "text": "FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP) transport system DctPQM involved in C4-dicarboxylates uptake. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TRAP transporter large permease family."}
+{"protein": "MAVLRPFDKLPELNSATILLVGAEGGPQQQLAEAMLREKKDFNINIHLASSLPLPSERDHLRPRIDLIAFVIDIKSKYSLKNVQASLAYVDVRFFLGKVCFLVTGVGRANNCSVEMNAIWKLGEDYCSPVIFCELELEGIRVATAQRLLRMLQICAGRVPGVSALYFSLLMRNSAGD", "text": "FUNCTION: Component of the CENPA-HI complex, 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."}
+{"protein": "MIIQRVVLNSRPGKNGNPVAENFRVEEFSLPDALNEGQVQVRTLYLSVDPYMRCKMNEDTGTDYLAPWQLAQVADGGGIGVVEESKHQKLTKGDFVTSFYWPWQTKAILDGNGLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGVQEKGHISAGSNQTMVVSGAAGACGSLAGQIGHLLGCSRVVGICGTQEKCLFLTSELGFDAAVNYKTGNVAEQLREACPGGVDVYFDNVGGDISNAVISQMNENSHIILCGQISQYSNDVPYPPPLPPAVEAIRKERNITRERFTVLNYKDKFEPGILQLSQWFKEGKLKVKETMAKGLENMGVAFQSMMTGGNVGKQIVCISEDSSL", "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": "MENQASLNSIQKTVWDGKLPLQITLASSESRTFDQTDPYLISCPRISYLPSLLPRLRSFFASSLIEPKSQPHEGWFSFEGVPLKWHLPIGLLYDLYAGADPASKGSRPDESEQIISSVGDTLPWRLTLHFSDWPDEELVRLDADGMVMHDAFINSVKEADFLRNGTAKGIMSLSKEDSSGLWEAVQDVDLPSFQRISNILLPAPNQPFRNVPIRFFLPLPPDSGSPSLKVVQSPLPPSIPASTANATQSTVLRGKPASQLQTIGSALHSLLPNLFPSRRTPVLAKPVLHGAAVPMSAPVEEVARSAAYGDGWVYIVVRMMG", "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": "MKEIWETLKQYFGDGFVPGSAPLRYEMHFCDMKEPLNKKQSMRYGVEIPEDAMPLFSVLGDTCAPPCSCQDISGVIEHIDRYLENAPIRHADDYTITSGKDDEDINQVSLYIMRDTLSWWVHWGGSLHPNNYWKLIYVAFAAIPDDVQVHPRDFIDGTYRFLGHSWNDCLNGLLAEGVPSDQVKLAEMTLWRQMATQYIEKVDPGLRSLLVSKTTLMTQYRVMTANTLGCAVLLLASEGVIVGDLDDGALEMASIAQCLSMDMAKEALGVLEGEKTETVAGDRRQLKRELRWLYVRCMKYLDAQPHAEFLRRFASSGLHYVPMMDRYLERVRGHIRFPIRESVARILEPFIKREPTPNKSGREADHIAQVVNEPITVAL", "text": "FUNCTION: Alpha-humulene synthase; part of the gene cluster that mediates the biosynthesis of eupenifeldin, a bistropolone meroterpenoid that acts as an antitumor agent (PubMed:30980906). The first step of eupenifeldin biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase eupA (PubMed:30980906). Oxidative dearomatization of 3-methylorcinaldehyde likely catalyzed by the FAD-dependent monooxygenase eupB is followed by oxidative ring expansion by the 2-oxoglutarate-dependent dioxygenase eupC to provide the first tropolone metabolite, tropolone stipitaldehyde (Probable). In parallel, generation of sesquiterpene alpha-humulene from farnesylpyrophosphate (FPP) is catalyzed by the terpene cyclase eupE (PubMed:30980906). The cytochrome P450 monooxygenase eupD then hydroxylates humulene to humulenol (PubMed:30980906). The putative Diels-Alderase eupF probably catalyzes the formation of the tropolone-humulene skeleton by linking humulenol and the polyketide moiety (Probable). The short-chain dehydrogenase/reductase eupG and the flavin-dependent monooxygenase eupH are also essential for eupenifeldin biosynthesis and are likely the additional decorating enzymes of the tropolone-humulene skeleton to produce final eupenifeldin or derivatives (Probable). SIMILARITY: Belongs to the terpene synthase family. Alpha-humulene synthase eupE subfamily."}
+{"protein": "MTVGKRKLSNGTVNEAKRLDDHVPVVAPSTNPDFENANGEDNEDIDDYSSEGEMSPQLENYFPQTTSWQKTITKVVKSVVSIQFSHVSNFDTESSAVSEATGFVVDSERGYILTNRHVVGPGPFCGYVVFDNHEEAVVRPIYRDPIHDFGFLQFDPKDIRYMKIEQLDLRPDLAQVGTEIRVVGNDAGEKLSILAGFISRLDRNAPDYGTLSYNDFNTEYIQAAASASGGSSGSPVVNKEGYAVALQAGGSTEASTDFFLPVYRPLRALQCIQQGQTITRGDIQVEWQLKPFDECRRLGLTPEAEAAARSQFPDKIGLLVAELVLPEGPADGKLKEGDTLISINGTPIASFISVDEILDEQVGQSLKFVIQRNGHEVSFDIVVGDLHSITPSRYVDIAGASFNDLSYQVARCFCIPVRGVFINDGSGSFELSPFEKNGWLLEYVDDKPTPNLDAFVEVMKSIPDRKKVSISYRHVSDFHTENITVIYVERHWQSTFRMAVRNDSTGIWDFTDIQDKPLPAEEPVPQNAKYIDIPFDDPEKSGCSQLTRSFVQVRTIAPVPVDSYPYRREIGYGVVVDAANGYVLVSRRFVPHDMCDIFVIFAESVELPGKVVFLHPNQNYAIVKYDPKLMLADVKTPKFSDKPLKRGERAFFVGYNYNLRVVTDDVKVSSVSSINVPVASLSPRYRGTNLECILLDSKLSQECDSGVLADYDGTLRAFWITYLGETNCDQTNDRVYRMGLDVTDVMSVIKSLHENKVPAGLRILDAEFASMTIFQGRLRGVPQEWISKFEEVCEDEMKFLAVDRVSAPALGQVATPLKTGDIVMSVNGSIVKTMRDLGIMYNQDSLDFVVIRQKKELHLNVPTIDTSTLNTSHVVFWCGSILQAPHHGVRQLIEKIPSEIYVTKKNSGGPANQYGIATNSFITHVNDTETKTLESFVSVVKGIPDNTYIKLRLVSFDSIPVAISVKTNYHYFPTFELKKVNGEWEETEHKV", "text": "FUNCTION: Nuclear serine protease which mediates apoptosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the peptidase S1C family."}
+{"protein": "MPFPNCSAPSTVVATAVGVLLGLECGLGLLGNAVALWTFLFRVRVWKPYAVYLLNLALADLLLAACLPFLAAFYLSLQAWHLGRVGCWALHFLLDLSRSVGMAFLAAVALDRYLRVVHPRLKVNLLSPQAALGVSGLVWLLMVALTCPGLLISEAAQNSTRCHSFYSRADGSFSIIWQEALSCLQFVLPFGLIVFCNAGIIRALQKRLREPEKQPKLQRAQALVTLVVVLFALCFLPCFLARVLMHIFQNLGSCRALCAVAHTSDVTGSLTYLHSVLNPVVYCFSSPTFRSSYRRVFHTLRGKGQAAEPPDFNPRDSYS", "text": "FUNCTION: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14- eicosatetraenoic acid (12-S-HETE), with much lower affinities for other HETE isomers (PubMed:21712392, PubMed:29227475). 12-S-HETE is a eicosanoid, a 12-lipoxygenase (ALOX12) metabolite of arachidonic acid, involved in many physiologic and pathologic processes (PubMed:26965684, PubMed:28619714, PubMed:29227475). 12-S-HETE-binding leads to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B pathways leading to cell growth (PubMed:21712392, PubMed:29227475). Plays a crucial role for proliferation, survival and macropinocytosis of KRAS- dependent cancer cells by mediating the translocation of KRAS from the endoplasmic reticulum to the plasma membrane (PM) and its association with the PM (PubMed:28619714). Contributes to enhanced immune responses by inducing dendrite protrusion of small intestinal CX3CR1(+) phagocytes for the uptake of luminal antigens (By similarity). Acts also as a key receptor for 12-(S)-HETE-mediated liver ischemia reperfusion injury (PubMed:29227475). FUNCTION: Proton-sensing G protein-coupled receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MADRSDIIIENYQVSPRIGFLPDKPPLARLPHPYYAGWEETISRVAPSRGDGRAREYIDEMPLLSTGKLRVLPEWHRAYTLLSILSQVYIWDGDEPSNRIPASIASPLLAVSEHLGLNPCASFASFCLWNIRPVGRHGLNYAAAYEPENLGQITSFTGTTDEEWFFSISAAIEARGGCLIPGMFDTIEAAREGNSQRVQEFLGTLASCVRHMCKDLKRMYEGCAPSVFYHDVRPFLNGGKGVNKDTQTPGGVFYENESGGGQWHQYQGGSNAQSSLIQLLDIFLGVDHSITAANKPHEGYHREMQSYMPGKHRQFLQLMSRLSNVREFVLCHPVTAEIRIEYSRATAELVALRQTHMIMASRYIVMQGRKGSMCRDSSKGTGGTEFMPFLKDARDCTLATCCPRP", "text": "FUNCTION: Indoleamine 2,3-dioxygenase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid (PubMed:35748771). Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine (PubMed:35748771). The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine (PubMed:35748771). 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme (PubMed:35748771). The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system (PubMed:35748771). Finally, a dehydration reaction completes the biosynthesis to yield aspcandine (PubMed:35748771). SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family."}
+{"protein": "MASDTEKLMCLTTENAEIPADFVELQPLDEIETVSLETNVSQTIEVYGDVGVDWAHGGHYHSPLIALQPLAGSNLSNGDHDQEMIIVQTREEVVDYQDSDNLLLGTEFESQMVLPVNEDDYLQPTTATFSGFMAAENGQDELSPYGGNLCGLTTIIEAGAEEGVNPDLGDKQWEQKQIQIDGLDGEFPFAMWEDNNLKEDPVAEEEAGESTPDYSEYMTGKKFPPEGIPGIDLSDPKQLAEFTSMKPKKPKGDFPRPVACSHKGCGKMFKDNSAMRKHLHIHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPYQCTFEGCGRRFSLDFNLRTHVRIHTGDKPFVCPFDACNKKFAQSTNLKSHILTHVKNKNDQ", "text": "FUNCTION: Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the YY transcription factor family."}
+{"protein": "MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSSGGTNGTSFSYTFHGDPHAMFAEFFGGRNPFDNFFGQRNGEEGMDIDDPFSGFPMGMGGFTNMNFGRSRPAQEPTRKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKRGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI", "text": "FUNCTION: Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, nucleolus Note=Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock."}
+{"protein": "MKAYAMLKIGATGWIEKPRPVCGPNDAIIRPLAVAPCTSDVHTVWEGGIGERHNMVLGHEGCGVVDEVGSEVKSFKVGDRVLVAAITPEWNSVNAQAGYPMHSGGMLGGWKFSNVKDGMFAEYFHVNDAEGNLALMPEGMDLADACMLSDMIPTGFHANELADIQYGVALSFFCAGPVGLMAIAGAALKGAGRIIVVDSRPDIVEIAKAYGATDYIDFKKVSVVDEILKWTNNEGVEKVLISGGGSTILETAIKVLRPGGKIGNVNYFGAGEFLTIPRVEWGVGMAHKAIHGGLMLGGRLRLEKLARLIMTKKLDPSKMITHRFKGFEHIEEALFLMKDKPKDLIKSVVIF", "text": "FUNCTION: Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde (By similarity). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MSFIMSSLRNLFLSPLRSFIQKDFHDAFDSMTLLDKLLFMMVHFVDKLILWHRLPVFLGLAYLAARRHLHQEYNLINVGRTPTGVRSNPEDYPYRTADGKYNDPFNEGAGSQFSFFGRNVMPVDQHDKLKKPDPMVVATKLLARKNFMDTGKQFNMIAASWIQFMIHDWIDHLEDTHQIELRAPEEVASECPLKSFKFYKSKKTPTGFYEIKTGYLNRRTSWWDGSAIYGSNTEALKKVRTFEDGKLKLSADGLLEQDENGNIISGDVRNPWAGLLALQALFIQEHNLVCDTLKKEYPKLEDEDLYRHARLVTSAVIAKVHTIDWTVELLKTDTLLAGMRANWYGLLGKKFKDTFGHVGGSSLGGFVGMKKPENHGVPYSLTEEFVSVYRMHQLLPDTLQLRNIDATPGPNKSLPLTNEIPMEDLIGGKGEENLSRIGYTKQMVSMGHQACGALELMNYPIWMRDLIPQDVDGNDRPDHIDLAALEIYRDRERSVARYNEFRRRMLQIPISKWEDLTDDEEAIKMLREVYGDDVEELDLLVGMSAEKKIKGFAISETAFFIFLIMASRRLEADKFFTSNYNEETYTKKGLEWVNTTESLKDVLDRHYPEMTGKWMNSNSAFSVWDSSPEPHNPIPIYFRVPQQ", "text": "FUNCTION: Alpha-dioxygenase that catalyzes the primary oxygenation step of a variety of 14-20 carbon fatty acids, containing up to three unsaturated bonds, into their corresponding 2R-hydroperoxides (Probable). Involved in the production of oxylipins that function in cell signaling, wound healing, and protection from infection (Probable). The lipid-derived signaling pathway is involved in the initial response of hot pepper plants to pathogen infection (Probable). SIMILARITY: Belongs to the peroxidase family."}
+{"protein": "MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYKRWHELMLDKAPVLKVIVNSLKNMINTFVPSGKIMQVVDEKLPGLLGNFPGPFEEEMKGIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWILGKKDVMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW", "text": "FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (PubMed:10610716, PubMed:7744740, PubMed:15655246, PubMed:11451951). 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 (PubMed:10610716). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (PubMed:7744740, PubMed:15655246). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (PubMed:12764132, PubMed:12815059). 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 (PubMed:12764132). Has also an N- acylethanolamine hydrolase activity (PubMed:15655246). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (PubMed:17713573). 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 (PubMed:22261821). FUNCTION: [Isoform 2]: May directly regulate steroidogenesis by binding the nuclear receptor NR5A1 and negatively regulating its transcriptional activity. SUBCELLULAR LOCATION: Lysosome Secreted Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus Cytoplasm Note=A localization to the nucleus and the cytoplasm has also been reported for ASAH1, most probably for isoforms devoid of a signal peptide. SIMILARITY: Belongs to the acid ceramidase family."}
+{"protein": "MSGKDRLPIFPSRGAQMLMKARLAGAQKGHGLLKKKADALQMRFRLILGKIIETKTLMGDVMKEAAFSLAEAKFTSGDINQVVLQNVTKAQIKIRTKKDNVAGVTLPVFESYQDGSDTYELAGLARGGQQLAKLKKNYQSAVKLLVELASLQTSFVTLDEVIKITNRRVNAIEHVIIPRIDRTLAYIISELDELEREEFYRLKKIQDKKREARIKADAKKAELLQQGIDVRQQANILDEGDDDVLF", "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 D subunit family."}
+{"protein": "MSKVSPANIRSSVETILKGSEEKKRNFTETVELQIGLKNYDPQRDKRFSGTIKLPNVPRPNMSICILGDAHDLDRAKHGGVDAMSVDDLKKLNKNKKLVKKLAKKYDAFIASEVLIKQIPRLLGPGLSKAGKFPSPVSHSDDLYGKIIEVKSTIKFQLKKVLCLGVAVGHVDMAEEQLAANLSLAINFLVSLLKKGWQNIGSLVIKSTMGKPYRLY", "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": "MSFFKKLAASAGIGAAKVDTILEKDAYFPGEEVQGTVHVKGGKIAQDIRYIDLQLSTRYVIVKDDEEHRKYATIHSFRVTGSFTIQPGEEHQFPFTFTLPLDTPITVGKVEVAVVTDLDIQGGIDKSDHDRIFVEAHPWIENVLEAIENLGFRLNEADCEQAPYFQRRLPFVQEFEFVPTSGYYRQMLDELELIFLLDEDGLEIIFEVDRRARGLRGWLEEMYNDGEQLVRVRFSQSELEDTEELEEVLEEILDQYAE", "text": "FUNCTION: Controls the expression of spo0A and is required to pass the morphological stage 0 of sporulation. SIMILARITY: Belongs to the spo0M family."}
+{"protein": "MVAAPLLRAHQAARLQSVSTSRLGLNPHVIKSAGRLQLLRGSSFSTATSKWQAGVLDRTRNIGIIAHIDAGKTTTTERMLYYSGFTRRIGDVDEGSTVTDFLPAERARGITIQSAAITFHWPPQTAGDGNTTPQEPQTPRSASSHTVNLIDTPGHADFTFEVMRSLRILDGAVCILDGVAGVEAQTEQVWHQASTYRIPRIVYVNKLDRDGAAFGRTVREVASRLGGWPAVCQIPWFEGGNGRFTGIADAINLQGLRWEEGDGKSVKMFNLEQLASEEPQLAQELKRARVALVELLSEHDEAMVEKFFDCEEDHLAVPPNDILESLRRCLLEEQGRKIIPIFAGASFRNIGVQPLLDAVTNLLPSPPETPEPEVSIGGVKGGLRRLLSGDLLVEQGEKAASAKGKHKKKSAIQAESRNAIEKLQGCALAFKVVNDPKRGVLVYVRVYSGSLDRNSILYNTNLNVSERAPRLLKMYANDAVEVDSIPEGHIGVVAGLKHTRTGDTLVTYSGNKATPPEPLNTLQLRPITVPPPVFFASVEPHSLSEEKRLQESLAMLLREDPSLHVTVDEDSGQTLLSGMGELHLEIARDRLLNDLKAKASMGRIEIGYRECPLGASGPITKIFDKEIAGRKGKAGCTATVEPFDPEETTTEPDPSTLSIQTTDGNQIIIQAPGLEVEVNKKGIEESPLLPPGLDVHALRTALQNGCLAALARGPQFTFPMHGTRVTLTFNPAEHLFGNESTPSALSAAARLATSSALRDLPSGAGTSLMEPVMNVIISVDEASLGAVVHDISSSRGGHIISLDEETPLQTTGITSNPTDDLLPPIDPNKVYAPPDPFQSSTVGIDLPSSANRPRTITAKVPLKEMVGYLKHLRSLSAGRGTFVMSVDRFEKMSAPRQKAVLAELRGDFF", "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": "MNVSKYVAIFSFVFIQLISVGKVFANADEWMTTFRENIAQTWQQPEHYDLYIPAITWHARFAYDKEKTDRYNERPWGGGFGLSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRPLADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPVTFQMTYIPGTYNNGNVYFAWMRFQF", "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. Phosphatidylglycerol (PtdGro), phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and phosphatidic acid (Ptd-OH) are all effective acyl donors. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the lipid A palmitoyltransferase family."}
+{"protein": "MKRSALLASFLPLALGCDSAETHSCASAFSVSSAAAASFCATFTASTVTATTGVPDVFLSNCDYKTKHLSSACSCLGTADGSAPASTPAAPAVSSSSKVGKAPAVAATRTSAIPTTFHTTAVRVPLSTSAAAAVTSQAVLPAQSSVAGNGGTTCTVTEYASISSAVASCSNILLSNINAPASSTIDLTGLQTGAAVIFAGETTFGDTYDSDFDPIVISGTDVTITGEEGHVINGNGEAYWDGEGSNGGQDKPDHFIVVKDMYNSKIENLNILNWPVHCFEIENTEYLTISGLILNNTAGDAANSKSDGDPAAHNTDGFDIKQSDFLTLSNSWVHNQDDCVAVTSGSSIVVDNLYCYGGHGLSIGSIGGKSNNTVDGVTFSNSQVINSENGCRIKSNADTTGEVYNVKYENITLSGISDYGIDIQQDYENGGATGDPTNGVKIENISFVNVKGTMSDGKDYYILCGDGSCSNFVFTDVDITGGSDDSCNYPSSGCP", "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). 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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
+{"protein": "MTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLDKGDKIAKESQFLKEELVAAVEDVRKQGDLMKSAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDVGHRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVNGISNAAQATTSDDASQHPGGSGGGELAYALNDFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI", "text": "FUNCTION: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1- dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). May play a crucial role in cell differentiation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell junction, adherens junction Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell junction Note=Found at cell-cell boundaries and probably at cell-matrix boundaries. SIMILARITY: Belongs to the vinculin/alpha-catenin family."}
+{"protein": "MLYNKLITIAALLVPALAAPQGLDVRDCDYTCGSHCYSASAVSDAQSAGYQLYSAGQSVGRSRYPHQYRNYEGFNFPVSGNYYEWPILSSGSTYNGGSPGADRVVFNDNDELAGLITHTGASGNGFVACSGW", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ribonuclease N1/T1 family."}
+{"protein": "MLKRVAIVLGGLLISAHALANTMVEMKTNLGNIEIELYNNKAPISAKNFESYVKNNFYNGTIFHRVIPNFMIQGGGFETNMKEKATAAPIKNEASNGLANTRGTLAMARTSNPDSATSQFFINVADNNFLNASRTDAGYAVFGKVIKGMDVVDKIANVPTSTYGMHQNVPKQPVKIISVQIKSINTAK", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This protein is not essential for growth. Presumably plays a role in signal transduction. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the cyclophilin-type PPIase family."}
+{"protein": "MSGEGMTAVSEPVQLTVPQMLAQLQGTDTSLRYYAAWWLGKFGLETATAAERQAIVSALIAALADEADRTELGGYPLRRNAARALGKLGDRQAVPALIECLRCEDFYVREAAAIALGQLGDPRAIAPLQSLLEGGVAMARLVPGRPHLVQPVEAVIESLGHLGATEAIALIEPFLAHEMPRVQFAAARALFQLTGDAVYGDRLLAALNSEDVQLRRTALLDLGAMGYLPAAEAILQAGVEASFKLIALHGILGQQLRQAAPAEQTLSLFQGLDQLL", "text": "FUNCTION: Required for the chromophorylation of the CpcA gene product. SIMILARITY: Belongs to the CpcE/RpcE/PecE family."}
+{"protein": "MTDRTPPQGRARRLFSRTSWPEARFLADVLRTETFGGGLLLLGAVLALLWANSPWADSYAALASWVPWPGGSDLHLDLDLATWAADGLLAIFFFVVGLELKREFVAGDLRDPRRAALPVVAAIGGMIVPALIYVGINLAAGGENLRGWAIPTATDIAFALAVLAVIGSHLPQGLRAFLLTLAVVDDLLAITVIAIFYTGDFKLTPLLVALLPIALFGLLVQRRKTWWWALIPLAVVAWTLVHESGVHATVAGVLLGFTVPVLRGREGDRHGLAEHLEHRWRPVSAGFAVPVFAFFAAGVSLRGADLGGIVTDPIVVGIVAGLVLGKVLGIFGSTFMLARFTRAELDRDITWTDLLGVSLLAGIGFTVSLLIGELAFEGGTAGDNVKAAVLTGSVIAALLASAVLSRRNKAYRRIAAKERLDSNRDGVPDVFQHRDG", "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": "MAKLLQPSPKFLPEEWHIANKNQYHRAEAQRSRSERLVAESQRLVDEIEKTTRKSQSDVNKKLEQRLEEVRFWKKELDDKLEQLVCTTEDLLTYQTRLQNALESLKEPLHITQMCLEYRDKRIGIDLVHDEVEQELLKEAEVIHGVMALLTRTMDEVTEQIRLNRSAKYNLEKDLKDKFVALTIDDVCFSLNNNSPGIYYSDSVVRVEPHSVSLEDWLDFSNTNVEKANRQRNNSLALKALVDRILSQTADDLRRQCDMVDTAFQMGLKETKAARDQLAAHLAKVMEEIACQEKNMTVLEKAILDQEGPAKVAHTRLETRTRRPNVELCRDVAQYRLVKEVGEIAQNVGRLKEALAQAQVELKGLNRRQLALQEEVQVKENTIYIDRVLCTHMRKSNPLRDGGDQGQWARACAPTPSAEDGTSHTD", "text": "FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the tektin family."}
+{"protein": "MDMTNAQRLILSNQYYLMSQLTPENEAKYRRLQTIVERGYGLQMRELDKDFGCLPEDACRNIIDYMEMHHALQESYKMLDDASQSQVEPRRLQFLGFDAATESQQVHYVRFLTEEEGLYPQFDKSEHQFNSQVQMQDKYQRMLQTWRNCPRQYHLSSSEITQILSA", "text": "SIMILARITY: Belongs to the UPF0304 family."}
+{"protein": "MKIISAEQVHQNLNFEELIPLLKQSFSRPFSMPQRQVYSLAPEQSENHDAFALLPSWNEEVIGNKAFTYFPDNAKKHDLPGLFSKIMLFKRQTGEPLALVDGTSVTYWRTAAISALASQLLSRKNSQHLMLFGTGNLASYLVKAHLTVRDIKQVTLWGRNAKKVSKLIADFSILYPAVTFKTSVDVNAEVASADIICCATGAKTPLFDGNSVSAGCHIDCLGNHMTDARECDTTTILRARVFVDSLTNTLNEAGELLIPMAEDAFNKDEIVGELADMCKTPSMLRQSSDEITLFKSVGTAISDLVAAHSVVEKLAD", "text": "FUNCTION: Catalyzes the reduction of Delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, using preferentially NADPH over NADH as the electron donor. Together with LhpH, is involved in a metabolic pathway that converts trans-3-hydroxy-L-proline (t3LHyp) to L-proline. To a much lesser extent, can also reduce Delta(1)-piperideine-2-carboxylate (Pip2C) to L-pipecolate in vitro; however, this activity has likely no physiological significance in vivo since C.psychrerythraea probably possesses no ability to metabolize D-lysine via the L-pipecolate pathway. Does not show ornithine cyclodeaminase (OCD) activity. SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin family."}
+{"protein": "MEDTLKITAEDLKNYIERIEKLEQEKRDVQDHIRDVYAKAADEGWDIKVMKQIIRLRKMDDDDREEQEILLDTYKRALGMNYEGE", "text": "SIMILARITY: Belongs to the UPF0335 family."}
+{"protein": "MVLAMLGALHPRAGLSLFALYLVLAAALLRPQPLRPQRAVPEEFSAPLELSAPLSGLVDDYGVRPKHPWPRGPRPLLSRAQQRKRDGPDMAEYYYDSRL", "text": "FUNCTION: Key regulator for male fertility expressed transiently in round spermatids where it recruits IZUMO1 at the endoplasmic reticulum (ER) membrane and coordinates the oolemmal binding multimeric complex (IZUMO1 complex) assembly. Upon complete assembly of the IZUMO1 complex, its ER retention is released, facilitating IZUMO1 complex export to the acrosome. Through the interaction with SPPL2C, inhibits its intramembrane protease activity directly accessing the catalytic center of an I-CLiP. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein."}
+{"protein": "MASFGYFLFLCGLSQALSSYPIWWSLAIGHQYSSLGTQPILCGSIPGLVPKQLRFCRNYVEIMPSVAEGVKIGIQECQHQFRGRRWNCTTVNDSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGSATICGCDTRHKGSPGEGWKWGGCSEDVEFGSMVSREFADARENRPDARSAMNRHNNEAGRTSIIELMHLKCKCHGLSGSCEVKTCWWSQPDFRVIGDYLKDKYDSASEMVVEKHRESRGWVETLRPKYNFFKAPTEKDLVYYENSPNFCEPNPETGSFGTRDRICNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCIFHWCCYVRCQECIRVYDVHTCK", "text": "FUNCTION: [Isoform 1]: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (PubMed:17488271). Regulates chick apical ectodermal ridge formation (PubMed:17488271). Required for normal embryonic mesoderm development and formation of caudal somites. Required for normal morphogenesis of the developing neural tube (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space, extracellular matrix Secreted. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MIKVGICDTTFARYDMGGAAIDELKKHTAGIKIIRRTVPGIKDLPVACKKLIEEEGCEMVMALGMPGPEEKDKVCAHEASTGLIQAQLMTNTHILEVFVHEDEEDDPEELKVLADNRAREHAQNLIMMLFKPDRLTREAGMGLREGKPDAGPL", "text": "SIMILARITY: Belongs to the DMRL synthase family."}
+{"protein": "MAADKPADQGAEKHEGTGQSSGITDQEKELSTNAFQAFTSGNYDACLQHLACLQDINKDDYKIILNTAVAEFFKSNQTTTDNLRQTLNQLKNQVHSAVEEMDGLDDVENSMLYYNQAVILYHLRQYTEAISVGEKLYQFIEPFEEKFAQAVCFLLVDLYILTYQAEKALHLLAVLEKMISQGNNNKNGKNETGNNNNKDGSNHKAESGALIEAAKSKIHQYKVRAYIQMKSLKACKREIKSVMNTAGNSAPSLFLKSNFEYLRGNYRKAVKLLNSSNIAEHPGFMKTGECLRCMFWNNLGCIHFAMSKHNLGIFYFKKALQENDNVCAQLSAGSTDPGKKFSGRPMCTLLTNKRYELLYNCGIQLLHIGRPLAAFECLIEAVQVYHANPRLWLRLAECCIAANKGTSEQETKGLPSKKGIVQSIVGQGYHRKIVLASQSIQNTVYNDGQSSAIPVASMEFAAICLRNALLLLPEEQQDPKQENGAKNSNQLGGNTESSESSETCSSKSHDGDKFIPAPPSSPLRKQELENLKCSILACSAYVALALGDNLMALNHADKLLQQPKLSGSLKFLGHLYAAEALISLDRISDAITHLNPENVTDVSLGISSNEQDQGSDKGENEAMESSGKRAPQCYPSSVNSARTVMLFNLGSAYCLRSEYDKARKCLHQAASMIHPKEVPPEAILLAVYLELQNGNTQLALQIIKRNQLLPAVKTHSEVRKKPVFQPVHPIQPIQMPAFTTVQRK", "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. Is not required for association of CNOT7 to the CCR4-NOT complex. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CNOT10 family."}
+{"protein": "MGSRSSHAAVIPDGDSIRRETGFSQASLLRLHHRFRALDRNKKGYLSRMDLQQIGALAVNPLGDRIIESFFPDGSQRVDFPGFVRVLAHFRPVEDEDTETQDPKKPEPLNSRRNKLHYAFQLYDLDRDGKISRHEMLQVLRLMVGVQVTEEQLENIADRTVQEADEDGDGAVSFVEFTKSLEKMDVEQKMSIRILK", "text": "FUNCTION: Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Binds to and activates SLC9A1/NHE1 in a serum-independent manner, thus increasing pH and protecting cells from serum deprivation-induced death. Also plays a role in the regulation of cell proliferation and tumor growth by increasing the phosphatase activity of PPP3CA in a calcium-dependent manner. Activator of the calcineurin/NFAT signaling pathway. Involved in the cytoplasmic translocation of the transcription factor NFATC3 to the nucleus. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell membrane Note=Predominantly localized in a juxtanuclear region. Colocalizes with SLC9A3 in the juxtanuclear region and at the plasma membrane (By similarity). Exported from the nucleus to the cytoplasm through a nuclear export signal (NES) pathway. May shuttle between nucleus and cytoplasm. SIMILARITY: Belongs to the calcineurin regulatory subunit family. CHP subfamily."}
+{"protein": "MGPKATSGTRGRGKKVGTKTAAPLPKYKDLIVEAVVSLAERGGSSRQAIKKFIRDKYAVGAKFDGQFNLAVKRGLEAGELAQPKGPAGSIKLLKKAAQPKPEEAKRAAKPAKRVVKAAKPAKAKPAKAAKAAKPAKPVKAAKAASAVKPAARKLAKPVVKKVGSKKVATKNAVVGKKSVVSSAASKKLLAKKAVPKKTAGRKPLVGKKVVAVSRKPAAKKLAKSA", "text": "FUNCTION: Could act as an H1-type linker histone. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H1/H5 family."}
+{"protein": "MGQWKVMILICLYGAVKEFRPTEPYMYEYQHTVLNISEHTLNSEVYPIWTYSYLVALIPSFLLTDVLLYKPILIIEALSYFACWMIFVFGRSVWCMQLLELFYGWATATEIAYFAYIYVKVPKEDYKSATAYTRAALLVGRFLAYTLAQLLIGLNWADYMTLNIINLVSMTFAVFLAAILPHVPWRNAYQKKLEDKKSVTDLESLVSEAKYSDYLKLFFVELHQNLYTIYKNPLVLKWSIWSALSSCIFYQIINYTQTLWGTLPEKENKYNGIPEALVPLLGIPADLITRQMNVNWNRWGDALISVGSLLQAGLLFWMSQSHEIIILYICYIIYRVIYQLTTTIAQSTLALTLDSRLFGLLFGINTFVALALQSILTAIVIDAEKLAIRAQFVVYSGYHIVVATLFGIIFGIWAIRTIWRKRSH", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter (TC 2.A.48) family."}
+{"protein": "MKTRTSRLFRLSALAAGLCLAQAALAADPGAAPSYQALPAGNLCPAAAYDSRYNTKYLGFFTHLVQAQDDWLFRTTYDLRTDFGTSAEGWRELRALRDELKRKGIELVVVYQPTRGLVNREKLSPAEKAGFDYELAKKNYLATIARFRQAGIWTPDFSPLFDEKEEHAYYFKGDHHWTPHGARRSAKIVAETLKQVPGFEEIPKKQFESKRVGLLSKLGTFHKAAAQLCGNSYATQYVDRFETEPVGASDSGDLFGDGGNPQIALVGTSNSGPAYNFAGFLEEFSGADILNNAVSGGGFDSSLLAYMTSEEFHKNPPKILIWEFATHYDMAQKSFYRQAMPLVDNGCSGRKTVLSRKVKLRQGRNEVLLNSAALPIRSGSYVADVTYSDPSVHELKNTIWYMNGRREQLKIEQSKAVDTGGRYVFQLRNDSDWADQQFLSLEIEAPEDMPQGLEVQASICQAAPAKASQSVAGR", "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. Acetylation of alginate causes the cells in the biofilm to adhere better to lung epithelium, form microcolonies, and resist the effects of the host immune system and/or antibiotics. Displays a low acetylesterase activity in vitro using a pseudosubstrate, 3-carboxyumbelliferyl acetate. Probably has acetyltransferase activity in vivo. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the AlgX family."}
+{"protein": "MKKVLALVVAAAMGLSSAAFAAETATTPAPTATTTKAAPAKTTHHKKQHKAAPAQKAQAAKKHHKNAKAEQKAPEQKAQAAKKHARKHSHQQPAKPAAQPAA", "text": "FUNCTION: Required for growth and/or survival at acidic conditions. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the Asr family."}
+{"protein": "MILIEDLTVVSQREIAPRIFEMVLKGEMVADMQLGQFVHLKVPDPSKLLRRPISISEIDYNKKEATIVYRVEREGTAILSKMVAGQTIDTMGPQGNGFDISIIEAGQKALLVGGGIGVPPLVETAKQLKAKGVEVVSVIGFANKNAVILEDKLRACGDVYVTTDDGSYGIKGYVSTVIDNFDWTPDAVYSCGAPGMLKYVDSKFENHPHAYVSMEARMACGMGACYACVVHVKGETDAKNLRVCEEGPVFPTGKVIV", "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": "MKYFVVALALVAAFACIAESKPAESEHELAEVEEENELADLEDAVWLEHLADLSDLEEARGFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKHYGKKSSSKSFRKIVISKSF", "text": "FUNCTION: Insecticidal, cytolytic and antimicrobial peptide. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 06 (cytoinsectotoxin) family."}
+{"protein": "MEEADRILIHSLRQAGTAVPPDVQTLRAFTTELVVEAVVRCLRVINPAVGSGLSPLLPLAMSARFRLAMSLAQACMDLGYPLELGYQNFLYPSEPDLRDLLLFLAERLPTDASEDADQSAGESAILLRAIGSRIRDHLALPWVPPLLRTPKLQYLQGSAHQKPFHASRLVMPELSSRGESREFQAGPLLLPVPAQVPQPAARAASLLEHHAIQLCQHTGRDRAGDEDWGHRTSRLPAQEDTRAQRQRLQKHLAEHLRQTWGRPGPPQQARDLGEVLQAWGAGARPGTPKGSRFTHSKKFTFHLEPEAQAAQVSDVPATSQRPEQDTWAAQEQELESLREQLEGVNHNIEEVEANMKTLGINLVQVETECRQSELSIVEREQALRLKSQAVELLPDGAANLAKLQLVVESSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKDAKKDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETEMGKKTLSNLDKIREDYRALRQENAGLLGRVREA", "text": "FUNCTION: Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. The CCC complex associates with SNX17, retriever and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGA5:ITGB1. Plays a role in copper ion homeostasis. 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 within the CCC complex and cooperation with the WASH complex on early endosomes. SUBCELLULAR LOCATION: Endosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the CCDC22 family."}
+{"protein": "MAATATEKLPQLKSAVDGLTEMSENEKSGFINLVSRYLSGEAQHIEWSKIQTPTDEIVVPYDKMANVSEDASETKYLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYNCKVPLVLMNSFNTHDDTQKIVEKYTKSNVDIHTFNQSKYPRVVADEFVPWPSKGKTDKDGWYPPGHGDVFPSLMNSGKLDAFLSQGKEYVFIANSDNLGAIVDLKILKHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPNPKEVDGVKVLQLETAAGAAIRFFDNAIGVNVPRSRFLPVKATSDLLLVQSDLYTLVDGFVTRNKARTNPTNPAIELGPEFKKVASFLSRFKSIPSIVELDSLKVSGDVWFGSGVVLKGKVTVKANAGTKLEIPDNAVLENKDINGPEDL", "text": "FUNCTION: Converts glucose 1-phosphate to UDP-glucose, which is the major glycosyl donor for polysaccharides. Acts redundantly with UGP2 and is essential for the synthesis of sucrose, starch and cell wall, and callose deposition (PubMed:19366709, PubMed:20435647). Involved in the regulation of the programmed cell death (PCD) induced by the fungal toxin fumonisin B1 (FB1) (PubMed:23438466). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UDPGP type 1 family."}
+{"protein": "MLTNLRIFAMSHQTIPSVCINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLHSIINPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVTKEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFSENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEECNCEFLQWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNSEAERLVLAGVEIPEPVFFCTIEPPSVSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHIEIIHDRIKREYGLEAYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPTETTSVMPVIEYAESIHEGLLKVSQEAIENGIYSACLQGPLLGSPIQDVAITLHSLTIHPGTSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQTRQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTNQAMNPQDQNTLLNRRSGLT", "text": "FUNCTION: Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. 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": "MTTATTLGDAVFSLNMTRGEDILYKSSGAIVAAIVVVVVIIVTLVLILLKMYNRRMRTRRELEPKSPKPPVPPALDPNSNGSQQPAAVTSDPADVPVETR", "text": "FUNCTION: Plays a role in myelin formation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Localized mainly in the Schmidt- Lanterman incisures and paranodes of noncompact peripheral nerve myelin."}
+{"protein": "MSAIAPGMILIAYLCGSISSAILVCRLCGLPDPRTSGSGNPGATNVLRIGGKGAAVAVLIFDVLKGMLPVWGAYELGVSPFWLGLIAIAACLGHIWPVFFGFKGGKGVATAFGAIAPISWDLTGVMAGTWLLTVLLSGYSSLGAIVSALIAPFYVWWFKPQFTFPVSMLSCLILLRHHDNIQRLWRRQETKIWTKFKRKREKDPE", "text": "FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl- PO(4). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PlsY family."}
+{"protein": "MSTKKIMLKSSEGKTFEIEEETARQCQTIAHMIEAECTDNVILVLKMTSEILEMVIEYCNKHHVDAANPCSDDDLEKWDKEFMEKDKSTIFALTNAANFLNNKSLLHLAGQTVADMIKGNTPKQMREFFNIENDLTPEEEAAIRRENKWAFE", "text": "FUNCTION: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SKP1 family."}
+{"protein": "MGKGWNASFHLGRRERLRQEVLHRVAGGPRPAPRDYTGHDGTHGSYYMKGWQSVDMPEILHHCLLYREKHYV", "text": "SUBCELLULAR LOCATION: Host cytoplasm."}
+{"protein": "MTPAKIRNALLAVVAIALSAAVYLGFQTQTQGISLEAQAQRAIPLATALDNGRPTLVEFYADWCTSCQAMAPDLAELKKNYGGSVNFAMLNVDNNKWLPEVLRYRVDGIPHFVYLDDTGTAIAESIGEQPLRVLEQNITALVAHEPIPYANVTGQTSVVENRTIEADPTSPRSHGNPRPS", "text": "FUNCTION: Required for disulfide bond formation in some proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the thioredoxin family."}
+{"protein": "MSQTHKHAIPANIADRCLINPEQYETKYKQSINDPDTFWGEQGKILDWITPYQKVKNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGVRAGRSIPLKKNVDDALKNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAIAMPS", "text": "FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs 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. Required for acetate recapture but not for acetate excretion when this organism is grown on ethanolamine (PubMed:16272400). FUNCTION: Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MASPPAHRSSKAADEELPKASSTFHPSLWGSFFLTYQPPTAPQRANMKERAEVLRERVRKVLKGSTTDQLPETVNLILTLQRLGLGYYYENEIDKLLHQIYSNSDYNVKDLNLVSQRFYLLRKNGYDVPSDVFLSFKTEEGGFACAAADTRSLLSLYNAAYLWKHGEEVLDEAISSTRLRLQDLLGRLLPESPFAKEVSSSLRTPLFRRVGILEARNYIPIYETEATRNEAVLELAKLNFNLQQLDFCEELKHCSAWWNEMIAKSKLTFVRDRIVEEYFWMNGACYDPPYSLSRIILTKITGLITIIDDMFDTHGTTEDCMKFAEAFGRWDESAIHLLPEYMKDFYILMLETFQSFEDALGPEKSYRVLYLKQAMERLVELYTKEIKWRDEDYVATMSEHLQVSAESIGANALTCSAYAGMGDMSITKETFEWALSFPQFIRTFGSFVRLSNDVVSTKREQTKDHSPSTVHCYMKEHGITMDDACEKIKELIEDSWKDMLEQSLALKGLPKVVPQLVFDFSRTTDNMYRDRDALTSSEALKEMIQLLFVEPIPE", "text": "FUNCTION: Non-functional sesquiterpene synthase having less than 1% of the activity found in TPS5A. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MFKNRKSIAILIAAVSITMIGFSYGSVPLYRIFCQVTGFGGTTQVADLESDILTLKDEQQENRIITVRFNGDVSDTMPWKFHPIQQEIKVMVGETALAFYSAENPTDSSIIGISTYNVNPQQAGIYFNKIQCFCFEEQRLKPHETIDMPVFFFIDPAILDDPKMSDIDSITLSYTFFNVEDL", "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. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side. SIMILARITY: Belongs to the COX11/CtaG family."}
+{"protein": "MRIDQSIINEIKDKTDILDLVSEYVKLEKRGRNYIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFVEAVKELGDRVNVAVDIEATQSNSNVQIASDDLQMIEMHELIQEFYYYALTKTVEGEQALTYLQERGFTDALIKERGIGFAPDSSHFCHDFLQKKGYDIELAYEAGLLSRNEENFSYYDRFRNRIMFPLKNAQGRIVGYSGRTYTGQEPKYLNSPETPIFQKRKLLYNLDKARKSIRKLDEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTSNITLMFDGDFAGSEATLKTGQNLLQQGLNVFVIQLPSGMDPDEYIGKYGNDAFTAFVKNDKKSFAHYKVSILKDEIAHNDLSYERYLKELSHDISLMKSSILQQKALNDVAPFFNVSPEQLANEIQFNQAPANYYPEDEYGGYIEPEPIGMAQFDNLSRQEKAERAFLKHLMRDKDTFLNYYESVDKDNFTNQHFKYVFEVLHDFYAENDQYNISDAVQYVNSNELRETLISLEQYNLNDEPYENEIDDYVNVINEKGQETIESLNHKLREATRIGDVELQKYYLQQIVAKNKERM", "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": "MASSLTRNCSRFSKAISVRFMSNLPENTVYGGPKPQNPNQRVTLTHLRQKHRRGEPITVVTAYDYPSAVHLDTAGIDVCLVGDSASMVVHGHDTTLPISLDEMLVHCRAVARGAKRPLLVGDLPFGTYESSSSQAVDTAVRVLKEGGMDAIKLEGGSASRITAAKAIVEAGIAVIGHVGLTPQAISVLGGFRPQGRNIASAVKVVETAMALQEAGCFSVVLECVPPPVAAAATSALKIPTIGIGAGPFCSGQVLVYHDLLGMMQHPHHAKVTPKFCKQYANVGEVINKALMEYKEEVSKKVFPGPSHSPYKITASELDGFLTELQKLGFDKAASAAALAAENMEPSK", "text": "FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PanB family."}
+{"protein": "MFARIARINPKILPFVIGAPTIALCSYYYSSGAFLRNESSKVFIGDNNWIDLPISRIEEISHDTKRFTFKYPSQDSVSGLVVASALLTKFVTPKGSNVIRPYTPVSDVDEKGSLDLVIKHYPDGKMTNHIFSLKVNDTLSFKGPIPKWKWVPNSFESITLIGGGTGITPLYQLIHAITKNPNDKTKIRLFYSNKTSQDVLMKKELDELQAKYPDQLRITYFITTPDKGYKGESGFISKEFIASNADKPSPKSHVFVCGPPPFMNAYSGDKKSPTDQGELVGILKELGYTIDQVYKF", "text": "FUNCTION: May mediate the reduction of outer membrane cytochrome b5. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family."}
+{"protein": "MKSIQFCFFFCCWKAICCNGCELTNITITVEREECRFCISVNTTWCAGYCYTRDLVYRDPARPNIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATECQCGKCDSDSTDCTVRGLGPSYCSFSEIKE", "text": "FUNCTION: Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways. Follitropin is involved in follicle development and spermatogenesis in reproductive organs. SUBCELLULAR LOCATION: Secreted Note=Efficient secretion requires dimerization with CGA. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family."}
+{"protein": "MESNSSQCEDETPSLLWGLDPVFLAFAKLYIRDILDLKESGQVQGVFFYNGHPIKQVDILGTVIGVREKDAFYSYGVDDSTGVINCICWKRLNNTKSSSATATPSARELSLTSQLKKLQETIAQRAKLEIGDIIRVRGHIRMFRGEREIHATTYYKVDDPVCNVQIARMLELPAIYRKVYDQPFHSPALKEDEALSNPGTLDLDSLTCLLSEKAKEFLVENRVQSFYQQELETVESLLSLANQPVIHSACSGQMGFKNDTTSRAIHSIFRNAVKLLQEEGLVFQKDGGFDNLFYVTREDKELHRKIHRIIQEECQKPNHVEKGCHFLHILACARLSLSPGLSEPVLQQVLQLLEDQSDIVSTTEKYYTAF", "text": "FUNCTION: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation. However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha. The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins. Required for efficicient replication of the duplex region of the telomere. Promotes efficient replication of lagging-strand telomeres. Promotes general replication start following replication-fork stalling implicating new origin firing. May be in involved in C-strand fill-in during late S/G2 phase independent of its role in telomere duplex replication (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the STN1 family."}
+{"protein": "MWQVLRGWRKGWQSPRGALAWAVQGQPCPPCSRAVASVGKDEYTFVVVGAGSAGCVLASRLTEDPNHRVLLLEAGPKDLLMGSKRLQWKIHMPAALVSNLCDDKYNWYYHTEPQPGMDSRVLYWPRGRVWGGSSSLNAMVYIRGHAEDYNRWHREGAEGWDYAHCLPYFRKAQRHELGANMYRGGDGPLHVSRGKTNHPLHQAFLQAARQAGYPFTEDMNGFQQEGFGWMDMTVHQGKRWSTACAYLHPVLSRPNLRAEVQTLVSRVLFEGTRAVGVEYIKDGQRHKAYVSREVILSGGAINSPQLLMLSGVGNADDLRKLDIPVVCHLPGVGQNLQDHLEVYVQQACTQPITLHSAQKPLRKVCIGLEWLWSYTGDGATAHLETGGFIRSRPGVPHPDIQFHFLPSQVIDHGRKPTQQEAYQVHVGTMRATSVGWLKLRSANPRDHPVIHPNYLSTETDVEDFRQCVRLSREIFAQEALAPFRGKELQPGSHVQSDKEIDAFVRAKADSAYHPSCTCKMGRSSDPTAVVDAQTKVIGVENLRVVDASIMPSVVSGNLNAPTVMIAEKAADIIKGHPALEDKNVPVYKPQTLDTQR", "text": "SUBCELLULAR LOCATION: Mitochondrion inner membrane. SIMILARITY: Belongs to the GMC oxidoreductase family."}
+{"protein": "MQNINQIKLTWISFFSYAFTGALIVITGMIMGDIADYFNLSVSEMSNIFTFLNAGILISIFLNSWLIDLISIKKQLIFGFLFSIIAILGIVFSTSILLFSINIFILGLVSGITMSIGTFIITCLYSGEKRGSQLLLTDSFFSMSGMIFPIISAYLLDRKILWYWIYVFLGIIYFLIFILTVKSHFPVSEEKTKNNNEIKNLNINIILLSISALLYILGQLSFISWVPQYTTEIININIKKTGVLVSNFWMAYMIGMWCFSFIIKFFNLQRMFIFLTGSSSVLMYCFIYSKSYLALKYTIISLGFFSSAIYTIIITLASLETKKPSAKLINLILFFGTIGTLLTFIITSPIVAKKGLYTTLIFSNVLYVIVFFLSCIIFKNSKKKDHC", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TsgA family."}
+{"protein": "MSDHPLKEMSDNNRSPPLPEPLSSRYKLYESELSSPTWPSSSQDTHPALPLLEMPEEKDLRSSDEDSHIVKIEKPNERSKRRESELPRRASAGRGAFSLFQAVSYLTGDMKECKNWLKDKPLVLQFLDWVLRGAAQVMFVNNPLSGLIIFIGLLIQNPWWTIAGALGTVVSTLAALALSQDRSAIASGLHGYNGMLVGLLVAVFSEKLDYYWWLLFPVTFASMACPVISSALSTVFAKWDLPVFTLPFNIALTLYLAATGHYNLFFPTTLVKPASSAPNITWSEIEMPLLLQTIPVGVGQVYGCDNPWTGGVILVALFISSPLICLHAAIGSIVGLLAALTVATPFETIYTGLWSYNCVLSCVAIGGMFYVLTWQTHLLALVCALFCAYTGAALSNMMAVVGVPPGTWAFCLSTLTFLLLTSNNPGIHKLPLSKVTYPEANRIYFLTAKRSDEQKPPNGGGGEQSHGGGQRKAEEGSETVFPRRKSVFHIEWSSIRRRSKVFGKSEHQERQTKEPLPYLYRKPTVELLDLNTMEESSEIKVETNTTRTTWIQSSMIAGGKRVSKALSYITGEMKECGEGLKDKSPVFQFLDWVLRGTSQVMFVNNPLSGILIVLGLFVQNPWWAISGCLGTIMSTLTALILSQDKSAIAAGLHGYNGVLVGLLMAVFSDKGNYYWWLLLPVIVMSMTCPILSSALSTVFSKWDLPVFTLPFNIAVTLYLAATGHYNLFFPTKLLQPAVTTPNITWSDVQVPLLLRAIPVGIGQVYGCDNPWTGGIFLVALFVSSPLICLHAAIGSTIGMLAALSIATPFDSIYFGLCGFNSTLACIAIGGMFYVITWQTHLLAIACALFAAYLGAALANMLSVFGLPPCTWPFCLSALTFLLLTTNNPGIYKLPLSKVTYPEANRIYFLSQEKNRRASMITKYQAYDVS", "text": "FUNCTION: [Isoform 4]: Mediates the transport of urea driven by a concentration gradient across the cell membrane of the kidney inner medullary collecting duct which is critical to the urinary concentrating mechanism. FUNCTION: [Isoform 2]: Mediates the transport of urea driven by a concentration gradient across the cell membrane of the kidney inner medullary collecting duct which is critical to the urinary concentrating mechanism. FUNCTION: [Isoform 1]: Mediates the transport of urea driven by a concentration gradient across the cell membrane of the kidney inner medullary collecting duct which is critical to the urinary concentrating mechanism. FUNCTION: [Isoform 3]: Mediates the transport of urea driven by a concentration gradient across the cell membrane of the kidney inner medullary collecting duct which is critical to the urinary concentrating mechanism. SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Vasopressin increases expression in the cell membrane. SIMILARITY: Belongs to the urea transporter family."}
+{"protein": "MSTREENVYMAKLAEQAERYEEMVEFMEKVAKTVDVEELSVEERNLLSVAYKNVIGARRASWRIISSIEQKEESKGNEDHVAIIKDYRGKIESELSKICDGILNVLEAHLIPSASPAESKVFYLKMKGDYHRYLAEFKAGAERKEAAESTLVAYKSASDIATAELAPTHPIRLGLALNFSVFYYEILNSPDRACSLAKQAFDDAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMTDEAGDEIKEASKPDGAE", "text": "FUNCTION: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes (PubMed:7972511, PubMed:7870824, PubMed:16407442). Involved in the regulation of nutrient metabolism (PubMed:22104211, PubMed:21094157). Reciprocal negative transcription regulation of miR396 (PubMed:22751317). Negative regulator of constitutive freezing tolerance and cold acclimation by controlling cold-induced gene expression partially through an ethylene (ET)-dependent pathway; prevents ethylene (ET) biosynthesis, probably by binding 1- aminocyclopropane-1-carboxylate synthases (ACS) to reduce their stability, thus contributing to establish adequate ET levels under both standard and low-temperature conditions (PubMed:25122152). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates from the cytosol to the nucleus when phosphorylated. SIMILARITY: Belongs to the 14-3-3 family."}
+{"protein": "MNALNIGRNDFSEIELAAIPYNILSEHYGDQAAREQLALEHEAYELGRQRFLKMLERQVKAGEFADNAAAKPLVLTLHPQLTKRIDDWKEEQANARGKKPRAYYPIKHGVASELAVSMGAEVLKEKRGVSSEAIALLTIKVVLGNAHRPLKGHNPAVSSQLGKALEDEARFGRIREQEAAYFKKNVADQLDKRVGHVYKKAFMQVVEADMISKGMLGGDNWASWKTDEQMHVGTKLLELLIEGTGLVEMTKNKMADGSDDVTSMQMVQLAPAFVELLSKRAGALAGISPMHQPCVVPPKPWVETVGGGYWSVGRRPLALVRTHSKKALRRYADVHMPEVYKAVNLAQNTPWKVNKKVLAVVNEIVNWKHCPVGDVPAIEREELPPRPDDIDTNEVARKAWRKEAAAVYRKDKARQSRRCRCEFMVAQANKFANHKAIWFPYNMDWRGRVYAVSMFNPQGNDMTKGSLTLAKGKPIGLDGFYWLKIHGANCAGVDKVPFPERIKFIEENEGNILASAADPLNNTWWTQQDSPFCFLAFCFEYAGVKHHGLNYNCSLPLAFDGSCSGIQHFSAMLRDSIGGRAVNLLPSDTVQDIYKIVADKVNEVLHQHAVNGSQTVVEQIADKETGEFHEKVTLGESVLAAQWLQYGVTRKVTKRSVMTLAYGSKESLVRQQVLEDTIQPAIDNGEGLMFTHPNQAAGYMAKLIWDAVTVTVVAAVEAMNWLKSAAKLLAAEVKDKKTKEVLRKRCAIHWVTPDGFPVWQEYRKQNQARLKLVFLGQANVKMTYNTGKDSEIDAHKQESGIAPNFVHSQDGSHLRMTVVHANEVYGIDSFALIHDSSGTIPADAGNLFKAVRETMVKTYEDNDVIADFYDQFADQLHESQLDKMPAVPAKGDLNLRDILESDFAFA", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase family."}
+{"protein": "MECDKCGRDAVMHAAYSGAHLCDDHFCASVEKRVRRRIREDNMLPRDASPENPQTWVIGLSGGKDSVVLTHILDDTFGRDPRIELVALTIHEGIEGYRDKSVDACVELAEDLDIHHELVTYEDEFGVQMDDVVEKDPENMAACAYCGVFRRDLLERFADELGADKLLTGHNLDDEAQTALMNFFEGDLKQVAKHFDASIGDFEKRRDAGEFIPRAKPLRDVPEKEVALYAHLKDLPAHITECPHSSEAYRGEIQQLLLKLEENHPGTRHSIMAGYEELAELTAREYRGEGRVDLNDCERCGSKTAGDVCRKCRLIESIEAV", "text": "FUNCTION: Required for thiolation of mcm(5)S(2)U at the wobble uridine position of tRNA specific for lysine (tRNA(Lys)). Probably acts by catalyzing adenylation of tRNA, an intermediate required for 2- thiolation. May also act as a sulfurtransferase that transfers sulfur from thiocarboxylated SAMP2 onto the uridine of tRNA at wobble position. Required for cell growth at elevated temperatures. SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily."}
+{"protein": "MATSGRLLCFCLVLGLVFESLGYSEARPPRDRKRTVTAKRYDPLAQRVDCGGSPCAFGCCENDVCRELDCEYAPPFGF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the teretoxin M (TM) superfamily."}
+{"protein": "MRLHLLLLLALCGAGTTAAELSYSLRGNWSICNGNGSLELPGAVPGCVHSALFQQGLIQDSYYRFNDLNYRWVSLDNWTYSKEFKIPFEISKWQKVNLILEGVDTVSKILFNEVTIGETDNMFNRYSFDITNVVRDVNSIELRFQSAVLYAAQQSKAHTRYQVPPDCPPLVQKGECHVNFVRKEQCSFSWDWGPSFPTQGIWKDVRIEAYNICHLNYFTFSPIYDKSAQEWNLEIESTFDVVSSKPVGGQVIVAIPKLQTQQTYSIELQPGKRIVELFVNISKNITVETWWPHGHGNQTGYNMTVLFELDGGLNIEKSAKVYFRTVELIEEPIKGSPGLSFYFKINGFPIFLKGSNWIPADSFQDRVTSELLRLLLQSVVDANMNTLRVWGGGIYEQDEFYELCDELGIMVWQDFMFACALYPTDQGFLDSVTAEVAYQIKRLKSHPSIIIWSGNNENEEALMMNWYHISFTDRPIYIKDYVTLYVKNIRELVLAGDKSRPFITSSPTNGAETVAEAWVSQNPNSNYFGDVHFYDYISDCWNWKVFPKARFASEYGYQSWPSFSTLEKVSSTEDWSFNSKFSLHRQHHEGGNKQMLYQAGLHFKLPQSTDPLRTFKDTIYLTQVMQAQCVKTETEFYRRSRSEIVDQQGHTMGALYWQLNDIWQAPSWASLEYGGKWKMLHYFAQNFFAPLLPVGFENENTFYIYGVSDLHSDYSMTLSVRVHTWSSLEPVCSRVTERFVMKGGEAVCLYEEPVSELLRRCGNCTRESCVVSFYLSADHELLSPTNYHFLSSPKEAVGLCKAQITAIISQQGDIFVFDLETSAVAPFVWLDVGSIPGRFSDNGFLMTEKTRTILFYPWEPTSKNELEQSFHVTSLTDIY", "text": "FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the glycosyl hydrolase 2 family."}
+{"protein": "MSVASDSPVHSSSSSDDLAAFLDAELDSASDASSGPSEEEEAEDDVESGLKRQKLEHLEEASSSKGECEHPGSFGNMCFVCGQKLEETGVSFRYIHKEMRLNEDEISRLRDSDSRFLQRQRKLYLVLDLDHTLLNTTILRDLKPEEEYLKSHTHSLQDGCNVSGGSLFLLEFMQMMTKLRPFVHSFLKEASEMFVMYIYTMGDRNYARQMAKLLDPKGEYFGDRVISRDDGTVRHEKSLDVVLGQESAVLILDDTENAWPKHKDNLIVIERYHFFSSSCRQFDHRYKSLSELKSDESEPDGALATVLKVLKQAHALFFENVDEGISNRDVRLMLKQVRKEILKGCKIVFSRVFPTKAKPEDHPLWKMAEELGATCATEVDASVTHVVAMDVGTEKARWAVREKKYVVHRGWIDAANYLWMKQPEENFGLEQLKKQLTEEE", "text": "FUNCTION: Processively dephosphorylates 'Ser-2' and/or 'Ser-5' 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 (By similarity). Required for normal plant growth. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "QDLPGNDNSTATLCLGHHAVPNGTLVKTITNDQIEVTNATELVQSSSTGKICNNPHRILDGINCTLIDALLGDPHCDVFQDETWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGGSNACKRGPDSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFDKLYIWGVHHPSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGLSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQT", "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 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": "MALEALTSPRLASPIPPLFEDSSVFHGVEHWTKGKRSKRSRSDFHHQNLTEEEYLAFCLMLLARDNRQPPPPPAVEKLSYKCSVCDKTFSSYQALGGHKASHRKNLSQTLSGGGDDHSTSSATTTSAVTTGSGKSHVCTICNKSFPSGQALGGHKRCHYEGNNNINTSSVSNSEGAGSTSHVSSSHRGFDLNIPPIPEFSMVNGDDEVMSPMPAKKPRFDFPVKLQL", "text": "FUNCTION: Transcriptional repressor involved in abiotic stress responses. Can repress the stress responsive genes DREB1A and LTI78. Probably involved in jasmonate (JA) early signaling response. May regulate the expression of the JA biosynthesis gene LOX3 and control the expression of TIFY10A/JAZ1, a key repressor in the JA signaling cascade. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MATRPGPLTEWPWHRLGNFKYVVMAPVVAHGARRVMRNGWGDLDIAFSLILPSLLLRMIHNQIWISLSRYQTARSKHRIVDRGIEFDQVDRERGWDDQILFNGLVFYAGYLAMPSVRRMPVWRTDGAVVTALVHTGPVEFLYYWFHRALHHHFLYSRYHSHHHASIVTEPITSVIHPFAEHVVYFILFAIPILSTIYLGNVSAMGIVGYIAYIDFMNNMGHCNFELVPEWIFQIFPPLKYLIYTPSFHSLHHTQFRTNYSLFMPFYDYIYNTMDKSSDELYESSLKGTEETPDLVHLTHMTNLQSAYHLRIGIASIASKPYSDSAWYMWTLWPLAWLSMVLAWIYGSSAFVVERIKLNKMKMQTWALPRYNFQYGLTWEREPINDLIEKAILDADMKGVKVISLGLLNQAKQLNGNGELFRQKYPKLGVRIIDGSGLATAVVLKSIPSDAKKVFLRTGTSKIARAIAIALCDRGVQVIMNEKEVYHMLKSQIPENRASYLKLSSDNVPQLWIVHNIDDNEQKMAPKGTIFIPISQFPLKKLRKDCTYMSTPAMRIPEEMKNIHSCENWLPRRVMSAWHIAGILHALEGWNMHECGDEMMDIEKSWSAAIRHGFLPLTKA", "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": "RVCRRRSAGFKGLCMSDHNCAQVCLQEGWGGGNCDGVMRQCKCIRQC", "text": "SIMILARITY: Belongs to the DEFL family. Protease inhibitor I18 (RTI/MTI-2) subfamily."}
+{"protein": "MSNATNNTLGSLLPQLEAAANSNSLYGGMVPNLRFNITMIVIWGILLTIHVVQLLMRQYWFSIAFICTGILEVLGFIGRTWSHSNVADMDAFLLNMICLTIAPVFTMGGIYYQLAKLIEVYGHRFSLLPSPMAYSFIFICSDIVSLVVQAVGGGLCGVAVTDGTSTTTGNHVFIAGLAIQVASMAIFLMLWFHFLFRIYISVRWEHINSRPISLSLLKISQTEVDYLYREKFHFLRLEPKRWVFHYFNLAMTVAVLTIFTRCCYRLAELVVGWDGYLITHEWYFIILDALMMAIATVTLTIFHPGFAFKGRSTSIPITPGHVDPETLPHTDDVEDILDTSDSKQFDIEKEEFQASMKYPISTFKQFMSKIANLFSSKKKAKL", "text": "FUNCTION: Catalyzes the ATP-dependent translocation of sphingoid long- chain bases (LCBs) from the cytoplasmic site toward the extracytoplasmic side of the membrane (flip-flop). Involved in the establishment of the functional lipid asymmetry of the plasma membrane. Regulates intracellular levels of LCBs, sphingolipid precursors that are growth inhibitory at increased levels (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the lipid-translocating exporter (LTE) (TC 9.A.26.1) family."}
+{"protein": "MAAAARWAALGLALWLCAAAHAEEPEGKRRAGPAKKKDIRDYNDADMARLLEQWEKDDDIEEGDLPEHKRPPAPIDFSKIDPGKPESILKLTKKGKTLMMFVTVSGNPTEKETEEITSLWQGSLFNANYDVQRFIVGSNRAIFMLRDGGYAWEIKDFLISQERCADVTLEGQVYPGKGADGSEKGRNKTKPEKAKKKKDAEKSKSSHEDNRAQTKQREDL", "text": "FUNCTION: Chaperone specifically assisting the folding of beta- propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway, since some LDLRs are coreceptors for the canonical Wnt pathway (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the MESD family."}
+{"protein": "MLADGQIFTALAVALVPGILALRLALELYKF", "text": "SUBCELLULAR LOCATION: Plastid, cyanelle thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaM family."}
+{"protein": "MTFVVTDNCIKCKYTDCVEVCPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPSGMENFIELNAELAEIWPNITERKDALPDAEEWDGKPGKIADLER", "text": "FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions."}
+{"protein": "MPGSALLSLQQELRRGFEALKAAKDTFDGGHAECQELVSSLGNLAPQLKALKQVQISETPLSGFPCLQQRLHYKLSLAVDALLAKLAEKMAALQKVWDAFAQQVFTVVQLYEKNTDALDISVCVSRSAVCPSVSDMLEWLQDADRYYRLQLMQSRLLLQTLTPTDLTSMETAPNRWRSVRSARQEERIADALCQVSIFLETE", "text": "FUNCTION: Involved in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles (By similarity). Plays an essential role in early embryonic development (PubMed:12006978). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MQSDDVIWDTLGNKQFCSFKIRTKTQSFCRNEYSLTGLCNRSSCPLANSQYATIKEEKGQCYLYMKVIERAAFPRRLWERVRLHKNYEKALEQIDENLIYWPRFIRHKCKQRFTKITQYLIRIRKLTLKRQRKLVPLSKKVERREKRREEKALIAAQLDNAIEKELLERLKQDTYGDIYNFPIHAFDKALEQQEAESDSSDAEEKDDEEDEEDVGKREFVEDDEVDESDISDFEDMDKLDASSDEDQDDKSSSEEEEKTLDAKHKGKTPLKGPLRRKRAYVEIEYEQETEPAAKAKTT", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the MAK16 family."}
+{"protein": "MELLSPPLRDVDLTGPDGSLCNFATADDFYDDPCFDSPDLRFFEDLDPRLVHVGALLKPEEHSHFPAAAHPAPGAREDEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSSNPNQRLPKVEILRNAIRYIEGLQALLRDQDAAPPGAAAAFYAPGPLPPGRSGEHYSGDSDASSPRSNCSDGMMDYSGPPSGARRRNCYDRAYYSEAPNEPRPGKSAAVSSLDCLSSIVERISTESPAAPALLLADAPPESSPGPQEAAAGSEVECGTPAPSPDTAPQGLAGANPNPIYQVL", "text": "FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. 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": "MKTSVMDLKVEPMDIDFDQPPPLQVFAHTSTLHGISHIFSYEKITAKCCLWVVFFLSSLTFLMYVCIDRIQFYLEYPHVTKLDEITTPVMVFPAVTICNLNSIRFSRITRNDLYHAGELLALLNSRHEVREAHLVEESVMEVLKSKTDFRSFKPRHFNMWEFYNRTGHDIKDMLLSCQFRGSPCRPEDFSVVFTRYGKCYTFNSGETGPPRVSVKGGMGNGLEIMLDIQQDEYLPVWGESDESSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVSCQEQRLVYLPAPWGSCKSTPPSSDYFRAYSISACRTDCETRYLVENCNCRMVHMPGDAPYCTPVLYKECAHPALDFLVETDSDYCSCETPCNITRYSKELSFVKIPSKASVKYLAKKYSKSEKYITENVMVLDVFFEALNYETIEQRKAYEVAGLLGDIGGQMGLFIGASILTILELFDYLYEVMKYRLCRCSNKKHHNNNNNTDHNAVFSLDDVNCHVSKFH", "text": "FUNCTION: Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC1 subfamily."}
+{"protein": "MNSVPNDLQTWKRFVKDGVLDEARLRKRIAESWHRCKKAEVNPYLEKGPKVLQQTELDQQSKKHSFFLTTAKPYLEKLLPAIKEMEMMALLIDSDGVVLALDGHPRALYEAKRINFVEGACWTETAVGTNAIGTALHISEPVAIQGSEHYSIASHLWNCSAAPIHHEDGSLAGVIDISCPAAGAHPHMLGIATAIAYAAERELAAKSREKELELISRFGERAASSVPMVLCNTKQHIISASMPIRTSMPDWQGRHLYELKERGYSIENAVTIGDGGTCFYLSEQKKKKAFRFNGVIGQSGRSQAMLMHLERAAATDASVCLSGETGTGKEVAARALHENSERRHGPFVAVNCGAIPSDLIESELFGYAEGAFTGAKRNGYKGAFQKANQGTLFLDEIGEISHSMQVALLRVLQERKITPIGGTKEIPVDIRVIAATHCDLRELAENGKIREDLFYRLHVYPIELPPLRDRTEDIPDLFEYYKQKNHWPGDLPSDFCNVLKQWKWPGNIRELFNVFERLSIRFPDGRLRDESLPALLEAAGLPASSAEKKPAAAGVLTFREQIQKDMMIKALESAKGNVSQAAKISGIPRSTFYKRLKKFNLSAES", "text": "FUNCTION: Acts as a transcriptional activator of the acoABCL operon encoding the acetoin dehydrogenase complex."}
+{"protein": "MYKHILVAVDLSEESLILLRKGAGLAEKCGAKLSLIHVDVNFSDLYTGLIDINMSSVQDGVIEETTKALDELALKIDYPVSQRLNGTGDFSQVLEEAVAKYQIDLLITGHHQDFWSKFMSSTRQVMNNVTVDMLVVPLIDE", "text": "FUNCTION: Required for resistance to DNA-damaging agents. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal stress protein A family."}
+{"protein": "MGSSSGQKPRRLEDLVDKLASGSLSHSRLEKELGNANEAALVRRLYLERLTGASLSSVASTILDFQELYGRNIENPIGAVQVPVGVAGPLRINGDYARGDFYIPLATTEGALVASVNRGAKAITLSGGARAKVIKDGMTRAPLLWTPSVYEAHRLAMWVEDRIEDLRSVVAGVTRHGRLQHIYPYIIGNLVWLRLSFSTGDAMGMNMVTISSDRICRYIEENYDGDAKCIALSGNMCTDKKPAAINKILGRGKYVVAEAVIKGEVVKNVLKTTPQNINLVNVTKNLLGSAAAGSHSFNAHFANIIAAIFIATGQDAAQVVESSMGYTWTEVRGEDLYISVTLPSLEVGTVGGGTRLPTQRELLALLGVAGGGNPPGSNALKLAEIIASAVLAGELNLLSAIAAGQLARAHELLGRGGLKIS", "text": "FUNCTION: Converts HMG-CoA to mevalonate. SIMILARITY: Belongs to the HMG-CoA reductase family."}
+{"protein": "AAAAAVSGAKRSLRAELKQRLRAISAEERLRCQRLLTQKVIAHRQYQKSQRISIFLSMPDEIETEEIIKDIFQQGKVCFIPRYRLQSNHMDMVKLASADEISSLPKTSWNIHQPSESDTREEALATGGLDLIFMPGLGFDRNGNRLGRGRGYYDTYLQRCLQQQGAKPYTIALAFREQICPQVPVDDTDVSVDEVLYVDAA", "text": "FUNCTION: Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5- formyltetrahydrofolate (5-CHO-H(4)PteGlu) to yield 5,10- methenyltetrahydrofolate. It can also use 5-formyltetrahydropteroic acid (5-CHO-H(4)Pte) and 5-formyltetrahydropteroylhistidine (5-CHO- H(4)PteHis) as substrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase family."}
+{"protein": "MGTTTMGVKLDDATRERIKSAASRID", "text": "FUNCTION: Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon."}
+{"protein": "METDAPQPGLASPDSPHDPCKMFIGGLSWQTTQEGLREYFGQFGEVKECLVMRDPLTKRSRGFGFVTFMDQAGVDKVLAQSRHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSVNTTVEDVKHYFEQFGKVDDAMLMFDKTTNRHRGFGFVTFESEDIVEKVCEIHFHEINNKMVECKKAQPKEVMSPTGSARGRSRVMPYGMDAFMLGIGMLGYPGFQATTYASRSYTGLAPGYTYQFPEFRVERSPLPSAPVLPELTAIPLTAYGPMAAAAAAAAVVRGTGSHPWTMAPPPGSTPSRTGGFLGTTSPGPMAELYGAANQDSGVSSYISAASPAPSTGFGHSLGGPLIATAFTNGYH", "text": "FUNCTION: RNA binding protein that regulates the expression of target mRNAs at the translation level. Regulates expression of the NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU- 3' and other sequences containing the pattern 5'-[GA]U(1-3)AGU-3'. May play a role in the proliferation and maintenance of stem cells in the central nervous system. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the Musashi family."}
+{"protein": "MAIPITVLDCDLLLYGRGHRTLDRFKLDDVTDEYLMSMYGFPRQFIYYLVELLGASLSRPTQRSRAISPETQILAALGFYTSGSFQTRMGDAIGISQASMSRCVANVTEALVERASQFIHFPADEASVQALKDEFYGLAGIPGVIGVVDCMHVAIKAPNAEDLSYVNRKGLHSLNCLMVCDIRGALMTVETSWPGSLQDCVVLQQSSLSSQFEAGMHKESWLLGDSSFFLRTWLMTPLHIPETPAEYRYNMAHSATHSVIEKTFRTLCSRFRCLDGSKGALQYSPEKSSHIILACCVLHNISLEHGMDVWSSPVTGPVEQPPEEEYEHMESLDLEADRIRQELMLTHFS", "text": "FUNCTION: Transposase-derived protein that may have nuclease activity (Potential). Does not have transposase activity (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Interaction with NAIF1 promotes translocation to the nucleus. SIMILARITY: Belongs to the HARBI1 family."}
+{"protein": "MTDQAAFDTNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKGSIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIILGSPEDVTELLEIYQKHAAK", "text": "FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain. SIMILARITY: Belongs to the FBPase class 1 family."}
+{"protein": "METDKRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGGFTVNGFSYAMKP", "text": "SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. SDR65C subfamily."}
+{"protein": "MLSFSLFIPSAAAAQTEENTDVAPNQYEKKDIEIDTNYLHEDTYYEEKTELPEEQKDITFDKPKDKDAELIKDLFTSTNAEDSNTIAAQSKQLGITFAEKPMTKTSSTETEDEQETSSLLLPMIYVVLILLGIAGIVFLIPKVTAQENKKA", "text": "FUNCTION: Required for YukE secretion. Probable component or regulator of the ESX/ESAT-6-like secretion system (BsEss). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the EssA family."}
+{"protein": "MKVSTTALAVLLCTMTLCNQVFSAPYGADTPTACCFSYSRKIPRQFIVDYFETSSLCSQPGVIFLTKRNRQICADSKETWVQEYITDLELNA", "text": "FUNCTION: Monokine with inflammatory, pyrogenic and chemokinetic properties. Has a potent chemotactic activity for eosinophils. Binding to a high-affinity receptor activates calcium release in neutrophils. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
+{"protein": "MSGLRAASVFSPVFKRMASSIPSQFKSIIYNSHSLEDCTGVLSVHNYKPKQDLNKSVVLRTLAFPINPSDINQLQGVYPSLPEKTLDYSTEKPSAIAGNEGLFEVVSLPEHGDHGELKVGDWVIPVQANQGTWSNYRVFDKASDLIKVNGLDLYSAATVSVNGCTAYQLVNNYVDWNADGNEWLIQNAGTSGVSKFVTQIAKARGVKTLSVIRDRDNFEEVAEVLEQKFGATKVISESQNNDKDFGKKELPKVLGDKARVRLALNSVGGKSSSAIARKLERDALMLTYGGMSKQPVTIPTSLHIFKGLTSKGYWVTENNKRDPTDKVNTIKGFIDLYKQGKIISPEEEIETMEWDANNGDDQQLLELVKRGITEKGKKKMVLLKW", "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": "ASTKGPSVFPLAPCSRSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYTCNVNHKPSNTKVDKRVELKTPLGDTTHTCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFKWYVDGVEVHNAKTKPREEQYNSTFRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESSGQPENNYNTTPPMLDSDGSFFLYSKLTVDKSRWQQGNIFSCSVMHEALHNRFTQKSLSLSPELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATVTFFKVKWIFSSVVDLKQTIIPDYRNMIGQGA", "text": "FUNCTION: Constant region of immunoglobulin heavy chains. 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:17576170, PubMed:20176268). SUBCELLULAR LOCATION: [Isoform 1]: Secreted. SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass membrane protein."}
+{"protein": "MSKFFYSSPNELDTEHQNENHNNQEPRLQSELLSTGNQVVQSPPLTERLHEWRNLLIHQYNVVVAEWSNLKSATKNEIDSGREYINRNVLNDPQENNRLLVPSSILSLGAFFCGRVLTNKNNWGYRSIVNRNPSILGRLLTSLPSRTVLPLALAGVVFNQLTPGTAKNACHTFERDFLSESFVQEYHRIWDQLYVQGIKQGSGQIGETFQNSLQNGIKSIRESISAINDDKKQ", "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; Multi-pass membrane protein. SIMILARITY: Belongs to the apolipoprotein O/MICOS complex subunit Mic27 family."}
+{"protein": "MKFALFSVLVLMLIATFVAADDCPRICTSDYTPVCGTPSGGRRSANRTFANQCGLDSHNCLNKGDTYDKLHDGECK", "text": "FUNCTION: Vasodilator protein that inhibits vasoconstriction of isolated rat femoral artery induced by phenylephrine. Since platelet aggregation and vasoconstriction are key hemostatic responses, particularly in small wounds, this protein likely participates in the antihemostatic responses during blood feeding. Blocks L-type calcium channels (Cav1/CACNA1) in left ventricular myocytes isolated from rat hearts. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "YGLELDNSIKADQEGHLEGDKTWVVKGDYEYVSKEGK", "text": "FUNCTION: Component of the cuticle of the larva of flesh fly."}
+{"protein": "MSFIHKLIQKFKPKKKLVDQVQQAVQEKSFFQANQKSYYQGLNKSANSFANTINKLAANYVTVNEQFQESLFEELVLLDIGYHAATKICDAIVQELKLQRVSDPQLIQEIIVDKLIVYYIQDKLFETDLTVEANKTNVYLFVGVNGVGKTTSLAKLADQLTKQNKRVLMVAGDTFRAGAVAQLAEWAQRIGCDIVLPNPKEETPAVIFRGVQQGIQNEYDFVLCDTSGRLQNKTNLMNELKKIYQIVQKVSSAKPQETLLVLDGTTGQSGLAQAKVFNEFTELTGIILTKMDSSSKGGIILAIKDLFNLPVKLIGFGETTADLAAFDLEQYVLGLTKNLSLNHEPNQT", "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 membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily."}
+{"protein": "MLRSTLSRSAWRTGRHQAARNASRAFSATAQRPAEVELTIDGKKVSIEAGSALIQACEKAGVTIPRYCYHEKLMIAGNCRMCLVEVEKVPKPVASCAWPVQPGMVVKTNSPLTHKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMRYGGDRGRFHEVGGKRAVEDKNMGPLIKTSMNRCIQCTRCVRFANDIAGAPELGSTGRGNDLQIGTYLEKNLDSELSGNVIDLCPVGALTSKPYAFRARPWELKKTESIDVLDGLGSNIRVDTRGLEVMRILPRLNDEVNEEWINDKTRFACDGLKTQRLTIPLVRREGKFEPASWDQALTEIAHAYQTLNPQGNEFKAIAGQLTEVESLVAMKDLANRLGSENLALDMPSGHKPLAHGVDVRSNYIFNSSIVGIESADVILLVGTNPRHEAAVLNARIRKQWLRSDLEIGVVGQTWDSTFEFEHLGTDHAALQKALEGDFGKKLQSAKNPMIIVGSGVTDHGDANAFYETVGKFVDSNASNFLTEEWNGYNVLQRAASRVGAFEVGFTVPSAEIAQTKPKFVWLLGADEFNEADIPKDAFIVYQGHHGDRGAQIADIVLPGAAYTEKAGTYVNTEGRVQMTRAATGLPGAARTDWKILRAVSEYLGVRLPYDDVAQLRDRMVEISPALSSYDIIEPPSLQQLSKVQLVEQNQGATATNEPLKKVIENFYFTDAISRSSPTMARCSAAKKTGDPRTNFMAPGMEEDRPMGQIAYGA", "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. 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. SUBCELLULAR LOCATION: Mitochondrion inner membrane. SIMILARITY: Belongs to the complex I 75 kDa subunit family."}
+{"protein": "MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIREAGQR", "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:23185017, PubMed:26985301, PubMed:29298880). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:29298880). 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 (PubMed:18350175). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein Cytoplasm, cytosol Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane (PubMed:29298880). The interaction with the mitochondrial outer membrane via the mitochondrial-binding peptide (MBP) region promotes higher stability of the protein (PubMed:29298880). Release from the mitochondrial outer membrane into the cytosol induces permeability transition pore (PTP) opening and apoptosis (PubMed:18350175). SIMILARITY: Belongs to the hexokinase family."}
+{"protein": "MGNLLKVLTCTDLEQGPNFFLDFENAQPTESEKEIYNQVNVVLKDAEGILEDLQSYRGAGHEIREAIQHPADEKLQEKAWGAVVPLVGKLKKFYEFSQRLEAALRGLLGALTSTPYSPTQHLEREQALAKQFAEILHFTLRFDELKMTNPAIQNDFSYYRRTLSRMRINNVPAEGENEVNNELANRMSLFYAEATPMLKTLSDATTKFVSENKNLPIENTTDCLSTMASVCRVMLETPEYRSRFTNEETVSFCLRVMVGVIILYDHVHPVGAFAKTSKIDMKGCIKVLKDQPPNSVEGLLNALRYTTKHLNDETTSKQIRSMLQ", "text": "FUNCTION: Negatively regulates RAC1 signaling and RAC1-driven cytoskeletal remodeling (PubMed:31285585). Regulates chemotaxis, cell migration and epithelial polarization by controlling the polarity, plasticity, duration and extent of protrusions. Limits Rac1 mediated activation of the Scar/WAVE complex, focuses protrusion signals and regulates pseudopod complexity by inhibiting Scar/WAVE-induced actin polymerization (By similarity). Protects against Salmonella bacterial infection. Attenuates processes such as macropinocytosis, phagocytosis and cell migration and restrict sopE-mediated bacterial entry (PubMed:31285585). Restricts also infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes (PubMed:31285585). Involved in the regulation of mitochondrial dynamics and oxidative stress (PubMed:29059164). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Mitochondrion. SIMILARITY: Belongs to the CYRI family."}
+{"protein": "MSPDKTEDEDKDVNVDQDQFNEEEESLGRVILPNKKKGEMFGIVEKMEGASRLSVMCEDGYTRNARIPGRMRKRMWIREKDLVIVKPWEFQPEKADVVYRYTKTQASYLSRNHMLPEVIDIFK", "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": "MAFALPSSLVSVCNKSFIKPSSLTPSTLRFHKLSFIDQSLSNMYIPCAFFYPKVQQRLEDSKNSDELSHIAHLLQTSLSQTLVSYYPYAGKLKDNATVDCNDMGAEFLSVRIKCSMSEILDHPHASLAESIVLPKDLPWANNCEGGNLLVVQVSKFDCGGIAISVCFSHKIGDGCSLLNFLNDWSSVTRDRTTTTLVPSPRFVGDSVFSTQKYGSLITPQILSDLNQCVQKRLIFPTDKLDALRAKVAEESGVKNPTRAEVVSALLFKCATKASSSMLPSKLVHFLNIRTMIKPRLPRNAIGNLSSIFSIEATNMQDMELPTLVRNLRKEVEVAYKKDQVEQNELILEVVESMREGKLPFENMDGYKNVYTCSNLCKYPYYTVDFGWGRPERVCLGNGPSKNAFFLKDYKAGQGVEARVMLHKQQMSEFERNEELLEFIA", "text": "FUNCTION: Participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum annuum (PubMed:15918882, PubMed:25884984, PubMed:36296471). Capsaicinoids, the alkaloids responsible for the heat or pungency of chili pepper, are synthesized from phenylpropanoid intermediates in the placental tissue of chili peper fruit (Probable). Can transfer an acyl from (6E)-8-methylnon-6-enoyl-CoA to vanillylamine forming capsaicin and CoA (PubMed:15918882, PubMed:25884984, PubMed:36296471). SIMILARITY: Belongs to the plant acyltransferase family."}
+{"protein": "MADKEALPKLREDFKMQNKSVFILGASGETGKVLLKEILGQNLFSKVTLIGRRKLTFEEEAYKNVNQEVVDFEKLDVYASAFQGHDVGFCCLGTTRSKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSRGADKSSSFLYLQVKGEVEAKVEELKFDRLSVFRPGVLLCDRQESRPGEWLARKFFGSLPDSWASGYAVPVVTVVRAMLNNLVSPSSGQMELLENKAILHLGKDRDVPKL", "text": "FUNCTION: Oxidoreductase required for tumor suppression. NADPH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. SUBCELLULAR LOCATION: Cytoplasm Nucleus envelope."}
+{"protein": "MNLSFFDQFLSPSLLGIPLIAMAIMIPWLIFPTPTNRWLNNRLMTVQSWFINRFTYQLMQPMNFGGHKWATILTALMLFLITINLLGLLPYTFTPTTQLSLNMAFAIPLWLTTVLIGMLNQPTVALGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLITIMPTVALLTSLILFLLTILEVAVAMIQAYVFVLLLSLYLQENV", "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": "MDSVEGLALGPVIWTASQEELLRQPYNHLVTQPGKNFRNTLIRVFNGFYGLSERQVAAVTELVEMLHVASLLIDDIEDNSAWRRGVAAAHVVYGSPMTINTANYMYFVSMSLLGQLAAQRPAGPLQDLLKVFNEEMMNLHRGQGLDIYWRDTFTVPSEHDYLRMVMHKTGGLFRLTVRIMEALREGPDGPGSTLVPLSNLLGVLYQVRDDYLNLTDSRMSENKGFADDITEGKFSYPIIHGLQYARVHDPAGYDFLVSVLRQRTTDITTKRRVVRYLADVSGSLAYTKQRIIELATLIKTKYIPASGTELCNVIDSLTSF", "text": "FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. May be involved in vesicle trafficking and protein sorting (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MATRNRTLLFRKYRNSLRSVRAPLSSSSLTGTRSGGVGPVIEMASTSLLNPNRSYAPISTEDPGTSSKGAITVGLPPAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGKEDQHNIESLTQEITFLLKKSEKQLQRLSASGPSEDSNVRKNVQRSLATDLQLLSMELRKKQSTYLKRLRQQKEDGMDLEMNLSRNRYRPEEDDFGDMLNEHQMSKIKKSEEVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASVLVILCFIMLLLLILKEIFL", "text": "FUNCTION: Contributes to the regulation of secretory and vacuolar transport pathways in the post-Golgi network, and to the maintenance of the Golgi apparatus and trans-Golgi network (TGN) morphologies (PubMed:22307646). Together with VTI12, required for membrane fusion (PubMed:15919093). Vesicle trafficking protein that functions in the secretory pathway and mediates liposome fusion; the fusion of phospholipid vesicles containing SYP41 and VTI12 is triggered by YKT61 and YKT62 (PubMed:15919093, PubMed:24021022). Required for extracellular resistance responses to a fungal pathogen (PubMed:22307646). Also involved in the protection of chloroplasts from salicylic acid-dependent biotic stress (PubMed:22307646). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein Note=SYP41 is found in a different region of the TGN than SYP42. SIMILARITY: Belongs to the syntaxin family."}
+{"protein": "MLSRLFLRHSNLRFVTLVSSKSNSQIFSSFIRPLSTNSSGGGGNGDGNGRNRNDVPWSFTGVNDDKSGPFSSDDSFGSSGVAGSGLPGGEGKWPEEPKRWNIKEEEEKVVFDTGGEVGQGIETSRERRGNEWEETKRWDMKEGEEKVVFGGGGDEVDGFGIRGEVKSNEWDVSKPWNLKEEEEGVVFDTGGEVPFSFENSLEMAEEERVKKELIEKEEKELLEVIKGPDRAFGDLIAKSGITDEMLDSLIALKDFQGVEGLPPLTEIENLRREKSSKKSSRAEIELQMQEDIAKARVRQVDETGRAYGTGRRKCSIARVWIQPGEGKFQVNEKEFDVYFPMLDHRAALLRPLAETKTLGRWDIKCTVKGGGTTGQVGAIQLGISRALQNWEPDMRTSLRAAGFLTRDSRVVERKKPGKAKARKSFQWVKR", "text": "FUNCTION: Mitochondrial ribosomal protein required for central cell maturation. May work together with PIA2 in controlling female gametophyte development, possibly by regulating the expression of some mitochondrial proteins. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
+{"protein": "MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGVSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQEPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQAREALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKCRYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAEQRRRTLLKDFHDT", "text": "FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:16118314, PubMed:17646546, PubMed:19340006, PubMed:24076655). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity). The initial ubiquitin is then elongated (By similarity). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex (PubMed:24076655). Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:16118314, PubMed:17646546, PubMed:19340006). May play a role in myelopoiesis (PubMed:19340006). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RBR family. Ariadne subfamily."}
+{"protein": "MVVKVYGQIKAANPQRVLLCFLEKDIEFEVIHVDLDKLEQKKPQHLLRQPFGQVPAIEDGYLKLFESRAIARYYATKYADQGTDLLGKTLEGRAIVDQWVEVENNYFYAVALPLVMNVVFKPKSGKPCDVALVEELKVKFDKVLDVYENRLATNRYLGGDEFTLADLSHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLMELAAY", "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": "MELKGVHQQNGTSNGTGAAGTEGESPPPAPAPATAEAAASLETTTEKVDAEQQKTERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSVVPGFVGVGYGQAFATICIITYYSSLLALTLFYLFVSFQSVLPWSYCWEEWMNCVDSRPQEDTDALLLSSSNVTNVTALTDTVKLQSSSELYFLNVVIKEKMDISDGIGDPDWKLTLALFVSWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFILLVRAVTLEGARDGIIFFLEPQWGELLNPTVWKNAVVQCFFSLAVGSGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLQIENIRDVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTILCDQFKSWKYWKVALATSICGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELAGIVWIYGMQNFCDDVEFMCNRRVSLYWRVCWSFFTPVMMIVIFIYSMVTIEPITYSEQFFPEAGNVAGWLLFGIGAAQFPLWWMWYISHHREGSLGQSFVASLRPSDKWGPANPETKRQWVIFKNEKAAQRATKKQSSKMGAFWQKLGHFCGSNT", "text": "FUNCTION: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family."}
+{"protein": "MARPRPREYKAGDLVFAKMKGYPHWPARIDELPEGAVKPPANKYPIFFFGTHETAFLGPKDLFPYKEYKDKFGKSNKRKGFNEGLWEIENNPGVKFTGYQTIQQQSSSETEGEGGNTADASSEEEGDRVEDGKGKRKNEKGGSKRKKSYTSKKSSKQSRKSPGDEDDKDCKEEENKSSSEGGDAGNDTRNTTSDLQKAGEGT", "text": "FUNCTION: Enhances DNA synthesis and may play a role in cell proliferation. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "FGERPYWWVHETKFYGAGPAPSLQQFPITCETGPGSPSGHAMGAAGVWYVMVTALLSIAREKQCPPLLYRFLYIGLWMLMGLVELVVCISRVYMAAHFPHQVIAGIITGTLVAEVVSKEKWIYSASLKKYFLITLFLTSFAVGFYVLLKALDVDLLWTMEKAQKWCIRPEWVHLDSAPFASLLRNMGSLFGLGLGLHSPFYKTTKMRIMSAPLRIGCIVISVSLLHLLDGWTFSPENHMTFYALSFGKSAVALLIPTTLVPWALSKIYPVKTEGKNL", "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": "MSELETGARKAQGKGTPPFAYKALYRASPVDRIGVIKKGVAASDLKRFIAALHVDQKVMFDALNLKTATVNKKAANNQPLSTEDSERVLGLAKLVGQLEDMVEESGETDGFDAPEWLSSWLRQPLPALGGVNPIDLLDTMEGQAVVSRALAQIQSGAFA", "text": "FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the bacteriostatic effect of cognate toxin ParT by inserting into its active site. SIMILARITY: Belongs to the MbcA/ParS/Xre antitoxin family."}
+{"protein": "MDGFDRSNAPVEYQRVEWISDIFVFGMGVCWLINYAGMIYTSLQEQTYSMAPLALCCNFAWEMVYGLIYPSKSRIEQGVFLAGLVVNLGVMYTAIRFAPNEWAHAPLVMNNITLIFALGVLGSLTGHLALAAEIGPALGYSWGAVACQLLLSVGGFCQLLGRSSSRGASYTLWLSRFIGSGCVVGFAILRYMYWSEAFNWLNSPLVLWSLGVFIAVDSLYGICLWNVKKYEHGQERSNARKAQ", "text": "FUNCTION: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NA). Nodulisporic acid A (NAA) and its chemically modified derivatives are of particular significance because of their highly potent insecticidal activity against blood-feeding arthropods and lack of observable adverse effects on mammals, in particular the tremogenicity associated with the paspaline-derived IDTs is not observed (PubMed:29283570). The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (PubMed:29283570). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase nodC then forms 3-geranylgeranylindole (3-GGI) (PubMed:29283570). Epoxidation by the FAD-dependent monooxygenase nodM leads to a single-epoxidized-GGI that is substrate of the terpene cyclase nodB for cyclization to yield emindole SB (PubMed:29283570). The terminal methyl carbon, C28, of emindole SB is then oxidized by the cytochrome P450 monooxygenase nodW to produce nodulisporic acid F (NAF), the pentacyclic core of NAA (PubMed:29283570). NAF is converted to nodulisporic acid E (NAE) via prenylation. This step is probably performed by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). Several oxidation steps performed by the FAD-linked oxidoreductase nodO and one of the cytochrome P450 monooxygenase nodR, nodX or nodZ further convert NAE to nodulisporic acid D (NAD) (Probable). NAD is substrate of cytochrome P450 monooxygenase nodJ to produce the precursor of nodulisporic acid C (NAC), converted to NAC by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). The FAD- dependent monooxygenase nodY2 then oxidizes NAC to nodulisporic acid B (NAB) (Probable). Finally NAB is converted to NAA by one of the cytochrome P450 monooxygenases nodR, nodX or nodZ (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the paxB family."}
+{"protein": "MGASGSKKHSRPPRGLQERLLRARAGACGGYWNESGGEYSRFQEGSDREQKSPSCEGRQYQQGDFMNTPWKDPAAEREKNLYRQQNMDDVDSDDDDQVRVSVTPKVPLRPMTHRLAIDMSHLIKTRGGLEGMFYSERRHKILNIYLEKEEGIIADWQNYTHGPGVRYPMFFGWLWKLVPVDVPQEGEDTETHCLVHPAQTSKFDDPHGETLVWEFDPLLAYSYEAFIRYPEEFGHKSGLPEEEWKARLKARGIPFS", "text": "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: In infected CD4(+) T-lymphocytes, down-regulates cell surface expression of CD4, CD28, CD3, and MHC-I or MHC-II molecules. 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: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. 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": "MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR", "text": "FUNCTION: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (PubMed:24554434). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (PubMed:25704143). Involved in the regulation of centrosome disjunction (PubMed:26220856). Phosphorylates CCDC102B either directly or indirectly which causes CCDC102B to dissociate from the centrosome and allows for centrosome separation (PubMed:30404835). FUNCTION: [Isoform 2]: Not present in the nucleolus and, in contrast to isoform 1, does not phosphorylate and activate NEK11 in G1/S-arrested cells. FUNCTION: [Isoform 1]: Phosphorylates and activates NEK11 in G1/S- arrested cells. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Note=Predominantly cytoplasmic. SUBCELLULAR LOCATION: [Isoform 4]: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Predominantly nuclear. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Nucleus, nucleolus Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore. Chromosome, centromere Note=STK3/MST2 and SAV1 are required for its targeting to the centrosome. Colocalizes with SGO1 and MAD1L1 at the kinetochore. Not associated with kinetochore in the interphase but becomes associated with it upon the breakdown of the nuclear envelope. Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end. SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily."}
+{"protein": "MSSVFANVVRAPEDPILGVTVAYHKDQSPNKLNLGVGAYRTEEGKPLVLNVVKKAEQMLVNDQSRVKEYLPIVGLADFNKLSAKLIFGADSPAIQENRVATVQCLSGTGSLRVGGEFLARHYHEHTVYIPQPTWGNHPKIFTLAGLSVKTYRYYNPETRGLDFEGMLEDLGSAPLGAIVLLHACAHNPTGVDPTIEQWEQIRQLMRSKSLLPFFDSAYQGFASGSLDADAQSVRIFVADGGECLAAQSYAKNMGLYGERVGALSIVCKTADVASKVESQLKLVIRPMYSSPPLHGASIVAAILKDGDLYNEWTLELKAMADRIISMRQELFNALQAKGTPGDWSHIVKQIGMFTFTGLNSEQVTFMTNEYHIYLTSDGRISMAGLSSRTVPHLADAIHAAVTGKA", "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: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDYEIVRLQLWDIAGQERFTSMTRLYYRDASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPNGEPVPCLLLANKCDLSPWAVSRDQIDRFSKENGFTGWTETSVKENKNINEAMRVLIEKMMRNSTEDIMSLSTQGDYINLQTKSSSWSCC", "text": "FUNCTION: The small GTPases Rab are key regulators in vesicle trafficking (PubMed:24788816). Essential for maintaining the integrity of the endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:24788816). Recruits LRRK2 to the Golgi complex and stimulates LRRK2 kinase activity (PubMed:29212815). Regulates neuronal process morphology in the intact central nervous system (CNS) (By similarity). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection (PubMed:22042847). FUNCTION: The small GTPases Rab are key regulators in vesicle trafficking (By similarity). Essential for maintaining the integrity of endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (By similarity). Recruits LRRK2 to the Golgi apparatus and stimulates LRRK2 kinase activity (By similarity). Regulates also neuronal process morphology in the intact central nervous system (CNS) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm Cytoplasm, perinuclear region Golgi apparatus Golgi apparatus, trans-Golgi network Vacuole Cytoplasm, cytoskeleton Note=Colocalizes with LRRK2 along tubular structures emerging from Golgi apparatus (PubMed:29212815). Colocalizes with GM130 at the Golgi apparatus (PubMed:22042847). Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus (PubMed:22042847). Colocalizes with TGN46 at the trans- Golgi network (TGN) (PubMed:24788816). In Salmonella enterica serovar Typhi (S.Typhi) infected epithelial cells, is recruited and colocalized with both S.Typhi-containing vacuoles and dynamic tubules as well as those emerging from the vacuole toward the cell periphery (PubMed:22042847). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm Cytoplasm, perinuclear region Golgi apparatus Golgi apparatus, trans-Golgi network Cytoplasm, cytoskeleton Note=Colocalizes with GM130 at the Golgi apparatus (By similarity). Colocalizes with LRRK2 at dynamic tubules emerging from and retracting to the Golgi apparatus (By similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN) (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MEGECRVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLTSQELHALYEGLKANNVNKYDYVLTGYTRDKSFLGMVVDIVQELKQQNSRLVYVCDPVMGDKWNGEGSMYVPQDLLPVYREKVVPMADIITPNQFEAELLSGRKIHSQEEAFAVMDVLHRMGPDTVVITSSDLPSPKGSDYLMALGSQRMRKPDGSTVTQRIRMEMRKVDPVFVGTGDLFAAMLLAWTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAGEGQKPSPAQLELRMVQSRKDIEDPEIVVQATVL", "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": "MDPGTEEYELNGDLRPGSPGSPDASPPRWGLRNRPINVNHYANKKSAAESMLDIALLMANASQLKAVVEQGNEFAFFVPLVVLISISLVLQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIVVVNIFITAFGVQKPVMDVAPRQ", "text": "FUNCTION: [Ninjurin-1]: Homophilic transmembrane adhesion molecule involved in various processes such as inflammation, cell death, axonal growth, cell chemotaxis and angiogenesis (By similarity). Promotes cell adhesion by mediating homophilic interactions via its extracellular N- terminal adhesion motif (N-NAM) (PubMed:19595672). Involved in the progression of the inflammatory stress by promoting cell-to-cell interactions between immune cells and endothelial cells (By similarity). Involved in leukocyte migration during inflammation by promoting transendothelial migration of macrophages via homotypic binding (By similarity). Promotes the migration of monocytes across the brain endothelium to central nervous system inflammatory lesions (By similarity). Acts as a regulator of Toll-like receptor 4 (TLR4) signaling triggered by lipopolysaccharide (LPS) during systemic inflammation; directly binds LPS (By similarity). Acts as a mediator of both programmed and necrotic cell death (By similarity). Plays a key role in the induction of plasma membrane rupture during programmed and necrotic cell death: oligomerizes in response to death stimuli to mediate plasma membrane rupture (cytolysis), leading to release intracellular molecules named damage-associated molecular patterns (DAMPs) that propagate the inflammatory response (By similarity). Plays a role in nerve regeneration by promoting maturation of Schwann cells (By similarity). Acts as a regulator of angiogenesis (PubMed:33028854). Promotes the formation of new vessels by mediating the interaction between capillary pericyte cells and endothelial cells (By similarity). Promotes osteoclasts development by enhancing the survival of prefusion osteoclasts (By similarity). Also involved in striated muscle growth and differentiation (By similarity). FUNCTION: [Secreted ninjurin-1]: Secreted form generated by cleavage, which has chemotactic activity. Acts as an anti-inflammatory mediator by promoting monocyte recruitment, thereby ameliorating atherosclerosis. SUBCELLULAR LOCATION: [Secreted ninjurin-1]: Secreted. SUBCELLULAR LOCATION: [Ninjurin-1]: Cell membrane; Multi-pass membrane protein Synaptic cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ninjurin family."}
+{"protein": "MSEQDSSSPKYMRFLLGNFTSAEMVTDGNFLIYCIEMGLLVIGVLENIFMIGAVFSTSCLHLNLRILICNCCLGFILMAVGRAMIAVPLCIAHLRDVDISSHAWCFIANAVHHSSADSVCLSFVFIMLERTAGTIWSKDYEKTKIHIFPCIFAFLQWFIPMFMILGNFLDRANRMEHFLLYPHLPCQIEYLTPTMFMITIFIIVIGFIASVGGITIVYNKNIKKYNTRDIWFNTVNLSERYQITENIRSTHLLFPLLALMLIFSTLSVSVLIYGGYWVSVMTKEPARFEEVVKWFGRGGEAAQLFDIITAIYTISFPICAFICHPNLFRFLRKFIGWNSYAVRPSNLNEIGGFEMSTAPIRTQTEFHFQELSRQWNT", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MPHSSLHPSIPRPRGHRAKKAAFVLLSTCLAALWELGEPADHILRWLVLHLASEQLGLLFKGLCSLAEEIRHVHSRYQGSYWRAFRACLGCPIRCGVLLLLSCYCYTFLPNTAGLPFAWIVALLGLSQALNILLDLQGLAPAVVSTVCEQGNFNVAHGLAWSYYIGYLRLILPGLQARIHTYNQRHNNTVRGTGVHKLYILLPLDCGVPDDLSVADPNIRFLHELPKQSADRAGIKGRVYTNSIYEILENGKPVGTCVLEYATPLQTLFAMSQDSRAGFSREERLEQAKLFCQTLGDILADVPESQYCRLIVYLDAAEGSSFSLSQEILKHLKQEEKEEVTVGTMGSSGVLESSTLDKEPQLLISGMDQPLPLRTDVF", "text": "FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting that the cGAS-STING pathway promotes a limited inflammatory response (PubMed:29478775). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cytoplasm, perinuclear region Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein Mitochondrion outer membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). SIMILARITY: Belongs to the STING family."}
+{"protein": "MGFVPITLSAGQNPLTQFDGKIETHFLEPPAGTAFQIMQIYKPLPKGDKSGAYRGPPPHFHLHQTERFKVIKGRVGIEVNDKVTVLRPKDGVAICPAGNIHRFIIDVDPKHDQDGEDDEEEDDGEIVFMVNATDSGKDFVLDRIFLENWYGVRVDSFKYGTKIDFIQQCATFDGGDHYLPFPATLPEWVPMSWSVAIRTFLGFWVTVIIGRYVGGLLGYQPFYREYTTDWELAVAKMQGTWFYRRNVQTAYRAATSWKELREMVPYSDEGAANMGLADAKVGNGAAVKKAINDRAANNGEDKKNL", "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 oxidoreductase OpS7 family."}
+{"protein": "MSFRVKGWSDQFSESFYERATTLLTAALNKGTKHSMIADHITVKELDLGPQPPQLEILEVGDLAPDRFQGLFNLHYSGDASLVLQTKIRANPLSVQKSNVPSFSSRNTMLASRAPLTVPMFLRLSDLKLNGIVVLVFSKQKGITVVFRNDPLESVRVSSSFDSIPAIARFLQREIEVQLVSLFQEELPSIIYKMSRIWFAKSDSNLSFQKIPFTSPNQSHTSLANYNPDLLDGPPDYHESTKVDTHLPIKMGPLDVQTHPNIRSIASLALSRKALLPISSPSIPMSIYRSTPPDTIIQQLTTQSDDISAVSSPATQYSASDYLGSNDTTARPSIFGRSHGTSQFRRRERVKKRHVIKIHEASNKSASSSETFVGSKNVDLTESAFDSIPDTPTKIITNINKLKRNYTITNNWLENLQQKIPSEVDNGKVSGLQYSAFKLLMLQRLMAAKGSF", "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": "MFKSGSGSLKRSGSISSVKSFSGDSEKGLPPISRGSVSIASQNSEPLIVPASSSSFAATSDFVPEKTKSEGNLKNKSSVITGNFGSSGPTNAHYNQNANGDRLAENLLLKESSKGRGSSTPDARHTATDSRLSQEVKQPFSEENASGNDLNTGRGSHGTGDGVEQYYKFDCEEGMSAYHKRVVDTFFKYFEYPAEDGHSTLYSDVMFLSGGGDLGLLVMSRYQEVMTLRLRSAIYGIFCYLQALTAYLTYFSAKVGQAVMLDEELEKYEIRLDVAQDDDPIVFQITTGVFTSGVAHDLRKLTQILETFSLER", "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": "MRELPHVLGIVLAGGEGKRLYPLTADRAKPAVPFGGAYRLIDFVLSNLVNARYLRICVLTQYKSHSLDRHISQNWRLSGLAGEYITPVPAQQRLGPRWYTGSADAIYQSMNLIYDEDPDYIVVFGADHVYRMDPEQMVQFHIESGAGATVAGIRVPRAEATAFGVIDADESGRIRSFVEKPADPPGTPDNPDEAFVSMGNYIFTTKVLIDAIRADADDDDSDHDMGGDIIPRLVSDGMAAVYDFSNNEVPGATERDHGYWRDVGTLDAFYDAHMDLVSVHPIFNLYNKRWPIRGESENLAPAKFVNGGSAQESVVGAGSIISAASVRNSVLSSNVYIDDGAIVEGSVIMPGTRIGRGAVVRHAILDKNVVVGPGEMVGVDLEKDRERFSVSAGGVVAVGKGIWI", "text": "FUNCTION: Involved in the biosynthesis of ADP-glucose, a building block, required in the biosynthesis of maltose-1-phosphate (M1P) and in the elongation reactions to produce linear alpha-1,4-glucans. 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": "MAPIEILKFPISSPGDISPLKKLQDAGYDPSNILAVVGKTEGNGCVNDFSRTLASAVWEPRIPSDAVTIFSGGTEGVLSPHVTFFLRSPGDKETGLSAAVGHTRRFEPHEIGTDEQAQQVATTTSSLIEQMGVTPDQVHMVLIKCPLLTSEKLETIRALGRVPVTTDTYESMARSRYASAVGIAAAVGEIQHTRIPEAVSKAGTWSAKASCSSGAELEDCHILVLASTSAQGSRLHAVSRPMADAMDAASILALMELAKKDGGKIVQVFAKAEADPSGHVREWRHTMNTDSDIHSTRHARAAVGGLIAGLVSDAEIYVSGGAEGQGPSGGGSLCLVYETSI", "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. Only active on cyanuric acid and N-methylisocyanuric acid. SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family."}
+{"protein": "MAARGVIAPVGESLRYAEYLQPSAKRPDADVDQQGLVRSLIAVGLGVAAFAFAGRYAFRIWKPLEQVITETAKKISTPSLSSYYKGGFEKKMSRREAGLILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAAKINEAKDLLETTTKH", "text": "FUNCTION: Negative regulator of the mitochondrial respiratory chain. Prevents mitochondrial hyperpolarization state and restricts mitochondrial generation of ATP. Acts as an import component of the TIM23 translocase complex. Stimulates the ATPase activity of HSPA9 (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein."}
+{"protein": "MDVTRLLLATLLVCLCFFTASSHLAPEEKSKDERSLRSNSSMNLLDFPSVSIVALNKKSKKISRKEAEKRSSKKKASMKKVAQPRPPRPAPCVANRDSCKPPALACCDPCAFCQCRFFRSACSCRVLNPTC", "text": "FUNCTION: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment) (By similarity). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MGLLDSEPGSVLNVVSTALNDTVEFYRWTWSIADKRVENWPLMQSPWPTLSISTLYLLFVWLGPKWMKDREPFQMRLVLIIYNFGMVLLNLFIFRELFMGSYNAGYSYICQSVDYSNNVHEVRIAAALWWYFVSKGVEYLDTVFFILRKKNNQVSFLHVYHHCTMFTLWWIGIKWVAGGQAFFGAQLNSFIHVIMYSYYGLTAFGPWIQKYLWWKRYLTMLQLIQFHVTIGHTALSLYTDCPFPKWMHWALIAYAISFIFLFLNFYIRTYKEPKKPKAGKTAMNGISANGVSKSEKQLMIENGKKQKNGKAKGD", "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 catalyzes the synthesis of very long chain saturated (VLC-SFA) and polyunsaturated (PUFA) fatty acids that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ELO family. ELOVL4 subfamily."}
+{"protein": "MTSTQFDCQYCTASLLGKKYVLKDDNLYCISCYDRIFSNYCEQCKEPIESDSKDLCYKNRHWHEGCFRCNKCHHSLVEKPFVAKDERLLCTDCYSNECSSKCFHCKRTIMPGSRKMEFKGNYWHETCFVCEHCRQPIGTKPLISKESGNYCVPCFEKEFAHYCNFCKKVITSGGITFRDQIWHKECFLCSGCRKELYEEAFMSKDDFPFCLDCYNHLYAKKCAACTKPITGLRGAKFICFQDRQWHSECFNCGKCSVSLVGEGFLTQNMEILCRKCGSGADTDM", "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": "MAYVQEEWIPLTGLGRMVAAGEITSIDEVLASGRPIKEPQIVDLLLPDLEDEVLDINMVQRMTDSGRRVKFRTVVVVGNRNGYVGFGQGKDVQVGNAIQKAIVNAKLNLIKVSRGCGSWECGCETAHSIPIEVTGKAGSVKVTLKPAPQGIGLVTGDIPKKVLMLAGIKDVWAFNRGQTRTTINYAKATFEALKQTNMVRIGGTE", "text": "FUNCTION: With S4 and S12 plays an important role in translational accuracy. SIMILARITY: Belongs to the universal ribosomal protein uS5 family."}
+{"protein": "MALRGLIRQSKVRRRREMLPQQVGFVCAVLALVCCASGLFGSLGHKTASAGKHVLLDTWRNRKLMAPINGTPLAKNCTDPAIHEFPTDLFSNKERQHGAVLLHILGALYMFYALAIVCDDFFVPSLEKICEKLHLSEDVAGATFMAAGSSTPELFASVIGVFITHGDVGVGTIVGSAVFNILCIIGVCGLFAGQVVRLTWWAVCRDSVYYTLSVIVLIAFIYDEEIVWWEGLVLIILYVFYILIMKYNMKMQTFFTTKQKSIANGNPVSNELEDGNDLYDGSYDDPSVPLLGQVKEKPPYGKTPVVMVDEILSSSPPKFTFPEAGLRIMITNKFGPRTRLRMASRIIINERQRLINSANGVNSKPLQNGRHENMENGNVPVENPEDPQQGQEQQPPPQPPPPEPESVETVFLSPFSMPEAKGDKAKWVFTWPLIFLLCVTIPNCSKPRWEKFFMVTFITATLWIAVFSYLMVWLVTIIGYTLGIPDVIMGITFLAAGTSVPDCMASLIVARQGLGDMAVSNTIGSNVFDILVGLGIPWGLQTMVINYGSTVKINSRGLVYSVVLLLGSVALTVLGIHLNKWRLDRKLGIYVLVLYAVFLCFSIMIEFNVFTFVNLPMCREDD", "text": "FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) (PubMed:22057188). Controls the rapid response termination and proper regulation of adaptation in olfactory sensory neurons (OSNs) which subsequently influences how odor information is encoded and perceived (PubMed:22057188). May play a role in calcium transport during amelogenesis (PubMed:23375655). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasm. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC24A subfamily."}
+{"protein": "MSSVTVTLPDGSTLEVASGATVEDVAHEIGPGLGRDTVAGKIDHELVAKEEPISEDCEIEIVTDQSDEYLDVLRHTAAHVLAQAIRRHHPDAKLTIGPYTDEGFYYDIANVELDADDLDEIQAEAASIIDDDLDVERVEYDRADAREHYADNEFKREILDAEAAGDGPVSFYTQGDFEDLCKGPHVDSTGEIGGFEVLETSAAYWRGDEERETLTRVYGTAFPTESDLQEYLARREEAKERDHRKLGREMDLFSIPDVTGPGLPLYHPNGKTVLRELSEYVRGLNSEMGYDEVETPHLFRTELWKQSGHYDNYVDDMFLLDVNDEEYGLKPMNCPGHATIFNEGSWSYRDLPVRYFEDGKVYRKEQRGELSGLSRVWAFTIDDGHVFARADQIEAEVRRLMDTITEVLDTFDLDYEVALATRPEKSVGSDDIWEQSERQLREVLDQQGVDYDVEPGDGAFYGPKIDFGFEDALGRSWDGPTVQLDFNMPDRFDLEYTGSDNDAHQPVMIHRALYGSYERFFMVLIEHYNGRFPTWLAPEQVRILPVTDDNLGYAHRVKNELGDYRVEVEDRDWTVGKKIQQAHDDNVPYMLVVGDDEEDADAVSVRDRQEREGKGVDLAEFRAHLDSEVDGKRTEPDFLD", "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). 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). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
+{"protein": "MEYDDKLVRFRQGHLNPFDKKGGAERHPADSETQPCKDSSTSSPLSVPEYNYPDRVMDLGVSEDHFSRPVGLFLASDVQQLRQAIEECKQEILELPENSDRQKDAVVRLIHLRLKLQELNDPLEDEPNLRVLLEHRFYKEKSKSVKHLCDKCSTFIWGLIQTWYTCTGCSYSCHSKCLNLITKPCVRSKVSHQAEYELSICPEAGLDSQDYRCAECRTPISLRAVPSEARQCDYTGQYYCISCHWNDLAVIPARAIHNWDFEPCKVSRYSMRYLALMLGRPVLKLREINPLLFNYVEELVEIRKLRQDILLMKPYFITCKEAMEDRLLLQLQDRQHFVENDDMYSLQDLLDISSGRLGCSLTEIHTTFAKHIKLDCERCQAKGFMCELCKEGDILFPFDSHTSVCQDCAAVFHRDCYYENSTSCPRCMRLNLRKQVQNPGAEP", "text": "FUNCTION: Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. Involved in bone resorption. SIMILARITY: Belongs to the DEF8 family."}
+{"protein": "MSNESTNCSFFLNLFMLLLLLIFYSADACQRECGGISIPYPFGIGKDCCLEKYYEIECRNTTSRKLVPLLSFINKEVVSISLPSADSHFAYEVSDQERHESFGLVRVKFPITSAGCFNDGKESGGGSKMNFTGSPFFIDRSNSLIAAGCNSKVSLMYIKPKMVGCELSCNTSKDSYSNSIPFVEAGCSSNVLPYSQDQGCPEEIAEETGCNGIGCCQASLPNEPQQVIGIRTENNDGNSTTKVECTVSAFLTDEIYALPKATKTEHLLAKRYATVSLGWVIQTSNRSFLDSLALACKDREDYRNTTNLERKCTCGRITISETSYANCGCTYGYTGNPYVLNGCKDIDECKVKFEYCGKTETCVNFEGGYRCVRDKTKAIMIGAGTGFGVLVLVGGLWWLRKFLIKRRITKRKKKFFKRNGGLLLLQELNTREGYVEKTRVFNSRELEKATENFSENRVLGHGGQGTVYKGMLVDGRTVAVKKSKVIDEDKLQEFINEVVILSQINHRHVVKLLGCCLETEVPMLVYEFIINGNLFKHIHEEESDDYTMLWGMRLRIAVDIAGALSYLHSSASSPIYHRDIKSTNILLDEKYRAKVADFGTSRSVTIDQTHWTTVISGTVGYVDPEYYQSSQYTEKSDVYSFGVILAELITGDKPVIMVQNTQEIVALAEHFRVAMKEKRLTDIIDARIRNDCKPEQVMAVAKVAMKCLSSKGKKRPNMREVFTELERICTSPEDSQVHNRIDEEEEEEEEEEEVVTTINRGDSWSISVTAPALSIVASSPSSDVEPLFPRLTW", "text": "FUNCTION: Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "VVYCNARTTCPSRTTCCRSPFGVWYCCPFLMGQCCRDGRHCCRHGYRCDSTSTLCLR", "text": "FUNCTION: Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the granulin family."}
+{"protein": "MLRNKPRAAVTTKKQTSLLMADQPPPPKPNTCHCSPSLFSSPKFRFFTSKMMMTPFDSDFSLVSPTSILEANPSIFSSKNPKPVSYFEPTIPNPQRFHSPDVFGLADLVKDGDSNRDHSRKPVNKMVLFGSKLRVQIPSSADFGTKTGIRYPPCQLSPCVQTKVLAVSEIDQTEDYTRVISHGPNPTITHIFDNSVFVEATPCSVPLPQPAMETKSTESFLSRCFTCKKNLDQKQDIYIYRGEKGFCSSECRYQEMLLDQMET", "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 (PubMed:24600465). Involved in seed dormancy control (PubMed:15159630). SUBCELLULAR LOCATION: Cytoplasm, Stress granule Cytoplasm, P-body. SIMILARITY: Belongs to the FLZ family."}
+{"protein": "MAKSEKHKLAQTLIDSINEIASISDSVTPMKKHCANLSRRLSLLLPMLEEIRDNQESSSEVVNALLSVKQSLLHAKDLLSFVSHVSKIYLVLERDQVMVKFQKVTSLLEQALSIIPYENLEISDELKEQVELVLVQLRRSLGKRGGDVYDDELYKDVLSLYSGRGSVMESDMVRRVAEKLQLMTITDLTQESLALLDMVSSSGGDDPGESFEKMSMVLKKIKDFVQTYNPNLDDAPLRLKSSLPKSRDDDRDMLIPPEEFRCPISLELMTDPVIVSSGQTYERECIKKWLEGGHLTCPKTQETLTSDIMTPNYVLRSLIAQWCESNGIEPPKRPNISQPSSKASSSSSAPDDEHNKIEELLLKLTSQQPEDRRSAAGEIRLLAKQNNHNRVAIAASGAIPLLVNLLTISNDSRTQEHAVTSILNLSICQENKGKIVYSSGAVPGIVHVLQKGSMEARENAAATLFSLSVIDENKVTIGAAGAIPPLVTLLSEGSQRGKKDAATALFNLCIFQGNKGKAVRAGLVPVLMRLLTEPESGMVDESLSILAILSSHPDGKSEVGAADAVPVLVDFIRSGSPRNKENSAAVLVHLCSWNQQHLIEAQKLGIMDLLIEMAENGTDRGKRKAAQLLNRFSRFNDQQKQHSGLGLEDQISLI", "text": "FUNCTION: Functions as an E3 ubiquitin ligase."}
+{"protein": "MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYEDDAVFRSYIDDEYMGHKWQCVEFARRFLFLNYGVVFTDVGMAWEIFSLRFLREVVNDNILPLQAFPNGSPRAPVAGALLIWDKGGEFKDTGHVAIITQLHGNKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTFDDTTILGWMIQTEDTEYSLPQPEIAGELLKISGARLENKGQFDGKWLDEKDPLQNAYVQANGQVINQDPYHYYTITESAEQELIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPRLRLSWQRRRHHMITGRMDFCMDERGLKVYEYNADSASCHTEAGLILERWAEQGYKGNGFNPAEGLINELAGAWKHSRARPFVHIMQDKDIEENYHAQFMEQALHQAGFETRILRGLDELGWDAAGQLIDGEGRLVNCVWKTWAWETAFDQIREVSDREFAAVPIRTGHPQNEVRLIDVLLRPEVLVFEPLWTVIPGNKAILPILWSLFPHHRYLLDTDFTVNDELVKTGYAVKPIAGRCGSNIDLVSHHEEVLDKTSGKFAEQKNIYQQLWCLPKVDGKYIQVCTFTVGGNYGGTCLRGDESLVIKKESDIEPLIVVKK", "text": "FUNCTION: Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. In vitro, the amidase active site also catalyzes hydrolysis of amide and ester derivatives of glutathione (e.g. glutathione ethyl ester and glutathione amide) but lacks activity toward acetylspermidine (N1 and N8) and acetylspermine (N1). FUNCTION: Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. May act synergistically with glutaredoxin to regulate the redox environment and defend against oxidative damage. SIMILARITY: In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family."}
+{"protein": "MLHLFSYSDLNHSLLVFLALFFVLFYEAINGFHDTANAVSTLIYTRAMSAHVAVIMSGIFNFLGVLLGGLTVAYTIVHLLPNDLLLNATSKNALAMVFSMLLAAIIWNLSTWYFCLPASSSHSLIGAIIGIGLTNAFVTDSSLVDAFNIPKMTSVFLSLVFSPIIGLIIAGSLIFLLRYYLNNNKIFYRIHMTPLERKEKDGKKIPPFLIRMALILSSIGVSYAHGANDGQKGIGLIMLVLIGIVPSSFLVNLNTNKYEINCTKHTLNHLEKYFLEKNIKKSNIIKNKEEINNLVVRSQSYNSIKNIKNTKLLLKNISNYNDLSIKKRFQLRHYLLCISDSIDKKVNSSDICSKDKRFLIHSKKVILKTIEYAPMWIILIVALSLSIGTMIGWKRIVVTIGEKIGKKRMTYAQAMSAQITASFSIGIASYTGIPVSTTHILSSSVAGTMLIDGDGIQTKTIKNIALAWILTLPVSMLLSSFLYWIALFLI", "text": "FUNCTION: Low-affinity inorganic phosphate transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family. Pit subfamily."}
+{"protein": "MHLLLAAAFGLLLLLPPPGAVASRKPTMCQRCRTLVDKFNQGMANTARKNFGGGNTAWEEKTLSKYEFSEIRLLEIMEGLCDSSDFECNQLLEQQEEQLEAWWQTLKKEHPNLFEWFCVHTLKACCLPGTYGPDCQECQGGSERPCSGNGYCSGDGSRQGDGSCQCHTGYKGPLCIDCTDGFFSLQRNETHSICSACDESCKTCSGPSNKDCIQCEVGWARVEDACVDVDECAAETSPCSDGQYCENVNGSYTCEDCDSTCVGCTGKGPANCKECIAGYTKESGQCTDIDECSLEEKACKRKNENCYNVPGSFVCVCPEGFEETEDACVQTAEGKVTEENPTQPPSREDL", "text": "FUNCTION: Protein disulfide isomerase (Probable). Might play a role in the unfolded protein response (Probable). May regulate transport of alpha4-beta2 neuronal acetylcholine receptor (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the CRELD family."}
+{"protein": "MSQDFINTDNHTSNLSSNNLYTNINAGNSIMSEELAVKDNSNSTVASDNTERTPCDAENGSIYTTGRSVVSDNAGNQDKGKNFPNGESSSASGKSENSHADDENDGSTENNSKLGQPSFSYDSEIFQLCQHYLTTKNHQGLALVARQKGLPPFLRFKIWPILLKHHPFVVNPFIEPDNEVNNENDTNTEEDLKSDIKRDLLKYIHRLNYTNLIDLNNASPEEQEVFKILESSILKFVKKWGKIMKYDHALTWIALGLAEWFPPIPNTSWVLVGRDFPSSKTSCIKNLFHDYSNYINNVPNLNEYLEDLVNDKEIINMSFRDVYERLVLVLLHAPEEKIKNKSKDLLGPKKINRKILPINGGTIEERVSFFIYCFRKLLPELSQYFQEEQILNKFGSHDDEWLIWWLKWCGSKVWSRLDRGRIWDLIFGWRLQNFKKSNSYYVEKLNLSDNLINKLGPDNFWSVSKDNDDSTIENYKKSSSFKDLINELNINESSNSNSPTSNSPSNSSINEDLLPPSPLSSSSFSSSNIAPADEFNIPFSKLDPHVELLFVTLALLKSKENTLMELDQHEIRQFLSRLPTKSINISNKYKHFKPQESDMNNNIISNDSRNNHKIDFMDNIINESGELWRKWLWSEMIDDN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the OCA5 family."}
+{"protein": "MTLTEIQNVEKENAGASVPKHSSNKLKLEKELEKLEIVDQTKAASAEETNNESEVNELDADEPMLQDLDNRFVIFPLKHHDIWNFYKKAVASFWTVEEVDLGKDMNDWEKMNGDEQYFISRILAFFAASDGIVNENLCERFSNEVQVSEARFFYGFQIAIENIHSEMYSKLIETYIRDETERNTLFNAVDEFEFIKKKADWALRWISDKKASFAERLIAFAAVEGIFFSGSFASIFWLKKRGLMPGLTHSNELISRDEGLHRDFACLLYSKLQKKLTQQRIYDIIKDAVAIEQEFLTEALPVDMIGMNCRLMSQYIEFVADHLLVELGCDKLYKSKNPFDFMENISIDGKTNFFEKRVSEYQRPGVMVNEAERQFDLEADF", "text": "FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small chain family."}
+{"protein": "MSIKRLSMRLKKGIHRSWNRMTSLEAGLEEEKEIKIVEEPEPRPWKVLITGGAGHLAENLVAKLEEMTRDSIRPKIREMLEKEMPAVISTKVDKEVEKRLPMYIQIVLVDVLEPRGRVLKHHVAFVKCSFDDECTMKTALEQVDTVYHLAAVGMTGQYARDRKACMDINAVGTMNLLIWARNSGVQRFIYTSSVGVVFSGEPMYNATEEVGYPDDFYNYYCESKAHAERIVQKASGHRMRTTVLRFNGIYGPGEKRVTERVVKFMLTGMWIATCKPNGVEAQTQLSSVANCIQGLVKAELALRWSDTPHGQIYNIMDKTPVGTFSFWTPLNIALGFSSSMITVPATPIRLFAYLSQIIADRMRIDPIVSVLEVDLLLVNNTFNIEKAERDLGYEPSVSAIPEIIEHYLHRLPPDVVRPKGRSDFYVKVAVLVLGTILIFVAVFSFTFWMYLIFQRLSRWNPF", "text": "FUNCTION: Hydroxysteroid dehydrogenase involved in the biosynthesis of dafrachonic acids (PubMed:18495818, PubMed:20178781, PubMed:24411940). Catalyzes the dehydrogenation of cholesterol or its derivatives and the isomerization of the double carbon bond on the sterol ring. Modifies sterols into a Delta(4)-3-keto-sterols such as cholest-4-en-3-one, precursor of Delta(4)-dafachronic acid (PubMed:18495818). Contributes to the production of Delta(7)-dafachronic acid in the XXX cells (PubMed:24411940). Dafachronic acids act as ligands and bind directly to the nuclear hormone receptor (NHR) daf-12 suppressing dauer formation and inducing reproductive growth (PubMed:18495818, PubMed:24411940). Acts in parallel to AKT-1 to promote reproductive development via DAF-16/FoxO and DAF-12 (PubMed:20178781). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 3-beta-HSD family."}
+{"protein": "MRIEAVVEVRFTEDRGKVLKALQNVFTPVSIEEKPSESGVLIVATCEGYTCLEKLRSAIWRQGIQDAARNVISKGIVSENTIIFSVNKQAAYVGVVSFVTETNESPLGPITFTVKTNNVRQFLDWLAPRTYRGRVYYEAPPPD", "text": "SIMILARITY: Belongs to the UPF0201 family."}
+{"protein": "MEEEIRNIEENDGIRLTWNVWPAKGDATTKIPLACLYNIHQTADVLECEPIYCMSCNSVLNPHCNIDFGRQSWNCVICNNNTTLPSHARGITPDNLLPELLPQNSTVEYVLSRESVFPVVFFLIVDICTFDGERHTLLKDTLKVVLEKIPEDALVGFVKYGTNIELLELNAEQPRRTHLFSGRKEYTAEILKSLGGASKSESQIVGRFLRRKDECQELLYNMVESLERDPFPVLPAYKPVRCTGSAVSLAISLLETSFPDMAVKYLLFTQGPCTFGPGTVTPIKFKEKGRNEHLEENDPMYAGPARKFYTGLAERMNSVGHSLDILAATIVDVGICHMERLTGMTGGMLIMAQDFDRDIYISSCSKILDRSSEGCLVQGFNAKMHVKTSKNLEYKGVIGQGRSFGGSWRMGSMFPSTNISLLFDKKPDAKHGEFGYVQLITQYQRSDKRLLVKVTTFARMFTDSREDVIYGFDQEAVAVFQARFLLLKKYEEIKDCERMIDKNLIRFTKTFARYDKGEPSSLALPDSMAYYPNYMFFFRRSLLVQTGNNSPDETTYYSTLLYNQRVSDALKLIKPTLISYHYQGGVEAVEVDSKSLEPDVILVLDTFHNVVVWRGEYVAQWVREGYHEQAEYEFLKDILKSSEERARLLCNERLPTPQFCITEQNKSQQRILHHYVNPSGGGSIITENINYEKFEEALRRVVVFNSE", "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. SEC23 subfamily."}
+{"protein": "MLVVQMPFSFPMAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQLRGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATASRIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQKFLRGLQVNGSQPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSPIFVVTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTGGDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH", "text": "FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N- linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway. 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 11 family."}
+{"protein": "MGMLRAGLCPGLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLSYKALVALRRVLLAQFSAFPLNGADLYEELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQLARELKILARDLGVAVVVTNHLTRDWDGRRFKPALGRSWSFVPSTRILLDVTEGAGTLGSSQRTVCLTKSPRQPTGLQEMIDIGTLGTEEQSPELPGKQT", "text": "FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction 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. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the RecA family. RAD51 subfamily."}
+{"protein": "MKTICVFAGSNPGGNEAYKRKAAELGVYMAEQGIGLVYGGSRVGLMGTIADAIMENGGTAIGVMPSGLFSGEVVHQNLTELIEVNGMHERKAKMSELADGFISMPGGFGTYEELFEVLCWAQIGIHQKPIGLYNVNGYFEPMMKMVKYSIQEGFSNESHLKLIHSSSRPDELIEQMQNYSYPILEKKWTEI", "text": "SIMILARITY: Belongs to the LOG family."}
+{"protein": "MTANGTAEAVQIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRFLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCDRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVALKVGGRYLKGDHAGVLKACAETIDPASLWEY", "text": "FUNCTION: Actin-binding protein that contains 2 major actin binding sites (By similarity). Organizes filamentous actin into parallel bundles (PubMed:7738015). Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (By similarity). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (PubMed:21685497). Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cell cortex Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, stress fiber Cell projection, growth cone Cell projection, filopodium Cell projection, invadopodium Cell projection, microvillus Cell junction Note=Colocalized with RUFY3 and F-actin at filipodia of the axonal growth cone (PubMed:24720729). Colocalized with DBN1 and F-actin at the transitional domain of the axonal growth cone (PubMed:24720729). SIMILARITY: Belongs to the fascin family."}
+{"protein": "MNEEIQTLLIYQICDSLRFQANMEDISVDDVMDVMQENIMVECLLDGVIMDKADVQKIVIQYVTDGELGEEAIGDKMESMYSNSRKKLLKEIDDLDNTISTNRKKDKLLNLYRDTVLNRLQNKKTVLDKLYHGMKEDSSVIRNRIYLERIKNETPNSIAELQLMLQRSIADCIMSEPIGSEKYNIAKEIQINLEDTIRFMKRALE", "text": "FUNCTION: 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 EAF5 family."}
+{"protein": "MQASRYSIEAEPGWYVSVQQPEEAVAAEEWSPLLSNEPRRQGSSGASFGLSVFNVMNAIMGSGILGLAYVMANTGILGFSFLLLLVALLASYSVHLLLAMCIHTAVTSYEDLGLFAFGLPGKVVVAGTIIIQNIGAMSSYLLIIKTELPAAISEVLPSDHSGAWYLDGQMLLIIICVGIVFPLSLLPKIGFLGYTSSLSFFFMVFFALVVVIKKWAVPCPLTLNCINAVFQISNATDDCKPKLFHFSKESVYAIPTMAFSFLCHTSVLPIYCELRSPSKKRMQNVTNTAIALSFLVYFVSALFGYLTFYDKVESELLQGYSKYLPHDAAVMAVKLCILFAVLLTVPLIHFPARKALMMILFSNYPFSWIRHSLTTLALNIIIVLLAIYVPDIRNVFGVVGASTSTCLIFVFPGLFYLKLSREDFLSWKKLGALSLLSTGTVVGSFSLVLIILDWVNK", "text": "FUNCTION: Probable sodium-dependent amino acid/proton antiporter, could be a neuronal transporter for glutamate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Colocalizes with synaptotagmins and SNAP25. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family."}
+{"protein": "MSTTTNIQLNNLTAISPIDGRYWGQVQVLSEYFSEYALIKYRVQVEIEYFIELSKLSELKPLNAVNKEDDHKKLRDIYLQFKESDAQKIKQIEKTTNHDIKAVEYFIKEKMHTELQYSEVVTEFIHFGLTSQDINNTAIPLSIVESVEKVLIPQLKQSILEPLRQFAQQWKSIPMLARTHGQPATPTTVGKELMVFIERLENQINHLEQSVPHTCKFGGATGNLNAHKVSYPAIDWVVFSEKFVKVLHPSLKRMRFTTQIEHYDNVASLLDAFKRINTILIDLCRDIWTYISMEYFNQKLVKGEVGSSTMPHKVNPIDFENAEGNMGVANALYEHLSAKLPISRLQRDLTDSTVLRSIGVPFSHSILSFKSIQRGLSKLVLNEANIAKDLDANWAVVSEAIQTILRREGFPKPYEALKELTRVSGSKKITESDIQTFIDSLSIPDDIKSELKLITPFNYIGIIPDF", "text": "SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily."}
+{"protein": "MVLFKAKFSFQRRVKLAQTLWLLSWLSVLVGCLTFGMGIFLKVQLWIHNEVMENTSAHAVPNTVITAGLVGILLGIYAGKVSQASMDVTKYQRWKSFMMPFFFLAILSCLVCLAALVLSVALRGTLEESLKIGLKNAIRFYKDTDTPGRCYQKRSMDKLQMDFQCCGNNHPKDWFEVQWISNRYLDFSSKEVKDRIKSNVDGRYLMDSVPFSCCNPSSPRPCIQMQITNNSAHYSYNYQSDELNIWVRGCREALLSYYTGIMATNGAAVTLSFLLQASVLVSLRYLHTSMDKISGPDDMEADTEGFILEKGVTETMNTTLEKMKGLFMSNQVETAEGGGEAAAAS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PRPH2/ROM1 family."}
+{"protein": "MALNTPQITPTKKITVRAIGEELPRGDYQRCPQCDMLFSLPEINSHQSAYCPRCQAKIRDGRDWSLTRLAAMAFTMLLLMPFAWGEPLLHIWLLGIRIDANVMQGIWQMTKQGDAITGSMVFFCVIGAPLILVTSIAYLWFGNRLGMNLRPVLLMLERLKEWVMLDIYLVGIGVASIKVQDYAHIQAGVGLFSFVALVILTTVTLSHLNVEELWERFYPQRPATRRDEKLRVCLGCHFTGYPDQRGRCPRCHIPLRLRRRHSLQKCWAALLASIVLLLPANLLPISIIYLNGGRQEDTILSGIMSLASSNIAVAGIVFIASILVPFTKVIVMFTLLLSIHFKCQQGLRTRILLLRMVTWIGRWSMLDLFVISLTMSLINRDQILAFTMGPAAFYFGAAVILTILAVEWLDSRLLWDAHESGNARFDD", "text": "FUNCTION: Component of a transport pathway that contributes to membrane integrity. FUNCTION: Component of a transport pathway that contributes to membrane integrity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PqiA family."}
+{"protein": "KTTNTFASVNDDEKPREECGVVGIYGDPEASRLCSLALHALQHRGQEGAGIVAVHDNLFHQVNGVGLVSDVFNEAKLSELPGSCAIGHVRYSTAGHSKLVNVQPFVAGYRFGSVAVAHNGNFVNYRSLRAKLEDNGSIFNTTSDTEVVLHLIATSKHRPFLLRVVDACENLKGAYSLVFLTEDKLVAVRDFGFRPLVMGRRKNGAVVFASETCALDLIDATYEREVNPGEVVVVDHTGIQSLCLVTHQEPKQCIFEHIYFALPNSVVFGRSVYESRRKFGEILATESPVECDVVIAVPDSGVVAALGYAAKAGVPFQQGLIRSHHVGRTFIEPSQKIRDFGVKLKLFPVRGVLEGKRVVVVDDSIVRGTTSSKIVRLIKEAGAKEVHMRIACPPIVASCYYGVDTPSKEELISNRMDVEEIRKFIGSDSLAFLPLDTLKSLLEDDAPNYCYACFSGKYPVQPENLNPTASMSLTGTMFQWQFETY", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family."}
+{"protein": "MGSGDLNLLKSWNPKLMKNRKKVWETEQDLITEQQKLNTRLKEIEKERELNELLNESSKDKPETLKNDLALKKSGLEWMYQDAKLSDEKEDYLLGKKKLDSSILNQPATPPVRAATTISASGAATSISSQKKKSKLLKDDPMSKFKVTKQQRRTPDSTKKRAMSQRGKPLSKPAPDLDY", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC25 family."}
+{"protein": "MAATPAASGSNPRKFSEKIALHNQKQAEETRAFDELMSDLTVSRVQFQKLQQLRLAQSRAQYYGGSLPNVNQISSSPTDFQPSFHPTDNIRGMRHHGLVERVSRNRLHSSHHRPIEKHGRQCDSSPYGSVYLSPPPDNNWRRTNSDSALHTSASSTKSQDPFMGGAQAMLRAPKPPQRNTSLQDGEIDNFGEVFSFPNAMTEENMLNVTKPLPKQIWEAQKVQCITSRPRSCEVPNIKVFPSSDSNASLSHFQGSLNTGGSLPDLTNLHFPSPLPTPLDPDDTAYANISAENSSGLPAAMTHLGISGSPGMQNTRSNPSIQATMNNNSLASNVNSHTPPGRNNPALHPSLRLSSLSNPSLPTSALGTSPRRRHTPVSPLTLTPGSESNRSISNQFSPTSPMNMPPNSQGVSMDRSPLSLPPLEPPPPYPLYSDQPQPHLHHTQQQMHESLDSQNYQPPSPVPCPPLDLNLANSSLSGFFGDSFFDQQQPTKQGKYLWQQQEQYDMFGSPSSSLPNTNAFFDPNMNLQYSQASLMGLGGSHGSLQDSFHLRPNYLYSNCGGSVPNIILTDDSSNSLSKDISNAVAGVSELGFDADNTFQLDDELKLGPLSLDGLSMLSDPDMVLPDPSIEDSFRSDKL", "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": "MDRDNGPRVRVPEQRTPSIPATADALRFTVLGPVRAWRGSELLSSGSPQQRALLTALLLREGRTATAGELIDAFWGEDPPSQALATIRTYASRLRKILGQDTLVSESGGYAIRTERSALDLTLAQDLAAEAEKARAAGDRCQARTLINKVLGLWDGEALASVPGPYADNQRTRLEEWRLQLTETRLDLDLEVGCHAEAVSELTALTAAHPLRERLRELLMVALYRSGRQAEALAVYADTRRLLAEELGVDPRPELAELQQRILRADEELARPADEPAPAPAPLKPAQLPATVPDFTGRSAFVTELGSRLATAEGSVMAVSAVAGIGGVGKTTLAVHVAHQARRHFPDGQLYVDLQGAGARAAEPETVLGSFLRALGTADSAIPDTLDERAALYRSTLDGRRILILLDNAHDAAQIRPLLPGTPGCAALVTSRVRMVDLAGAHLVDLDVMSPEEALQLFTRIVGAERVGAEREAALDVVAACGFLPLAIRIAASRLAARRTWTVSVLAAKLADERRRLDELQAGDLTVKATFELGYGQLEPAQAHAFRLLGLADGPDISLAAAAALLDLDPHVAEDLLEALVDTSLVESAAPGRYRYHDLVRLYARACAERDEQPPVRRELALSRLLDFYLATAAGVYALERPGERVLDHFTPTEYPGLTFPAREAALDWLFTESSGLLACARQSAAIGMPQRAADLLMAVVDLGESGANSHQFATAAKAVSEAAKAAGVPRAEARARTMLSHVHSVSGRFAEAEAEAMRALDLGRLAQDAVSQGQAPNQRGIIALYENRHDDAEAHLTQALTAFRADGNKPGEAAALCNLSRVHLATGRTATAVRLAEEGVAIYDSDASGLALIGSGRTDPARHVLLEALQIFRESRQQLWHGMTLFRLSELHLTEQEGAQAAAHAEQSLVVLRGIGGDWRRANVLTVLGRALTVIGQTDRAQVCWGEALTVFEELGSPEAEAVRQLLDPAGVG", "text": "FUNCTION: Component of the AfsK/AfsR system involved in the response of aerial mycelium formation to glucose. SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family."}
+{"protein": "MAPPVSDDSLQPRDVCVVGVARTPIGDFLGSLSSLTATRLGSIAIQAALKRAHVDPALVEEVFFGNVLTANLGQAPARQAALGAGIPYSVICTTINKVCAAGMKSVMLASQSIQLGLNDIVVAGGMESMSNVPKYLPDARRGSRLGHDTVVDGMMKDGLWDVYNDFGMGVCGEICADQYRITREEQDAYAIQSFERGIAAQNTQLFAWEIVPVEVSTGRGRPSVVIDKDEGLGKFDAAKLKKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLHVIAKIRGYADAAQAPELFTTTPALAIPKAIKRAGLDASQVDYYEINEAFSVVALANQKLLGLDPERLNAHGGAVSLGHPLGCSGARILVTLLGVLRAKKGKYGVASICNGGGGASALVLEFMSEKTIGYSAL", "text": "FUNCTION: Catalyzes the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA. SUBCELLULAR LOCATION: Cytoplasm Peroxisome. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
+{"protein": "MAAQESLHVKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEGRLQTPLASLVVIVCGGSNISLAQLQALKVQLGLNGLPE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the serine/threonine dehydratase family."}
+{"protein": "MSYQQQQCKQPCQPPPVCPTPKCPEPCPPPKCPEPCPPPKCPQPCPPQQCQQKYPPVTPSPPCQPKYPPKSK", "text": "FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cornifin (SPRR) family."}
+{"protein": "MIFLLPPVIFVMLLAESVLILGDSEDADLMEMVQMSRPFFNPIIPAVEFVDLREERQRACGHLHDPCPNDRPGHRTCCIGLQCRYGSCLVQVGR", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. OAIP-1 subfamily."}
+{"protein": "SCADDRNPLEECFRETDYEEFLEIARNGLTVTSNPKHVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIRKFGLQLNEFFQENENAWYFIKNIRKRVREVKNNPGILEYPVKPSEEGKSAAQLYVESLRKVVKELKRTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDRETKVTYQTSANEMPSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCKRKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHQLPKEDIQTFCRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDN", "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:23287728). Shows activity on L-Leu (PubMed:23287728). Damages cell membranes of the Gram-positive bacteria S.aureus (MIC=8 ug/ml and MBC=16 ug/ml) and the Gram-negative bacteria A.baumannii (MIC=16 ug/ml and MBC=32 ug/ml). This antimicrobial activity is dependent on the production of hydrogen peroxyde, since it is inhibited by catalase, a hydrogen peroxyde scavenger. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
+{"protein": "MSRLLHAEEWAEVKELGDHHRQPQPHHLPQPPPPPQPPATLQAREHPVYPPELSLLDSTDPRAWLAPTLQGICTARAAQYLLHSPELGASEAAAPRDEVDGRGELVRRSSGGASSSKSPGPVKVREQLCKLKGGVVVDELGCSRQRAPSSKQVNGVQKQRRLAANARERRRMHGLNHAFDQLRNVIPSFNNDKKLSKYETLQMAQIYINALSELLQTPSGGEQPPPPPASCKSDHHHLRTAASYEGGAGNATAAGAQQASGGSQRPTPPGSCRTRFSAPASAGGYSVQLDALHFSTFEDSALTAMMAQKNLSPSLPGSILQPVQEENSKTSPRSHRSDGEFSPHSHYSDSDEAS", "text": "FUNCTION: Transcriptional regulator. Activates E box-dependent transcription in collaboration with TCF3/E47, but the activity is completely antagonized by the negative regulator of neurogenesis HES1. Plays a role in the differentiation of subsets of neural cells by activating E box-dependent transcription (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAAAKQRKPHVSRNPELVRGIGKYSRSKMYHKRGLWAIKAKNGGVFPKHAPKSADSKAVEKPPKFYPADDVKKPLINKRKPKPTKLRASITPGTVLIILAGRFKGKRVVFLKQLSSGLLLVTGPFKVNGVPLRRVNQAYVIATSTKVDISGVNVEKFDDKYFGKKAEKKNKKGEGEFFEAEKKEVNVLPQEKKDDQKAVDVALLKAIEGVPELKAYLGARFSLKAGMKPHELVF", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL6 family."}
+{"protein": "TLQGQKDVIELLKEEGLRDKIKVMVGGAPATQAWADKIGADCYAENASEAVAKAKELLA", "text": "FUNCTION: Acts as a methyl group carrier between MtbB and MtbA. SIMILARITY: Belongs to the methylamine corrinoid protein family."}
+{"protein": "MTMRSSSPSSSSSYSLAFTSLSNRLETIFKKASELCTLCDIEACVIYYGPDGELKTWPKEKEKVRDIALRYSLLNEALRRKKSVNLHGFLNKKKNKGLKNPNKKMKTSLKNVNILKYPLADHYPPDQVSPLIQSLELHVSKFQERLRFLESQKQNQTKPDHQSLTPSSLNHYTQSLNPSQFSLFMYNHGDNTLSQIPVSASNFNQDYFSALLEESELKNQLMKPEICGYDQNQNMSMGDITNNKFQDPCVSNKEAVQESVNNFGLNQLMYKEFYGCDQNMSMGNINSNSFQNPCVSNTQHYSAVEESVKNPWLNQLMQNELYGYGYAGFC", "text": "FUNCTION: Probable transcription factor that may function in the maintenance of the proper function of the central cell in pollen tube attraction. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MRALFYKDGKLFTDNNFLNPVSDDNPAYEVLQHVKIPTHLTDVVVYEQTWEEALTRLIFVGSDSKGRRQYFYGKMHIQNRNAKRDRIFVRVYNVMKRINCFINKNIKKSSTDSNYQLAVFMLMETMFFIRFGKMKYLKENETVGLLTLKNKHIEISPDEIVIKFVGKDKVSHEFVVHKSNRLYKPLLKLTDDSSPEEFLFNKLSERKVYECIKQFGIRIKDLRTYGVNYTFLYNFWTNVKSVSPLPSPKKLIALTIKQTAEVVGHTPSISKRAYMATTILEMVKDKNFLDVVSKTTFDEFLSIVVDHVKSSTDG", "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 the specific target site 5'-[CT]CCTTp 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 undergoes passage around the unbroken 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. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the type IB topoisomerase family."}
+{"protein": "MAGRSLCLTRSSVPGTPFPPPVQQPSTPGPDLLALEEEYKRLNAELQAKTADVVQQAKEIIRDRQEVRSRPVSTQMKSCDDEDDYSLRGLLPSEGIVHLHSETKPKTKNIDPVNKVQNKLHSANKGRKTNSSVKLKYSDVQTADDVAIPEDFSDFSLAKTISKIEGQLEEEGLPEYIDDIFSGVSNDIGTEAQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQLSSVERELENKRRLQKQAASSQSATEVRLNRALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGELMIGFKKQLKLIDVLKRQKMHIEAAKMLSFTEEEFMKALEWGNS", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite."}
+{"protein": "MKPLCLVFGLCVLIGCFLSSECQRGFRGQHDPTRPLSPSNPSSHFYPQPDPNRVQISQPDNIPIFMFEQPHSLNICVPPPPLYLGEEFEKLPPNTHIPYILIRPDIEPPSKYIQPVPRKKSNATPAANNFITTATAPNSTDSF", "text": "FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MRTQNNLTVEVDCHSLGSNECPSMTSSFSPMDSPTPTPTSIYSQGSLASPGWQDAGSYPGHAYERHTGATPMRSAFRLAGMTSNENMGMSYGAMEAQERMPMPDFLSAYDDNVEHFWLPSDGPKTYETGTHSLPYPHTLPQCPPMVRSNYRPHAAYLPEAATNPCLSRSIFHHAERVPQSMSMGNMMPWIPQATESIAPQTIAPSQVGPVTPPPSYSEFPTSIQTFKTHSPTTPLRSCSIGTASGPDTPISRLSGGAADYLEDFQQSPPFRDGLNRLQRQPSRKMIRKQSSRQNMSLENLPSIIKQVQFKCKEPGCKGRFKRQEHLKRHMKSHSKEKPHVCWVPGCERAFSRSDNLNAHYTKTHSKRGGRNRYVATLDESSPDYDPDFRGQLTPDGLPIRGSTLDDPMPNSREYSVDGLDD", "text": "FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds promoters of target genes at brlA response elements (BREs) containing the conserved sequence 5'-(C/A)(A/G)AGGG(G/A)-3' (By similarity). Required for conidiophores formation (PubMed:17213655). Controls expression of abaA (PubMed:19850144). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MATQTVEDSSKPRPKRTGAGSLLKPLNSEYGKVAPGWGTTPFMGVAMALFAIFLSIILEIYNSSVLLDGILTN", "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. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single- pass membrane protein. SIMILARITY: Belongs to the PsbH family."}
+{"protein": "MEGKNKFNTYVVSFDYPSSYSSVFLRLRSLMYDMNFSSIVADEYGIPRQLNENSFAITTSLAASEIEDLIRLKCLDLPDIDFDLNIMTVDDYFRQFYK", "text": "FUNCTION: Antitoxin component of a type V toxin-antitoxin (TA) system. Neutralizes the toxic effects of toxin GhoT by digesting ghoT transcripts in a sequence-specific manner (PubMed:22941047). In concert with GhoT is involved in reducing cell growth during antibacterial stress (PubMed:24373067). Overexpression leads to transcript level reduction of 20 other mRNAs involved in purine or pyrimidine synthesis and transport. Not seen to bind its own promoter DNA (PubMed:22941047). FUNCTION: Antitoxin component of a type V toxin-antitoxin (TA) system. Neutralizes the toxic effects of toxin GhoT by digesting ghoT transcripts in a sequence-specific manner. In concert with GhoT is involved in reducing cell growth during antibacterial stress."}
+{"protein": "MELKAEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFHYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEVCSAEDFKVVFTRYGKCYTFNSGRDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVACQEQRLIYLPPPWGTCKAVTMDSDLDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHKLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC", "text": "FUNCTION: Isoform 1 does not display proton-gated cation channel activity. FUNCTION: Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate- independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4 (By similarity). SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC1 subfamily."}
+{"protein": "MVAVRSAHINKAGEFDPEKWIASLGITSQKSCECLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQLKATHTDSVSSEQVDNVRRMLLAMVDDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLDREHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGGARSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQVFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNLGYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNDVDELLAAIGGGDIRLNQMVNFLQSQFNKPSAEEQDAAALKQLQQKSYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRGISVHRADCEQLAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARRLHGS", "text": "FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response which 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. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c-di-GMP induces it. ppGpp activates transcription of CsrA-antagonistic small RNAs CsrB and CsrC, which down-regulate CsrA's action on translation during the stringent response (PubMed:21488981). 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": "MAASVEDEFEDAPDVEPLEPTLKNIIEQKSLKWIFVGGKGGVGKTTCSCSLAVQLAAVRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCRIDTHNIIVNQLVFPDNERPCKMCEARHKIQSKYLDQMEDLYEDFHIVKLPLLPHEVRGADKVNTFSKQLLEPYSPPKK", "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/WRB and CAMLG/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-CAMLG 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": "MTAASRQEVLGLYRSFFRLARKWQAASGQMEDTIKEKQYILNEARTLFQKNKNLTDPDLIKQCIDECTARIEIGLHYQIPYPRPIHLPPMGLTPRRGRGLQTQEKLRKFSKPLYLKSHDEVS", "text": "FUNCTION: May promote cell proliferation and inhibition of apoptosis of preadipocytes. SIMILARITY: Belongs to the complex I LYR family."}
+{"protein": "MISSASGTNWNRPDSFKGTQCRNIIIHGYCKFENEGCQFNHGNSKETEGQTTDEVPTQRSMTPLNVKFNAKTSSSFTPGKSPAVRSPDFSSLPAFQPGAPVNDQPMLADGPQISGTMSPSLMNSNATAFAPSFNPYASESFTPSVSAGGIPSSQELAGTLHGSNPSIPSPVPSNPYVNSAGLPSGGMLGVGHPMQGLPPPPPPGALPVNPITQFPTVYPPTHSVLQYHLYAPDPPPHLKIPLKPNERTPETLFINNHLRDRLVKNNQTALQVFPRGSLPDIVGDYFGLVPMDFHNRTSDKKRYNGHKNSLYKVFSNLDGKIYFMRRIHDVKITDSAQVSKPFQTWSHLRSANITVLKDSFVTSAFNDSSLCMVFDYYPQSQSLYETYGLANSVNELNQEYLWAFLVQLTIALQEVHSNGLALNDLDWKKVIVTGEPGRIKVTDIGVYDTLNYHQEGRMLHTEQQQNYLSLAELLLNLVQRLCGASGPLDDVKSYHIDPLFKKCIQYLQDTSNNNKNIEDFTKLFSHKVLSVVNSLQYNSEYLEQQLSRELENARLFRLMCKLNAIYGRLESRIDINWAESGEKFPIILFFDYVFHQKDDTGKNVMDLTHVLRCLNKLDAGVSERLMLVTPDEMNCIIISYKELKDLIDSTFRALTQ", "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": "MTIESVMSLFYDAMKVTLMISLPLLLSALCCGLIVSIFQAATQINEQTLSFIPKIAAVLVSIVIFGPWMLVILSDYTHTLFYNLSYITYS", "text": "FUNCTION: Role in flagellar biosynthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Bacterial flagellum basal body. SIMILARITY: Belongs to the FliQ/MopD/SpaQ family."}
+{"protein": "MKVVAVGGGTGLSTLLKGLKNIDSFEITAVVSVTDEGGSSGKLRKELNVPPPGDVRNNIVALAKDEDLLAKLMSYRFSEGSFKGHSLGNLIIAALTKIEGSFSEAIRILERVLAIKGRVLPVSEDHARLVARFEDGEEVIGETNIVRKGGKIVEVRLDRPIDALPEVLEAIERADIIIFGPGSLYTSIITNVLVNGVKDAIKKSKAKKIYVCNLMTQPGETTGYRVSDHVKELERYLEQSVDFVLVNTRKPSEEVLERYRKEGSDFVEIDAENIQNTILAEPFLVEIVDPSDGQRKIRHDSVKLADVIERISRW", "text": "FUNCTION: Required for morphogenesis under gluconeogenic growth conditions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the gluconeogenesis factor family."}
+{"protein": "MPEIYHYLQQLVNGLTVGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYIAFIAITLLAMMGLDSVPLMMLAAFAASIIVTSAFGYSIERVAYRPLRGGNRLIPLISAIGMSIFLQNAVMLSQDSKEKAIPTLLPGNFVFGESSMNGVVISYMQILIFVVTFLVMFGLTLFISRSRLGRACRACAEDLKMTNLLGINSNNIIALTFVIGAALAAVAAVLLGMQYGVINPGIGFLAGIKAFTAAVLGGIGSIPGAMLGGLLLGVAEAFGADVFGDQYKDVVAFGLLILVLLFRPTGILGRPEVEKV", "text": "FUNCTION: Component of the high affinity leucine, isoleucine, valine, transport system (LIV-I), which is operative without Na(+) and is specific for alanine and threonine, in addition to branched-chain amino acids. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. LivHM subfamily."}
+{"protein": "MPESNSAEGSDRSEEQVSGAKVIAQALKTQDVEYMFGVVGIPVTEIALAAQELGIKYIGMRNEQAACYAASAVGYLTGRPGVCLVVSGPGLIHALGGMANANMNCWPLIVIGGSSERNQEAMGAFQEFPQVEACRLYTKFSARPSTIELIPFIIEKAVRSSIYGRPGACYIDIPADFVTLQANVTSIKYKECCMPPPVSMAETSAVCAAASVLRDAKQPLLIIGKGAAYSHAEDSIRKLVEQCSLPFLPTPMGKGVVPDNHPNCVGAARSRALQSADVIVLFGARLNWILHFGLPPRYQADVKFIQIDICAEELGNNVRPSVILLGDIDAVSKQLLEQFDKTPWQCPPDSQWWKTLREKMKSNEAISKELASQKSLPMNYYTVFYHVQEQLPRDSFIVSEGANTMDIGRTMLQNCLPRHRLDAGSFGTMGVGLGFAIAAALVAKDRSPGQRVICVEGDSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDADTWEKMLHFQEAATTVPPMCLLPNSHYEQVMTAFGGKGYFVRTPEELQHSLRQALQDTSKPCLLNIMIEPQSTRKAQDFHWLTRSNM", "text": "FUNCTION: Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner (By similarity). Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids (By similarity). Plays a significant role in the biosynthesis of heptadecanal in the liver (PubMed:29027957). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the TPP enzyme family."}
+{"protein": "MSGSKQGSEKASITSLIDSEEQGDEATSVSTQNQSPKTQITQTENVEVQNSDLKVTENKPKNTEMKPTDPNTNASTTENTPITTSNAQVSEKSEKTVPAWMREPEEAQNRYDRYVPRVDNRRRGEPRVAEVRQDPRYAKYLRQDQEERRIRRPDDEYEGDHKRRRPEMVTQFDDRRQGTRKNHPGQAGQSESEENGDEQQGDDEEETPGNEEPVEAQPYSRLATSVQSTQHYHTFQSHIANKENKDINSIVRSHYNQRTIQSKMQGSRTKSPIYKLRNFNNAVKYMLLGNHVRKNPNPGSPTVILDMCCGKGGDLNKAEFVGADQYVGIDISDASVKEAFHRYRRNKARFIPRDGGRAGQRDSRKYNFEACFATGDCFQQSIPEILEPNFPGIVNGLFPVDCVSIQFSMHYSFESEERVRTMLNNVSKSLRPGGTFVGTIPSSDFIRDKIVNKDFLPGTNNKFGNELYSVTFDRTPPSDGIFRPPFGNKYDYFLKDAVDNVPEYVVPFEVFRSMCEEVGLTLRYKKNFIEIFNQEIPKYFHKLNRNLVDGMKRADGKYGAEGAEKEAVSFYLGFAFEKLG", "text": "FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family."}
+{"protein": "MDLLQFLAAFSVLLWPGTEVTGALKSTLDPSLKIYKKMFEVKRREQLLALKNLAQLNDIHQQYKILDVMLKGLFKVLEDSRTVLIAADVLPDGPVPQDEKLKDAFSHVVENTAFFGDVVLRFPKIVHHYFDHNSNWNLLIRWGISFCNQTGVFDQGPHSPILSLMAQELGITEKDSDFRNPFKTDQTEFIPSTDPFQKALREEEKRRKKEERRKEIRKGPRISRSQSEL", "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. Enhances cytotoxic anti-tumor activity of CD8(+) T cells. May inhibit ERK and JNK signaling activity. May suppress cell migration and invasion activity, via its effects on ERK and JNK signaling. Has a critical role in the regulation of osteogenesis and bone development. SUBCELLULAR LOCATION: Nucleus Cytoplasm Secreted Endoplasmic reticulum Note=Accumulates in the nucleus in response to UV irradiation. SIMILARITY: Belongs to the CCDC134 family."}
+{"protein": "MHNKIYNSFIDRKAKGIKSFAVLIDPDKVNPADIADLAAKCTAAKVDYIFLGGSLVITNHLDECVQQFKTLCDIPVVLFPGSPSQVSRYADALLYLSVISGRNPELLIGQHVLSAPAVKKSGLEVISTGYVLIDGGAPTTVSYISNTTPIPSDKDDIAMCTAMAGEMLGMKVVFMDAGSGARKPITESMISRVASQVSAPIIVGGGIRDAEKAYLNCKAGADIIVVGNAIEKETSLIKEMADAVHAAAPVLK", "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). SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group II subfamily."}
+{"protein": "MASISSLGVGSGLDLSSILDSLTAAQKATLTPISNQQSSFTAKLSAYGTLKSALTTFQTANTALSKADLFSATSTTSSTTAFSATTAGNAIAGKYTISVTHLAQAQTLTTRTTRDDTKTAIATSDSKLTIQQGGDKDPITIDISAANSSLSGIRDAINNAKAGVSASIINVGNGEYRLSVTSNDTGLDNAMTLSVSGDDALQSFMGYDASASSNGMEVSVAAQNAQLTVNNVAIENSSNTISDALENITLNLNDVTTGNQTLTITQDTSKAQTAIKDWVNAYNSLIDTFSSLTKYTAVDAGADSQSSSNGALLGDSTLRTIQTQLKSMLSNTVSSSSYKTLAQIGITTDPSDGKLELDADKLTAALKKDASGVGALIVGDGKKTGITTTIGSNLTSWLSTTGIIKAATDGVSKTLNKLTKDYNAASDRIDAQVARYKEQFTQLDVLMTSLNSTSSYLTQQFENNSNSK", "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. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the FliD family."}
+{"protein": "MNGINTANEEITRSLEESLNICKQSSRLMQRNLQTGRLMDAFRNCSISLVEMRNSALTPKQYYELYMFNMESLRLLGGTLLETHLNGTHNLMDLYELVQYAGSIVPRLYLMITVGSAYLETPNALVREIMNDLLDMCRGVQHPLRGLFLRHYLLTQTRKGLPLGSEDEEDASRKGTVLDSVKFLVINFTEMNKLWVRIQHLGPIKEFSKRTQERNELKVLVGLNLVRLSQLNLDIDTYRDHVLPAIIEQIIECRDSLAQEYLVEVICQAFSDNMHLQTLDTYFGTVIKLSPSVNVTQLVVAMLNRLTDYVQREYESDSSNEDESETVTEKLGDIKINEEVQQKDEQECPGDKVIPPEYAIQEVLWSHVVEVIQSRSGLPLDCIVSILSSILNFFLRCYPYKPQYADRVFQYINEHIINQPSLRSALHERPLQKSLCAILLLPLTYFPSFSYCLELQNFLPVFNAQDPNLRYDIARMIVQKIIEKGHSLSELTEAQELLGFVSVIIEKKGVDSLDDLQNVALMVHYLNNDDPQIQIEILRSLKDTFIKAGENVKYLLPVVVNRCIFLARNFRIFKCMDWAEKVRLLWEFVNTCINVLYKNGDSLELCLALYLSAAEMADQENYPDFAYEFFTQAFSIYEESVLDSELQYQQLLMIIGKLQKTRNFSVDDYDTLITKCTLYASKLLKKPDQCCGIYLASHLWWQVASGEDSRPFQDPKRVLECLQKSLKIADACMDQLTSLKLFINILERYFYYYDQHCESIIAKHISGLIDLTEQNMRSILISSPADLIASDPRAYASSIWEVANVSVIDSLKNHLERATAYAEKRSEDERWSSIFQ", "text": "FUNCTION: Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor vps10. Required to form proper forespore membranes. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the VPS35 family."}
+{"protein": "GSGASGSMPATTS", "text": "FUNCTION: Up-regulated in CNS of active, non-hibernating snails suggesting involvement in the regulation of hibernation and maintenance of the active state."}
+{"protein": "MILNSSTEDGIKRIQDDCPKAGRHNYIFIMIPTLYSIIFVVGLFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASGSVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPTIIHRNVFFIENTNITVCAFHYESQNSTLPVGLGLTKNILGFLFPFLIILTSYTLIWKTLKKAYEIQKNKPRKDDIFKIILAIVLFFFFSWVPHQIFTFMDVLIQLGLIRDCKIEDIVDTAMPITICLAYFNNCLNPPFYGFLGKKFKKYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSENGNSSTKKPAPCTEVE", "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": "MTFPVEKVRADFPILQREVNGLPLAYLDSAASAQKPNQVIDAESAFYRHGYAAVHRGIHTLSAQATESMENVRKQASRFINARSAEELVFVRGTTEGINLVANSWGTENIRAGDNIIISEMEHHANIVPWQMLCERKGAELRVIPLHPDGTLRLETLAALFDDRTRLLAITHVSNVLGTENPLPDMIALARQHGAKVLVDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGILYIKEALLQEMPPWEGGGSMISTVSLTQGTTWAKAPWRFEAGTPNTGGIIGLGAAIDYVTSLGLDKIGDYEQMLMRYALEQLAQVPDITLYGPAQRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAWYGVPAMCRASLAMYNTHEEVDRLVAGLTRIHRLLG", "text": "FUNCTION: Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily."}
+{"protein": "MSSGANITYASRKRRKPVQKTVKPVPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSTPADRSRGQDQCRAQVRDWQDLQEGEFLLQALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPSQCTDSAQGVDETHGLPQPAVYYTPDQLPPENTAFMERCFRCRLRCLLDNSSGFLAMNFQGRLKYLHGQNKKGKDGALLPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGQLILGYTEVELCNKGSGYQFIHAADMLHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIYRNGRPDYIIATQRPLTDEEGREHLQKRSMTLPFMFATGEAVLYEISSPFSPIMDPLPIRTKSNTSRKDWAPQSTPSKDSFHPNSLMSALIQQDESIYLCPPSSPAPLDSHFLMDSMSECGSWQGSFAVASNEALLKHEEIRHTQDVNLTLSGGPSELFPDNKNNDLYSIMRNLGIDFEDIRSMQNEEFFRTDSSGEVDFKDIDITDEILTYVQDSLNNSTLLNSACQQQPVSQHLSCMLQERLQLEQQQQLQQQHPTQTLEPQRQLCQVEVPQHELGQKTKHMQVNGMFASWNPAPPVSFSCPQQERKHYSLFSGLQGTAQEFPYKSEVDSMPYTQNFAPCNQSLLPEHSKGTQLDFPGRDFERSLHPNASNLEDFVSCLQVPENQRHGINSQSAMVSPQAYYAGAMSMYQCQAGPQHTPVDQMQYSPEIPGSQAFLSKFQSPSILNEAYSADLSSIGHLQTAAHLPRLAEAQPLPDITPSGFL", "text": "FUNCTION: Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed:7812217). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation. Xenobiotics can act as ligands: upon xenobiotic- binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists. Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands. Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus."}
+{"protein": "EAGEECDCGSPANPCCDAATCKLRPGAQCADGLCCDQCRFIKKGTVCRPARGDWNDDTCTGQSADCPRNGLYG", "text": "FUNCTION: [Disintegrin mojastin-2]: Inhibits ADP-induced platelet aggregation (IC(50) = 13.8 nM) probably by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) located on the platelet surface. FUNCTION: [Disintegrin mojastin-1]: Inhibits the three processes involved in platelet function (adhesion, activation and aggregation). It inhibits platelet adhesion to fibronectin with an IC(50) of 58.6 nM. It inhibits ATP release from platelet induced by ADP with an IC(50) of 19.5 nM on platelet-rich plasma, probably by binding to ADP receptors (P2RY1 and P2RY12). Finally, it inhibits ADP-induced platelet aggregation with IC(50) of 44.7 nM on platelet-rich plasma and 19.3 nM on whole blood, probably by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) (PubMed:20598348). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily."}
+{"protein": "MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVRKDHLGKSEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA", "text": "FUNCTION: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (By similarity). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane Nucleus Synapse Secreted Cell projection, axon Note=Membrane-bound in dopaminergic neurons (By similarity). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (By similarity). SIMILARITY: Belongs to the synuclein family."}
+{"protein": "MITTVVGSYPTEPRGPETLGERLLNFFGSYDRYRPAIEAAVRDQFRAGVDIISDGQVRGDMVGHFAAAIGGMKIEDGTSIIYSRITPPAGSIGAADLRYAYRILRGLTDDESRGVKGIITGPSTMIYASRIEGFYDPQKRDRAVMDMAGVLKIEAKHLQDAGAAMIQIDEPFLSTGIVDMKTAGRAIDHIAAGLDIEVSLHVCGDIRNVLSDLLRFKVDVLDLEFAGRPSNLEVLEEKWRGDKGVGFGCVDTTTERVESMEEIRNLIKRGADIVGEENLYIDPDCGMRKLPRKAAFSKLRNMVMAAGN", "text": "FUNCTION: Catalyzes the transfer of a methyl group to L-homocysteine resulting in methionine formation. Can use methylcobalamin and methylcobinamide as methyl donors, but methylcobalamin is not considered to be the physiological substrate. SIMILARITY: Belongs to the archaeal MetE family."}
+{"protein": "MSAVEIPHPSGCRVYDIRQQAQGSMNLQTAITDGLLSTPKTLPSLLLWDAEGLRLFDEFAHSASYYLRDKELTILRDRSHEIVTVVPAQSILVELGSLQKTGRLIRALEKQQKPVRYYAVDVSLSGLTNSLTELRKELGDLHFVDITGLLGTYDDCVNWISNPSGQDPMSSPTVTFLWMGNSISNLNHYIDSSSLLSQFRLACDASRLRCQFLIAADACQDAQVVRTAYDAQNPTLRAFLLNGLSHANSVLGRAAFSPQDWSCESGFYPEQGQLEVYYVPLRDVELDVGGDRVYRVQRGERVRAISSGKWGKKLMGRVACAAGFQMNHAWGDSAGQYYFYHLYGGTQTFTSGNERVSVAHR", "text": "FUNCTION: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of benzomalvin A and D (PubMed:28604695). The pathway begins with the loading of amino acid precursors onto the A domains of the non ribosomal peptide synthetases benY and benZ (PubMed:28604695). BenY and the A1 domain of benZ are loaded with anthranilate (Anth), while the A2 domain of benZ is loaded with phenylalanine (Phe) (PubMed:28604695). N-methylation of Phe by the methyltransferase benX may happen before loading of Phe onto benZ, after loading of Phe, or after dipeptide formation (PubMed:28604695). Condensation of Anth with the secondary amine of NmPhe or Phe is catalyzed by the C1 domain of benZ, forming a dipeptide intermediate (PubMed:28604695). This is followed by in trans condensation of the Anth-NmPhe dipeptide with Anth bound to the T domain of benY by the C2 domain of benZ to form the linear tripeptide Anth-NmPhe-Anth (PubMed:28604695). Cyclization and release of the tripeptide is then catalyzed by the C-terminal C domain of benY and the resulting 11-member macrocyclic intermediate is expected to spontaneously collapse to form the benzodiazepine core (PubMed:28604695). Benzomalvin A is in conformational equilibrium with its atropisomer, benzomalvin D (PubMed:28604695). SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "MKGTLLLLALLVTGELGFQTTEACIPFYEAFGAVVLGNKQVLDVVLSKFNATDKEREAFEKIQECYNDGGLKSKLLDTRVVYEVTVNSPCKEYYTKDTILKVEDLLFQIQRHIMG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the secretoglobin family."}
+{"protein": "MSKTLNIIWQYLRAFVLIYACLYAGIFIASLLPVTIPGSIIGMLILSVLLALQILPAKWVNPGCYVLIRYMALLFVPIGVGVMQYFDLLRAQFGPVVVSCAVSTLVVFLVVSWSSQLVHGERKVVGQKGSEE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0299 family."}
+{"protein": "MAGSGVRQATSTASTFVKPIFSRDMNEAKRRVRELYRAWYREVPNTVHQFQLDITVKMGRDKVREMFMKNAHVTDPRVVDLLVIKGKIELEETIKVWKQRTHVMRFFHETEAPRPKDFLSKFYVGHDP", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly. 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 to be not involved in catalysis. Required for proper complex I assembly (PubMed:30245030). 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 LYR family."}
+{"protein": "MAWMLLLILIMVHPGSCALWVSQPPEIRTLEGSSAFLPCSFNASQGRLAIGSVTWFRDEVVPGKEVRNETPEFRGRLAPLASSRFLHDHQAELHIRDVRGHDASIYVCRVEVLGLGVGTGNGTRLVVEKEHPQLGAGTVLLLRAGFYAVSFLSVAVGSTVYYQGKCLTWKGPRRQLPAVVPAPLPPPCGSSAQLLPPVPGG", "text": "FUNCTION: Cell membrane receptor of natural killer/NK cells that is activated by binding of extracellular ligands including BAG6 and NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring cells producing these ligands. It controls, for instance, NK cells cytotoxicity against tumor cells. Engagement of NCR3 by BAG6 also promotes myeloid dendritic cells (DC) maturation, both through killing DCs that did not acquire a mature phenotype, and inducing the release by NK cells of TNFA and IFNG that promote DC maturation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the natural cytotoxicity receptor (NCR) family."}
+{"protein": "MVAWRAAGLNYVRYSQIAAQVVRQCTKGGANVKKPQATLKTTAWENGKMVSKSQ", "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. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase epsilon family."}
+{"protein": "MKVLIIFAHPEPQSLNGALHRVAVEELEEQGHHVQVSDLYKMKWKSEVDREDFPNFPKDQRLDLWTASAEAYAENSLTQDVLDEQAKLRWADFVIFHFPLWWFTMPAILKGWVDRVYTYGFGHGLGEHSDKRWGDRYGEGTLTGKRAMLIVTLGGWKEHYSARGISGPIEDVLFPINHGILFYPGFEVLPPFVAFRVHKTSFDEMASTLRKRMREIEFTKPIPYRNQNDGEYSIPTLTLHESHGGDLASGFGLHTRTEVETTDVKEA", "text": "FUNCTION: Ribosyldihydronicotinamide dehydrogenase-like protein; part of the tra gene cluster that produces terrestric acid (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 NAD(P)H dehydrogenase (quinone) family."}
+{"protein": "MVSTKVKPTTTTTPTTTVNKTTQPTTTTTASKKVKQTKQSKAQAKEIQELASTPSVKQIQSQKVLVPKLEETKPITPPDQEEEDQEEEEQEQEEEENENNDNNTGNVSEKELGISKESIEFSNLPIEENTKKSIEEMGFKKMTPIQAKSILPLLEGKDLLGAARTGSGKTLAFLIPAIEVLVKSNFKPRNGTGVIIISPTRELALQIYGVARELMKYHTQTHGIVIGGASKKPEEERLEKGVNLLVATPGRLLDHLQNTKGFITKNLKCLIIDEADRILEVGFEEEMHQIIKKVPKTRQTMLFSATQTRKVDDIAKVSLNNSPVYVGVDDEREISTVEGLEQGYVVCPSERRFLLLYTFLKKNLSKKIIVFLSSCNAVKYTAELLNYIDIPVLELHGRQKQQKRTNTFYEFVNAEKGILICTDVAARGLDIPSVDWIIQYDPPDDPKEYIHRVGRTARGVGKKGRALLFLLPKELGFLKYLKLAKVPLNEYEFPKSKIANVQDQLEKVVSQNFYLYNSARDAYKAYICAYASHSLKDIFDVNALDLQCVAKAFGFLDPPKVNLNVNSSGKADFQKKSNNKSGFAQKQYGSKFPPKDGRQFDR", "text": "FUNCTION: ATP-binding RNA helicase which may be involved in the ribosome biogenesis. SUBCELLULAR LOCATION: Nucleus, nucleolus Chromosome. SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily."}
+{"protein": "MSGGLDILSLKEDDITKMLVATTHLGSENVNFQMEQYVYKRRADGVNILNLGKTWEKLQLAARAIVAIDNPSDIFVISSRPIGQRAVLKFAKYTDTTPIAGRFTPGAFTNQIQPAFREPRLLVVTDPNTDHQPIMEASYVNIPVIAFTNTDSPLRYIDIAIPCNNKSAHSIGLMWWLLAREVLRLRGTISRSVEWPVVVDLFFYRDPEEAEKEEAAAKELLPPPKIEEAVDHPVEETTNWADEVAAETVGGVEDWNEDTVKTSWGSDGQF", "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. 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. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=May associate with nascent RNP complexes within the nucleus. SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
+{"protein": "MAAARPIILRFESRNGQFRLSVSPQEQFPLLQEKILENLPKDVEPSSLVLSNKPIGTGGQERQLKDLAGVSIERVGLKHGDKLFIGYQDKQASQAAPAHKHVTADVSRRLNGAPVPETETVTFHPPTSPSATIKNPWEVVQQSPLDDMLDKKDGKIYRPRDPKMCNHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYMRKVNATTNKAELKSSFMPPLNEPYYRVRRDCPSGHPPWPEGICTKCQPSAISLQPQEFRMVDHVEFASPDLINSLLDFWRKSGAQRLGFLYGTYEEYTEVPLGIKAVVQAIYEPPQVDEIDGITLHEWPNEKEVDEVARQCGLEKVGVIFTDLLDAGRGDGSVVCKRHIDSYYLSSLEIAFASRMQAKHPKATKWSRTGRFGSNFVTCVLSGDEEGAITVSSYQASISAVEMVRADIVEPSAEPSVMLVQSEDDDTDNKSRYIPEVFYRKINEYGVSAQQNAKPSFPVEYLLVTLTHGFPTEASPMFSASTFPIENREVIGESQELRHVAKKLVSHGDPDKAIREVSDFHLLCFLHSLSMFSKEEEALLCRVATTHDPTEGLKLLNTPGWATLVTVLQESGERPPKRPWLNPADPPRPLSQQGKRHLSSRPESPKSESEQLAKRFKGASLE", "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": "MSVRRRTHSDDFSFRLERTRRPSKLDVLRESPTLPVQQGYSLTTVVLVSLVVTLVCQNVAPPAFSYLNQLIKNSPKRKIPGQSNRLNIGFISTNSPEKFAPAVQKPTFLVDPIYDEKWKGVHTAVPVMTTEPEEKRDNNHAKVKEAILAAKAASRSRRDGNLERAVTIMEHAMALAPNNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTNPLVSAIDRKMLKTVHDLRNEFAHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSKEHHEISIDDILEMHRRVLGNADPVEAGKIRTTQVYVGKFTPVAPEYVLEQLADMVDWLNDESTMAMDPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSGNVINGEEPNLTAEESKVSEKIETECRAGS", "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-273 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins. In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2. Can AMPylate core histone H3 in vitro (By similarity). Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus membrane; Single-pass membrane protein Note=Predominantly localized to the endoplasmic reticulum and to the nucleus. SIMILARITY: Belongs to the fic family."}
+{"protein": "MAPKVTSELLRQLRQAMRNSECVAEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDNNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLVPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLFIDGDRIDAPGVKQHLLLDLGLEAEYKIQVLPYKSILSELKTLCADLSPREKVWVSDKASYAVSEAIPKDHRCCMPYTPICIAKAVKNSAESAGMRRAHIKDAVALCELFNWLEQEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGRQEALEWLLRETEPISRQH", "text": "FUNCTION: Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg- Pro-Pro (PubMed:10095056). Contributes to the degradation of bradykinin (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M24B family."}
+{"protein": "GCIKTGSFCTLSKGCCTKNCGWNFHCNPPNQ", "text": "FUNCTION: Highly potent toxin against both insect and some mammalian sodium channels (Nav) (PubMed:34445875). It potently inhibits inactivation of insect sodium channels of B.germanica (BgNav1) (EC(50)=2.6 nM) and also delays the inactivation of mammalian Nav with potent activity on Nav1.1/SCN1A (hNav1.1/SCN1A; EC(50)=7.9 nM, rNav1.2/SCN2A; EC(50)=24.3 nM, rNav1.3/SCN3A; EC(50)=105.6 nM, rNav1.4/SCN4A; EC(50)=46.4 nM, hNav1.5/SCN5A; EC(50)=215.2 nM, mNav1.6/SCN8A; EC(50)=36.3 nM, hNav1.9/SCN9A; EC(50)=97.2 nM) (PubMed:34445875). 1 uM is enough to completely inhibits the inactivation, resulting in sustained non-inactivating currents (By similarity). In addition, the toxin significantly enhances the recovery from inactivation, and the open state is not required for the toxin to interact with the channel (By similarity). In vivo, injection into brine shrimp (Artemia salina) stops movement or causes death after 24 hours (EC(50)=2.8 uM) (PubMed:34445875). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the nemertide family."}
+{"protein": "MDGEEAADIDETNSSNPHAAAVVATEMQAVAEAERPEEQQQQQMPQTSSGEADGDVDGDGVSAIAALATRVRLENMLEVVDNMFDEVSELMVDVTELMQRASELTGTTTPTPTAPENQAENAPEIEPAQPATPPEIAELLEEAIAANPLGHNVLNPGDDARSISSRHSGSDMSLDSPGSEDDSDAEAVPRWIIPENRVRSAVDMLVSQARNQDGGIATLLRRENFLQRVRSMVFSQDRVRGRESDEANLDAGNVVDEELSPELSPAPLDIDMEEGVRFDTNLPAEHSYFGPNLNRVPGVDYLEVGSTHRMLIFMHQHILFPGEVLPFMIDGSIIDEEIHDTGRDGVIFGVGFPLMQPPDDNPHKLYGVTCQIYEKGESGRQMVFYKSRALQRIVINCDDIQGPPQYIARNPTMKCYSKVKVLPEYFLPEPLKCIDMGSLNRFRDLPSMQDKFRRYQLTSTPWPLEACEEYSFEHIVEMARKKLEVHKIDTMPKCPIQLSYWLVRNLHLTEKMMRLTFLTDSVNTRLQIIGSTLKQESLFYCRYCNSSLAYCSDLFAMSKHGVQTQYCNSAGYIHETNTVYRIIAHAVGYSGEPSTEFSWFPGYQWHIIICKFCAQHVGWEFKAVDPNLAPKVFFGLAGSSVRIGKTSERTPTQGNPFVVRNLLHLVFREIE", "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. Has an essential role in mediating growth by negatively regulating insulin signaling. It also has a role in maintaining presynaptic function in the neuromuscular junction synapses of third-instar larvae. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CRBN family."}
+{"protein": "MPVLHNRISNDALKAKMLAESEPRITISFYKYFHIADPKATRDALYQLFTALDVFGRVYLAHEGINAQISVPASNVETFRAQLYAFDPALEGLRLNIALDDDGKSFWVLRMKVRDRIVSDGIDDPHFDASNVGEYLQAAEVNAMLDDPDALFIDMRNHYEYEVGHFENALEIPADTFREQLPKAVEMMQAHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARKAREQGLPVRFIGKNFVFDERMGERISDEIIAHCHQCGAPCDSHTNCKNDGCHLLFIQCPVCAEKYKGCCSEICCEESALPPEEQRRRRAGRENSNKIFNKSRGRLNTTLGIPDPTE", "text": "FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5- carboxymethoxyuridine (cmo5U) biosynthesis. May be part of an alternate pathway, which is able to bypass cmo5U biogenesis in a subset of tRNAs under aerobic conditions. SIMILARITY: Belongs to the TrhO family."}
+{"protein": "MAGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDFFIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTPENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVKEFNKYDTDGSKWIKQYTGVNAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKPKPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS", "text": "FUNCTION: ATP-binding 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. Seems to contact the pointed end of the daughter actin filament. In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation. 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). Plays a role in ciliogenesis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection Nucleus Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection Nucleus Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes). SIMILARITY: Belongs to the actin family. ARP3 subfamily."}
+{"protein": "MKLSCLVFLIVSSLVSSSLATAPPNTSIYESFLQCFSNQTGAPPEKLCDVVLPQSSASFTPTLRAYIRNARFNTSTSPKPLLVIAARSECHVQATVLCTKSLNFQLKTRSGGHDYDGVSYISNRPFFVLDMSYLRNITVDMSDDGGSAWVGAGATLGEVYYNIWQSSKTHGTHGFPAGVCPTVGAGGHISGGGYGNMIRKYGLSVDYVTDAKIVDVNGRILDRKSMGEDLFWAIGGGGGASFGVILSFKIKLVPVPPRVTVFRVEKTLVENALDMVHKWQFVAPKTSPDLFMRLMLQPVTRNTTQTVRASVVALFLGKQSDLMSLLTKEFPELGLKPENCTEMTWIQSVMWWANNDNATVIKPEILLDRNPDSASFLKRKSDYVEKEISKDGLDFLCKKLMEAGKLGLVFNPYGGKMSEVATTATPFPHRKRLFKVQHSMNWKDPGTDVESSFMEKTRSFYSYMAPFVTKNPRHTYLNYRDLDIGINSHGPNSYREAEVYGRKYFGENFDRLVKVKTAVDPENFFRDEQSIPTLPTKPSSS", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
+{"protein": "MKKVVTVCPYCASGCKINLVVDNGKIVRAEAAQGKTNQGTLCLKGYYGWDFINDTQILTPRLKTPMIRRQRGGKLEPVSWDEALNYVAERLSAIKEKYGPDAIQTTGSSRGTGNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDKAFVASRTEGFEEYRKIVEGYTPESVEDITGVSASEIRQAARMYAQAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTGNLGKPHAGVNPVRGQNNVQGACDMGALPDTYPGYQYVKDPANREKFAKAWGVESLPAHTGYRISELPHRAAHGEVRAAYIMGEDPLQTDAELSAVRKAFEDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVFTAADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGFIQWPCRDTSDADQGTSYLFKEKFDTPNGLAQFFTCDWVAPIDKLTDEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPGYAQINTEDAKRLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQWWIGACNELVTENLSPITKTPEYKYCAVRVEPIADQRAAEQYVIDEYNKLKTRLREAALA", "text": "FUNCTION: Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family."}
+{"protein": "MISICCSRFSCILFLLFLIFSLVLSYIWWSPTKGGTNPEVLPVVLWHGMGDTCCVPFSLGAIMNLIVEQTKGGYVRSLQIGGNVLIDWQSGFFIHPNEQVDYVCKQLLQDEHLAKGYHAIGFSQGGQFLRAVAERCPNPPMRNLITLGGQHQGIFGLPMCPTLTEKPCDYITRLLDNAAYAPEVQKALVQATYWHDPIMENKYRLGSTFLADINNELFINKFYIENLQKLKKFVMVQFLNDTIVQPKESQWFQYYTTGQNKVIQPFTESKVYQDLGLDKMHRQGQLVFLGVEGDHLAISKAWFIQNIVPLLLEK", "text": "FUNCTION: Cleaves thioester-linked long fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the palmitoyl-protein thioesterase family."}
+{"protein": "MPKLEMMLLVLLILPLCYIDAVGPPPPWNMEDEIIEHWQKLHCHEISDPTPWILCSPEPLCGGKGCCAQEVCDCSGPVCTCPPCL", "text": "FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin D superfamily."}
+{"protein": "NRQPSKYGLEETI", "text": "SIMILARITY: Belongs to the 11S seed storage protein (globulins) family."}
+{"protein": "MHLLPEQATRHAVSIPELLVSRDERQARQHAWLTRHLTPLVSFTVVAPGPIKDSELTRRIFNHGVTALLAVAKKAGWSVREQAALASASGPEGFLAIEAPARDLKLATIELEHQHPLGRLWDIDVLTPEGDILSRRHFSLPARRCLLCEQSAAECARGKTHALSDLLIRMEALLHDADSSHIN", "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": "MDYEASRIVEMVEDEEHIDLPPGFRFHPTDEELITHYLKPKVFNTFFSATAIGEVDLNKIEPWDLPWKAKMGEKEWYFFCVRDRKYPTGLRTNRATEAGYWKATGKDKEIFKGKSLVGMKKTLVFYKGRAPKGVKTNWVMHEYRLEGKYCIENLPQTAKNEWVICRVFQKRADGTKVPMSMLDPHINRMEPAGLPSLMDCSQRDSFTGSSSHVTCFSDQETEDKRLVHESKDGFGSLFYSDPLFLQDNYSLMKLLLDGQETQFSGKPFDGRDSSGTEELDCVWNF", "text": "FUNCTION: Transcription activator that binds to DNA in promoters of target genes on a specific bipartite motif 5'-[ACG][CA]GT[AG](5- 6n)[CT]AC[AG]-3' (PubMed:23340744). Promotes lateral root development (PubMed:16359384). Triggers the expression of senescence-associated genes during age-, salt- and dark-induced senescence through a regulatory network that may involve cross-talk with salt- and H(2)O(2)- dependent signaling pathways (PubMed:9351240, PubMed:15295076, PubMed:20113437, PubMed:21303842). Regulates also genes during seed germination (PubMed:20113437). Regulates positively aging-induced cell death (PubMed:19229035). Involved in age-related resistance (ARR) against Pseudomonas syringae pv. tomato and Hyaloperonospora arabidopsidis (PubMed:19694953). Antagonizes GLK1 and GLK2 transcriptional activity, shifting the balance from chloroplast maintenance towards deterioration during leaf senescence (PubMed:23459204). Promotes the expression of senescence-associated genes, including ENDO1/BFN1, SWEET15/SAG29 and SINA1/At3g13672, during senescence onset (PubMed:23340744). SUBCELLULAR LOCATION: Nucleus Note=Localizes in the nucleus, where it interacts with NLA."}
+{"protein": "MSAPSTSTVVRVPFTELQSLLQAIFQRHGCSEAVARVLAHNCASAQRDGAHSHGVFRMPGYVSTLASGWVDGQATPQVSDVAAGYVRVDAAGGFAQPALAAARELLVAKARSAGIAVLAIHNSHHFAALWPDVEPFAEEGLVALSVVNSMTCVVPHGARKPLFGTNPIAFAAPCAEHDPIVFDMATSAMAHGDVQIAARAGQQLPEGMGVDADGQPTTDPKAILEGGALLPFGGHKGSALSMMVELLAAALTGGHFSWEFDWSGHPGAKTPWTGQLIIVINPGKAEGERFAQRSRELVEHMQAVGLTRMPGERRYREREVAEEEGVAVTEQELQGLKELLG", "text": "FUNCTION: Catalyzes the reduction of both Delta(1)-pyrroline-2- carboxylate (Pyr2C) and Delta(1)-piperideine-2-carboxylate (Pip2C) to L-proline and L-pipecolate, respectively, using NADPH as the electron donor. Can use NADH instead of NADPH, although with much less efficiency. Plays an essential role in the catabolism of D-proline and D-lysine, which allows P.putida to grow on each of these amino-acids as a sole carbon source; D-lysine appears to be catabolized only through the pipecolate pathway. Can also catalyze the reverse oxidation reactions, albeit at a much lower rate. To a lesser extent, is able to catalyze in vitro the NADPH-dependent formation of N-alkyl-L-amino acids from the corresponding alpha-oxo acids and alkylamines, e.g. the formation of N-methylalanine from pyruvate and N-methylamine; cannot use ammonia as substrate for these reductive amination reactions. Shows neither malate dehydrogenase nor lactate dehydrogenase activity. SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family."}
+{"protein": "MKGSISYQIYKGALLLSALLNSVSAQQVGTLTAETHPALTWSKCTAGXCSQVSGSVVIDANWPXVHSTSGSTNCYTGNTWDATLCPDDVTCAANCAVDGARRQHLRVTTSGNSLRINFVTTASQKNIGSRLYLLENDTTYQKFNLLNQEFTFDVDVSNLPCGLNGALYFVDMDADGGMAKYPTNKAGAKYGTGYCDSQCPRDLKFINGQANVDGWTPSKNDVNSGIGNHGSCCAEMDIWEANSISNAVTPHPCDTPSQTMCTGQRCGGTYSTDRYGGTCDPDGCDFNPYRMGVTNFYGPGETIDTKSPFTVVTQFLTNDGTSTGTLSEIKRFYVQGGKVIGNPQSTIVGVSGNSITDSWCNAQKSAFGDTNEFSKHGGMAGMGAGLADGMVLVMSLWDDHASDMLWLDSTYPTNATSTTPGAKRGTCDISRRPNTVESTYPNAYVIYSNIKTGPLNSTFTGGTTSSSSTTTTTSKSTSTSSSSKTTTTVTTTTTSSGSSGTGARDWAQCGGNGWTGPTTCVSPYTCTKQNDWYSQCL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family."}
+{"protein": "MESQQLSNYPNISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENLHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPETY", "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": "MQNDAGEFVDLYCPRKCSASNRLIHAKDHASVQLVIADVDPATGRAADSSKMYVVCGAIRRMGESDDCIVRLTKKDGILVKNY", "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 eukaryotic ribosomal protein eS21 family."}
+{"protein": "MITKQLRSWLAVLVGSSLLALPLSGQAVGKKESRVSELPQDVLLKEISGGFSKVATKATPAVVYIESFPKSQAVTHPSPGRRGPYENPFDYFNDEFFNRFFGLPSQREKPQSKEAVRGTGFLVSPDGYIVTNNHVVEDTGKIHVTLHDGQKYPATVIGLDPKTDLAVIKIKSQNLPYLSFGNSDHLKVGDWAIAIGNPFGLQATVTVGVISAKGRNQLHIADFEDFIQTDAAINPGNSGGPLLNIDGQVIGVNTAIVSGSGGYIGIGFAIPSLMANRIIDQLIRDGQVTRGFLGVTLQPIDAELAACYKLEKVYGALVTDVVKGSPADKAGLKQEDVIIAYNGKEVDSLSMFRNAVSLMNPDTRIVLKVVREGKVIEIPVTVSQAPKEDGMSALQRVGIRVQNLTPETAKKLGIAPETKGILIISVEPGSVAASSGIAPGQLILAVNRQKVSSIEDLNRTLKDSNNENILLMVSQGDVIRFIALKPEE", "text": "FUNCTION: Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the peptidase S1C family."}
+{"protein": "MRYIRLCIISLLATLPLAVHASPQPLEQIKQSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGASERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR", "text": "FUNCTION: This enzyme hydrolyzes cefotaxime, ceftazidime and other broad spectrum cephalosporins. SIMILARITY: Belongs to the class-A beta-lactamase family."}
+{"protein": "MSNKLATVGNNLDSRYTMAGGIRRQINKVFPTHWSFLLGEIALYSFIILILTGVYLTLFFDPSITKVIYDGAYLPLNGVEMSRAYMTALDISFEVRGGLFVRQMHHWAALMFVVSMMVHMMRIFFTGAFRRPREANWVIGVVLLILGIAEGFMGYSLPDDLLSGVGLRIMSAIIVGLPIIGTWMHWMIFGGDFPSDIMLDRFYIAHVLIIPGIILGLIAAHLALVWYQKHTQFPGAGRTENNVIGIRIMPVFAVKSVAFGAITLGFLSLLAGVTTINAIWNLGPYNPSQVSAGSQPDIYMLWTDGAARVMPAWELYFGNYTVPAVFWVAIMLGILVVLLIAYPWIEKKLTGDDAHHNLLQRPRDVPVRTSLGVMALIFYILLTISGGNDIWAYQFDVSLNAMTWIGRIGLIVFPAIGYFVTYRLCIGLQRSDREVLEHGIETGVIKQMPNGAFIEVHQPLGPVDEHGHPIPLPYSGAKVPKQLNELGFAEVESRGGFFGPDPESVATKANEIAHANHLEEVATLAAIQEENRKRDQAEGRI", "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": "MLFRNIEVGRQAAKLLTRTSSRLAWQSIGASRNISTIRQQIRKTQLYNFKKTVSIRPFSLSSPVFKPHVASESNPIESRLKTSKNVAYWLIGTSGLVFGIVVLGGLTRLTESGLSITEWKPVTGTLPPMNQKEWEEEFIKYKESPEFKLLNSHIDLDEFKFIFFMEWIHRLWGRAIGAVFILPAVYFAVSKKTSGHVNKRLFGLAGLLGLQGFVGWWMVKSGLDQEQLDARKSKPTVSQYRLTTHLGTAFFLYMGMLWTGLEILRECKWIKNPVQAISLFKKLDNPAIGPMRKISLALLAVSFLTAMSGGMVAGLDAGWVYNTWPKMGERWFPSSRELMDENFCRREDKKDLWWRNLLENPVTVQLVHRTCAYVAFTSVLAAHMYAIKKKAVIPRNAMTSLHVMMGVVTLQATLGILTILYLVPISLASIHQAGALALLTSSLVFASQLRKPRAPMRNVIITLPHSSKVTSGKILSEASKLASKPL", "text": "FUNCTION: Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin YAH1 and ferredoxin reductase ARH1. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the COX15/CtaA family."}
+{"protein": "MQILTLLFAVLLLMLRAEPGLSLARGLPQDCERRGGFCSHKSCPPGIGRIGLCSKEDFCCRSRWYS", "text": "FUNCTION: Has bactericidal activity. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "MKNNTGYIIGAYPCAPSFHQKSEDEEKAFWRQLADTPDIRGLEQPCLEHLHPLGDEWLMRHTPADWQIVVTAIMETMRRRGGNGGFGLASSDEEQRKACVAYYRHLYQKINAINAANAGKIVALELHAAPCASNPNVAQATDAFARSLKEVASWDWSCSLVLEHCDAMTGPAPRKGFLPLENVLETLAGYEISVAINWARSAIEGQDTTLPLTHTRQASQAGKLGALMFSGTTLNGEYGEWQDLHAPFSPFCAQSLMTHTHVRELLACAGSDALQFLGFKLLEINPDADVNHRIAILRDGIAALNKAQQ", "text": "FUNCTION: Member of the yiaKLX1X2PQRS operon; however YiaX1 is not required for L-ascorbate utilization under aerobic conditions. SIMILARITY: Belongs to the YiaX1 family."}
+{"protein": "MATTHTLLSFDNLEFLLHRKDLTDLYGKRCGTLNLVINPYELFLPDELDDDCCDDPFNCCFSDVYASIGTEYSYIDPPDLIYEEHCATNGTWPDGTPCEPILPPFTITGTHHYYATKPGEVVSGILSKLRVFLGSLLRSTADVNSNFTFRAESDGPGSTEIVTEEQGTIVQQQPAPAPTALATLATASTGKSVEQEWMTFFSYHTSINWSTVESQGKVLYSQALNPSINPYLDHISKLYSTWSGGIDVRFTVSGSGVFGGKLAALLVPPGVEPIESVSMLQYPHVLFDARQTEPVIFTIPDIRKTLFHSMDETDTTKLVIMVYKNGADTKTTCSITVETRPSADFTFALLKPPGSLIKHGSIPSDLIPRNSAHWLGNRWWSMISGFSVQPRVFQSNRHFDFDSTTTGWSTPYYIPIEITITAKVKGNNHWYHVIAHDKALVPGIPDGWPDTTIPSEVHASNGNFDYAKGFHDDKEIVNPANNNTHFKGTYICGTLSTIKDPEKAENQSESQKKSSTMYVATADLGDNKVKPQHKISSQKLVVYFDGPEKDLTMNATLSPLGYTLVDDQPIGSNSSTVVRIATLPEAFTQGGNYPIFYVNKTNKGYFDKATTDCYNSQILMTSQRLAEGNYSLPPDSLAVYRITDSSSQWFDIGINHDGFSYVGLPDLPADLTFPLTSTFMGVQLARVKLASKVKVTRNSIK", "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 encapsulates the genomic RNA and VP2 proteins. Attaches virion to target cells. 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": "MDVCSWKEMEVALVNFDNSDEIHEEPGYATDFDPTSSKGRPGSSPFSNWRVLISDNTNHETAFSKIPGEYVDPPGPEPVVLNEGNQRVIINIAGLRFETQLRTLNQFPETLLGDREKRMQFFDSMRNEYFFDRNRPSFDGILYYYQSGGKIRRPANVPIDVFADEISFYELGSEAMDQFREDEGFIKDPETLLPTNDFHRQFWLLFEYPESSSAARGVAVVSVLVVVISITIFCLETLPEFREDRELKVVRDPSINTNKTGLSQTMFTDPFFMVESTCIVWFTFELVLRFVVCPSKTDFFKNIMNIIDIISIIPYFATLITELVQETEPSAQQNMSLAILRIIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEVDEPESHFSSIPDGFWWAVVTMTTVGYGDMCPTTPGGKIVGTLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEKPNIPGELDKILNSMGSRMGSTESLNKTNGSCSAEKSRK", "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. 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": "MARKGSSIRLSSSRISTLLLFMFATFASFYVAGRLWQESQTRVHLINELDRVTGQGKSAISVDDTLKIIACREQKKTLAALEMELSSARQEGFVSKSPKLADGTETKKRPLVVIGIMTSLGNKKKRDAVRQAWMGTGASLKKLESEKGVIARFVIGRSANKGDSMDKSIDTENSQTDDFIILDDVVEAPEEASKKVKLFFAYAADRWDAQFYAKAIDNIYVNIDALGTTLAAHLENPRAYIGCMKSGEVFSEPNHKWYEPEWWKFGDKKAYFRHAYGEMYVITHALARFVSINRDILHSYAHDDVSTGSWFVGLDVKHVDEGKFCCSAWSSEAICAGV", "text": "FUNCTION: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family."}
+{"protein": "MSTSHGYRASWWTYILHQVPHTNFQFEVVDNQFAPQEWSYQQALLFLASIAGLCLAISLVLICVYLIKFCCCASQEDDDSKSHRVCCVTWSCVAAVIICCAGIGIGFYGNSETNDGVYQVTYSLMNANHTLTSINLLVSDTVELLSSVVKSDLTQLEEIFSTRTEFVVMIRNTRRQVESVAQQLTEISSFFWKGAELNPSALAEQVNFIEDYRWLAYILLLLLDLIICLFTLLSLAKQIKWLVIVMTVVSFFVLLLSWGSMGLEMATAVGLSDFCSDPDAYVMNQTQMITNINPDILQYYISCNQDVTNPFRQRLTMSQRALSNIHSQLHGLEREAVPQFPTAERNVLVVQGMLNTTEGNFHHLVALLNCRGLHKDYVDALKGLCYDGMEGILFLLLFSFLSALSFTAAVCSLPRAWKRFRNRDLDYDDMDEDDPFNPQESKRFVQWQSSI", "text": "FUNCTION: Probable chloride channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tweety family."}
+{"protein": "MAEGFVSFGLEKLWDLLSRESERLQGIDEQLDGLKRQLRSLQSLLKDADAKKHGSDRVRNFLEDVKDLVFDAEDIIESYVLNKLRGEGKGVKKHVRRLARFLTDRHKVASDIEGITKRISDVIGEMQSFGIQQIIDGVRSLSLQERQRVQREIRQTYPDSSESDLVGVEQSVEELVGHLVENDIYQVVSIAGMGGIGKTTLARQVFHHDLVRRHFDGFAWVCVSQQFTLKHVWQRILQELQPHDGNILQMDESALQPKLFQLLETGRYLLVLDDVWKKEDWDRIKAVFPRKRGWKMLLTSRNEGVGIHADPTCLTFRASILNPEESWKLCERIVFPRRDETEVRLDEEMEAMGKEMVTHCGGLPLAVKALGGLLANKHTVPEWKRVSDNIGSQIVGGSCLDDNSLNSVNRILSLSYEDLPTHLKHRFLYLAHFPEDSKIYTQDLFNYWAAEGIYDGSTIQDSGEYYLEELVRRNLVIADNRYLSLEFNFCQMHDMMREVCLSKAKEENFLQIIKDPTSTSTINAQSPSRSRRFSIHSGKAFHILGHRNNPKVRSLIVSRFEEDFWIRSASVFHNLTLLRVLDLSRVKFEGGKLPSSIGGLIHLRYLSLYGAVVSHLPSTMRNLKLLLFLNLRVDNKEPIHVPNVLKEMLELRYLSLPQEMDDKTKLELGDLVNLEYLWYFSTQHSSVTDLLRMTKLRNLGVSLSERCNFETLSSSLRELRNLEMLNVLFSPEIVMVDHMGEFVLDHFIHLKQLGLAVRMSKIPDQHQFPPHLAHIHLVHCVMKEDPMPILEKLLHLKSVALSYGAFIGRRVVCSKGGFPQLCALGISGESELEEWIVEEGSMPCLRTLTIHDCEKLKELPDGLKYITSLKELKIREMKREWKEKLVPGGEDYYKVQHIPDVQFINCDL", "text": "FUNCTION: Potential disease resistance protein. SIMILARITY: Belongs to the disease resistance NB-LRR family. RPP8/HRT subfamily."}
+{"protein": "MSFDNNYHGGQGYAKGGLGCSYGCGLSGYGYACYCPWCYERSWFSGCF", "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."}
+{"protein": "MMQVLLVTICLAVFPYQGSSIILESGNVNDYEIVYPQKVTALPIEAILQPEQKYEDAMQYEFEVNGEPVVLHLEKNKNLFTKDYSETHYSPDGREITTKPLIEDHCYYHGRIQNDAHSTASISACNGLKGHFKLQGETYLIEPLKIPDSEAHAVYKYENIEKEDEALKMCGVKHTNWESDEPIKEASQLFATSEQHRFRERYIEFFIVVDQRMYNKHNNDSAAIRTWIFEMLNTVNEIYLPWNIHVPLVGLEFWTQGDLINVVSSADKTLDSFGEWRRRDLLNRKAHDNAHLITAMHFDAQTLGLAYTGSMCHPKYSTGVFQDSSEINIFVAITLAHELGHNLGISHDVPSCTCQTKACIMSPYLSDQPTKLFSNCSEIQYERFLTQRNPKCMINKPLRTDIISPPVCGNGLLEREEECDCGSPENCRDPCCDAASCKLHSWVECESGECCDQCRFKRAGTLCRPARDDCDMAESCSGHSADCPIDGFHANGQPCSHNLGYCYNGKCPLTLYQCRAFLGKDVVGVQESCFQYNRLGNTYAYCRKENGRKIPCAPKDEKCGRLYCSYKSFGDYISCLPCYRANEEDKGMVDEGTKCGEGKVCSNGYCVDLNVAY", "text": "FUNCTION: Snake venom zinc metalloprotease that possesses high hemorrhagic activity. It inhibits collagen-induced platelet aggregation and activates prothrombin (F2). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily."}
+{"protein": "MFLKLFLLLSLVSFSHSDSSSTVSCPNGTDFHQLTTVFRYVSGFNSSWFSSNCSAVITHVVLPSRKLNGTVSWNPIRNLTRLRVLDLSNNSLDGSLPTWLWSMPGLVSVNLSRNRFGGSIRVIPVNGSVLSAVKELNLSFNRFKHAVNFTGFTNLTTLDLSHNSLGVLPLGLGSLSGLRHLDISRCKINGSVKPISGLKSLDYLDLSENSMNGSFPVDFPNLNHLQFLNLSANRFSGSVGFDKYRKFGKSAFLHGGDFVFNDSKIPYHHRIHRLPHRHPPPVRQRNVKTHRTNHTPLVIGLSSSLGALIIVIFAAAIILIRRRMKSARTKSRWAISNPTPLDFKMEKSGPFEFGTESGSSWVADIKEPTAAPVVMASKPLMNLTFKDLIVATSHFGTESVISDGTCGPLYRAVLPGDLHVAIKVLERIRDVDQNDAVTAFEALTRLKHPNLLTLSGYCIAGKEKLILYEFMANGDLHRWLHELPAGETNVEDWSADTWESHVGDSSPEKTNWLIRHRIAIGVARGLAYLHHVGTTHGHLVATNILLTETLEPRISDFGINNIARTGDDTNKNNVEFDVYSFGVILFELLTGKQGSDENVKSVRRLVKERRGEEALDSRLRLAAGESVNEMVESLRIGYFCTAETPVKRPTMQQVLGLLKDIRTVSR", "text": "FUNCTION: Can phosphorylate the myelin basic protein in vitro (PubMed:14720124). Required for endosperm development in embryos (PubMed:15634699). Maybe involved in auxin and osmotic stress responses (PubMed:21431781). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MSEFLPQRDWTVIVGSGMAGLMAAMTLAPQPVLLVTRGALGGETSSAWAQGGIAASLGPDDRAALHVADTLAAGDGLCDEDMVVGIVSSAPAVIDALERAGVRFDRDAGGNYVFGLEAAHSRRRILHAEGDGSGAAIVRALTDAVRRTPSITVLEGTEVRRLLTEDSVIAGLACAGPNGSFLLPASQVILATGGLGGLYDATTNPSGNFGQGIMLAARAGAILADMEFVQFHPTALSSPRRPLALVSEAVRGEGALLLNENGERFMAAVPGAELASRDIVARAIDREILRGGQVFLDARQALGSGFASRFPSIDLLCREAGIDPARELVPVRPAVHYHMGGVATDNKGRSSVRGLWVAGETACTGLHGANRLASNSLLEAAAMGMRAAQDIAGRPAPAARSAAAVSPNATADFSPADLAAVRPIVSRHLGIVRHAAGLAEAIRDLLPLAERNGPASDPAVVALSIAVFAALRRESRGAHFRDDFSQKDAKAMRRRLSLNDVVTVAHEFSSSSLATAGFARSA", "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": "MNKLPKGWNFTIVDDNADSTNSENIQGKRPRRSRTSVQRSDGASPIIRDNIVLIRTDDNEEFKVGDTIEITQGKGPEDPTTEYGLITEIKFGNSEFIEVIVDWFIRSSEIVGMPNDFFADNELLLTPFRSEVKFIDFIRPINVLSESQFADVVIDESNSHSTFLVKRATDNEGNFSDIFDYKDFSGKVLENPKKCAIQVKELISTTVQKELLKEFSKEQRKKKANKVSTTGRVTRFNKRKESVSTKAIKPENKQVKIEIDNDVLSDQSEEKQEESDYNEAEDANSALESDEENISQESEDSEVEYSTKKKLKNKKLSRRSKAAATPSPKRKLQKKDIEDIYSVVTPTKRMKLGKDDRDSLPVFLSPTKSVPSEFTDPKSVAFKEVKQRLHTSQKLNALPGREDEFAMIYMNHESAVNEKTGCCVYVCGLPGMGKTATIKDVVEQMTYSSERGEMEQFSYLELNGLKLLSPTVAYEALWHHISGDKVSASNAALLLEEYFKREDHKRKPLVILMDEFDQIATKKQNVMYNFFNWPTYSTSKLIVIAVANTMDLPERMLTNKIASRLGLRRIQFRGYTFQQLGDIITHRLEMITKNNRRKVVITSDAIGFASRKVASVSGDARRALTICRRAVEIAEKEYLENKKGEDDSEPYQVLISHISTAINETVNSPLSKYIASLPFASKLVLASLLRRSRRTGLAENSLGDIIDEMRNSFAMATHSEEQGSDELNMQDVLYSDKTFTATNETVPILNLRIHFFKQIVTSLVEAGIIIQQNSPGETSRLVKLDVPEEEVVSVFKKDNAISQFL", "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 in an ATP-dependent manner (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC1 family."}
+{"protein": "MEGVSALLARCPTAGLAGGLGVTACAAAGVLLYRIARRMKPTHTMVNCWFCNQDTLVPYGNRNCWDCPHCEQYNGFQENGDYNKPIPAQYLEHLNHVVSSAPSLRDPSQPQQWVSSQVLLCKRCNHHQTTKIKQLAAFAPREEGRYDEEVEVYRHHLEQMYKLCRPCQAAVEYYIKHQNRQLRALLLSHQFKRREADQTHAQNFSSAVKSPVQVILLRALAFLACAFLLTTALYGASGHFAPGTTVPLALPPGGNGSATPDNGTTPGAEGWRQLLGLLPEHMAEKLCEAWAFGQSHQTGVVALGLLTCLLAMLLAGRIRLRRIDAFCTCLWALLLGLHLAEQHLQAASPSWLDTLKFSTTSLCCLVGFTAAVATRKATGPRRFRPRRFFPGDSAGLFPTSPSLAIPHPSVGGSPASLFIPSPPSFLPLANQQLFRSPRRTSPSSLPGRLSRALSLGTIPSLTRADSGYLFSGSRPPSQVSRSGEFPVSDYFSLLSGSCPSSPLPSPAPSVAGSVASSSGSLRHRRPLISPARLNLKGQKLLLFPSPPGEAPTTPSSSDEHSPHNGSLFTMEPPHVPRKPPLQDVKHALDLRSKLERGSACSNRSIKKEDDSSQSSTCVVDTTTRGCSEEAATWRGRFGPSLVRGLLAVSLAANALFTSVFLYQSLR", "text": "FUNCTION: Involved in nuclear movement during fibroblast polarization and migration. Proposed to be involved in actin-dependent nuclear movement via association with transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow (By similarity). Overexpression can recruit Ran GTPase to the nuclear periphery (PubMed:27541860). FUNCTION: [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitotic spindle (PubMed:19494128). Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina (PubMed:21610090). SUBCELLULAR LOCATION: [Isoform 2]: Nucleus inner membrane; Multi-pass membrane protein Cytoplasm, cytoskeleton, spindle pole Note=The C- terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane in distinct micro-domains and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle. SIMILARITY: Belongs to the TMEM201 family."}
+{"protein": "METQKRHEYHSVCHTCRRTENTRMKVKMMSSSNRVLVIALALTLYIVEVASAETLCGGELVDALQFVCEDRGFYFSRPTSRSNSRRSQNRGIVEECCFRSCDLNLLEQYCAKPAKSERDVSATSLQIIPMVPTIKQDVPRKHVTVKYSKYEAWQRKAAQRLRRGVPAILRARKFRRQAVKIKAQEQAMFHRPLITLPSKLPPVLPPTDNYVSHN", "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": "MAEEKKAPISVWTTVKPFVNGGASGMLATCVIQPIDMIKVRIQLGQGSAASITTNMLKNEGVGAFYKGLSAGLLRQATYTTARLGSFKLLTAKAIESNDGKPLPLYQKALCGLTAGAIGACVGSPADLALIRMQADNTLPLAQRRNYTNAFHALTRISADEGVLALWKGCGPTVVRAMALNMGMLASYDQSAEYMRDNLGFGEMSTVVGASAVSGFCAAACSLPFDFVKTQIQKMQPDAQGKYPYTGSLDCAMKTLKEGGPLKFYSGFPVYCVRIAPHVMMTWIFLNQITKFQKKIGM", "text": "FUNCTION: Catalyzes the transport of dicarboxylates, such as oxoglutarate, oxaloacetate, malate, and succinate, and of tricarboxylates, such as citrate, isocitrate, cis-aconitate, and trans- aconitate by a counter-exchange mechanism across the inner mitochondrial membrane. Substrate preference in reconstituted proteoliposomes is oxaloacetate > malonate > malate > maleate > succinate > oxoglutarate > citrate > trans-aconitate > cis-aconitate > sulfate > isocitrate. May be important for plant metabolic functions requiring organic acid flux to or from the mitochondria, such as nitrogen assimilation, export of reducing equivalents from the mitochondria, and fatty acid elongation. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MIKKSALITLFLVSLILGVSLSQKPFYCQAPEPTPSLNTDGLTLKMVQILTRHGDRTPLYSTLKPTMNTWDCNLGWLMVSSLNNVPGAATDVDRLFRKVYMPNREYFPGNCSDGQLTSLGFQQHLQLGQSLRQLYVDKYELLPSELSVDAASTIWVRSTDVPRTIQSVQGHLTALFPPTTVTSGSGIPIININTMDNYYENMTPNPTLCPELAVLIANTTTTPEWGEFITNTTQLKEDVMETLGISVFPGWSSLMDLFFATQCHDFPLPEGVTQDMVTQVYEAAYWQYQYQLSFPMIARLGMSTFLEEVVDNIRAFVNGTSSVKYIVFSGHDDSVGPFTNLFGLMKEWPPYASHVELELWSDEKDNYFLQFKFNGQSYTLNGCEDVMCPIDSFFETAYSILVPNYADACSNSTMTF", "text": "FUNCTION: Cell-counting factor that limits the maximum size of the multicellular structure. Does not possess acid phosphatase activity. Cells with decreased levels of this protein form large groups while cells overexpressing this protein form small groups. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the histidine acid phosphatase family."}
+{"protein": "MSGDGLSNGPPPGARPDWTIDQGWETYTQAEHDVWITLYERQTDMLHGRACDEFMRGLDALDLHRSGIPDFARINEELKRLTGWTVVAVPGLVPDDVFFDHLANRRFPAGQFIRKPHELDYLQEPDIFHDVFGHVPMLTDPVFADYMQAYGEGGRRALGLGRLANLARLYWYTVEFGLMNTPAGLRIYGAGIVSSRTESIFALDDPSPNRIGFDLERVMRTLYRIDDFQQVYFVIDSIQTLQEVTLRDFGAIYERLASVSDIGVAEIVPGDAVLTRGTQAYATAGGRLAGAAAG", "text": "SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family."}
+{"protein": "MAGLTVRDPAVDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGTGAPVIESPYGETISPEDAPESISKAVASLPPEQMFELMKQMKLCVQNSPQEARNMLLQNPQLAYALLQAQVVMRIVDPEIALKILHRQTNIPTLIAGNPQPVHGAGPGSGSNVSMNQQNPQAPQAQSLGGMHVNGAPPLMQASMQGGVPAPGQMPAAVTGPGPGSLAPGGGMQAQVGMPGSGPVSMERGQVPMQDPRAAMQRGSLPANVPTPRGLLGDAPNDPRGGTLLSVTGEVEPRGYLGPPHQGPPMHHVPGHESRGPPPHELRGGPLPEPRPLMAEPRGPMLDQRGPPLDGRGGRDPRGIDARGMEARAMEARGLDARGLEARAMEARAMEARAMEARAMEARAMEVRGMEARGMDTRGPVPGPRGPIPSGMQGPSPINMGAVVPQGSRQVPVMQGTGMQGASIQGGSQPGGFSPGQNQVTPQDHEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAP", "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": "MTVGVLALQGSFNEHIAALRRLGVQGVEIRKADQLLTVSSLIIPGGESTTMAKLAEYHNLFPALREFVKMGKPVWGTCAGLIFLADRAVGQKEGGQELVGGLDCTVHRNFFGSQIQSFEADILVPQLTSQEGGPETYRGVFIRAPAVLDVGPDVEVLADYPVPSNKVLYSSSTVQIQEEDALPETKVIVAVKQGNLLATAFHPELTADTRWHSYFIKMTKEIEQGASSSSSKTIVSVGETSAGPEPAKPDLPIFQ", "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 PDX1. Involved in the indirect resistance to singlet oxygen-generating photosensitizers. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaminase PdxT/SNO family."}
+{"protein": "MFPLISFSPTSLDFTFFAIIISGFVFIITRWNSNSKKRLNLPPGPPGWPVVGNLFQFARSGKPFFEYAEDLKKTYGPIFTLRMGTRTMIILSDATLVHEALIQRGALFASRPAENPTRTIFSCNKFTVNAAKYGPVWRSLRRNMVQNMLSSTRLKEFGKLRQSAMDKLIERIKSEARDNDGLIWVLKNARFAAFCILLEMCFGIEMDEETIEKMDEILKTVLMTVDPRIDDYLPILAPFFSKERKRALEVRREQVDYVVGVIERRRRAIQNPGSDKTASSFSYLDTLFDLKIEGRKTTPSNEELVTLCSEFLNGGTDTTGTAIEWGIAQLIANPEIQSRLYDEIKSTVGDDRRVDEKDVDKMVFLQAFVKELLRKHPPTYFSLTHAVMETTTLAGYDIPAGVNVEVYLPGISEDPRIWNNPKKFDPDRFMLGKEDADITGISGVKMIPFGVGRRICPGLAMATIHVHLMLARMVQEFEWCAHPPGSEIDFAGKLEFTVVMKNPLRAMVKPRI", "text": "FUNCTION: Catalyzes the epoxidation of physiological unsaturated fatty acids in vitro. Can use laurate, oleate, linoleate, linolenate and vernolate as substrate. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MALTKAEMSEYLFDKLGLSKRDAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENASPKDE", "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: Plays a crucial role in the lysogenic life cycle of bacteriophage lambda, as it is required not only in the recombination reaction, which inserts lambda DNA into the E.coli chromosome, but also for the synthesis of int and cI repressor, two phage proteins necessary for DNA insertion and repression, respectively. The synthesis of int and cI proteins is regulated indirectly by IHF via translational control of the lambda cII protein. 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: One of the 2 subunits of integration host factor (IHF), a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. Binds to hundreds of transcriptionally inactive, AT-rich DNA sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome (PubMed:16963779). FUNCTION: Has an essential role in conjugative DNA transfer (CDT), the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI. SUBCELLULAR LOCATION: Cytoplasm, nucleoid Note=Scattered throughout the nucleoid (PubMed:21903814). SIMILARITY: Belongs to the bacterial histone-like protein family. SIMILARITY: Belongs to the bacterial histone-like protein family."}
+{"protein": "ADVPGNYPLNTNGNMYYCTILGENEFCRKVCKVHGVKYGYCFNSHCWCEYLEAKDVSVWNAAKNYCKNPVGK", "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": "MLFDYRKGGLFLGTISEKIFSRAAGTEAKANDFVLADVDYAMAHDGTSVLAVNAFKEMEMEKVWDPSRIVVPFDHIAPANNETSATLQREIREWVKEQGIPNFYEVGEGICHQVLPENGFALPGKLVVGADSHSCTYGAFGAFATGVGATDMAEIFATGKLWFKVPESFRMTVEGSLRKGVYAKDLTLYLIGKTGIAGATYKAVEFYGQAIRELTVAGRMTLCNMAIEMGAKTGIVPPDEKTFEFLKNRAAATYEPVYADPDAVYLEEFTYDADDIEPQVACPHQVDNVKPVGEVEGTHVDQVFIGTCTNGRLEDLEVAAAVLKGKQVAVRTIVIPASRTTLLAAIENGTMETLLKAGVTLATPGCGPCLGAHQGVLGEGEVCVSTANRNFKGRMGKGGFIYLASPATAAASALTGEITDPRTV", "text": "FUNCTION: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4- tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4- tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1- hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)- aconitate. These reactions are part of the biosynthesis pathway of coenzyme B. SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily."}
+{"protein": "MINEDSIQLDTLLKKYYEHSIEKIVFADDNGKIIAMNDAAKDILSEEDNYSAVANAICHRCEGYTNAYDVQSCKDCFLESMQVQATNFQVFMKTKDQKVMPFTATYQLIDQDRGIHAFTLQNVSSQIEQQEKLHQQHMMRKTISAQENERKRISRELHDSVIQEMLNVDVQLRLLKYQEDTTKLLEDAENIEYIVAKLIDDIRNMSVELRPASLDDLGLEAAFKSYFKQFEENYGIKIIYTSNIKNTRFDSDIETVVYRVVQEAILNALKYADVNEINVGIRQTGRHLVAEVIDAGNGFDPSSKPKGSGLGLYGMNERAELVSGSVNIETKIGEGTNVTLNIPI", "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": "MATRFPKFSQDLAQDPTTRRIWYGIATAHDFESHDGMTEESLYQKLFATHFGHLAIIFLWSSGNLFHIAWQGNFEQWVSNPTGVVPIAHAIWDPHFGKGAVEAFTPEGGAGPVNAAYSGLYYLYYTLGMRFNSDLYQGSIFLMVLATVFLIAGWLHLQPRFRPSLAWFKNAESRLNHHLSALFGVSSLAFAGHMIHVAIPAARGQRVDWSNFLNTLPHPAGLAPFFTGNWGVYADPQAGPPILTFIGGLNPATGTLWLTDIAHHHLAIAVIFIIAGHMYRTNFGIGHSIKEILDAHKGPLTGEGHRGLYDTINNSLHFQLGLALASLGVVTSLVAQHTYALPAYFYMPQDHTTMAALYTHHQYIAGFLMVGAFAHGAIFFVRDYDPKANENNVLARMLEHKEALISHLSWVSLFLGFHTLGLYVHNDVMLAFGRPEDQLLIEPVFAQFVQVQSGKIIEGIPALFGGPGVTAPGEFLTGWLGSVNANNSPIFLPIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGFAFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKWISIWGDNVAQFNASSTYLMGWLRDYLWANSAPLIGGYSPSGGTNALSVWAWMFLFGHLVWATGFMFLIAWRGYWQELIETLVWAHERTPLANLVRWKDKPVAMSIVQGRLVGLAHFTIGYILTYAAFLIASTAALYPNGPAAFTPAISAEQAKGVLSEFKAKPVPGGVMLLLPENIVFDFDKSSVKLDADPALNRVVGVIQFYGSEPVEILGHTDSLGEDAYNQKLSEERASAVKAFFEKKGIEAERLTAKGYGETKPVAPNAKPDGSDNPDGRQQNRRVEILIKTEVVPVS", "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: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family."}
+{"protein": "MEHSEGAPGDPAGTVVPQELLEEMLWFFRVEDASPWNHSILALAAVVVIISMVLLGRSIQASRKEKMQPPEKETPEVLHLDEAKDHNSLNNLRETLLSEKPNLAQVELELKERDVLSVFLPDVPETES", "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 (PubMed:16317684). Modulates SLC51A glycosylation, membrane trafficking and stability activities (PubMed:16317684). The Ost-alpha/Ost-beta complex efficiently transports the major species of bile acids (taurocholate) (PubMed:16317684). Taurine conjugates are transported more efficiently across the basolateral membrane than glycine- conjugated bile acids (By similarity). Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols (PubMed:16317684). Able to transport eicosanoids such as prostaglandin E2 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Mainly restricted to the lateral and basal membranes of ileal enterocytes. SIMILARITY: Belongs to the OST-beta family."}
+{"protein": "MSNSYQTQGYTVNNAGRRLVVDPITRIEGHMRCEVNIDEQNIITNAVSCGTMFRGLEIILQGRDPRDAWAFVERICGVCTGVHALASVYAIEDAIGIKVPDNANIIRNIMLATLWCHDHLVHFYQLAGMDWIDVLNALKADPRATSQLAQSLSAWPMSSPGYFFDVQNRLKKFVDGGQLGIFRNGYWGHPQYKLSPEANLMGFAHYLEALDFQREIIKIHTVFGGKNPHPNWIVGGMPCAINIDQSGAVGAVDMERLNLVQSIITRTADFINNVMVPDALAIGQFNKPWSQIGTGLSDKCVLSYGAFPDIANDFSAKSLLMPGGAVINGDFNNVMPVDLADQQQIQEFVDHAWYRYPDDQLGRHPFEGITEPWYNPGDVKGSDTDIQQLNEQERYSWIKAPRWRGHAMEVGPLARTLIAYHKGDAATIESVDRMMSALKLPLSGMQSTLGRILCRAHEAQWAVSKLQYFFDKLMTNLKNGNLATANTEKWEPASWPQQCRGIGFTEAPRGALGHWASIRDQKIDVYQCVVPTTWNASPRDPEGQIGAYEAALMGTQMAIPDQPLEILRTLHSFDPCLACSTHVLGDDGSELIAVQVR", "text": "SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family."}
+{"protein": "MDKKIQRFSCTTILVGKKASYDGSTMVARTEDSQNGDFTPKKMIVVKPEDQPRHYRSVQSSFEMDLPDNPMTYTSVPDALGKDGIWAEAGVNEANVAMSATETITTNSRVLGADPLVASGIGEEDMVTLVLPYIRSAREGVLRLGAILEDYGTYESNGVAFSDEHDIWWLETIGGHHWIARRVPDDAYVTNPNQFGIDHFEFNNPEDYLCSADLKDFIDTYHLDLTYSHEHFNPRYAFGSQRDKDRQYNTPRAWIMQKFLNPEIVQDPRSFALAWCQKPYRKITVEDVKYVLSSHYQDTGYDPYGSEGTPVSKKVFRPIGINRTSQTAILHIRPNKPQEIAAIQWMAYGSMPFNTMVPFFTQVKTIPDYFANTYENVFTDNFYWTNRLIAALADPHYNHHETDLDNYLEETMAKGHAMLHAVEVQLLAGETVDLEEENQKMSDYVQGETQTLLNKILFDASNLMTNRFSLSD", "text": "SIMILARITY: Belongs to the peptidase C69 family."}
+{"protein": "MSRRVILTLVLVTILVKTMAGMESKKVETTDEIKKRSGTSEKERESGRLLGVVKRLIVCFRSPFPGRRAISEQT", "text": "FUNCTION: Possesses antimicrobial activity against both Gram-negative (MIC between 23.8 and 51.2 uM) and Gram-positive (MIC between 11.8 and 46.5 uM) bacteria, as well as against the fungus C.tropicalis (MIC of 48.6 uM). Also possesses a relatively high hemolytic activity. 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. Medium-length antimicrobial peptide (group 3) family."}
+{"protein": "MAVFRSGLLVLTTPLASLAPRLASILTSAARLVNHTLYVHLQPGMSLEGPAQPQSSPVQATFEVLDFITHLYAGADVHRHLDVRILLTNIRTKSTFLPPLPTSVQNLAHPPEVVLTDFQTLDGSQYNPVKQQLVRYATSCYSCCPRLASVLLYSDYGIGEVPVEPLDVPLPSTIRPASPVAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDLRHTENEEDKVSSSSFRQRMLGNLLRPPYERPELPTCLYVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQMSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALLQKRIPKTHQALD", "text": "FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion matrix Note=The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but is also present in cell lysate. SIMILARITY: In the central section; belongs to the eukaryotic CoaD family."}
+{"protein": "MSYRSFSFLPNIDQNSVFSNRFNQIDKIFSTLTGEKPLSDTPAYNLFQIDEHKYELILSIPGYEEKELDISVHNSQLTVQGKKQNQENDDKKIKKYLHKGIIFNDFSLNFNFDHKIQVKKAELFSGLLKINFECRVPDEEKPKKIFINIPNKVKEIEKNKI", "text": "SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MASSDTQGKRVAVIGGGLVGALNACFLAKRNFQVDVYEAREDIRVAKSARGRSINLALSYRGRQALKAIGLEDQIVSKGVPMKARMIHSLSGKKSAIPYGNKSQYILSISRENLNKDLLTAVESYANAKVHFGHKLSKCIPEEGVLTVLGPDKVPRDVTCDLVVGCDGAYSTVRAHLMKKPRFDYTQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRNAYMMIALPNMDKSFTCTLFMPFEEFERLPTRSDVLDFFQKNFPDAIPLMGEQALMRDFFLLPAQPMISVKCSPFHLKSHCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNNNLSMCLPEFSRFRIPDDHAISDLSMYNYIEMRAHVNSRWFLFQKLLDKFLHAIMPSTFIPLYTMVAFTRIRYHEAVLRWHWQKKVINRGLFVLGSLIAIGGTYLLVHHLSLRPLEFLRRPAWMGTTGYWTRSTDISLQVPWSY", "text": "FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO subfamily."}
+{"protein": "MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSESEISQEADDMAMEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKNLKDVSFRLGSFNLEKVENPAEVIRELICYCLDTIAENQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLNAAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEKENSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI", "text": "FUNCTION: [Protein XRCC4, C-terminus]: Acts as an activator of the phospholipid scramblase activity of XKR4 (PubMed:33725486). This form, which is generated upon caspase-3 (CASP3) cleavage, translocates into the cytoplasm and interacts with XKR4, thereby promoting phosphatidylserine scramblase activity of XKR4 and leading to phosphatidylserine exposure on apoptotic cell surface (PubMed:33725486). FUNCTION: [DNA repair protein XRCC4]: DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination (PubMed:10757784, PubMed:10854421, PubMed:17124166, PubMed:16412978, PubMed:8548796, PubMed:25742519, PubMed:12517771, PubMed:17290226, PubMed:22228831, PubMed:25597996, PubMed:25934149, PubMed:26100018, PubMed:26774286). Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs) (PubMed:15385968, PubMed:20852255, PubMed:26774286, PubMed:27437582). Associates with NHEJ1/XLF to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired (PubMed:26100018, PubMed:27437582, PubMed:28500754, PubMed:21775435, PubMed:22287571, PubMed:21768349). The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other (PubMed:27437582). The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors (PubMed:27437582). Plays a key role in the NHEJ ligation step of the broken DNA during DSB repair via direct interaction with DNA ligase IV (LIG4): the LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is completed (PubMed:9242410, PubMed:10757784, PubMed:10854421, PubMed:12517771, PubMed:17290226, PubMed:19837014). XRCC4 stabilizes LIG4, regulates its subcellular localization and enhances LIG4's joining activity (PubMed:9242410, PubMed:10757784, PubMed:10854421, PubMed:12517771, PubMed:17290226, PubMed:21982441, PubMed:22228831). Binding of the LIG4-XRCC4 subcomplex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends (PubMed:10757784, PubMed:10854421). Promotes displacement of PNKP from processed strand break termini (PubMed:20852255, PubMed:28453785). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to site of double-strand breaks. SUBCELLULAR LOCATION: [Protein XRCC4, C-terminus]: Cytoplasm Note=Translocates from the nucleus to the cytoplasm following cleavage by caspase-3 (CASP3). SIMILARITY: Belongs to the XRCC4-XLF family. XRCC4 subfamily."}
+{"protein": "MAAVLEAGSAGQFEQLIQNSAKSLTVVHFWAPWAPQCTQMNEVMAELAKEQPQVMFVKLEAEAVPEVSEKYEVTSVPTFLFFKNSQKIDRLDGAHAPELTKRVQRHASSTSFPATPNSAPKEDLNGRLKKLINAAPCMLFMKGSPQEPRCGFSRQIVALLNDQKVQFSSFDILSDEEVRQGLKTFSNWPTYPQFYVKGELVGGLDIVKEMVASGELDQMCPKAQSLEERLKALVNKAPVMLFMKGNKEMAKCGFSRQILEIMNNTGVTYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIIKELKESGELVSVLKGDQ", "text": "FUNCTION: Together with bola2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. Required for hemoglobin maturation. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
+{"protein": "MEGSRPRILVGHLEPSPPAFDGELDLQRYSNGPGVSGTPGPGSPGMGAVGWSETRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQSSPAAEGLARPQVPSSSAFRCPFCKGKFRTSAERERHLHILHRPWKCSLCSFGSSQEEELLHHSLTAHGASERPLAATSTPEPPPPPQQEPRSALEPEPEPEPRPEPDREANPAPTPAPPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFLKNHMKVHTSKLGPLRAPGPGSAPARAPQPPDLSLLAYEPLGPALLLAPAPAPAERREPPSLLGYLSVRAGEVRPNGEGADPGGGRSYGGFRPLPSALPNRARRHRTEEPEEEEEVVEAEEESWARGRSLGSLTSLHPNPGEGSGQPAPAAGTQARSTATQEENGLLVGGTRSEAGRGATGKDCPFCGKSFRSAHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSSAGPGPPPEPPPPSQRGSLQPQSGAKPTQASATWVEGTASTRPPSSSTGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGAGGALHRCLFCPFATGAPELMALHLQVHHSRRARGRRQPRADTSPTYVRAPSGETPPSPPLEEEGSPGLSRSGEAGLGGQER", "text": "FUNCTION: Transcriptional regulator (PubMed:20940257). Recognizes and binds 2 copies of the core DNA sequence motif 5'-GGGGG-3' (PubMed:20940257). Binds to the HMGN1 promoter and may repress HMGN1 expression (By similarity). Regulates SNCA expression in primary cortical neurons (By similarity). Binds to the COL2A1 promoter and activates COL2A1 expression, as part of a complex with SOX9 (PubMed:20940257). Plays a role in chondrocyte differentiation (PubMed:20940257). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MAANYLHGVETIEKETGSRPVKVVKSAVIGLIGTAPIGPVNTPVQSLSDVDAAQFGPQLAGFTIPQALDAVYDYGSGTVIVINVLDPAVHKSNAANEPVTFDAATGRAKLAHPAAANLVLKNDSGGTTYAEGTDYAVDLINGVITRIKTGTIPPGATAAKATYDYADPTKVTAADIIGAVNAAGMRTGMKALKDTYNLYGYFSKILIAPAYCTQNSVSVELEAMAVQLGAIAYIDAPIGTTLAQALAGRGPAGTINFNTSSDRVRLCYPHVKVYDTATNAERLEPLSSRAAGLRARVDLDKGYWWSSSNQQLVGVTGVERPLSAMIDDPQSDVNMLNEQGITTVFSSYGSGLRLWGNRTAAWPTVTHMRNFENVRRTGDVINESLRYFSQQFVDAPIDQGLIDSLVESVNGFGRKLIGDGALLGFKAWFDPARNPKEELAAGHLLINYKYTVPPPLERLTYETEITSEYLLTLKGGN", "text": "FUNCTION: Polymerizes as an extended structure around the baseplate- tail tube complex. During ejection, the sheath shifts to a contracted form, thereby making the inner tail tube protrude through the host cell envelope. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Tail. SIMILARITY: Belongs to the myoviridae tail sheath protein family."}
+{"protein": "MAPAASGAKKQKKKWSKGKVKDKAQHAVILDKSTSDKLYKDVQSYRLVTVATLVDRLKINGSLARRCLKDLEEKGQIKQVVGHSKMKIYTRAIGADE", "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 eS25 family."}
+{"protein": "MTLQKAQAERIEKEIRELSRFSAEGPGVTRLTYTPEHAAARETLIAAMKAAALSVREDALGNIIGRREGTDPELPAIAVGSHFDSVRNGGMFDGTAGVVCALEAARVMLENGYVNRHPFEFIAIVEEEGARFSSGMLGGRAIAGLVADRELDSLVDEDGVSVRQAATAFGLKPGELQAAARSAADLRAFIELHIEQGPILEQEQIEIGVVTSIVGVRALRVAVKGRSDHAGTTPMHLRQDALVPAALMVREVNRFVNEIADGTVATVGHLTVAPGGGNQVPGEVDFTLDLRSPHEESLRVLIDRISVMVGEVASQAGVAADVDEFFNLSPVQLAPTMVDAVREAASALQFTHRDISSGAGHDSMFIAQVTDVGMVFVPSRAGRSHVPEEWTDFDDLRKGTEVVLRVMKALDR", "text": "FUNCTION: Involved in the asymmetric conversion of racemic 5- substituted hydantoins to the corresponding L-amino acids. Prefers L- carbamoyl-L-tryptophan and N-carbamoyl-L-tyrosine. Has weaker activity with N-carbamoyl-D,L-phenylalanine and N-carbamoyl-L-thienyalanine. Carbamoyl derivatives of beta-alanine and charged aliphatic amino acids are not accepted as substrates. SIMILARITY: Belongs to the peptidase M20 family."}
+{"protein": "MAKCRVRVSTGEACGAGTWDKVSVSIVGTHGESPLVPLDHLGKEFSAGAEEDFEVTLPQDVGTVLMLRVHKAPPEVSLPLMSFRSDAWFCRWFELEWLPGAALHFPCYQWLEGAGELVLREGAAKVSWQDHHPTLQDQRQKELESRQKMYSWKTYIEGWPRCLDHETVKDLDLNIKYSAMKNAKLFFKAHSAYTELKVKGLLDRTGLWRSLREMRRLFNFRKTPAAEYVFAHWQEDAFFASQFLNGINPVLIRRCHSLPNNFPVTDEMVAPVLGPGTSLQAELEKGSLFLVDHGILSGVHTNILNGKPQFSAAPMTLLHQSSGSGPLLPIAIQLKQTPGPDNPIFLPSDDTWDWLLAKTWVRNSEFYIHEAVTHLLHAHLIPEVFALATLRQLPRCHPLFKLLIPHIRYTLHINTLARELLVAPGKLIDKSTGLGTGGFSDLIKRNMEQLNYSVLCLPEDIRARGVEDIPGYYYRDDGMQIWGAIKSFVSEIVSIYYPSDTSVQDDQELQAWVREIFSEGFLGRESSGMPSLLDTREALVQYITMVIFTCSAKHAAVSSGQFDSCVWMPNLPPTMQLPPPTSKGQARPESFIATLPAVNSSSYHIIALWLLSAEPGDQRPLGHYPDEHFTEDAPRRSVAAFQRKLIQISKGIRERNRGLALPYTYLDPPLIENSVSI", "text": "FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators (PubMed:9305900, PubMed:10965849, PubMed:10625675, PubMed:16143298, PubMed:16112079, PubMed:15558016, PubMed:27435673). Catalyzes the peroxidation of arachidonate and linoleate into (8S)-HPETE and (9S)- HPODE respectively (PubMed:9305900, PubMed:10965849, PubMed:10625675, PubMed:16143298, PubMed:16112079, PubMed:15558016, PubMed:27435673). In addition to generate (8S)-HPETE from free arachidonic acid (AA), may produce other HETE isomers from phospholipid-esterified polyunsaturated fatty acids and minor products derived from (8S)-HPETE itself that may include leukotriene A4 and 8,15-diHPETE (PubMed:16143298, PubMed:16112079, PubMed:27435673). With free arachidonate as substrate, has no detectable 15S-lipoxygenase activity and only displays a 8S- lipoxygenase activity (PubMed:10625675, PubMed:16112079, PubMed:16143298, PubMed:15558016, PubMed:10965849, PubMed:9305900). However may have a 15S-lipoxygenase activity with (8S)-HPETE to produce (8S,15S)-diHPETE and when oxidizes directly arachidonic acid esterified to membrane-bound phospholipids to produce a phospholipid-esterified 15-HpETE (PubMed:27435673, PubMed:16112079, PubMed:16143298). May also catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE (PubMed:16112079). May play a role in keratinocyte differentiation through activation of the peroxisome proliferator activated receptor signaling pathway (PubMed:10965849). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. SIMILARITY: Belongs to the lipoxygenase family."}
+{"protein": "MASVNNYQVDCGSRSARIQPRINNGIHDEESLFEVLELSEEEFELDFHRLKSFNDVRVINNPDLSPECTNTAISRDETLESASSAFEVPSDEIAILSISSDSNKNSPPSEQPAPALRNIRSSSNSDRIDEWCLGSHLFNELHQNVPQSSDGVNHGFPVYSFKERELYTSAKLKKLTNAQRIAVQKLSRDLYPILRTCYREKTRRQLLTYHHERIFDDIPSFFPQRDFIFNYYSMPLEFDRLSDVDIDSSSRSRFTDESTGETLNRSPSAASSSLENTSWFGWTLLSRFLDREW", "text": "FUNCTION: Required for autophagic breakdown of peroxisomes, called pexophagy, through linking peroxisomes to the autophagy apparatus. Involved in regulation of the glyoxylate cycle. SUBCELLULAR LOCATION: Peroxisome Note=Recruited to peroxisomes by PEX3."}
+{"protein": "MELDECSPSIFIISFIFIAISIAILRRIRPKKTKALPPGPWKLPLIGNLHQFISRDSLPYKILRDLAQKHGPLMHLQLGEVSAVVASSPEMAKVITRTKDLEFADKPAIRAIRIVTYDYLDIAFNSYGKYWREMRKIFVQELLTPKRVRSFWSAREDVFSNLVKTINSANGKSINLTKLISSTTNSIINRVALGNVPYEREIFMELIKQLLTAAGGFKLVDLFPSYKIIHVLEGTERKLWKILGKIDKILDKVIDEHRENLLRTGKGSGENGQEDIVDILLKIEDGGELDHDIPFGNNNIKALLFDIISGGSDTSSTTIDWAMSEMMKNPQVMSKAQKEIREAFNGKKKIDENDVQNLKYLKSVIQETLRLHPPAAFLMRQCREECEIGGYHIPVGTKVFINIWAMGRDPEHWPNPESFIPERFENIPYDFTGSEHQLATFPFGSGRRICPGISFGLANVELSLALLLYHFNWQLPDSSTDLDMTEAIGIAARRKYDLHLIPTSYM", "text": "FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications (PubMed:31009114). Cytochrome P450 catalyzing the hydroxylation of (+)-vincadifformine to (+)- minovincinine (PubMed:31009114, PubMed:35660549). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKESKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHCYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEEDSENGVPESTSTDSPPGIDLHNQASVPLEPRPLRRESEI", "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. Can be blocked by extracellular barium and 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": "MADSGDAGSSGPWWKSLTNSRKKSKEAAVGVPPPAQPAPGEPTPPAPPSPDWTSSSRENQHPNLLGGAGEPPKPDKLYGDKSGSSRRNLKISRSGRFKEKRKVRATLLPEAGRSPEEAGFPGDPHEDKQ", "text": "FUNCTION: May have a role in proliferation and/or differentiation. SIMILARITY: Belongs to the PRR15 family."}
+{"protein": "MNFKVFLLAASTIAVGLVELIVGGILPQIASDLDISIVSAGQLISVFALGYAVSGPLLLAVTAKAERKRLYLIALFVFFLSNLVAYFSPNFAVLMVSRVLASMSTGLIVVLSLTIAPKIVAPEYRARAIGIIFMGFSSAIALGVPVGIIISNAFGWRVLFLGIGVLSLVSMLIISVFFEKIPAEKMIPFREQIKTIGNAKIASAHLVTLFTLAGHYTLYAYFAPFLETTLHLSSVWVSVCYFLFGLSAVCGGPFGGWLYDRLGSFKSIMLVTVSFALILFILPLSTVSLIVFLPAMVIWGLLSWSLAPAQQSYLIKIAPESSDIQQSFNTSALQIGIALGSAIGGGVIGQTGSVTATAWCGGLIVIIAVSLAVFSLTRPALKRKSA", "text": "FUNCTION: Involved in the efflux of purine ribonucleosides, such as guanosine, adenosine and inosine, as well as purine bases guanine, adenine and hypoxanthine, and purine base analogs 2,6-diaminopurine and 6-mercaptopurine. Therefore plays a role in maintaining the cellular purine base pools and protecting cells against toxic purine base analogs. Modulates expression of the purR and G-box regulons (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. PbuE (TC 2.A.1.2.25) subfamily."}
+{"protein": "MNKRHALLLTAVLGMATAYAQTAPTTTTVNTLQTVYRDPSLTSAPITANVGKYVGPLSTFLASIAKSAGYEVVFNFNIDALALINGEIVFGNSTASVTTSYATPLGRPQELPAKPVVHNFSNAPFNEAWPLLMDVYELDYQLVKVGSANVIRIGQRPKQLALPLKFISAESALTAIEKFFGEEKFETVISLDSNNKPFQTTRPTGKFGLPNSIKVIPDSSNKRLIIGSNSEDGIRIRSFVETIDVQSSGKVISTDSISEIYIVRGQKESVLQFLRDSFPELIVTDYASGGLAIEGPRTSVNRAIILLGQVDRAPEIPIVQRIYTVRGQAADITALLAAQYPTLRVTPVGQTGQLVLNGAQAQLDTALALLEQVDRPAPVAESRTVQRVFQLVNASAEEVKATLEGTLARDLTADSNNDVLPNVPVTATDANGNTTVVSVPNALGKTANQGTANAQAQTAQTPANTQQATLIADKRTNSLIVRGTPEQVAQVAELVPQLDQVVPQINVQVRIQEVNERALQSLGLNWRATFGGFNVAVSGGTGLAATFNPTQSFLGFNIFPTLTALETQGLTRRVYDGNVTMQSGQRSLSATGGAQNASSGAAASVKSGGRLEINIPSAAGNIVRQIDYGLNLDFFSPQVAPDGTITLRIRGQVNQPATAITADSLPNLIDFTNSEAQSTITFKNGQTILMSGLLGSTETTNRSGVPFLSSLPGVGAAFGEKRTEKTQSQLLVIITGTVVK", "text": "FUNCTION: Could be part of the type IV piliation system (T4P). May contribute at the cohesion between the S-layer and the outer membrane by forming oligomers. Could also be the main channel through which trafficking is managed. SUBCELLULAR LOCATION: Cell envelope. SIMILARITY: Belongs to the bacterial secretin family."}
+{"protein": "MPVLNTLRRSLLILALACTLPSLAMDRNALLDQANVLLLPRERAIPQLELVDQNDQPFSTETLKGRWHILFFGFTACPDICPTTLSEMRRLFGQLPAETREQLQLVLITADPARDTPQQLKTYLSYYRAGFIGLTGNMEQLQRLSKALGLPFVPATETEGDYSVSHSGNLALVGPDGSLRGHIRAPLKLDGLQRVLPQILDNER", "text": "SIMILARITY: Belongs to the SCO1/2 family."}
+{"protein": "MKFGVIGAGQMGGGIAQVAAQSGFDVVVHDQKQEFLDRGKGVIEKSLGKLHEKGKLTDAPETVLGRIHFTTDLQDFADCDLVVEAIVENQQIKNDLFKQLGQIVKPEGILASNTSSIPITALATASGRPAQFIGMHFMNPVPLMQLVEVIRGYQTSDETARIVTETAEKLGKTPLSCNDFPGFVSNRILMPMLNEAIQCVMEGVAEPEAIDGIMKLGMNHPMGPLTLADFIGLDTCLAIMEVLHQGLGDDKYRPSPLLRKMVQAGLLGRKSGEGFYKY", "text": "SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family."}
+{"protein": "MAVAVVFGASGISGWGITKALLDAKTQNAFSKIIALTNRSLSLAESGLPDDDRLQLHSGIDLQANVDDVIAKLRERIPSIGNVTHVFYTAFSTSHTDNQLMMKASNTKMLRTMVEAMETVAPSLSFIAVQTGSNHYGILFAEVLGERFGPVPLKEDLPRLPSPLRDSLMFYAMADEMDELSRGKSWKWCDIRPDMIVGYLPRPNSHSIAESIGYYLAFHAYLTPGEEVPFPGSEAAWNAKFSLTGQGVLGNFNVHLACKNSIENGEAFNIANKPFTTWASLWPLLAGYWGLKGTAPVGHHGIPDAASWVLDNMDRVKGWEEKYSMKPGRLFKIPWRYFHWALNMPFDRYLDLTRCEQTGFQQHEEHKESFETAWKCMQEAKLLPIVDKSSTPP", "text": "FUNCTION: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes the O-prenylation of L-tyrosine (L- Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O- dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl- L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide (PubMed:27390873). This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL (PubMed:27390873). The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification (PubMed:18272357). Phomamide is converted into phomalizarine via oxidation, probably by sirT (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. Highly divergent."}
+{"protein": "MDSTNGNGADLESANGANGSGVTEALPPPPPVIPPNVEPVRVKTELAEKKGPVRVPMARKGFGTRGQKIPLLTNHFKVDVANLQGHFFHYSVALFYDDGRPVEQKGVGRKILDKVHQTYHSDLDGKEFAYDGEKTLFTYGALPSNKMDFSVVLEEVSATRANGNGSPNGNESPSDGDRKRLRRPNRSKNFRVEISYAAKIPLQALANAMRGQESENSQEAIRVLDIILRQHAARQGCLLVRQSFFHNDPTNCEPVGGNILGCRGFHSSFRTTQGGMSLNMDVTTTMIIKPGPVVDFLIANQNARDPYSIDWSKAKRTLKNLRVKVSPSGQEFKITGLSDKPCREQTFELKKRNPNENGEFETTEVTVADYFRDTRHIDLQYSADLPCINVGKPKRPTYIPLELCALVPLQRYTKALTTFQRSALVEKSRQKPQERMTVLSKALKVSNYDAEPLLRSCGISISSNFTQVEGRVLPAPKLKMGCGSETFPRNGRWNFNNKEFVEPTKIQRWVVVNFSARCNVRQVVDDLIKIGGSKGIEIASPFQVFEEGNQFRRAPPMIRVENMFKDIQSKLPGVPQFILCVLPDKKNSDLYGPWKKKNLTEFGIVTQCMAPTRQPNDQYLTNLLLKINAKLGGLNSMLSVERTPAFTVISKVPTIILGMDVSHGSPGQSDVPSIAAVVSSREWPLISKYRASVRTQPSKAEMIESLVKKNGTEDDGIIKELLVDFYTSSNKRKPEHIIIFRDGVSESQFNQVLNIELDQIIEACKLLDANWNPKFLLLVAQKNHHTKFFQPTSPENVPPGTIIDNKICHPKNNDFYLCAHAGMIGTTRPTHYHVLYDEIGFSADELQELVHSLSYVYQRSTSAISVVAPICYAHLAAAQLGTFMKFEDQSETSSSHGGITAPGPISVAQLPRLKDNVANSMFFC", "text": "FUNCTION: Together with RDM3, required for transcriptional gene silencing (TGS) by DNA methylation and repressive histone modifications (H3K9me2) of several chromatin loci (PubMed:21738482). Component of the RISC complex that associate with the small interfering RNA (siRNA) pathway involved in direct cytosine methylation at endogenous DNA repeats. Forms a AGO4/NRPE1/siRNA complex in cajal body, facilitating its function in RNA-directed gene silencing of target loci. Required for CpNpG and asymmetric DNA methylation as well as histone H3 'Lys-9' methylation (H3K9me) at SUP and SN1 loci. May be not required for CpG methylation. Required for the production and maintenance of retrotransposon SN1 and Copia and ribosomal 5S 25 nucleotide siRNAs specialized in gene silencing at chromatin level. Involved in de novo methylation of FWA gene and required for the maintenance of RNA- directed DNA methylation (RdDM) triggered by inverted repeat transgenes. Interacts with miRNA miR390 and miR172, targeting respectively TAS3 and AP2 mRNAs, and mediates cleavage of miRNA targets. Associates mainly with small RNAs of 24 nucleotide in length and preferentially recruits small RNAs with a 5' terminal adenosine. Targeted by the turnip yellows virus (TuYV) protein P0 (via F-box-like domain) for probable proteasome degradation and thereby inactivating AGO4 function in RNA silencing. Required for resistance to the bacterial pathogen P.syringae. Works independently of the RdDM pathway in mediating resistance to P.syringae. RdDM is involved in viral genome methylation as an epigenetic defense against geminiviruses (PubMed:12522258, PubMed:14988555, PubMed:15242620, PubMed:16839878, PubMed:16839879, PubMed:16998468, PubMed:17869110, PubMed:17938239, PubMed:17993621, PubMed:18342361, PubMed:18596098, PubMed:19377477, PubMed:20173091). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Nucleus, Cajal body Note=Also located in AB-bodies that are distincts from the Cajal bodies and immediately adjacent to the condensed 45S ribosomal DNA (rDNA) loci (PubMed:18266474). Colocalizes with AGO4 and polymerase V in the nucleoplasm (PubMed:19410546). SIMILARITY: Belongs to the argonaute family. Ago subfamily."}
+{"protein": "MIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQMIPLRGCIDDRIPTDPTMYRFYEMLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPF", "text": "FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. SIMILARITY: Belongs to the cyanase family. SIMILARITY: Belongs to the cyanase family."}
+{"protein": "MGITKTSPNTTILLKTFHNNSMSQDYHHHHHHNQHQGGIFNFSNGFDRSDSPNLTTQQKQEHQRVEMDEESSVAGGRIPVYESAGMLSEMFNFPGSSGGGRDLDLGQSFRSNRQLLEEQHQNIPAMNATDSATATAAAMQLFLMNPPPPQQPPSPSSTTSPRSHHNSSTLHMLLPSPSTNTTHHQNYTNHMSMHQLPHQHHQQISTWQSSPDHHHHHHNSQTEIGTVHVENSGGHGGQGLSLSLSSSLEAAAKAEEYRNIYYGANSSNASPHHQYNQFKTLLANSSQHHHQVLNQFRSSPAASSSSMAAVNILRNSRYTTAAQELLEEFCSVGRGFLKKNKLGNSSNPNTCGGDGGGSSPSSAGANKEHPPLSASDRIEHQRRKVKLLTMLEEVDRRYNHYCEQMQMVVNSFDIVMGHGAALPYTALAQKAMSRHFRCLKDAVAAQLKQSCELLGDKDAAGISSSGLTKGETPRLRLLEQSLRQNRAFHQMGMMEQEAWRPQRGLPERSVNILRAWLFEHFLHPYPSDADKHLLARQTGLSRNQVSNWFINARVRLWKPMVEEMYQQESKEREREEELEENEEDQETKNSNDDKSTKSNNNESNFTAVRTTSQTPTTTAPDASDADAAVATGHRLRSNINAYENDASSLLLPSSYSNAAAPAAVSDDLNSRYGGSDAFSAVATCQQSVGGFDDADMDGVNVIRFGTNPTGDVSLTLGLRHAGNMPDKDASFCVREFGGF", "text": "FUNCTION: Transcription factor that establishes leaf shape by repressing growth in specific subdomains of the leaf. Negatively regulates knox homeobox gene KNAT1/BP expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/BELL homeobox family."}
+{"protein": "MRQPLICSGHSRPVSDLSFSNENSDGSFIVSACLDGSPMLRNGENGDWIGTFEGHKGAVWSSRFNSTASQALTASADYTVKLWDTLNGSEILSIEHQSIVKTADFSNNNSRVVTGGSEKILRIFDLERPNDPLLQISGHTNTIKTATWSVHNDDIVLSGGLDEVIRIWDLRSGTQVSLCAKSSITSMEFSKDRRFLVTTAGNEVTFWDAQSFYPLKVYSLPFDVNCASLHPDNSKFIAGGSDFWVHVYDFSTGNEIEVNKGHHGPVNCCRFSPDGASFASGSLDGTIRLWKGM", "text": "FUNCTION: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre- mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP may play a role in the cellular distribution of the SMN complex (By similarity). SIMILARITY: Belongs to the WD repeat STRAP family."}
+{"protein": "MGREKKQEYALFTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVVKKDYRIASYSLPIASIGACISLYHYVIQKVAAFSAAGAACGRVPCTGEYINWFGFVTIPFLALIGFITIAVCSFIVIKNK", "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": "MDALINLKDCKEYMTITINGNEHQIKLAGIIEDPYFCGKDVCTILGYKDKEQALRKRVKSKHKKSLSELFEKKLPVVTTGNFFLGTQNELSYHEGKSIYINEPGLYNLIMSSEAPFAEQFQDMVYEKILPSIRKYGSYSIEQKLSSAMEQLALKDKSEEELQIKLQEERIEKENAYMKLRSEAKRHKEQIKRTLEFNQATKQIEPLEYIYICTTEYYQQHHKFKVGGVQSFKDLKSRLTQYNSGESNSEAHFFIYVRKTVSYRSIEHIIKGLLSGFRENQSNELYIMHCDWLVKFLDAIMDGNAEFALLVNSNREQIALDTINKEPTILPPIKLEQIAYIRAGDEPRDLSSVLGQEMIDSIKEAIESFEPMDNTVKRKEFELHLLSKSPNVSLTGKRRDTWELTRQLGSSINPMWRYKY", "text": "SIMILARITY: Belongs to the IIV-6 201R/289L family."}
+{"protein": "MAEEQEFTQLCKLPVQPSHPHCVNNTYRSAQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLSRLTEQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYTLEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLDPSPLRDTVANALMYHRNESLQPSLQGPHTELRSDFQCVVGFGGIHSTPSTVLSDQAKYLNPLLGEWKHFTASLAPRMSNQGIAVLNNFVYLIGGDNNVQGFRAESRCWRYDPRHNRWFQIQSLQQEHADLCVCVVGRYIYAVAGRDYHNDLNAVERYDPTTNSWAYVAPLKREVYAHAGATLEGKMYVTCGRRGEDYLKETHCYDPDSNTWHSLADGPVRRAWHGMATLLDKLYVIGGSNNDAGYRRDVHQVACYSCTSGQWSSVCPLPAGHGEPGIAVLDTRIYVLGGRSHNRGSRTGYVHIYDVEKDCWEEGPQLDNSISGLAACVLTLPRTLLLEPPRGTPDRSQADPDFASEVMSVSDWEEFDNSSED", "text": "FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Nucleus Lysosome Note=Mainly cytoplasmic in prophase and prometaphase. Associates with the mitotic spindle as the cells reach chromosome bi-orientation. Localizes to the centrosomes shortly before cells enter anaphase After anaphase onset, predominantly associates with the polar microtubules connecting the 2 opposing centrosomes and gradually diffuses into the cytoplasm during telophase. Localizes to the nucleus upon amino acid starvation. Relocalizes to the cytosol and associates with lysosomes when amino acids are available."}
+{"protein": "MACRWSTKESPRWRSALLLLFLAGVYGNGALAEHSENVHISGVSTACGETPEQIRAPSGIITSPGWPSEYPAKINCSWFIRANPGEIITISFQDFDIQGSRRCNLDWLTIETYKNIESYRACGSTIPPPYISSQDHIWIRFHSDDNISRKGFRLAYFSGKSEEPNCACDQFRCGNGKCIPEAWKCNNMDECGDSSDEEICAKEANPPTAAAFQPCAYNQFQCLSRFTKVYTCLPESLKCDGNIDCLDLGDEIDCDVPTCGQWLKYFYGTFNSPNYPDFYPPGSNCTWLIDTGDHRKVILRFTDFKLDGTGYGDYVKIYDGLEENPHKLLRVLTAFDSHAPLTVVSSSGQIRVHFCADKVNAARGFNATYQVDGFCLPWEIPCGGNWGCYTEQQRCDGYWHCPNGRDETNCTMCQKEEFPCSRNGVCYPRSDRCNYQNHCPNGSDEKNCFFCQPGNFHCKNNRCVFESWVCDSQDDCGDGSDEENCPVIVPTRVITAAVIGSLICGLLLVIALGCTCKLYSLRMFERRSFETQLSRVEAELLRREAPPSYGQLIAQGLIPPVEDFPVCSPNQASVLENLRLAVRSQLGFTSVRLPMAGRSSNIWNRIFNFARSRHSGSLALVSADGDEVVPSQSTSREPERNHTHRSLFSVESDDTDTENERRDMAGASGGVAAPLPQKVPPTTAVEATVGACASSSTQSTRGGHADNGRDVTSVEPPSVSPARHQLTSALSRMTQGLRWVRFTLGRSSSLSQNQSPLRQLDNGVSGREDDDDVEMLIPISDGSSDFDVNDCSRPLLDLASDQGQGLRQPYNATNPGVRPSNRDGPCERCGIVHTAQIPDTCLEVTLKNETSDDEALLLC", "text": "FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. May act as a tumor suppressor. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein Membrane, coated pit. SIMILARITY: Belongs to the LDLR family."}
+{"protein": "MAYVLTETAAGYALLKASDKKIYKSSSLVQDLKSSENVLKQFKVAAFSKFASAANALEEANSVIEGKVSSQLEKLLAEAKSDKKSTLVVSETKLANAINKLGLNFNVVCDAVTLDIYRAVKEYLPELLPGMTDGDLSKMSLGLAHSIGRHKLKFSADKVDVMIIQAIALLDDLDKELNTYAMRCKEWYGWHFPELAKIVTDSVAFARIILTMGVRSNAAETDMSEILPEEIEERVKSAAEVSMGTEITQVDLDNIKSLAEQIVEFAAYREQLSNYLSSRMKAIAPNLTQLVGELVGARLIAHAGSLVSLAKAPASTIQILGAEKALFRALKTKHDTPKYGLLYHASLVGQATGKNKGKIARVLAAKAAVSLRYDALAEDRDDSGDIGLEARAKVESRLSQLEGRDLRTTPKVSRDAKKIEISEARAYNADADAATAPADSTPADSDDEEEEEKKVKKDKKDKKRKREEDAEEEDSKKSKKEKKEKKEKKEKKEKKEKKEKKEKKEKKEKKEKK", "text": "FUNCTION: Required for pre-18S rRNA processing. May bind microtubules (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NOP5/NOP56 family."}
+{"protein": "MPPATGDIDRQIEQLMECKALSETEVKMLCEHAKTILVEEYNVQPVKCPVTVCGDIHGQFYDLIELFRIGGSSPDTNYLFMGDYVDRGYYSVETVSLLVALKVRYRDRLTILRGNHESRQITQVYGFYDECLRKYGNANVWKHFTDLFDYLPLTALIESQVFCLHGGLSPSLDTLDNIRSLDRIQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDIATQFNHTNGLSLISRAHQLVMEGFNWCQEKNVVTVFSAPNYCYRCGNMAAILEIGENMDQNFLQFDPAPRQVEPETTRKTPDYFL", "text": "FUNCTION: Associates with the serine/threonine-protein phosphatase PP2A regulatory subunits A and B' to positively regulates beta-oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins (PubMed:25489022). Involved in the positive regulation of salt stress responses. May function by increasing chloride channel activities on vacuolar membranes (PubMed:27676158). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome Note=Interacts with B'THETA in the cytosol and peroxisomal import occurs by a piggybacking transport. SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily."}
+{"protein": "MAGPLQGGGARALDLLRGLPRVSLANLKPNPGSKKPERRPRGRRRGRKCGRGHKGERQRGTRPRLGFEGGQTPFYIRIPKYGFNEGHSFRRQYKPLSLNRLQYLIDLGRVDPSQPIDLTQLVNGRGVTIQPLKRDYGVQLVEEGADTFTAKVNIEVQLASELAIAAIEKNGGVVTTAFYDPRSLDIVCKPVPFFLRGQPIPKRMLPPEELVPYYTDAKNRGYLADPAKFPEARLELARKYGYILPDITKDELFKMLCTRKDPRQIFFGLAPGWVVNMADKKILKPTDENLLKYYTS", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
+{"protein": "MVEDSRVRDALKGGDQKALPASLVPQAPPVLTSKDKITKRMIVVLAMASLETHKISSNGPGGDKYVLLNCDDHQGLLKKMGRDISEARPDITHQCLLTLLDSPINKAGKLQVYIQTSRGILIEVNPTVRIPRTFKRFSGLMVQLLHKLSIRSVNSEEKLLKVIKNPITDHLPTKCRKVTLSFDAPVIRVQDYIEKLDDDESICVFVGAMARGKDNFADEYVDEKVGLSNYPLSASVACSKFCHGAEDAWNIL", "text": "FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)- methyltransferase that methylates pseudouridine at position 1189 (Psi1189) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. N1-methylation is independent on acp- modification at the N3-position of U1191. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 (RPS19A/RPS19B) during the formation of pre-ribosomes. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family."}
+{"protein": "MRLFIILSVASFGAIGVLSQGGGGGGAAGGLLEGGGGFEEYGHRSRGSIIGLSRGIEIGRHYGGGGGGGGEGEEGREHELRGGGLELGGGGGGGGGGGGGGGEGRHYEIGFGGSHFNTPVDVHHEEAIHLKAHPEYHSDYHVADHKTKDFKSKHEVRDGYKVKGTYSLLEPDHKTVRVVDYVSDKKRGFIARVSYRKHH", "text": "FUNCTION: Cuticular proteins play a significant role in determining the physical properties of cuticles."}
+{"protein": "MLSQKTKKKHNFLNHGLSLNLVIKPYLALEGSVAFPAENGVQDTESTLEKRETGDEENSAKFPIGRRDFDTLRCMLGRVYQRCWQV", "text": "SIMILARITY: Belongs to the melanin-concentrating hormone family."}
+{"protein": "MSRRSQRLTRYSQDDNDGGSSSSGASSVAGSQGTVFKDSPLRTLKRKSSNMKHLSPAPQLGPSSDSHTSYYSESVVRESYIGSPRAVSLARSALLDDHLHSEPYWSGDLRGRRRRGTGGSESSKANGLTAESKASEDFFGSSSGYSSEDDLAGYTDSDQHSSGSRLRSAASRAGSFVWTLVTFPGRLFGLLYWWIGTTWYRLTTAASLLDVFVLTRSRHFSLNLKSFLWFLLLLLLLTGLTYGAWHFYPLGLQTLQPAVVSWWAAKESRKQPEVWESRDASQHFQAEQRVLSRVHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLKEDLRRDTVAHIQEELATLRAEHHQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQFPDWIRQFLLGDRGARSGLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSEDRIGMVDYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH", "text": "FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome- nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for Rab5-GDP and participate in the activation of Rab5. SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II membrane protein Nucleus envelope Endosome membrane; Single-pass type II membrane protein Note=Colocalizes with KASH5 at sites of telomere attachment in meiocytes."}
+{"protein": "EFRPNSDGDKGPNSDGDKGPNSDGDKGPNSDGDKGPNSDGDKGPNSDGDKGPNSDGDKGPNSDGDKGPNSDGDTEF", "text": "FUNCTION: S antigens are soluble heat-stable proteins present in the sera of some infected individuals. SUBCELLULAR LOCATION: Parasitophorous vacuole Note=Localizes to the cell periphery in early schizonts and then to the parasitophorous vacuole in late schizonts. Following schizont rupture, the S-antigen is released in host sera."}
+{"protein": "KNYGNGVHCTKKGCSVDWGYAWTNIANNSVMNGLTGGNAGWHN", "text": "FUNCTION: Inhibits a wide spectrum of lactic acid bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family."}
+{"protein": "MFAARFDPTKVVREEPKIIPQKRAIPDDVESSDSDQDIEDGVEVGAVSKEQSGTDVTTTRAVDGKSESDSESESESESDSDDEMNFDMGGSSSSSDDDEVSSKDADVDDDGKHTSVLSRFKKTLSIQDKISALEEANTQDILEDGEAHDLAQIPQPAVVRDKKLQVKDISEMKNTAFRDTRKVHYDNSMTKSFEEYSDDLTPKLLNNIEKYFSKSTFPIQTAMLDQYLKLINFTLKTSKKNFTRRIGDILVNASTGSGKTLAYSIPIIQTLSSRTVNKLRVLIILPTKLLINQVFQTMSQLAEGTSLVITVSKLENSFNEEHKRLLKTEPDIFITTPGRLVDHLTNSSISLRNLKFLVLDEADRLLNQSFQNWIPEVMSKFKSDKFDQMPGSIIKMVFSATLTTNTEKLNDLQLYNPTLFATDSVKLYNLPPTLQEYQLQIPSAKSVYKPLYLLKLLEQLSGGKTLVFVRSNESSLKLEVLLKSLIKGHMTTLQIVVHSINSNNSKAENRRLVTDFTKESLPNQTNVLITTDLMSRGIDIENIANVINYDVPISSQQYVHRCGRTARANKDGKAYNMLVGKGEAQFWKDSIDEDISRDVSGCKPISYNDSYNKVHGDENARTSEPTRDLFTSIDSETSDKYNEILKNLTQK", "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. DDX51/DBP6 subfamily."}
+{"protein": "MKASMFLALAGLVLLFVVGYASESEEKEFPIELLSKIFAVDVFKGEERGCKGFGDSCTPGKNECCPNHACSNKHKWCKVYLGK", "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. 15 (Hntx-3) subfamily."}
+{"protein": "MSLEILDQLEGKIKQAVETIQLLQLEVEELKEKNQQAQQANDELRSENEQLKGEHNNWQERLRSLLGQIDNV", "text": "FUNCTION: Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA. SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to the septum at mid- cell, in a FtsZ-like pattern. SIMILARITY: Belongs to the ZapB family."}
+{"protein": "MDVRTLAVGKAHLEALLATRKMTLEHLQDVRHDATQVYFDGLEHLQNVAQYLAIPLSEFFVGQTQSDLDDGVKIARRNGGFKREEIRGGVHYYTYEHLVTTNQDPGLMALRLDLHSDDEQPLRLNGGHGSREIVYVTRGAVRVRWVGDNDELKEDVLNEGDSIFILPNVPHSFTNHVGGAKSEIIAINYG", "text": "FUNCTION: Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)- epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic. SIMILARITY: Belongs to the non-heme iron-dependent dioxygenase family."}
+{"protein": "MAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQGFQEGVSNASVIMQVPERIVVAGNNEDIPFSRPADLDLIQSTPFKPLALKTPPRVLTLSERPLDFLDLERPAPTPQNEEIRAVGRLKRERSMSENAVRQNGQLVKTDSMYGISNIDAMIEGTSEDMTVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR", "text": "FUNCTION: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein Peroxisome Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. SIMILARITY: Belongs to the Tango11 family."}
+{"protein": "MRAYFVLLVAATAILTYGGATATYSTSKGEMNLTGTVENNRPTRSLRVAPSGGNGEERSWSTIYGISRSKAETVRDWLMPRLNQGMDVQALAREMGITSRQAATQHQNWDALVKYLKMYNYAVRGEKMSKSMAESVLLHNVLTAKNNF", "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 (PubMed:24763622). Also partially attenuates INF1-triggered cell death (PubMed:24763622). SUBCELLULAR LOCATION: Secreted Host cytoplasm Host cell membrane. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MGFITRFLVFMSLFTSLVSGFALQKLPLIQFDEGYTQLFGDQNLIVHRDGKSVRLTLDERTGSGFVSNDIYLHGFFSSSIKLPADYSAGVVIAFYLSNGDLYEKNHDEIDFEFLGNIRGREWRIQTNIYGNGSTHLGREERYNLWFDPTEDFHQYSILWSLSHIIFYVDNVPIREVKRTASMGGDFPAKPMSLYSTIWDGSKWATDGGKYGVNYKYAPYVSQFTDLILHGCAVDPTEKFPSCKDEAVQNLRLASEITESQRNKMEIFRQKHMTYSYCYDHMRYKVVLSECVVNPAEAKRLRVYDPVTFGGIPHGHRRGKHRSRSRLARTESI", "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 (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 3 subfamily."}
+{"protein": "MRAIIYLLLISAMVFSMTKAVPEEEGLQLSEDERGGCLPHNRFCNALSGPRCCSGLKCKELSIYDSRCLG", "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": "MAKKVKSKVDTINTKIQLVMKSGKYVLGTQQSLKTLRQGRSKLVVISANCPPIRKAEIEYYCTLSKTPIHHYSGNNLDLGTACGRHFRACVLSITDVGDSDITSA", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL30 family."}
+{"protein": "MENVFDYEDIQLIPAKCIVNSRSECDTSVRLGGHTFKLPVVPANMQTIIDEKLAISLAENGYFYVMHRFEPETRIDFIKDMNARGLFSSISVGVKDEEYEFVRQLAEENLTPEYVTIDIAHGHSNAVIEMIQHLKKHLPDSFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAASKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESPGQTIEKDGKLYKEYFGSASEFQKGEKKNVEGKKMHVAHKGSIKDTLIEMEQDLQSSISYAGGTKLNAIRNVDYVIVKNSIFNGDKY", "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 (Probable). SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily."}
+{"protein": "MPADPSEEVAPQVPKTELEELQINAQGVADESLESTRRMLALCEESKEAGIRTLVALDDQGEQLDRIEEGMDQINADMREAEKNLSGMEKCCGICVLPCNKSQSFKEDDGTWKGNDDGKVVNNQPQRVMDDRNGMMAQAGYIGRITNDAREDEMEENMGQVNTMIGNLRNMALDMGSELENQNRQIDRINRKGESNEARIAVANQRAHQLLK", "text": "FUNCTION: May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion (By similarity). SUBCELLULAR LOCATION: Synapse, synaptosome Note=Complexed with macromolecular elements of the nerve terminal. SIMILARITY: Belongs to the SNAP-25 family."}
+{"protein": "MIGVIFGVIVPYIAVAIFVIGVIYRIVNWANSAVPLKIPTTGGQQKSFPFIKRTIYDRFDSPYTWWETAGRMLLEIFFFRSLLKNTRYYLDRVSQKDARWLWLFGILFHYSLLLVLIRHSRFFLDPVPSFVETLSEIEAFKGVFIPSVYMSGLAIVAALFLLWLRRIFLSRERTLSLPSDHFALILLLAITISGNVMRYFVKADLFAVKELLMSLMTFNIGHAVEVANTIEPIFYVHFALASFLLAYFPFSKLMHAGGVFFSPTRNMPNDNRARRHVNPWDPADVPLLAKGITVAGRVYKSKKLDWDTYYSMYTDQLQEIEEADYKIVPEEL", "text": "FUNCTION: Has menaquinol-oxidizing activity. HmeC and HmeD subunits may together mediate electron transfer from menaquinol to an unidentified electron acceptor on the cytoplasmic side of the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MFGRAPKKSDSTRYYEILGVPKDASPEDLKKAYKKAAIKNHPDKGGDPEKFKELAHAYEVLSDPEKREIYDQYGEDALKEGMGGGGGMHDPFDIFQSFFGGSPFGGVGSSRGRRQRRGEDVVHPLKVSLEDLFTGTTKKLSLSRNVICSKCTGKGSKSGASMKCSGCQGTGMKVSIRHLGPSMIQQMQHPCNECKGTGETINDKDRCPQCKGEKVVQEKKVLEVVVEKGMQHGQKITFPGEADEAPDTVTGDIVFVLQQKEHPKFKRKGEDLFYEHTLSLTEALCGFRFVLTHLDGRQLLIKSNLGEVVKPDQFKAIEDEGMPIYQRPFMKGKMYIHFTVEFPDSLNPDQVKSLEAILPPKPSMSLTYMELDECEETTLHNVNIEEEMKRKQTQAQQEAYDEDDEPAGGQRVQCAQQ", "text": "FUNCTION: Plays a continuous role in plant development probably in the structural organization of compartments. SUBCELLULAR LOCATION: Membrane; Lipid-anchor."}
+{"protein": "MPPYTIVYFPVRGRCEAMRILLADQGQSWKEEVITGETWGKGSLKSTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKDQREAALVDMVNDGVEDLRCKYVTLIYTKYEEGKDDYVKALPGHLKPFETLLSKNQGGKAFIVGDQISFADYNLLDLLLIHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPDHVNRPINGNGKQ", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Nucleus Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. SIMILARITY: Belongs to the GST superfamily. Pi family."}
+{"protein": "MKLKLNVLTIVLLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVAKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKAALLDINCVKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMYGGK", "text": "FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:28209804, PubMed:23766516, PubMed:9096315). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:9096315). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET (PubMed:23766516). Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (PubMed:23766516). Modulates prostaglandin E2 secretion (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type III membrane protein Peroxisome membrane; Single-pass type III membrane protein Microsome membrane; Single-pass type III membrane protein Endoplasmic reticulum membrane; Single-pass type III membrane protein Cell membrane. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MSFLSRFVCAVPRQAIFRTFSTLTGSSGCKYLPESTFNTIQKVSFCKKSAKGKDGDLKKKCAEAAKKEKEAAEKKKCAEAAKKEKEAAEKKKCAEAAKKEKEAAEKKKCAEAAKKEKEAAEKKKCAEAAKKEKEAAEKKKCAEAAKKEKEAAEKKKCAEAAKKEKEAAEKKKCAEAAQKKKCAELAKKEQEAAEKKKCAEAAKKEKEAAEKKKCEERAKKEKEAAEKKKCEERAKKEKEAAEKKKCAEAAKKEKEAAEKKKCAEAAQKKKCAELAKKAKEAAEKKKCAKKAGEKGSKQSGSDKGKKNGKKNDMKNKCAMLAKKAKEEALKKKCAAAQKKCEPKK", "text": "FUNCTION: Possible structural role in the sperm tail. It is associated with axonemal structures. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MIRIPFHLRQTPGRTLHSLVRSFASTKPADLSGTQEKSTRQKINFHELKHPSKVPQRPHKSTIDGQSTPTRIPVDAQKGQLLERLSLVDLDSAEAHRTLEDAIEFASQILSVDTDDVEPLYTVLERERLTLREDRVSDGNIQQDVLRNARVTEEENFVAPPENIPLEQEPRK", "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 GatC family."}
+{"protein": "MGESFDAFSLDEDMPMETNEKRKDGRDRGTRAQSAVVVQPVAASRHK", "text": "FUNCTION: Plays an important role in the cytoplasmic envelopment of tegument proteins and capsids during the assembly and egress processes. Participates also in viral entry at the fusion step probably by regulating the core fusion machinery. SUBCELLULAR LOCATION: Virion tegument Virion membrane; Lipid-anchor Host cell membrane; Lipid-anchor; Cytoplasmic side Host Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side Note=Virion membrane-associated tegument protein. Associates with host membrane lipids rafts. 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 HHV-1 UL11 family."}
+{"protein": "MNTLQGPVSFKDVAVDFTQEEWRQLDPDEKIAYGDVMLENYSHLVSVGYDYHQAKHHHGVEVKEVEQGEEPWIMEGEFPCQHSPEPAKAIKPIDRKSVHQICSGPVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLISFSSETSHM", "text": "SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family."}
+{"protein": "MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILSDDTALKEYKIDEKNFVVVMVTKPKAVTSAVPATTQQSSSPSTTTVSSSPAAAVAQAPAPTPALAPTSTPASTTPASTTASSEPAPTGATQPEKPAEKPAQTPVLTSPAPADSTPGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPPQAVSTGTPQSPAVAAAAATTTATTTTTSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGGGGGGGGGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED", "text": "FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with Cetn2 appears to stabilize Xpc. May protect Xpc from proteasomal degradation (By similarity). FUNCTION: 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:Rad22b induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity). FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 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. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RAD23 family."}
+{"protein": "MTELTTPIYPLQRNWSWWFLNDDRNASWQDRLKKVYTFNTVPEFWAFYEAILPPSGLNDLCDYNVFRDDIQPKWEAPENWDGGRWLIIINKGKTPEVLDAVWLEILLALIGEQFGKDMESICGLVCNVRGQGSKISVWTKNCNDDDTNMRIGVVLKEKLMAAASKAHSKPLFDVIHYQTHRNCVKKTTSALKYKFSLKSIV", "text": "FUNCTION: 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. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. SIMILARITY: Belongs to the eukaryotic initiation factor 4E family."}
+{"protein": "MKIRSAKVIVTCPGRNLVTLKIETDEGVYGIGDATLNGREKSVVSYLEDHVIPTLIGKDPQRVEDIWQYLYRGAYWRRGPVGMTAIAAVDVALWDIKAKLAGMPLYQLLGGKSREKVMVYGHATGLDIESCLEEVRKHVELGYKAVRVQCGIPGIPTTYGVSKEAGKPYEPADSALPAEHVWSTEKYLNNVPELFAAVRKEFGEDLHILHDVHHRLTPIQAARLGKEVEKFHLFWLEDCTAVENQSSYELIRKHTTTPLAIGEVFNSLSDCQELIQNQLIDYIRATITHAGGITNIRRIADFASVFHVKTGFHGATDLSPVCMGAALHFDTWVPNFGIQEHMPHTKETDLVFPHAYEFNDGFFTPGDVPGHGVDIDEEIAAKYPYKPAYLPVNRLEDGTLWNW", "text": "FUNCTION: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. GalD subfamily."}
+{"protein": "MLLLGLLLLTSALAGQRTGTRAESNLSSKLQLSSDKEQNGVQDPRHERVVTISGNGSIHSPKFPHTYPRNMVLVWRLVAVDENVRIQLTFDERFGLEDPEDDICKYDFVEVEEPSDGSVLGRWCGSGTVPGKQTSKGNHIRIRFVSDEYFPSEPGFCIHYSIIMPQVTETTSPSVLPPSSLSLDLLNNAVTAFSTLEELIRYLEPDRWQVDLDSLYKPTWQLLGKAFLYGKKSKVVNLNLLKEEVKLYSCTPRNFSVSIREELKRTDTIFWPGCLLVKRCGGNCACCLHNCNECQCVPRKVTKKYHEVLQLRPKTGVKGLHKSLTDVALEHHEECDCVCRGNAGG", "text": "FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function. SUBCELLULAR LOCATION: Cytoplasm, cytosol Secreted Nucleus Cytoplasmic granule Cell membrane Note=Sumoylated form is predominant in the nucleus (PubMed:16443219). Stored in alpha granules in platelets (By similarity). SIMILARITY: Belongs to the PDGF/VEGF growth factor family."}
+{"protein": "MNYEAEQPGANDDASGVAVALELARVLAKRKPAATIVFAAVAGEEQGLLGAQFMAQTFKNASVNVEGMLNVDLVGSSVGSRGEKEPNTVRLFCQGPPLTETPAQASQRLSIGGENDSPARQLGRFITEVAANKFTDMRVAMIYRLDRFLRGGDHRPFLEAGYAAVRFTEPNENFDHQHQDTRVEDGVQYGDLPEFLDYEYIARVAKVDLAAMWSLANAPAKVNNVRVNGTWLSNDSQLFWDPVNSTNLAGYEVVWRPTDAPLWTHALFVGDVRTATVELSKDNVIFGVRSVGKNGYKSPVTIPFPT", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily."}
+{"protein": "MASTLPTTWPHESVKFEDVSLRFTEEEWALLDRQQKCLYREIMMENLNNMISVEHHFSKANVMPQLEEVEDCWPMQREIPQDTLPECSGHSLDPEMNSFPAESPLMKIKVVEVLTLNKDMAGPRNALIQSLYPESGEDLNPGNLKPAQQPSKHLTDTEASRQKFRHFQYEESAGPQKSVSQLRKLCHQWLQPSTRSKKQILELLVLEQFLNALPEKLRVWVESQHPEDCKAVVALLENMTSVSKDDAWLACSSEATDELKEKRKDVATLPVTVPPEAPVTFQDVAVDFSQEEWQLLGPMQRTKYHDVMLETLGNLVSVGWEPTLGNRELTPDSPIPVVKPIHDPNPKDLSRNRTQSTLFESISPDEVQGRHTIESNPVGLLQEKGHPQQKLSESSKSQNQTCIDKSQCSLNEVLPRNHVKVKQKGTGKGKGRTNTISMTGGLRIRNQQKDSVEWRDRSGSTPVTHGSSIKNQQLGSEQGKTQTSRDPITLTVPAEFYQEATGSEEGRFRNSSNAMAADAPPKIHQKGPEWHKAGKSNNSMLQGSSAQNHQMGSRAGRARDNSILTHVKIHQKGYKEGKIQGNNNYLKHVKPHRKGSKEERLRELSTCQKHVPYVKQHLKTSGRGKGRKINASIKCGPYIKTYYRGSDVGRLRRANNCRKAISRHAQQISFIKIHKGSQVCQCSECGKMFRNARYFSVHKKIHTGERPYMCMSCGKAFVQSSSLTQHLRIHSGERPFECSECGRTFSDRSAASQHLRTHTGAKPYQCQHCGKAFRQSSHLTRHVRIHTGERPYVCTKCGKAFTQSSNLIGHQKTHRKKFKKQPKL", "text": "FUNCTION: Transcription regulator which may participate in NGFR/p75(NTR)-mediated apoptosis. Probably acts as a transcription repressor: specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin-modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD", "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 co- chaperones have been shown to not only regulate different steps of the ATPase cycle, 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 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. The co-chaperones are of three types: J-domain co-chaperones such as 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 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). 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 co- chaperones have been shown to not only regulate different steps of the ATPase cycle, 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 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. The co-chaperones are of three types: J-domain co-chaperones such as 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 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation (PubMed:28842558). 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 co- chaperones have been shown to not only regulate different steps of the ATPase cycle, 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 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. The co-chaperones are of three types: J-domain co-chaperones such as 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. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone- mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1- mediated SMAD3 ubiquitination and degradation and facilitates STUB1- mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. FUNCTION: (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Secreted Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "AYAEALGVDIDQLILSQPNTGEEGLQIADTLISSGAIDIVVVDSVAVLVPRAEIEGEMGDSHVGLQARLMSQALRKLSGTIAKTKTIAIFINQIREKVGVMFGN", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecA family."}
+{"protein": "MLRLSGVKSAVRARAAAGAAFSVSLSGPQAVSLLALPLVRHATKRAGGGKTNLKDSIGRRLGVKATEGTYVQPSDIIYRQRGTKFYPGENTWIGRDHTIYAKEPGYVRFYYDPFHPTRRFVGVGLTPEARLPTDHMAPRARRFGRNVISDPKRAEAELAWRPNKEQQLLEEISERRAVKQAEEQALTDKLAAKLKELGFDNSELAARAQKMAHYRTLGWTNAEAARFADAFLNTSSDVKDFDAKFEVTKFGTVVPKSSPETVEKELNETRDKLTKVRQPNAFISLSQIAKIDKILDATVYLSQSQKEQLADEFKVTASLLEAVQPHEEVVKAAKKGKGKLVKVYNVQRKGIDYVLAPKDAHFSEDIAFQKEFVH", "text": "FUNCTION: Component of the large subunit of mitochondrial ribosome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
+{"protein": "MASLLQSERVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSQHTIHVVDKYSLGTRLQRPRAGASISTLAGLSLREGEDQKEVKIEPAQAVAEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDLQPVSASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLLECDEGDPDNINSTAKVVVPPKELILAGKDAAAEYDELAEPQDFQDDPDIVAFRKANKVGIFIKVTPQREEGEVTVCFKMKHDFKNLAAPIRPVEEGDQGTEVIWLTQHVELSFGPLLP", "text": "FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, stress fiber Cytoplasm, cell cortex Cytoplasm, myofibril, sarcomere Note=Has a punctate cytoplasmic distribution as well as centrosomal distribution typical of dynactin (By similarity). Overexpression in cultured mammalian cells revealed colocalization with cortical actin, stress fibers, and focal adhesion sites, sites of potential interaction between microtubules and the cell cortex (By similarity). In skeletal muscles, costamere localization requires the presence of ANK2 (PubMed:19109891). SIMILARITY: Belongs to the dynactin subunit 4 family."}
+{"protein": "MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG", "text": "FUNCTION: An L-glutamate ligase that catalyzes the ATP-dependent post- translational addition of glutamate residues to the C-terminus of ribosomal protein bS6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. FUNCTION: An L-glutamate ligase that catalyzes the ATP-dependent post- translational addition of glutamate residues to the C-terminus of ribosomal protein bS6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. SIMILARITY: Belongs to the RimK family."}
+{"protein": "MKELHKTSFLESLLIQKRVIGALLMREIITRYGRNNIGFLWLFVEPLLLTLVMVLMWKFFRMHNVSALNIVAFTLTGYPMMMMWRNASNHAIGSISANTSLLYHRNVRVLDTIFARMLLEIAGATIAQVVIMFALVIIGWIDVPADIFYMLLAWLLMAMFAVGLGLVICSVAFHFEPFGKVWSTISFVMMPLSGVFFFVHNLPQQLQHYVLMIPMVHGTEMFRAGYFGDSVTTYENPWYILLCNLVLLLLGLAVVARFSKGVEPQ", "text": "FUNCTION: May form an ATP-driven capsule polysaccharide export apparatus, in association with the CtrB and CtrD proteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-2 integral membrane protein family."}
+{"protein": "MAEPDLLAPFADLPFPPGDDFPDFPTLGDDAFALEDFDLDDLDFDFDVDLFPPDAPPPVTTSSSSSAAGSPEAGTSSAGDGGSKNEESADSSSPSRSGSDGGGGKDGKDDEAKRRARLVRNRESAHQSRQRKKQYVEELEGKVKVMQATIADLTARISCVTAENAALKQQLGGAAGAGAAAPPPPMPMYPAVYPLPMPWIHPAYAMRGSQVPLVPIPRLKTQQPASTPEPPAKKARKTKKVAGVSLLGLLFLMMVCGCLVPAVNRMYGAAYTGEGAAIVPSHHGRILAVEGPQNSVSNGVDPKVPQNGSETLPALLYLPRNGKHVKINGNLVIKSIVASEKASSRLSNYGEKGSGNQGKEETSLAIPGYVAPLEAGEVMDSAKGMNELMALAPGDGSIYREDDGMLPQWFSEAMSGPMLNSGMCTEVFQFDLSPTTADANGIVPVYSGSVTNTSQNYTENLPSGPVQKVKNRRISYSEAIPLRGSTSNDTDHFKAPPKNHSQSHAGRKPVSSVVVSVLADPREASDRDGEGRISSNSLSRIFVVVLIDSVKYVTYSCVLPFKSHSPHL", "text": "FUNCTION: Transcription factor involved in endoplasmic reticulum (ER) stress response. Acts as ER stress sensor and activates the transcription factor BZIP50 and the chaperone BIP1. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus Note=The bZIP domain is translocated into the nucleus in response to ER stress. SIMILARITY: Belongs to the bZIP family."}
+{"protein": "MAAPALSWRLPLLILLLPLATPWASATVNGTSQFTCFYNSRANISCVWSQDGALQDTSCQVHAWPDRRRWNQTCELLPVSQASWACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMAIQDFKPFENLRLMAPISLQVVHVETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEEAPLLTLKQKQEWICLETLTPDTQYEFQVRVKPLQGEFTTWSPWSQPLAFRTKPASLGKDTIPWLGHLLVGLSGAFGFIILVYLLINCRNTGPWLKKVLKCHTPDPSKFFSQLSSEHGGDVQKWLSSPFPSSSFSPGGLAPEISPLEVLERDKVTQLLLQQDKVPEPASLSSNHSLTSCFTNQGYFFFHLPDALEIEACQVYFTYDPYAEEDADEGVAGAPTGSSPQPLQPLSGEDDTYCTFPSRDGLLLFSPSLLGGPSPPSTAPGGSGAGEERMPPSLQERVPRDWDPQPLGPPTPGVPDLVDFQPPPELVLREAGEEVPDAGPREGVSFPWSRPPGQGEFRALNARLPLNTDAYLSLQELQGQDPTHLV", "text": "FUNCTION: Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell surface. SIMILARITY: Belongs to the type I cytokine receptor family. Type 4 subfamily."}
+{"protein": "MAAAAAAAAICGEDETAARVGCTGEWAGGIERVDLGERKEAVAAAGAGKRSVYLMDCAPVWGCASTRGRSAEMEDASAAVPRFADVPVRLLASRRDLDALGLDADALRLPAHLFGVFDGHGGAEVANYCRERIHVVLSEELKRLGKNLGEMGEVDMKEHWDDVFTKCFQRVDDEVSGRVTRVVNGGGEVRSEPVTAENVGSTAVVALVCSSHVVVANCGDSRIVLCRGKEPVALSIDHKPDRKDERARIEAQGGKVIQWNGYRVSGILAMSRSIGDRYLKPFVIPKPEVMVVPRAKDDDCLILASDGLWDVVSNEEACKVARRQILLWHKNNGAASPLSDEGEGSTDPAAQAAADYLMRLALKKGSEDNITVIVVDLKPRKKLKNIS", "text": "FUNCTION: Protein phosphatase involved in abscisic acid (ABA) signaling. Together with PYL3 and SAPK10, may form an ABA signaling module involved in stress response. SIMILARITY: Belongs to the PP2C family."}
+{"protein": "MLACIACSTKDGGEGGHRSATATPNSGKSLTSQLKDMVLKFSGSGRHQYKSGGSPSLRTSRFHRSSRLAAYPGIIDESGFTSDGAGEAYTYMRTTTASAGARAAPSTWDLPPKVNHRSFQPRVIRSPSASGVPSIGEEDYDDDDDDDDEETVLLEEDRVPREWTAQVEPGVQITFVSIPGGAGNDLKRIRFSREMFNKWEAQRWWGENYDRVVELYNVQTFSRQQGFSTPTSSVDEAMQRDSFYSRVGSTRESPAMMMPPPPPLPSSGAGREHPISRTASSKAQLSSSSSVAAARPPFYPSTAVPDPSDHVWAHHFNLLNSAAAGPAAPYDPSRGTTSSRDEASVSISNASDLEATEWVEQDEPGVSITIREFGDGTRELRRVRFSRERFGEERAKVWWEQNRDRIHAQYL", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BRX family."}
+{"protein": "MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSEKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTTPELEGQGS", "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": "MAAAVLGQLGALWIHNLRSRGRLAWGVLPQSYVHTSASLDISRKWEKKNKIVYPPQLPGEPRRPAEIYHCRRQIKYSKDKMWYLAKLIRGMSIDQALAQLEFNDKKGAKIIKEVLLEAQDMAVRDHNVEFRSNLYIAESTSGRGQYLKRIRYHGRGRFGIMERVYCHYFVKLVEGPPPPPEPPKMAVAHAKEYIQQLRSRTIIHTL", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL22 family."}
+{"protein": "METLQVEVFFLFDFTSIMAGFKVPSWITYKSFWIAVSSSVTTACVILGTLEFRKHRSIRRLQSMIVPEAGKSIQLSSSGVPIEIYDAGEEDEGISKGVPYDENLIREQLARNYAFFGEDGMERLRNSFVIVVGCGGVGSWVINMLARSGVQKIRIVDFDQVSLSSLNRHSIATLQDVGTPKTLAIKKAIKKFAPWIEVDARNALFNPDSADDLLSGNPDFVIDAIDNIQTKVDLLSYCYNHKLPVIASTGSACKSDPTRVNIADISATSEDPLSRATRRRLRLLGIMEGIPVVFSTEKPDPRKASLLPLSEEEFEKGDVDELSALPEFRARILPVIGPMPGIFGLTIATYVLTSIAKYPMDPISTMTRPRLYEEAVKRLHAEARKAGVNLDKTFNASEMSYIIEEVYVGRSALPPHESQKVTVVRWNPQLPFDHTNLVAMTRNEARYHEDNVLAKNVDPSTVYGKDVIEVVHSFLRRLRMWEMLY", "text": "FUNCTION: Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HesA/MoeB/ThiF family."}
+{"protein": "MKFGMGSAQACPCQVPRAASTTWVPCQICGPRERHGPRTPGGQLPGARRGPGPRRPAPLPARPPGALGSVLRPLRARPGCRPRRPHPAARCLPLRPHRPTRRHRRPGGFPLAWGSPQPAPRPAPGRSSALALAGGAAPGVARAQRPGGSGGRSHPGGPGSPRGGGTVGPGDRGPAAADGGRPQRTVRAAETRGAAAAPPLTLEGPVQSHHGTPALTQGPQSPRDGAQLGACTRPVDVRDSGGRPLPPPDTLASAGDFLCTM", "text": "FUNCTION: [Isoform 3]: Does not affect cell growth. SUBCELLULAR LOCATION: Note=Contrary to isoforms 1 and 2, isoform 3 does not localize to the mitochondria."}
+{"protein": "MAAEEAEVVSPLIVDTAPDTSGTAAASLAAAVSAAAAAARTGSQAQVSKAALAAKLMSLSGVFAVHKPKGPTSAELLNRLKEKLLAEAGLPSPEWNKRQKQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRYIATGELGKATDTLDSTGKVTEEKPYDKITQEDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKRGETVEARPARPVTVHSISLLKYQPPFFTLDVECGGGFYIRSLVSDIGKELSSCATVLELTRTKQGPFTLAQHALPEDRWTINDIAQSLKRCTSLLPEELTFKKSKSEPSSDQALSCGYITLRETKREDDTVKTL", "text": "FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs and tRNAs. Mediates pseudouridylation of mRNAs with the consensus sequence 5'-GUUCNANNC-3', harboring a stem-loop structure. Constitutes the major pseudouridine synthase acting on mRNAs. Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs. Promotes the processing of pri-let-7 microRNAs (pri-miRNAs) independently of its RNA pseudouridylate synthase activity. Acts by binding to the stem-loop structure on pri-let-7, preventing LIN28- binding (LIN28A and/or LIN28B), thereby enhancing the interaction between pri-let-7 and the microprocessor DGCR8, which mediates miRNA maturation. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Catalyzes pseudouridylation of mRNAs in the nucleus. SIMILARITY: Belongs to the pseudouridine synthase TruB family."}
+{"protein": "MDQDAFILKEDSEVEREAPGGRESLSDVIGFLDAVLSSEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQDNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHRAFGGRTGTNSVSQDLGDGGDSGILENPPNERGYPRSGIEDENREMAAHPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLTPATVPGTRSPPLNRYNSTGSPPGKPPSTQDEHINSGDTPAVRVKDRKPPIGTRSVSDCPANGRPIHPGLESDSTKKGIGENTSSMKEMATLLTSLGVIQSAQEFESSRDASYVFARRALKSANYAEMTFNVCGLILSAEKSSARKVDENKQLLKQIQESVESFRDIYKRFSEYQKEQNSLLMSNLSTLHIITDRGGKTDNTDSLTRSPSVFAKSKENKTKATRFDPSMETLEDMKYKPDLIREDEFRDEIRNPVYQERDTEPRASNASRLLPSKEKPTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELVEEDIESLTN", "text": "FUNCTION: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. FUNCTION: Acts as a chaperone for newly synthesized free N protein, so- called N(0). Stabilizes the L protein upon binding it. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the respirovirus P protein family."}
+{"protein": "MSLSGASERSVPATKIEITVSCRNLLDLDTFSKSDPMVVLHTQSRASQEWREFGRTEVIDNTLNPDFVRKFVLDYFFEEKQNLRFDVYNVDSKANISKPKDFLGQAFLALGEVIGGQGSRVERPLTGVPGKKCGTILLTAEELSNCRDIATMQLCANKLDKKDFFGKSDPFLVFYRSNEDGTFTICHKTEVVKNTLNPVWQPFSIPVRALCNGDYDRTVKIDVYDWDRDGSHDFIGEFTTSYRELSKAQNQFTVYEVLNPRKKCKKKKYTNSGTVTLLSFSVDSEFTFVDYIKGGTQLNFTVAIDFTASNGNPLQPTSLHYMSPYQLSAYAMALKAVGEIIQDYDSDKLFPAYGFGAKLPPEGRISHQFPLNNNDEDPNCAGIEGVLESYFQSLRTVQLYGPTYFAPVINQVARAAAKISDGSQYYVLLIITDGVISDMTQTKEAIVSASSLPMSIIIVGVGPAMFEAMEELDGDDVRVSSRGRYAERDIVQFVPFRDYVDRSGNQVLSMARLAKDVLAEIPEQLLSYMRTRDIQPRPPPPVSPNPTPAPEQP", "text": "FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. Plays a role in dendrite formation by melanocytes. SIMILARITY: Belongs to the copine family."}
+{"protein": "MQLTSFTDYGLRALIYMASLPEGRMTSISEVTDVYGVSRNHMVKIINQLSRAGYVTAVRGKNGGIRLGKPASAIRIGDVVRELEPLSLVNCSSEFCHITPACRLKQALSKAVQSFLTELDNYTLADLVEENQPLYKLLLVE", "text": "FUNCTION: Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress. May require iron for activity. FUNCTION: Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress, such as ytfE, hmpA and ygbA. May require iron for activity. Does not regulate its own transcription."}
+{"protein": "MAAKRYTSMAYANADEMTFGVSKYPVKAGLDLEIGAGYTIPEINYAPRPEAGASKEKLIKEYERITTDVMERMVQVGFPAIILETEHVQQMSNNPSWGAEVAHAQKTIMEKYHDEYGIKCALRHTIGDIRENREFLQLRGDKYSVFLEAFEQCAENGADLLSVESMGGKEVFDYAVLRNDIPGLLYSIGCLGSIDMELIWTDISKIAKKTGTISAGDTDCAQANTAMFIGGGLLNKNLAHTIAVIARAISAPRSLVAYEAGAVGPGKDCGYENIIVKAITGMPMTMEGKTSTCAHSDVMGNLVMQCCDCWSNESVEYHGEFGGTTVQCWSETLAYDCALMNTALETKNDKVLRDLMMLSDRYRDPQAYMLAYDNAYRVGQSIVKDGDNIYLRAKNAAIECCNIIEEGAAGKLELSRFETKALADAKAALEALPDDMDKFMDDCLTKYKSEVKVFKPENYGF", "text": "FUNCTION: Methyltransferase involved in methanogenesis in the methanol pathway. Catalyzes the methylation of the MtaC-bound cob(I)amide. SIMILARITY: Belongs to the MtaB family."}
+{"protein": "MTMRIDTDKQMNLLSDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHKGSGQEAMKKAGLLQTYYDLALPMGVNIADKKGNILSTKNVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGGMSKVRKFVTDTEVEETGTFNIQADIHQPEINCPGFFQLCNGNRLMASHQGNLLFANPNNNGALHFGISFKTPDEWKNQTQVDFQNRNSVVDFLLKEFSDWDERYKELIHTTLSFVGLATRIFPLEKPWKSKRPLPITMIGDAAHLMPPFAGQGVNSGLVDALILSDNLADGKFNSIEEAVKNYEQQMFMYGKEAQEESTQNEIEMFKPDFTFQQLLNV", "text": "FUNCTION: An FAD-requiring monooxygenase active on some tetracycline antibiotic derivatives, which leads to their inactivation. Hydroxylates carbon 11a of tetracycline and some analogs. FUNCTION: Confers resistance to tetracycline via an oxidoreductase activity; NADPH is more active than NAD (Probable). Expression in E.coli leads to breakdown of tetracycline. Confers resistance to doxycycline, chlortetracycline, oxytetracycline and minocycline (PubMed:2644186). FUNCTION: This bacteria is able to grow in the presence of moderate concentrations of tetracycline and its analogs, presumably due to the presence of this protein (PubMed:19187139). Expression in E.coli leads to breakdown of tetracycline; the initial products include a monooxygenated compound. After 2 hours intact tetracycline is no longer detectable in the culture supernatant, while degradation intermediates remain detectable for at least 20 hours (PubMed:26038239). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aromatic-ring hydroxylase family. TetX subfamily."}
+{"protein": "MEEILIWIKKLEKYLYALNAKVAGIPLYKIIIASAIMLFTLILRRLIAFLIVKILTKLTIRTKTDVDELIVKAFVKPFSYFIVVFGFYLSLLVLEVPKVYADKFLKTFSLLILGWAIIRFLNLFHNKIVEFFVKVGGKDFAEEVGDFILKILKAFVVVIVGASLLQEWGVNIGAILASVGLLGLAVSLAAKDTFENILSGLIILLDKPVKVGETVKVKDFMGSVEDIGLRSTKIRTFDKSLVTIPNRDIVNNHVENFTRRNKRRVRFYIGVVYSTKREQLENILKEIRELLKEHPGVAKDEKFYVYFENYGDSSLNILIQYYANTNDYEEYLKIIEDINLKIMEIVEKNGSSFAFPSRSVYIEKMPKS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscS (TC 1.A.23) family."}
+{"protein": "MRKNVVRYLRCPHCAAPLRSSDRTLRCENGHTFDVARQGYVNLLRRPTKLAADTTDMVAARAALLDSGHYAPLTERLAGTARRAAGAGAPDCVVDIGGGTGHHLARVLEEFEDAEGLLLDMSKPAVRRAARAHPRASSAVADVWDTLPLRDGAAAMALNVFAPRNPPEIRRILRPGGTLLVVTPQQDHLAELVDALGLLRVRDHKEGRLAEQLAPHFEAVGQERLRTTLRLDHDALGRVVAMGPSSWHQDPDELARRIAELPGIHEVTLSVTFTVCRPLP", "text": "FUNCTION: Specifically methylates the guanosine in position 748 of 23S rRNA. Confers resistance to the macrolide antibiotic tylosine. SIMILARITY: Belongs to the methyltransferase superfamily. RlmA family."}
+{"protein": "MAREKSTDDGGGWKKFLWDSEKKQVLGRTGTSWFKIFVFYLIFYGCLAGIFIGTIQVMLLTISDFEPKYQDRVAPPGLSHSPYAVKTEISFSVSNPNSYENHVNGLKELLKNYNESKQDGNTPFEDCGVIPADYITRGPIEESQGQKRVCRFLLQWLKNCSGIDDPSYGYSEGKPCIIAKLNRILGFYPKPPKNGTDLPEALQANYNQYVLPIHCQAKKEEDKVRIGTIEYFGMGGVGGFPLQYYPYYGKRLQKNYLQPLVGIQFTNLTHNVELRVECKVFGDNIAYSEKDRSLGRFEVKIEVKS", "text": "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. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family."}
+{"protein": "MFPSISNISLSPSSLFTAYASLTGFLMLFRSLFNDEVPERLRSYITDLLNRFFTPKSKNLTMVIDEIIGFKRNQVFDAAEVYLRNKIGPETARLRVGKLPKQKHFTIYIEKGEEILDTFENSELRWTYVESENEASQKEKRYYELTFEKKLRDKVMNSYLSHVVAESEETKRDLRAVKLYSRDVRASKDDDGMAGAGWGCINLEHPSTFETLAMDPGAKKKIIDDMERFLKRREFYKRVGKAWKRGYLLYGPPGTGKSSLIAAMANYLKFDVFDLELSSIYENAQLKSILLSTTNRSILVIEDIDCSSAEVVDREADEYQEYEEGYYGRVTLSGLLNFVDGLWSSFGDERIIVFTTNHKERLDPALLRPGRMDMHINMSYCTGLGFRTLVSNYLGLGGLNHPLCEEIEALIDSTEVTPAELAEELMQEDDTDVVLRGVVSFVENRKVEISKTKELEGSTCRKLDGDDKHNVSSTNDLKKTKKKKKGGKGKAKGN", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily."}
+{"protein": "MGLTLSGRYISLFLAVQIAYLLQAVRAAGKCGTVFKGFSDCLLQLGENMANYPQELDEKENLQTICTYWDDFHSCATTALADCQEGATDLWEKLKKESRNLDFRGSLFELCAGGNGAIRSSVPFGVTLLITALSALVTWMQF", "text": "FUNCTION: Modulates postsynaptic dendritic arbor elaboration and synaptic maturation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Synapse. SIMILARITY: Belongs to the neuritin family."}
+{"protein": "MTSSADLTNLKELLSLYKSLRFSDSVAIEKYNSLVEWGTSTYWKIGVQKVTNVETSISDYYDEVKNKPFNIDPGYYIFLPVYFGSVFIYSKGKNMVELGSGNSFQIPDEIRSACNKVLDSDNGIDFLRFVLLNNRWIMEDAISKYQSPVNIFKLASEYGLNIPNYLEIEIEEDTLFDDELYSIMERSFDDTFPKISISYIKLGELKRQVVDFFKFSFMYIESIKVDRIGDNIFIPSVITKSGKKILVKDVDHLIRSKVREHTFVKVKKKNTFSILYDYDGNGTETRGEVIKRIIDTIGRDYYVNGKYFSKVGIAGLKQLTNKLDINECATVDELVDEINKSGTVKRKIKNQSVFDLSRECLGYPEADFITLVNNMRFKIENCKVVNFNIENTNCLNNPSIETIYGNFNQFVSIFNTVTDVKKRLFE", "text": "FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein OPG116. Serves as a bridge which links the DNA polymerase OPG071 and the uracil DNA glycosylase. SIMILARITY: Belongs to the orthopoxvirus OPG148 family."}
+{"protein": "MSGNNLSGNDEFDEQLRMQELYGGDPKEGDTQNEPSGEAHSLGQPPDDTPYEWDLDKKAWFPKITEDFIATYQANYGFSSDGASSSTANVQDANTKAVEEPPQKEVPETPDSKRKGEKRKAESGWFHVEEDRNTNVYVSGLPPDITVDEFIQLMSKFGIIMRDPQTEEFKVKLYKDDQGNLKGDGLCCYLKKESVELALKLLDEDEIRGYKLHVEVAKFQLKGEYDASKKKKKCKDYKKKLSLQQKQLDWRPERRAGPNRLRHERVVILKNMFHPMDFEDDPLVLNEIREDLRVECSKFGQIRKLLLFDRHPDGVASVSFREPEEADHCIQTLDGRWFGGRQITAQAWDGTTDYQVEETSREREERLRGWEAFLNAPEASRGLRRMDSIAGSERPGPSRMRHFSEHPSMSNMKAQEATTGMAFEETIDENKFEKAEEGGESEGDASEKDAKEGGSDGDHPEREGGEGCSKKENEEGCPERALEPEEGNPQTEAQENGPEREARKKSKMDYEKNGFSKESEDNDLGKESEGEDSLKKESEDDDSEEESEEDSSEKQSQDGSDKEIEENGVKKDVDQDVSDKEFPEDVEKESEENETDKSEFDEGSERVLDEEGSEREFEEDSDEKEEEGDDDEEEVVYERVFDDDSDDIEEEEEADEKECEDADDKEEDNDIDEKLFDDSDEKEDEEDTDGKKDDDASDKVFEDNSNEKLFDEEEGPNEKLFDDSDERGTVGNVKEDGSQSTDSSFALSSSDDDDDEV", "text": "FUNCTION: Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HTATSF1 family."}
+{"protein": "MAAAEAANCIMEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR", "text": "FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, FMR1, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP and MAP3K5/ASK1 (PubMed:12737817, PubMed:15837430, PubMed:18492485, PubMed:22095282, PubMed:19405910). Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway (By similarity). Methylates RBM15, promoting ubiquitination and degradation of RBM15 (By similarity). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity (By similarity). Methylates CHTOP and this methylation is critical for its 5- hydroxymethylcytosine (5hmC)-binding activity (By similarity). Methylates MAP3K5/ASK1 at 'Arg-85' and 'Arg-87' which promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5- induced activation of JNK (PubMed:22095282). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Plays a role in regulating alternative splicing in the heart (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Cytoplasm, cytosol Cytoplasm Note=Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family."}
+{"protein": "MSMRGSGKLWLVMADGQEDPAVFTSTCLPSDSRLLATVTNAYLGTRVYRNILHVSGVYNGAAGDTHRADIPSPVNVRMTVPDGDVPVETFTLNTRTGTFSHKLESSSYTATHQIYAHHSLVHLMAFSITIWRSAGTSQPITVQLQAPFVPKSQDLDLQQGPDFQGAHYIYGQTLVPEVEGGPQPTVHMLWTPVPQAVTLHEEEQERRWEFLTAVAESEEEAKRSYSEGLARMAAGSLHSSHTRAWAALWRGCCVDLEGPLPLRQALYGCLYYLLSAIPPQGTPGFHFHGISPGGLSNGTRGEDYWGHVFWDQDTWIFPNILLFYPEAARAILEYRIRTLEGALLNAQEQGYKGAKFPWESAATGREVCPEDIYGAQEIHITGDVLMAFEQYYHTTQDQKLFRTDGGWELVSAVAQYWCSRMVWSEEEQCYHIRGVMPPDEYHYQVDNSAYTNAVAQRSLNFAASVARDFFIPVPEEWVECAKKVKVPFDAVRKYHPEYDGYSPGEPVKQADVVLLGFPLMHPMHPEVRRNDLVMYEPVTELSGPAMTWSMFAVGWLELKETQRAQGLLNKCFSNITEPFKIWVENSDGSGAVNFLTGMGGFLQAVLFGYTGFRITKTNLRFDPAFPSDVSKLEVTGVSYLGSKLKFSITKEKMRIAVTKCPLHPPLEAVLEESGQRFPLHEGQSISFPTAAGCIQKAPSEGL", "text": "FUNCTION: Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins. SIMILARITY: Belongs to the glycosyl hydrolase 65 family."}
+{"protein": "MSDVPDDANAGCPGTGSAGAGKASGCAGCPNQGSCATGQGPPPDADVPKIQDRFSRIKHKILILSGKGGVGKSTLTSNLARALASDPSKQVAILDVDICGPSQPRMMGVEDEEVHNSADGWTPVGIQPNLTLMSIAFLLGDKNDAVIWRGARKNGMIKQFLKDVDWGEVDYLLIDTPPGTSDEHISLVQFLLQAGPLDGALIVSTPQEVSLLDVRKEVSFCVKTKVPILGVVENMARFVCPNCAHTTLLFPTSTGGAEQMCKDSNLELLAQLPLEPALAKALDNGEDFFETNPDSTLAKSFLDLAEKVKAKLV", "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 (By similarity). Regulates cilium formation and structure (PubMed:23807208). SUBCELLULAR LOCATION: Cytoplasm Cell projection. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily."}
+{"protein": "MTPARRSALSLALLLVALASDLAAGLKCVCLLCDSSNFTCQTEGACWASVMLTNGKEQVSKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITQHLPTASPDAPRLGPTELTVVITVPVCLLSIAAMLTIWACQDRQCTYRKTKRHNVEEPLAEYSLVNAGKTLKDLIYDATASGSGSGPPLLVQRTIARTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGMVKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCDTCAIADLGLAVKHDSIMNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGLVEEYQLPYYDMVPSDPSIEEMRKVVCDQKLRPNLPNQWQSCEALRVMGRIMRECWYANGAARLTALRVKKTISQLCVKEDCKA", "text": "FUNCTION: Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily."}
+{"protein": "METGPAPLVAPPRRHGAPAAPSPPPRGSRAGSHLVVEPGPPVTTATSAPVELVAPGEARPACVPGSSQTSASTPTTATSSTVVMLTLEASPEAAKTQEFPAPAAETGAETSVALALGTDTQKTEEVRASPVPGPGTPTRTPSRMAPGALTAKPPLAPKPGTTVASGVTARGGVGQVAGGHEAATSASAGSVPEDPSGPVTGPPGTCEAPAPTPVAVVTVTPAPEPVENFQDLGSTSSLGPGISGPRGQAPDTLSYLDSVSLMSGTLESLPDDVSSMGSDSEINGMALRKTDKYGFLGGSQYSGSLESSIPVDVARQRELKWLEMFSNWDKWLSRRFQKVKLRCRKGIPSSLRAKAWQYLSNSKELLEQNPGKFEELERAAGDPKWLDVIEKDLHRQFPFHEMFAARGGHGQQDLYRILKAYTIYRPDEGYCQAQAPVAAVLLMHMPAEQAFWCLVQICDKYLPGYYSAGLEAIQLDGEIFFALLRRVSPLAHRHLRRQRIDPVLYMTEWFMCIFARTLPWASVLRVWDMFFCEGVKIIFRVALVLLRHTLGSVEKLRSCQGMYETMEQLRNLPQQCMQEDFLVHEVTNLPVTEAWIERENAAQLKKWRETRGELQYRPSRRLHGSRAIHEERRRQQPPLGPSSSLLSLPSLKSRGSRAVGGAPSPPPPVRRASAGPVPGAVVIAEGLHPSLPSPTGNSTPLGTSKEIRRQEKERQKQEKDREKERQRQEKERERQEKERQKWEKEQEKEQQKQEKERQKLEKKGQGRKLSLRRRADGPPASHDGGDRSAAEARQDAYF", "text": "FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A, RAB27A and RAB35. Does not act on RAB2A and RAB6A (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MAASITAITVENLEYPAVVTSPVTGKSYFLGGAGERGLTIEGNFIKFTAIGVYLEDIAVASLAAKWKGKSSEELLETLDFYRDIISGPFEKLIRGSKIRELSGPEYSRKVMENCVAHLKSVGTYGDAEAEAMQKFAEAFKPVNFPPGASVFYRQSPDGILGLSFSPDTSIPEKEAALIENKAVSSAVLETMIGEHAVSPDLKRCLAARLPALLNEGAFKIGN", "text": "FUNCTION: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin. SIMILARITY: Belongs to the chalcone isomerase family."}
+{"protein": "MRYSKLFLCAGLTLATLPCWGRAYTFDSTMLDTNSGESIDVSLFNQGLQLPGNYFVNVFVNGRKVDSGNIDFRLEKHNGKELLWPCLSSLQLTKYGIDIDKYPDLIKSGTEQCVDLLAIPHSDVQFYFNQQKLSLIVPPQALLPRFDGIMPMQLWDDGIPALFMNYNTNMQTRKFREGGKSLDSYYAQLQPGLNIGAWRFRSSTSWWKQQGWQRSYIYAERGLNTIKSRLTLGETYSDSSIFDSIPIKGIKIASDESMVPYYQWNFAPVVRGIARTQARVEVLRDGYTVSNELVPSGPFELANLPLGGGSGELKVIIHESDGTKQVFTVPYDTPAVALRKGYFEYSMMGGEYRPANDLTQTSYVGALGMKYGLPRNLTLYGGLQGSQNYHAAALGIGAMLGDFGAISTDVTQADSQKNKQKKESGQRWRVRYNKYLQSGTSLNIASEEYATEGFNKLADTLNTYCKPNTRNDCRFDYAKPKNKVQFNLSQSIPGSGTLNFSGYRKNYWRDSRSTTSFSVGYNHFFRNGMSLTLNLSKTQNINKYGEKTSELLSNIWLSFPLSRWLGNNSINSNYQMTSDSHGNTTHEVGVYGEAFDRQLYWDVRERFNEKGRKYTSNALNLNYRGTYGEISGNYSYDQTQSQLGIGVNGNMVITQYGITAGQKTGDTIALVQAPDISGASVGYWPGMKTDFRGYTNYGYLTPYRENKVEINPVTLPNDAEITNNIVSVIPTKGAVVLAKFNARIGGRLFLHLKRSDNKPVPFGSIVTIEGQSSSSGIVGDNSGVYLTGLPKKSKILVKWGRDKNQSCSSNVVLPEKTDISGAYRLSTTCILNN", "text": "FUNCTION: A probable role in capsular biogenesis. It is likely that the caf1A molecule binds F1 antigen subunits during the extracellular secretion process. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family."}
+{"protein": "MAAAVPDEAVARDVQRLLVQFQDEGGQLLGSPFDVPVDITPDRLQLVCNALLAQEDPLPLAFFVHDAEIVSSLGKTLESQAVETEKVLDIIYQPQAIFRVRAVTRCTSSLEGHSEAVISVAFSPTGKYLASGSGDTTVRFWDLSTETPHFTCKGHRHWVLSISWSPDGRKLASGCKNGQILLWDPSTGKQVGRTLAGHSKWITGLSWEPLHANPECRYVASSSKDGSVRIWDTTAGRCERILTGHTQSVTCLRWGGDGLLYSASQDRTIKVWRAHDGVLCRTLQGHGHWVNTMALSTDYALRTGAFEPAEASVNPQDLQGSLQELKERALSRYNLVRGQGPERLVSGSDDFTLFLWSPAEDKKPLTRMTGHQALINQVLFSPDSRIVASASFDKSIKLWDGRTGKYLASLRGHVAAVYQIAWSADSRLLVSGSSDSTLKVWDVKAQKLAMDLPGHADEVYAVDWSPDGQRVASGGKDKCLRIWRR", "text": "FUNCTION: Plays a role in regulating Notch activity. Plays a role in regulating the expression of CDKN1A and several members of the Wnt pathway, probably via its effects on Notch activity. Required during embryogenesis for inner mass cell survival (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NLE1/RSA4 family."}
+{"protein": "MRLTALLSMAAKVALPHGYRYGTNRPWTIAARRLNPPGKRRRKVFVEPIANEDWPVVRGDTVEVLSGKEKGKQGKVAQVIRARNWVILEGLNTHYRYVGRSGDYRGTYLASEAPLLLKDIALIDPTDRKPTEIQWRYTEEGERVRVSVRTGRIIPKPVFQRKDGIVPQQWKDGPKDTSPEDTLQKTYTPSLKTLEEEVMEKMNIQENRRPRKSYWY", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
+{"protein": "MELRYLRYFVAVAEARNFTRAAHDLGISQPPLSQQIQRLEREIGTPLLRRLTRGVELTEAGESFYVDACQILALSDAALEKTKGIARGMNGSLVPGITSSAAFHSQIFSLLYQFQQRYPAVALRQVEGNMATLMHALGEAELDIAFVRLPCESSKAFNLRIIAEEPMVIALHRSHPLSGESALSLAQLSDAVPVIFPPEVAPGLYEQVYDGCRRAGVDMSRARQSSQISSSISMVDAGFGFALVPQSMTCICLPNVTWHPLQDASLKTEIAIAWRRFERSRTVKRFLEMF", "text": "FUNCTION: Regulator of the budABC operon for 2,3-butanediol synthesis. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MDTVIELSKLLHDEEFKDNASCTSTPTLKTARIIESAVTGITLTASVPMIIIVITTMILYHRVAKHNATSFYVITLFASDFVLMWCVFFMTVNREQLFSFNRFFCQLVYFIYHAVCSYSISMLAIIATIRYKTLHRRKQTESKTYSTGRNIGILLLASSMCAIPTALFVQINGAKKTTGKCVVYLSSPKAYELFLAVKIVFSFIW", "text": "SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MTTDQPVISLRPGGGGGGPRGGRLFAPAFAVAASGSGDFLRPHGGGASGVSRIGDLHSESRERVRYSRDQLLDLRKITDVTEQILRLQQEIEAELNGDDQSWVRNDSNVQLQTQAQPQVQAQNRFTETDNRDWRARTEKPPAPAVQEEKSWDNIREVKEQYNASGRQQEQFNRQDQSSSQKAQVGPPPALIKADVPWSARRGNLSEKDRVLKTVKGILNKLTPEKFDLLKGQLLDSGITTADILKDVISLIFEKAVFEPTFCPMYAQLCSELNDNLPTFPSEEPGGKEITFKRVLLNNCQEAFEGADSLRVEIASLTGPDQEMEKRDKERIFKLRTLGNIRLIGELLKQKMVPEKIVHHIVKELLGSDKKACPDEEHVEAICQFFNTIGKQLDENPKSRRINDTYFVQIRELVANPQLTPRSKFMVRDLIDLRSNNWVPRRAEIKAKTISEIHTEAEKNLGLRPGATANMRNGRNAPGGPLSPGGFSVNRPGTGGMMPGMPGSRKMPGMPGLDNDNWEVQRSRSMPRGDPLRNQGPLINKVPSINKPSPINPRLLPQGTGALIGKSALLGTGGPPSRPSSLTASPTPLPAQTTASPKPSSATPASVPIPDKAASSAKVIPAGLQKKTASLLEEYFGIRILDEAQQCIEELQSPDYHPEIVKEAINLALDKGASFVDPLVKLLEHLYTKKTFKTEDLENGCLLYGSLLEDIGIDLPKAPTQFGEVVARLILSCGLRFEAAEGILKAMEDTFFRKAIFTSVTKTLGADPAGQAILSSHAAVVDACNSLSI", "text": "SIMILARITY: Belongs to the eukaryotic initiation factor 4G family."}
+{"protein": "MKFTVFASLFASAAAFAPAQQAARTSVATNMAFESELGAQAPLGFYDPLGLVADGDQEKFDRLRYVEIKHGRISMLAVAGYLAQEAGWRLGGDIALDGTKFADIPNGFAALSAIPQAGLIQIIAFIGFLETSVMKDITGGEFVGDFRNGYIDFGWDSFDQETKLRKRAIELNQGRAAQMGILALMVHEQLGVNILPGV", "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. Energy is transferred from the carotenoid and chlorophyll C (or B) to chlorophyll A and the photosynthetic reaction centers where it is used to synthesize ATP and reducing power. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. Note=FCPs are probably transported across the endoplasmic reticulum membranes that surround the plastid via a signal peptide, followed by translocation across the thylakoid membrane via a transit peptide. SIMILARITY: Belongs to the fucoxanthin chlorophyll protein family."}
+{"protein": "MAGQRLAAGFLQVPAVTRAYTAACVLTTAAVQLELLSPFQLYFNPHLVFRKFQVWRLITTFLFFGPLGFGFFFNMLFVFRYCRMLEEGSFRGRKADFVFMFLFGGVLMTLLGFLGSLFFLGQALMAMLVYVWSRRSPHVRVNFFGLLNFQAPFLPWALMGFSLLLGNSVVTDLLGILVGHIYYFLEDVFPNQPGGKRLLLTPSVLKLLLDDPQEDPDYLPLPEEQPEL", "text": "FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded glycoproteins. May be involved in 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. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the derlin family."}
+{"protein": "MEDDDSYVPSDLTAEERQELENIRRRKQELLADIQRLKEEIAEVANEIESLGSTEERKNMQRNKQVAMGRKKFNMDPKKGIQFLIENGLLKNTCEDIAQFLYKGEGLNKTAIGDYLGERDEFSIQVLHAFVELHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCQCNTGVFQSTDTCYVLSFAIIMLNTSLHNPNVKDKPTVERFIAMNRGINDGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDSKKPNCFELYIPDNKDQVIKACKTEADGRVVEGNHTVYRISAPTPEEKEDWIKCIKAAISRDPFYEMLAARKKKVSSTKRH", "text": "FUNCTION: Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization, through regulation of ARF6 activity. FUNCTION: Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6 (PubMed:18042453, PubMed:20080746). Promotes the activation of ARF factors through replacement of GDP with GTP (PubMed:18042453). Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization, through regulation of ARF6 activity (PubMed:20080746, PubMed:29420262). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cytoplasm, cytosol Cell junction, tight junction Cell junction, adherens junction Note=Colocalized with TJP1 during epithelial polarization. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cytoplasm, cytosol Cell junction, tight junction Cell junction, adherens junction Note=Colocalized with TJP1 during epithelial polarization (PubMed:20080746)."}
+{"protein": "MPGPDVKCFCCRDGKECACGGGECCITGKCCKEGDRTCCGKCSNAACKCADGCKCEGACACTMGNCTC", "text": "FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals. SIMILARITY: Belongs to the metallothionein superfamily. Type 4 family."}
+{"protein": "MAVNQNHTVDRRWAAIPHGESLLKKCSEVDLSFPQSPPGSNLFSGTKRGALFLTSYRVIFVTSRADNDPMFSFTMPFHLMNNCTVEQPIFGANYIKGTIQAAPDGGWEGSATFKIVFRKGGAIDFAQLMAKAASAAAQGVPLRVASFWMGPLGIYVITGDRNMYAPQAYQVAYGAPPAGYGASPVGYGVPSAGYGAPPAGYGAPPVGYVAPSPGYDVLPPGYGAVRYGSPPPLYVATPMGYGVPPPGYGPPPVRYGSPPPGYEAPTMEYGAQPPRYGTTPMGSGSPPPRYEAPPMGYGTPPSGRESIPPGSRATSVAQEAPPAGSEAGHPMSVAVQNPEFQASFPSTSSSQVHSPRSKM", "text": "FUNCTION: May play a role in meiotic resumption and pronuclear formation, mediated by a WW domain-signaling pathway during fertilization."}
+{"protein": "MSRTIVALILLGLAALAAADHHEGHGAEKEWAGKAWLGKWVSTDRSENWDAFVEALGLPLAAYGGNHKTVHKLWKEGDHYHHQIIIADKSYKQDIQFKLGEEGRTAHNGTEVTFKYTEVGDNLQNEVKIPSKNKTISDSYVVKGDELEKTYKINDVVAKRWYKKHAHEPSTA", "text": "FUNCTION: Secreted heat soluble protein acting as a molecular shield in water-deficient condition (PubMed:28306513). Tardigrade-specific intrinsically disordered proteins (TDPs) are essential for desiccation tolerance by forming non-crystalline amorphous solids upon desiccation, and this vitrified state mirrors their protective capabilities (PubMed:28306513). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Secretory-abundant heat soluble protein (SAHS) family."}
+{"protein": "MEFVMKQALGGATKDMGKMLGGDEEKDPDAAKKEEERQEALRQEEEERKAKYAKMEAEREAVRQGIRDKYGIKKKEEREAEAQAALEANSEGSLTRPKKAIPPGCGDAAEEEDESILDTVIKYLPGPLQDIFKK", "text": "FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Perikaryon Presynapse Note=Enriched at synaptic-releasing sites in mature neurons. SIMILARITY: Belongs to the complexin/synaphin family."}
+{"protein": "MKPIPSPEPPGQLRLTPRRKDKGEAEWERHRTRERLEATLAGLAELDCLRHRQQLLVQNVLSPGTHGQDAAPTGDSPRSDEQKLLEENISLLKKQLNCLRKRDAGLLSQLHELDKQINDLKIDSEKTEETDSRPSSGFYELSDGTSGSLSNSSNSVFSECLSSCHSSTCFCNPLETSLNLTDGQAKSAEDFLEWLDYRESQHETGTVRCSFSAPHSNSVEVTADVHPKYQCDLVSKNGNDVYRYPSPLHAVAVQSPMFLISVMGNIKAEEPEEEIGPNDNDDCIVPELDHLKDEDSFLHQSSLCSLPLSSGKKMDGYILSIIHKKAHPVRTNKPRTSVNADPGKGILRHGSICVKQTVGVSQSNAVNLKNSKQTCLHSAGMISVDNSTYPSLKPCSKESLSEQLESKRMPSISTYPSCNVNELQSQNNSRNTVKSVCQGLARGSVAMTSNVQKENVTPNAPANLPNASSSVCNGSPRESTQNSALLPQEIKVVPPVKRVSLKNTLLSYHESSSFEERPPLDFKSEGSSSQSLDEGMLVNAHYIPAQQHGVKLHKNTKNVKIVKSSTLKHRADVQYVLENGSQTLKEKSKVVGKKCRFPEDLDTNKKVKKSTPRVKKIVHPHFEPAAVGRNPVAVRSGIKSHGHPKDVVLAKPKHKRSDYRRWKSSAEISYEEALRRARRRVQREMMGVCAQVPFSHASPYAYIASDSEYSAECESLFHSTVVDTSEDEQSNYTTNCFGDSESSLSEVEFVGESTTSSDTDESGGLIWSQFVHTLPMQATATAELQTTAKAFIKIKASHNLKKKILRFRSGSLKLMTTV", "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/dsh and impedes the degradation of beta-catenin (ctnnb1-A and possibly ctnnb1-B), thereby enhancing the transcriptional activation of target genes of the Wnt signaling pathway. Also promotes catenin delta/ctnnd1 stability which in turn promotes zbtb33/kaiso sequestration and thus is involved in the regulation of zbtb33/kaiso-mediated transcriptional repression. May also bind to and directly stimulate the transcriptional activity of tcf7l1-A. Required for eye development and neural patterning. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the dapper family."}
+{"protein": "MGLAATRTKQRFGLDPRNTAWSNDTSRFGHQFLEKFGWKPGMGLGLSPMNSNTSHIKVSIKDDNVGLGAKLKRKDKKDEFDNGECAGLDVFQRILGRLNGKESKISEELDTQRKQKIIDGKWGIHFVKGEVLASTWDPKTHKLRNYSNAKKRKREGDDSEDEDDDDKEDKDSDKKKHKKHKKHKKDKKKDKKDKKEHKKHKKEEKRLKKEKRAEKTKETKKTSKLKSSESASNIPDAVNTRLSVRSKWIKQKRAALMDSKALNEIFMITND", "text": "FUNCTION: Involved in rRNA-processing at A0, A1 and A2 sites through its action in U18 and U24 snoRNA 3'-end final trimming. Negative regulator of telomerase through competition for binding to EST2 with TLC1. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the PINX1 family."}
+{"protein": "MPSGMFSIDNILAARPRCKESVLLPQNGPVVFSSLGESLYGPADYSGFYNRAVAPTSTLQGVNGSRLGFNNYYYGQLHVQTHLGPSCCGTVQALGTQQCSCVPPATAYDGAGSVLMPPVPHQMLPYMNVGTLSRTELQLLNQLHCRRKRRHRTIFTDEQLEALENLFQETKYPDVGTREQLARRVHLREEKVEVWFKNRRAKWRRQKRSSSEESENAQKWNKSSKNSAEKADEQVKSDLDSDS", "text": "FUNCTION: Plays a central role in executing Spemann's organizer phenomenon (the dorsal blastopore lip of the early Xenopus laevis gastrula can organize a complete secondary body axis when transplanted to another embryo). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily."}
+{"protein": "MQFSIVVMAALASLASAQSMDGIPTCALQCLAQAVVTGGCEASDQACQCGPAREAITAAATPCLLSACTDAADLATAASVGNGMCDKYKMGGDDAAPSPSVNTPAAAAPYPTAPAPNGTVPIGTAAAPSPTANTNETTTVATGSAPQNVAGGLAGIFGLVVAAAFAL", "text": "FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Secreted Host nucleus Host cell membrane. SIMILARITY: Belongs to the RBT5 family."}
+{"protein": "MASATSSRRQEDVEAGRRKLEQFRKRKAAEKAKKASQNTQPVDNSQQSVIDSDGAGASISNGPLKQSAESTSNETHTKDVYNLSFSNTAMDDGSKERSRQDDGQESVGKVDFSNSLELIGSSKDLTVNTRPEVVPYSNIDKQSSESFDRASTLRETASLFSGTSMQMDGFIHGSGLTSSRKDSLQPTTRMAGSFDEVAKNQQGSGELGGSIVQKPTLSSSYLFNSPDTSSRPSEPSDFSVNITSSSPLNSAKSEATVKRSRPSFLDSLNISRAPETQYQHPEIQADLVTSSGSQLSGSDGFGPSYISGRRDSNGPSSLTSGASDYPNPFEKFRSSLYPAANGVMPGFTDFSMPKQNDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASSGGKSTDLSKNSTSRKNVSTSTEGLAISDTTPESSNQETDSTTLLESDSSNTAIIPETRQLTLEGFSLSVPADQMRVIHNINTLIAELAIEKEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDNVSPEKQQPDTHVVQERTPIADEGDEVVERVLGWIMKMFPGGPSKRRTSKLL", "text": "FUNCTION: Is required for normal leaf, flower and seed development and controls cotyledon and leaf patterning by inhibiting premature differentiation. Regulates the expression of a subset of PcG target genes. Is required for the repression of the floral specific genes PI, SEP2, and SEP3, but also for the activation of FLC (PubMed:20647345). Involved in response to cold. Involved in the regulation of COR15A, COR15B, BAM3 and AMY3 transcripts, and ascorbate levels in response to prolonged chilling temperatures (PubMed:20674078). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=May shuttle between the nucleus and the cytoplasm."}
+{"protein": "MDPLGPAKTQWSWRCCLTALLFQLLVAVCFFSYLRVSRDDPTVYPNGSPFPDSTGTPAHSIPLILLWTWPFNKPIALPRCSEMVPGTADCNITADRKVYPQADAVIVHHREVMYNPSAQLPRSPRRQGQRWIWFNLESPSHCWHLKAMDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWRPNSARVRYYQSLQAHLKVDVYGRSHKPLPQGTMMETLSRYKFYLAFENSVHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLAQYLQELDKDHARYLSYFRWRETLQPRSCSWALDFCKACWKLQEESRYQTRSIAAWFT", "text": "FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein- or glycolipid-linked sialopolylactosamines chain or of a distal or internal lactosamine unit of a neutral glycoprotein- or glycolipid- linked polylactosamines chain through an alpha-1,3 glycosidic linkage and participates in surface expression of the sialyl Lewis X (sLe(x)), Lewis X (Le(x)) and non sialylated VIM2 determinants. Moreover transfers fucose to H-type 2 (Fucalpha1-2Galbeta1-4GlcNAc) chain acceptor substrates and participates in difucosylated sialyl Lewis x determinants. Also fucosylates a polylactosamine substrate having a 6 sulfate modification at the GlcNAc moiety and gives rise to sialyl and non-sialyl 6-sulfo lewis X. Does not have activity towards type 1 ((Galbeta1-3GlcNAc)) and H-type 1 chain (Fucalpha1-2Galbeta1-3GlcNAc) acceptors substrates. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein Golgi apparatus Secreted Note=Membrane-bound form in trans cisternae of Golgi. SIMILARITY: Belongs to the glycosyltransferase 10 family."}
+{"protein": "MAKSKTKHRLCSRESSVSSLLASCSLSDSNSSNSDGSYHYKDKLYRSASQALQAYIDDFDLSQMYPGTSTGKINIDEDFTNMSQFCNYIYKPNNAFENLDHKKHSNFISCRRQTINDIDSMSLTTDDLLRLPADGSFSYTYVGPSHRTNKKNKKCHGRLGSSDVEKNPNFQGPSTPVGDKIELLILKAKRNLEQCTEELPKSMKKDDSPCSLDKLEAERSWENIPVTFKSPIPVNSDDSPQQTSRAKSATGVLEDFLNNDNQSCTLSGGKHHGPVEALKQMLFNLQAVQERFNQNKATEPKEEIKQVSEDDFSKLQLKERQF", "text": "FUNCTION: Might play a role in cell proliferation. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR", "text": "FUNCTION: Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (PubMed:3002446). The full-length protein has collagenase activity, while both the 116 kDa and 98 kDa forms act on gelatin (PubMed:7961400). In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain is also synergistic with ColH, although their overall efficiency is decreased (PubMed:18374061, PubMed:22099748). Digestion of collagen requires Ca(2+) and is inhibited by EDTA (PubMed:9452493). The activator domain (residues 119- 388) and catalytic subdomain (330-601) open and close around substrate allowing digestion when the protein is closed (PubMed:23703618). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M9B family. Collagenase subfamily."}
+{"protein": "MGIVEEAHNLRVVGEGKRGVIVLAHGFGTDQSVWKHLVPHLVADYRVVLFDTMGAGPTNPDYFDFSRYATLEGYALDLLAILQELRVASCIYVGHSVSAVIGAIASISRPDLFSKLVLLSASPRYLNDVDYYGGFEQEDLDELFEAMGSNYKAWCSGFAPLCVGGDMESVAVQEFSRTLFNIRPDIALSVAQTIFQSDVRSLLPLVTVPCHIVQSTKDLAVPVVVSEYLHKHLGGDSIVEVMPSEGHLPQLSSPDIVIPVLLRHIQHDIAV", "text": "FUNCTION: May be involved in strigolactone signaling pathway (By similarity). Essential for plant responses to karrikins, a class of butenolide compounds, structurally similar to strigolactones, released from burning vegetation that stimulate seed germination and enhance seedling photomorphogenesis. Mediates a specific perception of karrikin. Required for the establishment of symbiosis with the arbuscular mycorrhizal fungi (AMF) Rhizophagus irregularis and Gigaspora rosea (PubMed:26680197). Karrikin binding induces a conformational change (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily."}
+{"protein": "MPYIYLIIAISTEVIGSAFLKSSEGFSKFIPSLGTIISFGICFYFLSKTMQHLPLNITYATWAGLGLVLTTVVSIIIFKEQINLITIVSIVLIIVGVVSLNIFGTSH", "text": "FUNCTION: Multidrug exporter. Is implicated for the resistance to bacteriocidal quaternary ammonium compounds and ethidium bromide. 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": "MSQYAPSPDFKRALDSSPEANTEDDKTEEDVPMPKNYLWLTIVSCFCPAYPINIVALVFSIMSLNSYNDGDYEGARRLGRNAKWVAIASIIIGLLIIGISCAVHFTRNA", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CD225/Dispanin family."}
+{"protein": "MQTQLTEEMRQNARALEADSILRACVHCGFCTATCPTYQLLGDELDGPRGRIYLIKQVLEGNEVTLKTQEHLDRCLTCRNCETTCPSGVRYHNLLDIGRDIVEQKVKRPLPERILREGLRQVVPRPAVFRALTQVGLVLRPFLPEQVRAKLPAETVKAKPRPPLRHKRRVLMLEGCAQPTLSPNTNAATARVLDRLGISVMPANEAGCCGAVDYHLNAQEKGLARARNNIDAWWPAIEAGAEAILQTASGCGAFVKEYGQMLKNDALYADKARQVSELAVDLVELLREEPLEKLAIRGDKKLAFHCPCTLQHAQKLNGEVEKVLLRLGFTLTDVPDSHLCCGSAGTYALTHPDLARQLRDNKMNALESGKPEMIVTANIGCQTHLASAGRTSVRHWIEIVEQALEKE", "text": "FUNCTION: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate (PubMed:4557653, PubMed:8606183). Is required for E.coli to grow on glycolate as a sole source of carbon (PubMed:8606183). Is also able to oxidize D-lactate ((R)-lactate) with a similar rate (PubMed:4557653). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown (PubMed:4557653). SUBCELLULAR LOCATION: Cell inner membrane Note=Glycolate oxidoreductase activity was shown to be firmly associated with the cytoplasmic membranes (PubMed:2689218). And the GlcF subunit itself could only be detected in the membrane fraction (PubMed:8606183)."}
+{"protein": "MIEYIIGALGLIIASVQDFRSREIEDYIWIFLAVFGVLFAIYSSITLLDYSILINSISGFVICFILGYMMFLSGIGGGDGKMLIGLGALVPKFQMPIYTSLGTLLNLNYVPTFPIMVFINGIFFMVFLPFVILFRNILNGARPKTGKEFILMFFGEKMKVNVAKEQKRLIMGQNDKINFFPAADDEDFSKYSNNEEIWVTPQIPLIIPITLSYLVTPIIGDRILDFLIPF", "text": "FUNCTION: Cleaves the N-terminal leader peptide from preflagellins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A24 family. Archaeal preflagellin peptidase subfamily."}
+{"protein": "MAYDAKTDWLPDDPINEDDVNRWEKGIQDAHKDLAVHKNDMNNPHNTTKAQIGLGNVDNVQQASKKEFEEHRNDLQRHITPVERENWNAKETIVGAQEKADKALSDAKYYVDTNYKNNNLTLITGDNAIQDARTGGEEYPLGLTLMDIGQGNTTGYPLGYGIVKNEKYNNYRFTQYFYGTGNESGTYYDSTGVWIRHWWSGSGWTPWQKISGFAHANIGTTGVQYLKKIDHTKIAFNRVIKDSHNAFDTKNNRFIAPNDGMYLIGASIYTLNYTSYINFHLKVYLNGKAYKTLHHVRGDFQEKDNGMNLGLNGNATVPMNKGDYVEIWCYCNYGGDETLKRAVDDKNGVFNFFDIQELGGRNYPRF", "text": "SIMILARITY: To B.subtilis XkdV."}
+{"protein": "MQHELQPDSLVDLKFIMADTGFGKTFIYDRIKSGDLPKAKVIHGRARWLYRDHCEFKNKLLSRANG", "text": "FUNCTION: Transcription inhibitory protein for the torCAD operon. Also acts as an excisionase and plays an essential role in the defective prophage CPS53 excision (By similarity). FUNCTION: Transcription inhibitory protein for the torCAD operon. Also acts as an excisionase and plays an essential role in the defective prophage CPS53 excision. FUNCTION: Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site. SIMILARITY: Belongs to the phage alpA excisionase family. SIMILARITY: Belongs to the phage AlpA excisionase family."}
+{"protein": "MNPNQKIITIGSVSLGLVCLDILLHIISITITVLGLHKNGKQRRCNETVIREDNETVRIEKVTQWHNTNVIEYIEKLEGDHFMNNTEPLCHAKGFALFSKDN", "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 (By similarity). SIMILARITY: Belongs to the glycosyl hydrolase 34 family."}
+{"protein": "MAPAALWVALVFELQLWATGHTVPAQVVLTPYKPEPGYECQISQEYYDRKAQMCCAKCPPGQYVKHFCNKTSDTVCADCEASMYTQVWNQFRTCLSCSSSCTTDQVEIRACTKQQNRVCACEAGRYCALKTHSGSCRQCMRLSKCGPGFGVASSRAPNGNVLCKACAPGTFSDTTSSTDVCRPHRICSILAIPGNASTDAVCAPESPTLSAIPRTLYVSQPEPTRSQPLDQEPGPSQTPSILTSLGSTPIIEQSTKGGISLPIGLIVGVTSLGLLMLGLVNCIILVQRKKKPSCLQRDAKVPHVPDEKSQDAVGLEQQHLLTTAPSSSSSSLESSASAGDRRAPPGGHPQARVMAEAQGFQEARASSRISDSSHGSHGTHVNVTCIVNVCSSSDHSSQCSSQASATVGDPDAKPSASPKDEQVPFSQEECPSQSPCETTETLQSHEKPLPLGVPDMGMKPSQAGWFDQIAVKVA", "text": "FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA", "text": "FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases. FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1B family."}
+{"protein": "MQRVTITLDDDLLETLDSLSQRRGYNNRSEAIRDILRSALAQEATQQHGTQGFAVLSYVYEHEKRDLASRIVATQHHHHDLSVATLHVHINHDDCLEIAVLKGDMGDVQHFADDVIAQRGVRHGHLQCLPKED", "text": "FUNCTION: Transcriptional repressor of the nikABCDE operon. Is active in the presence of excessive concentrations of intracellular nickel. SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family."}
+{"protein": "MSWLNTKKASCWRSSGRSATKSVTTNDAGTGNPAEQPARGAKQQPATETSRAGRDLRAAIVVGLSIGLVLIAVLVFVPRVWVAIVAVATLVATHEVVRRLREAGYLIPVIPLLIGGQAAVWLTWPFGAVGALAGFGGMVVVCMIWRLFMQDSVTRPTTGGAPSPGNYLSDVSATVFLAVWVPLFCSFGAMLVYPENGSGWVFCMMIAVIASDVGGYAVGVLFGKHPMVPTISPKKSWEGFAGSLVCGITATIITATFLVGKTPWIGALLGVLFVLTTALGDLVESQVKRDLGIKDMGRLLPGHGGLMDRLDGILPSAVAAWIVLTLLP", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDS family."}
+{"protein": "MPYSRDITKFITATEPEVGLPLLALQRSKSVIGIILLVISLLLIFIGIIILSVSSHTTAGSVLVVLSLILGGGGFFLIYKDNS", "text": "SUBCELLULAR LOCATION: Virion membrane. SIMILARITY: Belongs to the asfivirus EP84R family."}
+{"protein": "MKKNIFKFSVLTLAVLSLTACTLVPGQNLSTSNKDVIELPDNQYDLDKMVNIYPVTPGLIDQLRAKPIMSQANPELEQQIANYEYRIGIGDVLMVTVWDHPELTTPAGQYRSASDTGNWVNADGAIFYPYIGRLKVAGKTLTQVRNEITARLDSVIESPQVDVSVAAFRSQKAYVTGEVSKSGQQPITNIPLTIMDAINAAGGLTADADWRNVVLTQNGVKTKVNLYALMQRGDLRQNKLLHPGDILFIPRNDDLKVFVMGEVGKQSTLKMDRSGMTLAEALGNAEGMNQDVADATGIFVIRATQNKQNGKIANIYQLNAKDASAMILGTEFQLEPYDIVYVTTAPLARWNRVISLLVPTISGVHDLTETSRWIQTWPN", "text": "FUNCTION: May be involved in polysaccharide transport. FUNCTION: May be involved in polysaccharide transport. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BexD/CtrA/VexA family."}
+{"protein": "MAQSLTPSVETDSKTGPSKAISFQDYLDLSALDWARLRAVLAPTLYVDYTKIGKEKWDAMSADDFMAMVSNDDFLGDLCVKTQHLIGATYWERVSESKVIGHHQLRAAHQVYTSPDLKTVKLRGHSHATNEHYYVKSGGVWKFAGLKPEVRWNEYKFEEVFKGSYTQSEKQSLP", "text": "FUNCTION: Scytalone dehydratase-like protein; part of the Pks2 gene cluster that mediates the formation of infectious structures (appressoria), enabling these fungi to kill insects faster (PubMed:29958281). The product of the Pks2 gene cluster is different from the one of Pks1 and has still not been identified (PubMed:29958281). SIMILARITY: Belongs to the scytalone dehydratase family."}
+{"protein": "MKLITAIVKPFTLDDVKTSLEDAGVLGMTVSEIQGYGRQKGHTEVYRGAEYSVDFVPKVRIEVVVDDSIVDKVVDSIVRAARTGKIGDGKVWVSPVDTIVRVRTGERGHDAL", "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 (By similarity). SIMILARITY: Belongs to the P(II) protein family."}
+{"protein": "GKDINNNMEKAACATSSLVTQDDLQYHSLSKQQNESPQPLVGTGKKSPESLVKPDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPTPPDELLPQAIEFVNLSLEISVQDQIPPVCNDCQYYGSFKEAKIEEHLA", "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": "MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYSALDFEQEMATAAASSSLEKSYELPDGQVITIGNERFRCPETLFQPAFIGMESAGIHETTYNSIMKCDIDIRKDLYANTVLSGGTSMYPGIADRMQKEITALAPSSMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "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. Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family."}
+{"protein": "MLFIFKNAIREIEQYFANTLSIRRMETREAAERGGERVARYDELLQFIRFCITGENHPIRLPAAPMYLDWIATAELEHGLTPKVENRFLGVVAIDGLPAESWPGILNSLDLMPLTYRWSSRFIFLDAEEARQKLERTRKKWQQKVRPFFDQLFQTQSRSVDRDAMTMVAETEDAIAQASSQLVAYGYYTPVIILFDSDREALQEKAEAIRRLIQAEGFGARIETLNATEAYLGSLPGNWYCNIREPLINTSNLADLIPLNSVWSGSPVAPCPFYPPNSPSLMQVASGSTPFRLNLHVDDVGHTLIFGPTGSGKSTLLALIAAQFRRYDRSQIFAFDKGSALLPLTLAAGGDHYEIGGDNAEGRKALAFCPLSDLESDADRAWAAEWIEMLVALQGVTITPDHRNAMSRQVTLMASAPGRSLSDFVSGVQMREIKDALHHYTVDGPMGQLLDAEHDGLSLGAFQTFEIEQLMNMGERNLVPVLTYLFRRIEKLLDGSPSVIVLDEAWLMLGHPVFRAKIREWLKVLRKANCAVVLATQSISDAERSGIIDVLKESCPTKICLPNGAAREPGTREFYERIGFNERQIEIISNATPKREYYVVTPEGRRLFDMALGPVALSFVGASGKEDLNRIRTLHSEYDRDWPVHWLQMRGFHDAASLFNVE", "text": "SIMILARITY: Belongs to the TrbE/VirB4 family."}
+{"protein": "MAVNPLLTPTGQQTIPLIPSPFGPPTVDRDVLPSTVAPTDPRQFCVPSQFGSSVLPNTNMANVLSSRIYPGWGILPPESIKAVARRNEMIQRHHTARTEMEMYAIYQQRRMEKINPKGLAGLGIPFLYGSSVPAAPAAYHGRSMLPAGDLHFHRSTLRNLQGNPMLAATAPHFEESWGQRCRRLRKNTGNQKALDSDAESSKSQAEEKILGQTHAVPYEEDHYAKDPDIEAPSNQKSSETNEKPTTALANTCGELEPTHRKPWGSHTTTLKAKAWDDGKEEASEQIFATCDEKNGVCPPVPRPSLPGTHALVTIGGNLSLDEDIQKWTVDDVHSFIRSLPGCSDYAQVFKDHAIDGETLPLLTEEHLRGTMGLKLGPALKIQSQVSQHVGSMFYKKTLSFPIRQAFDQPADTSPLLDPNSWSDTMNIFCPQDTIIPKGIERGSMRN", "text": "FUNCTION: Involved in the regulation of gene expression in the retina. It functions as a negative regulator of CRX-controlled genes. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MTESFAQLFEESLKEIETRPGSIVRGVVVAIDKDVVLVDAGLKSESAIPAEQFKNAQGELEIQVGDEVDVALDAVEDGFGETLLSREKAKRHEAWITLEKAYEDAETVTGVINGKVKGGFTVELNGIRAFLPGSLVDVRPVRDTLHLEGKELEFKVIKLDQKRNNVVVSRRAVIESENSAERDQLLENLQEGMEVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRVKHPSEIVNVGDEITVKVLKFDRERTRVSLGLKQLGEDPWVAIAKRYPEGTKLTGRVTNLTDYGCFVEIEEGVEGLVHVSEMDWTNKNIHPSKVVNVGDVVEVMVLDIDEERRRISLGLKQCKANPWQQFAETHNKGDRVEGKIKSITDFGIFIGLDGGIDGLVHLSDISWNVAGEEAVREYKKGDEIAAVVLQVDAERERISLGVKQLAEDPFNNWVALNKKGAIVTGKVTAVDAKGATVELADGVEGYLRASEASRDRVEDATLVLSVGDEVEAKFTGVDRKNRAISLSVRAKDEADEKDAIATVNKQEDANFSNNAMAEAFKAAKGE", "text": "FUNCTION: It is not clear if it plays a role in trans-translation (a process which rescues stalled ribosomes). Evidence for its role; binds to tmRNA with very high affinity, is required for binding of tmRNA to 30S subunit (PubMed:11101533, PubMed:15340139). Thought to play a role only in translation of the tmRNA in vitro (PubMed:17392345). Evidence against its role; overexpression of whole protein or various S1 fragments inhibits translation, they have no effect on trans- translation, and an in vitro system with S1-less ribosomes performs trans-translation (PubMed:15340139, PubMed:17376482). In trans- translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). 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 thus targeted for degradation. FUNCTION: In case of infection by bacteriophage T4, plays a significant role in substrate choice by viral endoribonuclease RegB. FUNCTION: In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex; this subunit is required for RNA replication initiation activity during synthesis of (-) strand RNA from the (+) strand genomic RNA but not for (+) strand synthesis from the (-) strand (PubMed:6358207, PubMed:25122749). Binds an approximately 70 nucleotide RNA internal to the viral replicase gene (the M-site) (PubMed:25122749). Others have reported it is not involved in RNA replication initiation but rather in termination of RNA synthesis and is required for termination whether it is the (+) or (-) strand that is being synthesized (PubMed:23653193). 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). FUNCTION: Required for translation of most natural mRNAs except for leaderless mRNA (PubMed:9677288, PubMed:7003157, PubMed:12068815, PubMed:17376482, PubMed:24339747). Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated (PubMed:24339747). Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides (PubMed:22908248). Has a preference for polypyrimidine tracts (PubMed:778845). Negatively autoregulates its own translation (PubMed:2120211). FUNCTION: Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine-Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family."}
+{"protein": "MHLSEGVLHTPILLAGAVLAVAGIAVGLRRLESERLPLTALFAAAFFVAGTIHVPVGIGSVHLILNGMAGLFLGWAVFPAFLIALLLQVIFFSFGGFAVLGVNLCVMATPAVIAHYLFRSRLQPQMALKDRLLVGIGAGVIGVGGAGALASFVLMLDGGKSYLNLVWLLLVSHIPVFILDSIISVGVITLLGKMYPEVMNRTENFS", "text": "FUNCTION: May be involved in metal transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiM family."}
+{"protein": "MESRVLSRTTAIAALPKLFRPSREAASFGFATGVKTPVGLVKDGGSLTWGRQLRPVLLLEPVQTGPVCSRREKTAVQPCRAASGSSGEAKTGFLEKYPALVTGSFFFMWYFLNVIFNILNKKIYNYFPYPYFVSVIHLFVGVVYCLASWSVGLPKRAPMDSKLLKLLIPVAVCHAIGHVTSNVSFAAVAVSFTHTIKALEPFFNAAASQFVLGQSIPITLWLSLAPVVIGVSMASLTELSFNWLGFISAMISNVSFTYRSLYSKKAMTDMDSTNIYAYISIIALFVCLPPAIIVEGPQLMKHGFNDAIAKVGLTKFISDLFWVGMFYHLYNQLATNTLERVAPLTHAVGNVLKRVFVIGFSIIAFGNKISTQTAIGTSIAIAGVALYSLIKAKMEEEKRQMKST", "text": "FUNCTION: Mediates the export of fixed carbons from the chloroplasts into the cytosol in the form of triose phosphates. SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. Note=Located in zones of contact between the inner and outer membrane of the chloroplast. SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9) subfamily."}
+{"protein": "MAFDISVNASKTINALVYFSTQQNKLVIRNEVNDTHYTVEFDRDKVVDTFISYNRHNDTIEIRGVLPEETNIGCAVNTPVSMTYLYNKYSFKLILAEYIRHRNTISGNIYSALMTLDDLAIKQYGDIDLLFNEKLKVDSDSGLFDFVNFVKDMICCDSRIVVALSSLVSKHWELTNKKYRCMALANIYLIVFQYLSYLDYDTIYVSIYAGTLRA", "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": "MKFSSIILLTLLICSMSIFGNCQVETNKKCQGGSCASVCRRVIGVAAGKCINGRCVCYP", "text": "FUNCTION: Blocker of A-type voltage-gated potassium channels of cerebellar granular cells. May also inhibit Kv4/KCND when coexpressed with DPP6 or DPP10. The occlusion of the outer entry of the K(+) conducting pore is partially reversible and affects both open and closed channels. It shares the same target in rat brain than BmTX3 (AC Q8I0L5) and AmmTX3 (AC P60208). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 15 subfamily."}
+{"protein": "MDVSNKVSRALTQEIETLANISRESGSKLWRDIAERLASRRRGYASVNLSKIDKYAKDGDIIVVPGYVLGVGKISKKVTVGAYKFSKTAMEKLSNSGCAFMNISEIAKDNPKGTNVKIMR", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family."}
+{"protein": "MAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAAYFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQAAGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFVQGIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIKQQREARVQ", "text": "FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6- phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:3352745, PubMed:11004567). It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:3352745, PubMed:11004567). SUBCELLULAR LOCATION: Cytoplasm Secreted. SIMILARITY: Belongs to the GPI family."}
+{"protein": "MGPFCLGCSHRKCYSPIRNLISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCDSPVSLHHGVFKNKGNIHAEVCFLYWFHDKVLKVLSPREEFKITWYMSWSPCFECAEQIVRFLATHHYLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVTMVAGDSGLGKRLLTNFRYQDSKLQEILRRMDPLSEEEFYSQFYNQRVKHLCYYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMELSQVTITCYLTWSPCPNCAWRLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPKRPFWPWKGLEIISRRTQRRLRRIKESWGLQDLVNDFGNLQLGPPMS", "text": "FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase- dependent and -independent mechanisms. 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": "MLFARLVLLLVYLAPGSLAKPASTKKRTQWDQIAIDACAKELESHKFDTDVKGRHATLCTYEPALGSWLHCAKDVLDSRKKSKKIFEKTFSKINQYCHDYHKDEVVSNEEYYRIFANASLFIRPLDEVKENIRYPVTPNKASLDRWVWAYFGPLDNIDKGNVYGVTICLYWIGVLFIAAVYHFLNFSRLKQTVFKNKVSAFLRGHYVLPALVHNHAMSVGRWFFIGLVPTRLETLVLFGYVLLHGFLLSSYNFDHNELLSDRRSQVLIFLSDRAGILAFAHFPLIVLFGGKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAIGYTYHAYIENYWKYVKYSDLWTSGRHAMIIVGILVFFSFFFFRRHYYELFVITHIILAIGFFHACWKHCYKLGWGEWIMACALFWIADRILRLIKIAIFGMPWAKLKLCGESMIEVRISKSSKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDSLVEDGELVVVITVKNGLTKKLQEYLLESEGYTEMRVLAEGPYGQSTRTHLFESLLFIAGGAGVPGPLSMAIKAGRQVKSNDSHQMIKFVWSVRNLDLLEVYRKEIMVLKELNIDTKIYFTGERKDESNTEEGAIANMSTEGRLLTTSKSAEMITDFGRPNIDEIIEEAVSGAKSLLVTCCGSEGFVDKTRELTAKRVLEHGDKWIEYVEEFQNW", "text": "FUNCTION: Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)- salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ferric reductase (FRE) family."}
+{"protein": "MGSSNKKKKEKKKDFNKAKLKVGKAKAKAANFTDTSFKSKSIVVNQHTLAALDGVDLVGLFKQHLNQAINSKSDKLRQEALVQLTKDLSSKPIFNPVGVPNLLTKLLPLITDSVANVRTNFLKLLRALPPSDVAPHVEKILMYIRGGMTHLSTEIRSDTLSVLDWLIDVCPDETVSCPGGWLKTMNSFSSMLGWNPSVASTLSVKGWTSATKTSLNKVSKKNGEAQAKQITTLAKFLEAGFRPETPLPYDEQRYWDSIYRMPTTPNPFAYLNLWGAQRDEDGEMYPDRISRQQVFERKWRAAIKTGVMGAKQEGGVIGRAASVLDKVLRTAEEGGKKVVEEQKIEEVEEAEA", "text": "FUNCTION: Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IPI1/TEX10 family."}
+{"protein": "MEAIKQKRSLISLKESFIYPHEWNHEPCDNKFILECFKESVNLGIFQIDDKKSFSYINSCLSSCAYMWPLCNHSQSLMTGRFIQWSFLIDDYLDSLEIDDKKTDSTVLNVEKALINGTITNKNSKLEEYTVFFRNKLFEYCGRERLDAFNLLINELVICLWTLVPFSKIHSKEKDFYPSYQLYRCIRTINVGIIACCALNFILFKDLDVKLWLNPRFRKILNRASIQISIVNDAVSYAKEILNENAYCNTFYFLQKDSTKFSTFDQVCEYLFNEANTYIKDIITDEPLLLHEFEDVEDRKVVQSLLNHVHYLISGNFVWSIENNQRYQSNIYFINLLQSTGKSIGSSWSNIKTFFR", "text": "FUNCTION: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes (PubMed:30254228). TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene (PubMed:31621716). SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MSNEPESSDSKTKKDFSTAILERKKSPNRLVVDEAINDDNSVVSLHPTTMEKLQLFRGDTILIKGKKRKDTVCIALADETCEEPKIRMNKVVRSNLRVRLGDVISVHQCPDVKYGKRVHILPVDDTVEGVTGNLFDAYLKPYFLEAYRPVRKGDLFLVRGGMRSVEFKVIETDPAEYCVVAPDTEIFCEGEPVKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTNGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERISKDTHGYVGADLAALCTEAALQCIREKMDVIDLEDDSIDAEILNSMAVSNEHFHTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSAGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDSALLRPGRLDQLIYIPLPDEDSRLNIFKACLRKSPVAKDVDVTALAKYTQGFSGADITEICQRACKYAIRENIEKDIENERRRSQNPEAMEEDMVDDEVSEIRAAHFEESMKYARRSVSDADIRKYQAFAQTLQQSRGFGSEFRFDSTAGVGRTTGVAAADPFATSAAAADDDDLYS", "text": "FUNCTION: Probably functions in cell division and growth processes. Interacts with certain SNAREs as part of specialized membrane fusion events where vesicles from the same organelle fuse (homotypic fusion) (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, phragmoplast Note=Primarily localized to the nucleus and, during cytokinesis, to the phragmoplast, a site where membrane vesicles are targeted in the deposition of new cell wall materials. SIMILARITY: Belongs to the AAA ATPase family."}
+{"protein": "MGKLTLLLLAILVWLQYSLWFGKNGIHDYTRVNDDVAAQQATNAKLKARNDQLFAEIDDLNGGQEALEERARNELSMTRPGETFYRLVPDASKRAQSAGQNNR", "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. 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. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum. Localization requires FtsQ and FtsL, but not FtsW and FtsI. Localization of FtsB and FtsL is codependent. SIMILARITY: Belongs to the FtsB family."}
+{"protein": "MALFYVARYPGPDAAAAAGPEGAEAGAHGRARALLERLQSRARERQQQREPAQTEAAASTEPATRRRRRPRRRRRVNDAEPGSPEAPQGKRRKADGEDAGAESNEEAPGEPSAGSSEEAPGEPSAGSSEEAPGERSTSASAEAAPDGPALEEAAGPLVPGLVLGGFGKRKAPKVQPFLPRWLAEPNCVRRNVTEDLVPIEDIPDVHPDLQKQLRAHGISSYFPVQAAVIPALLESAACGFLVGRGGYRPSDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTADGYRCLADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADRMIDSMHQSWLPRVVAAAFQSEDPADPCALLQRRQAQAVTAASTCCPQMPLQKLLFSATLTQNPEKLQQLGLHQPRLFSTGLAHRGLEDTDGDGDSGKYAFPVGLTHHYVPCSLSSKPLVVLHLVLEMGFSRVLCFTNSRENSHRLFLLVQAFGGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTLLLKVQERRFLRMLTEAGAPELQRHELSSKLLQPLVPRYEEALSQLEESVKEERKQRAA", "text": "FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6 subfamily."}
+{"protein": "MEDAGQNPLDDEAEITEIPTLEAIKQNLKYLNSDLEKDLQRLDEANQILLRKIQKKEESIQSLERDIALSIGRVPERDDFNEILAQKETALKDLELESAKLEKKNKTLSKNVMELQKKISKGLKNIASDPETLKKKVTEFKVKLQKSTESCAQQEKEIAKMESDYQSVFQLCEDQAHYIKKYQEILREMEKEKEVMLLEKEISKAQNDSSQVVKPGSTLVETIQSNMEKNIIKKQKRKFWLRHFRYLFFMVMIVIRLLGYVFFHLQYVNPDFLVDTLPMLMSRSSLKWLRDILFPFLTLEVEDVLPH", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TMCO5 family."}
+{"protein": "MRLPLLSFVIFALFALVFASGVVELQSLNELENTIRASKKGALIEFYATWCGHCKSLAPVYEELGALFEDHNDVLIGKIDADTHSDVADKYHITGFPTLIWFPPDGSEPVQYSNARDVDSLTQFVSEKTGIKKRKIVLPSNVVELDSLNFDKVVMDDKKDVLVEFYADWCGYCKRLAPTYETLGKVFKNEPNVEIVKINADVFADIGRLHEVASFPTIKFFPKDDKDKPELYEGDRSLESLIEYINKKSGTQRSPDGTLLSTAGRIPTFDEFAAEFLDMSNAAKEVVLEKVKQLALEDSSRWTKYYKKVFEKILNDENWVHKEAKRLSKLLRQKSIALASADDFKTRLNILNSFLPGNH", "text": "FUNCTION: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. SIMILARITY: Belongs to the protein disulfide isomerase family."}
+{"protein": "MALSEDEAEAEVSVNTKVPSCGRWNSGKLLPSGLEPDQPLHLGVEGGPLWRAEADPGCISGVFLSRVHTASKEPVADRSKPPLRGPLPSASVGTGEVLHSMGSQMEEDRLPASQDLLPALQVFGTITVCSGQEADSEDFQATLDPSQVLGLSQQPHTSGLPLPPQWKSTVSPGAPQLSSRSISASSVGSSLQDHQEKAGPQRASFANVSSPELTVPQAAHSVVGAGPPLQGSAQPLTSGSDATGLGKRHLSFQAEYWACALPNSLPPSPNRHSALWDPNKEYEDLLDYTYPLRPGPQLPKQPESHVLTEPVLQDSGVDLDSLSVSPASTLKSPTNVSHNCSSAEVPTLPFSGARESCLKRWPLGIFQKQGGTSLSSWNQLASTPRAPGTEDASWENREAALRGTAEDCLPIGEDLRMGSPQLKTKEKEPPFPRQKRGRQHVSCPACVTPGWPSEEEVGSDEEYLALPTRLTQVSSLVSYSGARPSFVNLHTGAAEEHSSLQVSDSDKPASPTLDSSHRKHPSGTSFQGPVGQNPCFRHSIQPQDSRGKSSLMSNQTLGVSSKPLKTQPASKAMTDRRLFSELVAGETLPRTTDEQEKASLVQCVQTFCCRLEELICWLYNVTDVADLSAPPRTSLTGLKSSLQLYRQFKKDVDEHQSLTESVLEKGEILLQCLLDNTPVLKDVLERIAKQSGELESRADHLYDSILASLDMLAGCTLIPDNRPTAAEHPHEGL", "text": "FUNCTION: Involved in maintenance of centrosome cohesion, probably as part of a linker structure which prevents centrosome splitting. Required for localization of CDK5RAP2 to the centrosome during interphase. Contributes to CROCC/rootletin filament formation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to thin fibers protruding away from the proximal ends of the two centrioles. Dissociates from interphase centrosomes at the onset of mitosis."}
+{"protein": "MATPYVEDQSGKYIAATQRPDGTWRKPRRVKDGYTPQEEVPVYENKFVKFFKGKPDLPPGMSPGNAAQARQQQGIPGIAENEIAGLSKTAKRNMKRKEKRKQQGPDSNVELLTNAVETMTFAEDGDNVTPASNPAGATYDPSSAIAEKAKKIKNIKKKLRQVEELQQKLDSGEIKQATKEQQEKLGRAKALQGELLQLEEDS", "text": "FUNCTION: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon- exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus, nucleoplasm Note=Shuttles between the nucleus and the cytoplasm. Nuclear export is mediated by XPO1/CRM1. SIMILARITY: Belongs to the pym family."}
+{"protein": "MSGAGEHSDEESYGEESFEEDSESEVEVEEEEIEYIEPEESKPSDALLLGESDTQSESDVKEEFLSGNPHARRYLGARVVSYLSSSSDDESQVVITKTVAEVNQLSLRVDTPPEDETPSVRTLMPGSAHSRVKDEDEAEDEDDDEGDGENDNDNEDENDDEDAEVEEIEEEEEEIPGDEDDAQSDGSMGRQSADDSDEEEGTDVEVEQLEEDEPIVTAVCKKTVQKELPPPQKDIVSLVDASDNSSEHSVVTMCASGDETDNTLVKYPRLRKQQPLTAKDSQSLKEQEEPEEPEQPEENQTEEHMPTSQPDLARVRYLEQQMTQMSELIMKSFQINGGAPNSQAFEQLAMATEMLQQRSDRRGDTESEMSSMTETTMTSARSLGGGIPPLTMRMERSQEALLTTRSSKLPRPKCRCPSESDLIEHEQKLDMGHELPHDLAANFGLGEGYLVDECGQGDGLMRHPQQRKPMELNRRAVSGTPSTFNSDGCEYQINVSRSRCSNDKINYKNLGRKSFSFTNPQVREIERQNQILLRKMMTVKPTATIKASTSSIKINGPEKRQTPPAPRLSSAAVNRKKNQRQIDLDNDLLKRKLEAIGTRRPQFK", "text": "FUNCTION: Involved in assembly and/or maintenance of motile cilia. Required during spermatogenesis for axoneme elongation. Necessary for optimal function of the chordotonal (hearing) organs. SUBCELLULAR LOCATION: Cell projection, cilium Perikaryon Cytoplasm. SIMILARITY: Belongs to the CFAP97 family."}
+{"protein": "MSCGNEFVETLKKIGYPKADILNGEDFDWLFEDVEDESFLKWFCGNVNEQNVLSEKELEAFSDLQRSGKPILEGTALDEVLRTCKTFDLKTCKLDDKEIQILEDEVQTLQKLNNSKIQRRNKYQLMVSETSYRFLALNAKQEEATKKLKQKQGFLNSVNTKLSNELQGLTEEVNNLMIFFRNSNLSERTNPMVFLSQFPLGKYISQEEQSTAALTLYTKKQFFQGMHEVVESSNEDNFQLLDIQTPSICDNEEILRERRLEMARLQMACICVQKQIIYLKTSNLSMKSSIKWAEENLNRLTNEVIDKENLDAEISSLNSEILKLEEQITHIKDKVLPAVVKEYAQLLNMPVVKGDFELQIAKQDYYTARQELVLNELIKQKASFELVQLSYEIELRKHWDTYRQLESLVQQLSQRNTVLCQHLAVLSDIPASEQLTSRTPIDTKDHSTHRLYELLEGDNKKKELFITHEHLEEVAEKLKQDVSVIQDQLAVSTQEHFFFLSKLNNDVDMLCDALYRGGNQLLLCDQELKEHFHQVESQLNELHHLLTDILADVKTKRRILATNKLHQVER", "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": "MPFDLLAERKRWNAGYESIDTSSQKLTEVVTPITVTWENIEVKTRKKLFSKKQKQLLNRVSGIAKPGEMVALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGRTLIHQPTAELFFQFDKIIFLSMGKTAFMGTPHESVKFFADCGHPIPKLFNPPEWIQSKLSVIPNNETKSRETIGKIIEFYEKSIIHQKSIVEIRVIATTELPPYIENPGFFAETGALLKRACLDVIRSPAQMRMKLIQKVVMGLFIGSLYWQQPLDPRGVRNTNSALYFLIAELTFSTMFGIMTFMEHELPLIAREYHDGLFYVISYYISRFLSYLPLFTIDGALMIVISYWMIGLNSTWQQVAKSILISVLVEQSATSCGLFLACLFETTSLAIAFAVPASGLFALLSGLYGNTNNFPVYIRWMQWTSWCRYGFEGLVVNQWSQVDNPKWDPFYRELILKQFSFNKDNYQLDVIGLCSIVIFFYLAGYIALFIRIRLSR", "text": "FUNCTION: Required for efficient RNA interference (RNAi) of pop-1 indicating a role in the germline development. 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": "MWPPRFPPPRPGMSEETRQSKLAAAKKKLREYQQKNSPGVPAGAKKKKKIKNGHSPERTSASDCQSAENVPTDHTAPAPPSTAAATMFLGVVPSPDADLIQSHDAGNCSNLMEETKTFSSTESLRQLSQQLNGLVSESTSYINGEGLTSSNMKELESRYQELAVALDSSYVTNKQLSSTIEELKQQNQDTLDQLEKEKKDYQQKLAKEQGALREQLQVHIQTIGILVSEKAELQTALAHTQQAARQKAGESEDLASRLQSSRQRVGELERTLSTVSTQQKQADRYNKDLTKERDALKLELYKNGKSNEDLRQQNSELEEKLRVLVAEKAAAQLGAEELQKKLEMSELLLQQFSSQSEASGSNEQLQQAMEERAQLESHVGQLMESLKQLQVERDQYAENLKGESAMWQQRVQQMAEQVHALKEEKEQRESQVQELEASLAELRSQMEEPPPPEPPTGPSEAEERLQGEVEQLQKELEGLTGQLRAQVQDNESLSHLNREQEGRLLELEREAQHWSEQAEERKQILESMQSDRTTISRALSQNRELKEQLAELQNGFVRLTNENMEITSALQSEQHVKKELARKLGELQERLGELKETVELKSQEAQGLQEQRDQCLSHLQQYAAAYQQHLTAYEQLTSEKEALHKQLLLQTQLMDQLQHEEVQGKMAAEMARQELQEAQERLKASSQENQQLQAQLSLLVLPGEDMDQEEQDEEVPQPSLTIPEDLVSREAMVAFCNAAIARAEEEQARLRVQLREQKARCRSLAHLAAPVQSKLEKEAVVPRDMGDSVSEESNQALHVAMEKLQNRFLEVMQEKVELKERVEELEHCCIQLSGETDTIGEYIALYQNQRAVLKARHLEKEEYISRLAQDKEEMKVKLLELQELVLRLVNERNEWQGKFLAVSQNPADVPAPVPTGSQEFGAADQQGDLREVSLADDTEPAQGEAGVPAPQENPTAQQIMQLLREIQNPQERPGLGSNPCIPFFYRADENDEVKIMVI", "text": "FUNCTION: Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane (PubMed:9150144, PubMed:20197635). Required for normal protein transport from the endoplasmic reticulum to the Golgi apparatus and the cell membrane (By similarity). Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus (PubMed:10679020, PubMed:11035033, PubMed:18167358). Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (PubMed:9753325). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (By similarity). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (By similarity). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum-Golgi intermediate compartment membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton, spindle pole Note=Associates with the mitotic spindle during mitosis. SIMILARITY: Belongs to the GOLGA2 family."}
+{"protein": "MSVQTIQSESFIEEKRRITVLLDRDGRSVEEKVVNRDGVITIPNQSGHVQDRAVLFVPQLASRPDFIHISWKRNAEADITPIKSYIPYGFNIFTNSSGSIAKFIDTPVGKVYYSDTFEDNALSKWFPPEFVDQLLRYSEDNDLDITVTRGRVEVNRYYELTDDNLFPLNGTESVKTEAGIFQVDTEDDTDTSLSGLRCTWHTGSGALNKCQRTLFFYNQIYADKSSLSEVSLTLSEPVNLHPVVQIDLTSKRPIHNCEYYAYFNLPKYFFIDQFQSIPTLLFGEHDLELPEYKLSGFGSISLFTLQPGSINEVTLHSRYIKPTNDGSAFFEAAFTPQVFYACDTSIELTKRSPFYTGKIGYEHFFTDNTKFYYLNSTKMTINLPKLDSSDNLCIQLFTLGLVLFSVLYLIRKLF", "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": "MKFTATFLMMAIFVLMVEPGECGWGSFFKKAAHVGKHVGKAALTHYLGDKQELNKRAVDEDPNVIVFE", "text": "FUNCTION: Antimicrobial peptide with potent activity against Gram- positive and Gram-negative bacteria. Activity against E.coli and B.subtilis. Weaker activity against L.mucor, s.marcescens and P.aeruginosa. May play a role in innate host defense. SUBCELLULAR LOCATION: Secreted Membrane; Peripheral membrane protein Note=Associates with phospholipid membranes via its amphipathic helix and can insert into the lipid bilayer. SIMILARITY: Belongs to the pleurocidin family."}
+{"protein": "MMFRDQVGVLAGWFKGWNECEQTVALLSLLKRVSQTQARFLQLCLEHSLADCAELHVLEGEANSPGIINQWQQESKDKVISLLLTHLPLLKPGNLDAKAEYMKLLPKILAHSIEHNQHIEESRQLLSYALIHPATSLEDRSALAMWLNHLEDRTSTSFGSQNRGRSDSVDYGQTHYYHQRQNSDDKLNGWQNSRDSGICISASNWQDKSLGCENGHVPLYSSSSVPATINTIGTGASTILSGQAHHSPLKRSVSLTPPMNVPNQPLGHGWMSHEDLRARGPQCLPSDHAPLSPQSSVASSGSGGSEHLEDQTTARNTFQEEGSGMKDVPAWLKSLRLHKYAALFSQMTYEEMMALTECQLEAQNVTKGARHKIVISIQKLKERQNLLKSLERDIIEGGSLRTPLQELHQMILTPIKAYSSPSTTPEVRCREPSLMESPSPDCKDSAAAVTSATASASAGASGGLQPPQLSSCDGELAVAPLPEGDLPGQFTRVMGKVCTQLLVSRPDEENISSYLQLLDKCLVHEAFTETQKKRLLSWKQQVQKLFRSFPRKTLLDISGYRQQRNRGFGQSNSLPTASSVGSGMGRRNPRQYQIASRNVPSARLGLLGTSGFVSSNQRHTAANPTIMKQGRQNLWFANPGGSNSMPSRTHSSVQKTRSLPVHTSPQNMLMFQQPEFQLPVTEPDINNRLESLCLSMTEHALGDGVDRTSTI", "text": "FUNCTION: Acts as a translational repressor of SRE-containing messengers. SUBCELLULAR LOCATION: Cytoplasm Cell projection, dendrite Synapse, synaptosome Note=Colocalizes throughout the cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1. Also frequently colocalizes in cytoplasmic stress granule-like foci with ELAVL1, TIA1 and TIAL1. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (By similarity). Enriched in synaptoneurosomes. SIMILARITY: Belongs to the SMAUG family."}
+{"protein": "MSFSRALLWARLPAGRQAGHRAAICSALRPHFGPFPGVLGQVSVLATASSSASGGSKIPNTSLFVPLTVKPQGPSADGDVGAELTRPLDKNEVKKVLDKFYKRKEIQKLGADYGLDARLFHQAFISFRNYIMQSHSLDVDIHIVLNDICFGAAHADDLFPFFLRHAKQIFPVLDCKDDLRKISDLRIPPNWYPDARAMQRKIIFHSGPTNSGKTYHAIQKYFSAKSGVYCGPLKLLAHEIFEKSNAAGVPCDLVTGEERVTVQPNGKQASHVSCTVEMCSVTTPYEVAVIDEIQMIRDPARGWAWTRALLGLCAEEVHLCGEPAAIDLVMELMYTTGEEVEVRDYKRLTPISVLDHALESLDNLRPGDCIVCFSKNDIYSVSRQIEIRGLESAVIYGSLPPGTKLAQAKKFNDPNDPCKILVATDAIGMGLNLSIRRIIFYSLIKPSINEKGERELEPITTSQALQIAGRAGRFSSRFKEGEVTTMNHEDLSLLKEILKRPVDPIRAAGLHPTAEQIEMFAYHLPDATLSNLIDIFVDFSQVDGQYFVCNMDDFKFSAELIQHIPLSLRVRYVFCTAPINKKQPFVCSSLLQFARQYSRNEPLTFAWLRRYIKWPLLPPKNIKDLMDLEAVHDVLDLYLWLSYRFMDMFPDASLIRDLQKELDGIIQDGVHNITKLIKMSETHKLLNLEGFPSGSQSRLSGTLKSQARRTRGTKALGSKATEPPSPDAGELSLASRLVQQGLLTPDMLKQLEKEWMTQQTEHNKEKTESGTHPKGTRRKKKEPDSD", "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. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules (PubMed:29967381). 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. SUBCELLULAR LOCATION: Nucleus Mitochondrion matrix Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the helicase family."}
+{"protein": "MRLLGRYLRLGSPRLCSRVWPTLPPSCSPHSTAAAAQAQGALSFSDGGVFKLKSSWEVARGLLIFRMCSFPSLVKHSEKMLSVSRRLLGRRLFEWGMKGSVYGQFVAGETLPEIRVCVDRLRQLGIHPMLAVPIEEDLGQAKSGERWYEQNESIMLDCVDLSAAGGDRPMMQLKITALMSAELCKLLSVHLSHPSNGPQLCPRSIVSIMEGKESAFSFLSEGENSHLRNSVRRLSRIAKHATANRVRVLVDAEYTYMNPALSLVTMAMMSQCNQSEPWIWNTYQCYLKDSFSLLSLDLDTARSLGLCFGVKLVRGAYMDKERKLSKQKGYADPIQHDWEATNRSYQRSLDKMLDLIGQNGQRHNLIVASHNEESVLHAVTRMAELGIDKGSGSVSFGQLLGMCDHVSLTLGQAGYLVYKSLPYGSVDSVLPYLIRRAQENQSVLQGIRKERDLLRRELKRRLFNQR", "text": "FUNCTION: Dehydrogenase that converts trans-4-L-hydroxyproline to delta-1-pyrroline-3-hydroxy-5-carboxylate (Hyp) using a quinone 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. SIMILARITY: Belongs to the proline oxidase family."}
+{"protein": "MVMGLHLLFLVFILGLGLTPPTLAQNDLRYNRFLEEHYDPKTKNGNDRYCDKMMRLRNMISPCKAINTFIHGKKESIKAICGTENGVPYNGNKRKSKSAFQVTICKHRGGSPRPPCQYRATAGSRNVVVACENGLPVHLDESIFRP", "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": "MAESAPRGFGRGGRGGRGRGRGRRGAKRDEEKEWVPVTKLGRLVKAGKIKSIEEIYLYSLPIKEYQIVDYFLPRLNDEVMKVVPVQKQTRAGQRTRFKAFVVIGDSDGHVGLGIKCAKEVATAIRGAIIMGKLSIMPIRRGYWGTALGDPHTVPVKVSGKCGSVTVRLVPAPRGAGLVAAPVTKRFLQLAGIEDCYTQSRGSTKTLGNFVKAAFAAASLTYGILTPNLWAERPFGQTPIEEYADILMQTEKKY", "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. uS5 is important for 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. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS5 family."}
+{"protein": "MRLLISLPVLIVVLAMALEGPAPAQATPDLSSAFENLPEKLKEFGNTLEDKARAAIEHIKQKEILTKTRTWFSETFGKLKEKLKTTFD", "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). Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein (By similarity). Binds free fatty acids and reduces their intracellular esterification (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C1 family."}
+{"protein": "MIVDTFTNRGSTFFSKLSTVLFFLCAVITFQGVIQRREVELDTPVYVHYAKYRSARFYHAFRNVRQQYAQVKFNMDADLSELWDWNTKHVVVYLVASYSTEKHEKNQVVVWDKILSSPEESKMFMKDTLSNIQAHPFNEYSNQFEGKNATYTLHWTVSPKMGFLSWGAGPGSYEIPFHKIITQPK", "text": "FUNCTION: Essential 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. Essential for the SPC catalytic activity, possibly by stabilizing and positioning the active center of the complex close to the lumenal surface. Essential for viability. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the SPCS3 family."}
+{"protein": "MAKIKIGINGFGRIGRLVARVALQSDDVELVAVNDPFISTDYMTYMFKYDTVHGQWKHHEVKVKDSKTLLFGEKEVAVFGCRNPEEIPWGSVGAEYVVESTGVFTDQEKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEKEYKSDINIVSNASCTTNCLAPLAKVINDKFGIVEGLMTTVHAITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPVLNGKLTGMSFRVPTVDVSVVDLTVRLEKSATYDEIKAAVKAEAEGSLKGILGYVEEDLVSTDFQGDSRSSIFDAKAGIALNGNFVKLVSWYDNEWGYSTRVVDLIRHMNSTK", "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": "MESLKRWNEERGLWCEKGVQVLLTTIGAFSAFGLMTIAISTDYWLYTRALICNTTNLTAGDDGPPHRGGSGSSEKKDPGGLTHSGLWRICCLEGLKRGVCVKINHFPEDTDYDHDSAEYLLRVVRASSIFPILSAILLLLGGVCVAASRVYKSKRNIILGAGILFVAAGLSNIIGVIVYISANAGEPGPKRDEEKKNHYSYGWSFYFGGLSFILAEVIGVLAVNIYIERSREAHCQSRSDLLKAGGGAGGSGGSGPSAILRLPSYRFRYRRRSRSSSRGSSEASPSRDASPGGPGGPGFASTDISMYTLSRDPSKGSVAAGLASAGGGGSGAGVGAYGGAAGAAGGGGAGSERDRGSSAGFLTLHNAFPKEAASGVTVTVTGPPAAPAPAPAPPAPAAPAPGTLSKEAAASNTNTLNRKTTPV", "text": "FUNCTION: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit (PubMed:21127204). 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 and by mediating their resensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic density membrane. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily."}
+{"protein": "MGKLLRKPLNERIAPGVTLVQDINQANSPLSYVGFRLIEMEKGAIYQEELTELECCIVALTGKITVSEGNDIFPEIGTRANVFEKIPTDSVFISGGRAFQVKADTEKARVALCYSPANQDLPTTLIKASDNSIEQRGKYQNKRLVHNILPDVSEVASSLLVVEVYTNGGNFSSYPPHKHDRDNLPAESLLEESYYHEINPEQGFIFQRVYTDERTLDETMAVEHQNAVIVPEGYHPVGVPDGYDSYYLNVMAGPNRVWKFHNDPDHEWILERD", "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": "MARFVVVALLVLLSLSGLEAIQHAPKIQVYSRHPAENGKPNFLNCYVSGFHPSDIEVDLLKNGKKIEKVEHSDLSFSKDWSFYLLYYTEFTPNEKDEYACRVSHVTLSTPKTVKWDRNM", "text": "FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity). FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-2-microglobulin family."}
+{"protein": "MAAFIKDSFWGQIIYRLSGRKLFRHNDELPDYVVPEKYLLDPKEEVLNSSDKSQSSENKEQTEGDQATIQNEPASEHIIVTWDGDDDPENPYNWPFAWKAIAAMQIGFLTVSVYMASAIYTPGVEEIMNQFNINSTLATLPLTMFVIGYGIGPLFWSPLSENSRIGRTPLYIITLFIFFILQIPTALSNHIAGLSVLRVIAGFFAAPALSTGGASYGDFIAMHYYSIALGVWSIFAVAGPSIGPLIGAAVINRSHDADGWRWSFWFMAILSGVCFIVLSFSLPETYGKTLLRRKAERLRKLTGNNRIISEGELEDGHKTTSQVVSSLLWRPLEITMLEPVVFLIDIYIALVYSIMYLIFESVPIVYAGIHHFTLVEMGATYVSTIIGIIIGGAIYLPTVYYKFTKKLLAGQNVTPEVFLPPAIFGAICMPIGVFIFGWTSSPDINWFVPLIGMALFAVGAFIIFQTLFNYMAVSFKVEYLASVFSSNAFFRSVSAGAFPLFGRALYNNLSIDKFPVGWGSSILGFISLGMIAIPVFFYLNGPKLRARSKYAY", "text": "FUNCTION: Probable transporter. Confers resistance to cycloheximide. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family."}
+{"protein": "MPFFGNTFSPKKTPPRKSASLSNLHSLDRSTREVELGLEYGSPTMNLAGQSLKFENGQWIAETGVSGGVDRREVQRLRRRNQQLEEENNLLRLKVDILLDMLSESTAESHLMEKELDELRISRKRK", "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": "ESRRGGGGPAAAAAAAGDPRGPMPGFGAPQHTIPTNVNVMQPSRVADLGALAHSAGFRIEDLANFSTNNLFNLKPNTHAYTSDPLQFGNYGKSISPTDLATTAAAAAAVTAVDPQALLQQKGVQPNLVALRTHNNDNWGESSMADTSPRTDTSTDPDIDIDERNQMFEQGQLAAPTASDSSDKSRDKLDHKSLRRLAQNREAARKSRLRKKAYIQNLESSRLKLTQLEQELQRARQQGIFISSSGDQSQSASGNGAVAFDMEYARWLEEHNKHINELRAAANAHAGDDDLRKIVDSIMSQYDEFFRLKGVAAKADVFHVLSGMWKTPAERCFMWLGGFRSSELLKLLAGQLEPLTEQQLTGICNLQQSSQQAEDALSQGMEALQQSLAETLASGSLGPAGSSGNVASYMGQMAMAMGKLGTLENFLRQADNLRLQTLQQMQRILTTRQSARALLAISDYFSRLRALSSLWLARPRE", "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. Binds to the hexamer motif 5'-ACGTCA-3' of histone gene promoters. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
+{"protein": "MVLSIRSQIIIGVVSSILLTSTILAIAYILMWFNGHMTLTLTLTTIITSCLTLLICSIFINPLIQKIKQFNIKTKQFANGNYASNDKTFNSPKEIYELNQSFNKMASEITQQMNQIKSEQQEKTELIQNLAHDLKTPLASIISYSEGLRDGIITKDHEIKESYDILIKQANRLSTLFDDMTHIITLNTGKTYPPELIQLDQLLVSILQPYEQRIKHENRTLEVNFCSEIDAFYQYRTPLERILTNLLDNALKFSNVGSRIDINISENKDQDTIDIAISDEGIGIIPELQERIFERTFRVENSRNTKTGGSGLGLYIANELAQQNNAKISVSSDIDVGTTMTVTLHKLDITS", "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 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MTSKDKAVVSLPVSPWDAILKAAKDQLPSLDSDSSLSDCEEEEPFIFQRNQPVLIPDLTEELAEDPVGVDESGTWVTAGRSPSPEPLLVPGRLAIEPRSEWMVRSKDLAHQERRGPGWSCQSCVKSSPILLDTKEAPAWPEGRGSQSPPWSSQGEGATFPLEGKLKTEPSDTDFKNSAKRRALRRERRKMIEREILQKVTQAAQNPASGDQGQVAELGPRPKATSEQSWEGRPVLSLKQLEGWDLDYILQSLPGQQGSQGDSASRSAWWLADRCQDQGHSTGPSQDILLEQLALLCATQSRVRHPTWKVSADKLQDTEEQVARTRSASAESGFQTERVQKRAESRRLKTEPPTVFLDLRLTEPSDPQEHQSQESSEHSSSDSEEEEVGSAGSIPVASSWEQRYCTGKSQLLQQLRAFRKGAVPPQLSAKDGPGGQKDQAQEDTGGSQTQRKKHIKLWAEKQNALNLGDPLGTRLLPGMGQL", "text": "FUNCTION: In cyliated cells, dynein axonemal particle-specific protein required for deployment of ODA to the axoneme. Interacts with outer dynein arm (ODA) subunits. SUBCELLULAR LOCATION: Dynein axonemal particle."}
+{"protein": "MGIQGLLQFLKEASEPVHVKKYKGKTVAVDTYCWLHKGAFACAEKLAKGEPTDQYVQFCMKLVHMLLSFGVKPILVFDGCTLPSKKDVEKARREKRQTNLQKGKQLLREGKLAEARECFSRSVNITSSMAHEVIKAARSEGVDYIVAPYEADSQLAYLNKNDFAEAIITEDSDLLAFGCKKVLLKMDKFGNGLEIDQARFGMCRSLGDVFTEEKFRYMCILSGCDYLPSIHGIGLAKACKLLKVANNPDITKVIQKIGQYLKTNITVPEGYIEGFLRANNTFLYQLVFDPVERKLIPLNPYGNDVNPEELNYAGPNMGDSVALQIALGNMDINTRKQIDDYNPDIPQLSHHRSQSWDNKQLNRKTAHTDSIWYTKSEPCKTTKIEEIHSPRGLILPSKKHTVKRSYEDGVSDTDLISQYSFSKNKKARPDGDDPMQQVPASTMILQPLDDCANTKPKKPIHQPKTRNAFATFLQRQKQDCSSVSATGTRSRFFYKPADEKPHCTEKEQIVCNGSALDIAKETHELTEESSIKTEKEDSLSTISEVCKPNNQRISPLQNQRSCFTWSGSLDSESSPTPKQSPMLLSLQKFHRTTPYMQNEAENKPSWQSSCIKSDTVSQIDSNEKLLKKQDIEDTDSDEHASTPESPCQFTMKASPAHQSFFPEPKGSAPKSKVPGLLKSQSVVSGLRTKVKPRAPAKVSGLTNRSNTKATRNNENVPGLQATIGDLWKNFSYKK", "text": "FUNCTION: 5'->3' double-stranded DNA exonuclease which may also contain a cryptic 3'->5' double-stranded DNA exonuclease activity. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for DNA mismatch repair (MMR) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily."}
+{"protein": "MAPIKVGINGFGRIGRMVFQSMCEDNVLGTELDVVAVVDMSTDAEYFAYQMKFDTVHGRPKYTVEVAKSSPSAKKPDVLVVNGHRILCVKADRNPADLPWGKLGVDYVIESTGLFTDKAKAEGHVKGGAKKVVISAPASGGAKTIVMGVNQHEYNPATHHVVSNASCTTNCLAPIVHVLTKENFGIETGLMTTIHSYTATQKTVDGVSIKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAALKKASQTYMKGILGFTDEELVSSDFINDARSSIYDSKATLQNNLPGEKRFFKVVSWYDNEWGYSHRVVDLVRFMGAKDRSSSKL", "text": "SUBCELLULAR LOCATION: Glycosome. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
+{"protein": "MHVTQSSSAITPGQTAELYPGDIKSVLLTAEQIQARIAELGEQIGNDYRELSATTGQDLLMITVLKGAVLFVTDLARAIPVPTQFEFMAVSSYGSSTSSSGVVRILKDLDRDIHGRDVLIVEDVVDSGLTLSWLSRNLTSRNPRSLRVCTLLRKPDAVHANVEIAYVGFDIPNDFVVGYGLDYDERYRDLSYIGTLDPRVYQ", "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 hypoxanthine and guanine to form the corresponding ribonucleotides IMP (inosine 5'- monophosphate) and GMP (guanosine 5'-monophosphate), with the release of PPi. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
+{"protein": "MKSPTLLSLGYMFLVLLFFQQAWAQFPRECATIEALRNGVCCPDLSPLSGPGSDRCGLSSGRGRCEVVIADSRPHSHHYPHDGRDDREGWPTRSFNRTCHCNGNFSGHNCGTCRPGWGGAACDQRVLTVRRNLLDLSTEEKNRFVRALDMAKRTTHPQFVIATRRSEEILGPDGNTPQFENISIYNYFVWTHYYSVKKTFLGAGQESFGEVDFSHEGPAFLTWHRYHLLQLERDMQEMLQDPSFSLPYWNFATGKNTCDICTDDLMGSRSNFDSTLISPNSVFSQWRVVCESLEDYDTLGTLCNSTEGGPIKRNPAGNVARPMVQRLPKPQDVAQCLEVGSYDTPPFYSNSTNSFRNTVEGYSHPTGRYDPAVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRYNADISTYPLENAPIGHNRQYNMVPFWPPVTNIEMFVTAPDNLGYTYEVQWPSRSFSISEIVTIAVVAALSLVAVIFAGASCLIRARSNMDEANQPLLTDQYQHYIEEYEKIHNPNQSVV", "text": "FUNCTION: Plays a role in melanin biosynthesis. Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6- quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized. Also to a lower extent, capable of hydroxylating tyrosine and producing melanin. 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": "MAETTKIFESHLVKQALKDSVLKLNPVYMIKNPIMFVVEVGMLLALGLTIYPDLFHQESVSRLYVFSIFIILLLTLVFANFSEALAEGRGKAQANALRQTQTEMKARRIKQDGSYEMIDASDLKKGDIVRVETGEQIPNDGKVIKGLATVDESAITGESAPVIKESGGDFDNVIGGTSVASDWLEVEITSEPGHSFLDKMIGLVEGATRKKTPNEIALFTLLMTLTIIFLVVILTMYPLAKFLNFNLSIAMLIALAVCLIPTTIGGLLSAIGIAGMDRVTQFNILAKSGRSVETCGDVNVLILDKTGTITYGNRMADAFIPVKSSSFERLVKAAYESSIADDTPEGRSIVKLAYKQHIDLLQEVGEYIPFTAETRMSGVKFTTREVYKGAPNSMVKRVKEAGGHIPVDLDALVKGVSKKGGTPLVVLEDNEILGVIYLKDVIKDGLVERFRELREMGIETVMCTGDNELTAATIAKEAGVDRFVAECKPEDKINVIREEQAKGHIVAMTGDGTNDAPALAEANVGLAMNSGTMSAKEAANLIDLDSNPTKLMEVVLIGKQLLMTRGSLTTFSIANDIAKYFAILPAMFMAAMPAMNHLNIMHLHSPESAVLSALIFNALIIVLLIPIAMKGVKFKGASTQTILMKNMLVYGLGGMIVPFIGIKLIDLIIQLFV", "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": "MRNSDLAPLYRSAIGFDRLFNLLESGQNQSNGGYPPYNVELVDENNYRIAIAVAGFAEQELEITTQDNLLIVRGSHANEPAQRTYLYQGIAERNFERKFQLAEHIKIKGANLVNGLLYIDLERLVPESLKPRRIEIK", "text": "FUNCTION: Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MQAASSPVVIVTQPGVGSGPAPQNSNWQTGLCDCFSDCGVCLCGTFCFTCLACQVASDMNECCLCGTSVAMRTLYRTRYGIPGSICDDFMVTHCCPLCSLCQIKRDINRRRANRTF", "text": "SIMILARITY: Belongs to the cornifelin family."}
+{"protein": "MIIHVTYLSGYLAAIISSIIVSAILGLPLTPERPARHSWTPSAIFPTPVIALGLTAISIKLGVTGIYGADLGAVAGVLSAIMTAYFLEDIFPRPEDS", "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": "MLREMLGCCKVYISEARNKTALEAIERALKPFPPAAIVNKFEDAAYGRVGYTVVSSLANGSSSSLKNAVFAMVKTALDTINLELHCGSHPRLGVVDHICFHPLSQTSIEQVSSVANSLAMDIGSILRVPTYLYGAAEKEQCTLDSIRRKLGYFKANREGHEWAGGFDLEMVPLKPDAGPQEVSKAKGVVAVGACGWVSNYNVPVMSNDLKAVRRIARKTSERGGGLASVQTMALVHGEGVIEVACNLLNPSQVGGDEVQGLIERLGREEGLLVGKGYYTDYTPDQIVERYMDLLNNS", "text": "FUNCTION: Involved in the regulation of root growth (PubMed:35637390). May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap (PubMed:35637390). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. SIMILARITY: Belongs to the formiminotransferase family."}
+{"protein": "MGCNQSKSANDVRGNKVNHVNSKKKNNKREDTNDGEEIAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCKEKNGHSEKAIKVIKKSQFDKGRYSDDNKNIEKFHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKNSLLNIKIVDFGLSSFFSKDYKLRDRLGTAYYIAPEVLKKKYNEKCDVWSCGVIMYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISDEAKELIKLMLTYDYNKRCTAEEALNSRWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNVLRNFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRRAFNLFDTDKSGKITKEELANLFGLTSISEKTWNDVLGEADQNKDNMIDFDEFVSMMHKICDHKTF", "text": "FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK4 and CDPK5 (PubMed:32866196). In the mosquito midgut and during the last stage of male gamete exflagellation, may play a role in the rupture of the host erythrocyte membrane (PubMed:22817984). In the mosquito midgut, required for the differentiation of the zygote into the ookinete by promoting the translational activation of a subset of repressed mRNAs; these mRNAs are kept repressed in the zygote by the DOZI- or CITH-containing mRNP complexes (PubMed:22817984, PubMed:24265753). Dispensable during the asexual blood stage (PubMed:24265753). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Cell membrane; Lipid-anchor; Cytoplasmic side Parasitophorous vacuole membrane; Lipid-anchor Cytoplasm Cell projection, cilium, flagellum Host cell membrane; Lipid-anchor Note=Calcium and/or autophosphorylation does not affect membrane localization. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily."}
+{"protein": "MSTSVKHREFVGEPMGDKEVTCIAGIGPTYGTKLTDAGFDKAYVLFGQYLLLKKDEDLFIEWLKETAGVTANHAKTAFNCLNEWADQFM", "text": "FUNCTION: DNA-binding protein which plays an essential role in nuclear envelope formation (PubMed:17170708). Required for normal chromosome segregation during mitosis (PubMed:12684533). Associates with the nuclear lamina via its interaction with LEM domain containing proteins emr-1 and lem-2 (PubMed:12684533). In association with lem-3, plays a role in radiation-induced DNA damage repair response (PubMed:22383942). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BAF family."}
+{"protein": "MEDGHSKTVEQSLNFFGTDPERGLTLDQIKANQKKYGPNELPTEEGKSIWQLVLEQFDDLLVKILLLAAIISFVLALFEEHEETFTAFVEPLVILLILIANAVVGVWQERNAESAIEALKEYEPEMGKVVRQDKSGIQKVRAKEIVPGDLVEVSVGDKIPADIRITHIYSTTLRIDQSILTGESVSVIKHTDAIPDPRAVNQDKKNILFSGTNVAAGKARGVVIGTGLSTAIGKIRTEMSETEEIKTPLQQKLDEFGEQLSKVISVICVAVWAINIGHFNDPAHGGSWIKGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVSRMFIFDKVEGNDSSFLEFEMTGSTYEPIGEVFLNGQRIKAADYDTLQELSTICIMCNDSAIDYNEFKQAFEKVGEATETALIVLAEKLNSFSVNKSGLDRRSAAIACRGEIETKWKKEFTLEFSRDRKSMSSYCTPLKASRLGTGPKLFVKGAPEGVLERCTHARVGTTKVPLTSALKAKILALTGQYGTGRDTLRCLALAVADSPMKPDEMDLGDSTKFYQYEVNLTFVGVVGMLDPPRKEVFDSIVRCRAAGIRVIVITGDNKATAEAICRRIGVFAEDEDTTGKSYSGREFDDLSPTEQKAAVARSRLFSRVEPQHKSKIVEFLQSMNEISAMTGDGVNDAPALKKAEIGIAMGSGTAVAKSAAEMVLADDNFSSIVSAVEEGRAIYNNMKQFIRYLISSNIGEVVSIFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMEKPPRKADEGLISGWLFFRYMAIGFYVGAATVGAAAWWFVFSDEGPKLSYWQLTHHLSCLGGGDEFKGVDCKIFSDPHAMTMALSVLVTIEMLNAMNSLSENQSLITMPPWCNLWLIGSMALSFTLHFVILYVDVLSTVFQVTPLSAEEWITVMKFSIPVVLLDETLKFVARKIADGESPIYKMHGIVLMWAVFFGLLYAMML", "text": "FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Sarcoplasmic reticulum membrane; Multi-pass membrane protein Note=Colocalizes with SclA and SclB at the sarcoplasmic reticulum and the diad, a structure composed of a single t-tubule paired with a terminal cisterna of the sarcoplasmic reticulum. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family."}
+{"protein": "MISHIKKFINLYTIVFLLYILYSNENFFVKGQKLPPGFCPSPLIYRNTTDRQSDIDIGFQFLGETNCVQPCPSLILTENEWNKVFNMSLVAGTISMFALIFLIITYSPLVNNIKDYTRHTVGILFLFSGILIAMTTDGRQLWDIDLGFKKYCPEPGRFARQSDSKCLVTAIFFQFGCVTALLWWAAISVDLWITIKKIKISKKLFIIYTIAVNIVTIVLTFGPVGSKQYGYIDAAIGCWLMDLKYQVGYFWAPVGFCLCVGCVSIVLILKEIYNVSDAVKKKLLAKHLKPLMLIILMLTEFIYMFIFYSYTTSKKNHYHDIIEEYVVCLFVHAANPSVCKIGSTISPSAHFFFHLCIRLMGLEVLIFYGFTRQTRKIWMRSFWFNNSFIKRFLPSISSSNDSKSSNNKTSGRVTGGFGESSEQSNEPEQSIELSGIDDSKHDP", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family."}
+{"protein": "SDSLSFSFINFDKDERNVIAQGDARLVGNNILQLTRTDSNGSPVKSTVGRILYVAQVRLWEKSTNRVANFQSQFSFFLESPLSNPADGIAFFIAPPDTAIPSGSAGGLLGLFSPKTAQNESANQVLAVEFDTFYAQNSNTWDPNYPHIGIDVNSIKSAKTVRWERREGVTLNVLVTYNPSTRTIDVVATYPDGQRYDLSVVVDVTTVLPEWVRVGFSAASGEQFQTHNLESWSFTSTLLYTAQKENN", "text": "FUNCTION: Mannose-specific lectin. Also binds alpha-methyl-D-mannoside, D-glucose, N-acetyl-D-glucosamine and sucrose but not D-galactose, D- arabinose, D-fructose, D-xylose, lactose or glycoproteins fetiun, PSM and ovalbumin. Shows agglutinating activity towards rabbit erythrocytes. SIMILARITY: Belongs to the leguminous lectin family."}
+{"protein": "MARSRSRSPRWKQRSLSPQSRNFEYHEERHFHGHYDPEYRHDQQRPFTWRMDDEKHGQNKPRIPPRVNSYHRSYVNRSPSPNVKPVEKFDTYKPHQEYFPGRGDDDRRSQYMPTYTESAATYMEHERDCYIPTVQGRYTPDDHRGRGRGSGRGEKPPQMSLGKPPKMSLGKPPQMSLADSLRFKEKWHEDELRHQRVQEESYPQSPRRGSEDFGTRNPFQKRYPEDHDFRKYGYTSKRPTDAARYENRDPARIPKWKPEHSFLPFQEKKEEWSFGAQGHRYTEREYPERSSTTRVSYDYRHKHHKLSESEQDFPDGRFHKHLKEEDRKYSSIKAPANRELDCFSTTRGREIENEQINGPFYLYNKNSVSYNHTNIKDADLEPCNDKWKKKISKEDCRKENASFSKQFDTSPKPEEKCYSLIKKKPLSVKVDRNKTDTFRSTSRYSAERQISHDLVAIGKTSDNFHPVFQHLDSTQNPENKPTEEFAQEIITLIHKVKADSFVTPDITLNERFSRIKNRQDADFNQTKSNSDPEFHRRIDMSLDDFQNKYTMVYEPDKTLVKVIEPNDLRHDIERRRKERLQNEDENIFHMASPTERNHQSPSFSKVKTIRADGFQKPPHFIKSNFRKFIQKPYINYTMQRKDAIDQKIFRVEENHQNRRGSKGSFKNFLGGRFQPHYKSHLVQKSMYIQAKYQRLRFAGPRGFITNKFRNRFLRKKKEYPVLPRTNNLELLQVEPTLYEDLTEHLIFVRNWN", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the BCLAF1/THRAP3 family."}
+{"protein": "MDLQYFILAFSSIFSILNPFGAVPVFITLTESYPKKERDLVAKKTVIYALAILLAFALFGEWILKFFGISLDAFKIAGGILLLLISLDMVRGQQEAKIHRKEIEAAYEIDEIALMPLATPLLAGPGSITACMVAMAEASDIGDKFLVILAILLSLGITYLTLLSAESVLDRIGRLGIRILTRMMGLILTAIAVQMIVNGIRGALL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0056 (MarC) family."}
+{"protein": "MWTLVPVTFALRLLSTFVQPLGSLGSSLGPLFLWLWAAFWRAGGDRSRQQLQGKTEAGEPPRAQEDSHLPTTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLWLLKEAGMEKINFSGGEPFIHDRGEYLGKLVRFCKEELQLPSVSIVSNGSLIWERWFKSYGEYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRTWCRDYKVAFKINSVINRFNVEEDMTEHIKALNPVRWKVFQCLLIEGENVGEDALREAEQFVISDEEFEEFLDRHKDVSCLVPESNRQMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEKAIKFSGFDEKMFLKRGGKYVWSKADLKLDW", "text": "FUNCTION: Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism. In turn, ddhCTP acts as a chain terminator for the RNA- dependent RNA polymerases from multiple viruses and directly inhibits viral replication. Therefore, inhibits a wide range of DNA and RNA viruses (PubMed:32719955, PubMed:31517388). Promotes also TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus Endoplasmic reticulum Lipid droplet Mitochondrion Mitochondrion inner membrane Mitochondrion outer membrane. SIMILARITY: Belongs to the radical SAM superfamily. RSAD2 family."}
+{"protein": "MARDYDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGEKVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYDVTSAESFVNVKRWLHEINQNCDDVCRILVGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVEEMFNCITELVLRAKKDNLAKQQQQQQNDVVKLTKNSKRKKRCC", "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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes. 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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes (By similarity). 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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Membrane, clathrin-coated pit Cytoplasmic vesicle, clathrin-coated vesicle Endosome Melanosome Note=Present on sorting endosomes and recycling endosome tubules (PubMed:16950109). Tends to be enriched in PIP2-positive cell membrane domains (PubMed:16950109). During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis (PubMed:16950109). Identified in stage I to stage IV melanosomes (PubMed:17081065). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Membrane, clathrin-coated pit Cytoplasmic vesicle, clathrin-coated vesicle Endosome Melanosome Note=Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Membrane, clathrin-coated pit Cytoplasmic vesicle, clathrin-coated vesicle Endosome Melanosome Note=Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MVSHSELRKLFCSADAVCFDVDSTVIREEGIDELAKFCGVEAAVSEMTRRAMGGALPFKDALTQRLALIQPSRDQVQRLLAEHPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVAAKLNIPTTNVFANRLKFYFNGEYAGFDEMQPTAESGGKGKVIRFLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE", "text": "FUNCTION: Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L- serine to L-serine. L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator. May also act on O-phospho-D-serine. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family."}
+{"protein": "MRADLITIQQTLTPEAATVLNQSIAEATRRNHGHTTPLHVAATLLSSSSGYLRQACIKSHPNSSHPLQCRALELCFSVALERLPTTSTTTTTTSSSSSSSPSQTQEPLLSNALTAALKRAQAHQRRGCPEQQQQPLLAVKVELEQLIISILDDPSVSRVMREASFSSPAVKSAIEQSLIGNSVSNSRQTGSPGIINPSAIGFGYRSVPAPVNRNLYLNPRLQQPGVGMQSGMMIQRTDEAKRVIEIMIRTRKRNPVLVGDSEPHILVKEILEKIENGEFSDGALRNFQVIRLEKELVSQLATRLGEISGLVETRIGGGGVVLDLGDLKWLVEHPAANGGAVVEMRKLLERYKGRLCFIGTATCETYLRCQVYYPSMENDWDLQAIPIAAKSSLPAIFPRLGSNNNNNAMLLSNNIISIESISPTRSFQIPMSKMSCCSRCLQSYENDVAKVEKDLTGDNRSVLPQWLQNAKANDDGDKKLTKDQQIVELQKKWNDLCLRLHPNQSVSERIAPSTLSMMKINTRSDITPPGSPVGTDLVLGRPNRGLSSPEKKTREARFGKLGDSFDIDLFKKLLKGLAKSVWWQHDAASSVAAAITECKHGNGKSKGDIWLMFTGPDRAGKSKMASALSDLVSGSQPITISLGSSSRMDDGLNIRGKTALDRFAEAVRRNPFAVIVLEDIDEADILLRNNVKIAIERGRICDSYGREVSLGNVIIILTANSSLGSAKNVASIDETRLESLVNKGWELRLSVCNSSKTRKRKPNWLYSDNDQTKQRKEICFDLNEAAEFDSSSDVTVEHDQEDNGNLVHKLVGLVDDAILFRPVDFDSIKSKTAESLKKRFSNGLADGLTVEIEDDALERIAGAIWLSKISLEEWLEEAMGSSLNSVKSRVSSSEDSVIRIELEDDLNDRISGGYLPSSIRTVVV", "text": "FUNCTION: Probable component of a transcriptional corepressor complex that acts specifically in the karrikin pathway (PubMed:26754282). Controls seedling growth redundantly with SMAX1, but is not involved in leaf morphology, shoot branching or germination control (PubMed:26754282). SIMILARITY: Belongs to the ClpA/ClpB family."}
+{"protein": "MSFQLAPYLAKSVPGIGILGGIVGGAAALAKNARLLKDKQITGTEAAIDTGKEAAGAGLATAFSAVAATAVGGGLVVSLGAALIAGVAAKYAWDLGVDFIEKELRHGKSAEATASDEDILREELA", "text": "FUNCTION: Plays a role in regulating magnetite crystal size (PubMed:17965152). The lumenal domain may bind the magnetite crystals, affecting crystal size and shape (By similarity). SUBCELLULAR LOCATION: Magnetosome membrane; Multi-pass membrane protein Note=Purified magnetosomes remain attached to each other (PubMed:11571158). Resistant to trypsin digestion in isolated magnetosomes (PubMed:14766587). Localizes as a filament-like structure in a straight line running through the center of the cell, in a position that corresponds to magnetosomes (PubMed:18539817, PubMed:22007638). SIMILARITY: Belongs to the magnetosome MamC family."}
+{"protein": "MKGLVRLLTVFSLLLGCWGWLGTTQIAQAGSLQSFLVPQVPVLAIESQNRADAKLATEFGKKIDLNNTNVRAFQQYPGLYPTLARKIIQNAPYSKVEDVLDLPGLSDGQKQLLQSNFDKFTVTELEPAFNEGDDRFNNGIYR", "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": "MKIKVTFQERIIEHNFETEITNLQQVTQKLCSLFLITNYYSYSLFLSSGQLVDNINLIDEGSEIIIKHLNRLGTISIGSGYSNSVVGTTNNNAPSSPSSSININGQQIQQQIQQQIQQQQQQQQQQQQQVQLSPDTLINNLLNNLKDNTFKKKAFFDLKDLKEEILIKKFVEKNGIEVIVCQLKELTGNTLSYALSALQTIMSYEFTITSMTSTDTASLITQLLPLTENTSNPSISKTSLSLLCLFLNQSNNLNFKQFSSTLVLEYNEKTKRNYNHTLVQLLSSSNTVDVQLNALTLINIIIGKTMSTTIPGLENGSVTGGENGFNKLLKELDEYEINQKLKKLVESIIVAPELKRQLYIYQRHRFQVITNRKNVTFNKESSEHDALLMKLWSLTYPGVKLESRVSEQWKQMGFQGTDPCTDFRAMGIWGLDNLIYFAQNYNEKFRKIVNSQIDRKEREYPTATAGIVLTFELYNSIFKMGTPNLNPYNSTTSNTTSNTTSTTNIDDLPFFPLFFSHPHAFEEVYCTTFQILDSTWDDMNGTYMHFQKIMSSVKNLIITALESKPTTLEAFDWKCQKNTKNSNGGTNSNQNNSSSNLLLSNFANGSSLLSLLNDLSSSSRDDMKKLLTGVNYQVLDLIKSQKISYFQEGFQFKLHKQLKTKQSLPLNWIFIRLFNNNNNNNNNNENCSYEIQYCFLSTELNQPPLPNQSIPTNYNTIKISDLFFNGESTNSNNKKKDKSLSYFNISIKDEQIQSLIQNQLPLSNLNNSSNSLQLDSSTSMNSIKDSIINISSSNNNIKDNLTNNNTNTNTNNTNNNTSNGNGNSNSVSMSSININNSGQLSPNTTSPILIPQQQQQQPQSSSLSVQHQQSSTPTPSSPVLLSSPSLQSSSSSSSSSSNPNLFTIDLISSNRDDVSNFWDSIKLLSGQEIKSQEGLDDYHSLLSINTSVKLLDLDGIDIPKETPQIPILPDNFDFRTV", "text": "FUNCTION: Functions as a negative regulator of actin polymerization. Modulates actin/myosin II at cortex actinomyosins to prevent excessive F-actin polymerization around the cell periphery, thereby maintaining proper cell shape during phagocytosis and chemotaxis."}
+{"protein": "MLWEETGAAPAPARASDLPYRISSDHLKKEEKMTMMAHQYPSWIFINEKTFITREQLNSLLKTYNIFYENQKNLHILYGETEDGKLIVEGMLDIFWGVKRPIQLKIQDEKPFSSFTSMKSSDVFSSKGMTRWGEFDDLYRISELDRTQIPMSEKRNSQEDYLSYHSNTLKPHAKDEPDSPVLYRTMSEAALVRKRMKPLMMDRKERQKNRASINGHFYNHETSIFIPAFESETKVRVNSNMRTEEVIKQLLQKFKIENSPQDFALHIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKDAEEISSDVAQYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCLQNKLVIKTETTV", "text": "FUNCTION: Involved in the induction of apoptosis, through both caspase- dependent and caspase-independent pathways. May act as a Ras effector protein. May suppress the serum-induced basal levels of NF-kappa-B (By similarity)."}
+{"protein": "MPGRWSAETRLALVRRARRMNRALAQAFPHVYCELDFTTPLELAVATILSAQSTDKRVNLTTPALFARYRTARDYAQADRTELESLIRPTGFYRNKAASLIGLGQALVERFGGEVPATMDKLVTLPGVGRKTANVILGNAFGIPGITVDTHFGRLVRRWRWTTAEDPVKVEQAVGELIERKEWTLLSHRVIFHGRRVCHARRPACGVCVLAKDCPSFGLGPTEPLLAAPLVQGPETDHLLALAGL", "text": "FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. Has a preference for oxidized pyrimidines, such as thymine glycol (prefers 5S isomers) 5,6-dihydrouracil:G, 5-hydroxyuracil:G, 5- hydroxycytosine:G and urea:A. Cleaves ssDNA containing an AP site. SIMILARITY: Belongs to the Nth/MutY family."}
+{"protein": "MAERTYRINIAAELAGVRVELIRAWERRYGVLTPRRTPAGYRAYTDRDVAVLKQLKRLTDEGVAISEAAKLLPQLMEGLEAEVAGRGASQDARPHAETWRESMLAATQAYDQPRVSDVLDEVLAALPPLKAFDEVLAPLLCDVGERWESGTLTVAQEHLVSQMVRARLVSLLHAAPLGRHRHGVLACFPEEEHEMGLLGAALRLRHLGVRVTLLGQRVPAEDLGRAVLALRPDFVGLSTVASRSAEDFEDTLTRLRQALPRGLPVWVGGAAARSHQAVCERLAVHVFQGEEDWDRLAGT", "text": "FUNCTION: Negative regulator of the carB operon in the dark. Binds specifically to the CarA operator, in the region around the carB promoter, which blocks access to the RNA polymerase. SIMILARITY: Belongs to the CarA/CarH B12-binding photoregulator family."}
+{"protein": "MEFPDHSRHLLQCLSEQRHQGFLCDSTVLVGDAQFRAHRAVLASCSMYFHLFYKDQLDKRDIVHLNSDIVTAPAFALLLEFMYEGKLQFKSLPVEDVLAAASYLHMYDIVKVCKKKLKQKATAEADSTKREEDTSSCSDKVESFSEGGSTGRPATADLLQSDDEDMENKRDSPQEPGSMWMRLPSDRTTSPTTSPREAETHGPDAGKSPAGSPSSSSGSLSRRSAASRRVSADTDCVLDLSVKSSLGGGPGENIAGNPYFCSSVTPDSLQSALVQVKVEKDTGSDDDELVSGDYEMEHSGVKEPPSTNGTHLSLVAQRRLGLEAHLSALREASLASELERDDKGGDDDTDVLGGDSDRVQEAAGVESSLLPYVSSMLGAPHTQIFMCPLCNKVFPSPHILQIHLSTHFREQEGVRAKPAGDVNVPTCSICGKTFSCMYTLKRHERTHSGEKPYTCTTCGKSFQYSHNLSRHAVVHTREKPHACKWCERRFTQSGDLYRHIRKFHCELVNSLSVKSEALNLPTVRDWALEDSSQELWK", "text": "FUNCTION: Transcriptional repressor that plays a role in various developmental processes. 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 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family. ZBTB18 subfamily."}
+{"protein": "MSSNNQSSSVAQAATSARTVSAGSAEATDANSTASNNNNNSSSTAAAGNNSDNSSPTTGTGTGASTGKLHGGHTAVNTKERVVDSVPFPPSHKLTLAEVFDQRTGKPNHELLKQHFILEGRIEEAPALKIIQDGAALLRQEKTMIDIEAPVTVCGDIHGQFYDLMKLFEVGGSPASTKYLFLGDYVDRGYFSIECVLYLWSLKITYPQTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEIHELEDIRRLDRFKEPPAFGPMCDLLWSDPLEDFGNEKNSDFYTHNSVRGCSYFYSYAACCDFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELMTEESEEPLSDDEAALRKEVIRNKIRAIGKMARVFSVLREESESVLQLKGLTPTGALPLGALSGGKQSLKNAMQGFSPNHKITSFAEAKGLDAVNERMPPRRDQPPTPSEDPNQHSQQGGKNGAGHG", "text": "FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily."}
+{"protein": "MKAEKTSLAVLTAQLTSPDGWQQLLPKGEFRSRDGSPTDVAHWFIDGTIAQNLIHKARQLNQDLLVDYDHETILKAKKGIDAGNVVAAGWFNADEIQWFDDETRQGLYIKPRWTPKAYQQIKDGEFAFLSAVFPYDENGTPLELRMAALTNDPGITGMQRLAVLSATLNPQENVKMPESLRKLLAKLGVEIAEGVELTEEQANTALNALETLQTDKTKADEQVATLSAKNTEVDLSQYVPKATYDAVMSQVAVLSAKTDDVEIDNHISKARNEGRAVEAEVEYLKQFGKQQGVAALSAMLEKRPQIAVLSAQQTQTTKVEKPVEKGTAVLSAADKEAAKLLGISEQDYAKELEAK", "text": "FUNCTION: Potential protease involved in virion morphogenesis. SIMILARITY: Belongs to the peptidase U35 family."}
+{"protein": "KFCEKPSGTWSGVCGNSGACKDQCIRLEGAKHGSCNYKPPAHRCICYYEC", "text": "FUNCTION: Antimicrobial peptide active against fungi, Gram-positive and Gram-negative bacteria. Inhibits growth of hyphae in the fungi A.niger (IC(50)=3.5 ug/ml), B.sorokiniana (IC(50)=3.0 ug/ml), F.oxysporum (IC(50)=9.5 ug/ml), F.graminearum (IC(50)=6.9 ug/ml), F.culmorum (IC(50)=6.9 ug/ml) and B.cinerea (IC(50)=27.4 ug/ml). Has no effect on spore germination. Destroys spores in germinated conidia by disruption of cell walls and membranes in A.niger and B.sorokiniana. Causes vacuolization of germinated macro- and microconidia in F.oxysporum, F.graminearum and F.culmorum. Strongly inhibits growth of P.infestans on potato tubers above concentrations of 13.6 ug/ml. Inhibits growth of Gram-positive bacteria C.michiganensis and B.subtilis and of Gram- negative bacteria P.syringae, E.carotovora and E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family."}
+{"protein": "MERRELCASLLAGGAAGMSVDLILFPLDTIKTRLQSPLGFSKSGGFRGIYAGVPSTAVGSFPNAAAFFVTYESAKRFLGSDSSYLSPIIHMAAAFLGELVACLIRVPSEVIKQRAQVSPSSTTYQMLSVTLREEGIKGLYRGYKSTVLREIPFSLVQFPLWEFLKNLWSWKQGRAVDCWQSAVCGAFAGGFAAAVTTPLDVAKTRIMLAKAGSGVANGNVLFALHEIWRTQGIMGLFAGVIPRMTMISLGGFIFLGAYDKVRSSLL", "text": "FUNCTION: Mitochondrial S-adenosyl-L-methionine/S-adenosyl-L- homocysteine antiporter. Mediates the exchange of cytosolic S-adenosyl- L-methionine, the predominant methyl-group donor for macromolecule methylation processes, for mitochondrial S-adenosylhomocysteine(SAH), a by-product of methylation reactions. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MSPIKHKTIRMIKDKIFLFIVGALTLLAILPLFHIIISIVEKGLPIIMERGLTFITGTLSEGGIGPAIVGTLMLTFLATLIGLPLAFLAGAYAYEFPNSFIGRATKMLLQIMLEFPTILVGTFVMGMLVVPMGTFSALAGALALALILTPYVAVYTEEAMAEVPKIYKEGGYALGCTRAQVIFKVITKMAKKGILTGILIGMAKVAGETAPLLFTAGGLYEVYPTNPLEPVGAIPLLIYTLVQSPSIEDHQMAWGAALVMLIIFLAIFVPIRYALKDDIKL", "text": "FUNCTION: Part of the binding-protein-dependent transport system for phosphate; 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. CysTW subfamily."}
+{"protein": "MSSKIRPSADDKKLQRVLYFFLERVRAAKDVSGQLLSPLIDNASVDTASVSPSSNGRPTTLKSIQSKIDEFQYHDFSEFVSDLAYLFINVKALYEGTQTYSFVQALEEFCIQQLRTFQQQGYIPVITWPNTDSPSATTSSPISRNPEYSVSPPNGSKFVKNEDEAYDSDLYVEEEDSDVKGRSMVGRDGRYKSEDLKRRKLQPSSKPLSSLEARAKVIMRQVRRYRDGSGRQLFAPFERLPDPRMFPEYYQAIEQPMALEVIQKKLSKHRYETIEQFVDDFNLMFDNAKSFNDPSSQVYRDADFLKNYLADVLRLEAGKLDSEFFNYETDSRASPQLPKNDIQPAVSIDGTLLNVGDWVLIRNPADSSKPIVSQIYRIWKSDDDINYVTVCWYLRPEQTVHRADAVFYENEVFKTSLYRDHPVSEIVGRCFVMYITRYIRGRPKGIRSTPVFVCESRYNDDTKQFSKIKSWKACMPQEVSGSEYEMILFDRPITLTKVASPLLHLLASKSQGLPSPATTDSNTHMLPSQGSLLPPSSISETKSFSTKASTPLSTDDIATPLSSAPNPPSVMPTYARKTSSHSERSSHSSYHNSSHVPTAAFNSPIMRTSTKSTSPIPARPFYAQSGSLQSLNTTQHSHQISGGHSGRMNVPYAKLSYTSHNGRHGGSNGNISGAKTPMTNYTINSMPSLPVFPPAFIVPGTHQKLDESSPVPGIDDVTVINTETAKMLDKDEHQNVLWYTVPPLDPIPLENRNGSLTHSVEYVLYKKSKGSQVITEKARSNELSREAKFENLVASLSDALIPP", "text": "FUNCTION: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. SUBCELLULAR LOCATION: Nucleus Note=Localizes to centromeric and flanking chromatin. SIMILARITY: Belongs to the RSC1 family."}
+{"protein": "MKLIGITGMPGSGKSAITKLAEKYKIVVVSMGDVVRYETLKQGMPLNPENVGNTAVKLREIYGKEAIAVPCLNYVNEKYNNEDFVIIEGIRSIYEVNYIKKHAELDIIAIHSSPKTRFERLSGRNREDDSNDWNTFVERDERELNFSIGRVISLADYMVVNEGNYMDFVNDLENTFKKIINVN", "text": "SIMILARITY: Belongs to the UPF0200 family."}
+{"protein": "MSWNLFKGGPKKQIVPKTVERDFEREYGKLQQLEDQIKKLQKDMKKSIEADLAMSKSAVRISSDLLGNPLCEPDVDFLQMVTALDTAMKRMDAFNQEKVNQIQKTVMDPLKRYSSVFPSLNMAVKRREQALQDYKRLQTKVEKYEEKDKTGAMIAKLHQAREELRPVRDDFEAKNHQLLDEMPKFYNSRTDFFKPSFQSLIRAQVVYYTEMSRVFGDLAQQVDEVQLSDAEREQENEARLAELRSLSIVADD", "text": "FUNCTION: Involved in cytokinesis and septation where it has a role in the localization of F-actin. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton."}
+{"protein": "MSQPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPPDIRHAAYNDINSASALIDDATCAVIVEPIQGEGGVVPASNAFLQGLRELCDRHNALLIFDEVQTGVGRTGELYACMHYGVTPDLLTTAKALGGGFPVGALLATEECASVMTVGTHGTTYGGNPLASAVAGKVLDLINTPEMLNGVKQRHDWFVERLNSINHHYSLFSEVRGLGLLIGCVLNADYAGQAKQISQEAVKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAAACEHFVSRGSS", "text": "FUNCTION: Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily."}
+{"protein": "MTAVFPGELLLAEGIHEIARVTALLSGPLRRAPRVAQVVGPGFAGRPWAPRLTDALRPLDPTVVVHDGPTTPDSVAALARQLRAIRADVAVAIGGGTVMDAAKAAAALADGGPPDADRVRQACAAGPAAGDTPPAVRVVAVPTTAGTGAEATPFATLWDLKHRRKLSLTGPRVRPSAAVLAPELLAGLGRRALATGILDALCQGAEASWSIRSTPESIRWGTSAVTLAAEALDQVQDDAPDAAARLALQRAAHHSGRAIALAQTSSCHAISYPLTLRLGLAHGHACGVTLGRLLRYNHAVPAGDCADPRGTGHVRRVLDALAAPLGGTPARAALRVERFITACGLTPYDALDVDHRSLAAEAVTYPRCHDNPRRLDRESLGRLLGERSEMEETCG", "text": "FUNCTION: Catalyzes the reduction of phosphonoacetaldehyde to 2- hydroxyethylphosphonate, a step in the biosynthesis of phosphinothricin tripeptide. Phosphinothricin tripeptide is both a natural-product antibiotic and potent herbicide. Can use both NAD and NADP but the preferred substrate is NAD. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family."}
+{"protein": "MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAEGGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELWGCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQIQRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVYRYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWRKGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIPVRPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQATERAATAGNGNEAAIEAQAAGVEQRLKDLVNQDGGENWAKIRDEMGLAMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDTSSVFNTDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGCTERDDVNFLKHTLAFRDADGTTRLEYSDVKITTLPPAKRVYGGEADAADKAEAANKKEKANG", "text": "FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used during anaerobic growth, and succinate dehydrogenase is used during aerobic growth. The QFR enzyme complex binds 2 quinones in or near the membrane; 1 near the [3Fe-4S] cluster (QP is proximal to the [3Fe-4S] cluster, on the cytoplasmic side of the membrane) while QD (the distal cluster) is on the other side of the membrane. It is not clear if both of the quinol- binding sites are functionally relevant (PubMed:10373108, PubMed:11850430). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily."}
+{"protein": "MSASPTARQAITQALPMITRKVVISDPIQMPEVYSSTPGGTLYSTTPGGTKLIYERAFMKNLRGSPLSQTPPSNVPSCLLRGTPRTPFRKCVPVPTELIKQTKSLKIEDQEQFQLDL", "text": "FUNCTION: Repressor of translation initiation that regulates eIF4E1 activity by preventing its assembly into the eIF4F complex (PubMed:11389445, PubMed:19804760, PubMed:25702871). Hypophosphorylated form competes with eIF4G1 and strongly binds to eIF4E1, leading to repress translation (PubMed:25702871). In contrast, hyperphosphorylated form dissociates from eIF4E1, allowing interaction between eIF4G1 and eIF4E1, leading to initiation of translation (PubMed:25702871). Acts as a regulator of various biological processes, such as innate immunity, cell growth or synaptic transmission (PubMed:10811906, PubMed:11389445, PubMed:27525480). Acts downstream of phosphoinositide-3-kinase (PI3K) to regulate cell growth (PubMed:11389445). Extends lifespan upon dietary restriction by regulating the mitochondrial translation (PubMed:19804760). Acts as a regulator of lifespan in response to cold by regulating the mitochondrial translation (PubMed:28827349). Acts as a negative regulator of presynaptic release of neurotransmitter in motor neurons: Thor expression is induced in response to insulin signaling, leading to prevent of translation of complexin (cpx), a protein known to regulate the exocytosis of synaptic vesicles (PubMed:27525480). Acts as a negative regulator of synaptic strength at the neuromuscular junction: Thor expression in response to acute fasting prevents translation, thereby suppressing retrograde synaptic enhancement (PubMed:27916456). SIMILARITY: Belongs to the eIF4E-binding protein family."}
+{"protein": "MAAAEPAVLALPNSGAGGAGAPSGTVPVLFCFSVFARPSSVPHGAGYELLIQKFLSLYGDQIDMHRKFVVQLFAEEWGQYVDLPKGFAVSERCKVRLVPLQIQLTTLGNLTPSSTVFFCCDMQERFRPAIKYFGDIISVGQRLLQGARILGIPVIVTEQYPKGLGSTVQEIDLTGVKLVLPKTKFSMVLPEVEAALAEIPGVRSVVLFGVETHVCIQQTALELVGRGVEVHIVADATSSRSMMDRMFALERLARTGIIVTTSEAVLLQLVADKDHPKFKEIQNLIKASAPESGLLSKV", "text": "SIMILARITY: Belongs to the isochorismatase family."}
+{"protein": "MEAVVNSDVFLTSNTGLKSSYTNQTLSLVDEDHIHTSDKSLSCSVCNSLSQIVDDDFISAGARNQRTKPKRAGNDQAQQTTKKDCMVSIDEVASTHDWSTRLRNDGNAIAKYLTTNKYDTSNFTIQDMLNIMNKLNIVRTNRNELFQLLTHVKSTLNNASVSVKCTHPLVLIHSRASPRIGDQLKELDKIYSPSNHHILLSTTRFQSMHFTDMSSSQDLSFIYRKPETNYYIHPILMALFGIKLPALENAYVHGDTYSLIQQLYEFRRVKSYNYMLLVNRLTEDNPIVITGVSDLISTEIQRANMHTMIRKAIMNIRMGIFYCNDDDAVDPHLMKIIHTGCSQVMTDEEQILASILSIVGFRPTLVSVARPINGISYDMKLQAAPYIVVNPMKMITTSDSPISINSKDIYSMAFDGNSGRVVFAPPNIGYGRCSGVTHIDSLGTNVMGSAVHSPVIVNGAMMFYVERRQNKNMFGGECYTGFRSLIDDTPIDVSPEIMLNGIMYRLKSAVCYKLGDQFFDCGSSDIFLKGHYTILFTENGPWMYDPLSVFNPGARNARLMRALKNQYKKLSMDSDDGFYEWLNGDGSVFAASKQQMLMNHVANFDDDLLTMEEAMSMISRHCCILIYAQDYDQYISARHITELF", "text": "FUNCTION: Major component of the virion core that undergoes proteolytic processing during the immature virion (IV) to mature virion (MV) transition. Essential for the formation of a structurally normal core. SUBCELLULAR LOCATION: Virion Note=Localizes to the virion core wall, the mature protein accounts for 11% of the dry mass of the virion. SIMILARITY: Belongs to the orthopoxvirus OPG129 family."}
+{"protein": "MRTKIFAAGTVLTCLMLCAGCTSAPPAPTPVIVPNACPKVSLCPMPGSDPQTNGDLSADIRQLENALARCASQVKMIKHCQDENDAQTRQPAQGAD", "text": "FUNCTION: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption is possibly due to local fusion between the inner and outer membrane performed by the spanin complex (By similarity). SUBCELLULAR LOCATION: Host cell outer membrane; Lipid- anchor; Periplasmic side."}
+{"protein": "MVTLMPYNYAAPRCGLIDKMIEPKVKRPKTDHTDTHERNRLCNLSQQQQQQQPQQQQTHQQQQQQQQQSHQQSHSSTVLASNGPSSAGAGMGVGVGGGGGSGGGVGGGVGQCSPLGLPPQSQPLQPTIGSLASLSGHYSNGNANPNVNSSSCSLATASSFAQSAGSSFSTYQQAGGTSGGVSGEDGVVGGATVMSHWTHDGTGSSAAVKSESRSPGQVHASLDNGSVAGSNLYGCSSASNPLDGGAVAVNSSAVAAAAAAVYDGKHDYYYYNSMQQYTPPPFYSGYGTPYAAATAARQAKMEPGAAAAAAAYLTPSYAASGNNNSQLYSSPYAGYNNFGQQDYGGYYNEQYGNYYSPANYSPYAVSSPSSSASHGHGFHVAASSNLSESPTDTHSTTPVHQTTHSPHSPLPISPSTGSGIGPLGNVSAAAAAAALNSSGGSSVGTAGSGGVATSKTTPTGKTGRARGRRHQQPSPTRSTASDTGNSEAVKPPERVFVWDLDETLIIFHTLLSGSYANRYTKDHSSLMTIAFRMEEMVFNMADTHFFFNEIEECDQVHIDDVSSDDNGQDLSAYNFATDGFHTNTPPGAPPNLCLPTGVRGGVDWMRKLAFRYRKIKDIYNSYRGNVGTLLGPGKREAWLQIRSEIEVATDNWATLALKCLSMISQRENCVNVLVTSTQLAPALAKVLLFGLGGIFNIENIYSAHKIGHETCYERIVTRFGRKSTYVVIGDGNEEETAAKAMNFPFWRISAHSDIRALYTALDMGFL", "text": "FUNCTION: Tyrosine phosphatase thought to play a role in transcription regulation during organogenesis through its intrinsic protein phosphatase activity (PubMed:14628052, PubMed:14628053). The phosphatase activity was shown in vitro. Appears to function together with So and Dac in eye development (PubMed:9428512, PubMed:9428513). Required for the survival of eye progenitor cells at a critical stage in morphogenesis (PubMed:8431945). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family."}
+{"protein": "MTDLVAVWDVALSDGVHKIEFEHGTTSGKRVVYVDGKEEIRKEWMFKLVGKETFYVGAAKTKATINIDAISGFAYEYTLEINGKSLKKYMEDRSKTTNTWVLHMDGENFRIVLEKDAMDVWCNGKKLETAGEFVDDGTETHFSIGNHDCYIKAVSSGKRKEGIIHTLIVDNREIPEIAS", "text": "FUNCTION: Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAIM1 family."}
+{"protein": "MKRWPVFPRSLRQLVMLAFLLILLPLLVLAWQAWQSLNALSDQAALVNRTTLIDARRSEAMTNAALEMERSYRQYCVLDDPTLAKVYQSQRKRYSEMLDAHAGVLPDDKLYQALRQDLHNLAQLQCNNSGPDAAAAARLEAFASANTEMVQATRTVVFSRGQQLQREIAERGQYFGWQSLVLFLVSLVMVLLFTRMIIGPVKNIERMINRLGEGRSLGNSVSFSGPSELRSVGQRILWLSERLSWLESQRHQFLRHLSHELKTPLASMREGTELLADQVVGPLTPEQKEVVSILDSSSRNLQKLIEQLLDYNRKQADSAVELENVELAPLVETVVSAHSLPARAKMMHTDVDLKATACLAEPMLLMSVLDNLYSNAVHYGAESGNICLRSSLHGARVYIDVINTGTPIPQEERAMIFEPFFQGSHQRKGAVKGSGLGLSIARDCIRRMQGELYLVDESGQDVCFRIELPSSKNTK", "text": "FUNCTION: Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Activates GlrR by phosphorylation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MKKYLALALIAPLLISCSTTKKGDTYNEAWVKDTNGFDILMGQFAHNIENFWGFKEVVIAGPKDYVKYTDQYQTRSHINFDDGTITIETIAGTEPAAHLRRAIIKTLLMGDDPSSVDLYSDVDDITISKEPFLYGQVVDNTGQPIRWEGRASNFADYLLKNRLKSRSNGLRIIYSVTINMVPNHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRSQGKSGTPSRSFLFDPASNIDTGTAYLAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMTPGDVYQTLTTRHPSAESRRYLYKVNTAQKSYRRR", "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": "MTDYYEPINIFRQCAISVKKRGQEHGLDVATRRVASWQRSAKLNSPTLRKVSDDYFLTKKVKSDYWQVSDMDLSATAFSSVGNLVMVTSNKDQDNVKLYTYAEDPNSMRQLQTITVPGAPITTATLLPAAEFNPTAYVPDHEQLLLTGHRDGIVNLISTSFTKGESRIVKRYNHRKHLVSMANEVMNIDTKHKDEIEQLLANHKQKSNSARAMPVRSIKPWNGMGFVSLINDSLFVFTLNNTKTPQYLNSFPGIQSFAIQTHSNPYLLGLTGTHFGANNIALLDLKKTLYIPDPVIDKEYRKSSSRSVSSDCTWISSCYLAQALGKEVNIWDVRRTDGKPKAKILPNKGVIEHLSYHYETDTLFSSDDQGNIIAWDLTNLDRLEYCGLVHGLDAVKYNMNLPINDSNYSQCGNVVVNGNNNSACTYRKLARKIEVNQRAGTLFSYCDHELGLHRLFSAPVEISLQLSDTETINYESEEEEVMVHVDKLHDNSHENSSILHSDSTTLHSRDFDSYSDNESANTTDNDNELAYMDTFKRPVPAFLDEKVAAYNNPVLSSSSSTLAYGYF", "text": "FUNCTION: Involved in cell wall metabolism and required for the separation of the mother and daughter cells. SIMILARITY: Belongs to the WD repeat DSE1 family."}
+{"protein": "MLDAFSRKAVSADSSGAFIGGGELASLKSFIADGNKRLDAVNALSSNAACIVSDAVAGICCENTGLTAPNGGVYTNRKMAACLRDGEIVLRYVSYALLAGDASVLQDRCLNGLRETYAALGVPTGSAARAVAIMKAASAALITNTNSQPKKAAVTQGDCSSLAGEAGSYFDAVISAIS", "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": "MAPPLAPLPPRDPNGAGPEWREPGAVSFADVAVYFCREEWGCLRPAQRALYRDVMRETYGHLSALGIGGNKPALISWVEEEAELWGPAAQDPEVAKCQTQTDPADSRNKKKERQREGTGALEKPDPVAAGSPGLKSPQAPSAGPPYGWEQLSKAPHRGRPSLCAHPPVPRADQRHGCYVCGKSFAWRSTLVEHVYSHTGEKPFHCTDCGKGFGHASSLSKHRAIHRGERPHRCLECGRAFTQRSALTSHLRVHTGEKPYGCADCGRRFSQSSALYQHRRVHSGETPFPCPDCGRAFAYPSDLRRHVRTHTGEKPYPCPDCGRCFRQSSEMAAHRRTHSGEKPYPCPQCGRRFGQKSAVAKHQWVHRPGAGGHRGRVAGRLSVTLTPGHGDLDPPVGFQLYPEIFQECG", "text": "FUNCTION: Zinc finger protein that functions as a cofactor for steroid hormone receptors, such as NR3C1/GR (PubMed:28139699). Directs NR3C1/GR transcriptional activity toward specific biologic pathways by changing NR3C1/GR binding and transcriptional activity on the glucocorticoid- responsive genes (PubMed:28139699). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MDEVTRTAQRSPSITETHAGETKLAGPGEKEGDVESPVDPSADSEQNRQQITGLQLFAILASVTLSAFLMLLDGSIIGVAIPNITSQFHSIDDIGWYTAAYQLASAALQPLSGKIYSSFSTKWTYLFFFGLFELGSLICGVANSSSMLIGGRAVAGLGSSGLLNGGMTIIAGAVPLEKRPVYTGIYLGISQLGIVCGPLIGGALTEYTTWRWCFYINLPVGAVTAILLLFLQVPELTEKPRFTFALVRRVIPELDLIGFTLFAPAAIMVLLALYYGGNDFPWDSSQVIGLFCGAGVTIIVFALWERRVGDRAMIPPSMVSHRIVYTSAINGAALVASILVAAQYLPIYFQGVRGYGPAMSGVNTLPGILSQLLTVILSGVLVQKVGYYLPFAAAGSAISAVGNGIVTLFSPTTPTAKWIGYQIVLGSGRGIGMQMGIIAIQNLLPPEKISVGIAFMIFCQNFAGAIFVVVGEVIFTQQLVKQIQAHAPSVKVDAALAAGASSSSLRALVPPGSPELQGVLLAFSNSVDRVFYLLMSLSLAGFVAAFGMGWVDTRKKNKSETE", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide and a linear 12 carbon dioic acid structure (PubMed:30598828). Required for the secretion of calbistrin A and calbistrin C, as well as of related compounds decumbenone A, B and C (PubMed:30598828). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
+{"protein": "EISCEPGTTFQDKCNTCRCGKDGKSAAGCTLKACPQ", "text": "FUNCTION: Probable serine protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I19 family."}
+{"protein": "MTNSLFLLAEGGLFDFNATLPLMVLQILLLMVVLNAIFYTPIARVLDERDEYIRKNLTQASETLAKAEAITKQYEQDLAKERRDAQMIIASSQQEAQEIVAMEIKQAQKDTELLVNEATTQLNSQKEKALQALEKQVNTLSEQIKNKLLSGQLAG", "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": "MSPMLATLPDVTAVLHSPSASPPSGLRAPAAVGMGMARTRFLAPRAAASAASAVSAKPAAVAPLYADRTVVRIGLPSKGRMSEQTLSLLKSCQLSVRHLNPRQYTADIPQVPNLEVWFQRPKDIVRKLQSGDLDLGIVGFDIVSEYGQGSDDLVVVHDALEFGHCRLSLAVPKEGIFENINTLEDLANMPEWTQERPLRVVTGFGYLGEKFMRENGFNHVSFLAGDGALESYPAMGMADVIVDLVSSGTTLRENNLKEIDGGVVLESQATLVACRRSLHKRNGVLEITHEMLERLEAHLTATGEIMVTANMRGNSAEEVAERVLSQTSLCGLQGPTISPVYRSRDGKVAVEYYAINVVVPQKSLYKSIQQLRSIGGSGVLVTKLTYIFDEETPRWRKLLSELGL", "text": "FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long subfamily."}
+{"protein": "MASGSNWLSGVNVVLVMAYGSLVFVLLFIFVKRQIMRFAMKSRRGPHVPVGHNAPKDLKEEIDIRLSRVQDIKYEPQLLADDDARLLQLETQGNQSCYNYLYRMKALDAIRTSEIPFHSEGRHPRSLMGKNFRSYLLDLRNTSTPFKGVRKALIDTLLDGYETARYGTGVFGQNEYLRYQEALSELATA", "text": "FUNCTION: General regulator of phagocytosis. Required to uptake Gram negative bacterium by macrophages. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Golgi apparatus Mitochondrion."}
+{"protein": "DTAPLEKKSHCLSQGLSGLLSLGKLFRDSSWTLSKEELSRGVSQFGLDFSDADVNKLFSDFEKKAAVEAAFKHLDKTGDGVVTVEDIKGVYSAKVVKGEATEEEILKKFLNMFESSTSVDGKVTKKEFLDYYSGLSK", "text": "FUNCTION: Possibly acts as a regulatory protein and not as a calcium buffer or transport protein."}
+{"protein": "MSGVTARMENSIITTDSGILFFDQNWTQVSSGGHQFQHISAFAYDEVKQKLYFSDLKDPKFRIFSLDANPQEEYHKVTKLLPKSDETAYITGLVFDHLERKLYWTERGTHALYSVEVDKIGNGTDAGSLISTVTKVEDNHDLAGLAIDECRRHLYWTNSYLQTSNVVRATMAGKVLNSHTEDVYEPKGIAVDHYSNRIYWVEKKFGRAFSIQSVNLEVEDVKTFISENDKAPTHVALNSRYLYWVDQQVGEVHETLKSDSTQSRVVYRGNRPTAIIIKSALLLNHQNNNPSCKSVIAKILDNVKRESEGELPQADKPTSAKPEMIICLNNGILNHNTNSCICLPEYQGNFCEIPICNNYCVHGKCVIGRDNRPTCECDAKFEGERCDRSKCDGFCLNSGNCSFSDATATCACPKNFSGKRCETAICTSDYCYNGRCMVEEGGSPKCQCNVGYRGERCEEYTCNNYCLNDGKCVLNNETMLVECRCGAEYTGKRCEIPKRFCSLDTGNPELQPYCDGIPLSSQQQQQQLVEPQISYCKNSFNRTVVYASLAFAASLFILMVILLIVRRFYEEGRPRITKRFKVTSNHTQMTSRPATQCEITIENCCNMNVCETPCFDTNLLQKSSSKAEDKQYLLDDIENIAGSYRKLPSCAGGDKNLP", "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": "MSQIVDFVEDKDSRNDASIQIIDGPSNVEIIALSESMDQDECKRAHVSSAEMIPSSPQRKSVSNDVENVDLNKSIELSAPFFQDISISKLDDFSTTVNSIIDSSLRNENNAKGNAKKLLDDLISDEWSADLESSGKKHNKSQYNLRDIAEKWGVQSLKNPEPIAVDCEYKTQGIGKTNSDISDSPKSQIGAADILFDFPLSPVKHENPTEEKHNSIANENSSPDNSLKPAGKQNHGEDGTSMAKRVYNKGEDEQEHLPKGKKRTIALSRTLINSTKLPDTVELNLSKFLDSSDSITTDVLSTPAKGSNIVRTGSQPIFSNANCFQEAKRSKTLTAEDPKCTKNTAREVSQLENYIAYGQYYTREDSKNKIRHLLKENKNAFKRVNQIYRDNIKARSQMIIEFSPSLLQLFKKGDSDLQQQLAPAVVQSSYNDSMPLLRFLRKCDSIYDFSNDFYYPCDPKIVEENVLILYYDAQEFFEQYTSQKKELYRKIRFFSKNGKHVILILSDINKLKRAIFQLENEKYKARVEQRLSGTEEALRPRSKKSSQVGKLGIKKFDLEQRLRFIDREWHVKIHTVNSHMEFINSLPNLVSLIGKQRMDPAIRYMKYAHLNVKSAQDSTETLKKTFHQIGRMPEMKANNVVSLYPSFQSLLEDIEKGRLQSDNEGKYLMTEAVEKRLYKLFTCTDPNDTIE", "text": "FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EME1/MMS4 family."}
+{"protein": "MAARLCTRCLPPVWLCRQAWQGQGRHYRAALCTELKQPLTIQEVAPRPVGPQEVRVDVHFCGVNFADILACRGQYQEKPPLPFTPGMEFSGAVLETGTDVSTVKKGDRVIGVSSFHAMAEQCITDQKTLWRIPENVSLQDAAVLPVSYGTAILAVDHRARIQPGETVLVTAAAGATGLAVIDVATNVFRAKVIAATGSDEKCKLAVQRGAQFSVNYSQGSLRDAVKKLAGSGGVNVAIDMVGGDVFLESLRSLAWEGRIVVLGFAGGNIASVPSNLLLLKNISAMGLYWGRYQHQDFAVFSKSMSTAMQYCQQGLIHPHTGAVFKLEKINDAFLHVMQRKSTGKVLLSLK", "text": "SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
+{"protein": "MVIENTKDISINTGYKRQEDALNTDSEDLIYRPKKIIKTNQEDAVHDLKYENFVSKNHVLQSDINGKKRDSNRDKAAVVTAPIASTHESNYEESVSKFKESWLPQLKDLIESHKTICESTLAYESDQAMASSNTLKRIKDLKSKPKNIIQLERLHMLSNGEHRLLSKDETDDIESAYLNLRSHLQVQEQVYAEKDHEYSLQLQSYREAAEKAKQDILETKENLSSELSISNIQLKEAKERLEAANASYQKLRREHKELALYHEKKTHSLVCNLNGERKSFGDFVENEVKSYKHEYANICESLRRALVLIQGSCTEKILRFKEKILDLLEMKQQEENDRISHIEYENDLTVKKLKRRISELEMAVKEYESEKSYSEKEYEEKISSLRIELEDKLAEIDMLRNKLLKEEHKHHSTSEKLEELSKYVASIQDKERNNGQNALELQARIQQLERRNEDMYNKLLAEEIIRRKLHNDIQELKGNIRVFCRVRPLLPSEESEYCIADVLQFPDKDALEPQKLILKGPNVESSLGHTYDRNYEFSFDRVFAPESDNSSVFEEISQLIQSAIDGYNVSIFAYGQTGSGKTYTMSSQDGMIAMSIKHIFNYLSTLREKGWVYKLRGQFLEIYNETIYDLLNKAEMLKNPKHDIHHDEKERRTTVDNVSIIDFNEEDTVYKMLNRAGENRFIAATKANERSSRSHTVFMLYIDGENSRTKQICKGTLNLVDLAGSERLSYSQAVGDRLRETQAINKSLSCLGDVIHALGNASNSTTKEKSHIPYRNSKLTYLLKYSLGKGAKTLMFVNVSPLKSQFMDTLNSLRFATKVNDTKVGSIKHYKR", "text": "FUNCTION: Microtubule-dependent motor that is involved in microtubule organization in the mitotic spindle. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. NCD subfamily."}
+{"protein": "MRKRKVAIIGSGNIGTDLMIKILRHGQHLEMAVMVGIDPQSDGLARARRLGVATTHEGVGGLMQMAEFADIDFVFDATSAGAHIKNDAALREAKPGIRVIDLTPAAIGPYCVPVVNLADNLHQGNVNMVTCGGQATIPMVAAVSRVAKVHYAEIVASIASQSAGPGTRANIDEFTETTSQAIEKVGGAGKGKAIIVLNPAEPPLMMRDTVYILSELASQEAIAASIAEMAAAVQAYVPGYRLKQQVQFEVIPEDRPVNLPGVGCFSGLKTAVYLEVEGAAHYLPAYAGNLDIMTSAALATAEQMAGAMHSAAGATA", "text": "FUNCTION: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds. SIMILARITY: Belongs to the acetaldehyde dehydrogenase family."}
+{"protein": "MNIFRFAGDLSHVFAIIILLLKIWKTRSCAGISGKSQILFAVVYLTRYLDLFTTYVSLYNSVMKVLFLATSGATVYLMYVKFKATYDHNHDSFRIEFLLVPCALLSLVINHEFTVMEVLWTFSIYLESVAILPQLFLVSRTGEAESITSHYLFALGSYRALYLLNWVYRYMVESHYDLIAIFAGVVQTVLYCDFFYLYITKVLKGKKLQLPA", "text": "FUNCTION: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERD2 family."}
+{"protein": "MHHNYYLSPLAVALALGMVSPAKAADPILLQNASFSEVKQKFALSTQGVAVAKDSLSFVSEHTDRNKVTHVRMQQKYVGFPVYGGYAIMHSMNTAKSLAATTQSTVEMNGVVYQGLQTELGQPDASFVQNADKALQQFKAKYANQNVGDEKVIPMVYIDKDNQAHWAYKVSIRVNHLDKAPERPTAIIDARTQQPFVQWNDIKTERVSVKGSGFGGNKKMGYYEFGKDFPYLDLTRDANNATCYMENESVKVIDMKHKYSSVKAAMSFACSTTDSDIYSTGYREDNGALSPSNDALYAGYVIKHMYTDWYGVNVLSNSNGSPMQLVMRVHYGDGYENAYWDGEQMTFGCGDRMMYPLVSLGVGAHEISHGFTEQHSGLEYYGQSGGMNESFSDMAAQAAEHYSVGKSSWQIGGEIMKESSGYDALRYMDKPSRDGESIDTADEYYSGLDVHYSSGVYNHLFYILATKPNWDTRKAFDVMVKANMDYWTPYSSFDEGGCGVLSAAKDLGFSLNDVKSSLQAVAINYSKCH", "text": "SIMILARITY: Belongs to the peptidase M4 family."}
+{"protein": "MDSELSQSMVGSYLNPPERMHLPSFTQNEAFQNCHPGTPPKMFNSPNNQALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKDISIQLSSAQSRCILLEKQLEYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLFQDRACEKTNCLKREPPQQRDHKFRTPTFERKKPFRTTSQARANPQSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQTMQPGNHSVSEDIEQELEQLAKKMESKGDQISKLKKHQDSVRKLQEKIENSRINESSGIHGNPKGSKNLKTSPRKCVSETSSFQRDRGFQPVQVHSLQSKLRRDDIKWEQ", "text": "FUNCTION: Centrosomal protein which may be required for microtubule attachment to centrosomes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the translokin family."}
+{"protein": "MPQLGLLPGRAWTVLLGLLRPPPGALCIRAVRSHSQVAEALFASQLKPHQEKSNFTIKTPKGTRDLSPQQMVVREKILDVVVSCFKRHGAKGLDTPAFELKEILTEKYGEDSGLIYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTIVQGRYREFYQCDFDIAGQFDPMIPDAECLKIMCEILSGLHLGDFLIKVSDRRILDGIFAVCGVPESKFHAICSSVDKLDKISWKDVRHEMVVKKGLAPEVADRIGDYVQCHGGISLVEQMFQDPRLSQNKQALEGLGDLKLLFEYLTLFGVAEKVSFDLSLARGLDYYTGVIYEAVLLQTPVHAEEEPLNMGSVAAGGRYDGLVGMFDPRGHKVPCVGLSIGVERIFSIVEQRIKTFGEKIRTTETQVFVATPQKNFLQERLKLIAELWDAGIKAELMYKNNPKLLPQLHYCENMGIPLVVIIGEQELKEGVIKLRSVASREEVAIKRENLVAEIQKRLSES", "text": "FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
+{"protein": "MSTAKTLTLEMHLGDLMIGELSFDATADTFAVHYTKDWQQSGFPLSPTIPLDGTGTSNQISMFLVNLLPENKGLDYLIESLGVSKGNTFALIRAIGLDTAGAIAFVPKGALLPETQLRPIKAEEVIQRIEDPTMWPMEIWDGKPRLSVAGVQPKLNLFYNGKEFAFAEGTLSSTHIVKFEKYHHLVINEFITMRLAKVLGMNVANVDIVHFGRYKALCVERFDRRNIPGEQRVLRRHIVDSCQALGFSVSKKYERNFGTGRDVKDIREGVSFNRLFSLAAKCRNPVAAKQDMLQWALFNLLTGNADAHGKNYSFFMTPSGMEPTPWYDLVSVDMYEDFEQQLAMAIDDEFDPNSIYAYQLAAFMDGLGLPRNLLISNLTRIARRIPQAIAEVILMLPPLDEDEASFVAHYKTQLLARCERYLGFVDEVRDVEV", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system; overexpression in wild-type temporarily inhibits cell growth, overexpression in a hipAB deletion leads to acute growth inhibition. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. In the ternary phosphoserine-HipA-HipB-DNA complex the DNA is bent about 125 degrees; all HipA in the crystallized ternary complex is phosphorylated. In E.coli phosphorylation of HipA is thought to release HipB from the HipA-HipB-DNA complex, suggesting the complex functions differently in the 2 bacteria (PubMed:25056321). Phosphorylates Glu- tRNA-ligase (GltX, on 'Ser-239') in vivo, with HipB probably acts as a corepressor for transcription of the hipBA promoter (By similarity). SIMILARITY: Belongs to the HipA Ser/Thr kinase family."}
+{"protein": "MAAVSSVASLRGADYENGLRGGAGPSGGGQDPGEDDPMGRGTLDLDLELLTQGRRNRRVGGRTAPGRRSGGRGGSGGGAGGLEELEDEELEEEEPGELTGDQTIEDPELEAIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSVEEKMEADARSIYVGNVDYGATAEELEAHFHGCGSVNRVTILCDKFTGHPKGFAYIEFSDKESVRTSLALDESLFRGRQIKVVPKRTNRPGISTTDRGFPRARYRARASSYSSRSRFYSGYTPRPRGRVYRGRARATSWYTPY", "text": "FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre- mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus."}
+{"protein": "MSDLRQNFERDGFVVIENVFNDQEIEEIKGAIGKIVEDMNLAEHPKSVFSTYDEDKHAADSYFLNSSDKIRFFFEEGAVDKDGELTVPKDKALNKIGHGLHLLDPTFKKMTFNSKIQKIFQGIGYQEPEVVQSMYIFKQPKIGGAVTDHVDSTFLRVNPIDHLTGVWIAIDEASVENGCLSFIPGSHKDTSTSDYRFVRTHDTTGGPLLKFIGTRPTYDQSKFQHVPISKGSLILIHGLVVHKSEANTSDKSRHAYTIHVMEKQNTEWSKDNWLQETEQYKFPNLYKQ", "text": "FUNCTION: Has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA (By similarity). SIMILARITY: Belongs to the PhyH family. PHYHD1 subfamily."}
+{"protein": "MEVPRLDHALSSPSSPCEEIKNLSLEAIQLCDRDGNKSQDSGIAEMEELPVPHNIKINNITCDSFKISWDMDSKSKDRITHYFIDLNKKENKNSNKFKHKDVPTKLVAKAVPLPMTVRGHWFLSPRTEYTVAVQTASKQVDGDYVVSEWSEIIEFCTADYSKVHLTQLLEKADVIAGRMLKFSVFYRNQHKEYFDYVREHYGNAMQPSIKDNSGSHGSPISGKLEGIFFSCSTEFNTGKPPQDSPYGRYRFEIAAEKLFNPNTNLYFGDFYCMYTAYHYVILVIAPVGSPGDEFCKQRLPQLNSKDNNFLTCTEEDGVLVYHHAQDVILEVIYTDPVALSLGTVAEITGHQLMSLSTANAKKDPSCKTCNISVGR", "text": "FUNCTION: May play a role in the development of the central system. SIMILARITY: Belongs to the PHYHIP family."}
+{"protein": "MKFENCRDCREEVVWWAFTADICMTLFKGVLGLMSGSVALVADSLHSGADVVASGVTQLSLKISNKPADERYPFGYGNIQYISSSIVGSLLLIGASFLMYGSVMKLISGTYEAPSIFAAVGASVTVIVNELMYRYQICVGNENNSPAIIANAWDNRSDAISSAAVMVGVIASVIGFPIADTIAAIGVSALVGRIGLELIGTSIHGLMDSSVDTELLQTAWQVAMDTPMVHSIYFLRGRHVGEDVQFDIRLRVDPNLRIKDSSMVAEAVRRRIQEEIPHARDIRLFVSPAPAAAARA", "text": "FUNCTION: Plays a dual, essential role in magnetosome formation; required for magnetosome vesicle formation as well as biomineralization (PubMed:20212111) (Probable). Probably binds and transports iron (By similarity). Requires heterodimerization with MamM for stability (By similarity). SUBCELLULAR LOCATION: Magnetosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family."}
+{"protein": "MSGGLSRRRVAAASSDEERPEMRSVSHSKSHLEGYDDDHKIAFDPKDLEQGAEREKQPRLTLMEEVLLLGLKDKQGYLSFWNDSISYSLRGCILMELAFRGKLRMQKDVNRKRFPLADRVVELVDEKLTGEVLLDEAIKMIHTSELMSVTSWIDLMSGETWNVMKIGYQLRQVRERLAKGLVDKGILRNEKKNFLLFDMPTHPIADTSIKDSIKKRVVSVLTSRVIEIDNSPSFPEYLSFRCLRTVALACSSYAANVLENALDNLNYEDREKAFSRVDELLCDFSQWPFDLHASSSVGANLPELISEELSSVKEEQLLFIEVVAAVLQVFTHLDSLL", "text": "FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Mediates the cis and medial Golgi localization of mannosyltransferases through direct binding of their cytosolic domains. Involved in vacuolar protein sorting (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral membrane protein; Cytoplasmic side Note=Phosphatidylinositol 4-phosphate-binding and oligomerization participate in the recruitment onto Golgi membranes. SIMILARITY: Belongs to the GOLPH3/VPS74 family."}
+{"protein": "MGKIRVRNNNAASDAEVRNTVFKFNKDFGQHILKNPLVAQGIVDKADLKQSDTVLEVGPGTGNLTVRMLEKARKVIAVEMDPRMAAEITKRVQGTPKEKKLQVVLGDVIKTDLPYFDVCVSNTPYQISSPLVFKLLQQRPAPRAAILMFQREFALRLVARPGDPLYCRLSANVQMWAHVKHIMKVGKNNFRPPPLVESSVVRIEPKNPPPPLAFEEWDGLLRIVFLRKNKTIGACFKTSSIIEMVENNYRTWCSQNERMVEEDFDVKSLIDGVLQQCNLQDARASKCGQTEFLSLLHAFHQVGVHFA", "text": "FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family."}
+{"protein": "MSLSPKHTTPFSVSDILSPIEETYKKFSGAMDGAPPGLGAPLGAAAAYRAPPPGPSSQAATVAGMQPSHAMAGHNAAAAAAAAAAAAAAAATYHMPPGVSQFPHGAMGSYCNGGLGNMGELPAYTDGMRGGAATGWYGANPDPRYSSISRFMGPSAGVNVAGMGSLTGIADAAKSLGPLHAAAAAAAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQLQQEGGLGPPPPPPPSPRRVAVPVLVKDGKPCQNGASTPTPGQAGPQPPAPTPAPELEELSPSPPALHGPGGGLAALDAAAGEYSGGVLGANLLYGRTW", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NK-2 homeobox family."}
+{"protein": "MNVDHEVNLLVEEIHRLGSKNADGKLSVKFGVLFRDDKCANLFEALVGTLKAAKRRKIVTYPGELLLQGVHDDVDIILLQD", "text": "SIMILARITY: Belongs to the costars family."}
+{"protein": "MEAFMVSFERQKDAKFCMYRENIPNFESTLSSITKSTNSIKILLEDISNVQKVITDPCEQSCSSCSPNVLNKFLGIEEKLVNNVEIPDSVPQKSTRPCLDDEKEGSSVVQPPESGNRHVQLISEQEFKSIPKYQLGRLTLDNLNEIVGKMDEFLTKKNAILGKTNKQITRQDREVLDNWRELEIKAKGRLPTTLFFIENDIRPLLTERLRLSFAKAIPCLRHIRRVREERCGPLTFYYA", "text": "FUNCTION: Component of the ska-1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The ska-1 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. 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. In the complex, it mediates the interaction with microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the SKA1 family."}
+{"protein": "MLLVLIDVDGFMGQLYNEKGTQTILIPREVVIFYWEKNTASKILQLFFHGGIDPIFEKINQRSFSFQSRHIHHFALDESPLPNSIALPTDTLQAFKAGKKMIFQHLVKITKDHEQILLLHKGGPEGEWVRSFNIPNATVQNLNDLCCPSVEKLVLKKKDYISSSIGCPKHIQGSNHCPVFECHVLFKWIQENTSIVQGVLERPSLPYEKAVLFIEHRINMVDNHPFKKDSIKQNQKKKNWIATQFVQHGMYVDNGILGKIYNKYSLF", "text": "SIMILARITY: Belongs to the asfivirus I267L family."}
+{"protein": "MSTLKLTLLQQPLVWLDAQANLRHFDMLLESIQQRDVIVLPEMFTTGFAMNAAENALPETEVIDWLRHWSVRTDALIGGSVALNTPDGAVNRFLLVQPDGTILRYDKRHLFRMAGEHHHYLAGKERKVVEWRGWRILPQVCYDLRFPVWSRNQQDYDLALYVANWPAARAKHWQTLLAARAIENQAYVAGCNRVGDDDNGHHYQGNSVILDALGEIQAQAEPGQAAQLDAELSLETLQAYRERFPAFHDTDKFLLL", "text": "FUNCTION: Hydrolyzes alpha-ketoglutaramate (a-KGM) to alpha- ketoglutarate (alpha-KG) and ammonia (specific activity 21 umol/min/mg), has very weak activity on L-glutamine, and no activity on deaminated glutathione (dGSH) or glutathione. May function as a metabolite repair enzyme. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family."}
+{"protein": "MATINQLVRKPRQATTYKSASPALDKCPQRRGVCTRVYTTTPKKPNSALRKVAKVRLTNQEEVISYIGGEGHNLQEHSVVLIRGGRVKDLPGVRYHTVRGSLDAAGVAKRRQGRSKYGAKRPKS", "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 (By similarity). 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. FUNCTION: With S4 and S5 plays an important role in translational accuracy. SIMILARITY: Belongs to the universal ribosomal protein uS12 family. SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
+{"protein": "MTRPPLVRGIFSLGLSVAVLKGVEKTVRKHLERQGWIEPQKVDYELIFTIDRLKNLVDNKREALTAEQPDAGELSWRKVFNFISRQSSELDARIYVLILLLSFLLPIAWTVLDGDRETTLEDKDNDCNVDLIENERRLKHYNDGERAVLQFGKNRSEPIILSYKDMNVLEGEHEFTSKEEHSNSHLTSKSENALSQVGSEDLLGCHLEKQLEEDKNEPNGEADGEDDNNREKDCSSSSEVESQSKCRKESTAEPDSLSRDTRTTSSLKSSTSFPISFKGSIDLKSLNQPSSLLHIQVSPTKSSNLDAQVNTEQAYSQPFRY", "text": "FUNCTION: Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13 (By similarity). SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass membrane protein."}
+{"protein": "MASKGIDKTIYFVRHGQVSHDVDENGVHREHDPLLNDEGRKQALQLQHDLDAEKLPIELILVSPMRRALETMKIGFQHYIEDKHIPVKVIPLLQDCGDWACNVGSYTKDLEKQFPGYDYTACHEDPVFPKKEKIYKADYKTSIQRSRVLAEFFAKVPEKVFAVVTHGVDIRLFQKIQKPEDSLDAVPKEHSFSPCQHEEFRMHYEDDKNWNFEPVK", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
+{"protein": "MAWNETKLKRLYQVWRGSNKFLCGGRLIFGPDASSLYLSTILILGPAVMFFVKMYTKMADPRTKNPNLCIPILCVSWILTILDIFFLLMTSSRDPGIVPRSFRPPETDDAPDSTTPSMEWVSGRTPNIRIPRVKDVTVNGHTVKVKFCDTCLLYRPPRASHCSICNNCVQRFDHHCPWVGQCIGVRNYRFFFMFISTSTTLCIYVFAFSWLNIFQRHMDEKISIWKAISKDVLSDILIVYCFITVWFVGGLTIFHSYLICTNQTTYENFRYRYDKKENPYNKGILGNIWEIFLSKIPPSMNKFRSFVKEEDYMMMMVETPTSNLGESLVSSKEKIDIEMGGGRIVDESGKSYSLPEILRNLNYEDLEDDCEEDDLKAKDHHHHHHHQHQHNEGIIPPFDPFFTNEIGSNKDERNGEESGGSSSDGENTGKRVRVSDEDEEKVEGYERNWSTDKGMNINAGSEDGASSPVSTSPMLRK", "text": "FUNCTION: Palmitoyl acyltransferase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
+{"protein": "MIGSVLYLVNSQMDTLSIITWLLVILPFPILGTLFLIYTKQDWGYRELKSLIKKSTQAIKPYFQYDQRILYKLKESHARTYNLAQYLHRSGGFPVYKNTKVTYFPNGQSKFEEMKKQLLKAEKFIFLEYFIIAEGLMWGEILSILEQKVQEGVEVRVMYDGMLELSTLSFDYAKRLEKIGIKAKVFSPITPFVSTYYNYRDHRKILVIDNKVAFNGGINLADEYINQIERFGYWKDTAVMLEGEGVASFTLMFLQMWSTTNKDYEFAPYLTQNFHEIVANGYVIPYSDSPLDHEKVGENVYIDILNQARDYVYIMTPYLILDSEMEHALQFAAERGVDVKIIMPGIPDKKVPFALAKRYFPALLDAGVKIYEFTPGFVHAKVFIADDIKAVVGTINLDYRSLYHHFECATYMYQTDCLVDIKADFKETLKQSRRVTRSTLQKEKISTKLIGLVVKLVAPLL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase subfamily."}
+{"protein": "MRTLWIMAVLLLGVEGSLIELGKMIFQETGKNPVKNYGLYGCNCGVGNRGKPVDATDRCCFVHKCCYKKVTGCDPKKDRYSYSWENKAIVCGEKNPPCLKQVCECDKAVAICLRENLGTYDKKHRVTVKFLCKAPESC", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that lacks enzymatic activity. Displays myotoxic activities (By similarity). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (By similarity). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane- disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (By similarity). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (By similarity). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (By similarity). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily."}
+{"protein": "MKAIIVLLMVVTSNADRICTGITSSNSPHVVKTATQGEVNVTGVIPLTTTPTKSHFANLKGTKTRGKLCPKCLNCTDLDVALGRPKCMGTIPSAKASILHEVKPVTSGCFPIMHDRTKIRQLPNLLRGYEHIRLSTHNVINAETAPGGPYKVGTSGSCPNVTNGNGFFATMAWAVPKNDNNKTATNPLTVEVPYICTEGEDQITVWGFHSDNEAQMVKLYGDSKPQKFTSSANGVTTHYVSQIGGFPNQAEDGGLPQSGRIVVDYMVQKSGKTGTITYQRGILLPQKVWCASGRSKVIKGSLPLIGERDCLHEKYGGLNKSKPYYTGEHAKAIGNCPIWVKTPLKLANGTKYRPPAKLLKERGFFGAIAGFLEGGWEGMIAGWHGYTSHGAHGVAVAADLKSTQEAINKITKNLNSLSELEVKNLQRLSGAMDELHNEILELDEKVDDLRADTISSQIELAVLLSNEGIINSEDEHLLALERKLKKMLGPSAVDIGNGCFETKHKCNQTCLDRIAAGTFNAGEFSLPTFDSLNITAASLNDDGLDNHTILLYYSTAASSLAVTLMIAIFIVYMVSRDNVSCSICL", "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": "MMAASASATTMLLKYPTTVCGIPNPSSNNNNDPSNNIVSIPQNTTNPTLKSRTPNKITTNAVAAPSFPSLTTTTPSSIQSLVHEFDPQIPPEDAHTPPSSWYTEPAFYSHELERIFYKGWQVAGISDQIKEPNQYFTGSLGNVEYLVSRDGEGKVHAFHNVCTHRASILACGSGKKSCFVCPYHGWVYGMDGSLAKASKAKPEQNLDPKELGLVPLKVAVWGPFVLISLDRSLEEGGDVGTEWLGTSAEDVKAHAFDPSLQFIHRSEFPMESNWKIFSDNYLDSSYHVPYAHKYYATELNFDTYDTQMIENVTIQRVEGSSNKPDGFDRVGIQAFYAFAYPNFAVERYGPWMTTMHIHPLGPRKCKLVVDYYIENSMLDDKDYIEKGIAINDNVQREDVVLCESVQRGLETPAYRSGRYVMPIEKGIHHFHCWLQQTLK", "text": "FUNCTION: Catalyzes the first step of the osmoprotectant glycine betaine synthesis. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the choline monooxygenase family."}
+{"protein": "MVKLGNNFAEKGTKQPLLEDGFDTIPLMTPLDVNQLQFPPPDKVVVKTKTEYEPDRKKGKARPPKIAEFTVSITEGVTERFKVSVLVLFALAFLTCVVFLVVYKVYKYDRACPDGFVLKNTQCIPEGLESYYTEQDSSAREKFYTVINHYNLAKQSITRSVSPWMSVLSEEKLSEQETEAAEKSA", "text": "FUNCTION: Plays a role in the recycling mechanism in neurons of multiple receptors, including AMPAR, APP and L1CAM and acts at the level of early endosomes to promote sorting of receptors toward a recycling pathway (PubMed:18299352, PubMed:15911354). Regulates sorting and recycling of GRIA2 through interaction with GRIP1 and then contributes to the regulation of synaptic transmission and plasticity by affecting the recycling and targeting of AMPA receptors to the synapse (PubMed:15911354). Is required for faithful sorting of L1CAM to axons by facilitating trafficking from somatodendritic early endosome or the recycling endosome (PubMed:18299352). In an other hand, induces apoptosis via the activation of CASP3 in response to DNA damage (By similarity). SUBCELLULAR LOCATION: Membrane; Single- pass type II membrane protein Golgi apparatus, trans-Golgi network membrane Endosome membrane Cell projection, dendrite Early endosome membrane Late endosome membrane Lysosome lumen Recycling endosome membrane Cytoplasmic vesicle membrane Golgi apparatus, Golgi stack membrane Endosome, multivesicular body membrane Endoplasmic reticulum membrane Note=Endocytosed from the cell surface, thus enters into early endosomes, trafficks to late endosomes and degradates in lysosomes (PubMed:28874679). Endoplasmic reticulum targeting is essential for apoptosis (By similarity). Found in both stationary and motile endosomes. A previous study supports a type I membrane protein topology (By similarity). SIMILARITY: Belongs to the NSG family."}
+{"protein": "MAARMGVLSVAGFRAAARAGGLLARPKQSTAVVPCRTVIASSAGAILPKPEKVSFGLLRVFTVVIPFLYIGTLISKNFAAVLEEHDIFVPEDDDDDD", "text": "FUNCTION: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria. Plays a central role in regulating the uniplex complex response to intracellular calcium signaling. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMDT1/EMRE family."}
+{"protein": "MGEEEEKKEKGDEIITAVYKVHLHCRKCACDIKKPLLRFQGVQNVDFDLEKNEIKVKGKIEVVKIHKQIEKWSKKKVELISPKPSEVKKTTTTTTTTSVVEKKTTEIKKDVIRTTVLKVHIHCAQCDKDLQHKLLKHKAIHIVKTDTKAQTLTVQGTIESAKLLAYIKKKVHKHAEIISSKTEEEKKKEEEDKKKKEEEDKKKKEDEKKKEEEKKKEEENKKKEGEKKKEEVKVEVTTKTITQVVEYKEIVKVEGQKDKDGNIPYFVHYVYAPQLFSDENPNACRIV", "text": "FUNCTION: Heavy-metal-binding protein. SIMILARITY: Belongs to the HIPP family."}
+{"protein": "MVRFQRRKLLASCLCVTATVFLMVTLQVVVELGKFERKKLKDSNVQDGHRDVEGEPKHLEPFPEKEALALAGRTKVDAGSYPIVLWWSPLTGETGRLGQCGADACFFTINRTFQHHPMTRAFLFYGTDFNIDSLPLPREAHHDWALFHEESPKNNYKLFHKPVITLFNHTATFSRHSHLPLTTQYLEGVDVLKSLRYLVPLQAKNNLRQKLAPLVYVQSDCDPPSDRDSYVRELMAYIEVDSYGECLQNRDLPQQLKNPASMDADAFYRVIAQYKFILAFENAVCDDYITEKFWRPLKLGVVPVYYGSPTIADWLPSNRSAILVSEFSHPRELASFIRRLDYDDGLYETYVEWKLKGKISNQRLLTALNEREWGVQDINQDNYIDSFECMVCRRVWANSRLQEQGLPPKQWKADVSHLHCPEPALFTFSSPASPALRGRSLRELWLPSFQQSKKEAQALRWLVDRNQNFSSEEFWALVFKD", "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 (PubMed:23986452). 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": "MDISYPVINAGGLKNIASQIIMEIELDKRENRPTDNVPPDDIGKIEVVDDAEMEQFYGSSTTDAYRLKSELVSQCMADIGMGRFQWKLFTVAGFGWIVDNFCSQGISAVQPPIQQEFSGIKQVSYSSVAYYVGMIIGASFWGISSDLIGRKPAFNSTLAIAGIFLCAAAGTSNFIAFSALWAVIGTAAGGNVVCDSMILLEFIPGSHQYLLTALSGWWNLGQLVVSLLAWVFLANFSCPTDATPDTCSRADNMGWRYTLITLGGLSLAFTFVRIFVFKMPETPRYLLSQGNDQAAVDAVNYVARQNGKPEPLTLSMLQAIDVRLGFTPNAEERLSTKDILKENMQEFRGEHYQALFATRKLSQHTALIWAVWLIIGIAYPLYFNFLPSYLATRFTQDSSLDLTYRNYCIQSAVGVVGPLSAAVLVNTFLGRRWMMGISSIVTGVFLFAYVGVKTPMSSLAFSCVTGLLANFANQLSEYAIMYAFTPESFPAPHRGTASGTAASLLRFGGLVASLIASETGFTTAPIYASAALWVGVGVLCFGLPFETHGHAAI", "text": "FUNCTION: Major facilitator-type transporter, part of the hnx cluster involved in the purine degradation (PubMed:29212709). The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism (PubMed:29212709). The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid (PubMed:29212709). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MAVRLMKRCTCLLREATRLVPTVAPVGRLRLAGVSCKTLTSSVSSPSSGSLAELLGKEQVFTPYPEHQELDFLIEKASRPEQLLELLGSDHSLHHNHAALILIRLSYLLSEKPKEKALLAEDARFQRLVKLVDSQITCVWHGTLVKLLRSLYTLVLPQISKELQSVEQEVRWRLRRLKYKHLVFLAESCASFMKEQHSQELLAELLMHLERRWTEINDSRTLVTMMTMAGHLSESLMNHLEDKCLELVEQFGPDELRKVLVTLAAQSRRSVPLLRAISYHLVQKPFPMTKGMLLDLAYAYGKLSFHQTQVSQRLAADLLPFIPSMTPGEVARCAKSFAFLKWLNLPLFEAFTQHLLSRVQDVSLSHVCSVLLAFARLNFHPEQEEDQFFSMVHEKLDPVLGSLEPALQVDLVWALCVLQHVHETELHTVLHPGLHARFLESKSPKDQSTFQKLVHINTTALLEHPEYKGPFLPASAVAPIPSPSNKKMTPLQKELQETLKALLGNTDKGSLEVATQYGWVLDAEVLLDADGHFLPLRNFVAPHLAQPVGNQPLPPGAKRIAFLRWEFPNFNSRSKDLLGRFVLARRHVLAAGFLVVDVPYYEWLDLKSEWQKSAYLKDKMRKAMAEELAK", "text": "FUNCTION: Plays a role in processing of mitochondrial RNA precursors and in stabilization of a subset of mature mitochondrial RNA species, such as MT-CO1, MT-CO2, MT-CYB, MT-CO3, MT-ND3, MT-ND5 and MT-ATP8/6. May play a role in cell cycle progression. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the FAST kinase family."}
+{"protein": "MAEAATPGTTATTSGAGAAAATAAAASPTPIPTVTAPSLGAGGGGGGSDGSGGGWTKQVTCRYFMHGVCKEGDNCRYSHDLSDSPYSVVCKYFQRGYCIYGDRCRYEHSKPLKQEEATATELTTKSSLAASSSLSSIVGPLVEMNTGEAESRNSNFATVGAGSEDWVNAIEFVPGQPYCGRTAPSCTEAPLQGSVTKEESEKEQTAVETKKQLCPYAAVGECRYGENCVYLHGDSCDMCGLQVLHPMDAAQRSQHIKSCIEAHEKDMELSFAVQRSKDMVCGICMEVVYEKANPSERRFGILSNCNHTYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEEKEEKQKLILKYKEAMSNKACRYFDEGRGSCPFGGNCFYKHAYPDGRREEPQRQKVGTSSRYRAQRRNHFWELIEERENSNPFDNDEEEVVTFELGEMLLMLLAAGGDDELTDSEDEWDLFHDELEDFYDLDL", "text": "FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase. Has negative and positive effects on RNA polymerase II- dependent transcription."}
+{"protein": "MVNVKKGVLVTSDPAFRQLLIHLDDSRQLGSKFIVRELDDTHLFIEKEIVPMLENKVEQIMENMNPEAVDK", "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 in RNA transcription by RNA polymerase II (By similarity). 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 (By similarity). In transcription, TFIIH has an essential role in transcription initiation (By similarity). When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape (By similarity). Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell (PubMed:34824371). Required for efficient binding of TFIIH to damaged DNA (PubMed:34824371). Dispensable for normal development, but required when transcription is challenged (PubMed:34824371). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localized to paired homologous chromosomes (bivalents) about 10 minutes after UV irradiation, but localization is lost after 35 minutes, probably as a result of successful DNA damage repair as part of the TFIIH complex. SIMILARITY: Belongs to the TFB5 family."}
+{"protein": "MPVRFRGLSEYKRNFRWKTPELCSPSQEQKSPWAGLRSDQLGITREPNFISKRRVPYHNPQISKSFEWTGDCDSDDPVETEALKTAESLAEHSNDVNQENTETPEGPRLPPKVRSHSSDSGVETALALAGNSMKKTPPVAPPNQKEAFVSPKKEAEKVNNGLHRVLQRKGGMNTPHLSTFPRNSEYQSQFVWKSPHEKSPILAAEEALYNTKREELIQKPAEDASKQEKSEQKHPKRKNKQHISQKPLSLHTHRGKMNTEYRSKFLSPAQYFYKDGAWSRIRSKVPNQASQNPLNSMWYMEVRELRARAKAYRQRIEGTHFSRYHLNQLLSDNNSLWDVSSNSSSEEGISNDIRALDLAGVSEKETAPRPKMLQQPGSREQSHQDDTEKKGLSDAPTVPVKRRLVWGEQEGTAEKDSQQLREEEEKENEQAAVVTQNLEKNNEGINEDNRIEGENTCLPNSPAAVSESSSVSSEPGGRLPTPKLRALGRAQRTHHDLTTPAVGGAVLVSPPKFKSSTSQQRMRSLGTDPSSVGQGAREASQRRSFRPGAKLKAVSLLTSPPAGLGTVDPLPLRQDQWHPNGVSGETVAINSAYQERSSTPPVLKSTKNRPMPCWSPSPRIQGTLKDPEFQHNGNVGNPKMGSFQLPLQERNYNNEDDRLSQISARSAASSSLASQILERAQKRKEDFWGKT", "text": "FUNCTION: Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localizes to the centriole lumen. SIMILARITY: Belongs to the MDM1 family."}
+{"protein": "MGTVHARSLEPLPSSGTDFGALGEEAEFVEVEPEAKQEILENKDVVVQHVHFDGLGRTKDDIIICEIGEVFKAKNLIEVMRRSHEAREKLLRLGIFRQVDVLIDTCHGEDALPNGLDVTFEVTELRRLTGSYNTMVGNNEGSMVLGLKLPNLLGRAEKVTFQFSYGTKETSYGLSFFKPQPGNFERNFSVNLYKVTGQFPWSSLRETDRGVSAEYSFPLWKTSHTVKWEGVWRELGCLSRTASFAVRKESGHSLKSSLSHAMVIDSRNSSILPRRGALFKVNQELAGYTGGDVSFIKEDFELQLNKPLALDSVFSTSLWGGMLVPIGDKPSSIADRFYLGGPTSVRGFSMHSIGPQSEGDYLGGEAYWAGGLHLYTPLPFRPGQGGFGELFRTHFFLNAGNLCNLNYGEGPKAHIRKLAECIRWSYGAGVVLRLGNIARLELNYCIPMGVQGGDRICDGVQFGAGIRFL", "text": "FUNCTION: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes. Required for the assembly of TOMM40 into the TOM complex. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Cytoplasm Mitochondrion. SIMILARITY: Belongs to the SAM50/omp85 family."}
+{"protein": "MQLTRLVQVDCPLGPDVLLLQRMEGREELGRLFAYELHLVSENPNLPLEQLLGKPMSLSLELPGGSRRFFHGIVARCSQVAGHGQFAGYQATLRPWPWLLTRTSDCRIFQNQSVPEIIKQVFRNLGFSDFEDALTRPYREWEYCVQYRETSFDFISRLMEQEGIYYWFRHEQKRHILVLSDAYGAHRSPGGYASVPYYPPTLGHRERDHFFDWQMAREVQPGSLTLNDYDFQRPGARLEVRSNIARPHAAADYPLYDYPGEYVQSQDGEQYARNRIEAIQAQHERVRLRGVVRGIGAGHLFRLSGYPRDDQNREYLVVGAEYRVVQELYETGSGGAGSQFESELDCIDASQSFRLLPQTPVPVVRGPQTAVVVGPKGEEIWTDQYGRVKVHFHWDRHDQSNENSSCWIRVSQAWAGKNWGSMQIPRIGQEVIVSFLEGDPDRPIITGRVYNAEQTVPYELPANATQSGMKSRSSKGGTPANFNEIRMEDKKGAEQLYIHAERNQDNLVENDASLSVGHDRNKSIGHDELARIGNNRTRAVKLNDTLLVGGAKSDSVTGTYLIEAGAQIRLVCGKSVVEFNADGTINISGSAFNLYASGNGNIDTGGRLDLNSGGASEVDAKGKGVQGTIDGQVQAMFPPPAKG", "text": "FUNCTION: Part of the H1 type VI secretion system (H1-T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (PubMed:21325275, PubMed:24794869). Forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein 1/Hcp1 (PubMed:26894531). Allows the delivery of the Tse6 toxin to target cells where it exerts its toxicity (PubMed:30177742). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the VgrG protein family."}
+{"protein": "MSYYGSSYRIVNVDSKYPGYPPEHAIAEKRRARRRLLHKDGSCNVYFKHIFGEWGSYMVDIFTTLVDTKWRHMFVVFSLSYILSWLIFGSIFWLIALHHGDLLSDPDITPCVDNVHSFTAAFLFSLETQTTIGYGYRCVTEECSVAVLTVILQSILSCIINTFIIGAALAKMATARKRAQTIRFSYFALIGMRDGKLCLMWRIGDFRPNHVVEGTVRAQLLRYSEDSEGRMTMAFKDLKLVNDQIILVTPVTIVHEIDHESPLYALDRKAVAKDNFEILVTFIYTGDSTGTSHQSRSSYVPREILWGHRFHDVLEVKRKYYKVNCLQFEGSVEVYAPFCSAKQLDWKDQQLNNLEKTSPARGSCTSDTNTRRRSFSAVAMVSSCENPEETSLSPQDECKEVPYQKALLTLNRISMESQM", "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. KCNJ16 may be involved in the regulation of fluid and pH balance (By similarity). In the kidney, together with KCNJ10, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Basolateral cell membrane Note=In kidney distal convoluted tubules, located in the basolateral membrane in the presence of KCNJ10. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ16 subfamily."}
+{"protein": "MSSTLTCYCPGDGSLLGEVKLFNKSDIDQSIILAEEAQKEWKSTSFAERRNFLKALKENIIRNQDKYAEIACKDTGKTLVDAAFGEILVTLEKINWTLANGEQSLRPTKRPNSLLTSYKGGYVKYEPLGVIAALVSWNYPLHNALGPIISALFAGNAIVVKGSELTAWSTHQYCEMVRSLLQSMGHSPELVQCITCLPDVADHLTSHSGIKHITFIGSQPIAKLVAASAAKQLTPLCLELGGKDPCILTDDHRLEEILSIVMRGVFQSAGQNCIGIERIIALDGVYDTIITKLYNRISTMRLGMYTQNDVDMGAMVSNNRFDHLESLIQDAVSKGARLVYGGHRFQHPKYPKGNYFLPTLLVDATNEMKIAQEECFAPIALVFRAKSPEHALEIANGTEFGLGASVFGRDKQLCQYFTDNLETGMVAVNDFGAFYLLQMPFGGCKKSGYGRFAGYEGLRGICNSKAIAYDRFSAIHTGIPPAVDYPIPDSQKAWQFVRGLMGTVYGAWISLVPNVYQLWRNS", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
+{"protein": "MTEHYDVVVLGAGPGGYVSAIRAAQLGKKVAVIEKQYWGGVCLNVGCIPSKSLIKNAEVAHTFTHEKKTFGINGEVTFNYEDAHKRSRGVSDKIVGGVHYLMKKNKIIEIHGLGNFKDAKTLEVTDGKDAGKTITFDDCIIATGSVVNTLRGVDFSENVVSFEEQILNPVAPKKMVIVGAGAIGMEFAYVLGNYGVDVTVIEFMDRVLPNEDAEVSKVIAKAYKKMGVKLLPGHATTAVRDNGDFVEVDYQKKGSDKTETLTVDRVMVSVGFRPRVEGFGLENTGVKLTERGAIEIDDYMRTNVDGIYAIGDVTAKLQLAHVAEAQGIVAAETIAGAETQTLGDYMMMPRATFCNPQVSSFGYTEEQAKEKWPDREIKVASFPFSANGKAVGLAETDGFAKIVADAEFGELLGAHLVGANASELINELVLAQNWDLTTEEISRSVHIHPTLSEAVKEAAHGISGHMINF", "text": "FUNCTION: Lipoamide dehydrogenase is an essential component of the pyruvate dehydrogenase (PDH) and 2-oxoglutarate dehydrogenase (ODH) complexes. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Also catalyzes a reversible NADH:NAD(+) transhydrogenation, and is able to transfer electrons from NADH to various redox-active compounds and quinones. May be involved in quinone redox cycling in C.glutamicum. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MLIPVVCFTCGFPIGTYAAIFDKARTEYIKTKMDGTLPQNIPLDASLQIELKDLITALGIPMRVCCRTHLITTLDYRKYY", "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. SIMILARITY: Belongs to the archaeal RpoN/eukaryotic RPB10 RNA polymerase subunit family."}
+{"protein": "MNGSPTPKRYSSKSSRLYDDYYNIPYQYSNPTPMNRDYNDVGSRINADKLVPEEYKRNTEFINKAVQQNKELNFKLREKQNEIFELKKIAETLRSKLEKYVDITKKLEDQNLNLQIKISDLEKKLSDANSTFKEMRFPKVKDPMVDDDPVSENYDQINVPKHRAPDATGNPRTTNKVSNTSDQDSRLKAIERTLSVLTNYVMRSEDGNNDRMSPLPSPLNTILPINNRLNFQEPKRYNPTVKVNPSDDDIMMYESAELKRVEEEIEELKRKILVRKKHDLRKLSLNNQLQELQSMMDGDDNIKLDNVSKHNHATHRHSSQSSRDYSPSSDACLECSNDLYEKNRVKPENNMSETFATPTPNNR", "text": "FUNCTION: Forms a polymeric layer at the periphery of the spindle pole body (SPB) central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. SIMILARITY: Belongs to the SPC42 family."}
+{"protein": "MSSVLINSIAVLAGLGFAVGVMLVIASKVFKIDSNPLIDDVASLLPGANCGGCGFAGCAACAEAIVEQGAPVNSCPVGGFEVAKQIGALLGQEVTESEKEFPFVRCQGGNQHCTTLYDYHGVENCKVALMLCDSRKGCTYGCLGLGTCVQACQFGALSMGEDGFPVVNKALCTSCGNCIAACPNGVLTFARDSEKVHVLCRSHDKGKDVKAVCEVGCIGCKKCEKECPAGAIRVTEFLAEIDQEKCTACGACVAICPQKAIELR", "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; Single-pass membrane protein. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily."}
+{"protein": "MKKIEIEPMTRLEGHGKIAIFLDDKGNVADAFYQIVEFRGYETFLRGLPIEEVPRTVSTICGVCRAVHHTASTKASDGVYGVEPTETAKKIRELYLNAHYVEDHCAILYALGLPDFVVGIEADPAERNLVGLIKKVGVDVGKTVLKKRFAAVKVLEMLGGKPIHPVAGLPGGWSKRITEDERKEIEALAKEMVELGELTLQVFEDVILKNEKLLELITADYYRVVVNYLGTVDDAGKVNYYDGWQVGIDTKGNEVFRFKGKDYLNYIAERVVPWSYVKMPYFKQLGWKGFVDGEGTSLYSVGPLARCNIGDMNTPKAKEAQEKMFDVLKERPIHYIMAYHWARAVELLNAAERVLELAQDPEITSPDVRAELGEVTGEGVGIIEAPRGTLIHHYKTDENGIVTDANLIVATTHNHAPINIAIKKAAQHFIQENKEINDKLLNYVEIAYRPYDICQACASHALPGRYPLEVLVYDSEGELIKTIRNF", "text": "FUNCTION: Part of a complex that provides reducing equivalents for heterodisulfide reductase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family."}
+{"protein": "MAYVKGGVWTNVEDEILRAAISKYGLNQWARVSSLLARKTAKQCKARWTEWLDPTIKKIEWSREEDEKLLHLAKIFPAQWRTIAPFVGRTAHQCIQRYERLLAEVAGEVEGEDASAVASAPATEGDQFPETKPARPDAVDMDEDEKEMLSEARARLANTQGKKAKRKDRERMLEDSRRLSQLQKRRELKNAGIDTRLSKRKKNEMDYNADIPFEHKPARGFYSTAEEEHENDSERLQHKQMHRTAADAPGPSQKRDKATLSKEDEEKKKEQQKTASAQRTLQLAQLDLQDQISKRRKLNLPEPQIQDQEMEEIVKLGAQGEALHKRYADGVASSLSGDYDDKIVDDSIRTPQIQQSKVKTTIEEIKAMENRSVLGKRTEEEVDDEAEADKDGFAIPKLPSNKAVTSVSAGSDIGGATPAGMTPIKRDALGLVGSVEATPVSILRQKLASLPKPKNDFEITAEDEEEDEEADKEKKPTDNLPVDKGEQARLKRIAEEQERQEALKTRSQTLQRGLPRATVPEVTYNDAIGQEVVALLREEELRFPNKGDSVALMQSEFSLDDLVDAETLIEMELMEGDEQEVQEEGIKTAALPGTVARSDESEEEFKTRVEIISDQLVETLTSLAETCQTEETALVDKFKAYAKRQATLSKKLTSRWSQLESVEVEIAVFSELARMEEIAIEQRSAALQEEVDWLVKKERAAQDKYRELKVKEQAAKGGH", "text": "FUNCTION: Involved in pre-mRNA splicing and cell cycle control. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CEF1 family."}
+{"protein": "MSDNSQKKVIVGMSGGVDSSVSAYLLQQQGYQVAGLFMKNWEEDDDEEYCSAATDLADAQAVCDKLGMELHTVNFAAEYWDNVFELFLAEYKAGRTPNPDILCNKEIKFKAFLEFAAEDLGADYIATGHYVRRQDVDGKSRLLRGLDGNKDQSYFLYTLSHEQIAQSLFPVGELEKPEVRRIAEQLDLVTAKKKDSTGICFIGERKFRDFLGRYLPAQPGPIMTVDGQLVGKHQGLMYHTLGQRKGLGIGGTKEGGDDPWYVVDKDLDSNTLLVAQGHEHPRLMSVGLVAQQLHWVDRQPVTAPFRCVVKTRYRQQDIPCTVTPLDDERVDVRFDDPVAAVTPGQSAVFYQGEICLGGGIIEQRYPLTNPA", "text": "FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmA/TRMU family."}
+{"protein": "MSRRLLPRAEKRRRRLEQRQQPDEQRRRSGAMVKMAAAGGGGGGGRYYGGGSEGGRAPKRLKTDNAGDQHGGGGGGGGGAGAAGGGGGGENYDDPHKTPASPVVHIRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGGPHGGYHSHYHDEGYGPPPPHYEGRRMGPPVGGHRRGPSRYGPQYGHPPPPPPPPEYGPHADSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKLNVCVSKQPAIMPGQSYGLEDGSCSYKDFSESRNNRFSTPEQAAKNRIQHPSNVLHFFNAPLEVTEENFFEICDELGVKRPSSVKVFSGKSERSSSGLLEWESKSDALETLGFLNHYQMKNPNGPYPYTLKLCFSTAQHAS", "text": "FUNCTION: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023). Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts (PubMed:2687284). Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter (PubMed:11809897). As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Cytoplasm Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules."}
+{"protein": "MESQVRQNFHKDCEAAINRQINLELYASYSYLSMAYYFDRDDVALPGFAHFFKQQSEEEREHAEKLLKFQNQRGGRIFLQDVKKPDRDEWGSGLDALECALQLEKNVNQSLLDLHKVCSEHNDPHMCDFLETHYLDEQVKSIKELGDWVTNLRRLGAPQNGMAEYLFDKHTLGK", "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. 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": "MITPIIMAGGNGSRLWPLSRTLYPKQFLCLDGSQSMLQTTITRINNLNASDPIVICNEQHRFIVAEQLKELSKSSGDIILEPVGRNTAPAVALAALKCLKKNALLLVLAADHIIKDEETFCKTIQDARKYAEAGKLVTFGIVPTMPETGYGYIRRGQALFSAENDCSLAFRVAEFVEKPNLETAQSYLDSGEYYWNSGMFLFRADRYIEELKIRPDIYKACSLAMESAVTDLDFIRVDEDSFCACPDESIDYAVMEKTNDAVVVPLNAGWSDVGSWSSLWEISDKDSNGNVTKGDVLSHNADNCYLHAETGLVTAVGVKDLIVVQTKDAVLVANTNCVQDVKKIVEKIKLENRHEHITHREVYRPWGKYDSIDFGERYQVKRITVKPGEGISEQQHYHRAEHWIIVAGTAKITIKGEVKILTENESVYIPVGVKHCLENPGKIALELIEVRSGAYLGEDDIVRFSDKYGRN", "text": "FUNCTION: Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS O antigen. SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family."}
+{"protein": "MSDYEEAFNDGNENFEDFDVEHFSDEETYEEKPQFKDGETTDANGKTIVTGGNGPEDFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEELIVDL", "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 polymerases are composed of mobile elements that move relative to each other. In Pol II, 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. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family."}
+{"protein": "MHRRAAIQESDDEEDETYNDVVPESPSSCEDSKISKPTPKKRRNVEKRVVSVPIADVEGSKSRGEVYPPSDSWAWRKYGQKPIKGSPYPRGYYRCSSSKGCPARKQVERSRVDPSKLMITYACDHNHPFPSSSANTKSHHRSSVVLKTAKKEEEYEEEEEELTVTAAEEPPAGLDLSHVDSPLLLGGCYSEIGEFGWFYDASISSSSGSSNFLDVTLERGFSVGQEEDESLFGDLGDLPDCASVFRRGTVATEEQHRRCDFGAIPFCDSSR", "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 II-e family."}
+{"protein": "MSTPFGLDLGNNNSVLAVARNRGIDVVVNEVSNRSTPSLVGFGPRNRYLGESGKTKQTSNVKNTVENLKRIIGLKFKDPEFDIENKFFTSKLVQLKNGKVGVEVEFGGKTHVFSATQLTAMFIDKVKHTVQEETKSSITDVCLAVPVWYSEEQRYNIADAARIAGLNPVRIVNDVTAAAVSYGVFKNDLPGPEEKPRIIGLVDIGHSTYTCSIMAFRKGEMKVLGTAYDKHFGGRDFDRAITEHFADQFKDKYKIDIRKNPKAYNRILIAAEKLKKVLSANTTAPFSVESVMDDIDVSSQLSREELEELVEPLLKRVTYPITNALAQAKLTVNDIDFVEIIGGTTRIPVLKKSISDVFGKPLSSTLNQDEAVAKGAAFICAIHSPTLRVRPFKFEDIDPYSVSYTWDKQVDDEDRLEVFPANSSYPSTKLITLHRTGDFSMKAVYTHPSKLPKGTSTTIAKWSFTGVKVPKDQDFIPVKVKLRCDPSGLHIIENAYTTEDITVQEPVPLPEDAPEDAEPQFKEVTKTIKKDVLGMTAKTFALNPVELNDLIEKENELRNQDKLVAETEDRKNALEEYIYTLRAKLDDEYSDFASDAEKEKLKNMLATTENWLYGDGDDSTKAKYIAKYEELASLGNIIRGRYLAKEEEKRQALRANQETSKMNDIAEKLAEQRRARAASDDSDDNNDENMDLD", "text": "FUNCTION: Has a calcium-dependent calmodulin-binding activity. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MTSRYRVEYALKSHRRDEFIEWIKGLLATPFVLHADDSHADAQIVAENCQARYYEIFKDVESLVKQTIFLDELNELDPKKKSISRLRTLVPSLGKFFTELPLADAFLLEDERRAISKRRLVSPSFNDVRMILNTAQIMALTNIYKQTENNINGISGKNQQQQQQKLKLITFDGDVTLYEDGKSLDENSEVVQRLVKLLSLGLYVGVVTAAGYPRQSGAEKYYERLKGLIDHLNSNHCTLKTYQKENLLVMGAESNYLFRYNNEMKGLKFIDDEEWFLPQVKNWNIGKINYIMDTLYKHLIYLRNNFNLEDSTTIIKKERSVGIIPNSGCRILREQLEEMVLSCSRKLNTILTSSSNFADSTEALCVDDIKVCAFNGGSDVWVDIGDKALGVESLQKYICHDETVDHVCPIGKSESLHIGDQFASLGANDFKARLSACTVWIASPRETVAILDDLIDFIEG", "text": "FUNCTION: IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation. SIMILARITY: Belongs to the ISN1 family."}
+{"protein": "MSDKPKTKPLPSFVEGRLDFYIQDLIEQNENQKHLVLGKRPQQGAVVMQSNDYLSLSHNLQIQQAHRDAIYEHDDNVVMSAIFLQDDDSKPAFETQLAEYVGMGSCLLSQSGWAANIGLLQTICPPETPVYIDFFAHMSLWEGIRAAGAQAHPFMHNNMNHLRKQIQRNGSGVIVVDSVYSTIGTIAPLRDIYEMAREFDCALVVDESHSLGTHGPNGSGLVKALELTEQVDFITVSLAKTFAYRAGAILGPEKLARTLPFVAFPAIFSSTVLPQEIVRLEKTLEVIRSADDKRTMLFKRAKELRTGLKQIGFHIRSESQIVALECGSERNTERVRDFLEERNVFGAVFCRPATGKNKNIIRFSINADMTSRDIDHVLTACQEAYNHPELEFA", "text": "FUNCTION: Required for the synthesis of the quorum-sensing autoinducer CAI-1 ((S)-3-hydroxytridecan-4-one) which probably functions as an intragenus signal. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MAKKTNYVKNGKEYYRVTVTIGRDENGKLIRKEFYGKTKKEAEAKKEEYLNGIRNGLNVDFQDVTLGDLMHTWLFEVVRMSRKPATFVKYEGHYRNYIKNSELYGMKISIIKSIQIQRYYNKLYQQGKSSKTIKALNNFLKTFFNYAVDEGYLAKNPCTGKKIVIPGTPEEKIETEIETFSDEEIKKIKEALKGHRLKALFLLAFGTGLRQGELLGLKWTDIDFEKKELRVQRMIKQVTIIDEKGNRKYKTIEQIPKTKNSIRTVPIPSSLIPMLKEHRNRQREEKLKAGSVYLNDVEKGYVFTTELGNTIDASNLLKTYKKILNRAGVPYRKFHAIRHTYATKLFERGVPLKTVSELLGHSNISITANIYTHVIPKQKTNAVETLNDLFI", "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."}
+{"protein": "MSEELPQIEIVQEGDNTTFAKPGDTVTIHYDGKLTNGKEFDSSRKRGKPFTCTVGVGQVIKGWDISLTNNYGKGGANLPKISKGTKAILTIPPNLAYGPRGIPPIIGPNETLVFEVELLGVNGQ", "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 FKBP-type PPIase family. FKBP1 subfamily."}
+{"protein": "MSRRRISCKDLGHADCQGWLYKKKEKGTFLSNKWKKFWVVLKGSSLYWYSNQMAEKADGFVNLSDFTVERASECKKKNAFKINHPQIKAFYFAAENLQEMNVWLNKLGFAVTHQESITKDEECYSESEQEDPEVAVEAPPPPYASTTSSPVAAQWASSSSPKRRETSCSFSSLENTVKAPSQFSSSGSKERQSWHNIVNSSPATEDAGLPLTFAEQVHTLAFSEASNCQAPENNCITSEGGLLNLLSSDDTSSLNNNKDHLTVPDRAAGSRMADREEIKSSEDDEMEKLYKSLEQASLSPLGDRRPSTKKELRKSFVKRCKNPSINEKLHKIRTLNSTLKCKEHDLAMINQLLDDPKLTARKYREWKVMNTLLIQDIYQQQAPQDPEVTPQEVMNPTSSDCVENSL", "text": "FUNCTION: Enhances the promotion of guanine-nucleotide exchange by PSCD2 on ARF6 in a concentration-dependent manner. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Translocated with PSCD2 to the plasma membrane upon epidermal growth factor (EGF) stimulation."}
+{"protein": "MAVKWTGGHSSPVLCLNASKEGLLASGAEGGDLTAWGEDGTPLGHTRFQGADDVTSVLFSPSCPTKLYASHGETISVLDVRSLKDSLDHFHVNEEEINCLSLNQTENLLASADDSGAIKILDLENKKVIRSLKRHSNICSSVAFRPQRPQSLVSCGLDMQVMLWSLQKARPLWITNLQEDETEEMEGPQSPGQLLNPALAHSISVASCGNIFSCGAEDGKVRIFRVMGVKCEQELGFKGHTSGVSQVCFLPESYLLLTGGNDGKITLWDANSEVEKKQKSPTKRTHRKKPKRGTCTKQGGNTNASVTDEEEHGNILPKLNIEHGEKVNWLLGTKIKGHQNILVADQTSCISVYPLNEF", "text": "SIMILARITY: Belongs to the WD repeat WDR53 family."}
+{"protein": "MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGGHFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNGYGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPVTNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRN", "text": "FUNCTION: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
+{"protein": "MLDFLELEETVGRAWHRLIGKTGSWPQYPDHAVQLVDIRQRLAICFRGFGGDIAVQIAPARARTSTHRLGLRQRMALGEEKLAQPLRDEATLMLPPEIALFPDRQLNYDLYVWLVGYMAVMPMDADALPEDALRRDLAALQIAEQTVERACRAFPGLKPRYKRLCAAILAERPKRPLHRLEQQVEARILSLLKQGADLPDDALPTIFPHRGPAGYLPALPVPLWPGLMKREEVAPRTGEDEPVRNSQSEGAETGRQIAQRERQDPRHADRSPFILNRFEKILAMAEMVSVDRPSDGSDEQNAKSADELDDLTLGERKGRPAARFRFDLDLPPEAVDRSLLTAELTYPEWDYRKGAYLPNHCAVLAAPVQEKEKPLELDAAAQSLVRRVRRQFEILRPGREVLRAQLDGTDLDLDAVVRSRCDLAAGGQGSDRVHLMSRPQANDLAVTLLVDVSLSTDAWVDNRRVLDVEKEALLVLANGIAACGDRCSILTFTSRRRSWVRVETVKDFDESFGPTVEHRIAALKPGFYTRMGAAMRHATAKLAEQPNRKKLLLLLTDGKPNDVDHYEGRFALEDSRRAAGEVRAKGVNVFAVTVDREASAYLPALFGRGGYALVANLAKLPVALPAIYRMLAG", "text": "FUNCTION: Part of the operon norEFCBQD encoding nitric oxide reductase. Essential virulence factor, probably involved in the detoxification of nitric oxide (NO) produced in the macrophages during the innate response against infection (By similarity)."}
+{"protein": "MNRSRQVTCVAWVRCGVAKETPDKVELSKEEVKRLIAEAKEKLQEEGGGSDEEETGSPSEDGMQSARTQARPREPLEDGDPEDDRTLDDDELAEYDLDKYDEEGDPDAETLGESLLGLTVYGSNDQDPYVTLKDTEQYEREDFLIKPSDNLIVCGRAEQDQCNLEVHVYNQEEDSFYVHHDILLSAYPLSVEWLNFDPSPDDSTGNYIAVGNMTPVIEVWDLDIVDSLEPVFTLGSKLSKKKKKKGKKSSSAEGHTDAVLDLSWNKLIRNVLASASADNTVILWDMSLGKPAASLAVHTDKVQTLQFHPFEAQTLISGSYDKSVALYDCRSPDESHRMWRFSGQIERVTWNHFSPCHFLASTDDGFVYNLDARSDKPIFTLNAHNDEISGLDLSSQIKGCLVTASADKYVKIWDILGDRPSLVHSRDMKMGVLFCSSCCPDLPFIYAFGGQKEGLRVWDISTVSSVNEAFGRRERLVLGSARNSSISGPFGSRSSDTPMES", "text": "FUNCTION: Chromatin-associated factor that regulates transcription (PubMed:29065309). Regulates Pol I-mediated rRNA biogenesis and, probably, Pol III-mediated transcription (PubMed:29065309). Regulates the epigenetic status of rDNA (PubMed:29065309). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Chromosome Note=Associates with chromatin regions of rDNA. SIMILARITY: Belongs to the WD repeat PWP1 family."}
+{"protein": "MADDVSEFLGQNPETAAWLELVHGECESDKLWRYRKEFILRNLSDVCGEAEVPPPPETNHKALDRLLAYSMVWANHVFTGCRYPLPVMEKVLKMAENIKVTDAPTHTTRDELVAKVKKRGISSSNEGVEEEPCKKQKSSDHGERESSYIEDTISDGNVPSTSLNKREARLSAAQRTDVNTEFYDKSSNRRSLPVSNAKSRLNLPEEAGYKHGATQGRKSHSDIRHQTSMKGPAQSSDNALKPTRRFTTEHTKERQPFFNRLYKTVAWKLVSAGGFNANLNHEELLNTCIESLKATLEVSFVPLTDLADLPQNKTSQENTVCELRCKSVYLGMGCGKTMETAKAVASREAVKLFLKKKVVVRICKRKFNGRDVEDLVLVDEEFRPVNLPPAIKNPQEIV", "text": "FUNCTION: May regulate DNA damage response and cell proliferation. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the CARF family."}
+{"protein": "MSMDVTFLGTGAAYPSPTRGASALVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSGSMVTKQPIEIYGPVGLRDFIWRTMELSHTELVFPYVVHELVPTADQCPTEELQESVQVDKTDNPPKEGEGRTILLDSEENSYLLVDDEQFVVKAFRLFHRIPSFGFSVVEKKRPGKLNAQKLKDLGVPPGPAYGKLKNGISVVLENGVTISPQDVLKKPIVGRKICILGDCSGVVDDAGVKLCFEADLLIHEATLDDTQMDKAKEHGHSTPQMAATFAKLCQAKRLVLTHFSQRYKPVALAREGEADGIVELKKQAESVLDLQEVTLAEDFMVISIPIKK", "text": "FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Specifically involved in tRNA repair: acts downstream of the ribosome-associated quality control (RQC) pathway by removing a 2',3'-cyclic phosphate from tRNAs following cleavage by ANKZF1. tRNAs are then processed by TRNT1. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=Mainly cytosolic. SIMILARITY: Belongs to the RNase Z family."}
+{"protein": "MNLLQVVRDHWVHVLVPMGFVFGYYLDRKNDEKLTAFRNKSLLYKRELKPNEEVTWK", "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 NDUFB1 subunit family."}
+{"protein": "MNLGDPDFVDVSKVISDMLSTNFAQGLKKKINDNKTFDPNYYGGRWDQINDHGTSHLSIIDSERNVVSLTSTINSYFGALMLSPSTGIVLNNEMDDFSIPMKSSSNLTVPPPAPANFIRPGKRPLSSMTPTIVLKDGKVKASVGASGGLYIIAGTTEVFLNYFFLKMDPLSSVLAPRIYHQLIPNIVSYEN", "text": "SIMILARITY: Belongs to the gamma-glutamyltransferase family."}
+{"protein": "MCENQPKTKADGTAQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQNNASYSCPRQRNCLIDRTNRNRCQHCRLQKCLALGMSRDAVKFGRMSKKQRDSLYAEVQKHQQRLQEQRQQQSGEAEALARVYSSSISNGLSNLNTETGGTYANGHVIDLPKSEGYYSIDSGQPSPDQSGLDMTGIKQIKQEPIYDLTSVPNLFTYSSFNNGQLAPGITMSEIDRIAQNIIKSHLETCQYTMEELHQLAWQTHTYEEIKAYQSKSREALWQQCAIQITHAIQYVVEFAKRITGFMELCQNDQILLLKSGCLEVVLVRMCRAFNPLNNTVLFEGKYGGMQMFKALGSDDLVNEAFDFAKNLCSLQLTEEEIALFSSAVLISPDRAWLIEPRKVQKLQEKIYFALQHVIQKNHLDDETLAKLIAKIPTITAVCNLHGEKLQVFKQSHPDIVNTLFPPLYKELFNPDCAAVCK", "text": "FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity. FUNCTION: Isoform 1 is critical for hindlimb motor control and for the differentiation of amacrine and horizontal cells in the retina. Regulates the expression of PTF1A synergistically with FOXN4. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
+{"protein": "MLPARLPFRLLSLFLRGSAPTAARHGLREPLLERRCAAASSFQHSSSLGRELPYDPVDTEGFGEGGDMQERFLFPEYILDPEPQPTREKQLQELQQQQEEEERQRQQRREERRQQNLRARSREHPVVGHPDPALPPSGVNCSGCGAELHCQDAGVPGYLPREKFLRTAEADGGLARTVCQRCWLLSHHRRALRLQVSREQYLELVSAALRRPGPSLVLYMVDLLDLPDALLPDLPALVGPKQLIVLGNKVDLLPQDAPGYRQRLRERLWEDCARAGLLLAPGHQGPQRPVKDEPQDGENPNPPNWSRTVVRDVRLISAKTGYGVEELISALQRSWRYRGDVYLVGATNAGKSTLFNTLLESDYCTAKGSEAIDRATISPWPGTTLNLLKFPICNPTPYRMFKRHQRLKKDSTQAEEDLSEQEQNQLNVLKKHGYVVGRVGRTFLYSEEQKDNIPFEFDADSLAFDMENDPVMGTHKSTKQVELTAQDVKDAHWFYDTPGITKENCILNLLTEKEVNIVLPTQSIVPRTFVLKPGMVLFLGAIGRIDFLQGNQSAWFTVVASNILPVHITSLDRADALYQKHAGHTLLQIPMGGKERMAGFPPLVAEDIMLKEGLGASEAVADIKFSSAGWVSVTPNFKDRLHLRGYTPEGTVLTVRPPLLPYIVNIKGQRIKKSVAYKTKKPPSLMYNVRKKKGKINV", "text": "FUNCTION: Involved in regulation of mitochondrial protein translation and respiration. Plays a role in mitochondria-mediated cell death. May act as a scaffolding protein or stabilizer of respiratory chain supercomplexes. Binds GTP. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOA1 subfamily."}
+{"protein": "MVKFALQFKASLENLTQLRPHGEDFRWFLKLKCGNCGEVSDKWQYITLMDSVPLKGGRGSASMVQRCKLCSRENSIDILAASLHPYNAEDSETFKTIVEFECRGLEPIDFQPQAGFAAEGAETGTPFHEINLQEKDWTDYDEKAKESVGIYEVEHRFTKC", "text": "SIMILARITY: Belongs to the UPF0587 family."}
+{"protein": "MFNRIMVPVDGSKGAVKALEKGVGLQQLTGAELYILCVFKHHSLLEASLSMVRPEQLDIPDDALKDYATEIAVQAKTRATELGVPADKVRAFVKGGRPSRTIVRFARKRECDLVVIGAQGTNGDKSLLLGSVAQRVAGSAHCPVLVV", "text": "FUNCTION: ATP-binding protein that negatively regulates activity of the tripartite ATP-independent periplasmic (TRAP) ectoine transport system TeaABC. May regulate uptake according to the ATP status of the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal stress protein A family."}
+{"protein": "MNAPLGGIWLWLPLLLTWLTPEVNSSWWYMRATGGSSRVMCDNVPGLVSSQRQLCHRHPDVMRAISQGVAEWTAECQHQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGEVKSCSCDPKKMGSAKDSKGIFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKAVKRFLKQECKCHGVSGSCTLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANERFKKPTKNDLVYFENSPDYCIRDREAGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMTKCGCKFHWCCAVRCQDCLEALDVHTCKAPKNADWTTPT", "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 (By similarity). FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Functions as upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MTENSELNNKISTIKLKKLIEIQNLTDNMNGTVIRIRGFIESITSCSSQIFILLRDRLEKVQCIIFKSTNVSSIYEFSRLKKLPLESFIEIEGQVVFAEIPIKRATKQNIEIVISTLNILGPVVSKLPFQLKDCKIAGKESDTNTITVGYNLRLDNRFLDFRLPVTQSIIKIIDQTMYTFRTYLRTHEFIEIKTSKIIQSGSEGGANLFSLNYFNKPAYLAQSPQLYKQLAIIGGLKRVYEIGHVYRAEVSNINRYLSEFVGLDIEMEMETTYIDFIHFLHSLFINIFESFKNEMKKELEIIRQYYEFVDLKYRSTPIIITYKDAVDMLKSKNIQIDYGCDFSREHERILGKIIKDKEDIDIFTIIDYPSSIRAFYSYIDETTKLTRSYDFIVRGEEILSGAQRENRYDYLKNAVIDKGLNPENLKNYLEAFKYGAPPHIGCGIGLERFLKAYFGFDDIRYFSLFPRDPNRIFP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily."}
+{"protein": "MTFSIMRFNPETDKKPYMQDFELDVSAIQGKMLLNALEALREKHPDIGLRRSCAEGVCGSDGMNINGKNALACVTQLKDLPDRVVVRPLPGFPIIRDLIVDMEQFYAQYKKVKPYLLNDQEAPQKERLQSPEERAKLDGLYECILCACCSSSCPSYWWNPDKFIGPAGLLWSYRFIADSRDSKEKERLDAMKDPYSVFRCRTIMDCATVCPKNLNPAKAIRKIRTEMLQETESGE", "text": "SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family."}
+{"protein": "MSKKYDAGVKEYRDTYWTPEYVPLDTDLLACFKCTGQEGVPREEVAAAVAAESSTGTWSTVWSELLTDLEFYKGRCYRIEDVPGDKESFYAFIAYPLDLFEEGSITNVLTSLVGNVFGFKALRHLRLEDIRFPMAFIKTCGGPPNGIVVERDRLNKYGRPLLGCTIKPKLGLSGKNYGRVVYECLRGGLDLTKDDENINSQPFQRWRERFEFVAEAVKLAQQETGEVKGHYLNCTATTPEEMYERAEFAKELDMPIIMHDYITGGFTANTGLANWCRKNGMLLHIHRAMHAVIDRHPKHGIHFRVLAKCLRLSGGDQLHTGTVVGKLEGDRQTTLGYIDNLRESFVPEDRTRGNFFDQDWGSMPGVFAVASGGIHVWHMPALLAIFGDDSCLQFGGGTHGHPWGSAAGAAANRVALEACVKARNAGREIEKESRDILMEAAKHSPELAIALETWKEIKFEFDTVDKLDVQ", "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": "MGTGKKEKQRRIREGNTKDGNLRVKGENFYRDTKRVQFLNMYKGGRSVRNAKGDIIKAAPLQDTAAPTARVAPDRRWFGNTRVISQDSLSHFREALGENKRDSYQVLLRRNKLPMSLLNEKDSAESPTAKILETEPFEQTFGPKAQRKKPRIAASSLEELISSTSTDNKTFEEKQELDSTLGLMGKQEEEDGWTQAAKEAIFHKGQSKRIWNELYKVIDSSDVVIHVLDARDPLGTRCKSVTDYMTNETPHKHLIYVLNKCDLVPTWVAAAWVKHLSKERPTLAFHASITNSFGKGSLIQLLRQFSQLHKDRHQISVGFIGYPNTGKSSIINTLRKKKVCQVAPIPGETKVWQYITLMKRIFLIDCPGIVPPSSKDSEEDILFRGVVRVEHVSHPEQYIPGILKRCKRQHLERTYEISGWKDSVDFIEMIARKQGRLLKGGEPDESGVSKQILNDFNRGKIPWFVPPPEKDKIEEKEPGDKKRPAEENQEDQEEEEKEQEEQEEPVSKKAKKE", "text": "FUNCTION: GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2 subfamily."}
+{"protein": "MFNVESVERVELCESLLTWIQTFNVDAPCQTAEDLTNGVVMSQVLQKIDPVYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGHDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQRDMEEKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSTRRSYPGHVQPATAR", "text": "FUNCTION: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Predominantly recruits 2 dyneins, which increases both the force and speed of the microtubule motor. Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell. FUNCTION: (Microbial infection) Serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Golgi apparatus Note=Enriched at the cis-face of the Golgi complex (By similarity). Localizes to microtubule asters in prophase (By similarity). Localizes to the manchette in elongating spermatids (PubMed:28003339). SIMILARITY: Belongs to the hook family."}
+{"protein": "MSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAFVAHALAIIKNRKFNGNLNAERIALLAMYHDASEVITGDLPTPIKYHNPKIAHEYKKIEKVAQQKLIEMLPKELQHDFRCLLDEHYYSEEEKALVKQADALCAYLKCLEELSAGNNEFIQAKARLEKTLAIRQSPEMDYFMAVFVPSFSLSLDEISLDSLD", "text": "FUNCTION: Catalyzes the strictly specific dephosphorylation of 2'- deoxyribonucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 5DNU family."}
+{"protein": "MEAEETMECLQEFPEHHKMILDRLNEQREQDRFTDITLIVDGHHFKAHKAVLAACSKFFYKFFQEFTQEPLVEIEGVSKMAFRHLIEFTYTAKLMIQGEEEANDVWKAAEFLQMLEAIKALEVRNKENSAPLEENTTGKNEAKKRKIAETSNVITESLPSAESEPVEIEVEIAEGTIEVEDEGVETLEEVASAKQSVKYIQSTGSSDDSALALLADITSKYRQGDRKGQIKEDGCPSDPTSKQEHMKSHSTESFKCEICNKRYLRESAWKQHLNCYHLEEGGVSKKQRTGKKIHVCQYCEKQFDHFGHFKEHLRKHTGEKPFECPNCHERFARNSTLKCHLTACQTGVGAKKGRKKLYECQVCNSVFNSWDQFKDHLVIHTGDKPNHCTLCDLWFMQGNELRRHLSDAHNISERLVTEEVLSVETRVQTEPVTSMTIIEQVGKVHVLPLLQVQVDSAQVTVEQVHPDLLQGSQVHDSHMSELPEQVQVSYLEVGRIQTEEGTEVHVEELHVERVNQMPVEVQTELLEADLDHATPEIMNQEERESSQADAAEAAREDHEDAEDLETKPTVDSEAEKAENEDRTAMPVLE", "text": "FUNCTION: May be involved in transcriptional regulation as a repressor of ESR1/ER-alpha signaling. Plays a role during development and organogenesis as well as in the function of the adult central nervous system (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MATNGEIFNTYGHNRQTATVTKITASNESSNGVCYLSETANLGKLICIPMALRAAMELNVFQLISKFGTDAKVSASEIASKMPNAKNNPEAAMYLDRILRLLGASSILSVSTTKKSINRGGDDVVVHEKLYGLTNSSCCLVPRQEDGVSLVEELLFTSDKVVVDSFFKLKCVVEEKDSVPFEVAHGAKIFEYAATEPRMNQVFNDGMAVFSIVVFEAVFRFYDGFLDMKELLDVGGGIGTSVSKIVAKYPLIRGVNFDLPHVISVAPQYPGVEHVAGDMFEEVPKGQNMLLKWVLHDWGDERCVKLLKNCWNSLPVGGKVLIIEFVLPNELGNNAESFNALIPDLLLMALNPGGKERTISEYDDLGKAAGFIKTIPIPISNGLHVIEFHK", "text": "FUNCTION: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:22535422, PubMed:22653730, PubMed:29610307). Catalyzes the conversion of (S)- scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422, PubMed:22653730). Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine (PubMed:22535422). Can convert (S)-norreticuline to (S)-norcodamine (PubMed:22535422). Can convert (S)-reticuline to (S)- codamine (PubMed:22535422). Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline (PubMed:22535422). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
+{"protein": "MSSGGLLLLLALLTLWAELTPISGHDRPTFCNLAPESGRCRAHLRRIYYNLESNKCEVFFYGGCGGNDNNFSSWDECRHTCVGK", "text": "FUNCTION: Serine protease inhibitor that inhibits plasmin and trypsin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family."}
+{"protein": "MANKKIDHREEAIELLKQDAKRILQLIKVQMDNLTLPQCPAYEEVLDTQMYGLSREINFATRLGLIEPEEGKKLISTLEKELSALHELSMSKK", "text": "SIMILARITY: Belongs to the UPF0358 family."}
+{"protein": "MEEKRNGLRVILFPLPLQGCINPMLQLANILHVRGFSITVIHTRFNAPKASSHPLFTFLQIPDGLSETEIQDGVMSLLAQINLNAESPFRDCLRKVLLESKESERVTCLIDDCGWLFTQSVSESLKLPRLVLCTFKATFFNAYPSLPLIRTKGYLPVSESEAEDSVPEFPPLQKRDLSKVFGEFGEKLDPFLHAVVETTIRSSGLIYMSCEELEKDSLTLSNEIFKVPVFAIGPFHSYFSASSSSLFTQDETCILWLDDQEDKSVIYVSLGSVVNITETEFLEIACGLSNSKQPFLWVVRPGSVLGAKWIEPLSEGLVSSLEEKGKIVKWAPQQEVLAHRATGGFLTHNGWNSTLESICEGVPMICLPGGWDQMLNSRFVSDIWKIGIHLEGRIEKKEIEKAVRVLMEESEGNKIRERMKVLKDEVEKSVKQGGSSFQSIETLANHILLL", "text": "FUNCTION: Involved in the N-glucosylation of cytokinins. Catalyzes the formation of both the 7-N and the 9-N-glucosides. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MSYKPNLAAHMPAAALNAAGSVHSPSTSMATSSQYRQLLSDYGPPSLGYTQGTGNSQVPQSKYAELLAIIEELGKEIRPTYAGSKSAMERLKRGIIHARGLVRECLAETERNARS", "text": "FUNCTION: Inhibitor of cyclin-dependent kinase CDK2 (By similarity). Also acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:20523938, PubMed:16428440, PubMed:28977666). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the CDK2AP family."}
+{"protein": "MPGKKSPAGEFAARKLREKRKKFRWKDERYKRRMLKLDEKADPLEGAPQARGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKQVTAFCPGDGAIDYIDEHDEVVIEGIGGPKGRAKGDIPGVRYKVVKVNDVALSELLKGKIEKPMR", "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": "MKCFAQIVVLLLVIAFSHGAVITGACDKDVQCGSGTCCAASAWSRNIRFCIPLGNSGEDCHPASHKVPYDGKRLSSLCPCKSGLTCSKSGEKFKCS", "text": "FUNCTION: Potent agonist for both PKR1/PROKR1 and PKR2/PROKR2, and inducer of a potent and long-lasting hyperalgesia (PubMed:16299550, PubMed:20677202). Shows an EC(50) of 0.264 nM, when tested on neuroblastoma cells (SH-SY5Y) which endogenously express mainly PKR2/PROKR2 (PubMed:20677202). Also potentiates capsaicin-induced TRPV1 current, when tested on DRG neurons (PubMed:16687502, PubMed:20677202). Induces a biphasic hyperalgesia to tactile and thermal stimuli after systemic injection of this protein into rat (PubMed:10422759, PubMed:12466223). The initial phase of hyperalgesia is caused by a local action on nociceptors, because intraplantar injection of this protein causes a strong and localized hyperalgesia with a similar time course to that of the initial phase of hyperalgesia seen with systemic injection. The secondary phase of hyperalgesia is not seen with local intraplantar injection and is therefore probably attributable to a central action of this protein (PubMed:16687502). At subnanomolar concentrations, this protein both induces potent chemotaxis of macrophages and stimulates LPS-induced production of the pro- inflammatory cytokines IL-1 and IL-12 (PubMed:16299550). In vivo, this protein potently stimulates the contraction of the guinea-pig gastrointestinal (GI) smooth muscle (at nanomolar concentration) (PubMed:10422759). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AVIT (prokineticin) family."}
+{"protein": "MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGLPDF", "text": "FUNCTION: Interconversion of serine and glycine (PubMed:8505317, PubMed:24698160). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family."}
+{"protein": "MDAALLLNVEGVKKTILHGGTGELPNFITGSRVIFHFRTMKCDEERTVIDDSREVGQPMHIIIGNMFKLEVWEILLTSMRVREVAEFWCDTIHTGVYPILSRSLRQMAQGKDPTEWHVHTCGLANMFAYHTLGYEDLDELQKEPQPLIFVIELLQVDAPSDYQRETWNLSNHEKMKVVPVLHGEGNRLFKLGRYEEASSKYQEAIICLRNLQTKEKPWEVQWLKLEKMINTLILNYCQCLLKKEEYYEVLEHTSDILRHHPGIVKAYYVRARAHAEVWNEAEAKADLQKVLELEPSMQKAVRRELRLLENRMAEKQEEERLRCRNMLSQGATWSPAEPPAEPPAESSTEPPAEPPAEPPAELTLTPGHPLQH", "text": "FUNCTION: May be important in protein trafficking and/or protein folding and stabilization. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MEGGWPARQSALLCLTVSLLLQGRGDAFTINCSGFDQHGVDPAVFQAVFDRKAFRPFTNYSIPTRVNISFTLSAILGVDAQLQLLTSFLWMDLVWDNPFINWNPKECVGINKLTVLAENLWLPDIFIVESMDVDQTPSGLTAYISSEGRIKYDKPMRVTSICNLDIFYFPFDQQNCTFTFSSFLYTVDSMLLGMDKEVWEITDTSRKVIQTQGEWELLGINKATPKMSMGNNLYDQIMFYVAIRRRPSLYIINLLVPSSFLVAIDALSFYLPAESENRAPFKITLLLGYNVFLLMMNDLLPASGTPLISVYFALCLSLMVVSLLETVFITYLLHVATTQPPPMPRWLHSLLLHCTSPGRCCPTAPQKGNKGLGLTLTHLPGPKEPGELAGKKLGPRETEPDGGSGWTKTQLMELWVQFSHAMDTLLFRLYLLFMASSILTVIVLWNT", "text": "FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand- gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Presumably retained within the endoplasmic reticulum unless complexed with HTR3A. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3C sub- subfamily."}
+{"protein": "MSAAGAIAAASVGRLRTGVRRPFSEYGRGLIIRCHSSGMTLDNINRAAVDRIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKNHLKKFNELMIAFRVRPTVLMPLWNVAGFALGAGTALLGKEGAMACTVAVEESIANHYNNQIRMLMEEDPEKYEELLQVIKQFRDEELEHHDTGLDHDAELAPAYALLKRIIQAGCSAAIYLSERF", "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 (By similarity). Involved in lifespan determination in a ubiquinone-independent manner (PubMed:19478076). 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. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ7 family."}
+{"protein": "MSWIIFYTVIAALLILDLRIIHKNNTIMSFKESVLFSLFYLVIACLFGIYVYYNTGADHAREYYTCFLIEKAMSLDNIFVISIIFQFFKIPWQYQHRVLFFGIIGVIIFRAVMIYGGIILINKFAWLLYIFAVILIATGIKTFYVSHKTFDIQNSYIYKSIIKNLNITPNLEGNKFIVKRNNKLYCTPLFISLVLIEAIDLVFAIDSIPAIFAITNDVYIIYTSNIFAILGLRALFFCLAEIVERFSYIKYSLALILIFISFKIFIHHYIAIPEYVAFTVTMTLLLFGIIASIIRKNMIDH", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TerC family."}
+{"protein": "MKLFFPALLSLGALGLCLAASKKSVRWCTTSPAESSKCAQWQRRMKKVRGPSVTCVKKTSRFECIQAISTEKADAVTLDGGLVYDAGLDPYKLRPIAAEVYGTENNPQTHYYAVAIAKKGTNFQLNQLQGLKSCHTGLGRSAGWNIPMGLLRPFLDWTGPPEPLQKAVAKFFSASCVPCVDGKEYPNLCQLCAGTGENKCACSSQEPYFGYSGAFKCLQDGAGDVAFVKDSTVFESLPAKADRDQYELLCPNNTRKPVDAFQECHLARVPSHAVVARSVNGKEDLIWKLLVKAQEKFGRGKPSGFQLFGSPAGQKDLLFKDSALGLLRISSKIDSGLYLGSNYITAIRGLRETAAEVELRRAQVVWCAVGSDEQLKCQEWSRQSNQSVVCATASTTEDCIALVLKGEADALSLDGGYIYIAGKCGLVPVLAESQQSPESSGLDCVHRPVKGYLAVAVVRKANDKITWNSLRGKKSCHTAVDRTAGWNIPMGLLSKNTDSCRFDEFLSQSCAPGSDPRSKLCALCAGNEEGQNKCVPNSSERYYGYTGAFRCLAENVGDVAFVKDVTVLDNTDGKNTEQWAKDLKLGDFELLCLNGTRKPVTEAESCHLAVAPNHAVVSRIDKVAHLEQVLLRQQAHFGRNGRDCPGKFCLFQSKTKNLLFNDNTECLAKLQGKTTYEEYLGPQYVTAIAKLRRCSTSPLLEACAFLMR", "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. May have anabolic, differentiating and anti-apoptotic effects on osteoblasts and may also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4 signaling (By similarity). 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": "MSEQEPYEWAKHLLDTKYIEKYNIQNSNTLPSPPGFEGNSSKGNVTRKQQDATSQTTSLAQKNQITVLQVQKAWQIALQPAKSIPMNIFMSYMSGTSLQIIPIMTALMLLSGPIKAIFSTRSAFKPVLGNKATQSQVQTAMFMYIVFQGVLMYIGYRKLNSMGLIPNAKGDWLPWERIAHYNNGLQWFSD", "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 (PubMed:29809151). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29809151). Involved in the cotranslational insertion of multi- pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151). 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 similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EMC4 family."}
+{"protein": "MQSVQSTSFCLRKQCLCLTFLLLHLLGQVAATQRCPPQCPGRCPATPPTCAPGVRAVLDGCSCCLVCARQRGESCSDLEPCDESSGLYCDRSADPSNQTGICTAVEGDNCVFDGVIYRSGEKFQPSCKFQCTCRDGQIGCVPRCQLDVLLPEPNCPAPRKVEVPGECCEKWICGPDEEDSLGGLTLAAYRPEATLGVEVSDSSVNCIEQTTEWTACSKSCGMGFSTRVTNRNRQCEMLKQTRLCMVRPCEQEPEQPTDKKGKKCLRTKKSLKAIHLQFKNCTSLHTYKPRFCGVCSDGRCCTPHNTKTIQAEFQCSPGQIVKKPVMVIGTCTCHTNCPKNNEAFLQELELKTTRGKM", "text": "FUNCTION: Immediate-early protein playing a role in various cellular processes including proliferation, adhesion, migration, differentiation and survival (PubMed:15181016, PubMed:15611078, PubMed:12695522, PubMed:21344378, PubMed:12050162). Acts by binding to integrins or membrane receptors such as NOTCH1 (PubMed:12695522, PubMed:21344378, PubMed:15611078). Essential regulator of hematopoietic stem and progenitor cell function (PubMed:17463287). Inhibits myogenic differentiation through the activation of Notch-signaling pathway (PubMed:12050162). Inhibits vascular smooth muscle cells proliferation by increasing expression of cell-cycle regulators such as CDKN2B or CDKN1A independently of TGFB1 signaling (PubMed:20139355). Ligand of integrins ITGAV:ITGB3 and ITGA5:ITGB1, acts directly upon endothelial cells to stimulate pro-angiogenic activities and induces angiogenesis. In endothelial cells, supports cell adhesion, induces directed cell migration (chemotaxis) and promotes cell survival (PubMed:12695522). Also plays a role in cutaneous wound healing acting as integrin receptor ligand. Supports skin fibroblast adhesion through ITGA5:ITGB1 and ITGA6:ITGB1 and induces fibroblast chemotaxis through ITGAV:ITGB5. Seems to enhance bFGF-induced DNA synthesis in fibroblasts (PubMed:15611078). Involved in bone regeneration as a negative regulator (By similarity). Enhances the articular chondrocytic phenotype, whereas it repressed the one representing endochondral ossification (PubMed:21871891). Impairs pancreatic beta-cell function, inhibits beta-cell proliferation and insulin secretion (By similarity). Plays a role as negative regulator of endothelial pro-inflammatory activation reducing monocyte adhesion, its anti-inflammatory effects occur secondary to the inhibition of NF-kappaB signaling pathway (PubMed:21063504). Contributes to the control and coordination of inflammatory processes in atherosclerosis (By similarity). Attenuates inflammatory pain through regulation of IL1B- and TNF-induced MMP9, MMP2 and CCL2 expression. Inhibits MMP9 expression through ITGB1 engagement (PubMed:21871891). SUBCELLULAR LOCATION: Secreted. Cytoplasm Cell junction, gap junction Note=Localizes at the gap junction in presence of GJA1. SIMILARITY: Belongs to the CCN family."}
+{"protein": "MGCIKSKRKDNLNDDGVDMKTQPVRNTDRTIYVRDPTSNKQQRPVPESQLLPGQRFQAKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLSSKREGFIPSNYVAKVNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDYDPMHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQSDGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSAQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEFMAKGSLLDFLKSDEGSKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRMENCPDELYDIMKMCWKESAEERPTFDYLQSVLDDFYTATEGQYQQQP", "text": "FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B (By similarity). Phosphorylates LPXN on 'Tyr-72' (By similarity). Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-96'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (By similarity). Phosphorylates CLNK (By similarity). Phosphorylates BCAR1/CAS and NEDD9/HEF1 (By similarity). SUBCELLULAR LOCATION: Cell membrane Nucleus Cytoplasm Cytoplasm, perinuclear region Golgi apparatus Membrane; Lipid-anchor Note=Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain- dependent but kinase activity independent manner and is mediated by exocytic vesicular transport (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily."}
+{"protein": "MVSDRSCIGYLRSVIAGSVDTHTGHECTITNHAAEEGGGTAAAAAVKVMTVSGSGKRGRYVRQVTGRHNDTDLHVAARGGDAGALRRALDEAAAAVATGEGREALEEVRRAVAAEPNEAGETPLVAAAERGHLEVVRELLRHLDAEGVAAKNRSGYDALHVAAREGRHAVVQEMLLHNRLLAKTFGPANTSPLISAATRGHTEVVKLLLELDDFGLVEMAKDNGKNSLHFAARQGHVEIVKALLEKDPQLARRNDKKGQTALHMAVKGTNCDVLRALVDADPAIVMLPDKNGNTALHVATRKKRAEIVAVLLRLPDTHVNALTRDHKTAYDIAEALPLCEESSEIKDILSQHGALRSRELNQPRDELRKTVTEIKKDVHTQLEQTRKTNKNVHGIAKELRKLHREGINNATNSVTVVAVLFATVAFAAIFTVPGGNANNGVAVVVQAASFRIFFIFNAIALFTSLAVVVVQITVVRGETKSERKVVEVINKLMWLASVCTTISFIASCYIVLGRHFQWAALLVSLIGGITMAGVLGTMTYYVVKSKRMRKIRKKEKMSRRSGSSSWYDNTELSETELNQVYAL", "text": "FUNCTION: Involved in salt stress tolerance. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MSPERRPVEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKARNAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHDVGFWQRDFELPAPPRPVRPVTQI", "text": "FUNCTION: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance. SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR subfamily."}
+{"protein": "MAEGSALLRGSSNHKVTLVTGNDGKRREVQACLEGHVLVENVNLDLPEMQSDSVFEISRNKALMAYDITKSPVLVEDTALCFDALGGLPGPYVKWFFERIGPTGLIKLLEGFDTRRAYATCVFTYCASPDVVLQFEGRCDGRIVEAPRGEGGFGWDSVFEPDEGCGQTFAEMQDEEKNRISPRAKALVALKAHFCL", "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": "MKFSLRWLQQIVDLNNIKFSTLVDKLSVSGFEVEDISRNSSNDDMIFDVTTTANRQDILCTVGLAREISSIFNRDLKYKLYKDSIAISTHCLNILNSVSLLDLSIVNVNYFYNNRSPLWLQYYLSSYNIKSLNLLTDIPQYIYLKWGQSIEIFDKNKISSVPIQYSLFNLQKKSHIIYDSPNIELEVLRYDDVILFPIGFSLNENIKCDAATNSIVIMGYVCDKQYITDIKKKLKLSTYLSQRCCNQGSRSDFLNAFYESVYLLGSFGFATLGKFYGYHKLYNISRILFIDKVKIQNILGSVKIGSYNYLTVKEIFTLLERLNFLPIYDSLKSSFKIHIPVYRQDDIVRPIDVIEEVARIYGFDNFISKLPLNPIDNKNIFLNNIFANKVYRIRYLLRCLGLHEAQNYSFYDYYPFNHDTQIKIYNPLAQDQSFLRSSLAVHLTLNQQDNLRQGNKDIEVFEIGKVFRLYSSSLEYDNTLNSFEFLHLSGLIANSIFLRPSWSDKEQSLSWFHAKGMVEEFLDRLEVPVVWKKISDLDQSNLFFNLMHLLNMNWTAIICNRFHEEIGIFGKLCNKSDFNSTYVFEFDLVKLIASIESLNHINSIINPYSSYPSLTRDISLTVKNSCTISFIKARILSYENNLIESIEVFNYYKDKSINAFYNVGLRIVYRAHNRTLNYSDINRIDQEIDDLLNEYKL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily."}
+{"protein": "MFAEQQREYLDKGYTKIESFFSAEEVAKILEDVKQIELGAIGVASDNETYQFEKKNGETTKLLRRVENPHLYFDAIDSLVRSEKIVDLLRHFLGENIRLHNSKINFKPPSGAPVQWHQDWAFYPHTNDDFLTLGIFLDETSEKNGAMACLPGSHKGKVYDHRNVETGEFCHAISRSNWDEALDPTEGELLTGPVGTVTLHHVRTLHGSGPNHSTIRRRFLLIGYAAADAWPLLGCGNYGDYESLMVSGRSTVFPRMVELPLTVPYPLSMYGDRIFESQRALTQKYY", "text": "FUNCTION: Required for hypophosphite oxidation. SIMILARITY: Belongs to the PhyH family."}
+{"protein": "MQLEQKSSLHCSKCRNFLQKFSQDMQAWNCRELDSPLPSDITLHNLEPARPDSGMSFSTDFDDDFFNLDLHQQERSASFGGVTQYSQQFLREKCSFSPYFHTSLETVDSGRTSLYGSNEQCGQLGGASSNGSTAMLHTPDGSNSHQTSFPSDFRMSESPDDTVSGKKTTTRRNAWGNMSYAELITTAIMASPEKRLTLAQVYEWMVQNVPYFRDKGDSNSSAGWKNSIRHNLSLHSRFMRIQNEGAGKSSWWVINPDAKPGRNPRRTRERSNTIETTTKAQLEKSRRGAKKRIKERALMGSLHSTLNGNSIAGSIQTISHDLYDDDSMQGAFDNVPSSFRPRTQSNLSIPGSSSRVSPAIGSDIYDDLEFPSWVGESVPAIPSDIVDRTDQMRIDATTHIGGVQIKQESKPIKTEPIAPPPSYHELNSVRGSCAQNPLLRNPIVPSTNFKPMPLPGAYGNYQNGGITPINWLSTSNSSPLPGIQSCGIVAAQHTVASSSALPIDLENLTLPDQPLMDTMDVDALIRHELSQAGGQHIHFDL", "text": "FUNCTION: [Isoform f]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:24834345). Transcript level in the early adult may play a role in lifespan modulation, but effect is more significant than that played by isoform a (PubMed:24834345). FUNCTION: [Isoform a]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:24834345). May play a role in lifespan modulation, but less significant than that played by isoforms d and f (PubMed:24834345). FUNCTION: Forkhead-type transcription factor (PubMed:9360933). Binds to the promoters of genes that contain the daf-16/FOXO binding element (DBE), TTGTTTAC, in their regulatory region (PubMed:10880363, PubMed:23770237, PubMed:26675724). Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway which affects lipogenesis, lifespan, starvation survival, heat shock and oxidative stress responses, sleep, associative memory, and dauer formation (PubMed:9360933, PubMed:8247153, PubMed:11747821, PubMed:11747825, PubMed:11381260, PubMed:14622602, PubMed:12750521, PubMed:17900900, PubMed:18358814, PubMed:18762027, PubMed:18832074, PubMed:19103192, PubMed:21531333, PubMed:22081913, PubMed:29523076, PubMed:26675724). Longevity signaling predominantly arises from expression in the intestine (PubMed:14622602). Transcriptional activity of daf-16/FOXO is negatively regulated by interaction with host cell factor homolog hcf- 1; and by cytoplasmic sequestration by association with ftt-2 (PubMed:11381260, PubMed:21531333, PubMed:18828672). Inhibition is required for the carbon dioxide (CO2) avoidance response (PubMed:18524954). Upon loss of inhibition, daf-16 translocates to the nucleus to regulate genes that result in delayed reproduction and growth while increasing stress resistance starvation tolerance and longevity (PubMed:11747825, PubMed:21531333). Association with arginine methyltransferase prmt-1 prevents phosphorylation and allows for translocation to the nucleus and the subsequent transcription of longevity-related genes (PubMed:21531333). Modulation of its activity by cGMP levels in sensory neurons regulates lifespan (PubMed:19489741). Has a protective role against muscle dystrophy (PubMed:18397876). Involved in mediating protection against aberrant protein aggregation proteotoxicity (PubMed:16902091). Influences transcription of genes that code for proteins involved in immunity as part of a general stress response (PubMed:17096597, PubMed:18245330). Targets genes that inhibit and stimulate tumor growth (PubMed:17934462). Targets kinases, phosphatases and transcription factors that are primarily involved in signaling and gene regulation (PubMed:24516399). Thought to regulate ins-7 in FOXO-to-FOXO signaling, which coordinates daf-16 expression (PubMed:18025456). Activity is positively regulated by shc-1-mediated inhibition of daf-2 and activation of JNK pathway (PubMed:18832074, PubMed:22916022). Through the regulation of its activity by shc-1- mediated inhibition of daf-2 and activation of JNK pathway, plays a role in maintaining the integrity of the gonad (PubMed:22916022). Functions by indirect interaction with jnk-1 of the mitogen-activated protein kinase (MAPK) pathway (PubMed:17894411). Involved in increased proteasome activity by activating expression of rpn-6.1 in response to proteotoxic stress, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity (PubMed:22922647). Also regulates proteasome activity in the intestine by preventing expression of deubiquitinase ubh-4 (PubMed:23770237). Represses transcription of natc-1 (PubMed:25330323). Involved in regulation of srh-234 expression (PubMed:25357003). Binds to the promoter of the AMPK-gamma regulatory subunit, aakg-4, and activates its transcription (PubMed:24516399). Also activates transcription of AMPK-gamma regulatory subunit, aakg-1 (PubMed:24516399). Maintains endoplasmic reticulum (ER) function by inducing protein degradation and elimination to remove misfolded secretory proteins from the ER independently of the ire-1/xbp-1 unfolded protein response pathway (PubMed:25448701). Regulates epidermal innate immunity to nematophagous fungal infection and physical wounding which trigger bli-3 induced ROS release, leading to daf-16 activation independently of daf-2 signaling (PubMed:24146615). May negatively regulate resistance to stress caused by oxidized cholesterol adducts by preventing the activation of daf-9 and nuclear hormone receptor daf-12, two members of the steroid signaling pathway (PubMed:24957743). Promotes apoptosis during embryonic development (PubMed:25383666). Probably through the regulation of the autophagy genes atg-18 and atg-16.2, plays a role in regulating stem cell number in the germline during larval development (PubMed:28285998). Plays a role in learning and memory; including associative memory, and aversive gustatory associated learning known as salt avoidance learning (PubMed:26675724, PubMed:30779740). Plays a role in regulating gene transcription in response to white light exposure (PubMed:29500338). Binds to the promoter of dex-1 to positively regulate its expression in seam cells during the dauer phase (PubMed:30409788). Plays a role in transgenerational lipid accumulation in response to a high-fat diet (PubMed:35140229). FUNCTION: [Isoform d]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:24834345). Transcript level in the early adult may play a role in lifespan modulation, but effect is more significant than that played by isoform a (PubMed:24834345). SUBCELLULAR LOCATION: [Isoform f]: Nucleus Cytoplasm Note=Ratio of nuclear to cytoplasmic localization is daf-2-dependent. SUBCELLULAR LOCATION: [Isoform a]: Nucleus Cytoplasm Note=Ratio of nuclear to cytoplasmic localization is daf-2-dependent. SUBCELLULAR LOCATION: [Isoform d]: Nucleus Cytoplasm Note=Ratio of nuclear to cytoplasmic localization is daf-2-dependent. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between cytoplasm and nucleus (PubMed:11381260, PubMed:17894411). Nuclear translocation is inhibited by phosphorylation by AKT proteins (PubMed:11381260, PubMed:11747825, PubMed:21531333). Association with ftt-2 sequesters daf-16 in the cytoplasm (PubMed:21531333). Association with prmt-1 allows for translocation to the nucleus (PubMed:21531333). Nuclear translocation is promoted by phosphorylation by unc-43 and inhibited by dephosphorylation by tax-6 (PubMed:23805378). Nuclear translocation is promoted by jnk-1 upon heat stress and by sek-1 upon oxidative stress (PubMed:15888317, PubMed:15767565). Nucleocytoplasmic shuttling is induced by starvation, heat treatment, hypergravity, reactive oxygen species (generated by juglone), exposure to tributyltin or 4-hydroxy-E- globularinin (4-HEG) and the flavonoids kaempferol and fisetin (PubMed:11381260, PubMed:17551714, PubMed:18832074, PubMed:19252938, PubMed:21531333, PubMed:23805378). Nuclear localization induced by nematophagous fungal infection (PubMed:24146615)."}
+{"protein": "MEKDFQDIQQLDSEENDHQLIGDEEQGSHVQNLRTENPRWGGQPPSRPFPQRLCSKFRLSLLALAFNILLLVVICVVSSQSMQLQKEFWTLKETLSNFSTTTLMEFKALDSHGGSRNDNLTSWETILEKKQKDIKADHSTLLFHLKHFPLDLRTLTCQLAFFLSNGTECCPVNWVEFGGSCYWFSRDGLTWAEADQYCQMENAHLLVINSREEQEFVVKHRGAFHIWIGLTDKDGSWKWVDGTEYRSNFKNWAFTQPDNWQGHEEGGSEDCAEILSDGLWNDNFCQQVNRWACERKRDITY", "text": "FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N- acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein."}
+{"protein": "MSMPGINVSNLLNEHEELGLRLLAGEKGLTNRINMSEINRPGLSLTGFYESFAHDRIQIFGKGEWAYITSRIPEDLKNIAADFFSFHLNCIIFTHGNMPPSIFTENCERLAIPLMISDVSTHKFITLISGILDRSLAPRTMRHGVLIEVFGIGILLSGKSGVGKSETALELIERGHRLVADDMVEIRRLSESYLIGTCSDLLRHHMEIRGLGILNIKDIFGIGSVRDHKLIELIIRLEEWTEDKDFDRTGLENPTEELLGVQIPLIRVPVKPGRNIPIIVETAAMNQRLRKLGKNAAQEFNQKLSNYLQQGKVERNPP", "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": "MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYGDLKNAIEKLSGKEINGRKIKLIEGSKRHRSRSRSRSRTRSSSRSRSRSRSRRSKSYSRSRSRSRSRSKSRSGSRSPVPEKSQKRGSSSRSKSPASVDRQRSRSRSRSRSVDSGN", "text": "FUNCTION: May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity). FUNCTION: May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity). Could play an important role in development and differentiation in the spleen and thymus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family."}
+{"protein": "MLRLCFFISFMCLVKSDTDETCPSFTRLSFHSAVVGTGLSVRLMLYTQRDQTCAQIINSTALGSLNVTKKTTFIIHGFRPTGSPPVWIEELVQSLISVQEMNVVVVDWNRGATTVIYPHASSKTRQVASILKEFIDQMLVKGASLDNIYMIGVSLGAHIAGFVGESYEGKLGRVTGLDPAGPLFNGRPPEERLDPSDALFVDVIHSDTDALGYKEALGHIDFYPNGGLDQPGCPKTIFGGIKYFKCDHQMSVYLYLASLQNNCSITAYPCDSYRDYRNGKCVSCGAGQIVPCPRVGYYADSWKEYLWDRDPPMTKAFFDTAETKPYCMYHYFVDIVSWNKSVRRGFITIKLRGEDGNITESKIDHEPSAFEKYHQVSLLARFNRDLDKVAEISLLFSTGSVVGPKYKLRVLQMKLRSLAHPDRPHLCRYDLVLMENVETSFQPILCSQQQM", "text": "FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2- acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid (By similarity). Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG) (By similarity). SUBCELLULAR LOCATION: Secreted Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
+{"protein": "MNDLRQLRHFVALAEHGHFARAAEAVNLSQPALSRSIQALENGLGCRLLDRGPRQVSLTAHGRLVLEHARRLLDGDRALRSAVSQLDNLGSGELRLGAGPYPGARLVPRALGRFAGAHPGVRVQLAIDTWYSLHQRLLDDALELFVADVRELRDDPQLEVTPLRSWPGVIFCRPGHPLLGRRRHRLTAADLAAYPLAGTQVPAEVAQALGQLAESGQPLGIECDNFMALKALVAESDVLSMAPLDVVAEEIEAGRLALLELAPGLLSQRSAYGLVSRAGRTLSPAAEAMRGLILDEDARTPPASAR", "text": "FUNCTION: Activates the transcription of the sdsA gene for sodium dodecyl sulfate (SDS) degradation. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MATTHTLLSFDDLEFLLHRKDLTDLYGERCGTLNLVINPYELFLPDELDDDCCDDPFNCCFPDVYASIGTEYSYIDPPELIHEEHCATNGTWPNGDPCEPILPPFTITGTHHYYATKPGEVVSGILSKLGSSWDPSLRSTADVSNSFTFRAESDGPGSAEIVTEEQGTVVQQQPAPAPTALATLATASTGKSVEQEWMTFFSYHTSINWSTVESQGKILYSQALNPSINPYLDHIAKLYSTWSGGIDVRFTVSGSGVFGGKLAALLVPPGVEPIESVSMLQYPHVLFDARQTEPVIFTIPDIRKTLFHSMDETDTTKLVINPYENGVENKTTCSITVETRPSADFTFALLKPPGSLIKHGSIPSDLIPRNSAHWMGNRWWSTISGFSVQPRVFQSNRHFDFDSTTTGWSTPYYVPIEIKIQGKVGSNNKWFHVIDTDKALVPGIPDGWPDTTIPDETKATNGNFSYGESYRAGSTTIKPNENSTHFKGTYICGTLSTVEIPENDEQQIKTEAEKKSQTMYVVTADFKDTIVKPQHKISPQKLVVYFDGPEKDLTMSATLSPLGYTLVDEQPVGSVSSRVVRIATLPEAFTQGGNYPIFYVNKIKVGYFDRATTNCYNSQILMTSQRLAEGNYNLPPDSLAVYRITDSSSQWFDIGINHDGFSYVGLSDLPNDLSFPLTSTFMGVQLARVKLASKVKAHTITAK", "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 (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the caliciviridae capsid protein family."}
+{"protein": "MERWTGRVALVTGASVGIGAAVARALVQHGMKVVGCARSVDKIEKLAAECQSAGYPGTLIPYKCDLSNEEEILSMFSAIKTLHQGVDVCINNAGLARPEPLLSGKTEGWRTMIDVNVMAVSICTREAYQSMKERNIDDGHIININSMNGHSVVPQSVVHFYSATKYAVTALTEGLRQELREAKTHIRATCISPGLVETGFAFKLHDNDPERAAATYESIRCLKAEDMANAVIYVLSAPPHVQIGDIQMRPTEQIS", "text": "FUNCTION: Catalyzes the conversion of the 17-keto group of estrone, 4- and 5-androstenes and 5-alpha-androstanes into their 17-beta- hydroxyl metabolites and the conversion of the 3-keto group of 3-, 3,17- and 3,20- diketosteroids into their 3-hydroxyl metabolites. Exhibits reductive 3-beta-hydroxysteroid dehydrogenase activity toward 5-beta-androstanes, 5-beta-pregnanes, 4-pregnenes and bile acids. May also reduce endogenous and exogenous alpha-dicarbonyl compounds and xenobiotic alicyclic ketones. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MATFELIPYRLYLSQSNTWIHRIKAEIKIYIVALLWISIFIFSYFKLCIIALSLIAISFTIRSKQNIIQKHLLQTLLMTFLTTVLSFSVAISYKQYAEQEQSQYLSDSKKYKNSSSYYYIQIANDQRIKRQYLITTLKPSLYFFITIYSIKLVMITTSPEVLVITIYRSRIINKIFKNELLFIFLLSSHIVTSIINRIDKVIQVTSLRGSLNLYNSLTRPLMFSLLIFQVFFLEIIRESKEIAQALYTRNLNQENNNFLKIYTVKSNFSDRLNIIISTLYFIILALA", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ycf92 family."}
+{"protein": "MGSQPTNSHFTLNEQTLCGTNISLLGNNRFIQIGNGLHMTYAPGFFGNWSRDLTIGPRFGGLNKQPIHVPPKRTETASIQVTPRSIVINRMNNIQINPTSIGNPQVTIRLPLNNFKSTTQLIQQVSLTDFFRPDIEHAGSIVLILRHPSDMIGEANTLTQAGRDPDVLLEGLRNLFNACTAPWTVGEGGGLRAYVTSLSFIAACRAEEYTDKQAADANRTAIVSAYGCSRMETRLIRFSECLRAMVQCHVFPHRFISFFGSLLEYTIQDNLCNITAVAKGPQEAARTDKTSTRRVTANIPACVFWDVDKDLHLSADGLKHVFLVFVYTQRRQREGVRLHLALSQLNEQCFGRGIGFLLGRIRAENAAWGTEGVANTHQPYNTRALPLVQLSNDPTSPRCSIGEITGVNWNLARQRLYQWTGDFRGLPTQLSCMYAAYTLIGTIPSESVRYTRRMERFGGYNVPTIWLEGVVWGGTNTWNECYY", "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 (By similarity). Prevents also necroptosis and extrinsic apoptosis by sequestering host ZBP1 into large, insoluble supercomplexes and impairing its ability to interact with RIPK3 (PubMed:32649716). SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae TRX1 protein family."}
+{"protein": "MAAKFLLTILVTFAAVASLGMADNVLLSGQTLHADHSLQAGAYTLTIQNKCNLVKYQNGRQIWASNTDRRGSGCRLTLLSDGNLVIYDHNNNDVWGSACWGDNGKYALVLQKDGRFVIYGPVLWSLGPNGCRRVNGGITVAKDSTEPQHEDIKMVINN", "text": "FUNCTION: Taste-modifying protein; sweet-tasting. After curculin, water elicits a sweet taste, and sour substances induce a stronger sense of sweetness."}
+{"protein": "MPPAVGGPVGYTPPDGGWGWAVVIGAFISIGFSYAFPKSITVFFKEIEGIFHATTSEVSWISSIMLAVMYGGGPISSILVNKYGSRIVMIVGGCLSGCGLIAASFCNTVQQLYVCIGVIGGLGLAFNLNPALTMIGKYFYKRRPLANGLAMAGSPVFLCTLAPLNQVFFGIFGWRGSFLILGGLLLNCCVAGALMRPIGPKPTKAGKDKSKASLEKAGKSGVKKDLHDANTDLIGRHPKQEKRSVFQTINQFLDLTLFTHRGFLLYLSGNVIMFFGLFAPLVFLSSYGKSQHYSSEKSAFLLSILAFVDMVARPSMGLVANTKPIRPRIQYFFAASVVANGVCHMLAPLSTTYVGFCVYAGFFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVVLIISGIYLFIGMGINYRLLAKEQKANEQKKESKEEETSIDVAGKPNEVTKAAESPDQKDTDGGPKEEESPV", "text": "FUNCTION: Bidirectional proton-coupled monocarboxylate transporter (PubMed:12946269, PubMed:33333023, PubMed:32946811). Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH (PubMed:12946269, PubMed:33333023). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart (PubMed:32946811). Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 309-Asp is essential for the conformational transition (PubMed:33333023). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Note=Expression at the cell surface requires the ancillary proteins BSG and EMB. Binds preferentially to BSG. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
+{"protein": "MFEINPVNNRIQDLTERSDVLRGYLDYDAKKERLEEVNAELEQPDVWNEPERAQALGKERSSLEAVVDTLDQMKQGLEDVSGLLELAVEADDEETFNEAVAELDALEEKLAQLEFRRMFSGEYDSADCYLDIQAGSGGTEAQDWASMLERMYLRWAESRGFKTEIIEESEGEVAGIKSVTIKISGDYAYGWLRTETGVHRLVRKSPFDSGGRRHTSFSSAFVYPEVDDDIDIEINPADLRIDVYRTSGAGGQHVNRTESAVRITHIPTGIVTQCQNDRSQHKNKDQAMKQMKAKLYELEMQKKNAEKQAMEDNKSDIGWGSQIRSYVLDDSRIKDLRTGVETRNTQAVLDGSLDQFIEASLKAGL", "text": "FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA hydrolase (PubMed:22857598, PubMed:27934701). In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center and releases the ribosome (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon (PubMed:22857598, PubMed:22922063, PubMed:25355516). 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. Note=Recruited to the 70S ribosome by ArfA even in the absence of mRNA (PubMed:22922063, PubMed:25355516, PubMed:27934701). SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family."}
+{"protein": "MYKILSSFVAGVAIGSGLVITYVLYNVPEPPELDLQRWWGIGTRPTEEDKSIRPFSIDFNDTVILDLKERLKNRRPFTKPLEGINSEYGMNTEYLETVLEYWLNEYNFKKRAELLNKFPHYKTRIQGLDLHFIRVKPEIKEGVQVLPLLMMHGWPSSSKEFDKVIPILTTPKHEYNIVFEVVAVDLPGYGFSEGTNKPGLNPVQIGVMMRNLMLRLGFEKFYIQAGDWGSQCATHMATLFPDQVLGLHTNMPLSSRPLSTVKLFIGALFPSLIVDAKYMDRIYPLKNLFSYILRETGYFHIQATKPDTIGVALTDSPAGLAGYLIEKMAICSNRDQLDTPHGGLENLNLDDVLDTVTINWINNCIVTSTRLYAEGFSWPEVLIVHRIPSMVPTAGINFKYEVLYQPDWILRDKFPNLVRSTVLDFGGHFAALHTPQALADDIFASAVQFLKFHDRKRNQKSS", "text": "FUNCTION: Catalyzes juvenile hormone hydrolysis. SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S33 family."}
+{"protein": "MAYVRLTSLAVLFFLAASVMLNVKKTEGGEFLKCGESCVQGECYTPGCSCDWPICKKNHIIATNAKTVNQHRLLCESHEDCFKKGTGNYCAFFPDSDVHFGWCFYAESDGYLLKDFFKMSKDNLKMPMTIIN", "text": "FUNCTION: Probably participates in a plant defense mechanism (Probable). Not active against Gram-negative bacteria E.coli ATCC 700926, K.pneumoniae ATTC 13883 and P.aeruginosa ATCC 39018 at concentration up to 100 uM (PubMed:21596752). Has cytotoxic but no hemolytic activity (PubMed:21596752). SIMILARITY: Belongs to the cyclotide family. Moebius subfamily."}
+{"protein": "DLLQFXDMMK", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that has antibacterial activity against S.aureus ATCC 25923 and ATCC 29213, acts by inducing bacterial membrane breakage. Displays a potent inhibitory effect on collagen-induced human platelet aggregation and has indirect hemolytic activity. Does not show cytotoxicity to murine skeletal muscle myoblasts. 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."}
+{"protein": "MIMPQSRLDVADNSGAREIMCIRVLNSGIGGKGLTTGGGGNKRYAHVGDIIVASVKDAAPRGAVKAGDVVKAVVVRTSHAIKRADGSTIRFDRNAAVIINNQGEPRGTRVFGPVARELRDRRFMKIVSLAPEVL", "text": "FUNCTION: Forms part of two intersubunit bridges in the 70S ribosome (By similarity). Binds to 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
+{"protein": "MQRSRGFRSKSRRKMTKVVREGRSNPITNKLQKFEEGDLVHITINPSIQKGQPHPRFHGKTGKITDKKGKAYIVSLTDGNKAKELIIRPDHLKLQTSQ", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family."}
+{"protein": "MEQASFVVIDETGIHARPATLLVQAASKYSSDVQIEYTGKKVNLKSIMGVMSLGIGKGADITIYTEGSDEKEAIEGLTEVLKKEGLAE", "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. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HPr family."}
+{"protein": "MNMKKKEKHAIRKKSIGVASVLVGTLIGFGLLSSKEADASENSVTQSDSASNESKSNDSSSVSAAPKTDDTNVSDTKTSSNTNNGETSVAQNPAQQETTQSALTNATTEETPVTGEATTATNQANTPATTQSSNTNAEELVNQTSNETTSNDTNTVSSVNSPQNSTNAENVSTTQDTSTEATPSNNESAPQSTDASNKDVVNQAVNTSAPRMRAFSLSAVAADAPAAGKDITNQLTNVTVGIDSGDTVYPHQAGYVKLNYGFSVPNSAVKGDTFKITVPKELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFTDYVDTKENVTANITMPAYIDPENVTKTGNVTLTTGIGSTTANKTVLVDYEKYGKFYNLSIKGTIDQIDKTNNTYRQTIYVNPSGDNVIAPVLTGNLKPNTDSNALIDQQNTSIKVYKVDNAADLSESYFVNPENFEDVTNSVNITFPNPNQYKVEFNTPDDQITTPYIVVVNGHIDPNSKGDLALRSTLYGYDSRFVWRSMSWDNEVAFNNGSGSGDGIDKPVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDNDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSNSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSDSESDSDSDSDSDSDSDSDSDSASDSDSGSDSDSSSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLIWGLLASIGSLLLFRRKKENKDKK", "text": "FUNCTION: Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor Note=Anchored to the cell wall by sortase A (By similarity). SIMILARITY: Belongs to the serine-aspartate repeat-containing protein (SDr) family."}
+{"protein": "MGERQTIADSKRAFHQAFPHVIAPLYRRLADELLVELHLLSHQSSFKTTPLFAVGLCTVFDTFSAGYRPEEHITGLLDALCSSNGYDANTFRKESKRCIDAAKTESVDAMDSHLAGQKLGEGSHYSRLMAIGVLRLFEEAKGDADQPDEADLRKRCKELSTALNFPAERVEKDLSLFASNSERMSAAIELVQETIAAERRKKERRQAEQAQRSES", "text": "FUNCTION: May be involved in photosynthetic membrane biogenesis. SIMILARITY: Belongs to the THF1 family."}
+{"protein": "MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI", "text": "FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (PubMed:25732850). Binds cholesterol (PubMed:25732850). 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": "MEKVNEERDAVFEDHIGDRRRSVRSLLEEAFADEMEKTSYDVEVADTPQPHIPIRFRHPPIAGPVHDVFGDAIHDIFQKMMKRGQAVDFCHWVSHLIATEIDEKFSEVAFRDVQYNPDIYVTDSTTEAKKLFNDKIWPAIDKILQQNAETCPILSEKWSGIHVSGDQLKGQRHKQEDRFLAYPNGQYMDRGEDPISVLAVFDGHGGHECSQYAAGHLWETWLEVRKSRDPSDSLEDQLRKSLELLDERMTVRSVKECWKGGSTAVCCAIDMDQKLMALAWLGDSPGYVMSNIEFRQLTRGHSPSDEREARRVEEAGGQLFVIGGELRVNGVLNLTRALGDVPGRPMISNEPETCQVPIESSDYLVLLACDGISDVFNERDLYQLVEAFANDYPVEDYAELSRFICTKAIEAGSADNVSVVIGFLRPPQDVWKLMKHESDDEDSDVTDEE", "text": "FUNCTION: Dephosphorylates auto-phosphorylated Ca(2+)/calmodulin- dependent protein kinase unc-43/CAMKII in vitro (PubMed:11559703, PubMed:23760267). Involved in the regulation of sex determination (PubMed:8824590). Together with fem-3, required for male sexual development by promoting the proteasomal-mediated degradation of tra-1, a transcription repressor of male-specific genes (PubMed:17609115). Promotes apoptosis (PubMed:11559703). SIMILARITY: Belongs to the PP2C family."}
+{"protein": "MSAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL", "text": "FUNCTION: Urate oxidase is a cofactorless enzyme involved in the metabolism of purines (PubMed:1339455, PubMed:17020862, Ref.3, PubMed:28272834). Catalyzes, in the presence of molecular oxygen, the hydroxylation of uric acid to metastable 5-hydroxyisourate (5-HIU) which is further degraded to allantoin (PubMed:1339455, PubMed:17020862, PubMed:28272834). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the uricase family."}
+{"protein": "MLQQDSNDDTEDVSLFDAEEETTNRPRKAKIRHPVASFFHLFFRVSAIIVYLLCGLLSSSFITCMVTIILLLSCDFWAVKNVTGRLMVGLRWWNHIDEDGKSHWVFESRKESSQENKTVSEAESRIFWLGLIACPVLWVIFAFSALFSFRVKWLAVVIMGVVLQGANLYGYIRCKVRSRKHLTSMATSYFGKQFLRQNTGDDQTS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TVP23 family."}
+{"protein": "MKSILLLFSLIVLGSATEEVSRTEQTSTLFSVEGEIALPSTRNCAKWSAGARIHLNHGQYMGFVRQDCTFRVDFVPTGTYIVQIENTDFVFEPIRVDITSKGKMRARKLTILQPNNVNTLPYPLRLSARGPARYFRKREEWRITDMLFSPMVLMLVVPLVVMLILPKMTANDPELKKEMENMQMPKVDMPDVGEMMANFFGGSAPAKKKAVTGGSGSGQRRK", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the EMC7 family."}
+{"protein": "MKQIVLDENCLAGNFIIVKDAKIYHHLVNVRRLKKGDKLNILLKDKELRASEIVKIGSNFIKFTTNKIDKIEKNNFEISIFISSLKGRKIDLVLRQVVEIGVSEINIINADRSVSKIDINNASAKILRFSKIIDEALKQSGNKIVPKINFYNNFFYLPYSFCTTRYYVAHPSGMILSKNESFDNFGKIGIIIGPEGCFSESEIVFFKEKGFNFVRFNTPILRADTAIIYSLAYFKALLEDYNG", "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": "MADLPQKVSNLSINNKENGGGGGKSSYVPPHLRSRGKPSFERSTPKQEDKVTGGDFFRRAGRQTGNNGGFFGFSKERNGGTSANYNRGGSSNYKSSGNRWVNGKHIPGPKNAKLEAELFGVHDDPDYHSSGIKFDNYDNIPVDASGKDVPEPILDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPVPEKAQSFYSRKGYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEECDMPSVENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSENITQRILYVDDMDKKSALLDLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSFFNSNNQNIVKGLMEILNEANQEVPTFLSDLSRQNSRGGRTRGGGGFFNSRNNGSRDYRKHGGNGSFGSTRPRNTGTSNWGSIGGGFRNDNEKNGYGNSNASWW", "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). Redundant to DED1, may be required in conditions in which DED1 expression is decreased. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1 subfamily."}
+{"protein": "MTNPKNVVPNSGTSSRHASIVEMLSSPPLLPHQHAQHAHVHRSQGRSESIESIPLQRSASGTSSITSMGSNNDSSSANAQSANPSAGSATNVGASGTPHSGSGLEAGNTDLSAVPMLQTPSQCLNSAHIHTWKHIQLSQLIEQNKLIFVPGSLSVEETFNTLIKYHLTSIPVEAVPGDMNCLTFDYNDLNSYLLLVLNKITINNKQVTQDCQNGKPVAVGDIVKLTPKNPFYKLPETENLSTVMGILGSGVHRVAITNPEMTQIRGILSQRRLIKYIWDNARSFGTLEPLLNSSLQDLKIGVLNTNSKPTSRQSRVISIQGEEPLIMALYKMHKERISSIAVIDPQGNLIGNISVTDVKHVTRTSQYPLLHKTCRHFISVILNSRGLETGKDSFPIFHVYPTSSLARTLAKLVATKSHRLWIVQPQEAPTATSSSSTSSSVNTGTISPNPTPTTTSASPAPGATPNALNNHSPLLSTVDDGHTVINPATQATNTTVIQPNLFEKEYRTGKLIGVVSLTDIINLLARKQTANTEVDPQTARRQRGPATQ", "text": "FUNCTION: Involved in DNA replication and cell separation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SDS23 family."}
+{"protein": "MAVGENKEQILNVRIEDEIKTSYLNYAMSVIVSRALPDVRDGLKPVHRRILYSMYEMGLRSDKAFKKAGRIVGDVLGKYHPHGDQSIYDALVRLAQDFSLRYPVIRGQGNFGSIDGDPPAAMRYTEAKMEKITEYIVKDIDKETVNFKSNYDDSLSEPEIMPSSFPFLLVNGSSGIAVGMATNMAPHNLREICDAIVYMLDNENASIFDLLKIVKGPDFPTFGEIVYNDNLIKAYKTGKGSVVIRARYHIEERAEDRNAIIVTEIPYTVNKSALLMKVALLAKEEKLEGLLDIRDESDREGIRIVLEVKRGFDPHVIMNLLYEYTEFKKHFSINNLALVNGIPKQLNLEELLFEFIEHRKNIIERRIEFDLRKAKEKAHVLEGLNIALNNIDEVIKIIKSSKLAKDARERLVSNFGLSEIQANSVLDMRLQKLTALEIFKLEEELNILLSLIKDYEDILLNPVRIINIIREETINLGLKFGDERRTKIIYDEEVLKTSMSDLMQKENIVVMLTKKGFLKRLSQNEYKLQGTGGKGLSSFDLNDGDEIVIALCVNTHDYLFMISNEGKLYLINAYEIKDSSRASKGQNISELINLGDQEEILTIKNSKDLTDDAYLLLTTASGKIARFESTDFKAVKSRGVIVIKLNDKDFVTSAEIVFKDEKVICLSKKGSAFIFNSRDVRLTNRGTQGVCGMKLKEGDLFVKVLSVKENPYLLIVSENGYGKRLNMSKISELKRGATGYTSYKKSDKKAGSVVDAIAVSEDDEILLVSKRSKALRTVAGKVSEQGKDARGIQVLFLDNDSLVSVSKFIK", "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 (PubMed:15897198). 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": "RYCPSGCRKKPYGGGCSC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the poneritoxin-Ae1 family."}
+{"protein": "MIIKGSNFSVMDNSGARKVQCIQTLEGKKPTSLLRVGDKIVVVIKKMEKRKGGKYKLKVKKSDVCYAVIVKSKQPVRRKSGIIVNAGENGVILLTKTKEPIGTRLTGVVFKEVQRTGLLKNVSISKYII", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
+{"protein": "MMLSLPKLSAGGVVVLLATLLHTLTVQGASVRHHRLRGGDQGGFLAPSSDMIKALEYIESLKQRADGPESPTGDYDEVDKFRFLVQLASLQDENTPTHEDATRWPDNKVPQWVRSLLRVLDQAGESPESQAAGNERRLHKTRRPVADGESPAGDYAGFVKPHKKYPLMFEDEENGRDNKRATEDLDEQYTPQSLANMRSIFEELGKLSAAQKRDDEEDGEDDDDLYRVRNAAYEDVTGGEEWVPLEEQLETEELVKGSHEEYKRALGDISEQGMENMERRGEEEDENPDDDTKLVDYYLLKVLEMTDQAQKRDLMEGRRRLLSRPSLIDPRAIKQLLSAISMKLQVPPEDLVGMLFMEETRKQQQRLPEPQLARNPSQPRYKSRVIKYYNGRQPEVTVSDIPHDVKTEDILKVLGLGNLANKNAKFSLLKQRPYKTAMTNYFNPNGRRGSLFLSELNKAPSKRKDDYDDDDAVDEDEESTFLAAKLLTEYPDTSSSNRKRAIDSAANGQLPYELYEEAMKDFFDQVDNGKSALAKRDTQGKEEPEGPQKPPAQDPAQETVDQTPPESGTEDGKEYHGKIVAGM", "text": "FUNCTION: Neuroendocrine protein of the granin family that regulates the biogenesis of secretory granules (By similarity). Required for neurovascular modeling of the hindbrain (PubMed:29757409). Acts in a non-cell autonomous manner and is required for migration and proliferation of central artery endothelial cells (PubMed:29757409). Required for normal courting behavior and spawning (PubMed:32467166). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the chromogranin/secretogranin protein family."}
+{"protein": "MNLKNLETCKGLIKGSYIDQAIQGTSQFNKLLETLLIHKKLPNIGYNDKIIELILNEISLMDSNNFIENIGVGEREGRIYSGLVEKRHYGFAHGIGRSGDITEQQPKAAGSSLIQKLTHSLVLDAMKLAGLEQSSLSNCLLLPMATGMTLALTMLTLKSINANNKRYVLWPRIDQKSCLKSIITAGLIPIVIPNQLDGDMIRTDLVAIEDKIKELGVDNILCVFSTTSCFAPRVPDKIIEISEICKRYNIGHIINNAYGLQCSKILHNISQACKLGRVDAFIQSTDKNFMVPVGGAIISGPNSEFIDQISRNYPGRANSSPILDVFITLLSMGKQGWLNLLKERKELLIYFNEQLSKFALENNEKLLNTINENKISFALTLSSNNFNNNEEIISNNNNNNNNTFSMIGSKLFSRSCSGSRVIDLKSNKKLLIGGLEFNNYGSHIDNYSTSYLTVACAIGITKLEIDTFIQRLSKLFNKK", "text": "FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- tRNA(Sec) required for selenoprotein biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SepSecS family."}
+{"protein": "MVGADPTRPRGPLSYWAGRRGQGLAAIFLLLVSAAESEARAEDDFSLVQPLVTMEQLLWVSGKQIGSVDTFRIPLITATPRGTLLAFAEARKKSASDEGAKFIAMRRSTDQGSTWSSTAFIVDDGEASDGLNLGAVVNDVDTGIVFLIYTLCAHKVNCQVASTMLVWSKDDGISWSPPRNLSVDIGTEMFAPGPGSGIQKQREPGKGRLIVCGHGTLERDGVFCLLSDDHGASWHYGTGVSGIPFGQPKHDHDFNPDECQPYELPDGSVIINARNQNNYHCRCRIVLRSYDACDTLRPRDVTFDPELVDPVVAAGALATSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWQKERVQVWPGPSGYSSLTALENSTDGKKQPPQLFVLYEKGLNRYTESISMVKISVYGTL", "text": "FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage. SUBCELLULAR LOCATION: Lysosome membrane; Peripheral membrane protein; Lumenal side Lysosome lumen Cell membrane Cytoplasmic vesicle Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. SIMILARITY: Belongs to the glycosyl hydrolase 33 family."}
+{"protein": "MEILDKQAFFETREKLYTLSRSLNIIKQRIQIAENDRKKCLITINELESLSSETKTYKAVGKMFVISPMTSLKTELKQQVQKDEEDVKGLINQSKYIDAQITDTERSLNELVRKK", "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": "MAAVPDTSDMMTYCSGNENDLFFEEDGPKQMKGSFQDLDLSSMGDGGIQLQFSHHLYNKTFKHAMSIIVAVEKLKKIPVPCSQAFQDDDLRSLFSVIFEEEPIICDNWDEGYVCDAAMHSVNCRLRDIYHKSLVLSGACELQAVHLNGENTNQQVVFCMSFVQGEEETDKIPVALGLKEKNLYLSCGMKDGKPTLQLETVDPNTYPKRKMEKRFVFNKMEIKGNVEFESAMYPNWYISTSQAEKSPVFLGNTRGGRDITDFIMEITSA", "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": "MKKNIISIIIVCLSFLTSIILYQYLPEEIPIQWSGNKPAAIVSKPLTIFIIPVVMLIYYLTFYMLTIKSTQKNKALLFLASNNMLILLYILQLSTLLISLGYEVNIDLIIGLGVGIFLIIGGNSMQLAEQNHLIGLRTPWTLKDETVWKLGNRFASKVLVVCGFIIAVLSFFTGEYIILIMIVLVLLALVISTLASYHYYKKLNGSR", "text": "FUNCTION: Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
+{"protein": "MSASASLSAGSDASGPGSPAGDQGNALPQLDSLISHLVAAKRSLSSINHVWRANEIVTSARSALEESVVISARTGFLRRGLNNQLRLLYSVRSEVEEVSLRGRSEFASVLKSLDTADARLRKTLDSLRDTIVHASFRPEGEEPRSLHDFVDERGVEELRAALKSSIDRTNEAQAELDTSNSAFDDELQSIKQALGNYREATKLASSSSSSSSASNSSLPSLSSMPPMLQSLEMHAQEMANLLESLVQHFDLCVTAVKHTEGGGAAARSITGDMPAAVTVSGRGVPNIEQGIHDNLNAPLDPLSESDYQEMVNVLIKDAAEAEDVVMEIQDRIGDMESILENILSQRDVLLSIYNATIGVFRHLSSLATARLPGYIAQAHSFTRVWGEEHDRINGGLADLSDLNTLYDGFLEAYDGLILEVARRRHVRQRVEKVLRETKHKLDQLYEEDVNARETFRVEQGDYLPSDIWPGIGREPMRIEFRRISGGILKGAPPEQPDAQDQPAAEPNEPQSGPSETTEEGEIIPHLPKSLVEEALHRLKARNRQAM", "text": "FUNCTION: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). SUBCELLULAR LOCATION: Cytoplasm Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG17 family."}
+{"protein": "MKVINLIPTLMLTSLIILTLPIITTLLQNNKTNCFLYITKTAVTYAFAISLIPTLLFIQSNQEAYISNWHWMTIHTLKLSMSFKLDFFSLTFMPIALFITWSIMEFSLWYMHSDPHINRFFKYLLLFLITMLILVSANNLLQLFMGWEGVGIMSFLLISWWHGRTDANTAALQAMLYNRIGDMGFIMMMAWFTIHLNSWEFQQIFLTNPKNTTLPLLGLLLASAGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVMAGVFTLIRFYPLMENNLTIQTSTLCLGAITTLFTAICALTQNDIKKIIALSTSSQLGLMMVTIGINQPQLAFIHMCTHAFFKAMLFLSSGSIIHNLNNEQDIRKMGGLYKTMPITSTAIIIGSLALTGMPFLTGFYSKDPIIETANMSYINTWALLITLIAVSMTASYSTRIIFFALLGQPRYPPLTQVNENNPYLVNPIKRLILGSIFMGFLISMNTIPHTTPQMTMPPHLKFMALAVTLLGFTVATELNNMTHNLMFKQPSRMHTFSTMLGYYPTTTHRVLPYPSLTMSQNLATTIMDSIWLEKMIPKNLTTMQKTAASLVSNQKGLMKLYFLSFLLSITLGLLIAL", "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 5 family."}
+{"protein": "MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY", "text": "FUNCTION: Curlin is the structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. SUBCELLULAR LOCATION: Fimbrium. Note=Part of the curli surface structure. SIMILARITY: Belongs to the CsgA/CsgB family."}
+{"protein": "MAVDSTDQRRDFVVRIDGEDNGDSEKFWRESSINFWHNDKSSKPPGGEEDDGSFDFMRRSSEKSEEPDPPSKLINQFLNKQKASGDEISLDMEANMPELQKNTVPPLSSTAVSGSASPVTAPVTASYRNGTGDAIRRRQNRVTLSPSVKDGDSSEDEENRVDGSEVVKCTSNRSTMRTKTLMKMKTRSRLMDPPTPTYPDMVSGRTPRSGNLNPGFSGRNTKPGTPNQGGSKDLEEEEDPFSEEDLPEGLRKEKICVWVIIEWIFLILIIASLICSLVIPYLRGKTLWDLALWKWEVMVLVLICGRLVSSWIVKLFVYFVESNFLWRKKVLYFVYGIRKPVQNCLWLGLVLIAWHFLFDKKVEREMRSTVLKYVTKVLICLLVAVIIWLIKTLLVKVLASSFHMSTYFDRIQESLFTQYVIETLSGPPRIEIHIEEEKVANDVKTFEIVGRKLSPLGPKAVSSPPQVTVGSGRLQKSPSRVGKSPVLSRSGSKKEGGEEGIRIDHLQRMNTKNVSAWKMKKLMNVIKKGTLSTLDEQIQDTTTQEDDKATQIRSEFEAKLAARKIFQNVAEPGSRYIYMEDFMRFLSEDESERAMDLFEGASECHKISKSCLKNWVVNAFRERRALALTLNDTKTAVNRLHRIVDVLVSIVILIIWLLILGIATTKFLLVISSQLLLVVFVFGNSCKTIFEAVIFVFVMHPFDVGDRCEIDGVQMIVEEMNILTTVFLRFDNQKIVYPNSLLGTKPIANYYRSPDMQDAIEFFVHIATPPEKTTALRQRILSYVDNKKDHWHPSPMIVFRDMCGLNSVKIAMWPTHKMNHQNMGERYVRRGQLLEEIGRLCRELDIEYRLYPLNINVKSLPAATPITSDRIPPSWNQQRSV", "text": "FUNCTION: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscS (TC 1.A.23) family."}
+{"protein": "MALILPCTFCTSLQKKNFPINRRYITNFRRGATTATCEFRIPVEVSTPSDRGSLVVPSHKVTVHDRQRGVVHEFEVPEDQYILHSAESQNISLPFACRHGCCTSCAVRVKSGELRQPQALGISAELKSQGYALLCVGFPTSDLEVETQDEDEVYWLQFGRYFARGPIERDDYALELAMGDE", "text": "FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions (Probable). Mediates alternative electron partitioning in conditions of acceptor limitation at photosystem I (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family."}
+{"protein": "MSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKKKASDGVTLTGINQTGDQVSQPNKHSSVSSYEKNQSYPTDWSDEESNNPFSSTDAKGDTNPFDEDTSPVMEVRVRALYDYEGQEQDELSFKAGDELTKMENEDEQGWCKGRLDNGQVGLYPANYVEPIQ", "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 junction, focal adhesion 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": "MALLCYNRGCGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPESVKPEVKTTEKKELSELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGNEENKKEEDNDEIKIGTSCKNGGCSKTYRGLESLEEVCVYHSGVPISHEGMKYWSCCRRKTSDFNTFLAQEGCTKGKHMWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFEQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLELPAAKKQEKQKDDTTD", "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": "MAEKDATASGDDAIRVSGMQFAYEVEDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVGGKNVVQVLSRSAFHDTQLVCSGDLSYLGGSWSKTVGSAGEVPLQGDFSAEHMIFGVEGTDPVRREKLIDLLDINLQWRMHKVSDGQKRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECDQRGATIVYATHIFDGLETWATHLAYIQDGELNRLSKMTDIEELKTSPNLLSVVESWLRSEIKLVKKKKKPVAPWKPSPFDNSPFRSSRHMAYYR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ABC transporter superfamily. ABCI family."}
+{"protein": "MLGICRGRRKFLAASLTLLCIPAITWIYLFAGSFEDGKPVSLSPLESQAHSPRYTASSQRERESLEVRVREVEEENRALRRQLSLAQGQSPAHHRGNHSKTYSMEEGTGDSENLRAGIVAGNSSECGQQPAVEKCETIHVAIVCAGYNASRDVVTLVKSVLFHRRNPLHFHLIADSIAEQILATLFQTWMVPAVRVDFYNADELKSEVSWIPNKHYSGIYGLMKLVLTKTLPANLERVIVLDTDITFATDIAELWAVFHKFKGQQVLGLVENQSDWYLGNLWKNHRPWPALGRGYNTGVILLLLDKLRKMKWEQMWRLTAERELMGMLSTSLADQDIFNAVIKQNPFLVYQLPCFWNVQLSDHTRSEQCYRDVSDLKVIHWNSPKKLRVKNKHVEFFRNLYLTFLEYDGNLLRRELFGCPSETDVNNENLQKQLSELDEDDLCYEFRRERFTVHRTHLYFLHYEFEPSADNTDVTLVAQLSMDRLQMLEAICKHWEGPISLALYLSDAEAQQFLRYAQGSEVLMSRQNVGYHIVYKEGQFYPVNLLRNVAMKHISTPYMFLSDIDFLPMYGLYEYLRKSVIQLDLANTKKAMIVPAFETLRYRLSFPKSKAELLSMLDMGTLFTFRYHVWTKGHAPTNFAKWRTATTPYQVEWEADFEPYVVVRRDCPEYDRRFVGFGWNKVAHIMELDAQEYEFTVLPNAYMIHMPHAPSFDITKFRSNKQYRICLKTLKEEFQQDMSRRYGFAALKYLTAENNS", "text": "FUNCTION: Bifunctional glycosyltransferase with both alpha-1,3- xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation of alpha-dystroglycan (DAG1) by glycosylation leading to DAG1 binding to laminin G-like domain- containing extracellular proteins with high affinity (PubMed:23125099, PubMed:23135544, PubMed:25138275, PubMed:32975514). Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (By similarity). Requires the phosphorylation of core M3 (O-mannosyl trisaccharide) by POMK to elongate the glucuronyl-beta-1,4-xylose-beta disaccharide primer (PubMed:32975514). Plays a key role in skeletal muscle function and regeneration (PubMed:15184894, PubMed:24132234). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: In the C-terminal section; belongs to the glycosyltransferase 49 family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 8 family."}
+{"protein": "MSTPTSFTFNIAYSVPINKDPSQPTLTLEEFWRGLHRGSEKPQLFAEYVADTEVLPNSKSANEFQRKLIMANGAVHTAKGVELLQDVRNADGLLDDGPDALYLTAVYELHVPDVEPGSERAKEIEREYAQLALGAARTVVETIRRWKVEGGLEDA", "text": "FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of acetylaranotin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide (PubMed:23586797). The first step of acetylaranotin biosynthesis is performed by the NRPS ataP which produces diketopiperazine cyclo-L-Phe-L-Phe via the condensation of 2 phenylalanines (L-Phe) (PubMed:23586797). The ataC domain of ataTC then catalyzes the formation of bishydroxylation of cyclo-L-Phe-L-Phe (PubMed:23586797). The glutathione S-transferase domain ataG in ataIMG further catalyzes the conjugation of two glutathiones to the bishydroxylated intermediate (PubMed:23586797). Next, the dipeptidase ataJ removes the Glu residues (PubMed:23586797). The following step is performed by the carbon sulfur lyase domain ataI of ataIMG which may convert the bis-cysteinyl adduct to yield an epidithiol intermediate (PubMed:23586797). The ataT domain from ataTC then catalyzes the oxidation of the free dithiols, followed by a cyclization step catalyzed by the cytochrome P450 ataF (PubMed:23586797). AtaF probably acts as an epoxidase to promote a dual epoxidation formation at C8 and C9 along with C8' and C9', followed by the spontaneous nucleophilic attack of the amide nitrogens N10 and N10' to yield an intermediate with the pyrrolidine partial structure (PubMed:23586797). The final steps of acetylaranotin biosynthesis involve the acetylation and ring rearrangement of an epitetrathiodiketopiperazine intermediate to produce acetylaranotin (PubMed:23586797). AtaH probably catalyzes the acetylation of epitetrathiodiketopiperazine to produce a diacetate and ataY is responsible for the formation of the dihydrooxepin moiety that converts the diacetate intermediate to acetylaranotin via acetylapoaranotin (PubMed:23586797). Both enzymes could function independently in the absence of the other (PubMed:23586797). The specific function of ataL within the pathway has still to be determined (PubMed:23586797). The acetylaranotin bis-thiomethyltransferase ataS located outside of acetylaranotin gene cluster is the main thiomethyltransferase responsible for converting acetylaranotin and its related intermediates to their methylated forms (PubMed:30096370)."}
+{"protein": "MPPNFGGFFMVRSYYPSECHADYFDFERIEALKPAIEACGISTLSQSPMLGFHKQMDNRIKLLEEILSFRMQGVEFDNGDMYVYGHKAASDVRDEFVSVTEKLMDELAQCYNVLPQLDINNTIDHPPEGDEKWFLENEKTVTQFCRKLAAERPLKDIRDEYNYPKKKGIKDECSRLLEASTMKSRRGFTIQRLMNAMRQAHADGWFIVFDTLTLADDRLEAFYDNPNALRDYFRDIGRMVLAAERRKANDSHADCYQYFCVPEYGTANGRLHFHAVHFMRTLPSGSVDPNFGRRVRNRRQLNSLQNTWPYGYSMPIAVRYTQDAFSRSGWLWPVDAKGEPLKATSYMAVGFYVAKYVNKKSDMDLAAKGLGAKEWNNSLKTKLSLLPKKLFRIRMSRNFGMKMFTMTNLSMECLIQLTKLGYDATPFNQILKQNAKREMRLRLGKVTVADVLAAQPVTTNLLKFMRASIKMIGVSNLQSFIASMTQKLTLSDISDESKNYLDKAGITTACLRIKSKWTAGGK", "text": "FUNCTION: The A* protein binds to double-stranded DNA and prevents their hydrolysis by nucleases. FUNCTION: The A protein is a specific endonuclease that cleaves the viral strand of supertwisted, closed circular DNA at a unique site in the A gene. The A protein also causes relaxation of supertwisted DNA and forms a complex with viral DNA that has a discontinuity in gene A of the viral strand."}
+{"protein": "MVVLQPDPFLSELTSMYERSTEKGSVWVTMKRSSMKCQARLKKMAAKGEAVEYRCLVRATDGKKNICTALSAKEYLKFQASYATVLKAHMHALKKRERKDKKKAAEVEKIPEKAPKKQKKAPSSKKSAGSKS", "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). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP (By similarity). The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SRP14 family."}
+{"protein": "MLDCGKKAVKSQVISGRLEKFVRLDSMDSRYSQTSDTGLNRCTLNLQGPTRGGGAQGNNVSSGSFKKGFRKGSKGLWSIGRSIGLGVSRAVFPEDLKVSEKKIFDPQDKFLLLCNKLFVTSCILAVSVDPLFLYLPFVKDNEKCIGIDRKLAIIATTLRTVIDAFYLFHMALRFRTAFVAPSSRVFGRGELVIDPAQIAKRYLQQYFIIDFLSVLPLPQIVVWRFLYISKGASVLATKRALRSIILVQYIPRFIRLYPLSSELKRTAGVFAETAWAGAAYYLLLYMLASHIVGAIWYLLALERYNGCWTKVCSNSSLDCHRNFLFCGNEKMDGYAAWTTIKDSVLQLNCPVNTTDNPPFDFGIYLRALSSGIVSSKSFVSKYFFCLWWGLQNLSTLGQGLETSTYPGEVIFSIALAIAGLLLFALLIGNMQTYLQSLTIRLEEMRVKRRDSEQWMHHRMLPPELRERVRRYDQYKWLETRGVDEENLVQNLPKDLRRDIKRHLCLALVRRVPLFENMDERLLDAICERLKPCLYTESSYLVREGDPVNEMLFIIRGRLESVTTDGGRSGFFNRSLLKEGDFCGEELLTWALDPKSGSNLPSSTRTAKALTEVEAFALIADELKFVASQFRRLHSRQVQHTFRFYSQQWRTWAAIFIQAAWRRYVKKKKLEQLRKEEEEGEGSVTSIRATFLASKFAANALRKVHKNRIEAKSTIELVKYQKPSEPDFSADDTS", "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": "MTVSFEKTSDTKGTLSFSIDQETIKTGLDKAFNKVKANISVPGFRKGKISRQMFNKMYGEEALFEEALNAVLPTAYDAAVKEAGIEPVAQPKIDVAKMEKGSDWELTAEVVVKPTVSLGDYKDLTVEVEATKEVSDEEVETRLTNSQNNLAELVVKETAAENGDTVVIDFVGSVDGVEFEGGKGSNHSLELGSGQFIPGFEEQLVGTKAGETVEVKVTFPENYQAEDLAGKEALFVTTVNEVKAKELPELDDELAKDIDEEVETLDELKAKFRKELEESKAEAYNDAVETAAIEAAVANAEIKEIPEEMIHEEVHRAMNEFLGGMQQQGISPEMYFQITGTSEDDLHKQYEADADKRVRTNLVIEAIAAAENFTTSDEEVKAEIEDLAGQYNMPVEQVEKLLPVDMLKHDIAMKKAVEVIATTAKVK", "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": "MKGFTATLFLWTLIFPSCSGGGGGKAWPTHVVCSDSGLEVLYQSCDPLQDFGFSVEKCSKQLKSNINIRFGIILREDIKELFLDLALMSQGSSVLNFSYPICEAALPKFSFCGRRKGEQIYYAGPVNNPEFTIPQGEYQVLLELYTEKRSTVACANATIMCS", "text": "FUNCTION: May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space. Note=Associated with CD180 at the cell surface."}
+{"protein": "MGVPLLDVSQLQAGPEARKQYLQALVQSFRDYGFVRLTKHDVPAKRVQRIFDLSTQMFNLDIDSKLEFANIADGSPQRGYSAVGVEKTASLHGNLIGRRVDEKLTDAREHFDCGSPLDKSFANRWPEKLQGFQQELESFYFELEQVTAGILGSLEEALNCPPGTLNNMITKENNASELRLNHYPPVPAGTLRNGNVARIWPHFDLGVITLLFTSAVGGLEVEDRNAPGPQTFIPVEPETEAELIVNISETLQRWTDDHLPAGLHRVTIPKDLDTEIQNDANVEIPGRYSIAYLCKADREADVGTLPVFQTGEAPRYKAMTASEYHRSRLLTAY", "text": "FUNCTION: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties (PubMed:29373009). These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment (PubMed:29373009). The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:29373009). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate- dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4- methylpyrroline-5-carboxylate that is further converted to 2S,3S- methylproline by the pyrroline-5-carboxylate reductase ucsG (PubMed:29373009). Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction (PubMed:29373009). Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL (PubMed:29373009). This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition (PubMed:29373009). Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine (PubMed:29373009). The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
+{"protein": "GKEGYPVDSRGCKVTCFFTGAGYCDKECKLKKASSGYCAWPACYCYGLPDSVPVYDNASNKCB", "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). This toxin is only active against insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
+{"protein": "MGNNVVVLGTQWGDEGKGKIVDLLTERAKYVVRYQGGHNAGHTLVINGEKTVLHLIPSGILRENVTSIIGNGVVLSPAALMKEMKELEDRGIPVRERLLLSEACPLILDYHVALDNAREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVADILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTRVGAGPFPTELFDETGEFLCKQGNEFGATTGRRRRTGWLDTVAVRRAVQLNSLSGFCLTKLDVLDGLKEVKLCVAYRMPDGREVTTTPLAADDWKGVEPIYETMPGWSESTFGVKDRSGLPQAALNYIKRIEELTGVPIDIISTGPDRTETMILRDPFDA", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylosuccinate synthetase family."}
+{"protein": "MKPTTISLLQKYKQEKKRFATITAYDYSFAKLFADEGLNVMLVGDSLGMTVQGHDSTLPVTVADIAYHTAAVRRGAPNCLLLADLPFMAYATPEQAFENAATVMRAGANMVKIEGGEWLVETVQMLTERAVPVCGHLGLTPQSVNIFGGYKVQGRGDEAGDQLLSDALALEAAGAQLLVLECVPVELAKRITEALAIPVIGIGAGNVTDGQILVMHDAFGITGGHIPKFAKNFLAETGDIRAAVRQYMAEVESGVYPGEEHSFH", "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. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanB family. SIMILARITY: Belongs to the PanB family."}
+{"protein": "MANTILKSTTRHIRIFTARVENNDLIADTSQLTLDIDPDNEFLWEQSTIEKIQSRFKELVECHTGADLTDYTLRRIGTELEGTLFSLLQAGELSYNPNARVLNYSMGLPRTTELS", "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; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I NdhM subunit family."}
+{"protein": "MKSLSYKRIYKSQEYLATLGTIEYRSLFGSYSLTVDDTVFAMVSDGELYLRACEQSAQYCVKHPPVWLTYKKCGRSVTLNYYRVDESLWRNQLKLVRLSKYSLDAALKEKSTRNTRERLKDLPNMSFHLEAILGEVGIKDVRALRILGAKMCWLRLRQQNSLVTEKILFMLEGAIIGIHEAALPVARRQELAEWADSLTPKQEFPAELE", "text": "FUNCTION: Induces low levels of natural DNA uptake by inducing transcription of the competence genes (the CRP-S regulon) required for DNA transformation. Induction of the CRP-S regulon also requires Sxy- activated promoter (CRP-S), cAMP receptor protein (CRP) and cAMP (PubMed:17068078, PubMed:22532864). Induces CRP-S site-containing genes which are involved in genome maintenance and transcription or encoding transposases and toxin-antitoxin pairs (PubMed:19502395). SIMILARITY: Belongs to the TfoX family."}
+{"protein": "MTDTPTQALPPKAPQAGPTVPGTVRRAVPGSAAAALVIAASHFAALSAFDPRILLVLLVIVVLASSGGLFAGLAATAVSALGLALRGLLSGDTVVADWQSLGLLTIAGAGIAVLGERLRRTRLDAVARDRALLAREAHLSSILDTVPDAMIVIDERGIMQSFSITAERLFGYSPSEVIGRNVSMLMPNPHRDQHDLYLSRYLTTGERRIIGIGRVVTGERKDGATFPMELAVGEMHSVSGRFFTGFIRDLTERQNTEARLQELQAELVHISRLTALGEMASTLAHELNQPLSAIANYIKGSRRLLDDGDPKRIPMLQGALDKAAEQALRAGQIIRRLRDFVSRGETERRVESLSKLIEEASALALVGAKEHGIQVRYQIDTSCDLVLADKVQVQQVLLNLMRNALEAMMDASRRQLLVQTTPAEDDMVTVSVCDTGHGISDEMRAQLFTPFVTTKAQGMGVGLSISRTIIEAHGGRIWAEPNAGGGTIFRFTLRTVDEEAMNDA", "text": "FUNCTION: Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MLNNLGANVLGPKDCDLPKAALTALHAGVNSFGQLPVGPNLADLGGGAGGGGSSGGVPVGGGVARLHISGGLCDNSNALNGGNGSSGNGNGNNNNGNGNNNNSMQQQDQKRHRTRFTPAQLNELERCFSKTHYPDIFMREEIAMRIGLTESRVQVWFQNRRAKWKKRKKTTNVFRTPGALLPSHGLPPFGANITNIAMGDGLCGTGMFGGDRWSVGVNPMTAGFGQLNQSSPLSSSLNSGLNSGINMGSALGAGSYQHYGLNALGDSMMYQHSVGGVSCGPSGSPSATTPPNMNSCSSVTPPPLSAQPNSSQNELNGEPMPLHQQQQQQTHQHQQQQTHQHHPMAPPTPTQQQQQLPQSMQSPSDGANDTLHSIAALRRRASELNAIPSYLQMAPHNYEHYNSNSNSVY", "text": "FUNCTION: May be involved in the development of the central nervous system. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily."}
+{"protein": "MSFELSAPVPLSDNSEAILEKEIGETVKIEGDLVEVYEINRTVDFIKSGNYNSVALQFPDEHLADSGKVASILTNLVEANVQILADTNYGSCCVDEVAAEHMSADAIVHYGRACLSPTSRLPVLYVFGRLPINLHKLEKCLTIPLDQNILLVSDTRWYYAQDSILKSLKTLGYQNVYESHLKERIEPNLEEASTSYTIPGRTYSLPKSLSLQDMTLLYIGPDSPTLSSILMSHYSLVNQFLSFDPLSNKIVEESSFTGAKLRRRYALVQRCRDAGVIGIVIGTLGVHRYLHVLNQLRKMILNAGKKPYMLAVGKLNPAKLANFQEIECFVLIACGENSLIDSKEFYRPIVTPFELVKALSSDMSWNNDFILSFDEVLKLSEGKQSKEPSEVLTEESAEPHFSLITGKFVNSTPMRHLDVTLETADAKNNDSSSASIEKRGMRSLAVNGVYSPAAAFLQSKSWSGLDSVDEGEGPSKLYEGQSGIAKGYVGEGSKEKIQRDFGK", "text": "FUNCTION: 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 similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the dph1 subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily."}
+{"protein": "MADNMTTTQIEVGPGATNATINFEAGILECYERLSWQRALDYPGQDRLNRLKRKLESRIKTHNKSEPESKRMSLEERKAIGVKMMKVLLFMNPSAGIEGFEPYCMKNSSNSNCPNCNWTDYPPTSGKCLDDIEEEPENVDDPTEIVLRDMNNKDARQKIKEEVNTQKEGKFRLTIKRDIRNVLSLRVLVNGTFLKHPNGYKSLSTLHRLNAYDQSGRLVAKLVATDDLTVEDEEDGHRILNSLFERFNEGHSKPIRAAETAVGVLSQFGQEHRLSPEEGDN", "text": "FUNCTION: Binds and inhibits the conjugation of the ubiquitin-like G1P2/ISG15 protein to its target proteins. Since G1P2/ISG15 is an early antiviral protein, NS1 may inhibit the host antiviral response. Prevents EIF2AK2/PKR activation, either by binding double strand RNA or by interacting directly with EIF2AK2/PKR. Also binds poly(A) and U6 snRNA. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the influenza B viruses NS1 family."}
+{"protein": "MALMTWTAAEFGTNVGFADDQHKTIFDMVNKLHDTAATGNRSEIGKQLDALIDYVVMHFKSEETEMQKKGYADFAAHKAEHDKLVGVCADLQKKFHAGEAEVNQDTTRFVRDWLVNHIPKVDKLYGPCLSA", "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": "MATVREKAVALDLCATYSPSQRPPGPNGSHRPFRATYIWSSIIQVLYTQVEVKKRRHHLKYHHDCFIGSEAVDVVFAHLVQHKYFGDMDIPRSKVVRVCQALMDCKVFEPIVTACMFGREKKRTVFEDSSCSLYRFLNSSNLLGVQVEKSNGRCTPQRPKHSSFQSASLQSPSLEDLWDNLSLTPADPTHINLTSNLPPKVVAEVWQEQTIRRLLQLVDLPLLDSLLEYTPVAPRIPNVKEEDHNLTSNYLDREILKAFSDAQADEWVSAAVDCLDFLPDHMVVDVSRNLPEQQAPDSKWKLLLFDTIGKHYSQNRAPLLRNQLFDIHTGIAELLVNGKTEPALEATQLCLKLLDSPSREEFRRLLYFMALAADPSEFRLNEETDNRMTVKRMFCRAIVNNKSLSKGKCDLLVLFILDHHKDVFKIPGSLHKMVSDKLVAIQQGTDPDRDTGYTFCQRVDKREFDSAAQNNTRTELCALLKTIYENNSLSPKEKKRLLGQFYKSHPETFIQYFGDRVSSVYT", "text": "SIMILARITY: Belongs to the DEPDC7 family."}
+{"protein": "MEVTRQNFKEVLPEVCNAVQEADFISIDGEFTGISDGPSVSALTNGLDTPEERYTKLRKHSMNFLLFQFGVCTFRYDQNQSTYITKAFNFYIFPKPFSRTSPDIKFICQSSSIDFLASQGFDFNKVFRSGIPYLNQEEECQLREQYEERRGQMNGAGPVSYTPPSGTGVCNVPEDQREFIRSVEEKVEALLKNTDQTLDLEPCTGFQRKLIYQTLNSKYSKGLHVEALETEKKERFIQISKVDDEERRRREQQKQQREQEELNDAVGFSRVIRAISKSGKLVVGHNMLLDVMHTIHQFCGPLPEELDDFKEVAMTVFPRLLDTKLMASTQPFKEIIHNTSLAELHKQLRQKPFRPPTTECPEGLQSYDTSTEQLHEAGYDAFITGLCFISMANYLGSFLTPPKSHISARSKLLEPFYNKLFLMRVIDIPYLNMSGPDLQPKRDHVLYVTFPKEWKTSDLYQLFSAFGNIQVSWVDDTSAFVSLSQTEQVQIAMNTSRYAESYRIQTYAEYLQSRQKNTHSSRKWASDGWADTSYPSVAMTTASGYSHTDNWHQAVKRSISPSLDEQNHGADSSWTNYSVKKIKTEGSCTQTYADVAGSCDWPRLQADEGGASVSPVAEEAELDEFSANQSQGKRSRKHKKRKSDASETTPPALFDVPQVW", "text": "FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. 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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CAF1 family."}
+{"protein": "MIFKVKFEVTQMILTSLINKSAKALVIVAFVAAPFLAHADDAQKPAVHVTYEPQLDNQRDPNQYCAKCHKFDKIDKNQTLDQSGGELHFGKFHGAHLDKKNPNNGKAITCVSCHGNISENHRRGAKDVMRFEGDIFGNKKPMYSVQEQNQVCFACHQPDKLREKLWAHDVHAMKLPCASCHTLHPKEDAMKGIQPKQRVKLCVDCHGEQQKRKAEQDKLIEQKDKL", "text": "FUNCTION: Plays a role in nitrite reduction. SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MTMAARLMLVAALLCAAAAAATAQQATNVRATYHYYRPAQNNWDLGAPAVSAYCATWDASKPLSWRSKYGWTAFCGPAGAHGQAACGKCLRVTNPATGAQITARIVDQCANGGLDLDWDTVFTKIDTNGIGYQQGHLNVNYQFVDCRD", "text": "FUNCTION: Shows antifungal activity towards B.cinerea and towards the wheat-specific pathogenic fungi F.culmorum and F.graminearum (groups 1 and 2)."}
+{"protein": "MPRAAPPALLLPLLGLAAAAAADCPSSTWVQFQDSCYIFLQEAIKVESIEDVRNQCTNHGADMISIHNEEENAFILDTLKKQWKDPADILLGMFFDTDDASFKWFDNSNMTFNKWSDQEDDEELVDTCAFLHTKTGDWKKGNCEVSSVEGTLCKAAIPYEKKYLSDNRILISALVIASTVILTVLGAVVWFLYKRSLDSGFTTVFSAAHQSPYNDDCVLVVAEENEYDIQFN", "text": "FUNCTION: Potential multifunctional C-type lectin receptor that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Cell projection, filopodium Cytoplasm, cell cortex Cell projection, microvillus Note=Colocalizes with F-actin in filopodia, cellular cortex and microvilli of the apical cell surface."}
+{"protein": "MQQSLNLKMPSPEFYGNTGGWLRSSDIEEKYAITWSSKNEDIFEIPTGGVAKMKAGDNLLYLAKKEQCLALGNQLKIKFKILNFKIYRIFPNGEAQFLHPKDGVFPEKVNEGRKPIGKIDHNIGKNLNPAEVKFTHKTIF", "text": "FUNCTION: PsaD can form complexes with ferredoxin and ferredoxin- oxidoreductase in photosystem I (PS I) reaction center. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the PsaD family."}
+{"protein": "MPELTRRRALGAAAVVAAGVPLVALPAARADDRGHHTPEVPGNPAASGAPAAFDEIYKGRRIQGRTVTDGGGHHGGGHGGDGHGGGHHGGGYAVFVDGVELHVMRNADGSWISVVSHYEPVDTPRAAARAAVDELQGARLLPFPSN", "text": "FUNCTION: This protein may function to deliver copper to tyrosinase. SIMILARITY: Belongs to the melC1 family."}
+{"protein": "MGLAAPRKRTKISHDPNNTTWSRSTDGFGHRILKAQGWTPGSFLGPRNAAHSDLFTTASASHIRVVLKDDNLGLGARPKRGLLDEPTGLDAFKGLLGRLNGKSETQLVVEQQKRDDIKLARYAAAKWQAVRFVSGGLLVQESNETLVPPTSQNGQADSEVKNVPQGREEGLADDETTNSDSEDRHSVEKRKKKETNSRGSREKERKREKRQMRRDKKRKTSESTESEAEMQEKTRVQGPSEDVKPTEPKAPTLSRERRPMGRQMFRGRYIAQKKRALMDDKSLNEIFMIST", "text": "FUNCTION: Involved in rRNA-processing at A0, A1 and A2 sites and regulates negatively telomerase. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the PINX1 family."}
+{"protein": "MAANKGKSQGSLVLHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKSEEDKIPLLVVGNKSDLEERRQVPVDEARGKAEEWGVQYVETSAKTRANVDKVFFDLMREIRAKKMSENKDKNGRKSSKSKKSFKERCCLL", "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 (By similarity). 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 (By similarity). 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). 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": "MDLIGLLKSQFLCHLVFCYVFIASGLIVNAIQLCTLVIWPINKQLFRKINARLCYCVSSQLVMLLEWWSGTECTIYTDPKASPHYGKENAIVVLNHKFEIDFLCGWSLAERLGILGNSKVLAKKELAYVPIIGWMWYFVEMIFCTRKWEQDRQTVAKSLLHLRDYPEKYLFLIHCEGTRFTEKKHQISMQVAQAKGLPSLKHHLLPRTKGFAITVKCLRDVVPAVYDCTLNFRNNENPTLLGVLNGKKYHADCYVRRIPMEDIPEDEDKCSAWLHKLYQEKDAFQEEYYRTGVFPETPWVPPRRPWSLVNWLFWASLLLYPFFQFLVSMVSSGSSVTLASLVLIFCMASMGVRWMIGVTEIDKGSAYGNIDNKRKQTD", "text": "FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Exhibits high acyl-CoA specificity for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA (22:6-CoA, DHA-CoA) (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family."}
+{"protein": "MADQDQLKALRLRIDSLDEKLLELISERARCAQDVARVKTQTLGEGEAPVFYRPEREAWVLKHIMQLNKGPLDNEEVARLFREIMSSCLALEQPLKVAYLGPEGTFTQAAALKHFGNAVISTPMAAIDEVFREVAAGAVNFGVVPVENSTEGAVNHTLDSFLEHDMVICGEVELRIHHHLLVGETTKTDNITRIYSHAQSLAQCRKWLDSHYPSVERVAVSSNADAAKRVKSEWNSAAIAGDMAASLYDLSKLHEKIEDRPDNSTRFLIIGNQEVPPTGDDKTSIIVSMRNKPGALHELLVPFHNNGIDLTRIETRPSRSGKWTYVFFIDFVGHHKEPLIKDVLEKIGQEAVALKVLGSYPKAVL", "text": "FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MRSGDAEIKGIKPKVIEEYSLSQGSGPSNDSWKSLMSSAKDTPLQYDHMNRESLKKYFNPNAQLIEDPLDKPIQYRVCEKCGKPLALTAIVDHLENHCAGASGKSSTDPRDESTRETIRNGVESTGRNNNDDDNSNDNNNDDDDDDDNDDNEDDDDADDDDDNSNGANYKKNDSSFNPLKRSTSMESANTPNMDTKRSKTGTPQTFSSSIKKQKKVKQRNPTEKHLIDFNKQCGVELPEGGYCARSLTCKSHSMGAKRAVSGRSKPYDVLLADYHREHQTKIGAAAEKRAKQQELQKLQKQIQKEQKKHTQQQKQGQRSKQRNVNGGKSAKNGGKSTVHNGNNINEIGHVNLTPEEETTQVLNGVSRSFPLPLESTVLSSVRYRTKYFRMREMFASSFSVKPGYTSPGYGAIHSRVGCLDLDRTTDYKFRVRTPQPINHLTNQNLNPKQIQRLQQQRALQAQLLSQQQQQQQQQQQHHSPQAQAQASTQQPTQGMVPNHFPGGATNSSFNANVSSKQIQQQQQQQQHKSQDTGLTPLEIQSQQQKLRQQQLQQQKFEAAASYLANATKLMQESNQDSHLSGTHNNNSSKNGNNNLMTMKASISSPNTSVNSIQSPPSVNSVNGSGQGVSTGINVSGNNGRIEVGIGNSVNPYNGRIN", "text": "FUNCTION: Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. 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). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ataxin-7 family."}
+{"protein": "MTEEKKINPPIFPFTAIVGQEEMKLALQLNVIDPKIGGVMIMGDRGTGKSTTIRAIADLLPEIEVVKDNQFNTAPSEDLNEEIVKIKTPMIDLPLGATEDRVCGTIDIEKALTDGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGLNTVEREGISIRHAARFVLVGSGNPEEGELRPQLLDRFGMHAVIKTVKDPKLRVRVVEERTLFDLNPEEWINKYREQQEALKTRIIAAQNLISSVTISDDFKLKISQVCSELDVDGLRGDIVTNRAAKAYAAFNNRTEVEIGDIEKVITLCLRHRLRKDPLETIDSGDKVQKLFEEIFD", "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": "MDQPAVATASTSIREDLVGGESFITASKPAQKTSSFEREGWWRIALTDTPIPGTYHLKTFIEESLLNPVIATYNFKNEGRKKPPLVQRNNPVLNDLPQYMPPDFLDLLKKQVATYSFKDKPRPSPSTLVDKDQSLQLSPGQYNVLPAPVPKYASRSCVFRSTVQRFPTTYFIPHEGPGPGHYNVKMPPTSSVTSCFQSRVPRFLPSCSKTPGPGAYTTLRQFPKQSPTIAKMGQEHSLFFNNNNWLLK", "text": "FUNCTION: Maternal factor that plays a role in epigenetic chromatin reprogramming during early development of the zygote. Involved in the regulation of gametic DNA demethylation by inducing the conversion of the modified genomic base 5-methylcytosine (5mC) into 5- hydroxymethylcytosine (5hmC). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes in female and male zygote pronucleus. Associates preferentially with the paternal chromatin during zygote development."}
+{"protein": "MLEAKFEEASLFKRIIDGFKDCVQLVNFQCKEDGIIAQAVDDSRVLLVSLEIGVEAFQEYRCDHPVTLGMDLTSLSKILRCGNNTDTLTLIADNTPDSIILLFEDTKKDRIAEYSLKLMDIDADFLKIEELQYDSTLSLPSSEFSKIVRDLSQLSDSINIMITKETIKFVADGDIGSGSVIIKPFVDMEHPETSIKLEMDQPVDLTFGAKYLLDIIKGSSLSDRVGIRLSSEAPALFQFDLKSGFLQFFLAPKFNDEE", "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. Involved in DNA repair. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PCNA family."}
+{"protein": "MSNELDYRPVMLLQNDISLQKYSSPNDDDAWSKYLENPMTAATKAMMRANGDDDGVAALSLLYDYYRVPKEKRIITQGSTGRCDQVKRSCSEYESDISAYESTQIMRYLNDNNSSTHEYSETHKKNSYLSLDCLLNPSKLTLTSGKLDTNGHDDFMATTCDVYEKNSLNTLFDPIHVPSPQQRWQPDSTFKEDTPEPLIFNDILRRQAESTCSEDYIPGEANRDFEYTLESPKAIHIKSGESPMAYLNKGQFYPVNLRTAEIRKCVHLTSNKVKSVVMVVFDNEKNPEEQLKRWKHWHSRQPTAKQRVIDVADYKENCNTVENIEEVAYNALSFVWNVNDEAKIFIGLNCLSTDFSSQKGVKGVPLNLQIDTYDFETGVKRLIHRAVCQIKIFCDKGAERKMRDEERKQFRRKGKCADQNNKDIKASVLPGYRGSDVTYLRPVTDMETHPVLFIPNIHYSNLQRCGVILQSVADNSDRLSLKRSSQSFPKGLEAPPSKQQTSEDSHRVLLYVRRETEEVFDALMLKTPDLKGLRNAISEKYELPEERIFRVYKKCKRGILVNMDNNIIQHYSNHVAFLLDLTDVDGKIQVTLKEL", "text": "FUNCTION: Transcription factor playing important roles in primary neurulation and in the differentiation of stratified epithelia of both ectodermal and endodermal origin. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily."}
+{"protein": "MKIAEIHVYAHDLPVKDGPYTIASSTVWSLQTTLVKIVADSGLAGWGETCPVGPTYAPSHALGARAALAEMAPGLIGANPLQPLVLRRRMDGLLCGHNYAKAAIDIAAYDLMGKHYGVRVADLLGGVAAERVPSYYATGIGQPDEIARIAAEKVAEGFPRLQIKIGGRPVEIDIETVRKVWERIRGTGTRLAVDGNRSLPSRDALRLSRECPEIPFVLEQPCNTLEEIAAIRGRVQHGIYLDESGEDLSTVIRAAGQGLCDGFGMKLTRIGGLQQMAAFRDICEARALPHSCDDAWGGDIIAAACTHIGATVQPRLNEGVWVAQPYIAQPYDEENGIRIAGGHIDLPKGPGLGITPDESLFGPPVASFS", "text": "FUNCTION: Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha- ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. Can also catalyze the racemization of L- proline betaine. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family."}
+{"protein": "MRRISIVLLIVFATSIFPFSIWNSAGESEYKNLLSIKKASKVGDILTIVIRESNNVSSERESLEIQKTLLNILGNVVNAAAGVNLNNFIPINNNSPERQRGGKVQSSVVAKISAVVVDIDPYGNLVVEGRKTIKVDKDYQEIIVKGKVRPDDIEIGNEVDSSKLADSEIWVNGKLVFSEEPGKESFFDKILAFLAGLFT", "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 Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgH family."}
+{"protein": "MDAIYFFLTIALAVGLTMLFTWFKKNNITLKWNEWVLGILGLLLALFAIQHTYASATYEFEYTSAWIVGVIVLLLAVVPLLFAARSVRRRVDK", "text": "FUNCTION: May act as a membrane anchor for the chloroethene reductive dehalogenase VcrA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PceB family."}
+{"protein": "MNFMVLPPEVNSARIYAGAGPAPMLAAAVAWDGLAAELGMAAASFSLLISGLTAGPGSAWQGPAAAAMAAAAAPYLSWLNAATARAEGAAAGAKAAAAVYEAARAATAHPALVAANRNQLLSLVLSNLFGQNLPAIAATEASYEQLWAQDVAAMVGYHGGASTVASQLTPWQQLLSVLPPVVTAAPAGAVGVPAALAIPALGVENIGVGNFLGIGNIGNNNVGSGNTGDYNFGIGNIGNANLGNGNIGNANLGSGNAGFFNFGNGNDGNTNFGSGNAGFLNIGSGNEGSGNLGFGNAGDDNTGWGNSGDTNTGGFNSGDLNTGIGSPVTQGVANSGFGNTGTGHSGFFNSGNSGSGFQNLGNGSSGFGNASDTSSGFQNAGTALTRASSTWADSPRAWPIRAPSRLQVWRTRATTARECSIRVIISRVSSTGAPPQKKVGNSG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mycobacterial PPE family."}
+{"protein": "MELTLWTYEGPPHIGAMRIASSMKGVHYVLHAPQGDTYADLLFTMIERRGQRPPVTYTTFQARDLGGDTAELVKGHIREAVDRFKPEALLVGESCTAELIQDQPGSLAKGMGYEIPIISLELPAYSKKENWGAAETFYQLVRGLLKDSPKSESEHNPSKWKTEGRRPRVNLLGPSLLGFRCRDDVLEVQKILAHHGIDINVVAPLGAAPADIIRINEADANICLYPEIAESTCIWLERNFGHPYTKTIPIGVGATNDFLNEIHQLLGMELPKQEEEDGSQSRLTWYSKSVDSNYLTGKRVFIFGDGTHVLAASRIAHKELGFEVVGLGTYSREMARKVRDAAKELGLEALITNDYLAVEEAIKESAPELVLGTQMERHSAKRLGIPCAVISTPMHVQDVPARYSPQMGWEGANVIFDDWVHPLMMGLEEHLIGMFRHDFEFTDGHQSHLGHLGGHSTEKETKAPSFYQEKVQSSRPEHFPHWTPEGESELAKIPFFVRGKVRKNTEKYANQIGCKEIDGETLLDAKAHFNA", "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": "MAAAVATGVAPATMVDQVPSPTAQTSVQVPVSIPLPSPVVVADQTHPNSSLYAGDLDPKVTEAHLFDLFKHVANVVSVRVCRDQNRRSLGYAYINFSNPNDAYRAMEALNYTPLFDRPIRIMLSNRDPSTRLSGKGNIFIKNLDASIDNKALFETFSSFGTILSCKVAMDVTGRSKGYGFVQFEKEESAQAAIDKLNGMLMNDKQVFVGHFIRRQERARDENTPTPRFTNVYVKNLPKEIGEDELRKTFGKFGVISSAVVMRDQSGNSRCFGFVNFECTEAAASAVEKMNGISLGDDVLYVGRAQKKSEREEELRRKFEQERINRFEKSQGANLYLKNLDDSVDDEKLKEMFSEYGNVTSSKVMLNPQGMSRGFGFVAYSNPEEALRALSEMNGKMIGRKPLYIALAQRKEDRRAHLQALFSQIRAPGPMSGFHHPPGGPMPGPPQHMYVGQNGASMVPSQPIGYGFQPQFMPGMRPGSGPGNFIVPYPLQRQPQTGPRMGFRRGATNVQQHIQQQQLMHRNPSPGMRYMNGASNGRNGMDSSVPQGILPPIIPLPIDASSISHQKAPLLPISKLTSSLASASPADRTRMLGEQLYPLVERHEPLHVAKVTGMLLEMDQAEILHLMESPEALKSKVSEALDVLRLSVDPTDHDLGFSTTD", "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 cytoplasm, affects both translation and mRNA decay. Inhibits the polyadenylated RNA degradation by the Rrp41p 3'-->5' exonuclease in vitro. Binds with the 5'UTRs of PAB2, PAB3 and with a lower affinity with the 5'UTR of PAB5. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family."}
+{"protein": "DCLKFGWKCNPRNDKCCSGLKCGSNHNWCKLHL", "text": "FUNCTION: Voltage-gated sodium channel Nav1.7/SCN9A inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 22 (Htx-4) subfamily."}
+{"protein": "MKLNISYPANGTQKLIEIDDDRRLRVFMEKRMGQEVPGDSVGPEFAGYVFKITGGNDKQGFPMFQGVLLPHRVRLLLRAGHPCYRPRRDGERKRKSVRGCIVGQDLAVLALAIVKQGEQDIPGLTDVTVPKRLGPKRASKIRRFFNLSKEDDVRQFVIRREVVPKKEGKKPYTKAPKIQRLVTPRTLQHKRHRFALKRRQAEKNREEAAEFAQLMAKRVAEAKQKKEVVKARRASSMKK", "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. eS6 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family."}
+{"protein": "MLDRIKVCFTESIQTQIAAAEALPDAISRGAIAMVQSLLNGNKILCCGNGTSAANSQHFAASMINRFEAERPSLPAIALNADNVVLTAIANDRLHEEIYAKQVRALGQAGDVLLAISTRGNSRDIVKAVESAVTRDMTIVALTGYDGGELAGLLGPQDVEIRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQND", "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": "MELDAILDNLSDEEQIELLELLEEEENYRNTHLLYEFTPYSKQREFIDAGHDYQSDVLWLVTSLVSHLLALLKSRFTLPGDTRERKVIRLMVNMAESGKVSVSMSQLSSGIGGETNETVTKTTQRILCGRIEENDEPGYGSPKEDSSWEKSSVLLILLIIFSLSHHRLMVLKMHSICYFKHTRRHRHAAGDTITAYGLTKRLPYSIYAEGLTRTNKYGQFSILTFTPLMGMSDGVTKFLKNPSKSQKVVNMTIYDAEHYTDEQKEQIIASYPEHEREARARGIPTMGSGRIFQIPEETIKCQPFECPDHFYVIDAQDFGWNHPQAHIQLWWDKDADVFYLARVWKKSENTAVQAWGAVKSWANKIPVAWPHDGHQHEKGGGEQLKTQYADAGFSMLPDHATFPDGGNSVESGISELRDLMLEGRFKVFNTCEPFFEEFRLYHRDENGKIVKTNDDVLDATRYGYMMRLRQDDARY", "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 full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. SIMILARITY: Belongs to the Lederbergvirus large terminase family."}
+{"protein": "MVGGGAKRRLRGEGPQCEKPVDMKKSKSCEADVPGDLRKEVESHYRLPLPEDFYHFWRFCEGLDPEQPADSLSASLGLRLVGPYDILAGKHKIKKKSASLNFNLHWRFYYDPPEFQTIIIGDSKTQFHMGYFRDSPDELPVFVGTNEAKKNCIIVQSGDNVFAAVKLFLMKKLKEVTDKKKSSLLKTIDEKLTEAARELGFSLEQRTVRMKQRDKKVVTKTFHGAGLVVPVDKNDVGYRELPETDASLRRICGTIVEAPSDADRLQAFAPVQEMMTYVQFANDECDYGMGLELGLDLFCHGSHYFHKVAGQLLPLAYNLLKRNLFAEIIEAHLANRSQDDVDQLAA", "text": "FUNCTION: Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response. Initiates the repair of double-strand DNA breaks: recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins. Serine ADP-ribosylation of target proteins, such as histones, promotes decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. HPF1 acts by completing the active site of PARP1 and PARP2: forms a composite active site composed of residues from HPF1 and PARP1 or PARP2. While HPF1 promotes the initiation of serine ADP-ribosylation, it restricts the polymerase activity of PARP1 and PARP2 in order to limit the length of poly-ADP-ribose chains. HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1. SUBCELLULAR LOCATION: Chromosome Nucleus Note=Localizes to DNA damage sites; chromatin localization is dependent on PARP1 and PARP2. SIMILARITY: Belongs to the HPF1 family."}
+{"protein": "MESLNALLQGMGLMHLGAGQAIMLLVSLLLLWLAIAKKFEPLLLLPIGFGGLLSNIPEAGMALTALESLLAHHDAGQLAVIAAKLNCAPDVHAIKEALALALPSVQNQMENLAVDMGYTPGVLALFYKVAIGSGVAPLVIFMGVGAMTDFGPLLANPRTLLLGAAAQFGIFATVLGALTLNYFGLIAFTLPQAAAIGIIGGADGPTAIYLSGKLAPELLGAIAVAAYSYMALVPLIQPPIMRALTSEKERKIRMVQLRTVSKREKILFPVVLLLLVALLLPDAAPLLGMFCFGNLMRESGVVERLSDTVQNGLINIVTIFLGLSVGAKLVADKFLQPQTLGILLLGVIAFGIGTAAGVLMAKLLNLCSKNKINPLIGSAGVSAVPMAARVSNKVGLESDAQNFLLMHAMGPNVAGVIGSAIAAGVMLKYVLAM", "text": "FUNCTION: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GcdB/MmdB/OadB family."}
+{"protein": "MDKMNPAHLLVLAAVCVSLLGASSIPPQALNLNQFRLMIKCTNDRVWADFVDYGCYCVARDSNTPVDDLDRCCQAQKQCYDEAVKVHGCKPLVMFYSFECRYLASDLDCSGNNTKCRNFVCNCDRTATLCILTATYNRNNHKIDPSRCQ", "text": "FUNCTION: Heterodimer: MitTx, a heteromeric complex between Kunitz- and phospholipase-A2-like proteins, potently, persistently and selectively activates rat and chicken acid-sensing ion channel ASIC1 (PubMed:22094702, PubMed:24507937). Both alternatively spliced rat isoforms ASIC1a and ASIC1b are activated, with a higher potency for ASIC1a (EC(50)=9.4 nM) vs ASIC1b (EC(50)=23 nM) (PubMed:22094702). The rat ASIC3 subtype is also sensitive to the heterodimer, but with a lower potency (EC(50)=830 nM) (PubMed:22094702). On rat ASIC2a, the toxin shows a very weak activation, but produces a remarkable potentiation (>100-fold) of protons when the extracellular pH drops below neutrality (PubMed:22094702). Moderate and weak activations are also observed on the heterotrimers Asic1a-Asic2a and Asic1a-Asic3 (expressed in CHO cells), respectively (PubMed:22094702). The binding sites of the beta subunit of MitTx and the spider psalmotoxin-1 toxin overlap, explaining why these toxins are mutually exclusive (PubMed:22094702, PubMed:24507937). In vivo, the heterodimer elicits robust pain-related behavior in mice by activation of ASIC1 channels on capsaicin-sensitive nerve fibers (PubMed:22094702). FUNCTION: Monomer: does not have phospholipase A2 activity but may maintain some lipid-binding character from its PLA2 lineage, which could aid in effecting neuronal depolarization. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. K49 sub-subfamily."}
+{"protein": "MTGKQGVALSESLNPAEKTSLVINGGSLQPKISATNPPPRCTGFGIQEILGLNKEPATAPRSPLSALPAGAHLIAARSVLGPAGVGVGMGLIGPAGIPSFYSQPAFLETVLADGHDVRLQPHNRSARPLDANQSVSSDSEDLSSSERKLSKSSVNQSKKRKKRRHRTIFTSYQLEELEKAFNEAHYPDVYAREMLAMKTELPEDRIQVWFQNRRAKWRKREKCWGRSTVMAEYGLYGAMVRHSIPLPESILKSAKDGIMESCAPWLLVQDGLPINRRYSKSEYPQLFAGMHKKSMEAANLPATAKCDAPQQPSAQRSEDVEAEEKRSDGKSTISKEEMRENSIAALRAKAQEHSAKVLGTVSPGKLLEGKQEKQAVGEKVSEPPSPTEEQKSP", "text": "FUNCTION: Acts as a transcriptional regulator (By similarity). Mediates the differentiation of V2a interneurons (By similarity). Plays a role in eye development and organization of the neuroretina (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family."}
+{"protein": "MDDLEQAIVISFETGAVDSALKSQAVTYCQQIKETPSICSICIEKLWFSKLVQVQFWCLQTLQDVLRVKYGSMSLDEQSYVRKSVFSMACLEVIDNENAGRVVEGPPFVKNKLAQVLATLIYYEYPLIWSSVFLDFMLHLCKGAVVIDMFCRVLNALDDELISLDYPRTPEEISVAARVKDAMRQQCVPQIARAWYDIVSMYKNSDPDLSATVLDCMRRFVSWIDIGLVANDAFVPLLFELILSDGLSEQVRGAAAGCVLAMVSKRMDPQSKLPLLQTLQISRVFGLVSGDVDSDLVSKVSALLTGYAVEVLECHKRLNSEDTKAVSMDLLNEVLPSVFYVMQKCEVDSTFSIVQFLLGYVSTLKGLPALKEKQLLHITQILEVIRIQICYDPMYRNNLNSLDKTGLEEEDRMSEFRKDLFVLLRTVGRVAPEVTQHFIRNSLANAVESSSESNVEEVEAALSLLYSFGESMTEEAMKTGSGCLSELIPMLLTTQFPGHSHRLVALVYLENITRYMKFIQENSQYIPNVLGAFLDDRGLHHQNFYVSRRAGYLFMRVVKLLKSKLVPFIDKILQNLQDTLSQLTTMNFASRELTGTEDGSHIFEAIGIIIGLEDVPAEKQSDYLSLLLTPLCQQIEAGLVQAKVASSEDFPVKIANIQFAIVAINALSKGFNERLVTASRPGIGLMFKQTLDVLLRVLIEFPKVEPLRSKVTSFIHRMVDTLGSAVFPYLPKALEQLLADSEPKEMVGFMVLLNQLICKFNSALHDILEEVYPVVAVRIFNVIPRDGLPSRPGAVTEEMRELIELQRMLYTFLHVIATHDLSSVFLTPKSRAYLDPMMQLVLNTSCNHKDITVRKACVQIFIKLIKDWCAEPYSEEKVPGFQNFVIEAFATNCCLYSVLDKSFNFSDANTHALFGEIITAQKVMYEKFGNTFLMHLMSKSFPSAHIPQDLAEQYCQKLQGNDIRSLKSYYQSLIENLRLQQNGSHVFR", "text": "FUNCTION: Probable tRNA nucleus export receptor which regulates tRNA processing and facilitates tRNA translocation across the nuclear pore complex. Is required for proper activity of the shoot apical meristem (SAM) and correct leaf initiation at different developmental stages, and may play a role in floral patterning. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the exportin family."}
+{"protein": "MSDPQTSMAATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPSKNSFGILSSKGNILQIQGSQLSTSYPGGQLVFAIQNPTVVNKGTRSNTSIQYQAVPQIQASSPQTIQVQPSLTNQIQIIPGTNQAIITPSPSSHKPVPIKPAPVQKSSTTTTPAQSGANVVKLTGGGGNVTLTLPVNNLVNTSDPGAATQLLTESPPAPLSKTNKKARKKSLPAAQPPVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQQALRVVQAASATLPTVPQKPSQNFQIQAAEPSPTQVYIRTPSGEVQTVLVQDSPPATAATASTTTCSSPASRAAHLSGTSKKHSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPTQIQLQMEQALAGETQPGEKRRRMACTCPNCKDGDKRSGEQGKKKHVCHIPDCGKTFRKTSLLRAHVRLHTGERPFVCNWFFCGKRFTRSDELQRHARTHTGDKRFECAQCQKRFMRSDHLTKHYKTHLVTKNL", "text": "FUNCTION: Binds to GC box promoters elements and selectively activates mRNA synthesis from genes that contain functional recognition sites. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family."}
+{"protein": "MLLSLIVTFLGAFLTLLFMRPIAQKIGLVDKPNFRKRHQGAIPLIGGVSLFVGNLCFYLLEWEQMRLPTLYLFSIFVLLVIGMIDDRFDISPFLRAGIQAILAILMIDLGNLYLDHLGQILGPFQLTLGSIGLIITVLATIAAINAFNMIDGIDGLLGGLSSVAFVSIGILLIKDNQLDLAYWSFALIIAILPYFMMNLGIPFGQKFKVFMGDAGSTLIGFTIIWILLLSTQGKGHPMNPVTALWIIAIPLIDMIAIMYRRLRKGKSPFRPDRLHVHHLMMRAGLTSRQAFLLITFAAAICATIGILGEIFYINEWLMFAGFILLFFMYSYSITRAWRITRWIRRMRRRAKRIHNKG", "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": "MRKFSTYDLAQISLLACLIIVTGMFKIPTGIPGSEFQLSAPIAVAIAAVFGFKRYFLAGIIASLILFLLGIHSILNVEISIIFRLTVGLIIVLLGTSIPVLVVAGPIGTMVARLGLAFTLGTPFLPLFVLAIPGMVITAVSVYPITKMLYAINKKVAGDHHVRNVL", "text": "FUNCTION: Does not seem to be a permease of pimelate. Its role in biotin synthesis is not clear. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MAHYKAADSKREQFRRYLEKSGVLDTLTKVLVALYEEPEKPNSALDFLKHHLGAATPENPEIELLRLELAEMKEKYEAIVEENKKLKAKLAQYEPPQEEKRAE", "text": "FUNCTION: May control the transcriptional activity of MYC. Stimulates the activation of E box-dependent transcription by MYC. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Note=Translocates into the nucleus in the S phase of the cell cycle upon an increase of MYC expression. Found in the mitochondria when associated with AKAP1. SIMILARITY: Belongs to the AMY1 family."}
+{"protein": "MGIKTQKNFICLKRTFSMNLRDAISVANPVQLEEEIKHDEVVSFLKSKNLLDKPVILNVEGKKVAKNFVSSRETLGKYLGVDAYSIARELSKIEDREAEIRVEPFSSLAMKKVDVNLQELPVIKYFPRDGGRYITAGIVIAQRNGVYNASIHRMLLLDESRVAARLVPPRHTYLMWREAVEREEELEVAVVIGTHPLFLFASATRVPSGKEFSYAAGLMGRLTLYRKGEMLVPDSEIILFGRITAETAKEGPFVDITGTYDIVRDEPVIVFDEMYVKEDYIYYSITPAGKEHQMLMGVPYEPVIYRFVSNVCKVKNVITTPGSCHYFHCVVQIEKKSEGDGKNAIIAALAANPSMKGVVVVDDDIDILSYEDMEFAIATRFQPDRDLVVVKGARGSSLDPSADKTTSKWGIDATKPLGKEGFDRVV", "text": "SIMILARITY: Belongs to the UbiD family."}
+{"protein": "MDVTAKYELIGLMAYPIRHSLSPKMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGLKALKMRGTGISMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA", "text": "FUNCTION: The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. SIMILARITY: Belongs to the shikimate dehydrogenase family."}
+{"protein": "MRKVMNSPDDGNGRRRFLQFSMAALASAAAPSSVWAFSKIQPIEDPLKSYPYRDWEDLYRKEWTWDSTGFITHSNGCVAGCAWRVFVKNGVPMREEQVSEYPQLPGVPDMNPRGCQKGAVYCSWSKQPDFLKYPLKRVGERGERKWKRISWDEAFTEIADKIIDTTVKRGPGNVCMPKRPFAVITSAGYSRLANLIGAIKPDVSSMTGDLYPGIQTVRMPARTVSTFDDWFTSDLILMWHKNPIVTRIPDAHFLTEARYNGARLVNISPDYNPSSVHADLHLPVTTGTDSHLAAAIVNVLIADKKYKADYLKEQTDLPFLVRTDNGKFLREKDFNKDGSDEVFYIWDSKSGKAVLAPGSMGSKDKTLKLGAVEPALEGTFDANGIEVTTVFARLKAEIAPYTPEATHKTTGIHPSVVRQLAGWIGDCKALRILDGYNNQKHFDGFQCGRLKILILTLIGHHGTTGSIDTTYEGWVLEGNKALGGVKGRPGRSVSMVLAQWVWGEQYRRSKAYFDDTELREQIGFGVDEMEALRKESEANGWMPNWQSIKDPVVYINAGINTFATSTGYQHLRENFLKRCELYVVVDFRLNSGAMYADIVLPAATNLEKLDIRETSSTRFIHAFGQPIKPMYDRRTDWQISVGLARKIQERARARGITRVDDPEIKSFIDFDKVYDEFTMNGAVEKDEDALRFVMEKSKALGPGSYEEVLKRGFVGVGPSAGKTGPVPADKPYRPFTVNVSEKVPYKTLTGRLQFYIDHDWYQRFGATVPKPQYGGGVLGPKKYPFVYNTPHTRWGVHSFARTDQWMLRHQRGEPDVRLNPAAMARKGIKDGDQVRIFNSSGEFFAMAKAWPGLPENMLFSEHGWEQYLYKNMTHYNSVNAELINPLELVGGYGHVKFAAGGFNPNRIFHETTVDVEKA", "text": "FUNCTION: Terminal reductase that allows anaerobic growth on selenate as the sole respiratory oxidant. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family."}
+{"protein": "MYQIFVTKHDTAIQTSRFSVTGSITPVAPTGNIPVINTGNITAEHAVVSLYANLTAGTSSDGSFIVAMKVDTSPADPNCVISAGVNLSFAGTSYPIVGIVRFESASDQPTSIAGSQIEHYPIEMSVGSGGVCSARDCVTVDIHPRAFGNNVFVGVICSSAKWTSGRVLGTIATTQVIREYQVLQPLK", "text": "FUNCTION: Attaches the circulating virion to the bacterial lipopolysaccharides which serve as receptor for the virus. Determines the phage host-range. Probably triggers with protein H the injection of the phage DNA into the host cytoplasm upon conformational changes induced by the interaction with host lipopolysaccharides (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the microvirus G protein family."}
+{"protein": "MSLQRIVRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGRERADTRRWRFDATLEIIVVMNSPSNDLNDSHVQISYHSSHEPLPLAYAVLYLTCVDISLDCDLNCEGRQDRNFVDKRQWVWGPSGYGGILLVNCDRDDPSCDVQDNCDQHVHCLQDLEDMSVMVLRTQGPAALFDDHKLVLHTSSYDAKRAQVFHICGPEDVCEAYRHVLGQDKVSYEVPRLHGDEERFFVEGLSFPDAGFTGLISFHVTLLDDSNEDFSASPIFTDTVVFRVAPWIMTPSTLPPLEVYVCRVRNNTCFVDAVAELARKAGCKLTICPQAENRNDRWIQDEMELGYVQAPHKTLPVVFDSPRNGELQDFPYKRILGPDFGYVTREPRDRSVSGLDSFGNLEVSPPVVANGKEYPLGRILIGGNLPGSSGRRVTQVVRDFLHAQKVQPPVELFVDWLAVGHVDEFLSFVPAPDGKGFRMLLASPGACFKLFQEKQKCGHGRALLFQGVVDDEQVKTISINQVLSNKDLINYNKFVQSCIDWNREVLKRELGLAECDIIDIPQLFKTERKKATAFFPDLVNMLVLGKHLGIPKPFGPIINGCCCLEEKVRSLLEPLGLHCTFIDDFTPYHMLHGEVHCGTNVCRKPFSFKWWNMVP", "text": "FUNCTION: Catalyzes the deimination of arginine residues of proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein arginine deiminase family."}
+{"protein": "MITLRKLPIALAVAAGVLSTQAMAVDFHGYARSGIGWTASGGEQQCFQTTGAQSKYRLGNECETYAELKLGQELWKEGDKSFYLDTNVAYSVSQRDDWESTDPAFREANVQGKNLIESLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLETIDLGFGKLSVAATRNSESGGSSAWIDNQRENAKYTINNVYDVRLAGLETNPGGSLELGVDYGRADTQEGYSLAPNASKDGVMLTAEHTQSLMGGFNKFVVQYATDSMTSYNTGHSQGTSVNNNGHLLRVIDHGAINLAEKWDMMYVALYQDIDLDNNNGNTWYSVGVRPMYKWTPIMSTLLEAGYDNVKSQHTGERNGQYKLTLAQQWQAGDSIWSRPAIRVFATYANWDEKWGYSDTTGVAQDGTIGTNSRGKNNEVTFGAQFEAWW", "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. SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family."}
+{"protein": "MSADLAMGPELPTSPLALEYVNDFDLMKFEVKKEAMAAHDRANIRQCNRLQPQGSVSSTPISTPCSSVPSSPSFSPTEQKNHLEELYWMPSGAYPQQIDPQTLSLTPEDAVEALIGATAHGHPPPPHVQQQLQAGAFDGYRGAHHHHGHAQQQQQQQPQHHHHQHQYGAIPHHPDDLSGHPGAHGHHPHHHHHHHHSQDPDSPSPTSPEQLHHRHHHHHHPHGHPGQQGHHGVGGGLNVEDRFSDDQLVTMSVRELNRHLRGFTKDEVIRLKQKRRTLKNRGYAQSCRFKRVQQKHLLENEKTQLINQVEQLKQEINRLARERDAYKLKCEKLTGANGFREAGSTSDNPSSPEFFM", "text": "FUNCTION: May act as a transcriptional activator or repressor. Involved in neurogenesis. Involved in the development of rhombomeres (r) 5 and 6 segments from their common precursor 'proto-segment' in the hindbrain. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Maf subfamily."}
+{"protein": "MKDISRRRFVLGTGATVAAATLAGCNGNGNGNGNGNGNGEPDTPEGRADQFLTDNDALMYDGDITDETGQDEVVVVTGAGNNGFAFDPAAIRVDVGTTVTWEWTGDGGAHNVVSEPESDFEFESDRVDEEGFTFEQTFDDEGVALYVCTPHRAQGMYGAVIVE", "text": "FUNCTION: Electron donor. Binds one copper ion. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
+{"protein": "MERVYLDNNATTRLAPEALQAMLPFLTEEFGNPSSLHGQGRAPARALMAARRAVLELIGAEADSEILFTSGGTEADTTAIRSALAADPSRREIVTSTVEHAAVLALCDHLERQEGVTVHRIPVDGDGRLDIEAYRAALSPRVALVSLMWANNETGTVFPVEGLAELAHRAGALFHTDAVQAVGKVPIVLRGTEIDMLSLSAHKFHGPKGVGALWLRKGVPFQPLIRGGRQQRGHRAGTENIPGIVGLGRAAELALGGDHGAVRLLRDRLEQGILARVPKARVLGDPLDRLPNTSCVAFDFAEGEAIVMLLDRAGICVSSGAACASGAMEPSHVIRAMKVPFTAAHGAIRFSLSHWTTAAEIDRLLEVLPPIVDQLRALSPFGAEEVK", "text": "FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Seems to participate in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for the Fe-S core formation. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily."}
+{"protein": "MAFKRKTRWLWQVLILSVGLNMLFLLLFYSAIFRKDIYKLHLFSGPLIAKSSRKVYLSEDFLNEISQASLDDLISLFKDERYMYGRPIKLWALSVAIASHHIDITPVLSKPLTYTELKGSSVRWLLPNIDLKDFPVILDYLRCHKYPYTSKGLFLLIEKMVQEGWVDEDCLYHFCSTPEFLYLRTLLVGADVQASSVASLARMVIRCGSERFFHFCNEESRTSMISATQRQKVLKSYLDCEESLAALLLLVHDSDVVLHEFCDEDLEKVIRLMPQESPYSQNFFSRLQHSPRRELACMSTQRVEAPRVQEDQDEEYVVQDGDSLWLIAKRFGIPMDKIIQKNGLNHHRLFPGKVLKLPAKQS", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the chlamydial CPn_0593/CT_474/TC_0759 family."}
+{"protein": "MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGTWGTRPGWYPGTSVPGQPAQDGCPQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPDMSQYWPRLQ", "text": "FUNCTION: May be a transcription factor with important functions in eye and nasal development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family."}
+{"protein": "MGIQHEFDIIINGDIALRNLQLHRGDNYGCKLKIISNDYKKLKFRFIIRPDWSEIDEVKGLTVFANNYVVKVNKVDDTFYYVIYEAVIHLYNKKTEILIYSDDEKELFKHYYPYISLNMISKKYKVKEENYSSPYIEHPLIPYRDYESMD", "text": "FUNCTION: Inhibits antiviral activity induced by type I interferons. Does not block signal transduction of IFN, but is important to counteract the host antiviral state induced by a pre-treatment with IFN (By similarity). SIMILARITY: Belongs to the orthopoxvirus OPG027 family."}
+{"protein": "MNEYNNDNMEQEKEKKKEEQKYKNIIKKEYFIFPRLYDKNKEIEYNKLRIHNIKEYICIHLTISLFIILIECFVFSFNLNIKDTTYVEICVVIFSILNCLMHIVVLIKMYFFTSESVYTKGVFIGYIVLNQVFQFLSLYFFTKRNEQSKNDIAHLKYYDNSFNLYVHFFVDSVFILCLPALSFFLSVLFMMMFLCLNILLINMIKFNKTNYGSDIYHICLLSVVLLMFLILRYMMEERNRLLFFFIKDMMFDNYKKWYSDYIGAHYDKDKDSTTINGDNNKYEKEKCEDYKFLFSNKCILFHDFTLNACYKDYYSMICFLNKLLKSCNIKEDMSSNTSVNINGDTYQNMNFHDNINSNIPKNYNSFYEELKKNLNESDILTIAYEVEVLKNIKKINCDEIGKNWDYSFIDSEYGKSTLVILEVGYHLISPYIENNENKKKKLQLFLLLINSMYFPNPYHNANHGATVCHLSKCLAHITDYDSYLNNTYMICYLIASIAHDVGHPGKTNSYLSETNHILSIRYNDMSILENYHCSITFSILQLIGFDFLINNEDTKLVEKNNYTNMRKFIIELIISTDMKLHFEYVDIFKKRKKSQNFDISDTDAINLGTINIKLADIGHTCLKWKDHAKWTMLVSEEFFSQKRVEELHKNKNIDPLNFSNFGKEDNIDEGMIFNYENIYINYINNINNINTYDYSYIKLNFIHHHDFVKSIPSTQVYFFEIIVMPLIKELQSMEKSKKEITQKVLHNLNINLQTWRLIEKNINLFYNTEKMTGTDYYKNLEKQKLLRGIRLLDIAEEDVISLTKNFKEEIKHGKL", "text": "FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes (PubMed:18452584). Probably by regulating cGMP levels, required for activation of gametogenesis (PubMed:18452584). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family."}
+{"protein": "MYPEESRGSGGVATVDFLEGTYDYAAPTPAPTPLYSHSTTGCYSAPLDAHGPLSDGSLQSLGSGPTSPLVFVPSSPRLSPFMHPPSHHYLETTSTPVYRSSHQPVPREDQCGTRDEAYSVGELGAGAGGFEMTKDTRFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGMRKDRGRVLRREKRRACDRDKPAKDLPHTRASPQDGRKRAMSSSSTSGGGGRSSLNNMPPDQVLLLLQGAEPPILSSRQKMSRPYTEVTIMTLLTSMADKELVHMITWAKKLPGFLQLSLHDQVLLLESSWLEVLMIGLIWRSIQCPGKLIFAQDLILDRNEGTCVEGMAEIFDMLLATASRFRVLKLKPEEFVCLKAIILLNSGAFSFCTGTMEPLHDSAAVQHMLDTITDALIFHISHLGCSAQQQSRRQAQLLLLLSHIRHMSNKGMEHLYSMKCKNKVPLYDLLLEMLDAHRIHRPVKPFQSWSQGDRDSPTASSTSSSGGGGGDDEGASSAGSSSGPQGSHESPRRENLSRAPTGPGVLQYRGSHSDCTRIP", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily."}
+{"protein": "MIELSLIDFYLCFLAFLLFLVLIMLIIFWFSLELQDHNETCHA", "text": "SUBCELLULAR LOCATION: Host Golgi apparatus membrane; Single-pass membrane protein Host endosome membrane; Single-pass membrane protein."}
+{"protein": "MARKKIREYDSKRLLKEHLKRLANIDLQIRSAQVTESTDFTELTNQESWLSSTKLVVKPDMLFGKRGKSGLVALKLDLAEVADFVKARLGTEVEMEGCKAPITTFIVEPFVPHDQEYYLSIVSDRLGCTISFSECGGIEIEENWDKVKTIFLPAEKSMTLEVCAPLIATLPLEVRAKIGNFIMGAFAVFQDLDFSFMEMNPFTLVDGEPFPLDMRGELDDTAAFKNFNKWGDIEFPLPFGRVLSSTENFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYARVVIDCATTDPDGRKRALLIGGGIANFTDVAATFNGIIRALREKETRLKASRMHIYVRRGGPNYQTGLARMRALGEELGVPLEVYGPEATMTGICKRAIDCIMLPDA", "text": "FUNCTION: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. In contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family."}
+{"protein": "MNPMLNIAIRAARKAGNVIAKNYERRDAIESTQKGINDYVTNVDKASEAEIIEVIRKSYPDHTIITEETGAIEGKDSDVQWIIDPLDGTRNFMTGLPHFSVSIAVRVKNRTEVGVVYDPIRNELFTAVRGEGAKLNEVRLRVDSKREIQGSILATGFPFKQPKLMPAQFAMMNALIEDAADFRRTGSAALDLCYVASNRIDGYFEMGLKAWDCAAGDLIVREAGGLVCDFDAGNSYLRSGNIIAAPSRVIKEMLNKIRPCLGAEFNH", "text": "FUNCTION: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
+{"protein": "MVTNKDSRGKGKRKMEEGESSGRWKGAVYKRRKQAYKVVPVKPPALCVFRYNWLNSDRTNIVVGNTPRVDLITCFAQGKADNNRHTNQTVLYKFNIQGTCYMSDASAPFIGPVRLYHWLVYDAEPKQAMPDATDIFTMPWNLLPSTWTVQRAWSHRFVVKRKWTVNLVTDGRKVGSKTVDQRYNWVVGKNIVDANKFFKGLRVTTEWMNTGDGKIGDIKKGALYLISSTRGGVTGDSASTAFDVVCAYTHACYFKAIGIQ", "text": "FUNCTION: Encapsidates the viral genome into characteristic twinned ('geminate') particles. Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus. Plays a role in protection of the genome from degradation, virus acquisition and transmission by insect vectors, infectivity, and systemic movement. The CP of monopartite geminiviruses is absolutely essential for virus movement (By similarity). 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": "MLNADLKQQLKQLLELMEGNVEFVASLGSDEKSKELKELLTEISDMSPRLSLSEKSLKRTPSFSVNRPGEETGVTFAGIPLGHEFNSLVLAILQVSGRAPKEKQSIIDQIKNLEGSFHFETFISLTCQKCPDVVQALNLMSVINPNITHSMIDGAVFREESENIMAVPAVFLNGEEFGNGRMTIQDILSKLGSTADASEFENKEPYDVLIVGGGPASGSAAIYTARKGLRTGIVADRIGGQVNDTAGIENFITVKETTGSEFSSNLAAHIDQYDIDAMTGIRATDIEKTDEAIKVTLENGAVLESKTVIIATGAGWRKLNIPGEEQLINKGVAFCPHCDGPLFENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKADNVLQDRLRSLSNVDIKTNAKTTEVVGEDHVTGIRYEDMSTGEEHLLNLDGIFVQIGLLPNTSWLKDAVELNERGEIVIDCNNNTNVPGIFAAGDVTDQKNKQIIISMGAGANAALNAFDYIIRN", "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": "MLVLFGQPENWHEQDFRAVDDRVRGGSSISHLTEEKDSDGKSRAKFWGTLDTKTLGGAGFCSQATNIKDRTWNLKEFKGIELDIAKSDSYKYTFIIKDCHQDWETSDEKSSLSYEYDFTPIYSKEDQVVSIPFSEFKPTYRGRPVEGAPELDVSKITQFSIMIRSFFNSQSGDYELVLNSIRAIPKNVPFTTHKMSNEKQRLFDDYEKEIAGGSWCICQ", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CIA30 family."}
+{"protein": "MYLNQRIKFFLERVVRMMDENRSKGNRWGVWAFFGILLVPLLVPLLCCAGPILLVALGSTGIGALFAGATGNWWLTGIFAALAIVMIALILSKLLKNKYNSPEGNGKTKNKTDCCTPPESVDRKHETR", "text": "FUNCTION: Involved in mercuric transport. Passes a mercury ion from the MerP protein to the mercuric reductase MerA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MTNQDVVVSEMGIAAGAALPGGPAGPAGGLFACRSAAASMRQTYLDLAAAAVAARSASCTSWADAMRASSPTRSSRSASDVDEFTAWVRKHPSALSKFEEIAAKSRGKKIVMFMDYDGTLSPIVADPDTAYMSDAMRAAVREVAKTFPTAIVSGRCRDKVRNFVGLSDLYYAGSHGMDIKGPSSNPESALCQPASEFLPMIDEVYKTLVEKTKSTPGAKVENNKFCLSVHFRCVDEKRWNALGEQVKAVIKEYPKLKLTQGRKVLEIRPSIEWDKGKALEFLLESLGFANCGDVMPVYIGDDRTDEDAFKVLRKRGQGLGILVSKCPKDTNASYSLQDPTEVMEFLLRLVEWKRKSSSSSLMIRPRV", "text": "FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity). SIMILARITY: Belongs to the trehalose phosphatase family."}
+{"protein": "MLGGLGKLAAEGLAHRTEKATEGAVHAVEEVVSEVVGHAKEVGEKAINDALKKAQESGDRVVKEVTEKVTHTITDAVTHAAEGLGRLGQ", "text": "SIMILARITY: Belongs to the FAM25 family."}
+{"protein": "MKAVIPYKKSSAKSRLSPVLTREEREEFVDLMLNQVIDTLKEAGVGTIDILSPSMYGLENMTKANVLLDKNDLNEALNGYLEQAEEPVIIVMADLPLLSPDHVKGITSTKEDVCIVPGKGGGTNALFIKNPSCYRVRYYGSSFLTHCSIAEKTGQSVEVYDSFFAGTDIDEPEDLVELLIHGSGAAKEYISKKFRLEMSRGRVGLVHI", "text": "FUNCTION: Guanylyltransferase that catalyzes the activation of (2S)-2- phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor. SIMILARITY: Belongs to the CofC family."}
+{"protein": "MTEEGPGIVSLGKLRRPRMLRLWGICRVQIFSAIFMLMSPAGVGAGAKDDFSLVHPLVTMEQLLWVSGKQIGSVDTFRIPLITTTPRGTLLAFAEARKMSTSDKGAKFIALRRSMDQGSTWSPTAFIVDDGETPDGLNLGAVVSDTTTGVVFLFYSLCAHKAGCQVASTMLVWSKDDGVSWSSPRNLSLDIGTEMFAPGPGSGIQKQREPRKGRLIVCGHGTLERDGVFCLLSDDHGVSWRYGGGVSGIPYGQPKRENDFNPDECQPYELPDGSVVINARNQNNYHCHCRIILRSYDACDTLRPRDVTFDTELVDPVVAAGAVATSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWRKETVQLWPGPSGYSSLTTLEGNVDGKDEAPQLYVLYEKGRNQYMESISLVKVSVYGTL", "text": "FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Peripheral membrane protein; Lumenal side Lysosome lumen Cell membrane Cytoplasmic vesicle Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. SIMILARITY: Belongs to the glycosyl hydrolase 33 family."}
+{"protein": "MAAMPGGPDLAGAGGAVAVAVDAMQVDDPPRASAEEKHGPTIMGGNDPVTGHIISTTIGGKNDEPKRTISYMAERVVGTGSFGVVFQAKCLETGETVAIKKVLQDKRYKNRELQIMRSMDHCNVISLKHCFFSTTSRDELFLNLVMEFVPESLYRVLKHYKDMKQRMPLIYVKLYMYQIFRGLAYIHTVPGVCHRDIKPQNILVDPLTHQVKVCDFGSAKMLIKGEANISYICSRYYRAPELIFGATEYTTSIDIWSAGCVLAELLLGQPLFPGESAVDQLVEIIKVLGTPTREEIRCMNPNYTEFKFPQIKACPWHKIFHKRMPPEAIDLVSRLLQYSPNLRCTALEACAHSFFDELREPHAKLPNGRPFPPLFNFKQELANTHPELVSRLLPEHAQRHSGF", "text": "FUNCTION: Probable serine-threonine kinase that may regulate brassinosteroid signaling. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily."}
+{"protein": "KAEEEVEKNKEEAEEKAEKKIAE", "text": "FUNCTION: Internal peptide VII: Cleavage product of Gp22 that is incorporated into the mature phage head. FUNCTION: Gp22 functions in head assembly."}
+{"protein": "MAGRRLARASISAVGVWLLCALGLQATEAELPSAPAELPGGAACLSRFTSGVPSFVLDTEASVSNGATFLGSPTARRGWDCVRSCCTTQNCNLALVELQPDGGEDAISACFLMNCLYEQNFVCKFAPKEGFINYLTQELYRSYRELRTRGFGGSRIPRIWMGIDLKVQLQKPLVLNEADNTDWHLLQGDSDVRVERKRPEEVELWGLKEGTYLFQLTRTDSDQPEETANLTITVLTAKQTEDYCLASYKVGRCRGSFPRWYYDPKEQICKSFTFGGCLGNKNNYLREEECMLACKDVQGISPKRHHPVCSGSCHATQFRCSNGCCIDGFLECDDTPDCPDGSDEATCEKYTSGFDELQNIHFLSDKGYCAELPDTGFCKENIPRWYYNPFSERCARFTYGGCYGNKNNFEEEQQCLESCRGISKKDVFGLRREGSIPTVGSAEVAIAVFLVICIIVVLTILGYCFFKNQRKEFHSPLHHPPPTPASSTVSTTEDTEHLVYNHTTQPL", "text": "FUNCTION: Inhibitor of HGF activator. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MPVFLGLPVLARFIGWLAGALIAYVAKFFTLGIARIALAISLFLGLIIGLNGLLVSYLSDLTSVLPPEIASAVSYVVPANAAPCLYAIFSLKAAVFIFDVKDRIIGYLDWNKS", "text": "FUNCTION: Plays essential roles both in the entry of the viral genome into the bacterial host and in budding process. The formation of the G3P-G6P complex termed adsorption complex is essential for correct termination of filamentous phage assembly (By similarity). SUBCELLULAR LOCATION: Virion Host membrane; Multi-pass membrane protein Note=Prior to assembly, G6P is found associated with the bacterial host inner membrane. There are about five copies of G6P in the mature virion. They are located together with G3P at the head side of the filamentous virion (By similarity). SIMILARITY: Belongs to the inovirus G6P protein family."}
+{"protein": "MAALTASCIDLNIQGNGAYSVLKQLATIALQNGFITDSHQFLQTLLLREKMHSTGFGSGVAVPHGKSACVKQPFVLFARKAQAIDWKASDGEDVNCWICLGVPQSGEEDQVKIIGTLCRKIIHKEFIHQLQQGDTDQVLALLNQTLSS", "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 FrvAB PTS system is involved in fructose transport. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MISGILASPGIAFGKALLLKEDEIVIDRKKISADKVDQEVERFLSGRAKASAQLEAIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQATALEELDDEYLKERAADVRDIGKRLLRNILGLAIIDLSAIQEEVILVAADLTPSETAQLNLQKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTAQVKNGDYLILDAVNNQVYVNPTNDVIEQLRAVQEQVATEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAVRIAMDRKEILRDQVRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC", "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). 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": "MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFGQLKIEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPADVYSPEAAAKVIETDEKVFRHNVSLTYEQWLDYPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFLADLENLSALQAQQKGLRFNLEPTLPLPHQVITDGTRLRQILWNLISNAVKFTQQGQVTVRVRYDEGDMLHFEVEDSGIGIPQDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSRRLAKNMGGDITVTSEQGKGSTFTLTIHAPSVAEEVDDAFDEDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTKRYPREDLPPLVALTANVLKDKQEYLNAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVTTEENSKSEALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYVSVLESNLTAQDKKGIVEEGHKIKGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVGEWIEEMKEEWRHDVEVLKAWVAKATKK", "text": "FUNCTION: Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576. FUNCTION: Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576 (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MIPESHPRYKSLITREKLAQYTKTGIVSLEGLTAHGRGEAFDYLLGEETTESALRAEKIAAALLLSANHPVISVNGNTAALAAKEIAQLQLASKARVEVNLFHRTDERVQAISGLLKEHGITLVEGTVSRYIPLDHDRGLCHFDGMHSADVVLVPLEDGDRAQALIDLGKKVIAIDLNPLSRTSKVATVPVIDEVTRALANIARFCTELDQDEITGLTREIHGTGFIRDALEYIRERLLNVLD", "text": "FUNCTION: Catalyzes the condensation of (R)-4-phosphopantoate and beta- alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway. SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase family."}
+{"protein": "MSGRDNRGAGGGGGGHQPLSNAMGKLKEKLTRVGDELGYHRVESNLSTSNTATSLDTILPEDPFLFPQVSPQRHPQTVRTQRLLEDEPPLSFRPLLEDDDINEPPTQQPHRSPLRASGSLELTPLPPPPTSLEIREHRDRQQRGAQGDELQRSKQSLKGSRVSFERRDTGNSNTNNNKAAESSDEDSFEEKRTGFQQQKATSVDHKGILKDLKHILANDNRRQFQAKKHVSLDVKGTRFLQDLLKESSSEEEFHKTRREFQGRKHQSLDPRVTFKLDKVLQGSSTDSDEEGEDAEHKRLIHRPKDITKPVIIDLKDLESESDEDFLTSRQHFQQQRSISTDSRKSRRLYEMDEMGNKRGENIRHAVPFVRQITEDGKPKLEVYRPTTNPIFIWTQVLAALSVSLGSLVVGFVSAYTSPALVSMTDRNITSFEVTQDAGSWVGGIMPLAGLAGGIAGGPLIEYLGRRNTILATAVPFIVSSLLIACAVNVAMVLCGRFLAGFCVGIASLSLPVYLGETVQPEVRGTLGLLPTAFGNIGILLCFVAGSFMNWSMLAFLGAALPVPFLILMFLIPETPRWFVSRGREERARKALSWLRGKEADVEPELKGLMRSQADADRQATQNTMLELLKRNNLKPLSISLGLMFFQQLSGINAVIFYTVQIFKDAGSTIDGNICTIIVGVVNFLATFIGIVLIDRAGRKILLYVSNIAMILTLFVLGGFFYCKAHGPDVSNLGWLPLTCFVIYILGFSLGFGPIPWLMMGEILPAKIRGSAASVATAFNWSCTFVVTKTFQDLTVAMGAHGAFWLFGAICFVGLFFVIIYVPETQGKTLEDIERKMMGRVRRMSSVANIKPLSFNM", "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": "MALVSAVPLNSKLCLCRTLFGFSHELKAIHSTVPNLGMCRGGKSIAPSMSMSSTTSVSNEDGVPRRIAGHHSNLWDDDSIASLSTSYEAPSYRERADRVIGEVKNIFDLMSVEDGVFTSPLSDLHHRLWMVDSVERLGIDRHFKHEINSALDHVYSYWTEKGIGRGRESGVTDLNSTALGLRTLRLHGYTVSSHVLDHFKNEKGQFTWSAIQTEGEIRDVLNLFRASLIAFPGEKIMEAAEIFSTMYLKDALQKIPPSGLSQEIEYLLEFGWHTNLPRMETRMYIDVFGEDTTFETPYLIREKLLELAKLEFNIFHSLVKRELQSLTRWWKDYGFPEITFSRHRHVEYYTLAACIANDPKHSAFRLGFGKISHMITILDDIYDTFGTMEELELLTAAFKRWDPSSIECLPDYMKGVYMAVYDNINEMAREAQKIQGWDTVSYARKSWEAFIGAYIQEAKWISSGYLPTFDEYLENGKVSFGSRITTLEPMLTLGFPLPPRILQEIDFPSKFNDLTCAILRLKGDTQCYKADRARGEEASAVSCYMKDHPGITEEDAVNQVNAMVDNLTKELNWELLRPDSGVPISYKKVAFDICRVFHYGYKYRDGFSVASVEIKNLVTRTVVETVPL", "text": "FUNCTION: Monoterpene 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:23679205). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (+)-alpha-pinene (PubMed:23679205). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
+{"protein": "MCLGIPGQVVEVGKTITENALVDVCGVKREVNIALVCEGEPDTMIGKWVLVHVGFAMSIVNEQEAQETLNALMAMGEVEDDVSAFLYGEESTAKRA", "text": "SIMILARITY: Belongs to the HupF/HypC family."}
+{"protein": "MGVEVPPEESNRCVRGCCRSAAIPLHLPPSSFSLLSPIAKGSESTVYEARLGGERVAAKKPVLSTSDDLDKFHYQLQLLWWVLPIELDHPGLARLVAAHARPPNYLMFFDFFEPPNLADKIHVEEWNPSVQQVVTIATDLAKALQYLNILGIVHRDIKPANILIDKDFHPHLADFGLAMYQKDIKHVSVENWRSSGKPTGGFHKKNMVGTLIYMAPEILRKDIHTEKSDVYSFAISINELLTGVVPYTDLRAEAQAHTVLEMTYTEQQLTAAIVSQGLRPALALPESGAPPSLLSLIQRCWDSDPQQRPSFKDITEELKIIEKHIAVNSCSLASPANKSQNGNTEVHHYQEALSWLNQGELFAKGNKLDSTVDHWSDIFDQSSKYCPTLSWGSFATCGRRETMEDTHFMLPHMSEEKDLHAFGIFDGHRGSAAAEFSVRAVPGFLKQFNSNTSPTDALTEAFVRTDIAFREELILHQKSKRITQKNWHPGCTAVTALIVRNKLFVANAGDCRAILNRAGEPFPMTRDHVASCPKERERIVKEGTEVKWQIDTWRVGAAALQVTRSIGDDDLKPAVTAQPEVIETILSPDDEFLVMASDGLWDVMSNEDVLSIIKDTVKEPGMCSKRLATEAAARGSKDNITVIVVFLRPVSTAERIY", "text": "SIMILARITY: In the N-terminal section; belongs to the protein kinase superfamily. Ser/Thr protein kinase family. SIMILARITY: In the C-terminal section; belongs to the PP2C family."}
+{"protein": "MTYSVKEIFLTLQGEGGQAGKAAVFCRFSGCNLWSGREQDRAKAVCTFCDTDFVGTDGENGGKFATAEDLAAAVEAQWTGGPDDRLVVCTGGEPFLQLDDAAIAALHARGFQIAVETNGTITAPAGVDWICVSPKADAPVVQTSGQELKLVFPQEKAMPERFAALDFERFYLQPMDGPDRDANTQLAVAYCLSHPQWRLSVQTHKYLGLP", "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": "MSFRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEAIEAELAQLAEQPIEKDWRTAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLAKYLTMLHQELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDDAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINEMIDDLMEHISLENNVLFPRALAGE", "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": "MAEQLVEAPAYARTLDRAVEYLLSCQKDEGYWWGPLLSNVTMEAEYVLLCHILDRVDRDRMEKIRRYLLHEQREDGTWALYPGGPPDLDTTIEAYVALKYIGMSRDEEPMQKALRFIQSQGGIESSRVFTRMWLALVGEYPWEKVPMVPPEIMFLGKRMPLNIYEFGSWARATVVALSIVMSRQPVFPLPERARVPELYETDVPPRRRGAKGGGGWIFDALDRALHGYQKLSVHPFRRAAEIRALDWLLERQAGDGSWGGIQPPWFYALIALKILDMTQHPAFIKGWEGLELYGVELDYGGWMFQASISPVWDTGLAVLALRAAGLPADHDRLVKAGEWLLDRQITVPGDWAVKRPNLKPGGFAFQFDNVYYPDVDDTAVVVWALNTLRLPDERRRRDAMTKGFRWIVGMQSSNGGWGAYDVDNTSDLPNHIPFCDFGEVTDPPSEDVTAHVLECFGSFGYDDAWKVIRRAVEYLKREQKPDGSWFGRWGVNYLYGTGAVVSALKAVGIDTREPYIQKALDWVEQHQNPDGGWGEDCRSYEDPAYAGKGASTPSQTAWALMALIAGGRAESEAARRGVQYLVETQRPDGGWDEPYYTGTGFPGDFYLGYTMYRHVFPTLALGRYKQAIERR", "text": "FUNCTION: Catalyzes the cyclization of squalene into hopene. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the terpene cyclase/mutase family."}
+{"protein": "MWLPNLVRFVAVAYLICAGAILTYASGASASSSQSTPATPTHTTPNLTTAHGAGSDNTTNANGTESTHSHETTITCTKSLISVPYYKSVDMNCTTSVGVNYSEYRLEIYLNQRTPFSGTPPGDEENYINHNATKDQTLLLFSTAERKKSRRGGQLGVIPDRLPKRQLFNLPLHTEGGTKFPLTIKSVDWRTAGIYVWSLYAKNGTLVNSTSVTVSTYNAPLLDLSVHPSLKGENYRATCVVASYFPHSSVKLRWYKNAREVDFTKYVTNASSVWVDGLITRISTVSIPVDPEEEYTPSLRCSIDWYRDEVSFARIAKAGTPSVFVAPTVSVSVEDGDAVCTAKCVPSTGVFVSWSVNDHLPGVPSQDMTTGVCPSHSGLVNMQSRRPLSEENGEREYSCIIEGYPDGLPMFSDTVVYDASPIVEDRPVLTSIIAVTCGAAALALVVLITAVCFYCSKPSQAPYKKSDF", "text": "FUNCTION: Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Also plays a role in host immune evasion by inhibiting the host complement cascade activation (By similarity). FUNCTION: Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Also plays a role in host immune evasion by inhibiting the host complement cascade activation. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the herpesviridae glycoprotein C family."}
+{"protein": "MLSVVKPLQEFGKLDKCLSRYGTRFEFNNEKQVIFSSDVNNEDTFVILEGVISLRREENVLIGITQAPYIMGLADGLMKNDIPYKLISEGNCTGYHLPAKQTITLIEQNQLWRDAFYWLAWQNRILELRDVQLIGHNSYEQIRATLLSMIDWNEELRSRIGVMNYIHQRTRISRSVVAEVLAALRKGGYIEMNKGKLVAINRLPSEY", "text": "FUNCTION: Involved in oxidative stress resistance. SIMILARITY: Belongs to the IprA family."}
+{"protein": "MTNQNMPPETPIIWLNFSPALRRFDRPLLRQLGKSQAILQWDYHQTADEPNCLTVGLDLIGEYLENFHQPVHLIGHSTSGLLALLYARQCPEKVRSLSLLSVGVYPALDWQAHYYSQFDAMRYSRHLLLGQMAHHLFNCRSLRQTQTIVNILENDLLTSISPHSLYKQLIILPNHIAVPLLVAVGETDGIIDTSLFNGWQRWKKPGDRLWLCPEGKYFFQFEHPEITAFQLQQFWRSLQGQEASSSTSLLA", "text": "SIMILARITY: To Anabaena PCC 7120 alr2406."}
+{"protein": "XVPCNKEFVXNXF", "text": "FUNCTION: Functions in the pathway of anaerobic degradation of trihydroxybenzenes by catalyzing reduction of the aromatic nucleus prior to ring fission."}
+{"protein": "MAEWKEEVEVLVQRVVKDITGAFRRNPNIDEIGLIPCPEAKYNRSPIVLVENKLGVESWCIKFLLPYVHNKLLLYRQKKLWLNRDELIDVTCTLLLLNPDFTTAWNVRKELIQSGTLNPVKDLQLGKLALTKFPKSPETWIHRRWALQRLVQELVVAAVVDKDAICPETSERIQAIVEEEMHVCCEAAGRYPSNYNSWSHRIWVVQHLGNLKATLLIDELSSTKHWVSMHVSDHSGFHYRQFLLKSLLSKTLKDFDNVGAITDLIANEENLCLPRDGEANWNQICFDLPYLLEEEMDLNRELVDSFPGHETLWCHRRQIFNLIHQLLLEQSQSATPQSTSASIPDGSGNISQMSTTFQSYVTNPMDIDGMSDPNKQGYTQEIKRLKRAPVQDSLSFDSELRFINCVLTNCCSPEQSRFAASYRKWLLSLQGH", "text": "SIMILARITY: Belongs to the protein prenyltransferase subunit alpha family."}
+{"protein": "MVLSDILFSIYEHREKSPVFSWFAYLLRILDWIIQFLSFGLIPSIGGDLYDLVDNGLFKFVLDRNIQKKQNQLYDKFRLGTVKMCLVFDGELTKKLLLDNSIRRGGLYNLLTKFFGKGIFTSNIHSRWMKQRKAIFKLFSPQNLIQITPELTTSMFEELDRLITIKKDLDLVTVLSLIGLVGFCKVIFGVDVTDMSEELIEPLNDLLIYINGAVEPVLITADPSYRRFITNKKFVHNWMRKLIDKARKSENCFEIMRQQLDDIGSDDETELIEFILSVVLGGHETTARLMLGIIYSVCHNKEIIEKLNNETDEYPKGDYINLKKRPYLNNIIKEGTRLFPPVWLLSREAKNDTTIDNHFFKKGTQFLISPLIILRDYNVWGSNAEKFDPERFSNMDPKSKASKLYIPFIVGSEDCPGKKFAILESAIVVSKLFKEYEITVLKHKLNPMSAGTFRLSDKLPVSIKKLKN", "text": "SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein Virion. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MAFAEQSPLTLHRRDLCSRSIWLARKIRSDLTALMESYVKHQGLNKNISLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRVHFTPTEGDFHQAIHTLTLQVSAFAYQLEELMALLEQKVPEKEADGMPVTIGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHHMGISAHESHYGAKQM", "text": "FUNCTION: CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CNTF family."}
+{"protein": "MELRQLRYFMEVAEREHVSEAADHLHVAQSAISRQIANLEEELNVTLFEREGRNIKLTPIGKEFLIHVKTAMKAIDYAKEQIDEYLDPHRGTVKIGFPTSLASQLLPTVISAFKEEYPHVEFLLRQGSYKFLIEAVRNRDIDLALLGPVPTNFSDITGKILFTEKIYALVPLNHPLAKQKTVHLIDLRNDQFVLFPEGFVLREMAIDTCKQAGFAPLVSTEGEDLDAIKGLVSAGMGVTLLPESTFAETTPRFTVKIPIEFPQVKRTVGIIKPKNRELAPSANDFYEFVIQFFSKLEQYQ", "text": "FUNCTION: Positive regulator of glutamate biosynthesis (gltAB genes). Negatively regulates its own expression. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MNLATIKVTLPELIGRYQSQADFISIRLEQSEGTQISLRSDQVETLSEGIAMGGQVRVCHQGGWGFASFNRWEQLRQRLEEAIAAARLIGDDETLLAPIDPVQQTFINPLTGKDPRQISLADKKALCDHYNDLLRGTSDKITTTHVRYSDSQQTVLLATSEGTLLEQCWWDLEMRFAATAKDGNGVQVGRETTGSRRGYGDLENLDQVVQGAAQRAVKALTLPTVQGKTYPVVIDPILTGLFVHEAFGHLSEADMLYENPDFLEVMSLGRRFGPPELQIFDGAAPPGHRGSYGFDDEGVPASTTQLIKDGELVGRLHSRETAGKLGEKPTGNARCLNYHYPPIVRMTNTWIGRGETPVANLLDGIEEGIYAQNWLGGMTNGEMFTFSAGEAWMIRHGQLAEPVKDVTLSGNVFKTLANIEAIADDFYWDESGGCGKGGQNGLAVGCGGPSLRIRDVVVGGDAA", "text": "FUNCTION: Probable metalloprotease. SIMILARITY: Belongs to the peptidase U62 family."}
+{"protein": "MTVQSPDDSTRAPATSTAAPATADPKIKARGVKVFYGDKQALFDVDLDIPAKSVTAFIGPSGCGKSTFLRCINRMNDTIPSARVEGSILIDGADVNAKSVDPVVLRSRVGMVFQKPNPFPKTIFENVAYGPRIHGLATGKAELEAIVESSLKKAGLWNEVADRLHQPGTGLSGGQQQRLVIARAIAVSPEVILMDEPCSALDPIATAKIEELIDELRSQFCIVIVTHSMAQAARVSQRTAFFHLGKLVESGPTEEMFTNPRDSRTQDYITGRFG", "text": "FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. 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": "MTTASCIFPSQATQQDNIYGLSQITASLFISNSAVANDKLTLSNNHITTIINVSAEVVNTFFEDIQYVQVPVSDAPNSYLYDFFDPIADHIHGVEMRNGRTLLHCAAGVSRSATLCLAYLMKYHNMTLLDAHTWTKTCRPIIRPNNGFWEQLIHYEFKLFSRNTVRMIYSPIGLIPNIYEKEAYLMELM", "text": "FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
+{"protein": "MNRNPDQNTFPNITLKIIETYLGRVPSVNEYHMLKLQARNIQKITVFNKDIFVSLVKKNKKRFFSDVDTSASEIKDRILSYFSKQTQTYNIGKLFTIIELQSVLVTTYTDILGVLTIKAPNVISSKISYNVTSMEELARDMLNSMNVAIIDKAKVMGRHNVSSLVKNVNKLMEEYLRRHNKSCICYGSYSLYLINPNIRYGDIDILQTNSRTFLIDLAFLIKFITGNNIILSKIPYLRNYMVIKDENDNHIIDSFNIRQDTMNVVPKIFIDNIYIVDPTFQLLNMIKMFSQIDRLEDLSKDPEKFNARMATMLEYVRYTHGIVFDGKRNNMPMKCIIDENNRIVTVTTKDYFSFKKCLVYLDENVLSSDILDLNADTSCDFESVTNSVYLIHDNIMYTYFSNTILLSDKGKVHEISARGLCAHILLYQMLTSGEYKQCLSDLLNSMMNRDKIPIYSHTERDKKPGRHGFINIEKDIIVF", "text": "FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. SIMILARITY: Belongs to the poxviridae poly(A) polymerase catalytic subunit family."}
+{"protein": "MQFSRVLAALCGVLLCASGLFAASGDFCDSSLCLNGGTCLMGQDNDIYCLCPEGFTGLVCNETEKGPCSPNPCFHDAKCLVTEDTQRGDIFTEYICQCPVGYSGIHCELGCSTKLGLEGGAIADSQISASSVYMGFMGLQRWGPELARLYRTGIVNAWTASSYDSKPWIQVDFLRKMRVSGVMTQGASRAGRAEYLKTFKVAYSLDGRRFEFIQDESGTGDKEFMGNQDNNSLKINMFNPTLEAQYIRLYPVSCHRGCTLRFELLGCELHGCSEPLGLKNNTIPDSQITASSSYKTWNLRAFGWYPHLGRLDNQGKINAWTAQSNSAKEWLQVDLGTQKKVTGIITQGARDFGHIQYVASYKVAHSDDGVQWTVYEEQGTSKVFQGNLDNNSHKKNIFEKPFMARYVRVLPLSWHNRITLRLELLGC", "text": "FUNCTION: Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction. Appears to participate in the O-acetylation of GD3 ganglioside sialic acid. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Secreted Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Peripheral membrane protein Note=Located in the acrosomal region of zona-pellucida bound sperm."}
+{"protein": "MREILSIHIGQAGAQVGNACWELYCLEHGIKPDGQMPSDKSVGGGDDAFNTFFSETSSGKHVPRAIFLDLEPTVIDEIRTGTYRQLFHPEQLITGKEDAANNYARGHYTVGKELVDLCLDRVRKLADQCSGLQGFLVFHSVGGGTGSGFGSLLLERLSVDYGKKSKLDFCVYPSPQVSTAVVEPYNSVLSTHGLLEHTDVAFMLDNEAIYDLCKRSLDIERPSYANLNRLVAQVISSLTTSLRFDGALNVDITEFQTNLVPYPRIHFMLASYAPVISAEKAFHEQLSVAELTNTVFDPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVAVIKTKRTIQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRALCMISNTTAIAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEVEFSEAREDLAALEKDYEEVGAETAEDDGADEEM", "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, spindle. Nucleus. Note=Mitosis in the slime mold Plasmodium differs from the process in many eukaryotes. The tubulin chains must be transported to the nuclei for intranuclear assembly of the spindle. SIMILARITY: Belongs to the tubulin family."}
+{"protein": "MSVDFNAVATEFCNFYYNQFDSDRSQLGNLYRNESMLTFETSQLQGARDIVEKLASLPFQKVAHRISTLDAQPASANGDILVMVTGELLIDEEQNAQRYSQVFHLIPDNGSYYVFNDIFRLNYS", "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": "MEGADLLTAGVLFLFAAVAAVPLAARLGIGAVLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFIIGLELNPSRLWQLRRSIFGVGAAQVLLSAAVLAGLLMLADFLWQAAVVGGIGLAMSSTAMALQLMREKGMNRSESGQLGFSVLLFQDLAVIPALALVPLLAGSADEHFDWFKVAMKVLAFAVMLIGGRYLLRPVFRFIAASGVREVFTAATLLLVLSAALFMDALGLSMALGTFIAGVLLAESEYRHELENAIDPFKGLLLGLFFISVGMSLNLGVLYTHLLWVAASVVILVVIKMLTLYLLARLYGIRSSERMQFASVLSQGGEFAFVLFSTASSQRLFQGDQMALLLVTVTLSMMTTPLLMKGIDKWLSRRLNGPEENDEKPWVEDDKPQVIVVGFGRFGQVIARLLMANKMRITVLERDIGAVNLMRKYGYKVYYGDATQVELLRSAGAEAAESIVITCNEPEDTMKLVALCQQHFPHLHILARARGRVEAHELLQAGVTQFSRETFSSALELGRKTLVSLGMHPHQAQRAQLHFRRLDMRMLRELIPEHSDMVQISRAREARRELEEIFQREMQQERRQLDGWDEFE", "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": "AQLQNLVLKDREATPNDHTFVPRDIRDNVGEVVESTGVPIGESRFTISLRKTSNGRYKSTLKLVVPVVQSQTVNGIVTPVVVRTSYVTVDFDYDARSTTKERNNFVGMIADALKADLMLVHDTIVNLQGVY", "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": "MQKSCNEKEGKPKGSEAKREDEQPCGALEGQRLEGNFRQRLLQSLEEFKEDIDYRHFKGEEMTGEEEEMERCLEEIRSLRKKFRALHSNRTHSRDHPF", "text": "FUNCTION: Plays a role in the negative regulation of NF-kappa-B signaling at the basal level by modulating transcriptional activity of NF-kappa-B on its target gene promoters. Associates with cyclin D1 promoter containing Myc E-box sequence and transcriptionally represses cyclin D1 expression. Regulates telomerase reverse transcriptase expression and telomerase activity in both ALT (alternative lengthening of telomeres)and telomerase-positive cell lines (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFS-II family. TFA subfamily."}
+{"protein": "MQQVLENLTELPSSTGAEEIDLIFLKGIMENPIVKSLAKAHERLEDSKLEAVSDNNLELVNEILEDITPLINVDENVAELVGILKEPHFQSLLEAHDIVASKCYDSPPSSPEMNNSSINNQLLPVDAIRILGIHKRAGEPLGVTFRVENNDLVIARILHGGMIDRQGLLHVGDIIKEVNGHEVGNNPKELQELLKNISGSVTLKILPSYRDTITPQQVFVKCHFDYNPYNDNLIPCKEAGLKFSKGEILQIVNREDPNWWQASHVKEGGSAGLIPSQFLEEKRKAFVRRDWDNSGPFCGTISSKKKKKMMYLTTRNAEFDRHEIQIYEEVAKMPPFQRKTLVLIGAQGVGRRSLKNRFIVLNPTRFGTTVPFTSRKPREDEKDGQAYKFVSRSEMEADIKAGKYLEHGEYEGNLYGTKIDSILEVVQTGRTCILDVNPQALKVLRTSEFMPYVVFIAAPELETLRAMHKAVVDAGITTKLLTDSDLKKTVDESARIQRAYNHYFDLIIINDNLDKAFEKLQTAIEKLRMEPQWVPISWVY", "text": "SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the MAGUK family."}
+{"protein": "MKFIIVLLLLTALTLTSIPVIEGILKRCKTYDDCKDVCKARKGKCEFGICKCMIKSGK", "text": "FUNCTION: First cyclic scorpion trypsin inhibitor (Kd~0.5 nM). Does not inhibit chymotrypsin. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MALDKDIVGSIEFLEVVGLQGSTYLLKGPNGENVKLNQSEMNDDDELEVGEEYSFFIYPNRSGELFATQNMPDITKDKYDFAKVLKTDRDGARIDVGLPREVLVPWEDLPKVKSLWPQPGDYLLVTLRIDRENHMYGRLASESVVENMFTPVHDDNLKNEVIEAKPYRVLRIGSFLLSESGYKIFVHESERKAEPRLGESVQVRIIGHNDKGELNGSFLPLAHERLDDDGQVIFDLLVEYDGELPFWDKSSPEAIKEVFNMSKGSFKRAIGHLYKQKIINIETGKIALTKKGWSRMDSKE", "text": "FUNCTION: Contributes to the expression of virulence factors and to pathogenicity via both agr-dependent and agr-independent pathways. Involved in the production of hemolysin, DNase, protease and protein A. Contributes to virulence in silkworm-infection model and murine model of systemic infection. FUNCTION: Contributes to the expression of virulence factors and to pathogenicity. Involved in the production of hemolysin, DNase, protease and protein A (By similarity). SIMILARITY: Belongs to the CvfB family."}
+{"protein": "MAKISRLFGSTVKAAITAQAGFHGKRIPAVSSLQEHIVKSTPARYNSTQACLENDISGTDNKGFKGHDMLAPFTAGWQSTDVDPLIIEKSEGSHVYDMQGRKYIDTLAGLWCTALGGNEPRLVDAATKQLNTLPFYHSFWNRTTKPSLDLAKELLDMFTAKKMAKAFFTNSGSEANDTQVKLVWYYNNALGRPNKKKFIARAKAYHGSTLISASLTGLPALHQNFDLPAPFVLHTDCPHYWRYHLPGETEEEFSTRLAKNLEDLILKEGPETIAAFIAEPVMGAGGVIPPPATYFDKIQAVVKKYDILFIADEVICAFGRLGTMFGSDMYNIKPDLVTLAKALSSAYMPIGAVLVSPEVSDVIHSQSNKLGSFSHGFTYSGHPVACAVALEAIKIYKERNMVERVNRISPKFQEGLKAFSDSPIIGEIRGLGLILATEFANNKSPNDHFPPEWGVGAYFGAQCQKNGMLVRVAGDTIMMSPPFVVTPEELDELIRIYGKALRETEKRVEELKSQK", "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. Acts predominantly in vegetative tissues. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MRQDKLTGSLRRGGRCLKRQGGGGVGTILSNVLKKRSCISRTAPRLLCTLEPGVDTKLKFTLEPSLGQNGFQQWYDALKAVARLSTGIPKEWRRKVWLTLADHYLHSIAIDWDKTMRFTFNERSNPDDDSMGIQIVKDLHRTGCSSYCGQEAEQDRVVLKRVLLAYARWNKNVGYCQGFNILAALILEVMEGNEGDALKIMIYLIDKVLPESYFVNNLRALSVDMAVFRDLLRLKLPELSQHLDTLQRTANKESGGGYEPPLTNVFTMQWFLTLFATCLPNHTVLKIWDSVFFEGSEIILRVSLAIWAKLGEQIECCETADEFYGTMGRLTQEMLEQDLLQSHELMQTVYSMAPFPFPQLAELREKYTYNITPFPATIKPTSVSGRHSKARDSDDENGPDDEDAVASAVGCLGPLSGLLAPELQKYQKQIKEATEEQTLRSNNIAELSPGAINSCRSEYHAAFNSMMMERMTTDINALKRQYSRIKKKQQQQLHQVYIRADKGPVTSILPSQANSSPVINHLLLGKKMKITNRAAKNAVIHVPGHPGGKISPVPYEDIKTKLNSPWRTHIRVHKKNMPRTKSHLGCGDTVGLIEEQSEGCKASSLGAAEEFPSGRTVTAHSEGSSGDGDGGGSTPRTIEGQSPEPVFGDADVDVAAVQVKLEALELNQRDAAAETEPKVHFPCQRHASELADAPGENQTAIKLLPGSTSKTPIFSPFPSVKPLRKSATARNLGLYGPTERTPNVHFPQMSRGFNKSGIGNSSTKKR", "text": "FUNCTION: GTPase-activating protein (GAP) with broad specificity. Acts as a GAP for RAB3A. Also exhibits significant GAP activity toward RAB22A, RAB27A, and RAB35 in vitro (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein."}
+{"protein": "MDFIAILIGLGPLLGWGLFPTIASKFGGRPVNQIFGATVGTLIFAIVLALFKGIGLPGGMALVFSLISGAGWAFGQIITFKAFELVGSSRAMPITTAFQLLGASLWGVFALGNWPGITNKIIGFLALLVILIGARMTVWTETKQQEYSKNLRSAVILLLVGEIGYWIYSAAPQATDIGGFKAFLPQAIGMVIVAVIYALMNMSKGNAFKEKVSWQQTISGFFFAFAALTYLISAQPNMNGLATGFVLSQTSVVLATLTGIFFLNQKKTSKELMITIVGLVLILVAASITVFIK", "text": "FUNCTION: Could be involved in the uptake of ribose. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GRP transporter (TC 2.A.7.5) family."}
+{"protein": "MLLEKAYRIKKNADFQRIYKKGHSVANRQFVVYTCNNKEIDHFRLGISVSKKLGNAVLRNKIKRAIRENFKVHKSHILAKDIIVIARQPAKDMTTLQIQNSLEHVLKIAKVFNKKIK", "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": "MGRSPCCDKLGLKKGPWTPEEDQKLLAYIEEHGHGSWRSLPEKAGLHRCGKSCRLRWTNYLRPDIKRGKFNLQEEQTIIQLHALLGNRWSAIATHLPKRTDNEIKNYWNTHLKKRLVKMGIDPVTHKPKNETPLSSLGLSKNAAILSHTAQWESARLEAEARLARESKLLHLQHYQTKTSSQPHHHHGFTHKSLLPNWTTKPHEDQQQLESPTSTVSFSEMKESIPAKIEFVGSSTGVTLMKEPEHDWINSTMHEFETTQMGEGIEEGFTGLLLGGDSIDRSFSGDKNETAGESSGGDCNYYEDNKNYLDSIFNFVDPSPSDSPMF", "text": "FUNCTION: Involved in the control of epidermal cell morphogenesis in petals. Promotes unidirectional cell expansion once outgrowth has been initiated (PubMed:17376813). Coordinately with WIN1/SHN1, participates in the regulation of cuticle biosynthesis and wax accumulation in reproductive organs and trichomes. Functions in cuticle nanoridge formation in petals and stamens, and in morphogenesis of petal conical cells and trichomes (PubMed:23709630). Functions as a major regulator of cuticle formation in vegetative organs by regulating the cuticle biosynthesis genes CYP86A8/LCR and CER1 (PubMed:24169067). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MDLVLSAADYYFFTPYVYPATWPEDNIIRQTVSLLVVTNLGAYILYFFCATLSYYFVYDHSLMKHPQFLKNQVSREIMFTVKSLPWISIPTVSLFLLELRGYSKLYDDIGDFPNGWIHLIMSVISFLFFTDMLIYWIHRGLHHRLLYKHIHKPHHIWKIPTPFASHAFHPVDGFLQSLPYHIYPFVFPLHKVVYLGLYVLVNVWTISIHDGDFRVPQIFRPFINGSAHHTDHHMLFDYNYGQYFTLWDRIGGSFKHPSSFEGKGPHSYVKNMTEKESNSLAENGCKSKKLCNGEFTKNE", "text": "FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol in cholesterol biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
+{"protein": "MKDQYDLVVVGAGPAGSIAATTAAKKGLSVLMLEKRQEIGEPVRCAEGVGKKRLRQHIELDEKWLCGEVSSAKIISPNGTTLTMAEEDAGSEVGYVLDRKIFDRTLVELSGEAGVDIMVKARVTGLIIEENTVCGVEMMHLGKTYSIRSKLVIGADGVESKVGRWAGIDTSLKPSHIETCAQFLVSGVDIDQSSCYFYMGNKVAPGGYVWVFPKGNNMANVGIGILGSRAGEKKPIEYLTDFVEANYPNGSIIEQVAGAVPASGPIEKTIANGLMLVGDAARQSDPFTGGGISNAMDAGLYAGEVAAEAIAQDDVSEKILQKYEKRWRGSFGNEIANNLIVKETFFSLSDEDLDSLALSIKDVDFKKMDLIDFIAALFKANKKLLWNLRPLFTQKLKQKFSGLTKFKR", "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": "AVVNGVNYVGETTAA", "text": "FUNCTION: Diaminopimelinoyl-alanine endopeptidase. Has antibacterial activity. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MVKGEKRSEMMLNLFGDNSEEEEIESEHECNRRQPNYASDEAEGGVEPEGEGEAEVEVHGEAEAESDGEQGDVELDPGESEGEREQSSQEADPQEESEARDSDSDNKEEEHGGRVAKKRRQEVVESGSERSGEKHYESEDEEVDQTRSPRSPSEEKEEVQVAQSDVNIRNVFGSSDDEDAEEYVRNDVEQDEHRSPIEDEEGSEKDLRPDDMVLDDIIPEEDPQYESEAEHVEARYRERPVGPPLEVEVPFRPPPGDPVKMNMIKVSNIMGIDPKPFDAKTFVEEDTFMTDEPGAKNRIRLDNNIVRHRFVKSRDGKTYSESNARFVRWSDGSLQLLIGNEVLNITEQDAKEDQNHLFIKHEKGILQSQGRILKKMRFTPSSLTSNSHRLLTAIVESRQKKAFKVKNCVTDIDPEREKEKREKAESQNLKASTKLSQAREKIKRKYPLPVERRQLSTGYLEDALDEDDEDYRSNRGYEEDLEAEAQRERRILNAKKSHKGIPGRSSMTSARPSRRQMEYSESEREESEYETEEEEEEKSPARGRGKDSEDEYEEDAEEDEEERGKSNRYSDEDEEEEEVAGGRAEKDHRGSGRKRKGIESDEEESPPRKAPTHRRKAVIDDSDED", "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 repressor and MADS box gene FLC (PubMed:12207655). Involved in the control of seed dormancy and germination (PubMed:21799800). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the LEO1 family."}
+{"protein": "MDRDPSEEDSMADLSFEAESPVLPPDELLEGLPSYDWLLQGRERQVFFPPLEALGRSQEPACWSSVLEHSRVPVVTEEVAREALLSFVNSHCCYSSAAAGNLIIQELRQQTLCRYRLETFSESRVSEWTFQPVTNHSVDGPQRGTSPRLWDMKVQVPPMFQEDTRKLQVPHSSLVKECHKCHGRGRYKCSGCHGAGMVRCSSCSGTKRKAKQPRRCHLCSGSGRRRCSTCSGRGNKTCATCKGERKLEHFVQLVIMWKNSLFEFMSPHHLHCPKELLAKARGENLFRDENATVYPIVDFPLQDISLASQRGIEEHSTMLASRARILQQMFFYSGGPFHHS", "text": "FUNCTION: Plays a role in odontogenesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MPVNFVAARKKRDGVNTHIELQKAIYKSRSFTEINNILDGILPDAHRETPFATYFEANLGCRRPDCMIVFDDLPKQIITCVLVEFKTTSRTAFDKRKKDAVQQYQLHQGEEQVRDAVKILSSITGRGCNLRVWGFLLFYQQSTLRVLHKTIPECAVTLTDRWAFSALLKKSKNESFHAFLQKSCTASTTGPQKELFGIHKPENSEVETVGATKSTRKGAEKSRLSRRSRKSN", "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": "MGRRRSHERRDLPPNLYIRNNGYYCYRDPRTGKEFGLGRDRRIAITEAIQANIELLSGNRRESLIDRIKGADAITLHAWLDRYETILSERGIRPKTLLDYASKIRAIRRKLPDKPLADISTKEVAAMLNTYVAEGKSASAKLIRSTLVDVFREAIAEGHVATNPVTATRTAKSEVRRSRLTANEYVAIYHAAEPLPIWLRLAMDLAVVTGQRVGDLCRMKWSDINDNHLHIEQSKTGAKLAIPLTLTIDALNISLADTLQQCREASSSETIIASKHHDPLSPKTVSKYFTKARNASGLSFDGNPPTFHELRSLSARLYRNQIGDKFAQRLLGHKSDSMAARYRDSRGREWDKIEIDK", "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": "MRAIAIVLARSSSKRIKNKNIIDFFNKPMLAYPIEVALNSKLFEKVFISSDSMEYVNLAKNYGASFLNLRPKILADDRATTLEVMAYHMEELELKDEDIACCLYGASALLQEKHLKNAFETLNKNQNTDYVFTCSPFSASPYRSFSLENGVQMAFKEHSNTRTQDLKTLYHDAGLLYMGKAQAFKEMRPIFSQNSIALELSPLEVQDIAHFRRFRISQAQIQPFEKRMPVKILCDCFLTSGLGHVRRCEKILSFIEKLGVEASLYLHKQNNISAFLEGVGGNDFLITDSYCLNSKDFYLLKEKAKSLMVIEDTEHAKGFYPKNTKILNFTLNALKHYHHLSKDYQYYLGVGFYPVDARFIYDRPINTENKEVLITLGGSEQKTLKEIVKILENKNVNLHIISPYTPKNPPKNTHYYSPLNPLEFSSLMKSCACAISAAGQTLYELALSQTPSLILPIASNQIIQSKEFESLGIFKQTSLKTLAKDFENLQIQKNQAWAKNLVFGDKLEGALREFLEI", "text": "FUNCTION: Catalyzes the fourth and sixth steps in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. The C-terminus mediates the fourth step of the pathway and catalyzes the removal of UDP from C-1 of UDP-2,4-diacetamido-2,4,6- trideoxy-beta-L-altropyranose forming 2,4-diacetamido-2,4,6-trideoxy- beta-L-altropyranose. The N-terminal part mediates the last step of the pathway by mediating activation of pseudaminic acid with CMP by forming CMP-pseudaminic acid. SIMILARITY: In the N-terminal section; belongs to the CMP-NeuNAc synthase family. SIMILARITY: In the C-terminal section; belongs to the PseG family."}
+{"protein": "MCPSFLVTLLLLQLSSLVVVLVVWAEQLPEFNVRRDDFPSNFVFGAGTSALQVEGAIAEDGKTPNIWDVDSHMGHMPDKSTTDIACDSYHRYKEDVKIMSDIGLEAYRFSIAWTRILPYGRGFINPKGVEYYNNLIDTLLEHGIQPHATIYHIDHPQILEDEYGGWLSPRMIEDFTTYADVCFREFGDRVSHWTTINEPNIISLGAYDSGQIPPHRCTPPGAYNCTAGNSSVEPYKAMHHFLLAHASAVQIYRTKYQAKQKGLIGLNVYGFWCAPQTNSRADIEATKRATAFYTGWAADPLVFGDYPIIMKENVGSRLPSFTKNESELVKGSFDFIGLNHYFVFYIQDDPEEITTPISLRNFDSDMRVKASVKPGDSGDPSGLKNLLRYFKDNYGNPPVYVHENGFGSPQNETLDDDMGRIRYISGYIGSMLEAIKNGSDTRGYFVWSFMDAFEILSGYQTRYGIVHVDFDDKSLKRQLKPSAQWYSNFIKKKNTTEDEISYSSQ", "text": "FUNCTION: Beta-glycosidase that catalyzes the transfer of glucose moiety to anthocyanidin 3-glucoside at the 7 position. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
+{"protein": "MKTIKKTLLAAAIASFFSSGLYAQTPIDLGVVNEDKLIEMLVRTGQIPADASDVDKRIALERYLEEKIRSGFKGDAQFGKKALEQRAKILKVIDKQKGPHKARVFALDVGQKRTDKVLALLIDFPDLPWDDNRLTKEHTEMLYDRYEPSHYQDLLFSDKGYTGPNGENFISMRQYYESESGNSYSVSGQAAGWYRASKNAAYYGGNSPGTNNDMNARELVREALDQLARDPNINLADYDIEDRYDYNGNGNFREPDGVIDHLMIFHASVGEEAGGGVLGADAIWSHRFNLGRYHVLEGTKSNVPGRFNGQFAAFDYTIQPIDAAAGVCAHEYGHDLGLPDEYDTQYTGTGEPVSYWSIMSSGSWAGKIGGTQPTAFSSWAKQFLQNSIGGRWINHEQLSINELEAKPRVVTLFQTTDNSRPNMVKVTLPMKRVEGIKPAEGEFSFYSNRGDDLKNRMSRPLTIPAGSQATLRFKAWFQIEKDYDYARVLINGKPIAGNITTMDDPFKSGLVPAISGQSDGWVDAQFDLSAWAGQTVELAFDYLTDGGLAMEGLYVDDLRLEVDGNQTLIDNAEGTSSFAFQGFTKNGGFHEANHYYLLQWRSHNDVDQGLANLKRFGQLMSFEPGLLVWYVDESYADNWVGKHPGEGWLGVVDADQNALVWSKTGEVAQTRFQVRDATFSLFDQAPLKLVTADGNTLEDMNLTANASFSDDQDYSSPQAPDSGRKVMPFGLKIDLLSQSKENEYGVVRLSKVTTENIAPVARFELKVEGLSVMSQNTSSDSDGNIVSYLWDFGNGQTSTEAAPTWSYTKAGSYSVTLTVTDDKGDSDTHQQTIKVDTPNALPQASANYIHLGRWVTMWSTSTDSDGRIVDTEWTLPNGKIKRGRMFTAIFPSYGHHDVQLKVMDDRGAVTTITIKVKL", "text": "FUNCTION: Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen. FUNCTION: Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M6 family."}
+{"protein": "MAASLQASTTFLQPTKVASRNTLQLRSTQNVCKAFGVESASSGGRLSLSLQSDLKELANKCVDATKLAGLALATSALIASGANAEGGKRLTYDEIQSKTYLEVKGTGTANQCPTVEGGVDSFAFKPGKYTAKKFCLEPTKFAVKAEGISKNSGPDFQNTKLMTRLTYTLDEIEGPFEVSSDGTVKFEEKDGIDYAAVTVQLPGGERVPFLFTIKQLVASGKPESFSGDFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELQKENNKNVASSKGTITLSVTSSKPETGEVIGVFQSLQPSDTDLGAKVPKDVKIEGVWYAQLEQQ", "text": "FUNCTION: Stabilizes the manganese cluster which is the primary site of water splitting (By similarity). Binds GTP after preillumination of photosystem II core complex. This binding is inhibited by DCMU. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the PsbO family."}
+{"protein": "MTVHIHPYVDNGVKQGSGHFAGGTLVCKCHDRPVKVAVKGDVAHNHACGCTKCWKPSGATFSVIAVVPRQNVTVLENGDKLKIVDPSAVIQRYACTGCGTHMYGRIENTGHPFYGLDFIHPELFQEQGSAAPAFAAFVSSVIESGVKPEQMGEIRARLKELGLEPYDCLSPALMDAIATHVAKAKAA", "text": "FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione. SIMILARITY: Belongs to the Gfa family."}
+{"protein": "MENILCFLNSYTETGLSPDSHCLDIDLNFICLSGLGLFILYLFYMVLTLYSSPTEKNNDTQKHQGRARRKRKSVTFKDRKSLQKEAEEERKLHSFLKSFGPPVSCSPLGQHHDTTLFRRLLCPDPVCRVCNRATADIQRLLSWESLKDAAPSVSPLASSASGAESSFTLASTPSATTPEDLILSSRPKPSPPPPLILSPDLITTLADLFSPSPLRDPLPPQPVSPLDSKFPIDHSPPQQLPFPLLPPHHIERVEPSLQPEASLSLNTIFSFGSTLCQDISQAVNRTDSCARHHGPPTPSALPPEDCTVTQSKSNLTVLKTFPEMLSLGGSGGSSTSAPTTKGIDHSCPASSEFSWWQPHAKDSFSSNFVPSDFMEELLTLHSSEASLGGHSVANIIQPVNISFLSHDIPALLERQVKRRGDFLMWKENGKKPGSFPTQLRPNYQLNSSRNMLTSTAVKHDLAESFPFWASKGKLEWQHIHQQPPYSKCFEDHLEQKYVQLFWGLPSLHSESLHPTVFVQHGRSSMFVFFNGITNTSMSHESPVLPPPQPLFLPSTQPLPLPQTLPRGQSLHLTQVKSLAQPQSPFPALPPSPLFLIRVCGVCFHRPQNEARSLMPSEINHLEWNVLQKVQESVWGLPSVVQKSQEDFCPPAPNPVLVRKSFKVHVPISIIPGDFPLSSEVRKKLEQHIRKRLIQRRWGLPRRIHESLSLLRPQNKISELSVSESIHGPLNISLVEGQRCNVLKKSASSFPRSFHERSSNMLSMENVGNYQGCSQETAPKNHLLHDPETSSEEDLRSNSERDLGTHMMHLSGNDSGVRLGQKQLENALTVHLSKKFEEINEGRMPGTVHSSWHSVKQTICLPEKSHSQIKHRNLAALVSEDHRVDTSQEMSFLSSNKQKMLEAHIKSFHMKPILNLSI", "text": "FUNCTION: May play a role in spermatogenesis. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SPATA31 family."}
+{"protein": "MATGGKVSFKVTLTSDPKLPFKVFSVPEGAPFTAVLKFAAEEFKVPPQTSAIITNDGIGINPQQSAGNVFLKHGSELRLIPRDRVGAVFVMDP", "text": "FUNCTION: Ubiquitin-like modifier protein which binds to a number of as yet unidentified target proteins. SIMILARITY: Belongs to the UFM1 family."}
+{"protein": "MAKFKIRPATASDCSDILRLIKELAKYEYMEDQVILTEKDLLEDGFGEHPFYHCLVAEVPKEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMAAEE", "text": "FUNCTION: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)- acetylspermine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Also acts on 1,3- diaminopropane and 1,5-diaminopentane. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the acetyltransferase family."}
+{"protein": "MPEVKSMFREVLPKQGQLSMEDVPTMVLCKPKLLPLKSVTLEKLEKMQKDAQEIIRQQELALKEQPPSEKAE", "text": "FUNCTION: Required for primary cilia assembly. SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm. SIMILARITY: Belongs to the BBIP10 family."}
+{"protein": "MTEQIESMELAAVAHIKATKNDTFVHITDMTGSETIAKITGGMRVKAQRDEGSPYAAMLAAQDVATKILGRGVKVLHFKLRGAGGVKPMALGPGAQTAIRTLIRAGLRVGRIEDVTPVARDRVRKRGGHRGRRV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
+{"protein": "MAEASSANLGSGCEEKRHEGSSSESVPPGTTISRVKLLDTMVDTFLQKLVAAGSYQRFTDCYKCFYQLQPAMTQQIYDKFIAQLQTSIREEISDIKEEGNLEAVLNALDKIVEEGKVRKEPAWRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLADAVLAGRRQVEELQLQVQAQQQAWQALHREQRELVAVLREPE", "text": "FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Note=Associated with the kinetochore."}
+{"protein": "MWIPSKLTRPGRLHNAIVRPRVLDLLQQAPYYKLVLFRSPAGYGKTTMAAQWLSDKPNVGWYSIDDSDNDGFRFVNYLLQALNKATNFSCSNAQKLAEKRQISSLRSLFSEVFAEMADFHQECYVVLDDYHLITNDEIHESMRFFLKHMPDNLTVVVTSRAAPPLGTANLRVRDLMIEIGNEMLAFDTEETTRFFNQRIADGIDEDMANSLRTYVEGWPSAMQLIALQAQHQNRTLAQTVESVSQFNHAHLWDYLVEEVFDLLDHETRHFLMQVSVLDHFNDELVFALTQREDALGLIESLNRYGLFIYPLEGEHNWFRFHNLFGEFLSHERQARIPQQEKDLHRNAAVAWLQQKSPHQAIHHAQKSNDKDLVVEILNEFGWKMFNQGELSTLEHAINKLDAELLFSHPKLTMLRAWLAQSQHRYNQVGQLLEEAEEEHKKRNIELDIHYQGQANALLAQVAINSNQPEKALELAELALSQLDNTIYRSRIVATSVVGEVNHVLGKLDRALPMMQQTEKLARQYQVYHQALWAILQQSEILIAQGYVQAAFELQDSGFRLIEDQQLQHVPLHEFLLRIRAQVLWCWNRLDEAEECAYRGLQILENHSPSKHLHSYSMLARIAIGRGELDKAGKFIEHIQHLMKQSTYHVDWTANASLSLILFWQARGNTEAMQEWLNTAVRPESACNHFLQLQWRNIVRAHINLGQYEEARQALNFLQSEARRTNLITDTNRNLVVEAVLAARQKDEEQAKALLKEALVMTNQTGMVGNFLIDGATIGGLLEKLSLRHELGDLERHRAQQLMKDISSNQRSRSIHFDEDFIEKLVNHPNVPELVRTSPLTQREWQVLGLIYSGFSNEQIAQELDVAGTTIKTHIRNLYQKLNIANRKEAIVTAENLLQLMGY", "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": "MHPPTDLPRWVYLPAIAGIVFVAMPLVAIAIRVDWPRFWALITTPSSQTALLLSVKTAAASTVLCVLLGVPMALVLARSRGRLVRSLRPLILLPLVLPPVVGGIALLYAFGRLGLIGRYLEAAGISIAFSTAAVVLAQTFVSLPYLVISLEGAARTAGADYEVVAATLGARPGTVWWRVTLPLLLPGVVSGSVLAFARSLGEFGATLTFAGSRQGVTRTLPLEIYLQRVTDPDAAVALSLLLVVVAALVVLGVGARTPIGTDTR", "text": "FUNCTION: Part of the binding-protein-dependent transport system ModABCD for molybdenum; probably responsible for the translocation of the substrate across the membrane. FUNCTION: Part of the binding-protein-dependent transport system ModABCD for molybdenum; 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. CysTW subfamily."}
+{"protein": "MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVQNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRKGRKTNKPNRRFKCKML", "text": "FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MMLFGKVSQQLCGIKKLPWSCDSRYFWGWLNAVFNKVDYDRIRDVGPDRAASEWLLRCGAMVRYHGQERWQTDYNHLPTGPLDKYKIQAIDATNSCIMSIGFDHMVGLQHVEKIRLCKCHFIEDDCLLRLGQLENLQKSILEMEIISCGNITDKGIIASRHLRNLKYLLLSDLPGVREKENLIQVFETALPSLELKLQLK", "text": "FUNCTION: Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane. SIMILARITY: Belongs to the ATP synthase subunit s family."}
+{"protein": "MKNLVVFGTESHPKLTESICEHLCLDIGRVELSKFSNGETSVRIKQSVRGCDVYIVSPASGQVNDHLMELLIMISACKTASAKKVTAVLPVFPYSRQPDQKFSFSGAPLSDLQDAVVPCKKQTGYHPWIAQSGTLVADLLMCSGADHIITMDLHDPQFQGFFDIPVDNLFGRPLLKHYISLNIPNYHNAVIVSPDAGGAKRATAIADALGLDFALIHKNRRHEYGTSLMLVGDVQNKVAILIDDLIDTAYTLVRAAEFVKEHGASKIYALVTHCVLSGDAIERVKLSCIDKLIVTNTAPQTITPSGCFDIIDVAPTFAEAIRRIHNGESISILYDHNQVWV", "text": "FUNCTION: 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family."}
+{"protein": "MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLAFIKQSKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLDPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGDAQMNPTERAKKVEDMMKKLWGDRYFDPATGKFSKSATGPDGKKLPRTFCQLILDPIFKVFDAIMTFKKEEAAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAIGIKNCDPRGSLMMYISKMVPTSDKGRFYAFGRVFSGLVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVMCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVTEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGVLCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYACVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDSASRPSQVVAETRKRKGLKEGIPALDNFLDKL", "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 Nucleus. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
+{"protein": "MHSFGYRANALLTFAVTILAFICAIASFSDNFSNQNPSAQIQILNINWFQKQPHGNDEVSLTLNITADLQSLFTWNTKQVFAFVAAEYETSKNALNQVSLWDAIIPEKEHAKFWIQISNKYRFIDQGHNLRGKDFNLTLHWHVMPKTGKMFADKIVMSGYRLPNAYR", "text": "FUNCTION: Essential 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). Essential for the SPC catalytic activity, possibly by stabilizing and positioning the active center of the complex close to the lumenal surface (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the SPCS3 family."}
+{"protein": "MKTLVLVAVLGLASLYLLSYASEVQQLSRDEEEFRALVASFGGLFDTEERGVDKEGCRKLFGGCVGDGDCCLHLGCKTRKLPPFADPYCAWDWTFGRK", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 25 (ICK4) subfamily."}
+{"protein": "MSLEDCYNVTQSYAAVAIHKEQTADYVEAIALFQKAKRNILMNPEFKYARERLHVMDYEDRHYVETLLCMLEQLTIRIEFLTKEIAQQEAAYKDIQNTQKSLVTQSSTGSANVAYISGNGPGDRSFIDDGNYSASSFERQNRTAPLQSKVTTASLKPNIPRTSMSSSPTASRTSLRKGAGELETHSAVKSAKKASVKSKSVLPPSKSLARTGLPAEVSTQNNANRAALLAWGSLNSSKPKHALPPSYISSEAAQASRSSFQVERHRPTPDNSAVIEAARRTYSSISSSSSPFKKKTQSHLPNRTTEVPSISKQLSKSSTSIATVAPSLASVSSVTKSPSPTPQSAPRAQSASTETAQDLDFLTPPRLSVNNPFLSDLYPASEQGLSSCEEKDSPVDGDEFFNHTNEEEIIEKQFQSTSISAMTSEKQEQILRECPDIDEELGKSILREIVVSGDEVHWDDISGLEFAKHSLKEAVVYPFLRPDLFQGLREPARGMLLFGPPGTGKTMLARAVATESRSVFFSISASSLTSKFLGESEKLVRALFTLAKKLSPSIIFVDEIDSLLSARSSDGNEHETSRRIKTEFLIQWSSLARAAASRQTADHPRVLVLAATNLPWCIDDAARRRFVRRTYIPLPDETTRRLHLNNLLKYQKHSLSLEDIEAIVKATEYYSGSDLTALAKDAAMGPLRSLGESLLFTKMESIRPINLDDFKTSIKVIRPSVNLQGLERYSEWDKEFGSQGH", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AAA ATPase family."}
+{"protein": "MDREEPAESECTLRALVEEYNGACKEAPKEMSKQFTDYNTFKRYTTSKKDHAPQMRLVYSVRKPWPISMTPSKEIPLVFNGTKLKDTILDLGESKRTRANIVVPDYWSKYGSQTSLEVVNAILYAEDLKVQRFFSTEWGEIRYGRMLPFRKPVQACPTIEEVNPASIPHTLLQVFCPQYTTLDSKRKAHMGAVEKLKRVMEPICKVQTQESAVHIARSLIDSNKKWLPTVVDHTPRTAEMAHFLCSKYHYVHTNTQDLSDTRSIDNLCGELVKRSLKCRCPKETLVANLDKITIQGRPMREVLADHDGELPYLGICRVAMGLSTHHTMKIRSTKFSILNSDHPRIEVKKVFSLSPDVQVTIPYRRFKGKAKVYFQNDQIQGYFSCTDRQIDEIKISAPKNAPLLEPLLDICYYGSFIEPGFEQTFGFYPAGKREFVDSFFMHHSKDHKAFLIHMGLDKDLSLPLSPELNWKEPALSKVCRVTELDSTVQPYTSATREFVLGETLNVYTQHENGLELLICPTEIRSTRGPLPPGTNLSGSEFIDIYQDPFSRAKSLLKSTILHAERCKEFVGNMLEEYQDPAETTVQSLVPINTWGKSAKRKLQEEITSDPDWHQCPRKRAKMSYLAIIAGSIQDRDKKQTNVPRAFMLRGSQIEYDMKATRGLVVDTTNRIIVGGETVLREGKGGPEGYVQTGVFEEQPRCYLVDTPDHGLSMGLSRFCVHSQGRYFQYEKKISIWEETDNIKATIDSQRDLKRRRDIEEMVSKRARIV", "text": "FUNCTION: subunit of the 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: Virion. Host nucleus. SIMILARITY: Belongs to the influenza viruses PB2 family."}
+{"protein": "MNRTKLVLGAVILGSHSAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNQAHAYKK", "text": "FUNCTION: A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side Secreted, cell wall; Peptidoglycan-anchor Note=Attached via its lipidated N- terminus to the inner leaflet of the outer membrane. Attached to the peptidoglycan network (PGN) via its C-terminus. SIMILARITY: Belongs to the Lpp family."}
+{"protein": "MAMKIGTDAFKERVSQGIDNEFMRGAVSGAQERLRTRRLEAAEELGNWEEWRSLSEEIRQHVLENLDFYLGQLAENVAKRGGHVYFAKTAEEASSYIRDVIQKKNGKKIVKSKSMVTEEINLNEVLEKEGCEVVETDLGEYILQIDDHDPPSHIVAPALHKNKEQIRDVFKERLDYQHTEKPEELVMHARAILRKKFLEADIGITGCNFAIADTGSVSLVTNEGNGRLVSTLPKTQITVMGMERIVPSFSEFEVLVSMLTRSAVGQRLTSYITALTGPKLEGEVDGPEEFHLVIVDNGRSNILGTEFQSVLQCIRCAACINVCPVYRHVGGHSYGSIYSGPIGAVLSPLLGGYDDYKELPYASSLCAACSEACPVKIPLHELLLKHRQNIVEKEGRAPISEKLAMKAFGLGASSLSLYKMGSKWAPAAMTPFTEDEKISKGPGPLKNWTQIRDFPAPHKSRFRDWFADRETSERTKEEQ", "text": "FUNCTION: Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present. SIMILARITY: Belongs to the LutB/YkgF family."}
+{"protein": "MEALVYTFLLVSTLGIIFFAIFFREPPKVPTKK", "text": "FUNCTION: Seems to play a role in the dimerization of PSII. FUNCTION: Seems to play a role in the dimerization of PSII. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbT family. SIMILARITY: Belongs to the PsbT family."}
+{"protein": "MSVLKKDSTSEKRTQLESILEERNNKLTQLFWLSRLNELKSGGDLQSVRQELAEFLVQNDLTKNLTFDISSLRTYRPQEPPMDRRPLRSKSSTPLENGTINRKREDAEPHMEETRKRLREHIIPEEDDDREHEQRPVKLQKVGLSHDEELPKRLEPPTIPIRKISSAGDNQETGSVIGEKKSEQPVSTSRNRPIHTQLSTNPFYQHMDISTLRAEPTPVEVKRKRNYIIDEIIKTQSKSTDTSDSHSTAGGRDSVYLVMKETVPSKLARAIPLSELKYVSQTLPLIRLIPPTHKALTTDLYNTALNEGRITVVSSRIEELRRLNLWSLRQPKKFLDPWRQKQPSTHRGYMLEEARWMREDFHEFKKFKVSVCAVNSKAIMDYWKYGKACCIKRRSISHLQKSVNEVQEADTLGNIDDLLNKISDKKLAGMIEEQKKVIAVDAKLSSSKIAPSEEIHAPHIWEDPLDELDEQGCKPIFKTYMSYNGVSPLEKTILEDLPIYKGILDEQAAEDNSVPFVPISKSTVLLDDDYFMKLIEKDIVDDEPSFVALSKRRGMFYGNRRSHYLKPPSAPALRYLKFRTPTIWSPEDDQELVKNINQYAYNWDLIGALVSSSNGRSYISNIERRTPWQCFERFVQLNEKFSVHDMKGPRANAAQMWLYEAHKLQQQQKRRISPLGVGSESIQRGHRRLRWATMFEAMRKTIKKRENAPRPNPSQPRKPLDVKSAAVPTPAEMSELKAQRDETLRREGQMRRAAKQRIHLAQLQQQQQRVQQDVVQQRPQSRSQPDPPLSQQIPRVQSPRPQQPLAQQLIEDKGKLLPGVSVSAPTSKEASNNGKNLMALRQVQSSPVNGDLQKATAQVPPRGPNKPLTEKEIIESYARKIIAQKPDFTPELALKAAESYYQNVTLKQNTIGKQIVSQPLSAATVSTPPSNGRAVHKIRSPTPQEILQRIQQKKNDS", "text": "FUNCTION: 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 EAF1 family."}
+{"protein": "MQVLTKRYPKNCLLTVMDRYSAVVRNMEQVVMIPSLLRDVQLSGPGGSVQDGAPDLYTYFTMLKSICVEVDHGLLPREEWQAKVAGNETSEAENDAAETEEAEEDRISEELDLEAQFHLHFCSLHHILTHLTRKAQEVTRKYQEMTGQVL", "text": "FUNCTION: Plays a role in the regulation of lipogenesis, especially in lactating mammary gland. Important for the biosynthesis of triglycerides with medium-length fatty acid chains. May modulate lipogenesis by interacting with MID1IP1 and preventing its interaction with ACACA. May function as transcriptional coactivator. May modulate the transcription factor activity of THRB (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the SPOT14 family."}
+{"protein": "MMGSWKHCLFSASLISALIFVFVYNTELWENKRFLRAALSNASLLAEACHQIFEGKVFYPTENALKTTLDEATCYEYMVRSHYVTETLSEEEAGFPLAYTVTIHKDFGTFERLFRAIYMPQNVYCVHLDQKATDAFKGAVKQLLSCFPNAFLASKKESVVYGGISRLQADLNCLEDLVASEVPWKYVINTCGQDFPLKTNREIVQYLKGFKGKNITPGVLPPDHAVGRTKYVHQELLNHKNSYVIKTTKLKTPPPHDMVIYFGTAYVALTRDFANFVLQDQLALDLLSWSKDTYSPDEHFWVTLNRIPGVPGSMPNASWTGNLRAIKWSDMEDRHGGCHGHYVHGICIYGNGDLKWLVNSPSLFANKFELNTYPLTVECLELRHRERTLNQSETAIQPSWYF", "text": "FUNCTION: [Isoform C]: Determines the expression of the blood group I antigen in erythrocytes. FUNCTION: Branching enzyme that converts linear into branched poly-N- acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 14 family."}
+{"protein": "MDTTQVTLIHQILAAADERNLPLWIGGGWAIDARLGRVTRKHDDIDLTFPGERRGELEAMVEMLGGRVTEELDYGFLAEIGDELLDCEPAWWADEAYEIAEAPQGSCPEAAEGVIAGRPVRCNSWEAIIWDYFYYADEVPPVDWPTKHIESYRLACTSLGAEKVEVLRAAFRSRYAA", "text": "FUNCTION: Mediates bacterial resistance to kanamycin, gentamicin, dibekacin, sisomicin, neomycin and tobramycin by adenylating the 2''- hydroxyl group of these antibiotics."}
+{"protein": "MSQVQVQVQNPSAALSGSQILSKNQSLLSQPLMSIPSTTSSLPSENAGRPIQNSALPSASLTPTSAAAESITPTVELNALCMKLGKKPMYKPVDPYSRMQSTYNYNMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKTRQAAKHDAAAKALRTLQSEPLPERPEGRRPGEQVNGRESEEENLNKSEISQVFEIALKRNLPVNFEVARESGPPHMKSFVTRVSVGEFVGEGEGKSKKISKKNAAIAVLEELKKLPPLPTFERVKPRIKKKTKSIVRLQGSTDCSQGMNPISRLAQIQQAKKEKEPEYLLLTERGLPRRREFVMQVKVGNHTAEGTGTNKKVAKRNAAENMLEILGFKVPQAQPTKPALKSEEKTPIKKPGDGRKVTFFEPGSGDENGTSNKEDEFRLPYLSHQQLPAGILPMVPEVAQAVGVSQGHHTKDFTRVAPNPAKATVTAMIARELLYGGTSPTAETILKNNISSGHVPHGPLTRPSEQLDYLSRVQGFQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILKLLSELDQPSTEMPRTGNGPMSV", "text": "FUNCTION: Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site (By similarity). SUBCELLULAR LOCATION: Cytoplasm Rough endoplasmic reticulum Note=Localizes exclusively with the rough reticulum endoplasmic (RER)."}
+{"protein": "MTLFNSISSISNSTGISKHSLIGNFESNNSRSGGNSISWLGGFDGCGGCGGCGGCGGCGCGSSNLNIINVDIDIGRRRRRRCC", "text": "SIMILARITY: Belongs to the UPF0512 family."}
+{"protein": "MPGRKARKSAQPGPTRAPEELEVECAIQLRKFGDKLNFRQKLLNLLSKLFRSGT", "text": "FUNCTION: Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BAK1 and with BIM/BCL2L11 for binding to MCL1; can displace BAK1 and BIM/BCL2L11 from their binding sites (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PMAIP1 family."}
+{"protein": "MNARTEPEVFDTLAALIAVRAAQWPDKPYLLSPDSGHALTFGALATDAGTLGRSYAAAGLGSGQTVSVYLPNGEQTARLLLGTMACGLVVNPINLLCQPAQLRYILAHSDTRLVFTWPDGEAAIREALREAGLDVPVLVTAPDANSLPALPATHDAASPLPPPQPDAPALLMYTSGTTGTPKGVLLTQRNLVANGTNVSREHCLGPADRVLATLPLYHINGLVVTAIAPLVHGGSVVMPMRFSASAFWQDSARHGCTWLNVVPTIIAYLLNDPHGQAPAGVRFCRSASAALPPEHHRAFEARFGIGVIETMGMTETAAPAFSNPLDPGQRRIGSIGRPSGTRARVLGRDGKPAPDGQVGEIVLQGESVMAGYYKAPDITREAFTHDGWLRTGDLGYRDADGYFYISGRAKELIIKGGENIAPREIDEALLRHPGVLEAAAVGVPDPAYGQEIVAYVVMREAARCDDAALRAHCLRELGRYKTPKEFRFIAELPRGPSGKVQRLKLLNHA", "text": "FUNCTION: Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and AMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MMKLSVSFLLLLMLLPFITGEENSDSDVLKSGAAVRQGRGRCRGFREDCSQHRDCCGDLCCNGNTCVITVIACPKW", "text": "FUNCTION: Antimicrobial peptide that potently inhibits growth of Mycobacterium tuberculosis (H37Rv strain) (MIC=3 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin I1 superfamily."}
+{"protein": "MQPPPRKVKPAQEVKLRFLEQLSILQTWQQREADLLEDIRSYSKQRAAIEREYGQALQKLAGPFLKREGHRSGEMDSRGRTVFGAWRCLLDATVAGGQTRLQASDRYRDLAGGTGRSAKEQVLRKGTENLQRAQAEVLQSVRELSRSRKLYGQRERVWALAQEKAADVQARLNRSDHGIFHSRTSLQKLSTKLSAQSAQYSQQLQAARNEYLLNLVATNAHLDHYYQEELPALLKALVSELSEHLRDPLTSLSHTELEAAEVILEHAHRGEQTTSQVSWEQDLKLFLQEPGVFSPTPPQQFQPAGTDQVCVLEWGAEGVAGKSGLEKEVQRLTSRAARDYKIQNHGHRVLQRLEQRRQQASEREAPSIEQRLQEVRESIRRAQVSQVKGAARLALLQGAGLDVERWLKPAMTQAQDEVEQERRLSEARLSQRDLSPTAEDAELSDFEECEETGELFEEPAPQALATRALPCPAHVVFRYQAGREDELTITEGEWLEVIEEGDADEWVKARNQHGEVGFVPERYLNFPDLSLPESSQDSDNPCGAEPTAFLAQALYSYTGQSAEELSFPEGALIRLLPRAQDGVDDGFWRGEFGGRVGVFPSLLVEELLGPPGPPELSDPEQMLPSPSPPSFSPPAPTSVLDGPPAPVLPGDKALDFPGFLDMMAPRLRPMRPPPPPPAKAPDPGHPDPLT", "text": "FUNCTION: Promotes actin polymerization mediated by SNX9 and WASL. SUBCELLULAR LOCATION: Cytoplasm Perikaryon Cell projection Cytoplasmic vesicle Note=Detected on neuronal cell bodies and cell projections, in part on cytoplasmic vesicles."}
+{"protein": "MLGVSLGARLLRGVGGRRGQFGARGVSEGSAAMAAGESMAQRMVWVDLEMTGLDIEKDQIIEMACLITDSDLNILAEGPNLIIKQPDELLDSMSDWCKEHHGKSGLTKAVKESTVTLQQAEYEFLSFVRQQTPPGLCPLAGNSVHADKKFLDKHMPQFMKHLHYRIIDVSTVKELCRRWYPEDYEFAPKKAASHRALDDISESIKELQFYRNNIFKKKTDEKKRKIIENGENEKPVS", "text": "FUNCTION: 3'-to-5'exoribonuclease that preferentially degrades DNA and RNA oligonucleotides composed of only two nucleotides (By similarity). Binds and degrades longer oligonucleotides with a lower affinity (By similarity). Plays dual roles in mitochondria, scavenging nanoRNAs (small RNA oligonucleotides of <5 nucleotides) that are produced by the degradosome and clearing short RNAs that are generated by RNA processing (By similarity). Essential for correct initiation of mitochondrial transcription, degrading mitochondrial RNA dinucleotides to prevent RNA-primed transcription at non-canonical sites in the mitochondrial genome (By similarity). Essential for embryonic development (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space Mitochondrion matrix Mitochondrion Cytoplasm Nucleus. SIMILARITY: Belongs to the oligoribonuclease family."}
+{"protein": "MLFNNFLCFAVSAIPLVSAMPLGNAPYHHHHHAGLNASNITVGVNVTNTTAFSKRDGGFPDGVYDCSSFPDDQNGVVRLDYLGFGGWSGVQKNDGKYGTASTCQDNTYCSYACKPGMSKTQWPSEQPDNGVSVGGLYCKNGKLYLTQKDNSNLCEDGKGTAYVKNTLSSNVAICRTDYPGTENMNIPTNIDGGSKQPLSDVDEDSYYNWGGKKTSAQYYVNKSGRSAEDVCVWGNEGDDYGNWAPMNFGSGYTDGKTWLSMSFNPLSSAKLDYNIRIKSDGGSLSGDCYYEDGSFHGSTADSSGCTVSVTGGNAYFELY", "text": "FUNCTION: Cell surface beta-glucosidase involved in cell wall biogenesis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SUN family."}
+{"protein": "MATGTDQVVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLIPLATGLLLLLFVGLFITYVMLKSRRLTKKAQ", "text": "FUNCTION: Regulates the biosynthesis of dolichol phosphate-mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1. 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. May act by regulating the GPI-GNT complex. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DPM2 family."}
+{"protein": "MGSKRRFSSEHPDPVETSIPEQAAEIAEELSKQHPLPSEEPLVHHDAGEFKGLQRHHTSAEEAQKLEDGKINPFTGREFTPKYVDILKIRRELPVHAQRDEFLKLYQNNQIMVFVGETGSGKTTQIPQFVLFDEMPHLENTQVACTQPRRVAAMSVAQRVAEEMDVKLGEEVGYSIRFENKTSNKTILKYMTDGMLLREAMEDHDLSRYSCIILDEAHERTLATDILMGLLKQVVKRRPDLKIIIMSATLDAEKFQRYFNDAPLLAVPGRTYPVELYYTPEFQRDYLDSAIRTVLQIHATEEAGDILLFLTGEDEIEDAVRKISLEGDQLVREEGCGPLSVYPLYGSLPPHQQQRIFEPAPESHNGRPGRKVVISTNIAETSLTIDGIVYVVDPGFSKQKVYNPRIRVESLLVSPISKASAQQRAGRAGRTRPGKCFRLYTEEAFQKELIEQSYPEILRSNLSSTVLELKKLGIDDLVHFDFMDPPAPETMMRALEELNYLACLDDEGNLTPLGRLASQFPLDPMLAVMLIGSFEFQCSQEILTIVAMLSVPNVFIRPTKDKKRADDAKNIFAHPDGDHITLLNVYHAFKSDEAYEYGIHKWCRDHYLNYRSLSAADNIRSQLERLMNRYNLELNTTDYESPKYFDNIRKALASGFFMQVAKKRSGAKGYITVKDNQDVLIHPSTVLGHDAEWVIYNEFVLTSKNYIRTVTSVRPEWLIEIAPAYYDLSNFQKGDVKLSLERIKEKVDRLNELKQGKNKKKSKHSKK", "text": "FUNCTION: Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. DDX15/PRP43 sub-subfamily."}
+{"protein": "MRLVVCLVFLASFALVCQGQGYKGPYTRPILRPYVRPVVSYNVCTLSCRGITTTQARSCCTRLGRCCHVAKGYSG", "text": "FUNCTION: Antibacterial and antifungal activity. Presents chitin- binding activity (By similarity). 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": "MAVDVPRAVINKLMLFTAAMVVLPVLTFFIIQQFTPNTLISGGLAAAMANVVLIVYIVVAFREDTEDHKVDGNKKED", "text": "FUNCTION: Functions with VOA1 in assembly of the integral membrane sector (also called V0 sector) of the V-ATPase in the endoplasmic reticulum. Escorts the assembled V0 sector in COPII vesicles. Also required for normal packaging of the SNARE BOS1 and possibly the ER to Golgi transport receptor ERV29. FUNCTION: Functions with VOA1 in assembly of the integral membrane sector (also called V0 sector) of the V-ATPase in the endoplasmic reticulum. Escorts the assembled V0 sector in COPII vesicles. Also required for normal packaging of the SNARE BOS1 and possibly the ER to Golgi transport receptor ERV29. 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": "MAERSQTAPEAGNDTGNEDAIGGNVNKYIVLPNGYSGQPKKGHLTFDACFESGNLGRVEQVSDFEYDLFIRPDTCNPRFRVWFNFTVENVKELQRVIFNIVNFSKTKSLYRDGMAPMVKSTSRPKWQRLPPKNVYYYRCPDHRKNYVMSFAFCFDREDDIYQFAYCYPYTYTRFQHYLDSLQKKNMDYFFREQLGQSVQQRQLDLLTITSPENLREGSEKKVIFITGRVHPGETPSSFVCQGIIDFLVSQHPIARVLREHLVFKIAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWAHPTLHGVKQLIIKMYNDPKTSLEFYIDIHAHSTMMNGFMYGNIFEDEERFQRQSIFPKLLCQNAEDFSYTSTSFNRDAVKAGTGRRFLGGLLDHSSYCYTLEVSFYSYIIGGTTAAVPYTEEAYMKLGRNVARTFLDYYRLNSLVEKIAVPMPRLRSKEERRLGWEHPSCLRAEQPLEVLGIPMCSGKALNEHLGNDIQWHLDCGSSTLPLGLISCSPSSSASWNDMAMSNSILLPDHSFH", "text": "FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins (PubMed:21074048, PubMed:25103237, PubMed:26829768, PubMed:29593216). Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein (PubMed:21074048, PubMed:25103237). Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate (PubMed:25103237). Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK (PubMed:21074048). Mediates the deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation (PubMed:26829768). Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis (PubMed:29593216). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Golgi apparatus Cytoplasm, cytoskeleton, cilium basal body Note=Colocalizes with gamma- tubulin in the centrioles at interphase and dividing cells and with glutamylated tubulin in basal bodies of ciliated cells. SIMILARITY: Belongs to the peptidase M14 family."}
+{"protein": "MQIALAPMEGLVDDILRDALTKVGGIDWCVTEFIRVSERLMPAHYFYKYASEFHNGAKTDAGTPLRLQLLGSDPVCLAENAAFACELGAPVLDLNFGCPAKTVNRSRGGAILLKEPELLHTIVSQVRRAVPKDIPVTAKMRLGYENTDGALDCARALADGGAAQIVVHARTKVDGYKPPAHWEWIARIQEVVKVPVVANGEIWTVEDWRRCREICGARDIMIGRGLVARPDLARQIAAAQKGEEVVPMTWAELQPMLRTFWQACLVKMTLVQAPGRLKQWLVLLTKSYPEATLMFNTLRRETDCDRITVLLGCSTKS", "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. Specifically modifies U16 in tRNAs. SIMILARITY: Belongs to the Dus family. DusC subfamily."}
+{"protein": "RLAPEYEAAATRYGVSGYPTLKDGEEAGAYDGPRTADGIVSHLKFISDKDASVVGFFRDLFSDGHSEFLKFAHTNVESLVKEYDDNGEGITLFRPSHLANKFEDKDLLTAYYDVDYEKKTFSHELSDFGLESTTGEVPVVAIRFVMQEEFSRFLQDYFDGNLKRYLKSEPIPETNDGPVKMDATANDVPSPYEVKGFPTIYFSPANKK", "text": "FUNCTION: Disulfide isomerase which catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds (By similarity). Associates with calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (By similarity). Association with calcitriol does not affect its enzymatic activity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum Endoplasmic reticulum lumen Melanosome. SIMILARITY: Belongs to the protein disulfide isomerase family."}
+{"protein": "MCAAEVDRHVSQRYLIKRRLGKGAYGIVWKAMDRRTGEVVAIKKIFDAFRDQTDAQRTFREIMLLREFGGHPNIIRLLDVIPAKNDRDIYLVFESMDTDLNAVIQKGRLLEDIHKRCIFYQLLRATKFIHSGRVIHRDQKPANVLLDAACRVKLCDFGLARSLSDFPEGPGGQALTEYVATRWYRAPEVLLSSRWYTPGVDMWSLGCILGEMLRGQPLFPGTSTFHQLELILETIPLPSMEELQGLGSDYSALILQNLGSRPRQTLDALLPPDTPPEALDLLKRLLAFAPDKRLSAEQALQHPYVQRFHCPDREWTRGSDVRLPVHEGDQLSAPEYRNRLYQMILERRRNSRSPREEDLGVVASRAELRASQRQSLKPGVLPQVLAETPARKRGPKPQNGHGHDPEHVEVRRQSSDPLYQLPPPGSGERPPGATGEPPSAPSGVKTHVRAVAPSLTSQAAAQAANQPLIRSDPARGGGPRAVGARRVPSRLPREAPEPRPGRRMFGISVSQGAQGAARAALGGYSQAYGTVCRSALGRLPLLPGPRA", "text": "FUNCTION: Atypical MAPK protein that regulates several process such as autophagy, ciliogenesis, protein trafficking/secretion and genome integrity, in a kinase activity-dependent manner. Controls both, basal and starvation-induced autophagy throught its interaction with GABARAP, MAP1LC3B and GABARAPL1 leading to autophagosome formation, SQSTM1 degradation and reduced MAP1LC3B inhibitory phosphorylation. Regulates primary cilium formation and the localization of ciliary proteins involved in cilium structure, transport, and signaling. Prevents the relocation of the sugar-adding enzymes from the Golgi to the endoplasmic reticulum, thereby restricting the production of sugar- coated proteins. Upon amino-acid starvation, mediates transitional endoplasmic reticulum site disassembly and inhibition of secretion. Binds to chromatin leading to MAPK15 activation and interaction with PCNA, that which protects genomic integrity by inhibiting MDM2-mediated degradation of PCNA. Regulates DA transporter (DAT) activity and protein expression via activation of RhoA. In response to H(2)O(2) treatment phosphorylates ELAVL1, thus preventing it from binding to the PDCD4 3'UTR and rendering the PDCD4 mRNA accessible to miR-21 and leading to its degradation and loss of protein expression (By similarity). Also functions in a kinase activity-independent manner as a negative regulator of growth (PubMed:9891064). Phosphorylates in vitro FOS and MBP (PubMed:11875070). During oocyte maturation, plays a key role in the microtubule organization and mei- otic cell cycle progression in oocytes, fertilized eggs, and early embryos (By similarity). Interacts with ESRRA promoting its re-localization from the nucleus to the cytoplasm and then prevents its transcriptional activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Cell junction, tight junction Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasmic vesicle, autophagosome Golgi apparatus Nucleus Cytoplasm Cytoplasm, cytoskeleton, spindle Note=Co-localizes to the cytoplasm only in presence of ESRRA. Translocates to the nucleus upon activation (By similarity). At prometaphase I, metaphase I (MI), anaphase I, telophase I, and metaphase II (MII) stages, is stably detected at the spindle (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
+{"protein": "MKTQIEIAREGTISSQMMAVAAEEHVSPDYVRQMVAEGKIVIPGNHSRKPRAVGIGKGLRTKVNASIGTSSDIIDYGAEVRKALAAQEAGADTLMELSVGGDLDRVRREVIAAVDLPVGNVPLYQAFCEAARKYGDPNKLDPEMLFDLIEKQCEDGMAFMAVHCGINLYTIERLKRQGYRYGGLVSKGGVSMVAWMMANRRENPLYEQFDRVTSILRKYDTVLSLGNGLRAGAIHDSSDRAQIQELLINCELAELGREMGCQMLVEGPGHVPLDEVEGNIQLQKRMSGGAPYYMLGPISTDVAPGFDHITAAIGAAQSSRYGADLICYITPAEHLALPNEEDVRQGVKAAKIAAYIGDMNKYPERGRERDKEMSKARRDLDWKKQFELALFPEDAKAIRASRTPEDEATCTMCGDFCASRGAGKLFAADLRGDKI", "text": "FUNCTION: Catalyzes the conversion of aminoimidazole ribotide (AIR) to 5-hydroxybenzimidazole (5-HBI) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Is thus involved in the anaerobic biosynthesis of the benzimidazole lower axial ligand of the cobamide produced by G.metallireducens. SIMILARITY: Belongs to the ThiC family. 5-hydroxybenzimidazole synthase subfamily."}
+{"protein": "LPLRF", "text": "FUNCTION: May function as a neurotransmitter or modulator. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
+{"protein": "MSKRPGDIIISTPGSKVRRRLNFDSPYRNRATAPTVHVTNRKRAWVNRPMYRKPTMYRMYRSPDIPRGCEGPCKVQSFEQRDDVKHLGICKVISDVTRGPGLTHRVGKRFCIKSIYILGKIWLDETIKKQNHTNNVIFYLLRDRRPYGNAPQDFGQIFNMFDNEPSTATIKNDLRDRFQVLRKFHATVVGGPYGMKEQALVKRFYRLNHHVTYNHQEAGKYENHTENALLLYMACTHASNPVYATLKIRIYFYDSIGN", "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": "MASPMEAVARSSLVLAPRRRRALGLLPAAAAPFVLDCRRRHNGGMRRPHVSFACSAELDTGRRQLPSTGTRAVMSSCPGYVEGRMVGENTSQINMGREARIRRHLENPEFLPSSYDIAWVAMVPLPGTDHLQAPCFPECVEWILQNQHSNGSWGVNEFDSSASKDILLSTLACIIALEKWNVGSEQIRRGLHFIAKNFSIVIDDQIAAPIGFNLTFPAMVNLAIKMGLEFPASEISIDQILHLRDMELKRLSGEESLGKEAYFAYIAEGLEESMVDWSEVMKFQGKNGSLFNSPAATAAALVHRYDDKALGYLYSVVNKFGGEVPTVYPLNIFSQLSMVDTLVNIGISRHFSSDIKRILDKTYILWSQRDEEVMLDLPTCAMAFRLLRMNGYGVSSDDLSHVAEASTFHNSVEGYLDDTKSLLELYKASKVSLSENEPILEKMGCWSGSLLKEKLCSDDIRGTPILGEVEYALKFPFYATLEPLDHKWNIENFDARAYQKIKTKNMPCHVNEDLLALAAEDFSFCQSTYQNEIQHLESWEKENKLDQLEFTRKNLINSYLSAAATISPYELSDARIACAKSIALTLVADDFFDVGSSKEEQENLISLVEKWDQYHKVEFYSENVKAVFFALYSTVNQLGAMASAVQNRDVTKYNVESWLDYLRSLATDAEWQRSKYVPTMEEYMKNSIVTFALGPTILIALYFMGQNLWEDIVKNAEYDELFRLMNTCGRLQNDIQSFERECKDGKLNSVSLLVLDSKDVMSVEEAKEAINESISSCRRELLRLVVREDGVIPKSCKEMFWNLYKTSHVFYSQADGFSSPKEMMGAMNGVIFEPLKTRGN", "text": "FUNCTION: Involved in the biosynthesis of momilactone A and B phytoalexins. Catalyzes the conversion of syn-copalyl diphosphate to the phytoalexin precursor syn-pimara-7,15-diene. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MCEENVHVSEDVAGSHGSFTNARPRLIVLIRHGESESNKNKEVNGYIPNHLISLTKTGQIQARQAGIDLLRVLNVDDHNLVEDLAKKYIKDESSRRTLPLKDYTRLSREKDTNIVFYTSPYRRARETLKGILDVIDEYNELNSGVRICEDMRYDPHGKQKHAFWPRGLNNTGGVYENNEDNICEGKPGKCYLQYRVKDEPRIREQDFGNFQKINSMQDVMKKRSTYGHFFFRFPHGESAADVYDRVASFQETLFRHFHDRQERRPRDVVVLVTHGIYSRVFLMKWFRWTYEEFESFTNVPNGSVMVMELDESINRYVLRTVLPKWTDCEGDLTT", "text": "FUNCTION: Metal-independent, broad-range acid phosphatase. Involved, either directly or indirectly, in the bidirectional transport of sterols between the endoplasmic reticulum and the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the phosphoglycerate mutase family."}
+{"protein": "MAEYTLPDLDWDYAALEPHISGQINEIHHTKHHATYVKGVNDALAKLEEARANEDHAAIFLNEKNLAFHLGGHVNHSIWWKNLSPDGGDKPTGELAAAIDDAFGSFDKFRAQFSAAANGLQGSGWAVLGYDTVGSRLLTFQLYDQQANVPLGIIPLLQVDMWEHAFYLQYKNVKADYVKAFWNVVNWADVQKRYAAATSKAQGLIFG", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
+{"protein": "MLGRSRLTFVLLSVTVTCSVAQHVPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMVDKAPALKVIVNYLKNMINAFEPSGKIVQLVDQKLPGLLGSFPGPFEEEMKGIAAVTEIPLGEIILFNIFYEFFTICTSIITEDKEGHLLHARNMDFGVFLGWNVNNNTWVVTEELKPLTVNLDFQRNSKTVFKAAGFAGYVGMLTGFKPGLFSLTLNERFSTNGGFMGVIEWILGKKDAKWIGFIIRSVLENSTSYEEAKTILTKSKILAPAYFILGGSKSGEGCVITRDRVQSLDIYELDPKQGIWYVVQTNYDRWKNPFFLDNRRTPAKMCLNRTTQENISFATMYDVLSTKPVLNKLTVYTALIDVTKGQFETYLRDCPDPCIGW", "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": "MADGSKVFKKTSPDGKITVYLAKRDYVDHVEFVEPVDGMIVIDPEYQKEKKVFVTMTCAFRYGRDDMELIGLSFRKDIYVQSCQVHPPLPGEKKALTPLQEKLKAKLGANAFPFSFNMATNLPCSVTLQPGPEDSGKACGVDFEVKGFWGDDVEEKVSKKNVARLIIRKVQYAPETAGAAPHAEITKQFMMSDKPLQLEASLNKEIHYHGEPIIVNVKINNSTNKIVKKIKITVEQITDVVLYSLDKYTKVVCCEEMNDTVAANSAFTKAYQVTPLLANNTEKRGLALDGKLKHGDTNLASSTTLRPGMDKEVMGILVSYKIRVNLMASRGGILGDLISSDVSVELPLILMHPKPAEGTTSAEDVVIEEFARQKLQGEQDDDEDKEEAS", "text": "FUNCTION: May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins. SIMILARITY: Belongs to the arrestin family."}
+{"protein": "MAHVLPDLPYAYDALEPYISRQIMELHHKKTSSDLCECAQHCRGCLRHSTAVVGGFDLSLFFILTTLGHINHSLFWQNLAPAAGAGGQLKPGPLKDAIDQTFGGLDNLKKEFNTTTAGIQGSGWGWLGVNPSNKRLEISTTPNQDPLLNLVPIIGVDIWEHAFYLQYLNVKADYLNAIWSVINFDEAQRRYVEATQGSKL", "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": "MGRSPCCEKAHTNKGAWTKEEDDRLVAYIRAHGEGCWRSLPKAAGLLRCGKSCRLRWINYLRPDLKRGNFTEEEDELIIKLHSLLGNKWSLIAGRLPGRTDNEIKNYWNTHIRRKLLSRGIDPTTHRSINDGTASQDQVTTISFSNANSKEEDTKHKVAVDIMIKEENSPVQERCPDLNLDLKISPPCQQQINYHQENLKTGGRNGSSTLCFVCRLGIQNSKDCSCSDGVGN", "text": "FUNCTION: Transcription factor. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKEIIRNLVRLDVRSDVDENSKKTQELVEKLPHEVLELYKNVGGEIYITDKRLTQHEELSDSSHKDMFIVSSEGKSFPLREHFVFAKGGKEPSLIIHAEDYASHLSSVEVYYELGKAIIRDTFPLNQKELGNPKFINAINEVNQQKEGKGVNAKADEDGRDLLFGKELKKNLEHGQLVDLDLISGNLSEFQHVFAKSFALYYEPHYKEALKSYAPALFNYMLELDQMRFKEISDDVKEKNKNVLDFKWYTRKAESWGVQTFKNWKENLTISEKDIITGYTGSKYDPINEYLRKYDGEIIPNIGGDLDKKSKKALEKIENQIKNLDAALQKSKITENLIVYRRVSELQFGKKYEDYNLRQNGIINEEKVMELESNFKGQTFIQHNYMSTSLVQDPHQSYSNDRYPILLEITIPEGVHGAYIADMSEYPGQYEMLINRGYTFKYDKFSIVKPTREEDKGKEYLKVNLSIYLGNLNREK", "text": "FUNCTION: A probable mono(ADP-ribosyl)transferase; it is not known which residue is targeted for ADP-ribosylation. Upon expression in yeast cells causes cell death. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEDVRAVLKSFLESVIRDAVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG", "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 (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H4 family."}
+{"protein": "MPPKKGGDGIKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQYHKPASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAVRGGDKKLKPEYDIMCKVKSWVIDQKKPVRFYHDWNDKEIEVLNKHLFLTSKPMVYLVNLSEKDYIRKKNKWLIKIKEWVDKYDPGALVIPFSGALELKLQELSAEERQKYLEANMTQSALPKIIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYEDFKEEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFNTPQQPKKK", "text": "FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, nucleolus Note=Predominantly cytoplasmic, shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily."}
+{"protein": "MMDELDKDQIAMLKKAFDGFDHEKKGAINCDVVATILRMMGQAYNAQTLKELIDEVDADGSGMLEFEEFVTLAAKFIIDDDAEAMAKELKEAFRLYDKAGKGYIPTSALKDILKELDETLNAEDLDNIIGEIDTDGSGTVDFDEFMEMMTG", "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": "MVDHKRIPKQVIVGVSGGIAAYKACTVVRQLTEASHRVRVIPTESALRFVGAATFEALSGEPVCTDVFADVPAVPHVHLGQQADLVVVAPATADLLARAAAGRADDLLTATLLTARCPVLFAPAMHTEMWLHPATVDNVATLRRRGAVVLEPATGRLTGADSGAGRLPEAEEITTLAQLLLERHDALPYDLAGRKLLVTAGGTREPIDPVRFIGNRSSGKQGYAVARVAAQRGADVTLIAGHTAGLVDPAGVEVVHVSSAQQLADAVSKHAPTADVLVMAAAVADFRPAQVATAKIKKGVEGPPTIELLRNDDVLAGVVRARAHGQLPNMRAIVGFAAETGDANGDVLFHARAKLRRKGCDLLVVNAVGEGRAFEVDSNDGWLLASDGTESALQHGSKTLMASRIVDAIVTFLAGCSS", "text": "FUNCTION: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'- phosphopantotheine (By similarity). Required for growth and persistence in mice (PubMed:27676316). FUNCTION: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'- phosphopantotheine. SIMILARITY: In the C-terminal section; belongs to the PPC synthetase family. SIMILARITY: In the N-terminal section; belongs to the HFCD (homo- oligomeric flavin containing Cys decarboxylase) superfamily."}
+{"protein": "MASSINGRKPSEIFKAQALLYKHIYAFIDSMSLKWAVEMNIPNIIQNHGKPISLSNLVSILQVPSSKIGNVRRLMRYLAHNGFFEIITKEEESYALTVASELLVRGSDLCLAPMVECVLDPTLSGSYHELKKWIYEEDLTLFGVTLGSGFWDFLDKNPEYNTSFNDAMASDSKLINLALRDCDFVFDGLESIVDVGGGTGTTAKIICETFPKLKCIVFDRPQVVENLSGSNNLTYVGGDMFTSIPNADAVLLKYILHNWTDKDCLRILKKCKEAVTNDGKRGKVTIIDMVIDKKKDENQVTQIKLLMDVNMACLNGKERNEEEWKKLFIEAGFQHYKISPLTGFLSLIEIYP", "text": "FUNCTION: Transfers a methyl group to 7-hydroxyls of the isoflavones daidzein, genistein and 6,7,4'-trihydroxyisoflavone. Can also methylate (+)6a-hydroxymaackiain with lower efficiency. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
+{"protein": "MSTASNRVSTQIVDEHKQFNNELPKFMQSVGLLDAGFNYHVVAVLGSQSTGKSTLLNNLFGTSFSVMDASKRQQTTKGIWLSKANNSPILVMDVEGTDGRERGEDQDFERKSALFSISTSEVIIVNMWENQVGLYQGSNMALLKTVLEVNLQLFHNKKERCLLQFVIRDFLGNTSMENLADTIMTDLNNIWASLSKPEGFENSVINDFFDVGFTGLPHKILCSDAFSEAVDSLRERFVDNNNSDYIFNVSYHKKIPADGFSLYTREIWDTIENNKDLDLPTQQQLLAQYRCDEIITEVMEPFSTACTILQKEFLPGNLCKDLPTKLLNMFETVIEAYDRQASRYNVHIYQKKKQELIASVDSHLYVFFQAQLNALHKELIKSFFDASNEFPSDTPFKESSSIKINELVNKMREEGESLSLPHVHWDVDPFILKLSEELTQNSETLCKEKLKEKLEELFTGFEFEVSEAVEVAFQKLSHNVWDTLLNEFLAAQNTTIEKIKNIVPFYVDIDDTKTTEEYIINFKKNSWLFFRKKIDSEMSEVLLQQRLRVYFEELFRYDSDGMPKLWKKSGTIDRDYRESLTKTLDLINVLASIKVSDGNYPDLNVDIKTLEPEYTSPASFFTILNRRRVSDISVNFKRSADLIFMDCKRSVINTTTRIPPYFWVLLIVLGWNEFMAILRNPFVFMILMFGGTVVYGLYISGLIWPAKMVLERATNNLVDLATDRFSNTYQEQVQQRAMQRTEKSGSPVASADDAEAEKTALS", "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": "MSSKGIQKKTKAVDATKKLAEKIKKQALKQKALASASSAASTKESLPVSETISISTSETPVSDVSELSNKEDLSTKKDQSSASSSSSTSSSSSPPSVQSFTEFDLVPELLESIQSLKYTQPTPIQAAAIPHALQGKDIVGIAETGSGKTAAFAIPILQTLYTAAQPYYALVLAPTRELAFQIKETFDALGSSMGLRSVCIIGGMSMMEQARDLMRKPHVIIATPGRLIDHLEHTKGFSLKKLQYLVMDEVDRMIDLDYAKAIDQILKQIPSHQRITYLYTATMSREIEKFKRSLNSPVQVEIVKLEKVPDKLKQTMCLTSPNTKDTRLIQIVNLDSMKRVIIFTRTVVHTRRCCLMLLNLGFKCVELHGQMPQSRRLGAINKFKAGTPILVATDVAARGLDIPAVDLVINYDIPDPTLYIHRVGRTARAGKAGKAISLVTQYDLESYLRIENTLGTKLPKEDLPLDEMQGLQVSVDRALSKAIQMLRNEENDNKLRHRGRSNNK", "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": "MASRHRRGAFPAGAKAAPEAEAAKESVAVAVRFRPLSPREVRRGEKIAWYADGETVARSEQSNLAYAYDRVFGPTTTTRHIYDAVAQYVVNGAMKGINGTIFAYGVTSSGKTHTMHGDQISPGVIPLAVKDIFNIIQETPNREFLLRVSYLEIYNEVVNDLLNPAGQNLRIREDLQGTIVEGIKEEAVLSPVHALSLIAAGEELRHVGSTNFNLLSSRSHTIFTLTIESSPRGQSNEAEAVTLSQLNLIDLAGSESSRVETAGVHQKEGSYINKSLLTLGKVISKLTDEKATHIPFRDSKLTRLLKSSLSGQGRVSLICTVTPASSNSEETHNTLKFAHRAKHIEIQATQNKIMDARSLIKKYQNEIRQLKEELEQLRRSIRTGTPIEDTMQKKHHLLETKEDCNVKLQSRLEQGEEAKAALLERIEHLTELILVSAKASRTTKSSHCPRRRHSFGEEELAYLPYERQDIILDNESNMLFVPIEGFGEKFKSSPKEETENQKGHLNWLNLRKCDSGSTNLTSSDGENPSSTKSLPALSTPLGIGFFNVTSEQRMSDYMLAENVPANLLCVGHREFPSDSLPVQETPLVSRKTSDHVDILREQFNILSGEVALHQSVLKRLSEEAGKNAMNEQIEMEMKVVNDEVKLNKQKIASLERRISNSMSNSRGMHDNLELSLPYIEIPEQLNEKAFQLEASECQEFLLSERTTFQHNTGIVQETGSQAHKGKPLPSDVSDEFLKKASQAEIDELKQRVSELTEAKSQLDSCNHKLLEESTYAKGLASVTSVELKALSVKVTKLMKQNERLSSELASGRNQRRGSHGPRGARRESHTKRYEPARRGDMNALEAMLKEKDQRQAELHTKIEESKQKEAFLEKELANMWTVLANLKKTRGIDQEDFDSKYNGSWA", "text": "SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-7 subfamily."}
+{"protein": "MVTYVSALFYGFGGIVVAGVALLVAFQEKLVYVPVLPGLSKSYPITPARLNLIYEDIWLQSSDGVRLHAWFIKMFPECRGPTILFFQENAGNIAHRLEMVRIMIQKLKCNVFMLSYRGYGASEGYPSQQGIIKDAQAALDHLSGRTDIDTSRIVVFGRSLGGAVGAVLTKNNPDKVSALILENTFTSILDMAGVLLPFLKWFIGGSGTKSLKLLNFVVRSPWKTIDAIAEIKQPVLFLSGLQDEMVPPFHMKMLYAKAAARNPQCTFVEFPSGMHMDTWLSGGEVYWKTNLQFLEKYAPEKRKEDTGR", "text": "FUNCTION: Involved in the regulation of root growth. Involved in the suppression of the root bending in response to touch stimuli, gravity and light. Regulates negatively stimulus-induced root bending through inhibition of root tip rotation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the serine esterase family."}
+{"protein": "MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLALGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNILSQGVLKEDVFSFYYNRDSENAQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIPMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAH", "text": "FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. SUBCELLULAR LOCATION: Secreted Membrane Note=Associated to membranes via binding to ATP6AP2. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MKALILVGGFGTRLRPLTLSVPKPLVDFGNKPMILHQIEALKEVGVTEVVLAINYQPEVMLNFLKDFESKLGIKITCSQETEPLGTAGPLALARDKLADGSGDPFFVLNSDVISEYPFAELIQFHKSHGGEATIMVTKVDEPSKYGVVVMEDETDKVERFVEKPKVFVGNKINAGIYLLNPSVLDRIELKPTSIEKEVFPRIAADNGLFAMVLPGFWMDIGQPRDYITGLRLYLDSLRKKAPAKLASGAHVLGNVLVHETAVIGEGCLIGPDVAVGPGCVVEAGVRLSRCTVMRGARVKKHACISSSIIGWHSTVGMWARVENMTILGEDVHVCDEVYSNGGVVLPHKEIKSSILKPEIVM", "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": "MGILFTRIWRLFNHQEHKVIIVGLDNAGKTTILYQFSMNEVVHTSPTIGSNVEEIVINNTRFLMWDIGGQESLRSSWNTYYTNTEFVIVVVDSTDRERISVTREELYKMLAHEDLRKAGLLIFANKQDVKECMTVAEISQFLKLTSIKDHQWHIQACCALTGEGLCQGLEWMMSRLKIR", "text": "FUNCTION: Lacks ADP-ribosylation enhancing activity. SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
+{"protein": "MVKDILAPGLRVVFCGINPGLSSANTGFPFAHPANRFWKVIHLAGFSDRQLKPEEAEKLLDFRCGVTKLVDRPTVQATEVKLHELRSGGRNLIDKIEDYQPAALAVLGKQAFEQGFSQRGIAWGKQKIAIGATMVWVLPNPSGLNRIKTEKLVEAYRELDQALIMRGL", "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": "MRPRPIRLLLTALVGAGLAFAPVSAVAAPTATASASADVGALDGCYTWSGTLSEGSSGEAVRQLQIRVAGYPGTGAQLAIDGQFGPATKAAVQRFQSAYGLAADGIAGPATFNKIYQLQDDDCTPVNFTYAELNRCNSDWSGGKVSAATARANALVTMWKLQAMRHAMGDKPITVNGGFRSVTCNSNVGGASNSRHMYGHAADLGAGSQGFCALAQAARNHGFTEILGPGYPGHNDHTHVAGGDGRFWSAPSCGI", "text": "FUNCTION: This enzyme catalyzes carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism. It effectively catalyzes the transfer of the N-alpha, N-epsilon-diacetyl-L-lysyl-D- alanyl electrophilic group of the standard tripeptide substrate N- alpha,N-epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolyzing penicillin into penicilloate at a very low rate. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M15 family."}
+{"protein": "MKMTSKKMKDELMKRLSRPEWDFQYDSEKEVLRIEQKDSKKGINVSLPGVVAKWEVNKEKAIEEVAYYVQEALIAMHKEENSAAKILPVIRSTSFPKQAEEGNPFIMTDHTAETRIYYALDSNKTYRLIDERLLQKLGLTEQQVREMALFNARSLSYEFKQDTVAGNTFYFLNTNDGYDATRILNESLLQSMREKISGDMVVAVPHQDVLIIADIVNEIGYDIIAQMTMKFFAEGHVPITSLSFVYEDGDFEPIFILAKNRKKTDGKEKG", "text": "SIMILARITY: Belongs to the UPF0354 family."}
+{"protein": "MTDERGNFYYNTPPPPLRYPSNPATAIFTNAQTYNNAPGYVPPATRDNKMDTSRSNSTNSVAIAPYNKSKEPTLDAGESIWYNKCVDFVQKIIRYYRCNDMSELSPLMIHFINTIRDMCIDTNPINVNVVKRFESEETMIRHLIRLQKELGQGNAAESLPSDSNIFQASFVLNSLPAYAQKFYNGGADMLGKDALAEAAKQLSLAVQYMVAESVTCNIPIPLPFNQQLANNYMTLLLKHATLPPNIQSAVESRRFPHINMINDLINAVIDDLFAGGGDYYYYVLNEKNRARIMSLKENVAFLAPLSASANIFNYMAELATRAGKQPSMFQNATFLTSAPTRSIRLPLI", "text": "SIMILARITY: Belongs to the baculoviridae gp41 family."}
+{"protein": "MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRHHPMASWLCAMLHCFGSYILADLLLGEPVIDYFSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFVMIATGWVKGSGVTLMSNLEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVLEAYICPVLFGSASGGDHHHNNHGGSQGGSGPGSPHSPLPSKSKEELSEGSRKKKTKKAD", "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": "MSSTAHPTNLAPSGNGSAACVHCHRRKVRCDARLVGLPCSNCRSAGKTDCQIHEKKKKLAVRSILDPVPIRCRPPNPEEAPKPISSLSPSSEPPNAFTTALRAVQSDITAPSGVANRVAHIRSRSSQYDTKGTRSNNNSGNNTQYQNVLPEPDSPPYSRPAASDPSEGESRADIEKRLVNLIDGEASDSRAIQRGVRAIYVGHELSNMSFLIRQQRDTGDDVYHFAGNEIPRRQLRTGHDQLLMDALTLPEPALADELVHAYFAQVNPGYPIVEEELFMSQYRNRDPADAPPILLLQTILLVGAHVTRPKSERDTLKDIFFRRAKWLFDNRIERNRDILVQAALLLTWHSDLADDDVSANAHYWIGIAARIATGLGMHRNPVCSRFVPRDRRMWRRLWYILVQFDVMVSLSYGRPQALNLEDSDVSPLTFSDFEGCGARVQADFVIHFSELCTMISYIVRERFGLRISAERRKAALLEADEALANWSLRLPDRLRLRASDMDPWSAMLHLTYNNFLILLHRPHPRASAYSDDYGPHDAEICSAAAGVIASIFEELRIHDRLKQVWYSGVHTLFTAMIQVRVELRFSNPVLAINALRRFDSASYSLRELAQYWSHASTILRLFEESRRLQEDLRTTTSDRPRRFSNLSNNSTNSPASQQKNTSGIPHLANINSSDATPPSAPSIPPLQPSSQLSYEVPTTESAHHNPRSQPTLSAHTHTYTTQPFDTWIPSNNLTPMDTVDNSREMLDWRQLFSFTDLEGPVLPSTMEGITELEDEWRQIYWQETPMSDLLQDGGWMHG", "text": "FUNCTION: Positively regulates the expression of 5 genes involved in the catabolism of certain amides (amdS), omega amino acids (gatA and gabA), and lactams (lamA and lamB) in the presence of omega amino acid inducers. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MDAAEKKEVIKKKYQEIATLGGSCCSGGGCCGDLSAADLSRSLGYSEADVQAVPDANLGLGCGNPTAFAELKPGDIVLDLGSGAGFDSFLAAQRVGSLGKVIGVDMTQEMVKKAQDNARKYGYSNVEFRQGDIEALPLDDRSVDVIISNCVINLAPDKEKVFREAFRVLKPGGRMYVSDMVLLEDLPEDLKNDCDLLAGCVAGALLKEEYLGLLKKAGFSFKILAEDSDVSKRQYEGLPVESLKLKAWV", "text": "FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to arsenite, producing methylated arsenicals. Involved in the conversion of As(III) to a number of methylated products. Reduces the arsenic toxicity in the cell and may contribute to the global arsenic cycling. SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite methyltransferase family."}
+{"protein": "MSRRALRRLRGEQRGQEPLGPGALHFDLRDDDDAEEEGPKRELGVRRPGGAGKEGVRVNNRFELINIDDLEDDPVVNGERSGCALTDAVAPGNKGRGQRGNTESKTDGDDTETVPSEQSHASGKLRKKKKKQKNKKSSTGEASENGLEDIDRILERIEDSTGLNRPGPAPLSSRKHVLYVEHRHLNPDTELKRYFGARAILGEQRPRQRQRVYPKCTWLTTPKSTWPRYSKPGLSMRLLESKKGLSFFAFEHSEEYQQAQHKFLVAVESMEPNNIVVLLQTSPYHVDSLLQLSDACRFQEDQEMARDLVERALYSMECAFHPLFSLTSGACRLDYRRPENRSFYLALYKQMSFLEKRGCPRTALEYCKLILSLEPDEDPLCMLLLIDHLALRARNYEYLIRLFQEWEAHRNLSQLPNFAFSVPLAYFLLSQQTDLPECEQSSARQKASLLIQQALTMFPGVLLPLLESCSVRPDASVSSHRFFGPNAEISQPPALSQLVNLYLGRSHFLWKEPATMSWLEENVHEVLQAVDAGDPAVEACENRRKVLYQRAPRNIHRHVILSEIKEAVAALPPDVTTQSVMGFDPLPPSDTIYSYVRPERLSPISHGNTIALFFRSLLPNYTMEGERPEEGVAGGLNRNQGLNRLMLAVRDMMANFHLNDLEAPHEDDAEGEGEWD", "text": "FUNCTION: Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:30244831). In the RQC complex, required to promote formation of 'Lys-48'-linked polyubiquitin chains during ubiquitination of incompletely synthesized proteins by LTN1 (PubMed:30244831). Also acts as a transcriptional repressor: represses transcription of SRF in vitro and so may play a role in heart development (PubMed:16574069). May play a role in cell death control (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Mainly nuclear. SIMILARITY: Belongs to the TCF25 family."}
+{"protein": "MALQRTHSLLLLLLLTLLGLGLVQPSYGQDGMYQRFLRQHVHPEETGGSDRYCNLMMQRRKMTLYHCKRFNTFIHEDIWNIRSICSTTNIQCKNGKMNCHEGVVKVTDCRDTGSSRAPNCRYRAMASTRRVVIACEGNPQVPVHFDG", "text": "FUNCTION: This RNase has marked specificity towards the 3' side of uridine nucleotides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pancreatic ribonuclease family."}
+{"protein": "SLGGFLKGVGKVLAGVGKVVADQFGNLLEAGQ", "text": "FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermatoxin subfamily."}
+{"protein": "MLKPPLPLRSLLFLQLSLLGVGLNSTVPMPNGNEDITPDFFLTATPSETLSVSSLPLPEVQCFVFNVEYMNCTWNSSSEPRPTNLTLHYWYKNSNDDKVQECGHYLFSREVTAGCWLQKEEIHLYETFVVQLRDPREPRRQSTQKLKLQNLVIPWAPENLTLHNLSESQLELSWSNRHLDHCLEHVVQYRSDWDRSWTEQSVDHRNSFSLPSVDGQKFYTFRVRSRYNPLCGSAQRWSEWSHPIHWGSNTSKENPLFASEAVLIPLGSMGLIISLICVYYWLERSIPRIPTLKNLEDLVTEYHGNFSAWSGVSKGLAESLQPDYSEWLCHVSEIPPKGGAPGEGPGGSPCSQHSPYWAPPCYTLKPETGALIP", "text": "FUNCTION: Common subunit for the receptors for a variety of interleukins. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell surface. SIMILARITY: Belongs to the type I cytokine receptor family. Type 5 subfamily."}
+{"protein": "MLLSAIASQTLLSSNPNLHFSNSIPNPRPSNPSLKLLNASSSSSSSSSSSIFTRGLRYVNHTVSNEESEPGGGETMVASASAIASAIRGASTTPVEFTQMIEKDHLKTKIILPSPDFQRLCLEQLDLFRQIVDPNAVLSIYVRPAGSYVMDRLELRRVTCYPSVNAGDVVILVGNFGIPAGLRAAEASLSSQQVELVSKHRAAVFPMVKHPFVVGFLVAELPVEAEEEEEEEEEEKPHGVNQFLSPEEAYALPASANTKSPRVKLPSVKVFTEEQRSYAINISRTLAMAYVMDQKTMLLQQSSWQNNVRMSKLVEQIRGPLSTMRTLSKMLSTHTKRNQISHDIVEDLIVQGDQIKDTLEELQDAVHLTKANIVRHNEEALKKINKTHNETRRSKYEHKDPIDGSQISSTRLSLGSGLDDSEMPMPPLALAPLQMHSIRPCDISNVLLDMVETVRPLALTQQRVVELGENSASLQVAVEEPALRQALSNLIEGALLRTHVGGKVEILSTRAPAGGSLVVIDDDGPDMRYMTQMHSLTPFGAELLSENMVEDNMTWNFVAGLTVAREILESYGCVIRVISPRSSDAALGAGGTRVELWLPAFPAAVSEANEA", "text": "FUNCTION: Sensor kinase that senses the plastoquinone (PQ) redox state involved in stoichiometry adjustment of both photosystems (e.g. long- term adaptation via transcriptional regulation of reaction center genes of photosystems I and II) and state transitions (e.g. short-term adaptation involving reversible post-translational phosphorylation of light-harvesting complex II, LHC II), thus linking photosynthesis with gene expression in chloroplasts (PubMed:18632566, PubMed:22039472). Autophosphorylates, probably on a tyrosine residue (PubMed:18632566). Probably phosphorylates SIGA/SIG1 in response to plastoquinone redox state modification (PubMed:23754813). Reduced PQ suppresses its autophosphorylation activity. Represses expression of a number of chloroplast-encoded genes (PubMed:31925322). SUBCELLULAR LOCATION: Plastid, chloroplast stroma Note=Associates with thylakoid membranes. SIMILARITY: Belongs to the chloroplast sensor kinase protein family."}
+{"protein": "MLSDEEREAFRQQAAAQQMSLSNWLRQAGLRQLEAQRQRPLRTAQELREFFASRPDETGAEPDWQAHLQVMAESRRRGLPAP", "text": "FUNCTION: Putative antitoxin component of a possible type II toxin- antitoxin (TA) system. The cognate toxin is VapC23."}
+{"protein": "MMQKLQMYVYIYLFMLIAAGPVDLNEGSEREENVEKEGLCNACAWRQNTRYSRIEAIKIQILSKLRLETAPNISKDAIRQLLPRAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQADGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMSPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS", "text": "FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
+{"protein": "MGKTLSEIAQQLSTPQKVKKTVHKEVEATRAVPKVQLIYAFNGTGKTRLSRDFKQLLESKVHDGEGEDEAEQSALSRKKILYYNAFTEDLFYWDNDLQEDAEPKLKVQPNSYTNWLLTLLKDLGQDSNIVRYFQRYANDKLTPHFNPDFTEITFSMERGNDERSAHIKLSKGEESNFIWSVFYTLLDQVVTILNVADPDARETHAFDQLKYVFIDDPVSSLDDNHLIELAVNLAGLIKSSESDLKFIITTHSPIFYNVLFNELNGKVCYMLESFEDGTFALTEKYGDSNKSFSYHLHLKQTIEQAIADNNVERYHFTLLRNLYEKTASFLGYPKWSELLPDDKQLYLSRIINFTSHSTLSNEAVAEPTPAEKATVKLLLDHLKNNCGFWQQEQKNG", "text": "FUNCTION: Anticodon endonuclease (ACNase) that triggers the cleavage ligation of tRNA(Lys). It is activated by T4 stp protein and masked by the prrD protein (the endonuclease subunit of EcoprrI) (PubMed:1691706). The prr locus restricts phage T4 mutants lacking polynucleotide kinase or RNA ligase; T4 mutants lacking these genes manifest a T4-induced anticodon nuclease (ACNase). It is thought that Stp and other T4-encoded ACNase factors counteract the masking agents, thus activating the latent ACNase (Probable)."}
+{"protein": "MGAIISAIAGLFELGALGGLAVDAAVNTAEIEAFIGELVLQDFSVAEIFDAIETSGIPLANTAVPVAELQQTAATSGLIGQALSAPSLIAASVKAFAGDPVAAGNNMALQVWRDQMDILFPGAEWFSNAVHNINPLAWAQSLYEQVGQSIWNYMTGNIGQAVIHQIEERTTALIVYQSRGIYDILARALETARWTLTTAAVDTYQTLKSYYGELPAVSGRVEAFRRYHEVAQGRSFFEDSDIQDVLEGKKAQKRIEGPQEMTGQTIEQQTPPGGAMQRHANDWLLPLILGLYGDLTPEWRYQLKERLNVPKRKRKLPTTSAGTSPPSKRRYRGVRRKVRSR", "text": "FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C- terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane. SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family."}
+{"protein": "MSRKMFSCDFETTTKLDDCRVWAYGYMEIGNLDNYKIGNSLDEFMQWVMEIQADLYFHNLKFDGAFIVNWLEQHGFKWSNEGLPNTYNTIISKMGQWYMIDICFGYRGKRKLHTVIYDSLKKLPFPVKKIAKDFQLPLLKGDIDYHTERPVGHEITPEEYEYIKNDIEIIARALDIQFKQGLDRMTAGSDSLKGFKDILSTKKFNKVFPKLSLPMDKEIRKAYRGGFTWLNDKYKEKEIGEGMVFDVNSLYPSQMYSRPLPYGAPIVFQGKYEKDEQYPLYIQRIRFEFELKEGYIPTIQIKKNPFFKGNEYLKNSGVEPVELYLTNVDLELIQEHYELYNVEYIDGFKFREKTGLFKDFIDKWTYVKTHEEGAKKQLAKLMLNSLYGKFASNPDVTGKVPYLKDDGSLGFRVGDEEYKDPVYTPMGVFITAWARFTTITAAQACYDRIIYCDTDSIHLTGTEVPEIIKDIVDPKKLGYWAHESTFKRAKYLRQKTYIQDIYVKEVDGKLKECSPDEATTTKFSVKCAGMTDTIKKKVTFDNFAVGFSSMGKPKPVQVNGGVVLVDSVFTIK", "text": "FUNCTION: Polymerase responsible for protein-primed viral DNA replication by strand displacement with high processivity and fidelity (By similarity). To start replication, the DNA polymerase forms a heterodimer with a free primer terminal protein (TP), recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP (PubMed:23110220). This polymerase possesses three enzymatic activities: DNA synthesis (polymerase), primer terminal protein (TP) deoxynucleotidylation, which is the formation of a covalent linkage (phosphoester) between the hydroxyl group of a specific serine residue in TP and 5'-dAMP, a reaction directed by the third T at the 3' end, and 3' to 5' exonuclease activity (PubMed:23110220, PubMed:19011105). Exonuclease activity has a proofreading purpose (By similarity). Since the polymerase initiates the replication on the third thymine, the TP- dAMP initiation product translocates backwards to recover the template information of the 2 terminal nucleotide (sliding back-mechanism) (PubMed:23110220, PubMed:19011105). SIMILARITY: Belongs to the DNA polymerase type-B family."}
+{"protein": "MFTLKKSLLLLFFIGVIKLSLCEEERNADDDERRDDPDEMDVEVENRSAVGRHGRRFGLRKHRKH", "text": "FUNCTION: Antimicrobial peptide. Has activity against the Gram-positive bacterium S.aureus (MIC=6 uM) and the Gram-negative bacterium E.coli (MIC=3 uM). Lacks hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
+{"protein": "MGKKSLAEQIADIANKPQVEDFDIENDEGVFQHGGSDSDVSSGDESEEELKKQHYVAVGKSKLRNVVDQGLAVKDKKYVGSKGSRAELFNDEEMDAPEQGESESEAESGSEESDAVSFRSDSEDVSESEATSESEIEKDREEDEETAMKKEKLAKIVQTQTKQVINNLAHSAQRDASKGYAILQQNKFFDKILDSRIKLQKALSASNQLPLSQQSWDELLDENNSKLLTSTFKVLEKVLTQCVTVRHKFQIGDHINQSENPSDFDNSKKRSFKELVHETVTLDSDLKSYRSAVLNKWSAKVSASSGKSLLQASKFKAINQSADVQVDNQLADMPRLLKRTKLNRSNTKPLLFDEDLQKGLLKELQLEENVEGDIEEENNLDIPKNYDPRRKDNNALDFTQNPYIYDDEDFYRVLLNDLVEKKISNSQQSNGVTLAITSRSENKLKKNIDTKASKGRKLNYSIQEPIANYEASVNTGYKWSDEQIDEFFAGLLGQKINFNEDDELEADTMHNEEDEEIKNDDIQIFG", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the AATF family."}
+{"protein": "MAPSGGQEAQICDSETFGDSDFVVVANRLPVDLERLPDGSTTWKRSPGGLVTALEPVLRRRRGAWVGWPGVNDDGAEPDLHVLDGPIIQDELELHPVRLSTTDIAQYYEGFSNATLWPLYHDVIVKPLYHREWWDRYVDVNQRFAEAASRAAAHGATVWVQDYQLQLVPKMLRMLRPDLTIGFFLHIPFPPVELFMQMPWRTEIIQGLLGADLVGFHLPGGAQNFLILSRRLVGTDTSRGTVGVRSRFGAAVLGSRTIRVGAFPISVDSGALDHAARDRNIRRRAREIRTELGNPRKILLGVDRLDYTKGIDVRLKAFSELLAEGRVKRDDTVVVQLATPSRERVESYQTLRNDIERQVGHINGEYGEVGHPVVHYLHRPAPRDELIAFFVASDVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELRHAYLVNPHDLEGVKDGIEEALNQTEEAGRRRMRSLRRQVLAHDVDRWAQSFLDALAGAHPRGQG", "text": "FUNCTION: Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1- phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose (PubMed:12473104, PubMed:27513637). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to D-glucose 6- phosphate (Glc-6-P) to form trehalose-6-phosphate (PubMed:12473104). Is specific for the glucosyl acceptor (Glc-6-P cannot be replaced by either mannose-6-P, fructose-6-P or glucosamine-6-P), but any of the glucose sugar nucleotides can be used as glucosyl donors (PubMed:12473104). It is more active with the purine sugar nucleotides than with the pyrimidine sugar nucleotides (PubMed:12473104). FUNCTION: Probably involved in the osmoprotection via the biosynthesis of trehalose and in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Probably also able to use ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc as glucosyl donors. SIMILARITY: Belongs to the glycosyltransferase 20 family. SIMILARITY: Belongs to the glycosyltransferase 20 family."}
+{"protein": "MSSDKIFAEGESCKSAWHDATAGYDETDTHLEIMGKPVMERWETPYMHSLATVAASKGGRVLEIGFGMAIAATKLEEYNIEEHWIIECNDGVFKRLQEWATKQPHKIVPLKGLWEEVVPTLPDGHFDGILYDTYPLSEETWHTHQFNFIKSHAYRLLKPGGVLTYCNLTSWGELLKTKYNDIEKMFKETQTPQLVDAGFKSENISTTVMDLVPPEDCRYYSFKKMITPTITKV", "text": "SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family."}
+{"protein": "MYSLEISLRYSPFPLSIQKKEYEDIKRIYDEIKDSMNSDNQNSPLIELSCEKVQDKLITVLAKEVISVQIYEKSAVAGGSKRPGFSLDI", "text": "SIMILARITY: Belongs to the UPF0367 family."}
+{"protein": "ATFDIQNKXTYTVWAAAWAPSYPGGXKQLD", "text": "FUNCTION: Has antifungal activity against P.infestans."}
+{"protein": "MDKENAADAQPATGQTHNDLFDYDVDLDAILGESSTRSNINAPQTSESRGLGLGLDDEVKVTRKRQPIAKLDEGRLLSQAGIPKLRRSAKQKLKFKGKGHEFSDAARLLNFYQLWLDDLFPRAKFTDGLAMIEKLGHSKRIQTMRREWIDQEKPRQRDDDDEPLQEAEGSHHNETSNAADQPSDRQSNSRQSPHPNDDSNDLFMSDEGNPQYVVDRPEAPEEDDLEALLREQEDEVVDKPDGPEEDDLDALLREQADVAVPQQKTSTAPSMDEDRLRVPVDHLYDCDVTHIRNVIVPSNMME", "text": "FUNCTION: Forms a fork protection complex (FPC) with tof1 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CSM3 family."}
+{"protein": "MEQSVSARWLRRYRPVLIILVLIFGIQLFLAYKSVDIGGGSGSGLDVDAAQRSQRDLASNPVIAEPPESLPRPARLTANQLGFQPECDIQAKEAISALQRAKTKDCRQHIAQIACSIQAGRFYAIQLKSSCPSGNHTANVSLGCYRDEKDRRLLGGYYTSFKNSNSPNLCLELCLQSGYPYAGVQYGRECFCGFDTPPKAAKLPDSSCNIKCLGNAREICGGFYAMNIYETGIAKFTAQLAASTPPTGAKRVRIAFLLTINGRALRQVHRLLKALYAPEHVYYIHVDERQDYLYRKLLELEQKFPNIRLARKRFSTIWGGASLLTMLLQCMEDLLKSKWQWDFVINLSESDFPVKTLDKLVDFLSANRGRNFVKGHGRETQKFIQKQGLDRTFVECDTHMWRIGDRKLPAGIQVDGGSDWVALSRPFVAYVTHPKKEDELLQALLKLFRHTLLPAESFFHTVLRNTHHCHTYVDNNLHVTNWKRKQGCKCQYKHVVDWCGCSPNDFMPDDWPRLLATEQKSLFFARKFEPIINQAVLLQLEEWLYGPYTSEYLNLHGYWQSLYHHEDVHGSADDLVRSVGDSLMRLAGSQARVDPLELLELTHYLHRDQYKGFLVRFSARRATGQDVQLETRVRPVQHGKLARNARFSKRLRNFEVSTDFDQKEQVARNFGKLLGPQSDLVLSYTYQGSTDSGAASHSYNLTLLWIDPLGRLQDFNELHVEDSSTDLINHSKTLLSHPITPGVWTAKLIGRSSIYAQLKFLISPMAYGNGEPLETTPEAEKRNGGLGIALPDDFELPVEWQQHLHTDDEQFSLREEALANGKLTGPPLHRWIDDLVGKFFQLRESCVVDAGTELSLPLCSDAPWSSLAPDPKSDVDALLK", "text": "FUNCTION: Catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes. 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 14 family. XylT subfamily."}
+{"protein": "MWVLVVFLTLSVTWIGAAPLILSRIVGGWECEKHSQPWQVLVASHGRAVCGGVLVHPQWVLTAAHCIRSHSVILLGRHNPYYPEDTGQVFQVSHSFPHPLYNMSLLKNRYLGPGDDSSHDLMLLRLSEPAEITDAVQVLDLPTWEPELGTTCYASGWGSIEPEEHLTPKKLQCVDLHIISNDVCAQVHSQKVTKFMLCAGSWMGGKSTCSGDSGGPLVCDGVLQGITSWGSQPCALPRRPSLYTKVVRYRKWIQDTIMANP", "text": "FUNCTION: Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily."}
+{"protein": "MGFYNSGGYSGNSGYSNGFGSSFALIVVLFILLIIVGAAIFNY", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SscA family."}
+{"protein": "MAATDVDIFSNEEKRNLSLGGHVGFDSLPDQLVSKSVTQGFCFNILCVGETGIGKSTLMNTLFNTMFENEEASHYQNGVYLRPRTYDLQESNVHLKLTIVDTVGFGDQINKEESYKPIVDYIDTQFENYLQEELKVKRSLFNYHDTRIHICLYFISPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTISKSELHKFKIKIMSELVSNGVQIYQFPTDDEAVTEINSSMNAHLPFAVVGSVEEVKVGNKTVRARQYPWGVVQVENESHCDFVKLREMLIRVNMEDLREQTHARHYELYRRCKLEEMGFKDTDPDSQPFSLQETYEAKRKEFLGDLQKKEEEMRQMFVNKVKETEAELKEKERELHEKFEQLKRMHQEEKRKVEEKRRELEEEMNAFNRRKVAAETLSLSQPLKKDKDKKN", "text": "SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
+{"protein": "MSASTKRKRDQAEESVPAENPASTDVEKAIKPAQKQEEETSFVDLGLDPRLLQAIAQQKFAKPTLVQRKAIPLALNGQDVLAKADCGSGKTAAYVLPLLSSILKRKATDSTAFTTALILVPTRELADQVSKAIEQFASFCAKDISTAKLTDKVSSKVQRALLSNSPDIVISTPSTAWQNVNSSALSIDKLTHLILDEADLVLSYGYSEDLENLSRSVPKGVQVMMMSATLSDEVDTLKGIFRRDPTLLDLKEKEAEGEGITQFVAKCGEDEKFLLAYVIFKLKLIKGKCIIFVSDIDRCYRLKLFFEQFGIRSCILNSELPLNSRVHVVEEFNRHVYDIIIAADEKNEMLGDDEEPAETAEAQDDAKKSNEGDDAETEAKRPKKKAKKSKGGDKEYGVSRGVDFKKVSAVINFDLPTTASAYTHRIGRTARAGQTGMALSFVVPKDLYRKHMPTSTPACENDEKIMARIIRQQAKRDKEVKPYNFNMKQVDPFRYRMNDALRAVTKVAIREARTRELRQELLKSEKLKRYFEENPTELSHLRHDGELRTARQQAHLKHIPEYLMPKDGKQALTEDVGFVAMRKDKKGKGKKGRGFKVGSRKRDPLKTFKARRKTK", "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. DDX56/DBP9 subfamily."}
+{"protein": "MAQASGMDPLVDIEDERPKWDNKLQYLLSCIGFAVGLGNIWRFPYLCQTHGGGAFLIPYFIALVFEGIPLFYIELAIGQRLRRGSIGVWKTISPYLGGVGLGCFSVSFLVSLYYNTVLLWVLWFFLNSFQHPLPWSTCPLDLNRTGFVQECQSSGTVSYFWYRQTLNITSDISNTGTIQWKLFLCLVACWSTVYLCVIRGIESTGKVIYFTALFPYLVLTIFLIRGLTLPGATEGLIYLFTPNMKTLQNPRVWLDAATQIFFSLSLAFGGHIAFASYNPPRNNCEKDAVIIALVNSMTSLYASIAIFSVMGFKASNDYGRCLDRNILSLINEFDLPELSISRDEYPSVLMYLNATQTARVAQLPLKTCHLEDFLDKSASGPGLAFIVFTEAVLHMPGASVWSVLFFGMLFTLGLSSMFGNMEGVITPLLDMGILPKGIPKEVMTGVICFACFLSAICFTLQSGGYWLEIFDSFAASLNLIIFAFMEVVGVIHIYGMKRFCDDIEWMTGRRPGLYWQVTWRVVSPMLLFGIFLSYIVLLIQTPPSYKAWNPQYEHFPSREEKFYPGWVQVTCVLLSFLPSLWVPGVALAQLLSQYKQRWKATHLESGLKLQESRGC", "text": "FUNCTION: Symporter that transports one amino acid molecule together with two sodium and one chloride ions in kidneys and plays a role in the neutral amino acids reabsorption (PubMed:19478081, PubMed:26240152, PubMed:20377526). Preferentially transports neutral amino acids such as L-glycine and L-alanine but also other neutral amino acids (PubMed:19478081, PubMed:26240152, PubMed:20377526). Required CLTRN for cell surface expression and for its amino acid transporter activity (PubMed:26240152, PubMed:20377526). The transport mechanism is pH- independent (PubMed:19478081). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=In kidneys localizes to the apical membrane in distal segments of the proximal tubule (PubMed:19478081, PubMed:20377526). Cell membrane expression is CLTRN-dependent (PubMed:20377526). SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family. SLC6A18 subfamily."}
+{"protein": "MGQCLGLVQIDQSTVAIKENFGKFSEVLEPGCHFLPWCIGQQIAGYLSLRVKQLDVRCETKTKDNVFVTVVASVQYRALADKASDAFYKLSNTREQIQSYVFDVIRATVPKLNLDDAFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIIDIEPDVHVKRAMNEINAAARLRVAANEKAEAEKILQIKKAEGEAESKYLAGVGIARQRQAIVDGLRDSVLAFSENVPGTTAKDIMDMVLVTQYFDTMKEIGASSKSTSVFIPHGPGAVKDVAAQIRDGLLQANAERND", "text": "FUNCTION: Positive regulator of hypersensitive response (HR)-like cell death. May be involved in potassium ion channel regulation."}
+{"protein": "MAHKQIYYSDKYFDEHYEYRHVMLPRELSKQVPKTHLMSEEEWRRLGVQQSLGWVHYMIHEPEPHILLFRRPLPKDQQK", "text": "FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. SIMILARITY: Belongs to the CKS family."}
+{"protein": "MRAPLLLPLLPLLLFGVSSGNNDKTTHSTTVSPETTKQITTITVTTSQVQGSISASKPSSTAPTAVMSFTKAQEAATSSKQHDSSTSSIPPPSTSITPSIITTSPQGKTPSTPALTHTPDQNTKTTGRQDDTSHVSVASTSASQQVSSSASAAVPTTTSAVTSSATQQKVSPTDSSEILLKPSASPNSTQVTSPSRTPKGFLSTVTTSPHIADNGSTALNQLKSTVSSSEVPVSSFLDKDHSVSSSTSATNQHLSLSSHRPTSPVPKFECSTPHSGSVPSTSSKTSLSSPSSSTKNATVTTTMTTAKAAYTSQGDGSVTHKSGVTAQSPTSAPLPTPTLKDHMKSKSPDQTHSNVSPPNEVICEDQIGEVRPILNLKEEKTCDDWKKASNEAFFEVFCSGRRHAFNSTRDRCTVKLASSNHRRWAVHVIVHRVLDPAAVFEELKEKRNELEKLGITNVTYLNQEMEEEIKDQSSTPLIITIVTLAGSLLLIAAIYGCCHQRFSQKKSQQRLTEELQTMENGYHDNPTLEVMETGSEMQEKKVNLNGELGDSWIVPLDTIMKEDLEEEDTHL", "text": "FUNCTION: Involved in the regulation of both adhesion and cell morphology and cancer progression. Functions as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro- adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Involved in the formation of a preapical plasma membrane subdomain to set up initial epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells (By similarity). Induces the formation of apical actin-dependent microvilli. SUBCELLULAR LOCATION: Apical cell membrane Cell projection, microvillus Membrane raft Cell projection, lamellipodium Cell projection, filopodium Cell projection, ruffle Membrane; Single- pass type I membrane protein Note=In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with NHERF2 at the apical plasma membrane during epithelial polarization. Colocalizes with NHERF1 at the trans-Golgi network (transiently). Its association with the membrane raft is transient. Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with actin filaments, ezrin and NHERF1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with EZR and NHERF2 at the apical cell membrane of glomerular epithelium cells (By similarity). Colocalizes with NHERF1 at the apical cell membrane. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis (By similarity). SIMILARITY: Belongs to the podocalyxin family."}
+{"protein": "MSQAAKNVIVKLIVGAGQAAPSPPVGPALGSKGIKAIDFCKEFNARSANYQPGVPVPVLITIKPDRTFTFEMKSPPTGYLLLKALKMDKGHGQPNVGTMLGSAPAKGPTRALGELSLKHVYEIAKIKKSDERHSLLEMEGIVKSIVGVAKSMGIKVVP", "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 uL11 family."}
+{"protein": "MQMDWLFIAVISGIGLLSSGVPGTQGAYTTEQCRALNGSCNFYACFPKNVIIGKCDWWGWSCCARTPLERCTAKKGTCTKTGCTKTDTDHGPCDGGAQCCQRDPVKYCKFHGNVCGRGKCPMDHIPIGECTPGYPCCKRDGPAYCKSKGGKCLNRCPQIVPTNVIGVCATGVPCCKSRQSTG", "text": "FUNCTION: Lethal toxin which possesses an inhibitory effect on direct electrical stimulation of the isolated hemi-diaphragm of mice. Neither hemorrhagic nor hemolytic activities are detected. Phospholipase A2 activity, proteolytic activity and arginine esterolytic activity are absent (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family. Helofensin subfamily."}
+{"protein": "MDFRRQTLVSNGGSSQPQPSVPSSAIKKASRLGPARQSLAPSQIQSRTSILGVSNSQENASHGMMGSRKSTVPGKMGDRDQLMSASRGDGGIYGRTPQMNRGIPGSVRRSSVFTSNSQGRTSMAPGVYSTAYKDPRPLRDKVFQSNCMRNVNEYLISVRYPLPLTAKTLTSPTAKEFQSIFKFLVNDLVDPGAAWGKKFEDDTLSILKDLKYPGMDSVSKTALTAPGAPQSWPNMLAMLNWLVDLCKALDNWDDPEIISDPLMVPATELPLDYPNLDDRLLWDFAAKTYSQWFDGEAEEFDEAEQELEHAYGKSYSIVLNDTEQATDRMASATVAECEKLEREIQKRNVEIQQLHVQEVCSPITDRISFADKSYKPPLKKLEDEYVQLMSDKNKFISFLDQQGQKIEKIRLRISKVKEAVISQEAELEARQSELAHIEQAVAAQNLSPDEVQRMNHERDSLTRSLEDLRNKISEASQFAYDQEMVVTKSMDRFEGLLTDYNSLAHQIGLLDFSLDVPSLAANVNYNLDVDLGAEELEEVKAVGVRMRSTIWQALQTCREMFRQEALGLGNGTIALEDEFDKLGQSVERQKEEVGNLEVRLKIVHNQAEDAQSQIASENSDTNKIITQLETEVTNMLAASQQGVLSTQSQLESTRIAFKELRHKTALFQDSVVAEVGEHIDAIIKAKEHTANSLKSIRALAETQ", "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": "MKIYFLLGTFLTFLLHTRICQGIKWLALSKTPLSLPLNQTQHCKQLEGLVSSQMQLCRSNLELMQTIIHAAKEVKKTCVKAFTDMRWNCSSIELAPTFHQDLERGTRESAFVHALSAAAISHTIARACTTGDIPGCSCAPIPGESPGPGYRWGGCADNLNYGILMGSKFSDAPMKMKKSGSQANKLMHLHNSEVGRQVLKASLEMKCKCHGVSGSCSIKTCWRGLQELREIALDLKTKYLSATKVVHRPMGTRKHLVPKDIDIRPVQETELIYLQSSPDYCLKNEKIGSHGTHERQCNKTSNGSDSCDLMCCGRGYNPYMDKVVERCLCKYHWCCYVTCKKCERTVERYVCK", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Shares much functionality with wnt11b. Signals through a non-canonical Wnt pathway to activate Jun-N- terminal kinase (JNK) to regulate gastrulation movements. Acts in a non-cell-autonomous manner to control neural crest migration, probably acting as an extracellular signal from surrounding tissue, but is not required for neural crest induction. Acts redundantly with wnt11b during pronephros induction. Regulates cardiac morphogenesis through the activation of JNK, but is not required for cardiac differentiation. Essential for dorsal fin development; required for an epithelial to mesenchymal transformation event prior to migration of cells into the fin, and ultimately for maintenance of fin structure. Mediates dorsal fin development through a non-canonical pathway mediated by Ca(2+). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MLLDAGAQYPAIGVTTFGSSRHHSAGDVTDREVALGINPFADGMGAFKLNPSSHDLASGQTAFTSQAPGYAAAALGHHHHPGHVSSYSSAAFNSTRDFLFRNRGFGEAASAQHSLFASAAGGFPGPHGPHADTTGHLIFPGLHEQAASHASPNVVNGQMRLGFSGDMYGRPDQYGQVTSPRSEHYASSQLHGYGPMNMNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLANPKKSCNKTFSTMHELVTHVTVEHVGGPEQSNHICVWEECPREGKPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHEASSQGSQPSPAASSGYESSTPPTIVSPSAENQSTSSLSPSSSAVHHTSNHSTLSSNFNEWYV", "text": "FUNCTION: Transcriptional activator that induces expression of multiple genes including pax3, en2, snai2/slug, feb and a subset of wnt genes. Has multiple key roles in the regulation of neural induction and neurogenesis: acts as a neural competence factor, sensitizing the presumptive neuroectoderm to respond to subsequent neuralizing signals. Promotes both preplacodal cell fates and neural crest cell fates, two of the cell populations that arise from the neural plate border. Cooperates with pax3 in concert with wnt signaling to determine neural crest fate. Synergizes with the bmp-inhibitor noggin/nog and acts through the wnt pathway to induce expression of en2. May bind to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family."}
+{"protein": "MLSEGYLSGLAYRNDIQWSYPSSNEQVAEEKEEEMEATAAASLSYSSVDETQVQNLYVSCKSSGKVISSVYSRESQHSRNPRITVLQTNPNPVYESPNLAAVELYRDTSRETYLVPPSCKSICKNYNDLQIAGGQVMAINSATTDFPSEGSFQYGPLLKSSEIPLSMEDSMFTQPSDLPPTPIQRYSSYWRITSIKEKNSLQMQKPISNAVLNEYLEQKLVELYKQYFMDTGFHDSSPTQILASELIMTNVDQISIQVSIEKNLEISKARDIVINRLLQYGSTEISTQSLHISQYSNVNP", "text": "FUNCTION: Innate immune adapter that mediates the recruitment and activation of IRF5 downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9. Following recruitment to endolysosome by SLC15A4 downstream of TLR7, TLR8 and TLR9, specifically recruits IRF5 transcription factor via its pLxIS motif, leading to IRF5 activation and subsequent expression of type I interferons. Plays a role in the regulation of endolysosomal pH in immune cells such as B-cells, dendritic cells and monocytes. SUBCELLULAR LOCATION: Lysosome membrane Endosome membrane Nucleus Cytoplasm Note=Recruited to endolysosome following interaction with SLC15A4. May colocalize with TLR7 in the endosomal pathway."}
+{"protein": "MAAATTTTTTSSSISFSTKPSPSSSKSPLPISRFSLPFSLNPNKSSSSSRRRGIKSSSPSSISAVLNTTTNVTTTPSPTKPTKPETFISRFAPDQPRKGADILVEALERQGVETVFAYPGGASMEIHQALTRSSSIRNVLPRHEQGGVFAAEGYARSSGKPGICIATSGPGATNLVSGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRIIEEAFFLATSGRPGPVLVDVPKDIQQQLAIPNWEQAMRLPGYMSRMPKPPEDSHLEQIVRLISESKKPVLYVGGGCLNSSDELGRFVELTGIPVASTLMGLGSYPCDDELSLHMLGMHGTVYANYAVEHSDLLLAFGVRFDDRVTGKLEAFASRAKIVHIDIDSAEIGKNKTPHVSVCGDVKLALQGMNKVLENRAEELKLDFGVWRNELNVQKQKFPLSFKTFGEAIPPQYAIKVLDELTDGKAIISTGVGQHQMWAAQFYNYKKPRQWLSSGGLGAMGFGLPAAIGASVANPDAIVVDIDGDGSFIMNVQELATIRVENLPVKVLLLNNQHLGMVMQWEDRFYKANRAHTFLGDPAQEDEIFPNMLLFAAACGIPAARVTKKADLREAIQTMLDTPGPYLLDVICPHQEHVLPMIPSGGTFNDVITEGDGRIKY", "text": "FUNCTION: Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TPP enzyme family."}
+{"protein": "MDLRKHLGLLTLLLVAVFAFYGRPADACSCMPSHPQTHFAQADYVVQLRVLRKSDTIEPGRTTYKVHIKRTYKATSEARRMLRDGRLSTPQDDAMCGINLDLGKVYIVAGRMPTLNICSYYKEYTRMTITERHGFSGGYAKATNCTVTPCFGERCFKGRNYADTCKWSPFGKCETNYSACMPHKVQTVNGVISRCRWRRTQLYRKCMSNP", "text": "FUNCTION: Metalloproteinase inhibitor that acts on both matrix metalloproteinases Mmp1 and Mmp2 in vitro (PubMed:14567681). Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor (By similarity). Required for wing maturation which is the final step in morphogenesis of the adult fly (PubMed:16962574). Involved in the negative regulation of developmental tissue invasion for imaginal disk eversion during metamorphosis by inhibiting Mmp-mediated basement membrane (BM) degradation (PubMed:17301221). Required for oogenesis and for the long-term maintainance of germarial structure and shape in the adult ovaries. Required for maintaining composition and biophysical properties of the extracellular matrix (ECM), and for the normal organization and cyst production of the germline stem cell (GSC) niche (PubMed:26808525). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family."}
+{"protein": "MSDIAKDKAARLLKKRGSIISLGSHDVKPRGSFSKTKDSVSTVSYIDEPGHHDEIQSPAILMENTYQIGPAKRFPVASVNNILKDVLTSYLQEEKYEAELCRQMTKTISEVIKARVKDLMIPRYKIIVLIYIGQLNDQSMRVGSRCIWDPANDTFSSYSFKNSSLFALANVYGVYYE", "text": "SIMILARITY: Belongs to the dynein light chain Tctex-type family."}
+{"protein": "MERVSGLLSWTLSRVLWLSGFSEHGAAWQPRIMEEKALEVYDLIRTIRDPEKPNTLEELEVVTESCVEVQEINEDDYLVIIKFTPTVPHCSLATLIGLCLRVKLQRCLPFKHKLEIYISEGTHSTEEDINKQINDKERVAAAMENPNLREIVEQCVLEPD", "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 (PubMed:23891004). As a CIA complex component and in collaboration with CIAO1 specifically matures ACO1 and stabilizes IREB2 (PubMed:23891004). May play a role in chromosome segregation through establishment of sister chromatid cohesion. May induce apoptosis in collaboration with APAF1 (PubMed:25716227). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MIP18 family."}
+{"protein": "MRPARALIDLQALRHNYRLAREATGARALAVIKADAYGHGAVRCAEALAAEADGFAVACIEEGLELREAGIRQPILLLEGFFEASELELIVAHDFWCVVHCAWQLEAIERASLARPLNVWLKMDSGMHRVGFFPEDFSAAHERLRASGKVAKIVMMSHFSRADELDCPRTEEQLAAFAAASQGLEGEISLRNSPAVLGWPKVPSDWVRPGILLYGATPFERAHPLADRLRPVMTLESKVISVRDLPAGEPVGYGARYSTERSQRIGVVAMGYADGYPRHAADGTLVFIDGKPGRLVGRVSMDMLTVDLTDHPQAGLGSRVELWGPNVPVGALAAQFGSIPYQLLCNLKRVPRVYSGA", "text": "FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. SIMILARITY: Belongs to the alanine racemase family."}
+{"protein": "MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAVSAAPPGAHLQQQQQQQQQQETSPRQQQQQQQGDDGSPQAQSRGPTGYLALDEEQQPSQQRSASKGHPESACVPEPGVTSATGKGLQQQQPAPPDENDSAAPSTLSLLGPTFPGLSSCSTDLKDILSEAGTMQLLQQQRQQQQQQQQQQQQQQQQQQQEVVSEGSSSGRAREAAGASTSSKDSYLGGSSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGGPPAVRPCAPLAECKGSLLDDGPGKGTEETAEYSPFKAGYAKGLDGDSLGCSSSSEAGGSGTLEMPSTLSLYKSGALDEAAAYQSRDYYNFPLSLGGPPPHPPPPHPHTRIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPSSGSPSATTSSSWHTLFTAEEGQLYGPCGGSGGGSAGDGGSVAPYGYTRPPQGLAGQEGDFPPPDVWYPGGVVSRVPFPSPSCVKSEMGSWMESYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASNVTSPTEEPTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ", "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": "MASSFLPAGAITGDSGGELSSGDDSGEVEFPHSPEIEETSCLAELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKKLDPGWNPQIPEKKGKEANTGFGGPVISSLYHEETIREEDKNIFDYCRENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGADPTLRDQDGCLPEEVTGCKTVSLVLQRHTTGKA", "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. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "NIPQLTPTP", "text": "FUNCTION: Has antibacterial activity against the Gram-positive bacteria L.monocytogenes, L.lactis subsp lactis and L.curvatus H28, but not against the Gram-positive bacteria L.curvatus CWBI-B28, L.brevis and L.plantarum or the Gram-negative bacteria E.coli and Pseudomonas sp 55. Has no antifungal activity against S.cerevisiae, Penicillium sp BKS- TAN2 or A.niger. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MHKHRKPTEADVTPESLFYQRRRVLKALGISAAALSLPLSAQADLLAWFKGSDKPKAPPGKPLTFSQPTDWKLDLPLTPEDKVTGYNNFYEFGLDKADPAANAGGLKTDGWTIKIDGDVAKPLTLDIDDLLKRFPLEERIYRFRCVEAWSMVIPWVGFELAKLIKFAEPTSNARYVAFQTLHDPEQMPGQKDRFMGGGLDYPYVEGLRMDEAMNPLALLAVGVYGKTLPPQNGAPIRLVTPWKYGFKNIKSIVHIRLTRERPPCTWNLAAPDEYGFYANVNPHVDHPRWSQATERVIGSGGLLNVERQPTLLFNGYAEQVASLYRGLNLRDNF", "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": "MGARRWLVSGVGYRLEESLEYRTLVPEALSIWRMAGANRMLFDCFDVDSKAARRSVAILSSCLRIECWGRDVVLRALNSNGRALLAPLSEDCPAQVTCLRDGDTLHWRFPQEESHADEWRRLHGLSSLEALRRVLGTLGDAEGPVLLGGLFSFDLAEQFEPLPAPAEPARHCPDYLFLVPELLLDIDHLARRTSLQAFVHDPAGHDRLAASLRQCADEFHGAVEEASESPVAGVRAGNYQVDLDDASFARQVERLQAHVRAGDVFQIVPSRSFSMPCADPWRAYRQLCLRNPSPYRFFLDAGDFCLFGASPESALKYDAESREVELYPIAGTRPRGRDARGAIDAELDNRLEAELRLDAKEIAEHMMLVDLARNDLARVCRSGTRQVRDMLKVDRYSHVMHLVSRVAGELHGELDALHAYRACLNMGTLVGAPKVRAMQLLRQYEDGYRGSYGGAIGILDSAGNLDTSIVIRSAEVREGIARVRAGAGVVLDSDPRLEAEETRNKALAVLTAVAAAERERGERDAHHAVG", "text": "FUNCTION: Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, a precursor for Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which is required to induce the genes for the biosynthesis of the virulence factor pyocyanine (PCN), a characteristic blue-green phenazine pigment produced by P.aeruginosa (PubMed:11591691, PubMed:2153661, PubMed:23449919). In the first step, the glutamine-binding beta subunit (PhnB) 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 (PhnA) to produce anthranilate (By similarity). SIMILARITY: Belongs to the anthranilate synthase component I family."}
+{"protein": "MARNMNILTLFAVLIGSASAVYHPPSWTAWIAPKPWTAWKVHPPAWTAWKAHPPAWTAWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKAPPPTWTAWKATPKPWTAWKAPPPAWTAWKATLKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTVWKATPKPWTAWKATPKPWTAWKAPPPAWSAWKATPKPWTVWKATPKPWTAWKATPKPWTAWKATPKPWTVWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKAPPPTWTAWKATPKPWTAWKAPPPAWSAWKATPKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTAWKVPPPAWTAWKAHPPAWTAWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKATPKPWTVWKATPKPWTAWRATPPPTWTAWHGHGYGGYGKPGKPGKPGSKGPRGPAGPPGATGKTGRTGATGKRGPPGYPGKPGVPGRNGYVHIVFDGYGKWEIGKIERKNIREAVAKAWTAWNAGHGHGWTAWTAPPAYG", "text": "FUNCTION: Provides adhesiveness to the mussel's foot. Mussels produce one of the strongest water insoluble glues. The mussel's adhesive is a bundle of threads, called a byssus, formed by a fibrous collagenous core coated with adhesive proteins (By similarity). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MAKRTAPLLLLTLAVGLAGGSQGDREPVYRDCVLRCEERNCSGDALKHFRSRQPIYMSLAGWTCRDDCKYECMWFTVGLYLQEGHRVPQFHGKWPFSRFLFIQEPASAVASLLNGLASLVMLCRYRASVPASSPMYHTCMAFAWVSLNAWFWSTVFHTRDTDLTEKMDYFCASAVILHSVYLCCVRTVGLQHPSVASAFGALLLLLLTGHISYLSLVHFDYGYNMMANVAIGLVNLAWWLVWCLRNRQRLPHTRRCMVVVVLLQGLSLLELLDFPPLFWVLDAHAIWHISTIPVHTLFFRFLEDDSLYLLKESGAMFKLD", "text": "FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Mainly localizes to Golgi apparatus. SIMILARITY: Belongs to the PGAP3 family."}
+{"protein": "MSVTLHTTHGDLKVELFCEAVPKTAENFIALCAAGAYNDTPFHRLIPGFMIQGGDISLGPAANSQGTTPMLPFDDIPKGGTSIYHPSALNQEIHLPALRHNTRGILSMASRPVKNQTAPGSQGATGPTINGSQFFITFAAAPHLDGSSTVFGKVLNLTAEDEGGDVLSKLEKANVKTDKKGKVVQPKENEETEYETLRINRVTIHANPFAT", "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. PPIL3 subfamily."}
+{"protein": "MSSLVRPINLGKINHSQSTVKDYILLMKPRVMSLVIFTGFVGMWLAPYSVHPFIAGIAVVCIALGAGSAGAINMWYDRDIDSLMKRTQKRPIVRGVIESDEALSFGLITGFFAVFFMALCVNLLASFLLLFTIFYYICIYTIWLKRRSIQNIVIGGVSGALPPVIGYAAVSNTISLESIILFLIIFIWTPPHSWALALFCNDDYKNCKVPMMPAVKGTLYTKKQILIYSILLFIVSLMPFFIGMNNFIYLIISGILGVVFLYYAGSLFYDTPDNKQAKRFFAYSIFYLFFIFLLLYSTNTISTIS", "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. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily."}
+{"protein": "MLKFVILLCSIAYVFGAVVPLGMLSQSDGRIVGGVESKIEDFPWQISLQRDGRHYCGGSIYSKNVIITAAHCLRNVVAEELRVRVGSSYWEHGGSLRNISKFQIHESYVEPTKEYDVALLKLDSDLSFNSTIKAIELTNEIPPEYADAIVSGWGETLVPPPGIPDQLRSVDVKIIHREKCASRNFGYGSNIKASMICAYAIGKDSCQGDSGGPLVVNNLLVGVVSWGIDCARPSYPGVYVDVSHVRSLIVSNAESI", "text": "FUNCTION: Specificity, limited to carboxyl side of arginine residue in B-chain of insulin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MDRSEGMDTLENSMSGGMSMGMSMGGHQGHPPDIKPDISSLTSPTSTHGGYYGFGPGSMSSMSSSTQPSPGPQQMHSPGMHSPTSSMGSPPMLCLSPTGPSPSPGLPHSSLHTKHICAICGDRASGKHYGVYSCEGCKGFFKRTVRKDLTYACRDDKNCMIDKRQRNRCQYCRYMKCLSMGMKREAVQEERQRVKEKGDGEVESTSGANNDMPVEQILEAELAVDPKIDTYIDAQKDPVTNICQAADKQLFTLVEWAKRIPHFTELPLEDQVILLRAGWNELLIAGFSHRSIMAKDGILLATGLHVHRSSAHQAGVGTIFDRVLTELVAKMREMKMDKTELGCLRAVVLFNPDAKGLTAVQEVEQLREKVYASLEEYTKTRYPEEPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDQPIDTFLMEMLENPSPTT", "text": "FUNCTION: Ligand-dependent transcription factor probably involved in the retinoic acid response pathway. Binds 9-cis-retinoic acid (By similarity). Involved in embryo development, in particular eye and shell formation. May play a role in growth cone steering. SUBCELLULAR LOCATION: Cytoplasm Nucleus Membrane; Peripheral membrane protein Cell projection, axon Cell projection, growth cone Note=Not present in nucleus of neurons in adult CNS. Detected in neurites and growth cones of cultured neurons. SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 subfamily."}
+{"protein": "MSSFSESALEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSNRKLTFLYLANDVIQNSKRKGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGEFIQQLKLSMEDSKSPPPKATEEKKSLKRTFQQIQEEEDDDYPGSYSPQDPSAGPLLTEELIKALQDLENAASGDATVRQKIASLPQEVQDVSLLEKITDKEAAERLSKTVDEACLLLAEYNGRLAAELEDRRQLARMLVEYTQNQKDVLSEKEKKLEEYKQKLARVTQVRKELKSHIQSLPDLSLLPNVTGGLAPLPSAGDLFSTD", "text": "FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the UPF0400 (RTT103) family."}
+{"protein": "MPFLGQDWRSPGWSWIKTEDGWKRCESCSQKLERENNHCNISHSIILNSEDGEIFNNEEHEYASKKRKKDHFRNDTNTQSFYREKWIYVHKESTKERHGYCTLGEAFNRLDFSSAIQDIRRFNYVVKLLQLIAKSQLTSLSGVAQKNYFNILDKIVQKVLDDHHNPRLIKDLLQDLSSTLCILIRGVGKSVLVGNINIWICRLETILAWQQQLQDLQMTKQVNNGLTLSDLPLHMLNNILYRFSDGWDIITLGQVTPTLYMLSEDRQLWKKLCQYHFAEKQFCRHLILSEKGHIEWKLMYFALQKHYPAKEQYGDTLHFCRHCSILFWKDSGHPCTAADPDSCFTPVSPQHFIDLFKF", "text": "FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) (By similarity). SUBCELLULAR LOCATION: Nucleus Note=In the nucleus, associates with a subnuclear dot-like structure."}
+{"protein": "MLLMIDNYDSFTYNIVQYFGELNQDVKVVRNDQVTLEDIERWQPKYLVVGPGPCSPTEAGISIPAIHHFAGRIPLLGVCLGHQAIGQAFGGNIIRAKTVMHGRLSDMYHTDKGIFSNLPSPFSATRYHSLVIEQESLPECLEVTCWTNQNDGSIEEIMGVKHKTLPVEGVQFHPESILSQHGHQIFKNFLEIYA", "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": "MLLNIANLVGKHTIKFAQSVGIFALFSFIAISSIIKPPLYLSLIMRQLLFIGFHSLPVVAMTTFFSGAVLALQSYTGFSRFSAENSIATVVVLSLTRELGPVLAGLIVAGRVGASIAAEIATMKVTEQVDALYTLSTDPIKYLVCPRVIAAIITMPCLVLIGDVIGVMGGYLVGIYKLNFNSTAYLTSTFQYLELIDVISGLVKATVFGFIISIISCYSGYYSGKGAKGVGRATTSAVVNSSILILISNYLITELLFKV", "text": "FUNCTION: Could be part of an ABC transporter complex. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MlaE permease family."}
+{"protein": "MACAPLLLEQFIYKKRNFAYAFVRHRLFVLCKQSLIRVQSAEGIKRIEISPKSNLKHLYDSVQNALKVDGFGLFKERNFLTELQASGSQLVGTSLRHGDMVYLKQMAGTSSRRTSTTVLDSQAFKTSTISNPNSARPSFNVIEDDVDQALSKADGTIKRERDSKLCHHNANGRCVHCSALEPYDESYLKEHNIKHLSFHSYIRKQTSGMDQGKYFVFDDINCRIKPGCREHPPWPKGICSKCQPSAITLNRQTYRHVDNVMFENTKIVERFLNYWRTTGHQRMGYLYGTYEQHTDVPLGIRAKVAAIYEPPQESTRDSINIQPDEFADDVDAVASALGLKKIGWIFTDLITDDASIGTVKQIRGIESHFITAQECITAGELQNRHPNPCKYASNGVFGSKFVTICVTGDKTKQVHMEGYAVSAQCMALVRDNCLIPTKDAPELGYVRESTDKQYVPDVFYKEKDLYGNEVQRLARPLPVEYLLVDVPASTPLQPIYTFTEYDKRQPFPIENRYIDGHLQDFNALSCYLSAWGEEEFLEAISDFHLLVYLYKMDMLPLRQHMGPLLEAVRTKNPNQAAQFKVVDVWKLLESLIQASSGGSGGTTSYPSGGASASAGASGSEAMDLDANTWTCNHCTFINRGELTSCEICSLPR", "text": "FUNCTION: May be part of a complex that binds ubiquitinated proteins and that is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. SIMILARITY: Belongs to the NPL4 family."}
+{"protein": "MVVRHSSDKGKIGVGVPLEPFLHQVGGHLSVLQYDAYTVCKPLVSQEQKFYESLPLAMKCFTPKYKGTITVRLRRDSRGHLGLVANPLKENLEPFQVSPESRAVALWQTLQQTTGSESSPCPLTQLARSLKESAAKVLLRSDCHLSTQASPLVESEDGSQVERKGFNPWGLHCHQAHLTRLCSQYPEDKRHRFLLLENVVSQYKQPCILDLKMGTRQHGDDASEEKKARHMKKCAQSTSACLGVRICGMQVYQTDQKSFLCKDKYYGRKLSVEGFRQALSQFLHDGTRLRAELLEPILRRLQALLTVIRSQSSYRFYSSSVLIIYDGEPPQTTQGSTSGGVTSGDPAKVDVRMIDFAHTTFKGSWNEHTTYEGPDPGYIFGLENLIGILRDIQEGE", "text": "FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family."}
+{"protein": "MQILAALSAIGALVATATAAAVPNAPAKQSMIDIQLSATGNTLIKATITNKGDKALNLLQFNTILDKNPTRKVRVYQNGTEVKFTGMLARYKMSNLSPDYFTTLGPKSSVESTFDIARTHDLTRGGKITVMASGTIPTAEGHGNGTSITGYARYESNKLELDVDAKKASSVAQAMGKVNKSRSTIDKRTNIDTSSCSQSQLEALEGALYNSAALAQAAAEAAPQSTDTVAEFFKSTSRNTIKTLVSRFQSVARESTYVNDGRTTYYCTDSMNGCSPGVLAYTLPDQNLIFNCPIYYSDLPPLAQSCYEQDQATTTLHEMTHNSAVVSPFCDDLGYGYDDATSLSASQALQNADSYALFANAIYLGC", "text": "FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine. May be involved in virulence (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M35 family."}
+{"protein": "MLKPRITARQLIWISAFLLMLTILMMTWSTLRQQESTLAIRAVNLGASMPDGFSVLHHLDANGIHFKSITPKNDMLLITFDSPAQSAAAKTVLDQTLPHGYVVAQQDDDNETVQWLSRLRESSHRFG", "text": "FUNCTION: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MzrA family."}
+{"protein": "MEIVSDKKISEKGIASAAELLYKGAKMLAHSCPECKMPLFEKDGKIFCPSCGREVVIEEDSAAKAESEEKPPESTKPAVKADYDEAVEKIEMAISKVCDMMVESRSVEEVRVLSDSLEKLVDALKKLRE", "text": "SIMILARITY: Belongs to the UPF0148 family."}
+{"protein": "MSTLEPAAQSKPPGGFKLWLSQLQMKHGRKLVIALPYIWLILLFLLPFLIVFKISLAEMARAIPPYTELMEWADGQLSITLNLGNFLQLTDDPLYFDAYLQSLQVAAISTFCCLLIGYPLAWAVAHSKPSTRNILLLLVILPSWTSFLIRVYAWMGILKNNGVLNNFLLWLGVIDQPLTILHTNLAVYIGIVYAYVPFMVLPIYTALIRIDYSLVEAALDLGARPLKTFFTVIVPLTKGGIIAGSMLVFIPAVGEFVIPELLGGPDSIMIGRVLWQEFFNNRDWPVASAVAIIMLLLLIVPIMWFHKHQQKSVGEHG", "text": "FUNCTION: Part of the ABC transporter complex PotFGHI involved in putrescine uptake (PubMed:8416922, PubMed:23719730). Responsible for the translocation of the substrate across the membrane (Probable). Imports putrescine for maintenance of the optimal concentration of polyamines necessary for cell growth in the presence of glucose (PubMed:23719730). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily."}
+{"protein": "MEDERSLSDICGGRLALHRRYYSPSCLEFCLSCPRISLRSITAVTCTVWLAAYGLFTLCENSMILSAAIFITLLGLLGYLHFVKIDHETLLIIDSLGIQMTSSYASGKESTTFIEMGKVKDVIINEAIYMQKVIYYLCILLKDPVEPHGISQVVPIFQSAKPRLDCLIEVYRSCQEILAHQKAASTSP", "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: Cytoplasm. SIMILARITY: Belongs to the PIGH family."}
+{"protein": "MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMNLHPVEFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGYPPITILKEQRSEYYHVLEVANEGDVRPFIRFIAKCTEVTLDTLLLATTEYSVALPEAQPNHSGLKETLPVRP", "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 (PubMed:27918543). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (PubMed:27918543). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:27918543). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (PubMed:26673894, PubMed:29064368, PubMed:27918543). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (PubMed:27918543). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the fic family."}
+{"protein": "MTARPSVSVYSASEDKVVGTCSLPAVFTAPIRHDVVQFVHTNMAKNSRQPYAVNRLSGMKHSTESWGTGRAVARIPRIHGGGTSMSGAGAFGNMCRGGRMFAPTKIFRRWHRKINLHQKRFAVVSALAASSLPALVMSRGHKIENVAEVPLVVEDGVRAYEKTKEAMTFLKTVGAIDDVNRVNDSRQIRAGRGKMRNRRYVARRGPMLVMPDNKGTRAFRNIFGLDLANVNSLNLLHLAPGGHVGRFIIWTKSAFEKLDKIFGTFTEPSTVKSGFMLPAPMLTSTDVTRIMQSEEVRRVLKPKKLQPKRPSRYRQPTNGIRNRRLRLRLNPFQKKEKAMAKGMQNKKNREARHAAKVVRLAKARKNVAKALKKK", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL4 family."}
+{"protein": "AILGQDGSVWAQGLHLGGAKYVIAGEPGAVIRLGDYLLDQGL", "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. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family."}
+{"protein": "MSSSHFASRHRKDISTEMIRTKIAHRKSLSQKENRHKEYERNRHFGLKDVNIPTLEGRILVELDETSQGLVPEKTNVKPRAMKTILGDQRKQMLQKYKEEKQLQKLKEQREKAKRGIFKVGRYRPDMPCFLLSNQNAVKAEPKKAIPSSVRITRSKAKDQMEQTKIDNESDVRAIRPGPRQTSEKKVSDKEKKVVQPVMPTSLRMTRSATQAAKQVPRTVSSTTARKPVTRAANENEPEGKVPSKGRPAKNVETKPDKGISCKVDSEENTLNSQTNATSGMNPDGVLSKMENLPEINTAKIKGKNSFAPKDFMFQPLDGLKTYQVTPMTPRSANAFLTPSYTWTPLKTEVDESQATKEILAQKCKTYSTKTIQQDSNKLPCPLGPLTVWHEEHVLNKNEATTKNLNGLPIKEVPSLERNEGRIAQPHHGVPYFRNILQSETEKLTSHCFEWDRKLELDIPDDAKDLIRTAVGQTRLLMKERFKQFEGLVDDCEYKRGIKETTCTDLDGFWDMVSFQIEDVIHKFNNLIKLEESGWQVNNNMNHNMNKNVFRKKVVSGIASKPKQDDAGRIAARNRLAAIKNAMRERIRQEECAETAVSVIPKEVDKIVFDAGFFRVESPVKLFSGLSVSSEGPSQRLGTPKSVNKAVSQSRNEMGIPQQTTSPENAGPQNTKSEHVKKTLFLSIPESRSSIEDAQCPGLPDLIEENHVVNKTDLKVDCLSSERMSLPLLAGGVADDINTNKKEGISDVVEGMELNSSITSQDVLMSSPEKNTASQNSILEEGETKISQSELFDNKSLTTECHLLDSPGLNCSNPFTQLERRHQEHARHISFGGNLITFSPLQPGEF", "text": "FUNCTION: Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell contact in intestinal epithelial cells. SIMILARITY: Belongs to the SAPAP family."}
+{"protein": "MTSTITTTETLQDAVPFVAPPSPPEDTSNKELPEKPYYDVEFNYRLDPRDGGDEVIWGGTVGLMRRKYETRTVRINNERGNEHNFNLDTHGFAWVKHKTSVTEFADYLAIRQGPYFGEVAEMLKRVTGATKVHVIGHLHRSLNYNDTTEEEKNAPDMTMTKGQTPGRFVHVDQSYQGAVRRLYLDLPQEEARRLEKTRWAIINVWRPVRKVTNEPLAVCDARSVREDELFNTLHLVPMRWPDAAPQENQMWAVAPPKTPTQHKWHYVSGMTEDEALLIKMFDSKKDGTARRVPHSSFPTPDDFGEPRASTETRCFVFWEDQEAE", "text": "FUNCTION: Hydroxylase/desaturase; 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 asaB hydroxylase/desaturase family."}
+{"protein": "MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSGKKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGFTRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSLDVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLEILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPISLDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRSWLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE", "text": "FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (PubMed:18983167). May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development (PubMed:18983167). Binding to RAF1 reduces RAF1 'Ser-259' inhibitory- phosphorylation and stimulates RAF1-dependent EGF-activated ERK- signaling (PubMed:23509299). Protects against cell death induced by hydrogen peroxide and staurosporine (PubMed:23509299). SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE8 subfamily."}
+{"protein": "MAAVALMPPPLLLLLLLASPPAASAPSARDPFAPQLGDTQNCQLRCRDRDLGPQPSQAGLEGASESPYDRAVLISACERGCRLFSICRFVARSSKPNATQTECEAACVEAYVKEAEQQACSHGCWSQPAEPEPEQKRKVLEAPSGALSLLDLFSTLCNDLVNSAQGFVSSTWTYYLQTDNGKVVVFQTQPIVESLGFQGGRLQRVEVTWRGSHPEALEVHVDPVGPLDKVRKAKIRVKTSSKAKVESEEPQDNDFLSCMSRRSGLPRWILACCLFLSVLVMLWLSCSTLVTAPGQHLKFQPLTLEQHKGFMMEPDWPLYPPPSHACEDSLPPYKLKLDLTKL", "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. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the TMEM59 family."}
+{"protein": "PPKPQPKPPPKPQPKPPPAPTPSPCPPQPPKPQPKPPPAPTPSPCPPQPPKPQPKPPPAPGPSPKPGPSPSPPKPPPSPAPKPVPPPSPSPKPSPPKPPAPSPKPSPPKPPAPSPPKPQNKTIPAVFFFGDSIFDTGNNNNLDTKLKCNYRPYGMDFPMGVATGRFSNGRVASDYISKYLGVKEIVPAYVDKKLQQNNELQQSDLLTGVSFASGGAGYLPQTSESWKVTTMLDQLTYFQDYKKRMKKLVGKKKTKKIVSKGAAIVVAGSNDLIYTYFGNGAQHLKNDVDSFTTMMADSAASFVLQLYGYGARRIGVIGTPPIGCTPSQRVKKKKICNEDLNYAAQLFNSKLVIILGQLSKTLPNSTIVYGDIYSIFSKMLESPEDYGFEEIKKPCCKIGLTKGGVFCKERTLKNMSNASSYLFWDGLHPSQRAYEISNRKLVKKYIHFI", "text": "SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family."}
+{"protein": "MAALATSQLVATRAGLGVPDASTFRRGAAQGLRGARASAAADTLSMRTSARAAPRHQQQARRGGRFPSLVVCASAGMNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVVSPRYDQYKDAWDTSVVSEIKMGDGYETVRFFHCYKRGVDRVFVDHPLFLERVWGKTEEKIYGPVAGTDYRDNQLRFSLLCQAALEAPRILSLNNNPYFSGPYGEDVVFVCNDWHTGPLSCYLKSNYQSHGIYRDAKTAFCIHNISYQGRFAFSDYPELNLPERFKSSFDFIDGYEKPVEGRKINWMKAGILEADRVLTVSPYYAEELISGIARGCELDNIMRLTGITGIVNGMDVSEWDPSRDKYIAVKYDVSTAVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFHMGRLSVDCNVVEPADVKKVATTLQRAIKVVGTPAYEEMVRNCMIQDLSWKGPAKNWENVLLSLGVAGGEPGVEGEEIAPLAKENVAAP", "text": "FUNCTION: Required for the synthesis of amylose in endosperm. SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. Note=Amyloplast or chloroplast, granule-bound. SIMILARITY: Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily."}
+{"protein": "MLLATFKLCAGSSYRHMRNMKGLRHQAVLAIGQELNRRALGDPSPGWMGQVRRRSSLLGSQLEATLYSDQELSYIQQGEEAMQKALGILNNQEGWKKESQQENGDEVLSKVVPGVGKVFRLEVLLDQPMDRLYEELVDRMEAMGEWNPNVKEIKVLKKIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKRRGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPLAGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFASHLRKRLESSPASEAQC", "text": "FUNCTION: Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Mediates the transfer of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane where it is cleaved to pregnenolone (By similarity). SUBCELLULAR LOCATION: Mitochondrion."}
+{"protein": "MCVTKASLPMLSPTGSPQEVEVGKILQGKRHGTISPESCAKLYCYYGVIMVLTVAVIALSVALSATKTEQIPVNKTYAACPQNWIGVENKCFYFSEYPSNWTFAQAFCMAQEAQLARFDNQDELNFLMRYKANFDSWIGLHRESSEHPWKWTDNTEYNNTIPIRGEERFAYLNNNGISSTRIYSLRMWICSKLNSYSLHCQTPFFPS", "text": "FUNCTION: Receptor for KLRB1B that protects target cells against natural killer cell-mediated lysis (PubMed:14990792, PubMed:16751398). Inhibits osteoclast formation (PubMed:11278931, PubMed:12374791). Binds high molecular weight sulfated glycosaminoglycans (PubMed:15123656). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
+{"protein": "MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQQQRLKIMEYYEKKEKQVELQKKIQSSNMLNQARLKVLKVREDHVSSVLDDARKRLGEVTKNQSEYETVLTKLIVQGLFQIMEPKVILRCREVDVPLVRNVLPAAVEQYKAQINQNVELFIDEKDFLSADTCGGVELLALNGRIKVPNTLESRLDLISQQLVPEIRNALFGRNVNRKFTD", "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 E subunit family."}
+{"protein": "MIIVKVVLPLPIRKYFKYFMPDSMCPIIGGRIVVPFRSKDIVGIVISFCNKKNISNLNLAFVKSCIDTESIYSDVVFSILIWLSRYYYFPIGSIFFSILPKYLKKICLIDNKNYKFAILRKTKYKDFKTFNLLFFCKKKSFIDKDLEKYTFFDFFLKKNFLQKSCKNYFYHENIPHIYQNYLIKKKFFLNKKIIFIINKILMKNCFTSWLITKNNFYLKVKFYLGLIKECLSKNLQILILVPFVKDIYQILFFLKKYFNVYIDIIHSQLNNEDYLKKWIRTKSGKNSIIIGTKNSVFFPFLKLGLIIVNQEHHLNYRNLDQCRYNVRDIAILRAYKQNIPIILDSDTPSLRTLYNILHKKCFYIKFIKNKKTFFLKNNVIDLRKERIKIGLSSTLINEIFNNIQKNYPVLLVLNKFSFVFFGLICRRCGKIEKCHICNDYFETKKYDNFLFCRNCLIKIKKPLFCYNCKNFSLIVFDFGIKKIKNSFKKIFPNINLFFLLSLKKNKTKKLKIQFFKFPISNACIIITTEKISQHYYFPYVRFIALTNVDHYFFSFHFCSIEHFLQFYFNLINLTGENKKLLKIFIQTSYPNNKFLLNLCSSDYFLFCRKILSLRKKYFLPPWNFQVIFYSSSKFFEKSFIFLECIQIILKKQSKRDNVSLWFVGPHPVFSLKDRKKCFYQLLIHSPSRTYLKKILKESINIVQCFSISQNVQWFLDIDIY", "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": "ATTTTTTHNSKNKQYLAKQKPVELTLGYQNPNGCKVCSFGSKGSIYQKVSSGFKGVSVMTDDKSTMPSVEEDFENIGILNVDSSLEPFKDHFKYRLKRYLHQKKLIEEYEGGLQEFAKGYLKFGFNREEDGISYREWAPAAQEAQIIGDFNGWNGSNLHMEKDQFGVWSIQIPDADGNPAIPHNSRVKFRFKHSDGVWVDRIPAWIKYATVDPTRFAAPYDGVYWDPPLSERYQFKHPRPPKPKAPRIYEAHVGMSSSEPRINSYREFADDVLPRIRENNYNTVQLMAVMEHSYYASFWYHVTKPFFAVSSRSGSPEDLKYLIDKAHSLGLNVLMDVIHSHASNNVTDGLNGFDVGQSSQQSYFHAGDRGYHKLWDSRLFNYANWKSSFLLSNLRWWLEEYKFDGFRFDGVTSMLYHHHGINMAFTGDYNEYFSEETDVDAVVYLMLANSLVHDILPDATDIAEDVSGMPGLGRPVSEVGIGFDYRLAMAIPDKWIDYLKNKKDSEWSMKEISLNLTNRRYTEKCVSYAESHDQSIVGDKTIAFLLMDEEMYSSMSCLTMLSPTIERGISLHKMIHFITLALGGEGYLNFMGNEFGHPEWIDFPREGNGWSYEKCRLTQWNLVDTNHLRYKFMNAFDRAMNLLDDKFSILASTKQIVSSTNNEDKVIVFERGDLVFVFNFHPENTYEGYKVGCDLPGKYRVALDSDATEFGGHGRVGHDADQFTSPEGIPGIPETNFNNRPNSFKVLSPPHTCVVYYRVDERQEESNNPNLGSVEETFAAADTDVARIPDVSMESEDSNLDRIEDNSEDAVDAGILKVEREVVGDN", "text": "FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch 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. May preferentially transfer long chains during branching. SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB subfamily."}
+{"protein": "MALTRFERFLGRLLRAVVWILFAAFKLFAPQQRHGVSRLPPITNPLLLLSAMQLARKIRRKEVTSVEVVQAYIDRIQEVNPLINAMVKDRFSAALQEAAQVDKLIEEETGGEDVLEDRLPLLGVPITVKEAFALQGMPNSTGLLTRRDLVSGADAPSVALLKRAGAIPLGVTNCSELCMWLESHNHLYGITNNPYDFERIVGGSSGGEGSILGAGSSVIGIGSDIGGSIRIPCFFNGIFGHKPSVGIVNNEGQYPPASGQQMGFLCTGPMCRYAEDLIPMLSIMGGPNAEKLSLFTEVDLKKLRFFSVPHNGGSHLVSPVEPQLLHAQKMVVKRLEADLGVKVQELLIPQLKYSFQIWGTMMASPGKDGKPPTTFAELMSEGGKKVWPAWELFKWFLGFSSHTLAAIGLALVELFQSSHPSPFIMQQKESLQQELEELLGTDGVLLYPSHPLIAQKHHHPIFTPFNFSYTGIFNILGLPVTQCPLGLSAEGLPLGVQIVAGKLQDRLSLATALYLEKAFGGWREPGKTTIKP", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the amidase family."}
+{"protein": "MLKSLLCILLIFGCLCRIHGVMFHLTPNTQKCLKEDIQANQLVMGEYEVSDVPGQIIDYIARDTKGHILSQKEHITKGKFSFTSEVFDAYEICFISKVPPHQRGISQEVSLVTKKGVETKNYEGIGEASKLKPLEVDLKRLEDLSDSIVRDFAVMRKREEEMRDTNEKTNSRVLFFSIFSMCCLLGLATWQVLYLRRYFKAKKLIE", "text": "FUNCTION: Eca and bai are essential, though not redundant, for dorsoventral patterning of the embryo. Specifically required during early embryogenesis for the activity of maternal tkv, while the zygotic tkv is not affected (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the EMP24/GP25L family."}
+{"protein": "MSEPEFQQAYEEVVSSLEDSTLFEQHPEYRKVLPIVSVPERIIQFRVTWENDKGEQEVAQGYRVQYNSAKGPYKGGLRFHPSVNLSILKFLGFEQIFKNSLTGLDMGGGKGGLCVDLKGRSNNEIRRICYAFMRELSRHIGQDTDVPAGDIGVGGREIGYLFGAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGYGLVYYTQAMIDYATNGKESFEGKRVTISGSGNVAQYAALKVIELGGTVVSLSDSKGCIISETGITSEQVADISSAKVNFKSLEQIVNEYSTFSENKVQYIAGARPWTHVQKVDIALPCATQNEVSGEEAKALVAQGVKFIAEGSNMGSTPEAIAVFETARSTATGPSEAVWYGPPKAANLGGVAVSGLEMAQNSQRITWTSERVDQELKRIMINCFNECIDYAKKYTKDGKVLPSLVKGANIASFIKVSDAMFDQGDVF", "text": "FUNCTION: Catalyzes the incorporation of an ammonium ion into alpha- ketoglutarate to form L-glutamate, the major route of assimilation of ammonia into an organic form in yeast. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
+{"protein": "MKDDFAEEEEVQSFGYKRFGIQEGTQCTKCKNNWALKFSIILLYILCALLTITVAILGYKVVEKMDNVTGGMETSRQTYDDKLTAVESDLKKLGDQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQLKETLENNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQNQMYSHNVVIMNLNNLNLTQVQQRNLITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLNSFTGQMENITTISQANEQNLKDLQDLHKDAENRTAIKFNQLEERFQLFETDIVNIISNISYTAHHLRTLTSNLNEVRTTCTDTLTKHTDDLTSLNNTLANIRLDSVSLRMQQDLMRSRLDTEVANLSVIMEEMKLVDSKHGQLIKNFTILQGPPGPRGPRGDRGSQGPPGPTGNKGQKGEKGEPGPPGPAGERGPIGPAGPPGERGGKGSKGSQGPKGSRGSPGKPGPQGSSGDPGPPGPPGKEGLPGPQGPPGFQGLQGTVGEPGVPGPRGLPGLPGVPGMPGPKGPPGPPGPSGAVVPLALQNEPTPAPEDNGCPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRESHWIGLTDSERENEWKWLDGTSPDYKNWKAGQPDNWGHGHGPGEDCAGLIYAGQWNDFQCEDVNNFICEKDRETVLSSAL", "text": "FUNCTION: Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May also play a role in the clearance of amyloid-beta in Alzheimer disease. SUBCELLULAR LOCATION: Membrane; Single- pass type II membrane protein Note=Forms clusters on the cell surface."}
+{"protein": "MSKKGPFNIRNAAADTFAMVVFCFITGMFIEILISGMTFEQSLASRTLSIPVNIAIAWPYGVFRDFMLRQGARISPSKFMKNIADLVAYVTFQSPAYAMILLVVGATPEQIITAVSSNVVVSCVMGVFYGYFLDACRKAFKVPGYYTPQA", "text": "FUNCTION: Exports L-alanine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AlaE exporter family."}
+{"protein": "MNHLPMPTFGPLAGVRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWEHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGMTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEICPRMTKGKDPYYAGCGLYKCADGYIVMELVGITQINECFKDIGLAHILGTPEVPEGTQLIHRVECPYGPLVEEKLDAWLATHTIADVQARFAELNIACAKVLTIPELEGNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGKIWRGMPSHGMDTAAILKNIGYSEADIKELVGKGLAKVED", "text": "FUNCTION: Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L- carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA. FUNCTION: Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L- carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CoA-transferase III family. CaiB subfamily."}
+{"protein": "MNHLVMISLALLLLLGVESVRDAYIAKNYNCVYECFRDAYCNELCTKNGASSGYCQWAGKYGNACWCYALPDNVPIRVPGKCHRK", "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. The dissociation is voltage- dependent. This toxin is active on insects. It is also highly toxic to crustaceans and has a measurable but low toxicity to mice. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
+{"protein": "MESYLVDTYQGVPYTAAVQTDLVEKDQLPARLTVWFPLFQTNTPPTVLLEQLKTLTITTLYTASQNGPILKVNASAQGAAMSALPKSFDVSASVALDDYSKLEFDKLTVCELKAVYLTTMKPYGMVSKFVNSAKAVGKKTHDLIALCDFLDLEKGVPVTIPAYIKSVSIKESESATVEAAIGGEADQAITQARIAPYAGLIMIMTMNNPKGIFKKLGAGVQVIVELGAYVQAESISRICRNWSHQGTRYVLKSR", "text": "FUNCTION: Has a crucial role in virus assembly and budding. The matrix interacts with the RNP complex and this association serves two functions: facilitate virion assembly and inhibit the viral transcriptase activity. Early in infection, M is localized to the nucleus and may inhibit host cell transcription. Later on, M can associate with lipid rafts supposely by interacting with the cytoskeleton and with the cytoplasmic tail of glycoprotein G. The binding of M to host membrane is stabilized by the surface expression of the viral glycoproteins. These interactions may allow virus formation by mediating association of the nucleocapsid with the nascent envelope (By similarity). SUBCELLULAR LOCATION: Virion Host cytoplasm Host nucleus 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 paramyxoviruses M protein family."}
+{"protein": "MAGENSDNEPSSPASPSSAGFNTDQLPISTSQNSENFSDEEEAAVDTQVIRDEPDEAEDEEEEEGEDLFNDTFMNDYRKMDENDQYESNGIDDSVDDERDLGQAMLDRRAADADLDARENRLANRKLPHLLHDNDSDDWNYRPSKRSRTTVPPRGNGGDPDGNPPSSPGVSQPDISMTDQTDDYQDEDDNDDEAEFEMYRIQGTLREWVMRDEVRRFIAKKFKDFLLTYVKPKNENGDIEYVRLINEMVSANKCSLEIDYKEFIHVHPNIAIWLADAPQPVLEVMEEVSEKVIFDLHPNYKNIHTKIYVRVTNLPVNDQIRNIRQIHLNTMIRIGGVVTRRSGVFPQLQQVKYDCNKCGAVLGPFFQNSYSEVKVGSCSECQSKGPFTVNVEQTIYRNYQKLTIQESPGTVPAGRLPRHKEVILLNDLIDCARPGEEIEVTGIYTNNFDLSLNTKNGFPVFATVVEANYVTKKQDLFSAYKLTQEDKTQIEELSKDPRIVERIIKSIAPSIYGHEDIKTALALAMFGGQEKNIKGKHRLRGDINVLLLGDPGTAKSQFLKYVEKTGQRAVYTTGKGASAVGLTAAVHKDPVTREWTLEGGALVLADRGICLIDEFDKMNDQDRVSIHEAMEQQSISISKAGIVTSLQARCSVIAAANPVGGRYDSSKSFAQNVELTDPILSRFDILCVVKDVVDPVTDEMLAEFVVNSHFKSQPKGGKMEDSDPEDGIQGSSGSTDPEVLPQNLLKKYLTYSKLYVFPKLGELDAKKLETVYANLRRESMNGQGVSIATRHLESMIRMSEAHARMHLRQYVTEEDVNMAIRVLLDSFISTQKFGVQRTLRESFKRYITYKKDFNSLLLVLLKELVKNALKFEEIISGSNSGLPTIEVKIEELQTKAKEYDIADLRPFFSSTDFSKAHFELDHGRGMIKCPKRLITW", "text": "FUNCTION: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells. May play a crucial role in the control of de- differentiation and cell proliferation processes required for lateral root formation. Is essential for embryo development. Is involved in the geminivirus mungbean yellow mosaic virus (MYMV) DNA replication, presumably in conjunction with other host factors. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MCM family."}
+{"protein": "MKIIRTLFLLLIAVYGSSVVAKPMLKATFSSTTMYYGIGPNSDKSIVAEVTIATPEGVYYGSWNLSGHRKGETLTADSWSGPEPAPKVVLKDFDNTVSRSACKNLPSNWRGCGSFTLEITVQSDDYGCPWLASSHIVATTFITNETYSPPDTRSSVCPKVPVDTFDISWDANVSKQKTTLMLDATGGTVNRTLHTYLMEGGKLCDGSKFDNRGAYCRFVSSGITLNVLGCDQSSVTTSAVDHPITDVELHDINVAVNTRNIGSGQFTSTCSFQYIIDEL", "text": "SIMILARITY: To E.coli YfcO."}
+{"protein": "MSPSSVALLAAVVIVVMGGAAEAANTKFVSASCNTEKIARGSPFFNNLRDAIEDLRQNTAYIGYDYKTSHVGSGGAPTAYGRAICKQSISQSNCTSCLSNVATRIYGICGNAIGARVQLTDCYMQYEQRSF", "text": "FUNCTION: Exerts antifungal activity through its carbohydrate-binding specificity."}
+{"protein": "AGEVEKREGMMKQIGGAMGSLAAISKGEKPFDADTVKAAVTTIGTNAKAFPEQFPAGTETGSAAAPAIWENFEDFKAKAAKLGTDADIVLANLPGDQAGVATAMKTLGADCGTCHQTYRLKK", "text": "FUNCTION: Low-spin monoheme cytochrome c."}
+{"protein": "MNRLPSSASALACTAHALNLIEKRTLDHEEMKQLNREVIDYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFSNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPGFRHVPFGDINAMRTMLTECRKTGDDVAAVILEPIQGEGGVILPPLGYLPAVRKLCDEFDALLILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATVATEEVFSVLFDNPFLHTTTFGGNPLSCAAALATINVLLEQNLPAQAEQKGDMLLDGFLQLGREYPDLVQDARGKGMLIAIEFVDNEIGYSFASEMFRQRILVAGTLNNSKTIRIEPPLTLTIEQCEQVLKATRTALAALRVSVEEA", "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": "MIRLRTYAGLSFMATLAVIYHAFSSRGQFYPATVYLSTSKISLVLLLNMCLVLMLSLWHLVKFVFLGSLREAEVERLNEQAWRELMEILFAITIFRQDFSSGFLPLVVTLLLIKALHWLAQKRVEYIETTPSVSKLSHFRIVSFMGFLLLVDSLFMYSSIRHLIQSRQASVSLFFSFEYMILATTTVAIFVKYVFYVTDMLMDGQWEKKPVYTFYLELIRDLLHLSMYICFFFVIFMNYGVPLHLLRELYETFRNFQIRVSDYLRYRKITSNMNDRFPDATPEELTASDATCIICREEMTNAKKLICGHLFHVHCLRSWLERQQTCPTCRALVVPPENATSAAPGQRELHQGSQQGTSSSGNQGSEISSSAGVSNNSLSRHHARLQAAASAASVYGKSMVYPSANTVAWSSGVPGTEQVSTEPDQTLPQHNLPVENSHAYANMSETKLEEMRKSLETHLEILRNRLHFLETRKPESAGEPENKGKSVADAAE", "text": "FUNCTION: Probable component of the HRD1 ubiquitin ligase complex that mediates the rapid degradation of misfolded endoplasmic reticulum (ER) proteins, a process called ER-associated degradation (ERAD). Targets the misfolded LRR receptor kinase BRI1. Functions redundantly with HRD3B. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HRD1 family."}
+{"protein": "MAGVSFSGHRLELLAAYEEVIREESAADWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAALPKYVLINWVGEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLSNGLARLSSPVLHRLRLREDENAEPVGTTYQKTDAAVEMKRINREQFWEQAKKEEELRKEEERKKALDERLRFEQERMEQERQEQEERERRYREREQQIEEHRRKQQTLEAEEAKRRLKEQSIFGDHRDEEEETHMKKSESEVEEAAAIIAQRPDNPREFFKQQERVASASAGSCDVPSPFNHRPGSHLDSHRRMAPTPIPTRSPSDSSTASTPVAEQIERALDEVTSSQPPPLPPPPPPAQETQEPSPILDSEETRAAAPQAWAGPMEEPPQAQAPPRGPGSPAEDLMFMESAEQAVLAAPVEPATADATEIHDAADTIETDTATADTTVANNVPPAATSLIDLWPGNGEGASTLQGEPRAPTPPSGTEVTLAEVPLLDEVAPEPLLPAGEGCATLLNFDELPEPPATFCDPEEVEGESLAAPQTPTLPSALEELEQEQEPEPHLLTNGETTQKEGTQASEGYFSQSQEEEFAQSEELCAKAPPPVFYNKPPEIDITCWDADPVPEEEEGFEGGD", "text": "FUNCTION: Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (PubMed:20215400). Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (PubMed:20215400). Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines (By similarity). Involved in memory-related synaptic plasticity in the hippocampus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, dendrite Cytoplasm, cell cortex Cell junction Cell projection, growth cone Note=In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm (PubMed:20215400). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation clusters (SMAC) (PubMed:20215400). Colocalized with RUFY3 and F-actin at the transitional domain of the axonal growth cone (By similarity)."}
+{"protein": "MGEFNEKKATCGTVCLKYLLFTYNCCFWLAGLAVMAVGIWTLALKSDYISLLASSTYLATAYILVVAGVVVMVTGVLGCCATFKERRNLLRLYFILLLIIFLLEIIAGILAYVYYQQLNTELKENLKDTMIKRYHQSGHEGVTNAVDKLQQEFHCCGSNNSRDWRDSEWIRSGEADSRVVPDSCCKTVVTGCGKREHASNIYKVEGGCITKLESFIQEHLRVIGAVGIGIACVQVFGMIFTCCLYRSLKLEHY", "text": "FUNCTION: Essential for the proper assembly of the glomerular and tubular basement membranes in kidney. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MGSEEEKVVVPRNFRLLEELERGEKGIGDGTVSYGMDDADDILMQSWTGTILGPHNTAYEGKIFQLKLFCGKDYPESPPTVRFQSRINMACVNPENGVVDPSHFPMLSNWRREFTMEDLLIQLKKEMMSSQNRKLAQPLEGNEEGRTDPKGLVVKCCVM", "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. May play a role 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": "MGISLSKRRRDNNNNHHHPHHNPPYYYSDPPPQQPPPQNGYSYSHNYPVSTPQLSLPPPPAQPPSSSQPPPSQISYRPYGQNYHQNQYYPQQAPPYFTGYHHNGFNPMMRPVYFGPTPVAVMEPPAPYVEHQTAKKVKNDVNVNKATVRLVADDLNPGHYLVSFVFDALFDGSFTIIFFGEEESKCTIVPHLPEAFPPIKVPFQKGAGQKFLQAPGTGIDLGFFSLDDLSKPSPEEVYPLVISAETVISPSSVSEEPLVHKQITQAVLEKTNDGSFKVKVMKQILWIEGERYELQELYGIDNSITQGTAASGLEDTGGKECVICLTEPKDTAVMPCRHLCLCSDCAEELRFQTNKCPICRQPIHELVKIKVESSDEQH", "text": "FUNCTION: Acts as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates (in vitro). SIMILARITY: Belongs to the RING-type zinc finger family. LOG2 subfamily."}
+{"protein": "MNDQAPVAYAPLWRTAWRRLRQRPFQYILLVLGIALGVAMIVAIDVSSNSAQRAFDLSAAAITGKSTHRLVSGPAGVDQQLYVDLRRHGYDFSAPVIEGYVLARGLGNRAMQFMGTDPFAESAFRSPLWSNQNIAELGGFLTRPNGVVLSRQVAQKYGLAVGDRIALQVKGAPTTVTLVGLLTPADEVSNQKLSDLIIADISTAQELFHMPGRLSHIDLIIKDEATATRIQQRLPAGVRMETSDTQRDTVKQMTDAFTVNLTALSLIALLVGIFLIYNTVTFNVVQRRPFFAILRCLGVTREQLFWLIMTESLVAGLIGTGLGLLIGIWLGEGLIGLVTQTINDFYFVINVRNVSVSAESLLKGLIIGIFAAMLATLPPAIEAMRTVPASTLRRSSLESKITKLMPWLWVAWFGLGSFGVLMLWLPGNNLVVAFVGLFSVLIALALIAPPLTRFVMLRLAPGLGRLLGPIGRMAPRNIVRSLSRTSIAIAALMMAVSLMVGVSISVGSFRQTLANWLEVTLKSDVYVSPPTLTSGRPSGNLPVDAVRNISKWPGVRDAVMARYSSVFAPDWGREVELMAVSGDISDGKRPYRWIDGNKDTLWPRFLAGKGVMLSEPMVSRQHLQMPPRPITLMTDSGPQTFPVLAVFSDYTSDQGVILMDRASYRAHWQDDDVTTMFLFLASGANSGALIDQLQAAFAGREDIVIQSTHSVREASMFIFDRSFTITIALQLVATVVAFIGVLSALMSLELDRAHELGVFRAIGMTTRQLWKLMFIETGLMGGMAGLMALPTGCILAWILVRIINVRSFGWTLQMHFESAHFLRALLVAVVAALAAGMYPAWRLGRMTIRTAIREE", "text": "FUNCTION: Probably part of an ABC transporter complex involved in host cell binding either through secretion of an adherence factor or through maintaining the architecture and integrity of the mycobacterial cell envelope (PubMed:17030567). Could be required for host endothelial-cell invasion and/or intracellular survival (PubMed:16586367). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-4 integral membrane protein family."}
+{"protein": "MAARNAFYAQSGGVTAVINASACGVLETARQYPDRIGTVYAGRNGIVGALTEDLIDTGQESAEAIAALRHTPSGAFGSCRYKLKGLEENRAQYERLIEVFRAHDIGYFFYNGGGDSADTCLKVSQLSEKLGYPLQAVHIPKTVDNDLPITDCCPGFGSVAKYIAVSVREASFDVRSMAATSTCIFVLEVMGRHAGWIAAAGGLASDERHELALVILFPEQVFDPERFLRAVDEKVRSHGYCSVVVSEGIRGADGRFVAESGSRDVFGHARLGGVAPVIADLIKERLGYKYHWAVADYLQRAARHIASRTDVEQAYAVGKAGVEMALKGLSAVMPAIVRTSDSPYRWEITAASLAEVANVEKKMPLEFISADGFGITEACRRYLRPLIEGEDYPPYAGGLPDYVTLCNVAVPKKLAASFSV", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily."}
+{"protein": "MDLIPQQLKAVTLTHVRYRPGDQLGHFLAWISLVPVFISLGGFVSHFLFRRELQGIFFGIGLVISQFINEFIKTSVEQARPETCTLLEACDSHGWPSSHSQFMFFFATYFSLMGCKGIGFWFGLRSRWIMNLLHWSLAVVTMYSRVYLGYHTVAQVFAGAALGGIVGASWFWVVNSVLYPFFPVIEESVLGRWLYVKDTSHIPDVLKFEYDNARAARKDMDSAKSD", "text": "FUNCTION: Exhibits phosphatidate phosphatase (PAP) activity in vitro. May play a primary role as PAP in plastids. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family."}
+{"protein": "MTEYKLVIVGGGGVGKSALTIQLIQNHFIDEYDPTIEDSYRKQVTIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSFDEIASFREQILRVKDKDKVPMIVVGNKCDLEGERQVTTGEGQDLARSFGCPFMETSAKSRVNVEESFYQLVREIRKDSRTDTKGPGGKGGKKTLKCLLL", "text": "FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Note=Inner surface of plasma membrane. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "NQSERAEDSGNESDGDKDELSTLVEMGHHAPWDIDDM", "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. SIMILARITY: Belongs to the HIV-1 VPU protein family."}
+{"protein": "MKALLNKDIREEIQALIEIAEENLSAAKILFENKLYRDAVARAYYAIFHSAKALLLTKNLNPKKHAGVIKMFGLYFVNEGYIEEIYGRIITKSYNLRWKADYTTDKPTEEEAESIIYEAEMFVDRIKKALKEIL", "text": "FUNCTION: Putative toxin component of a putative type VII toxin- antitoxin (TA) system. Its cognate antitoxin might be MJ0604. SIMILARITY: Belongs to the UPF0332 family."}
+{"protein": "MEETEIPQNIVLTRLDDLINWGRANSLWPMFFGLSCCFVEMMTSFTSRYDISRFGAEVLRGTPREADLMVIAGTVFKKMAPSILRLYEQMAEPKWVISMGSCANSGGMYDVYSVVQGVNQIIPVDVHVPGCPPRPEAFLQGVMLLQEKIRREERPARKVLHMAGGTEGTTRPVLVDGVTKSRDTRGPGMEGIAIRGTPVQHPRFWMSRSDEMWRPPAPRHDYPDFGLAGELETIFGGRVAVEQAATDMLTYRCPPELVPEVLRHLKSRSSAPFRRLEDVVCVDESCRRERERFPDFTVNYHLLNFDIPGHLRIKTELMGETPELPSATGVFPAADWYEREAFDMYGIRFAGHPNLRRILMPPDWEGHPLRKEHPFRATEMPPYTTDDARRHQALPASDFFDRIDEETLIINLGPQHPGTHGIIRFILKLDGEEIVDMDTDIGYHHRGAEKIGERQHWNQFIPYTDRIDYLAGVQNNLAYVNSVERLCGITVPDRAITIRVMLAELFRIASHLVWLGTFAADVGAMTPVFYTFTDREKIFDIIEMVTGGRMHPSWFRIGGVTEDLPEGWDGAVKEFLDWMPGRLKEYEDLLKENPIFKARLKGVGVITKDEAMEWGITGPNLRACGMAWDLRKKIPYNGYQHFHFEIPTEEGGDCWARYRIRVEEIRQSLHIVAQCRKEMPAGRWITDDYRYVLPKKRDTLHDIESLIHHFINATRGMAPPRGENYSAIEAPKGENGYFVVSDGLNVPYRVRIKTPSFPHIQALPLMSRGWLVADFLAIIGSIDFVLADLDR", "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 central 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. SIMILARITY: In the N-terminal section; belongs to the complex I 20 kDa subunit family."}
+{"protein": "MGARNSVLRGKKADELEKIRLRPGGKKKYKLKHIVWAANELDRFGLAESLLESKEGCQKILTVLDPLVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVQRHLVAETGTAEKMPNTSRPTAPPSGKNFPVQQVAGNYTHIPLSPGTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDVAHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDINQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTTCQGVGGPGQKARLMAEALKEVMAPAPIPFAAAQQRKTFKCWNCGKEGHSARQWSAPRRQGCWKCGKSGHVMANCPDRQAGFLGIGHWGKKARNFPAAQVPQGLTPTAPPLDPAVDLLEKYMQQGKRQREQRERPYKEVTEDLLRFEQAETPCRETTEDLLHLNSLFGKDQ", "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: [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: [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: [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). FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion (By similarity). Most core are conical, with only 7% tubular (By similarity). The core is constituted by capsid protein hexamer subunits (By similarity). The core is disassembled soon after virion entry (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 (By similarity). Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). The capsid interacts with high affinity with human NONO, promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation (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": "MDIIGQVYCFTGAPHTITCLLREQFINWYIKYKRSENYPAFRELVVMYRLFLALGFLTFINAAGQRCRFTDVERDKGYTGMLLKGRLRKTAGNGRTVELICGRGNHNYTCESGVLKESSPRQARCGCKGILEMLFDMPKEERPSPMYDSVTYDPTPNTPTTVGKDGIWNGVDYRNGSTVKPYCDTGPVINGSSKAVCVSGKWVPTLGVCPKMCSIGSLKENGKFVDVTATTKGDELNPPPREQTLIPIVRKVDKDKVQHGVKVVALCKAEDSTTAAEGVQEFECDNGKWKPEPVPCP", "text": "FUNCTION: Secreted protein which suppresses the host allergic response by inhibiting the interaction of host IL33 with its receptor in order to maintain parasitic infection (PubMed:29045903). Binds to both host IL33 and host nuclear DNA and this dual binding blocks the interaction of IL33 with its receptor, and tethers IL33 within necrotic cells, preventing its release, and blocking allergic response initiation (PubMed:29045903). SUBCELLULAR LOCATION: Secreted Host nucleus."}
+{"protein": "MSLVVPDNFQHILRLLNTNVDGKVKVMFAMTQIKGVGRRYANIVCKKADIDMSKRAGELTTEELERIVTIIQNPSQFKIPSWFLNRQKDINDGKSFQLLANNVDSKLREDLERLKKIQTHRGLRHALDLRVRGQHTKTTGRRGKTVGVSKKK", "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. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS13 family."}
+{"protein": "MAGLEVLFASAAPAITCAQDALVCFLHWEVVTHGYYGLGAGDQPGPNDKKSELLPVEWNSNKDLYVLRYESKDGSRKLLVKAVTVENSMIINVLEHGSQQVSDLTLNLNDYIDSEHLVDFHRVYKNSEELRSRIVSGIITPIHEQWEKANLSPHREFPPATAREVDPLRIHPQHPHTSRQPTWCDPLGPFAVGGEDLDPFGCRRGGMIVDPLRSGFPRALIDPSSGLPNRLPPGAVPPGARFDPFGPIGTSPSGPNPDHLPPPGYDDMYL", "text": "FUNCTION: Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the proteasome inhibitor PI31 family."}
+{"protein": "MNAPLGGIWLWLPLLLTWLTPEVNSSWWYMRATGGSSRVMCDNVPGLVSSQRQLCHRHPDVMRAISQGVAEWTAECQHQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGEVKSCSCDPKKMGSAKDSKGIFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKAVKRFLKQECKCHGVSGSCTLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANERFKKPTKNDLVYFENSPDYCIRDREAGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMTKCGCKFHWCCAVRCQDCLEALDVHTCKAPKNADWTTAT", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (PubMed:20018874). Functions as upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MSKTIPIVDAQHAGSAYQHVPGHPDPQLSAVAKGTPTGEYLRRYWQPVALSADVTDRPQMVRILGEDLVLFRDKAGRPGLLYPRCMHRGTSLYYGHVEEAGIRCCYHGWLFAVDGTCLNQPCEPEGGLRREAARQPWYPVEERYGLVFAYMGPPEKKPVLPRYDILEDLEEGEFIEVISGGFVSYADHVEDPNVPYHWLQNWENIMDPYHVYILHSTFSGIQFAENFKILPRVDFEAVDGGVIYHAWRDLEDGRQLERINSALFPNISAIPMIDLSPGQGRWIGWHVAVDDQHYRGFFAARTRQPGNFAPIKMHNGKSWTELSEQEKQDFPGDFEAQFGQGRVTLHGEEHLATSDHGIALLRRQMKQQIAIVQQGGDPAGVHFNEADALVRIRSGNFYTTSDKTETAAD", "text": "FUNCTION: Degrades exclusively diarylether compounds having carboxyl groups in the 3- or 4-position. Yields a hemiacetal that spontaneously hydrolyzes to phenol and protocatechuate. SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family."}
+{"protein": "MDFLTNLRFTEGISEPYIEIFEQPRQRGTRFRYKCEGRSAGSIPGEHSTDNNKTFPSIQILNYFGKVKIRTTLVTKNEPYKPHPHDLVGKGCRDGYYEAEFGPERQVLSFQNLGIQCVKKKDLKESISLRISKKINPFNVPEEQLHNIDEYDLNVVRLCFQAFLPDEHGNYTLALPPLISNPIYDNRAPNTAELRICRVNKNCGSVKGGDEIFLLCDKVQKDDIEVRFVLGNWEAKGSFSQADVHRQVAIVFRTPPFLGDITEPITVKMQLRRPSDQAVSEPVDFRYLPDEEDPSGNKAKRQRSTLAWQKPIQDCGSAVTERPKAAPIPTVNPEGKLKKEPNMFSPTLMLPGLGTLSSSQMYPACSQMPTQPAQLGPGKQDTLHSCWQQLYSPSPSASSLLSLHSHSSFTAEVPQPGAQGSSSLPAYNPLNWPDEKNSSFYRNFGNTHGMGAALVSAAGMQSVSSSSIVQGTHQASATTASIMTMPRTPGEVPFLRQQVGYRS", "text": "FUNCTION: This transforming protein appears to have a protein-kinase activity. SUBCELLULAR LOCATION: Host cytoplasm."}
+{"protein": "MAERSQNLQDLFLNSVRKQKISLTIFLINGVKLTGIVTSFDNFCVLLRRDGHSQLVYKHAISTIMPSQPVQMFEGEEA", "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 (By similarity). Contributes to long-term survival under nutrient deprivation, to stationary phase-dependent hydrogen peroxide and acid stress resistance and is required for prolonged survival in the intracellular environment of the host macrophage. Therefore, contributes not only to a generalized stress response in stationary phase but also to pathogenesis in mice, allowing the brucellae to adapt to the harsh conditions encountered within macrophages. 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": "MAALKEDRSYGLSCGRVSDGSKVSVFHVKLTDSALRAFESYRARQDSVSLRPSIRFQGSQGHISIPQPDCPAEARTFSFYLSNIGRDNPQGSFDCIQQYVSSHGEVHLDCLGSIQDKITVCATDDSYQKARQSMAQAEEETRSRSAIVIKAGGRYLGKKVQFRKPAPGATDAVPSRKRATPINLASAIRKSGASAVSGGSGVSQRPFRDRVLHLLALRPYRKAELLLRLQKDGLTQADKDALDGLLQQVANMSAKDGTCTLQDCMYKDVQKDWPGYSEGDQQLLKRVLVRKLCQPQSTGSLLGDPAASSPPGERGRSASPPQKRLQPPDFIDPLANKKPRISHFTQRAQPAVNGKLGVPNGREALLPTPGPPASTDTLSSSTHLPPRLEPPRAHDPLADVSNDLGHSGRDCEHGEAAAPAPTVRLGLPLLTDCAQPSRPHGSPSRSKPKKKSKKHKDKERAAEDKPRAQLPDCAPATHATPGAPADTPGLNGTCSVSSVPTSTSETPDYLLKYAAISSSEQRQSYKNDFNAEYSEYRDLHARIERITRRFTQLDAQLRQLSQGSEEYETTRGQILQEYRKIKKTNTNYSQEKHRCEYLHSKLAHIKRLIAEYDQRQLQAWP", "text": "FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968, PubMed:23932780). Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (PubMed:23932780). ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Nucleus, Cajal body Note=Colocalizes with EAF2 to nuclear speckles (PubMed:12446457). Colocalizes with coilin in subnuclear cajal and histone locus bodies (PubMed:12686606). 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(PubMed:23932780). SIMILARITY: Belongs to the ELL/occludin family."}
+{"protein": "MGKEKKTESYNNDSGSYNYRMFKFYNRKFKINEVTPTDDVRDAFCQFAVGGGGGGTDGDSSDGDGSTGVMGAEQLCSFLDDHGESTTVAEAQRLIDEVIRRRHHVTRFTRHGLDLDDFFNFLFYDDLNPPITPHVHQDMTAPLSHYFIYTGHNSYLTGNQLSSDCSEVPVIKALQRGVRVIELDLWPNSTGTDINVLHGRTLTTPVPLMKCLKSIRDYAFSSSPYPVIITLEDHLTPDLQAKVAEMATQIFGQMLYYPESDSLLEFPSPASLLHRIIISTKPPKEYLESRNPIVKQKDNNVSPSSEDETPRTEEIQTLESMLFDQDFESKSDSDQEDEEASEDQKPAYKRLITIHAGKPKGTVKEEMKVVVDKVRRLSLSEQELDRTCSSNSQDVVRFTQRNLLRIYPKGTRFNSSNYKPLIGWTHGAQMIAFNMQGYGKSLWLMHGMFRANGGCGYVKKPNFLMKKGFHDEVFDPRKKLPVKETLKVKVYMGDGWRMDFSHTHFDAYSPPDFYTKMFIVGVPADNAKKKTKIIEDNWYPIWDEEFSFPLTVPELALLRIEVREYDMSEKDDFGGQTCLPVAELRPGIRSVPLYDKKGEKMKSVRLLMRFIFE", "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": "MVNLRLQVAVVGAPTVGKTAFVQMLHSNGTTFPKNYLMTLGCDFIVKEVPVDDDNTVEMIIFDVSGQREYEPMVSSYLQNTAVFIVMYDVSNKVTFEACARWVNQVRTNSKESVGILIANKSDLSDKAEVTDRQGKDLANANKMKFYKISTLRGVGITEPIDEIARHYVDAYQKRIEQLTQMR", "text": "FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B required for both anterograde and retrograde intraflagellar transport. May be involved in cargo loading of the retrograde transport. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MDWRVIVVVSPLLIAATWAAINIGAAAIRQLQDVLGREA", "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": "MNDQYHRAARDGYLELLKEATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYLDSIAAKQSSLNPKLVGKLKDKAFREAERRIRECAKLQRRHHERMERRYRRELAERSDTLSFSSLTSSTLSRRLQHLALGSHLPYSQATLHGTARGKTKMQKKLERRKQGGEGTFKVSEDGRKSARSLSGLQLGSDVMFVRQGTYANPKEWGRAPLRDMFLSDEDSVSRATLAAEPAHSEVSTDSGHDSLFTRPGLGTMVFRRNYLSSGLHGLGREDGGLDGVGAPRGRLQSSPSLDDDSLGSANSLQDRSCGEELPWDELDLGLDEDLEPETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERPPALEDTEL", "text": "FUNCTION: Plays a role in pre-mRNA splicing by regulating the release and transfer of U4/U6.U5 tri-small nuclear ribonucleoprotein (tri- snRNP) complexes from their assembly site in Cajal bodies to nuclear speckles, thereby contributing to the assembly of the pre-catalytic spliceosome on target pre-mRNAs (PubMed:34023904). May also participate in recycling of snRNPs back to Cajal bodies during splicing (PubMed:34023904). Plays a role in regulating MAGI2-mediated endocytosis (PubMed:24608321). Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal development and maintenance of cochlear hair cell bundles. Required for normal hearing. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein Cell projection, cilium Nucleus speckle Nucleus, Cajal body Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Photoreceptor inner segment Note=Detected at the tip of cochlear hair cell stereocilia. Recruited to the cell membrane via interaction with CDH23 or PCDH15 (By similarity). In photoreceptor cilia, detected predominantly at the cilium base (By similarity). Expressed in the pericentriolar region of the centrosome (By similarity)."}
+{"protein": "MNHSNQMHHDNHESHNHHSGHAHHHGNFKVKFFVSLIFAIPIILLSPLMGINLPFQFTFPGSEWVVLILSTILFFYGGKPFLSGGKDEIATKKPGMMTLVALGISVAYIYSLYAFYMNNFSSATGHTMDFFWELATLILIMLLGHWIEMNAVGNAGDALKKMAELLPNSAIKVMDNGQREEVKISDIMTDDIVEVKAGESIPTDGIIVQGQTSIDESLVTGESKKVQKNQNDNVIGGSINGSGTIQVKVTAVGEDGYLSQVMGLVNQAQNDKSSAELLSDKVAGYLFYFAVIVGVISFIVWMLIQNDVDFALERLVTVLVIACPHALGLAIPLVTARSTSIGAHNGLIIKNRESVEIAQHIDYVMMDKTGTLTEGNFSVNHYESFKNDLSNDTILSLFASLESQSNHPLAISIVDFAKSKNVSFTNPQDVNNIPGVGLEGLIDNKTYKITNVSYLDKHKLNYDDDLFTKLAQQGNSISYLIEDQQVIGMIAQGDQIKESSKQMVADLLSRNITPVMLTGDNNEVAHAVAKELGISDVHAQLMPEDKESIIKDYQSNGNKVMMVGDGINDAPSLIRADIGIAIGAGTDVAVDSGDIILVKSNPSDIVHFLTLSNNTMRKMVQNLWWGAGYNIVAVPLAAGALAFVGLILSPAVGAILMSLSTVIVAINAFTLKLK", "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": "MGTKAKVGSTELLLFTSMILCSLALGRGAVQTYEPVVRVPENNPAKLSCSYSGFSSPRVEWKFTHGDIRGLVCYNNKITASYENRVTFSDTGITFHSVTRKDTGMYTCMVSDEGGNTYGEVTVQLIVLVPPSKPTINVPSSVTIGTRAVLTCSERDGSPPSEYKWFKDGVEMPLEPKSNRAFSNSSYTLNQKTGELIFDPVSASDTGDFTCQAQNGYASPVKSDTVHMDAVELNVGGIVAAVFVTLILLGALIFGIWFAYSRGYFDRAKKGTSNKKVIYSQPNARSDGEFRQTSSFLV", "text": "FUNCTION: Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration. Involved in platelet activation. SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Single-pass type I membrane protein Note=Localized at tight junctions of both epithelial and endothelial cells. SIMILARITY: Belongs to the immunoglobulin superfamily."}
+{"protein": "MTLSPEKQHVRPRDAADNDPVAVARGLAEKWRATAVERDRAGGSATAEREDLRASGLLSLLVPREYGGWGADWPTAIEVVREIAAADGSLGHLFGYHLTNAPMIELIGSQEQEEHLYTQIAQNNWWTGNASSENNSHVLDWKVSATPTEDGGYVLNGTKHFCSGAKGSDLLFVFGVVQDDSPQQGAIIAAAIPTSRAGVTPNDDWAAIGMRQTDSGSTDFHNVKVEPDEVLGAPNAFVLAFIQSERGSLFAPIAQLIFANVYLGIAHGALDAAREYTRTQARPWTPAGIQQATEDPYTIRSYGEFTIALQGADAAAREAAHLLQTVWDKGDALTPEDRGELMVKVSGVKALATNAALNISSGVFEVIGARGTHPRYGFDRFWRNVRTHSLHDPVSYKIADVGKHTLNGQYPIPGFTS", "text": "FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner. FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner. In (PubMed:7961424) DBTO (dibenzothiophene-5-oxide) was reported not to be a substrate, in (PubMed:7574582, PubMed:9634856, PubMed:8824615, PubMed:9308179) it is reported to be a substrate (PubMed:7961424, PubMed:7574582, PubMed:9634856, PubMed:8824615, PubMed:9308179). Can also use benzyl sulfide and benzyl sulfoxide as substrates, although benzyl sulfoxide is a poor substrate (PubMed:8824615). The pathway substrate specificity has been augmented using mutagenesis, however no mutations allowed use of alkylated thiophenes (PubMed:11823208). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DszC flavin monooxygenase family."}
+{"protein": "MDSEFFQPVYPRHYGECLSPTSTPSFFSTHMCTILVAIVVLIIIIIVLIYLFSSRKKKAAAPAIEEEDIQFINPYQDQQWAGATPQPGTSKPAGATTGNVGKPITDRPATDRPVTNNPVTDRLIMATGGPAAASAPSAELYTTATTQNTASQTMPAVEALRQRSTYTHKDLENSL", "text": "FUNCTION: Inner envelope protein involved, through its interaction with host dynein, in the intracellular microtubule-dependent transport of viral capsid toward viral factories (By similarity). Seems to induce caspase-3 activation and apoptosis (By similarity). Plays a role in virion morphogenesis by recruiting and transforming the host ER membranes into the precursors of the viral envelope (By similarity). Involved in virus attachment to the host cell (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Host cytoplasm, host cytoskeleton Host endoplasmic reticulum membrane Note=Localizes to the viral factory at 16 hpi. Host DYNLL1 and viral p54 interact at the microtubular organizing center (By similarity). Found in the inner envelope of the virus (By similarity). SIMILARITY: Belongs to the asfivirus envelope protein p54 family."}
+{"protein": "MPGPQGGTGAPTMSLGKLSPVGWVSSSHGKRRLTADMISPPLGDFRHTMHVGRGGDVFGDTSFLSNHGGRSGNTHRSPRSFLARKLQQVRRVGVPPRRMASPAAPSPAPPPISPIIKNAISLPQLNQATYDSLVMGKLSFDSTPASSTDGHSGYGLESGFCTISRLPRVEKHSNRDRDRDPDHSQDREQSSFPSEPTPNPELRRSDSLLSFRFDLDLGPSLLSELLGVMSLSEAPAAETPVPTANPPAPAANPAPTAKPPAHAITTLDAVTSLPASAVTSLPAPAAASSPSRGHFPNGVTSVLGPAAEAKPSPVGEGPQVPSNMTFDRHGASWGASRASWGASRASRHYTEMDARRELAGVLPQVHGSWESLNEDWSTPPASVRAPVPTSVQVNAFEFADAEEDDEVKV", "text": "FUNCTION: Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts (By similarity). SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the BORG/CEP family."}
+{"protein": "MTTSASLERTPSKRDRDRERDNSSGLGSAGSLPASPQSAITVSPSSPATPKRPLRTSTPSLERKREREDREDREDRKERQERHERDRDHERFAAVFSTASTTVPTNTSSSSGLAPEQLRIPTGAAAFSGFPGLHSMSSLMLPSSAAVAAAAAAPFLPWSPILLPPWNHALLPAAFYPAALRNALPGLFDAKVPSSQRSGFHISDILNLEGSELKNAAAAAAAAAHHGSDLSHHSASESTSGHRGQGSHTSPSALSPTPAGVSADEHHNGSGTGGGAGEADHHSTTEHHAPPSHPQQQHPHHQQHHHPHLLLPQQHHQQAVAPLPLAHHQSGEAQSHAHANAAAAHLLASHNAAAAAAVAAGQYLPNLPKNFPGSFGDEMSSYHHMAQTMLQHSGRSAWIKENELYGTQQPASPDSTSPVTSEVSYTYIGSNCQTSPALSGDYKSYSRSADSDALSVGDALHTLHGSSGNGSAGGAPTAHALHNNNNNTTNNNNHSLKAEGINGAGSGHDDSLNEDGIEEDIDDVDDADGSGGGDANGSDGLPNKKRKRRVLFTKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKTKRAQNEKGYEGHPGLLHGHATHPHHPSALPSPRRVAVPVLVRNGKPCLGDSSKLGADCVSVSSATATAMQNAAAHHLVALNGAAAYQHAAAAAAGLHAHAHAHAHAHGHGHPHAHAQRAAWWP", "text": "FUNCTION: Probable transcriptional regulator involved in the regulation of the proneural AS-C genes and the neurogenic genes of the enhancer of split complex. Could specifically activate proneural genes in the ventral-most neuroectoderm. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NK-2 homeobox family."}
+{"protein": "MIKLNIDGSEIEVSEGSTVYQACTQAGKEIPHFCYHERLKIAGNCRMCLVEMEKSPKPIASCAMPVSNGMVIHTDTPMVKKAREGVMEFLLINHPLDCPICDQGGECDLQDQAFRYGKGTNRFHENKRSIKDKYMGPLIKTAMTRCIQCTRCIRFANDIAGIEEMGAIHRGEHMEVTSYLEQTLDSEMSGNMIDICPVGALNSKPYAFKARKWELKHTASIGVHDAEGSNIRIDSRGDEVMRILPRVNEEINEEWLSDKNRFSYDGLKYQRLDLPYIRKNGKLVEASWSEALKTIADKIKSVKPEKIAAIAGSLVSVEAMFMLKTLLQKLGSNNYSVNQFDYKFDTTQRGNYLFNTTIAGVEKADLCLLIGANLRQIAPVLNSRIGQRVRAGSLKVARIGEGHNQTYRIQDLGSDIKIIEELAIGTHEFTKALKAAKYPMIIVGDGVYARDDGYAILSLIHKIVAEYNIMRDDFQGFNMLHNHASIVGGLDIGFNTPIKLEELELTYLLGADELPFDKLKSAFIIYQGHHGDSGAANADVILPAAAYTEQSGIYVNLEGRPQIAEKAVAPVGVAKEDIEIIKELAGSLKIDIGMDNLQEVRVRLAKEYKIFANIDKIVESKFAKFSFKDKLSKEPITMGPINYYMTDVISKNSVTMAKCVEAKEKRNERAA", "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 75 kDa subunit family."}
+{"protein": "MSGRTVPHAHPATAEYEFANPSRLGEQRFGEGLLPEEILTPTLYHGYYVRPRAARAGEGGRAGASELRLSEGKFQAFLDVSHFTPDEVTVRTVDNLLEVSARHPQRLDRHGFVSREFCRTYVLPADVDPWRVRAALSHDGILNLEAPRGGRHLDTEVNEVYISLLPAPPDPEEEEEVARVEP", "text": "FUNCTION: May regulate the kinase DMPK. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes to nuclear foci. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MPKKKTGPRKKAENRREREKQLRASRSTVDLAKHPCNASMECDKCQRRQKNRAFCYFCNSVQKLPICAQCGKTKCMMKSSDCVIKHAGVYSTGLAMVGAICDFCEAWVCHGRKCLSTHACACPLTDAECVECERGVWDHGGRIFSCSFCHNFLCEDDQFEHQASCQVLEAETFKCVSCNRLGQHSCLRCKACFCDEHTRSKVFKQEKGKQPPCPKCGHETQETKDLSMSTRSLKFGRQTGGEEGDGASGYDAYWKNLSSDEYADTGYHDDEEEDEAEDEEEEEDGKDSDAESSDLFTSLNLGRTYASGYAHYEEQEN", "text": "SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Chromosome, centromere Note=Predominantly expressed in nucleolus. In mitosis associated with centromeres and concentrated at the midbody in cytokinesis (By similarity). SIMILARITY: Belongs to the NOA36 family."}
+{"protein": "MTVAITQTGPALQEFVERHQRLFVLSGAGCSTDSGIPDYRDLQGGWKRPQPVTFQAFMGELSTRQRYWARSLVGWPRFGLARPNATHHALAALEARGQLELLLTQNVDRLHQAAGSQAVIDLHGRLDVVRCMGCEQRMPRTEFQLLLERDNPGWADLEAAQAPDGDADLDNVAFDNFVVPACPACGGVLKPDVVFFGENVPRERVERAFAHLQAADAVLVVGSSLMVYSGFRFVQAAARAGLPIAALNFGRTRADDLLSLKVEQSCAQALAFLQQPPDPLHTATARYHSARSA", "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 II subfamily."}
+{"protein": "MARRAAAGLLRRHLGPLAAGETLQARGMYPKQYGAANHAFSRFYSIQGQQRSLYGFRTNVETDDTQQSARMNFEVQKRSFSSAAAHVQRNPAYSVLNSDDVSYFKSILGDSGVVQDEDRVSVANMDWMGKYKGSSQLLLLPKSTAEVSKILSYCNSRRLAVVPQGGNTGLVGGSVPVYDEVIISLGGMDKIITFDNVNGILTCEAGCVLENLSSYVENKGFIMPLDLGAKGSCHIGGNISTNAGGLRFIRYGSLHGSVLGLEVVLADGTVLDMLTTLRKDNTGYDLKHLFIGSEGSLGIVTKIAILTPAKLPSTNVAFLSCNDYISCQKLLLAARRSLGEILSAFEFMDRHCINLAMKYLEGVHNPLPVSPYNFYVLIETTGSDESYDKAKLEAFLLRSMEDGLVADGVIAQDISQASNFWRIREGISEASVKVGAVYKYDLSIPVEKLYDIVEEMRSRVGDMGQVLGYGHLGDGNLHLNILSTKYSDKMLAQIEPFVYEWTSKQRGSISAEHGLGLMKADKIHYSKSSEAVQLMTSIKKLLDPNSILNPYKVLPQSVL", "text": "FUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha- ketoglutarate. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type 4 family."}
+{"protein": "MAASVMLSSVTLKPAGFTVEKMSARGLPSLTRASPSSFRIVASGVKKIKTDKPFGVNGSMDLRDGVDASGRKGKGYGVYKFVDKYGANVDGYSPIYNEDEWSASGDVYKGGVTGLAIWAVTLAGILAGGALLVYNTSALAQ", "text": "FUNCTION: Associated with the oxygen-evolving complex of photosystem II. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane. Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the psbR family."}
+{"protein": "MNYPAVAKELLTLLGGKSNITALAHCATRLRLAVADEQKIDEQAIDNLEGVKGQFKVAGQYQIIFGSGIVNQVYAEMAKLTGMSEMSTNDVASAGAEKQNIVQPAVKGLSDIFVPIIPAIVAGGLLMGIYNLLTAQGLFIDGKSLIEANPGLTDLANMINTFANAPFVYLPILLAFSASKKFGGNPYLGAALGMLMVHPDLLNGWGFGGASVSGNIPVWNILGFEIQKVGYQGSVLPVLVSAFILAKVELGLRKVIPSVLDNLLTPLLAIFIAGLLTFTVVGPFTRDIGFLLGDGLNWLYNTAGFVGGAVFGLIYAPFVITGMHHSFIAIETQLLADIATTGGTFIFPIAAMSNVSQGAAALAVGVMSKDKKMKGIAIPSGVTGLLGITEPAMFGVNLKLRYPFIAAVCAAALSSAFITMFNVKAQALGAAGLPGIISITPDKIGYYIAGMVIAFLTAFVLTIVLGIGDRAKVGKKAAA", "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 sucrose transport. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "METPQPDKTGMHILLKLASLVVILAGIHAAADIIVQLLLALFFAIVLNPLVTWFIRRGVQRPVAITIVVVVMLIALTALVGVLAASFNEFISMLPKFNKELTRKLFKLQEMLPFLNLHMSPERMLQRMDSEKVVTFTTALMTGLSGAMASVLLLVMTVVFMLFEVRHVPYKMRFALNNPQIHIAGLHRALKGVSHYLALKTLLSLWTGVIVWLGLELMGVQFALMWAVLAFLLNYVPNIGAVISAVPPMIQVLLFNGVYECILVGALFLVVHMVIGNILEPRMMGHRLGMSTMVVFLSLLIWGWLLGPVGMLLSVPLTSVCKIWMETTKGGSKLAILLGPGRPKSRLPG", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family."}
+{"protein": "MTEAGKLPLPLPPRLDWFVHTQMGQLAQDGVPEWFHGAISREDAENLLESQPLGSFLIRVSHSHVGYTLSYKAQSSCCHFMVKLLDDGTFMIPGEKVAHTSLDALVTFHQQKPIEPRRELLTQPCRQKDPANVDYEDLFLYSNAVAEEAACPVSAPEEASPKPVLCHQSKERKPSAEMNRITTKEATSSCPPKSPLGETRQKLWRSLKMLPERGQRVRQQLKSHLATVNLSSLLDVRRSTVISGPGTGKGSQDHSGDPTSGDRGYTDPCVATSLKSPSQPQAPKDRKVPTRKAERSVSCIEVTPGDRSWHQMVVRALSSQESKPEHQGLAEPENDQLPEEYQQPPPFAPGYC", "text": "FUNCTION: May be a modulator of the apoptotic response through its ability to affect mitochondrial stability (By similarity). Adapter protein involved in tyrosine kinase and CD28 signaling. Seems to affect CD28-mediated activation of the RE/AP element of the interleukin-2 promoter. SUBCELLULAR LOCATION: Cytoplasm. Nucleus."}
+{"protein": "MSQNVYQFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPFLIANTKQLMGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMPGSRREVKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHNMEWLAKHSVELDSQGRIIAPEGSDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWLEV", "text": "FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate."}
+{"protein": "MAMLVTNLSSSSFCFFSSPHLQNQKEIRSGVRVRKYVIFNRASLRTVSDCVDSITTFDRSVTDANTQLRRFCESGNLENAVKLLCVSGKWDIDPRTLCSVLQLCADSKSLKDGKEVDNFIRGNGFVIDSNLGSKLSLMYTNCGDLKEASRVFDEVKIEKALFWNILMNELAKSGDFSGSIGLFKKMMSSGVEMDSYTFSCVSKSFSSLRSVHGGEQLHGFILKSGFGERNSVGNSLVAFYLKNQRVDSARKVFDEMTERDVISWNSIINGYVSNGLAEKGLSVFVQMLVSGIEIDLATIVSVFAGCADSRLISLGRAVHSIGVKACFSREDRFCNTLLDMYSKCGDLDSAKAVFREMSDRSVVSYTSMIAGYAREGLAGEAVKLFEEMEEEGISPDVYTVTAVLNCCARYRLLDEGKRVHEWIKENDLGFDIFVSNALMDMYAKCGSMQEAELVFSEMRVKDIISWNTIIGGYSKNCYANEALSLFNLLLEEKRFSPDERTVACVLPACASLSAFDKGREIHGYIMRNGYFSDRHVANSLVDMYAKCGALLLAHMLFDDIASKDLVSWTVMIAGYGMHGFGKEAIALFNQMRQAGIEADEISFVSLLYACSHSGLVDEGWRFFNIMRHECKIEPTVEHYACIVDMLARTGDLIKAYRFIENMPIPPDATIWGALLCGCRIHHDVKLAEKVAEKVFELEPENTGYYVLMANIYAEAEKWEQVKRLRKRIGQRGLRKNPGCSWIEIKGRVNIFVAGDSSNPETENIEAFLRKVRARMIEEGYSPLTKYALIDAEEMEKEEALCGHSEKLAMALGIISSGHGKIIRVTKNLRVCGDCHEMAKFMSKLTRREIVLRDSNRFHQFKDGHCSCRGFW", "text": "FUNCTION: Plays a major role in single RNA editing events in chloroplasts. Acts as a site-recognition transacting factor involved in the edition of the unique site (corresponding to cytidine-488) of rpoC1, which is a plastid-encoded subunit of the chloroplast DNA- directed RNA polymerase. May provide the catalytic activity for editing site conversion (PubMed:24194514). Involved in leaf vasculature patterning (PubMed:18643975). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. PCMP-H subfamily."}
+{"protein": "MAMAEFVFCRPLFGLAIVLLVAPIDAAQRHTASDNPSTYNIGGVLSNSDSEEHFSTTIKHLNFDQQYVPRKVTYYDKTIRMDKNPIKTVFNVCDKLIENRVYAVVVSHEQTSGDLSPAAVSYTSGFYSIPVIGISSRDAAFSDKNIHVSFLRTVPPYYHQADVWLEMLSHFAYTKVIIIHSSDTDGRAILGRFQTTSQTYYDDVDVRATVELIVEFEPKLESFTEHLIDMKTAQSRVYLMYASTEDAQVIFRDAGEYNMTGEGHVWIVTEQALFSNNTPDGVLGLQLEHAHSDKGHIRDSVYVLASAIKEMISNETIAEAPKDCGDSAVNWESGKRLFQYLKSRNITGETGQVAFDDNGDRIYAGYDVINIREQQKKHVVGKFSYDSMRAKMRMRINDSEIIWPGKQRRKPEGIMIPTHLRLLTIEEKPFVYVRRMGDDEFRCEPDERPCPLFNNSDATANEFCCRGYCIDLLIELSKRINFTYDLALSPDGQFGHYILRNNTGAMTLRKEWTGLIGELVNERADMIVAPLTINPERAEYIEFSKPFKYQGITILEKKPSRSSTLVSFLQPFSNTLWILVMVSVHVVALVLYLLDRFSPFGRFKLSHSDSNEEKALNLSSAVWFAWGVLLNSGIGEGTPRSFSARVLGMVWAGFAMIIVASYTANLAAFLVLERPKTKLSGINDARLRNTMENLTCATVKGSSVDMYFRRQVELSNMYRTMEANNYATAEQAIQDVKKGKLMAFIWDSSRLEYEASKDCELVTAGELFGRSGYGIGLQKGSPWTDAVTLAILEFHESGFMEKLDKQWIFHGHVQQNCELFEKTPNTLGLKNMAGVFILVGVGIAGGVGLIIIEVIYKKHQVKKQKRLDIARHAADKWRGTIEKRKTIRASLAMQRQYNVGLNSTHAPGTISLAVDKRRYPRLGQRLGPERAWPGDAADVLRIRRPYELGNPGQSPKVMAANQPGMPMPMLGKTRPQQSVLPPRYSPGYTSDVSHLVV", "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. 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": "MIVSQYLSALTFVLLLFKESRTWSYHASTEMMTFEEARDYCQKTYTALVAIQNQEEIEYLNSTFSYSPSYYWIGIRKINGTWTWIGTNKSLTKEATNWAPGEPNNKQSDEDCVEIYIKREKDSGKWNDEKCTKQKLALCYKAACNPTPCGSHGECVETINNYTCQCHPGFKGLKCEQVVTCPAQKHPEHGHLVCNPLGKFTYNSSCSISCAEGYLPSSTEATRCMSSGEWSTPLPKCNVVKCDALSNLDNGVVNCSPNHGSLPWNTTCTFECQEGYKLTGPQHLQCTSSGIWDNKQPTCKAVSCAAISHPQNGTVNCSHSVVGDFAFKSSCHFTCAEGFTLQGPTQVECTAQGQWTQRVPVCEVVRCSRLDVSGKLNMNCSGEPVLGTECTFACPERWTLNGSVVLTCGATGHWSGMLPTCEAPTVSQTPLAVGLSTAGVSLVTIPSFLFWLLKRLQKKAKKFSPASSCSSLKSNGCYSTPSKLI", "text": "FUNCTION: Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the selectin/LECAM family."}
+{"protein": "MEPRRAAPRLPSQASSSVGAGSAAELVYHLAGALGTELQGLARRFGPDAAAGLVPLVVRALELLEKAAVGPAPDSLQVSAQQAEVELRRLREENQRLRQELGSGPQEERALLRQLKEVTDRQRDELRAHNRDLQRRSQETEALQEQLQRLLLINSELRHKLAAVQTQLRAAQDRERERQIAQDGSSQLAKEQSLEPDAATSDDPVDTQKQPGNLPEAVQCGFSREELKQILQERNELKANVFLLKEELAYFQRELLTDHRVPGLLLEAMKVAVKKQRRKIKAKMLGTPEEAESSEDEDGSWLLLSNDKEDVPLVPESRIQNFFGLWYRGETEAPEAETSNPASSSLQKGEETPQQPHLQPVNSPPAPNS", "text": "FUNCTION: Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes. SUBCELLULAR LOCATION: Late endosome membrane Lysosome membrane Cytoplasmic vesicle, phagosome membrane Note=Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7A is necessary for its recruitment to phagosomes."}
+{"protein": "MALKLLGFNQDATCFSVISSNKGVTIYNCDPFGKCFELEKSTSNDEELDFLVEMLFSTSLIAVVDKTIGASKRKKLKIVNTKRKATICELTFPHEIMDVIMNRKIICVVLKSDQIFVYDISCMKLLRTIDVRGEKLKSTSKFRNSEAVGDIGVRVSLSTDNNSILCYSSYSKSDKENAPLNDIVVFDALKCIQINVLPAVHQSNIVCIACSPDGMLMATASEKGTIIRVFKTIDTENDEPILVNEFRRGSRPSRISEMKFNHDNTLLACVGESDTIHIFALPVTTTEADANEDDTLQQSSHSLSSSINGLQYISKGLANRFGKIIVSKIPTQSQQRHVAYIKIPENAKYRIGFPKDTTNTIHICGEDGNYLVYSIPRNEVGPCTLVKSNTFD", "text": "FUNCTION: Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Note=Vacuolar and perivacuolar punctate structures. SIMILARITY: Belongs to the WD repeat PROPPIN family."}
+{"protein": "MDVTIYLRWSAYATIASFIFMVLAFVFRWGFRFRLVGVTSFMTVLTIGIFGLGLGMFDRPTVEGSVKFNRVYDNGANQIVISVPVTVSATEVEATLKQAANNYFSLGRISTDGKEQMVIRARTLIHPQPGLTKPLYLGSAYRTLGTKENDQIEIKLDRKALRELERNQAA", "text": "SIMILARITY: Belongs to the ycf51 family."}
+{"protein": "MKFVVFLCAIAAVVATIQGQEQQQQQQLPATIDHDQVKPFPQPQPVTISERAAMKFKPQLHVVDGCHPYPAVNDAGETGGGLKTTGSPTAGCKGSGWGSQVYGRSTWHRDVWAIMYSWYFPKDSPSTGLGHRHDWEHVIVWISNPDVPNPTILAVTPSAHSGYSKYAPPSADTVDGTSIKVRYESTYPMNHATDVTTEAGAFQDLIMWDQMTDAARNALNTVSFGDANVPMNDGNFVPKLDKAWPF", "text": "FUNCTION: Secreted effector that contributes strongly to virulence during infection by P.capsici. Causes large necrotic areas in both host C.annuum and non-host N.benthamiana. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Necrosis inducing protein (NPP1) family."}
+{"protein": "MGAAGSKLEKALGDQFPEGERYFGFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVADAEENLMTCLADLFSQISSQKKKTGVIAPKRFVQRLKKQNELFRSYMHQDAHEFLNYLLNEVVDILEKEAKATKTEHETSSSSSPEKIANGLKVPQANGVVHKEPIVTWVHNIFQGILTNETRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRFKYIEQLGRYKKLSYRVVFPLELKLSNTVEPYADVEYSLFAVVVHVGSGPNHGHYVSLVKSHNHWLFFDDENVEMIEESAVQTFFGSSQEYSSNTDHGYILFYESLGPTK", "text": "FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Required for the correct development of pollen. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the peptidase C19 family."}
+{"protein": "MFDFIIDFETMGSGEKAAVIDLAVIAFDPNPEVVETFDELVSRGIKIKFDLKSQKGHRLFTKSTIEWWKNQSPEARKNIAPSDEDVSTIDGIAKFNDYINAHNIDPWKSQGWCRGMSFDFPILVDLIRDIQRLNGVSENELDTFKLEPCKFWNQRDIRTRIEALLLVRDMTTCPLPKGTLDGFVAHDSIHDCAKDILMMKYALRYAMGLEDAPSEEECDPLSLPTKR", "text": "FUNCTION: 3'-5' exonuclease that preferentially uses ssDNA as substrate. Plays a role in group I intron homing. May play a role in the final step of host DNA degradation, by scavenging DNA into mononucleotides."}
+{"protein": "MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEINAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFPWVREKLKKAREEAMTDLPAGDRLTGIPSHILNSSPSDRQINQLAQRLGPEWEPMVLSLGLSQTDIYRCKANHPHNVQSQVVEAFIRWRQRFGKQATFQSLHNGLRAVEVDPSLLLHMLE", "text": "FUNCTION: Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis (PubMed:9044836, PubMed:15073321, PubMed:16652156, PubMed:17159900, PubMed:17289572). Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the tumor necrosis factor-mediated signaling pathway (PubMed:8985253). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MIRVNNVCKKYHTNSGWKTVLKNINFELQKGEKIGILGRNGAGKSTLIRLMSGVEPPTSGTIERSMSISWPLAFSGAFQGSLTGMDNLRFICRLYDVDPDYVTRFTKEFSELGDYLYEPVKKYSSGMKARLAFALSLSVEFDCYLIDEVIAVGDSRFAEKCKYELFEKRKDRSIILVSHSPSAMKSYCDNAVVLENGIMHHFEDMDKAYQYYNETQK", "text": "FUNCTION: Putative ATP-binding protein, and an energy-coupling component of capsule polysaccharide export apparatus. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MNLLPKTREEFAQTDYWNEFFKKRGEKAFEWYGEYLDLCDHIHKYIKPVDKILMLGCGNSKLSMDMYDSEYRDITNIDISPVAVKKMLEQNARTRPDMKFLQMDATAMTFPDESFSVALDKGTLDALFVDDAPETKAVVENYFKEILRTMRNGGRYFCVSLLQEHILNFLVEFLPRHNCMLRIVHCLGVEQANKEKNADDAMKMPVFVVIATKFKSLPMPILEFGLGNDKMQRFTESSELSNAVRSVQKAALVFNGLARSSIAGHDEVTLDLYRPSENTPRYSIYILDQAAARGLNKYAAFIVPQGREIEWLFGTPSGRKKLQASAKFQRLAVVTLHRDQVYNTLEEVQAELGDTVFSLAPHGHIKQIPYLSLGSDVGKRETLISGFSKISGEFRIEEVEAGGKTLRRLIFLSNQFVVQSEALVKTIKIKGKKERKKIDFGYLACQHHLYMSVGVQLATTLQNPKKDVQKDVLVIGLGGGGLCSFLHAALPQSRITAVEIDPIMLEVAEQYFELKQDKRFHVVIDDGLAFVERCRNEDIHFDAVLFDVDSKDLSLGMSCPPQGFLAHDVLLHIKEIIGPKGLFMLNLVCRDETLKTEAIANLQKVFPAVCSYKLEEDINEVVYCANDEKYKTVEHWQKAMGTAGRGLNTTIKEHKLASEDPLEVAEFLSELKL", "text": "FUNCTION: Dual methyltransferase. It catalyzes N-terminal methylation of target proteins via its C-terminus. It catalyzes dimethylation on lysine residues of target proteins via its N-terminus. SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "MEGISITKLLVIAVLIVLLFGTNKLRTLGSDLGAALKGFKKAMNDETPAAKKSDGAEAAPRVENKE", "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. TatE shares overlapping functions with TatA. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatA/E family. TatE subfamily."}
+{"protein": "DDCIVVEYYIVTDSAFTKRFKSNSALTNYVTVMFTGVQNLMDTLELGIGVRLLGVTTFTEKTEPSFIKDNLIPGPPAAFDPDVLISAMSKYYCNHQTGLAKDTDLIFLITARGMGDPREDGTVDINTAGIANSAGVCKPCFKSGIATDDSDYNERVDTLAHESVHLLGSPHDGEGPNLVSLEGSPGAANCPAKAGYIMGNRNDKNKYKFSPCTKKCVEYLLSKPTASCIFQQCRD", "text": "FUNCTION: Acts as a metalloprotease. Penetrates intact tissue and specifically cleaves the vesicle-associated membrane protein 2 (VAMP2) (part of the SNARE complex) involved in pancreatic secretion, thus disrupting the normal vesicular traffic (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family."}
+{"protein": "MSAELAPPPPLAPGGLRVTALGGISEIGRNMTVFEHLGRLLIVDCGVLFPGHDEPGVDLILPDLRHIEDRLDEIEALVVTHAHEDHIGAIPFLLKLRPDIPVVGSKFTIALVREKCREHRLKPKFVEVAERQSSQHGVFECEYFAVNHSIPGCLAVAIHTGAGTVLHTGDIKLDQLPLDGRPTDLPGMSRLGDAGVDLFLCDSTNSEHPGVSPSESEVGPTLHRLIRGAEGRVIVACFASNVDRVQQIIDAAVALGRRVSFVGRSMVRNMGIARELGYLKVDDSDILDIAAAEMMPPDRVVLITTGTQGEPMAALSRMSRGEHRSITLTSGDLIILSSSLIPGNEEAVYGVIDSLSKIGARVVTNAQARVHVSGHAYAGELLFLYNGVRPRNVMPVHGTWRHLRANAALAASTGVPPENIVLAENGVSVDLVAGRASISGAVTVGKMFVDGLITGDVGDATLGERLILSSGFVSITVVVHRGTGRPAGPAHLISRGFSEDPKALEPVAQKVERELEALAADNVTDPTRIAQAVRRTVGKWVGETYRRQPMIVPTVIEI", "text": "FUNCTION: An RNase that has endonuclease and 5'-3' exonuclease activity. The 5'-exonuclease activity acts on 5'-monophosphate but not 5'-triphosphate ends. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Plays the major role in pre-23S rRNA maturation, and a minor role in processing of pre- 5S and pre-16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily."}
+{"protein": "MADGFPWLTAIILLPLVASAFIPLLPDKEGKLVRWYALGVGIADFVLMCYTFWHHYDTSSATFQLVEKYDWLPQIGFSWAVSVDGISMPLVLLAGFVTTLSMLAAWQVNLKPRLFYFLMLVLYSAQIGVFVAQDLLLFFIMWELELVPVYLLVSIWGGQKRRYAATKFLLYTAAASIFILIAGLAMALYGDNTTFDIVELGAKNYPLALELLLYAGLLIAFGVKLAIFPLHTWLPDAHGEASAPVSMILAGVLLKMGGYGLIRLNLELLPDAHIYFAPVLATLGVINIIYGGLNSFAQTHMKRRLAYSSVSHMGFVLLGIASFTDVGVSGAMLQMLSHGLIAAVLFFLAGVTYDRTHTMAMDNLGGIGQAMPKVFALFTAGTMASLALPGMSGFVSELKVFIGVTTSDIYSPTFCTVMVFLAAVGVILTPIYLLSMLRQVFYGTGAELSCNINNGAYQNQEDEGTACFGTDCLLPGEAVYRDASVREVFIAVSFLVLIIGVGVYPKIATQLYDVKTVAVNTQVRQSYTQIAQSNPQIYAKGFFTPQIVEPEVMAVSGVIK", "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 (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family."}
+{"protein": "MTTLSDYVDFSQDSFKYAALSIAFNPIFWNVVARAEYRSHFLTRIFGSPYRGCYFLAITIFSLGILRDHIYQQALEDQPYYAPVHQPVLGGALFAVGSVLVLSSMYALGVTGTYLGDYFGILMDAPVTGFPFNVTGSPMYWGSTLNFLGVALYKGKVAGILLTALVFVLYWFALKWEDPFTAEIYAKRERERAKSKRGGKNQ", "text": "FUNCTION: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family."}
+{"protein": "MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLVCTFSLTLTWLYFWWGVHNDYDEFNWYLYNRMGYWSDWSVPILVTSAAAFTYIAGLLVLALCHIAVGQQLNLHWIHKMGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGTAPFLHIGALVAITALSWIVAGQFARAERSSSQLTILCTFFAVVFTFYLIPLTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQRLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELAKGNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGFPQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHTLSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISDGVEVSDELSVCSDSSYDTYANANSTATPVGPRNAGSRAKTVTEQSGH", "text": "FUNCTION: Glycerophosphodiester phosphodiesterase that promotes neurite formation and drives spinal motor neuron differentiation (PubMed:17275818, PubMed:18667693). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (By similarity). May contribute to the osmotic regulation of cellular glycerophosphocholine (PubMed:18667693). SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Cytoplasm, perinuclear region Cell projection, growth cone. SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family."}
+{"protein": "MGLLRIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRAKLERAIARHEVREIEQRHTMDGPRQDATLDEEEDIIIIYNRVPKTASTSFTNIAYDLCAKNRYHVLHINTTKNNPVMSLQDQVRFVKNITTWNEMKPGFYHGHISYLDFAKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVAEGGSDCAPEKLWLQIPFFCGHSSECWNVGSRWAMDQAKSNLINEYFLVGVTEELEDFIMLLEAALPRFFRGATDLYRTGKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVREKDGDLYILAQNFFYEKIYPKSN", "text": "FUNCTION: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand- binding interactions and signaling processes. Required for metanephric development of kidney formation, suggesting that 2-O-sulfation within HS is essential for signaling between ureteric bud and metanephric mesenchyme. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 3 family."}
+{"protein": "MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMRDGEGEEFDNTCCPEKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQENDEFGQPSDNRKLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANIKDSVDDNHLSPSRWKWARKALSETSSNKSYENKYQEVSQKDSHEQLNNTSSSSPQHLSAQKLEMLYNEITKTQTHSHPNPDCQEQPERPSAYEEEIEMEEVVCPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGMDEHQRVRAPPFLTLSRDKGPAAREAALDYAPIDITVNLDAGASHGPLQPDSASDSPKSSLKGSNPLKSRSLKVNFQENRGSAPQTPPSTARPLPVTTADFPLTTPQHMSTILLEESPPPGTETLPGADVSAHCQGPSKGLSPRVPKQKLFPFSSRERRSFTEIDTGEDEDFLDLQRPRPDKQADPSPNCLADKPGEARDPLREEGCVGSSSPQNTDHNCRQDIYQAVGEVKKDSSQEGYKMENHLFAPEIHSNPGDTGYCPTRETSM", "text": "FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells (PubMed:1550672). Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:1550672). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:20202934). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes (PubMed:9305895). 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. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells (PubMed:1550672, PubMed:20202934). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Perikaryon Cell projection, dendrite Note=Localized uniformly throughout cell bodies and dendrites (PubMed:10719893). Colocalizes with KCNB1 to high- density somatodendritic clusters on cortical pyramidal neurons (PubMed:20202934). SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.2/KCNB2 sub-subfamily."}
+{"protein": "MSTVLTYIRAVDIYEHMTESLDLEFESAYRGESVAFGEGVRPPWSIGEPQPELAALIVQGKFRGDVLDVGCGEAAISLALAERGHTTVGLDLSPAAVELARHEAAKRGLANASFEVADASSFTGYDGRFDTIVDSTLFHSMPVESREGYLQSIVRAAAPGASYFVLVFDRAAIPEGPINAVTEDELRAAVSKYWIIDEIKPARLYARFPAGFAGMPALLDIREEPNGLQSIGGWLLSAHLG", "text": "FUNCTION: Involved in cellular response to chemical stress and may contribute to resistance toward antimicrobial natural compounds as well as drugs. Catalyzes the methylation and detoxification of the P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to 2- heptyl-1-methoxy-4(1H)-quinolinone (HMOQ). FUNCTION: Involved in cellular response to chemical stress and may contribute to resistance toward antimicrobial natural compounds as well as drugs (Probable). Catalyzes the methylation and detoxification of the P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to 2-heptyl-1-methoxy-4(1H)-quinolinone (HMOQ) (PubMed:33064871). Can also methylate 3-bromo-2-heptyl-1-hydroxy-4(1H)-quinolinone, and shows much lower activity with 1-hydroxyquinolin-4(1H)-one, quercetin, 4- hydroxyquinolin-2(1H)-one (DHQ) and 4-hydroxyisoquinolin-1(2H)-one (PubMed:33064871). In addition, N-methylates and abolishes the mycobactericidal activity of 3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1- yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile (compound 14), an inhibitor of DprE1 (PubMed:27432954). Also methylates and reduces the inhibitory effect of TPSA (2-[5-(2-{[4-(2-thienyl)-2- pyrimidinyl]sulfanyl}acetyl)-2-thienyl]acetic acid), an inhibitor of GlmU acetyltransferase (PubMed:31380295). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE", "text": "FUNCTION: Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L- serine to L-serine. L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator. May also act on O-phospho-D-serine. FUNCTION: Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L- serine to L-serine (PubMed:12213811, PubMed:15291819, PubMed:9222972, PubMed:14673469, PubMed:25080166). L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator (PubMed:14673469). May also act on O-phospho-D-serine (Probable). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family."}
+{"protein": "MFNFRLFSRRGKSLGLLAIVLLLFGFYSLKSSMPVYSNSIGSPSAHSSSYKGVSKAKTSPQDPDSVVMLIVSFDDHYDSSRSDSSSVFLDKVLSDRTEYALRHGYTLVHKKARDIQARYGVYGTWSIIPALRETLAEYPDAGWIWLLDAKAVIMNPSESLKDRVLKPEKLSQHLLLNSPIDPLKNYIRTRRKMDPSDVFVITTSDYNGISTRSLLIKNNNFAPFLLDAWNEPLLKSAGFDQAERSALSHLLEAHNTILDHVALVSPKVLNSYTNSAVDLNYEEGDFLVILQDCENAAACERIFDNYYQQRKLPAIKKQLSEETVDEQS", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyltransferase 34 family."}
+{"protein": "MAQPGDPRRLCRLVQEGRLRALKEELQAAGGCPGPAGDTLLHCAARHGHRDVLAYLAEAWGMDIEATNRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRKNLGVIQELVEHGANPLLKNKDGWNSFHIASREGDPLILQYLLTVCPGAWKTESKIRRTPLHTAAMHGHLEAVKVLLKRCQYEPDYRDNCGVTALMDAIQCGHIDVARLLLDEHGACLSAEDSLGAQALHRAAVTGQDEAIRFLVSELGVDVDVRATSTHLTALHYAAKEGHTSTIQTLLSLGADINSKDEKNRSALHLACAGQHLACAKFLLQSGLKDSEDITGTLAQQLPRRADVLQGSGHSAMT", "text": "FUNCTION: Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity. Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing the charging of Ser adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent peptides. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MAAAGGLPASATLLLLVIAAVAVAPLASAVRPVSDAHRSAAAELFAASPDGSFGDLETTYEAVRTFQILGVEKDKGLIGKACKFAAEKLASSSSSPAKDLFHAARISGVLKCSVDSGVYDDVATRLKAVIKDTNSLLELYYSVGGLLSIKEQGHNVVLPDADNTFHAIKALSQSDGRWRYDTNSAESSTFAAGIALEALSAVISLADSEVDSSMIAVVKNDIVKLFDTIKSYDDGTFYFDEKHVDAAEYKGPITTSASVVRGVTSFAAVASGKLNIPGEKILGLAKFFLGIGLPGSAKDCFNQIESLSFLENNRVFVPLVLSLPSKVFSLTSKDQLKVEVTTVFGSAAPPLRVNLVQVLGSDSKVITTETKELQFDLDNNVHYLDIAPLKIDVGKYSLVFEISLQEQEHETIYATGGTNTEAIFVTGLIKVDKAEIGISDNDAGTVESVQKIDLQKDTSVSLSANHLQKLRLSFQLSTPLGKTFKPHQVFLKLKHDESKVEHLFVVPGSARQFKIVLDFLGLVEKFYYLSGRYDLELAVGDAAMENSFLRALGHIELDLPEAPEKAPKPPAQAVDPFSKFGPKKEISHIFRSPEKRPPKELSFAFTGLTLLPIVGFLIGLMRLGVNLKNFPSLPAPAAFASLFHAGIGAVLLLYVLFWIKLDLFTTLKYLSFLGVFLVFVGHRALSYLSSTSAKQKTA", "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 SWP1 family."}
+{"protein": "MRKVIHIGLPKLSEEELIEIGDIAQRVIIDYIFEHLAKSEVRDMEVTARINQGETLDLELEVYVEVPIFVRVDVESLIDEAIDKAYEVVERHLRKLAKGKGNEGREEAEEASGKSK", "text": "SIMILARITY: Belongs to the UPF0440 family."}
+{"protein": "MSSRVGDLSPQQQEALARFRENLQDLLPILPNADDYFLLRWLRARNFDLQKSEDMLRRHMEFRKQQDLDNIVTWQPPEVIQLYDSGGLCGYDYEGCPVYFNIIGSLDPKGLLLSASKQDMIRKRIKVCELLLHECELQTQKLGRKIEMALMVFDMEGLSLKHLWKPAVEVYQQFFSILEANYPETLKNLIVIRAPKLFPVAFNLVKSFMSEETRRKIVILGDNWKQELTKFISPDQLPVEFGGTMTDPDGNPKCLTKINYGGEVPKSYYLCEQVRLQYEHTRSVGRGSSLQVENEILFPGCVLRWQFASDGGDIGFGVFLKTKMGEQQSAREMTEVLPSQRYNAHMVPEDGSLTCLQAGVYVLRFDNTYSRMHAKKLSYTVEVLLPDKASEETLQSLKAMRPSPTQ", "text": "FUNCTION: Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids."}
+{"protein": "MEVTLKEFRELCTSISTESSYVKKTKLISEFIHRGRDYNDVYIITKLLLPGTGKLIYNINDKQLVKLFSKIFCHDADEMYKYVINIGDVAYVIGSFLKKSKSVVDYATESTLTLHEVDCFLTRLSTVTRENDQIKEIKKIIPRCTPNDLRHIIRLIKHDLRMNIGPKHVLSGLHKDAYGIFKLCNNLEQVVQRSLEDNIKPLIELMVPLQPMLASACKTFSEAVKKCPNGIIVEFKYDGERIQIHKHDKNFKYFSRSLKPITPHKVTDFEELLDRAFPSAKNMILDGEIILIDTETNQPLPFGTLGINKKSMYHNACVCIFIFDCLYFNDTVLIDKPLIERRNIIHANIKEIPNRILLSEVKNISTDEELSKLLHIVLSKNIEGFVLKDAKGVYEPGMRRWLKIKKDYLDGCVMADKADLVVLGAYYGKGNKSGILSSFLMGCYDTKSEKWCTVTKCSGGHTDLELQEINDNLSVVPFDRNAIPDWLSINKIHYPDVIISDISLAPVWEIIGSEFTRSSTHTASNISIRFPRCSRIREDKTYETANNLNDIKQLYAVSISPPEE", "text": "FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. It is not essential for viral replication and recombination. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
+{"protein": "MHRTAIFLTYRSCMRNFSTLSKTLTVSSGKVIRNGPFRRVIREKNQITKAPSVKAFKENSNSGIIKVHDPIATTILNEPTVIIERQIEFMNVFLGFEQANRYAIMDVNGNKIASMMERDFSITKAIMRQFYRLHRPFLVDVFDNWGNVIMTIKRPFSFINSHIKTIIPPSAYVDNGSDSTHYHDGKEGTTVGETIQNWHLWRRRYELFQKDGVEGSTFDQFGKIDAPFLSFDFPVTDADGKIMASVDRNWVGLGREMFTDTGVYVVRFDSQRCFDNIYPTEMLSSQVLTLDQRAVLLANAVSIDFDYFSRHSRQTGGFLSFGGGYDE", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the phospholipid scramblase family."}
+{"protein": "MVSFKYLFLAASALGALAAPVEVEESSWFNETALHEFAERAGTPSSTGWNNGYYYSFWTDNGGTVNYQNGNGGSYSVQWKDTGNFVGGKGWNPGSARTINYSGSFNPSGNAYLTVYGWTTNPLVEYYIVENYGTYNPGNGGTYRGSVYSDGANYNIYTATRYNAPSIEGDKTFTQYWSVRQSKRTGGTVTTANHFNAWAQLGMSLGTHNYQIVATEGYQSSGSSSITVY", "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": "MFHLYLLLVFETRYTCLMKCSISTCSYRWLRRREWFCLIYSGCCRKILVIEGLQRSDVAFLFTRRTIMHYVPFRGLFCASCVGYFSIRCCSRCEHFCTKTPTKSFGTEAWS", "text": "FUNCTION: Secreted effector that acts as an elicitor that induces cell death in host plant cells. SUBCELLULAR LOCATION: Secreted Host nucleus. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MSAYAALQKMSGASSILYGINGESDNDESGTIGYLRNSSDEEVEAEEAEVPTTSTMAPTPNIIRTPSIVPKINSFICESNFIPNDDNFIVFHDHIIIGLKANEYILINGQSKMTIQRGAILINTGHYMFAHPNNCIPIIASQSQSLPIISSTQVVDRSGIKDSKTDENMHLFSSNYKSIIKLENLYTGLEKIGTYHPPFKRLFYSHAVIEDEDLTEYERLFKTYSFEIILRDRGCIGISIEKLWLNQIQLLISDIHEDLIPKTIMIIGNKNSGKSTLSKTLLNSLILANQNTVSYLDLDPGQSEFSMPYCLSLTNHSKPIIGMNVPKVSGDEDSVSHYYGFTTPQSQPSQYVSIIKALFREYDQVYRPRGHHLIINTPGWIKGYGKELLNELTAFINPNQLILLSNNTDNDNMDNSDNLSGLTFQNSRCFQGIYQTSKYSPFQLRMYNKLSYFHQVDTLKFDFNSHILLRSPLKLSYETVNSSKDFKGINMVSVLNYDTGLNFELNDLLSMIDTSIMGLYLIDHEYYSSLKASLKKSEDCDYLPQYLNSTDYVNLINYSSSNNIFMGLCMVHSINTKDEFFNIYLPGHNQHRLTEMITKRDYKMLLVKGDGDIPSPDLLMFDMLLKQQEDLKRLNKKRKKNPNVDDKDVLKIPYVTFENKNKIGGIWKTRRNVMRRSHQR", "text": "FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily."}
+{"protein": "MEAALLVCQYTIQSLIQLTRDDPGFFNVEILEFPFYPACNVCTADVNATINFDVGGKKHKLNLDFGLLTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINITTGEEQQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPYIKWDNCNSTNITAVVRAQGLDVTLPLSLPTSAQDSNFSVKTEMLGNEIDIECIMEDGEISQVLPGDNKFNITCSGYESHVPSGGILTSTSPVATPIPGTGYAYSLRLTPRPVSRFLGNNSILYVFYSGNGPKASGGDYCIQSNIVFSDEIPASQDMPTNTTDITYVGDNATYSVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPSGCENISGAFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSMLVLQWASLAVLTLLLLLVMADCAFRRNLSTSHTYTTPPYDDAETYV", "text": "FUNCTION: Responsible for EBV binding to the CR2 receptor on human B- cells. FUNCTION: Initiates virion attachment to host B-lymphocyte cell, leading to virus entry. Acts by binding to host CR2 at the surface of B-lymphocytes, facilitating the binding of viral glycoprotein gp42 to HLA class II molecules. Attachment triggers virion-host membrane fusion and invasion of the host cell (By similarity). SUBCELLULAR LOCATION: Virion membrane. Note=Most abundant component of the viral envelope. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein. Host membrane; Single-pass membrane protein. Note=Most abundant component of the viral envelope. SIMILARITY: Belongs to the Epstein-Barr GP350 family."}
+{"protein": "MESRKEKRAFLIGRFQPFHKGHLEIVKRILSENDSIIIGIGSAQYSHTVVNPFTAGERHLMISRTLEKERIYNYYLVPIEDVNANSLWVSHVEALTPKFDIVYTNNPLVRRLFMERKYEVRSLPMVNRKEWTGTKIREKMIAGEPWENDVPDPVVEVIHEIDGISRIRQLSTTDEDITQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family."}
+{"protein": "MAARRSLRYSGNPGAKHSKNTLRSTYSRKQKAGPKPRPKDVFDFSNNSDASSIPGALEEEEETYETFDPPLHSTAIYAEDELSKHCVSSSSLATHRGKASRNLDPSEDEASGNESIKVSTKKPRRKLEPISGESDSSADDVRRRVASAEGPRSQQRQAAPAAPSPPERPAEPVTPRRTRLHSAQLSPVDETPATQSQLKTQKKVRPSPGRRKRPRRGHTDTDGSESMHIWCLEGKRQSDITELDVILSVFEKTFLEYKQRVESESCNQAINKFYFKMKGELIRMLKEAQMLKALKMKNTKIIANMEKKRQRLIEVQDELIRLEPQLKQLQTKYDDLKERKSSLKKSKHFLSNLKQLCQDYSNVQEKGPKGTGKYDSSSLPALLFKARSILGAENHLRTINYQLGKLLELD", "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. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, centromere, kinetochore Note=Localizes in the kinetochore domain of centromeres. Colocalizes with PLK1 at the interzone between the inner and the outer kinetochore plates (By similarity). SIMILARITY: Belongs to the CENP-U/AME1 family."}
+{"protein": "MAIEQEHRKKASGWAARDSSGVLSPFNFYRRETGEKDVTFKVLYCGICHSDLHMVKNEWGFSTYPLVPGHEIVGEVTEVGSKVQKFKVGDRVGVGCIVGSCRSCENCTDHLENYCPKQILTYGAKYYDGSTTYGGYSDIMVADEHFIVRIPDNLPLDGAAPLLCAGITTYSPLRYFGLDKPGMHVGVVGLGGLGHVAVKFAKAMGVKVTVISTSPKKEEEALKHLGADSFLVSRDQDQMQAAIGTMDGIIDTVSAQHPLLPLIGLLNSHGKLVMVGAPEKPLELPVFPLLMGRKMVAGSGIGGMKETQEMIDFAARHNITADIEVIPIDYLNTAMERLVKADVRYRFVIDIGNTLKVRS", "text": "FUNCTION: Oxidizes mannitol to mannose. Provides the initial step by which translocated mannitol is committed to central metabolism and, by regulating mannitol pool size, is important in regulating salt tolerance at the cellular level (By similarity). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MDDENLWKVVKKDSIFETTHFSSKPVFTRSFSTKTSSSSSKPVFTRSFSTKPTSYSSSEPIFRRSFSAKPTSSKSPFLSRSGSTKCPVDTSSTSKCSISRSLSQKGASVTRKCRNMAKEHKSRFYIMKRCVLMLVCWHKHACDS", "text": "FUNCTION: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the DVL/RTFL small polypeptides family."}
+{"protein": "MTKPLDGINVLDFTHVQAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQDKPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGALDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAATTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEMRHKTGRGQKVAVAMQDAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSVPRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEWKDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVMSMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLLGEHTDEVLKELGLDDAKIKELHAKQVV", "text": "FUNCTION: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate (PubMed:15213226, PubMed:18162462, PubMed:18245280, PubMed:2361939, PubMed:9150242). It can also use succinate as acceptor (PubMed:18245280, PubMed:2361939). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CoA-transferase III family. Frc subfamily."}
+{"protein": "MQRTSRLKRELSLLAAEPPPGITCWQDGDRMEDLRAQILGGANTPYEKGVFKLEVHIPERYPFEPPQIRFLTPIYHPNIDSAGRICLDVLKLPPKGAWRPSLNIATLLTSIQQLMAEPNPDDPLMADISSEFKYNKPVFFKNARQWTEKHARQKTDEEGMPGSLPEVGGSEGPSAAQKRKAGQLSSGGKRFCPDV", "text": "FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination. SUBCELLULAR LOCATION: Nucleus Note=Accumulates to chromatin. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "MKEIAVTIDDKNVIASVSESFHGVAFDASLFSPKGLWSFVDITSPKLFKLLEGLSPGYFRVGGTFANWLFFDLDENNKWKDYWAFKDKTPETATITRRWLFRKQNNLKKETFDDLVKLTKGSKMRLLFDLNAEVRTGYEIGKKMTSTWDSSEAEKLFKYCVSKGYGDNIDWELGNEPDHTSAHNLTEKQVGEDFKALHKVLEKYPTLNKGSLVGPDVGWMGVSYVKGLADGAGDHVTAFTLHQYYFDGNTSDVSTYLDATYFKKLQQLFDKVKDVLKNSPHKDKPLWLGETSSGYNSGTKDVSDRYVSGFLTLDKLGLSAANNVKVVIRQTIYNGYYGLLDKNTLEPNPDYWLMHVHNSLVGNTVFKVDVSDPTNKARVYAQCTKTNSKHTQSRYYKGSLTIFALNVGDEDVTLKIDQYSGKKIYSYILTPEGGQLTSQKVLLNGKELKLVSDQLPELNADESKTSFTLSPKTFGFFVVSDANVEACKK", "text": "FUNCTION: Hyaluronidase that mediates hydrolysis of (1->3)-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate. Very specific to hyaluronate: not able to hydrolyze chitin, heparin or chondroitin sulfate. SIMILARITY: Belongs to the glycosyl hydrolase 79 family."}
+{"protein": "MESSRTAATSTNGTEKSRRRNTDYLQIDPSSTFINNTGRGFAEELPENFLDTISPHPITPSASTSSATSATEEPATSSAPQLASLAPMSMSSEQPSSSFSSASLLSSSYETIKNEPEFSGSTAGLLSPLHVDSRRRESHDFNTSPYIKEEEDLDGSHLLMGGIRPDTPTNDRSTDLGSISSLLNEDHHTNTIGQSPSPRSTFGSDPTPMIQRQLIKNEDGVSPGSMGFSKNHQGYQKPRNGDRMEYEKAPYQRNSRKQKKPLGLLNQALSSVISTPTISSSNIPTPPSAHIAQPRRIYSTQDSNDPLNAEIGDDIYIDTKDLCKRIAFELKNHSIPQAIFAERILCRSQGTLSDLLRNPKPWNKLKSGRETFRRMYNWVAQPLATRLAILDMKTEDVNRASGMSPPTPAQNVRTHRRSTSDHDGPVSKRPRLVFTDIQKRTLQAIFKETQRPSREMQQTIAEHLRLDLSTVANFFMNARRRSRLGGNIDEPTPFQQVKNISPPPVGDTSDALLNGDDHVPLLNTVMAEMYKEGAIATSNHSAEQREMIERGFGVSIPGPSHSGELLNGDSHEDDEELDELNDSELAYEEDVEIGDEEEEDEEQANGDILPTPKVEELEEKTVIKEEAPDDGEYGATKLAAN", "text": "FUNCTION: Probable DNA-binding regulatory protein involved in cell-fate specification. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CUT homeobox family."}
+{"protein": "MSHPNTHMPRTHAVHGRAAPQRRGCRTSVEKTDQSGHSRSSLAESAMEQAQLRSRGEAGGGRSVLCASGEPGSAHKWAGAVTCSGAEEQPLHWAESRARGLARHLHYWELPYAWRENRYIIYGHRFYHSHRKSLLSVLNAYGWHNETINIWSHLVGAAVLAYLLCWGWPRSDVYRAAQVPRLAKWAIGAFLACGVKCMASSVAWHTFNGTCHLKLRSRFVCVDYTGITLLVTASVVTTVAVTLYGLSRPLMYAYMVASIGLGTAAGVMNWSPHFDRPEARPLRIAVYVGLAALGLVSFVHVWMQVRWASAHLMAPLVYKSLVWYGIGVVFYATLVPERWRSDVTLDCCSGPVHEAACRQFRDLPPVARKDRQFWSLWWVDYFCHSHFLWHVFVVLGVVGHYRAVLQMSRIVWLDAGRAF", "text": "FUNCTION: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ADIPOR family."}
+{"protein": "MAPKNNAKGGDKKGKGKDASEGDKGKGGGKGLKPATSINVRHILCEKFSKKEEALEKLRNGAKFDDVAREYSEDKARQGGSLGWKVRGSLNADFEKAAYELEPSTTANPKYVEVKTGFGYHIIMVEGRK", "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 PpiC/parvulin rotamase family. PIN4 subfamily."}
+{"protein": "MKSKDTLKWFPAQLPEVRIILGDAVVEVAKQGRPINTRTLLDYIEGNIKKTSWLDNKELLQTAISVLKDNQNLNGKM", "text": "SIMILARITY: To E.coli YdfK."}
+{"protein": "MHSCSHTHFVSFKLPHFFAPKSFVVSSRRELRVFAVATTVEEASGNIPAAPISLPQGSWKQIAGGVTAAKGFKAAGMYAGLRAAGKKPDLALVTCDVEAVAAGVFTTNVVAAAPVVYCKKVLETSKTARAVLINAGQANAATGDAGYQDMLDCVGSIATLLKVKPEEVLIESTGVIGQRIKKEELLHALPTLVNSRSDSVEEADSAAVAITTTDLVSKSVAVESQVGGIKIRVGGMAKGSGMIHPNMATMLGVITTDALVESDIWRKMVKVAVNRSFNQITVDGDTSTNDTVIALASGLSGSPSISSLNCKEAAQLQACLDAVMQGLAKSIAWDGEGATCLIEVTVKGTETEAEAAKIARSVASSSLVKAAVYGRDPNWGRIAAAAGYAGVSFQMDKLKISLGEFSLMESGQPLPFDRDGASNYLKKTGEVHGTVTIDISVGDGAAIGKAWGCDLSYDYVKINAEYTS", "text": "FUNCTION: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ArgJ family."}
+{"protein": "MTTSFAAAALRDPKLQIPNYHGLRSSSAASSLSRNALSVPSSTRSSSLIRAVSTPAKSETATEKKRSKVEIFKEQSNFIRYPLNEDMLTDAPNLSEAATQLIKFHGSYQQYNRDERGSRTYSFMIRTKNPCGKVSNQLYLTMDDLADQFGIGTLRLTTRQTFQLHGVVKKDLKTVMGSIIRNMGSSLGACGDLNRNVLAPAAPIVSKDYLFAQETSENIAALLTPQSGFYYDVWVDGERFMSAEPPEVIQARNDNSHGTNFTDSPEPIYGTQFLPRKFKIAVTVPTDNSVDILTNDIGVVVVTGDGGEPQGFNLYVGGGMGRTHRMETTFPRLAEPLGYVPKEDILYAVKAIVVTQRENGRRDDRRYSRMKYLIDSWGIDKFRNVVEEYYGKKFEPFRSLPEWEFKSYLGWHQQGDGGLFCGLHVDNGRIAGKMKTALREVIEKYHLNVRLTPNQNLILTDIRAAWKRPITTILSQAGLLLPRYVDPLNITAMACPAFPLCPLAITEAERGIPSILKRIRDMFEKVGLKYNESVVVRITGCPNGCARPYMAELGLVGDGPNSYQIWLGGSSNQTSIARSFMDKVKPQDLEKVLEPLFYHWKQKRQSKESFGDFTVRLGFEKLKEFIEKWEGPAVPPTRHNLKLFTDKDTYEAMDGLAKLQNKNAHQLAMEVVRNYIASNLNGKGE", "text": "FUNCTION: Essential protein with sulfite reductase activity required in assimilatory sulfate reduction pathway during both primary and secondary metabolism and thus involved in development and growth. FUNCTION: DNA-binding protein that binds to both double-stranded and single-stranded DNA without significant sequence specificity to reversibly repress the transcriptional activity of chloroplast nucleoids by promoting DNA compaction and possibly regulate DNA replication. SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid. Plastid, chloroplast stroma. Plastid stroma. SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family."}
+{"protein": "MDALEEESFALSFSSASDAEFDAVVGCLEDIIMDDEFQLLQRNFMDKYYQEFEDTEENKLTYTPIFNEYISLVEKYIEEQLLERIPGFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRGLDLSSGLVVTSLCKSSSTPASQNNLRH", "text": "FUNCTION: Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion intermembrane space Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cytoplasm, cytoskeleton, cilium basal body Note=Detected in the midbody matrix. 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 SLC25A4 is expressed in mitochondria. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization (By similarity). SIMILARITY: Belongs to the ARL2BP family."}
+{"protein": "MAAGISLTKPNIGVYTNPNHDLWVADAKPTLEEVKSGSDLKPGQVTVEIRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGVVIAVAPDVKTLKPGDRVAIEPNIICNKCEPCLTGRYNGCEAVEFLSTPPVDGLLRRYVNHPAIWCHKIGDMSFEDGALLEPLSVALAGMDRAGVRLGDPVLVAGAGPIGLVTLLCVRAAGATPIVITDIDEGRLRFAKELVPEVRTYRVQTGLSAEENAAGILDALNDGNGSAPDAIRPRVAMECTGVESSVASAIWSVKFGGKVFVIGVGKNEMKVPFMRLSTWEIDLQYQYRYCNTWPKAIRLVKNGVINLKKLVTHRFPLEDAVKAFETAANPKTGAIKVQIMSSEEDIKAASGVNGASN", "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. NADP cannot act as a cosubstrate. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MALEQLCAVLKVLLITVLVVEGIAVAQKTQDGQNIGIKHIPATQCGIWVRTSNGGHFASPNYPDSYPPNKECIYILEAAPRQRIELTFDERYYIEPSFECRFDHLEIRDGPFGFSPLIDRYCGMKSPALIRSTGRFMWIKFSSDEELEGLGFRAKYSFIPDPDFTYLGGILNPIPDCQFELSGADGIVRSSQVEQEEKTKPGQAVDCIWTIKATPKAKIYLRFLDYQMEHSNECKRNFVAVYDGSSAIENLKAKFCSTVANDVMLKTGVGVIRMWADEGSRLSRFRMLFTSFVEPPCTSSTFFCHSNMCINNSLVCNGVQNCAYPWDENHCKEKKKAGLFEQITKTHGTIIGITSGIVLVLLIISILVQVKQPRKKVMACKTAFNKTGFQEVFDPPHYELFSLREKEISADLADLSEELDNYQKLRRSSTASRCIHDHHCGSQASSVKQSRTNLSSMELPFRNDFAQPQPMKTFNSTFKKSSYTFKQAHECPEQALEDRVMEEIPCEIYVRGRDDSAQASISIDF", "text": "FUNCTION: Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the agonist sensitivity of kainate receptors. Slows the decay of kainate receptor-mediated excitatory postsynaptic currents (EPSCs), thus directly influencing synaptic transmission (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single- pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MASFTLSSATPSQLCSSKNGMFAPSLALAKAGRVNVLISKERIRGMKLTCQATSIPADNVPDMQKRETLNLLLLGALSLPTGYMLLPYASFFVPPGGGAGTGGTIAKDALGNDVIAAEWLKTHAPGDRTLTQGLKGDPTYLVVESDKTLATFGINAVCTHLGCVVPFNAAENKFICPCHGSQYNNQGRVVRGPAPLSLALAHCDVDDGKVVFVPWTETDFRTGEAPWWSA", "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": "MSDDFLWFEGIAFPNMGFRSETLRKVRDEFVIKDEDVIILTYPKSGTNWLIEILCLIHSNGDPKWIQSVPIWERSPWVETEMGYKLLSEEEGPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNPRDVFVSGYFFWNSVKFVKKPKSWQQYFEWFCQGNVIYGSWFDHIHGWMPMREKKNFLLLSYEELKQDTRRTVEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNFSLLSVDFVEEKAQLLRKGISGDWKNHLTVAQAEAFDKLFQEKMTDLPRELFPWE", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands (PubMed:31100221). Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis. Plays a key role in bile acid metabolism (By similarity). In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the sulfotransferase 1 family."}
+{"protein": "MAKVSLEKLLRIPPSLTQSISQTKVDYLNLGHSGLRVSRPILGGLHLGSRKWLPWVLDEEKALPILKAAYDLGVNTWDTANVYSNGESERIIAKALSKYKIPRNKVVLMTKCYRVMSDPERFDPGSGVTMHHELADYSKDYVNQWGLSRRALFSAVEASLDRLNTSYIDVLQIHRFDHTVPPEETMSALNDLIRAGMVRYIGASSMWTFQFATLQHIAETKGLTKFISMQNHYNLIYREEEREMNQYCKMTGVGLIPWGPLASGRLARRPTQEEGSLRASCSAHGSLYESDDYNVDRIIQRVAEIAEKRGWPMSHVSLAWLNRRVTAPIIGFGSVGRIEEALAARGKELSRDEEQYLEELYVPQRIQGHS", "text": "FUNCTION: Aldo-keto reductase; part of the gene cluster that mediates the biosynthesis of destruxins, insecticidal cyclic hexadepsipeptides which induce flaccid paralysis and visceral muscle contraction in insects through targeting the calcium channels and vacuolar-type ATPases (PubMed:22232661). The aldo-keto reductase dtxS3 converts alpha-ketoisocaproic acid from deaminated leucine into alpha- hydroxyisocaproic acid (HIC), which is the first substrate for destruxin assembly by dtxS1 (PubMed:22232661). L-aspartate decarboxylase dtxS4 converts aspartic acid into beta-alanine, the last substrate for the destruxin assembly line performed by dtxS1 (PubMed:22232661). The nonribosomal peptide synthetase dtxS1 synthesizes destruxins B and B2, whereas the cytochrome P450 monooxygenase dtxS2 is required to convert destruxin B into other destruxin derivatives, including destructins C, D, A and E (PubMed:22232661). Destruxin E-diol (ED) is further produced in a non- enzymatic manner from destruxin E (PubMed:22232661). Destruxins play an important role in virulence and escape from insect host immune defenses (PubMed:22232661). SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MQRLACVLIWLFLLEEQAFEIPANEYSEFAGYSNLVELAPDKFPFVQENRRYQRSLPEESGEMTDNVDQVTLYSYKVQSTITSRMATTIIQSKLVNNSPQSQNVVFDVQIPKGAFISNFTMTVNGITFTSTIREKTVGRALYSQARAKGKTAGWVRSRTLDMENFNTEVNIPPGAKVQFELHYQEMKWRKLGSYEHKIHLQPGRLAKHLEVNVWIVELQGMRFLHVPDTFEGHFQGVPVISKGQKKSHVSFKPTVAQQRKCPNCTYTAVDGELVVMYDVNREEKVGELEVFNGYFVHFFAPENLDPIPKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTEDQFSVVDFNHNVRTWRNDLVSATKTQITDAKRYIEKIQPSGGTNINEALLRAIFILNEASNLGMLNPDSVSLIVLVSDGDPTVGELKLSKIQKNVKQNIQDNISLFSLGIGFDVDYDFLKRLSNENRGIAQRIYGNRDTSSQLKKFYNQVSTPLLRNVQFNYPQASVTDVTQNSFHNYFGGSEIVVAGKYDPSKLAEVQSIITATSTNTELVLETLSQMDDLEDFLSKDKHADPNFTKKLWAYLTINQLLAERSLAPTAAIKRKITKTILQMSLDHHIVTPLTAMVIENEAGDERMLADSPPQDHSCCSGALYYGTKVASASIPSWASPSPTPVMAMLAVGANRLESTPPPHVIRVENDPHFIIYLPKSQKNICFNIDSEPGKILSLVSDPESGILVNGQLIGAKKAENGKLRTYFGKLGFYFQKEDMKIEISTENITLINGSSTTSLFWSDTAHLGNQRVLISVKKGKSVTLTLNKEMFFSVLLHHVWKKHPVNVDFLGIYLPPTNKFSPSAHGLLGQFMNKPNIHIFNERPGKDPEKPEASMEVKGHKLTVTRGLQKDYRTDIAFGTDVPCWFVHNSGKGFIDGHYKDYLVPQLYSFLKRP", "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": "MGSSLVSVAEQLLKDLQRTYSEIKQIPDDLLIALRFVFGPCALQALDLVDQHSVTCVSSPSGRKAFQVLGGSGRLYTCFTSCHYCPCPAFSFTVLRRNESLMCKHLLAVILSQAMGLCQQEQVSDQQMTHILSRQPEAST", "text": "FUNCTION: Involved in early stages of 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 SWS1 family."}
+{"protein": "MFKKLFGQLQRIGKALMLPVAILPAAGLLLAIGTAMQGESLQHYLPFIQNGGIQSVAEMMTGAGGIIFDNLPMIFAMGVAIGLASGDGVAAIAAFVGYLVMNKTMGAFLHVSPDNVNDAASGYASVLGIPTLQTGVFGGIIIGALAAWCYNKFYNISLPSYLGFFAGKRFVPIMMATTSFILAFPMAWIWPSIQTGLNAFSEGLLDSNTGLAVFLFGFIKRLLIPFGLHHIFHAPFWFEFGAWKNAAGEMIHGDQRIFIEQIREGSKLTAGKFMQGEFPVMMFGLPAAALAIYHTAKPENKKVVAGLMGSAALTSFLTGITEPLEFSFLFVAPVLFFVHAILDGLSFLILYLLNVHLGYTFSGGFIDYVLLGVLPNKTQWWLVIPVGVVYAFIYYFVFRFLILKFKYKTPGREDKQAQFTNSSASELPFNVLKAMGGEENIKHLDACITRLRVEVKEKGKVDVAGLKALGASGVLEVGNNMQAIFGPKSDQIKHDMSLIMKGEITKPQETTVTEEESEEVVHIERASEVNIYAPGNGQVIPLSEVPDQVFAQKMMGDGVGFIPADGKIVAPFDGTVKTIFPTKHAIGLESDQGLELLIHIGIDTVKLNGEGFESFVETDDRVHKGQVLMQIDLDYITAHAPSTVTPLIITNLEDRQLSVEDVKDVTAEQLIIKVIDDK", "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 glucose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MVEALLSGIVLGSIPITLAGSFVTAYPQYRRGDQLDLR", "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: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetG family."}
+{"protein": "MTETEIFAYIEAASIAIGIPLEPARARAVAHHFSRTALLAEMLESVPLSPESELAEIYRPAPFPAEDI", "text": "FUNCTION: Important for the activity of the AtzE subunit of 1- carboxybiuret hydrolase."}
+{"protein": "MELSEHEEDAGDVGGGCSSPPTPPHRVLTSAAPETIRCRYHECLRNHAAASGGHVVDGCGEFMPASTEEPLACAACGCHRSFHRRDPSPGRAGAARLPQLHLPASINSRAPPALLLPPAAAASKQGLPFPGYGTPSGGTGTTTASSSDERLRPSPVQPRRRSRTTFTREQKEQMLAFAERVGWRIQRQEEATVEHFCAQVGVRRQALKVWMHNNKHSFKQKQQQENRQEQQQ", "text": "FUNCTION: Putative transcription factor. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLARPETDTSVDYYAILKLQKNATFQQIRKQYLFLALQYHPDRNPGDEERAVKRFQRLQLAHEVLSDATKRLIYDQLFGLSTRTRSQYKPNSTSNPSKHTSAYASYNKGKNSKWSSPFASTTKKPQESSEKYSKKSSTRKKEHFNKKPSFPRDTEYSHIYNMKYDPRSGIGIRVKRQEPESLKKENNNSDYLPKSAMKQKKGGPKDSSKHPSNDGKIPESKPSVYKSRASNLFSSNEQSIHSSFGSKFHFDKSSNPFSFEFSPSSNAAKPSNSEECNIPKFNSSFKTSNDFFTFTKTEESSPYSFSFKLEDSNTPKFKSSSKPVKSSFVFTKPEAESSNPFSFDFGSSGPKSRSDTRNNIRTPLWTSSVFEKPESDLPNKTAFGFMRSNTSTFNQKCDDFSSASFMKEKTEFEEQLQEDNDHSLGDLFSKINISTESPSVAMPSIPVIQPPSFPIFSSIDFNVRNREYWNQLMVFQKLYSKYCTESQHFINSWINIKKELHIVPVNWEIFEKVEKSWDQCEEFVAEFRQTEEKYFLFLKRLRELINKNQML", "text": "FUNCTION: Has a role in sporulation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Associates with the microtubule cytoskeleton."}
+{"protein": "MDSKNGINNSQKARRTPKDRHLKIGGRDRRIRIPPSVAPQLFRLTKELGFKTDGETVSWLLQNAEPAIFAATGHGVTTTSNEDIQPNRNFPSYTFNGDNISNNVFPCTVVNTGHRQMVFPVSTMTDHAPSTNYSTISDNYNSTFNGNATASDTTSAATTTATTTV", "text": "FUNCTION: Required during early processes in pollen development. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "YLRHVEEWELSCIMQLCIVDLKPETLAHLHNMDPRILETWNLGFIQPPTNIEDQYRFIKSLATKCPGKEETAEKEDPYAKYKFWDINLTERFSSNWNMYLGRNFLFQIGKRGSKRPAPKTVTFDSSSKKAPKRRRKNA", "text": "FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and about 55 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. The capsid encapsulates the genomic DNA, but does not bind DNA. Essential for the initial attachment to the host cell (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the papillomaviridae L1 protein family."}
+{"protein": "MLRCVIPSVRATATTRTFVRFASSQGYIDGIAALKQDLKKAMLAKDNLRKTTIRGVLSTIKNKEIDSKDKDLDEFVLYDVYAKLISQRKDSIAEFVKNKREDLVEKEANEIKILENYQTALPVASREEVDARVVQILTDLKESEPSIQLKQVFGKIDWKTLPGELKASPAAIRSSISSQFKKVFQ", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM41 family."}
+{"protein": "MEANRSRLLAAARPYIQIYSIFGLTPPIQFFTRTLHKRRRGIVILGYACYLISISLMVIYECYANIVALQKDIHKFHAEDSSKVMGNTQKVLVVAMFVWNQLNILLNFRRLARIYDDIADLEIDLNNASSGFVGQRHWWRFRFRLALSVGLWIVLLVGLTPRFTLVALGPYLHWTNKVLTEIILIMLQLKCTEYCVFVLLIYELILRGRHILQQISVELEGNQSRDSVQELCVALKRNQLLAGRIWGLVNEVSLYFTLSLTLLFLYNELTILQIVNWALIKSVNPNECCQYRRVGTCLLLSINIFLSCLYSEFCIQTYNSISRVLHQMYCLSAAEDYLILKMGLREYSLQMEHLKLIFTCGGLFDINLKFFGGMVVTLFGYIIILVQFKIQFFAQSNFMQNINSTELKAYTA", "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. Gr2a subfamily."}
+{"protein": "MLEKNKYLYIFRHIQTNQVLLSQGNVLKKTALFQLPYPLQKPVAPNGMRPAKLRKDHWVPLLKVEFPNESMFQSVFMQLLNYRKYRSVQPLTSDLLKLPIPVRRRKIMRQEVPNTIADLADILNKEKFPENSVRLQLSDKSDSEYADWPPSVQIDSEEIKLSRGFREKTTVDEAR", "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. mL67/mhr1 also has extraribosomal functions, being involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells. mL67/mhr1 also acts as transcription factor involved in regulation of RNA polymerase II- dependent transcription. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL67 family."}
+{"protein": "MEFDELMQCPYDKNHMIRPSRFPYHLVKCRENNRAAAKILATCPYNARHRVPKQELDLHMASCEYRVTMEPISAAFSHQKVETSTWQSPPCEEVWETDEDPVSRPKPFILNDFTPSQPFNMSEGDGNMPYTGISSNYRPEVQPMNSVMQVKQNQPEPEPFTSSERNYDPRSKEPPNPKQPAVNGYKPATTNTNPWCRQTGGSRGAAPPKLGAKSSDEGPRNKEFPTPKANLMNEYVPVAANANPWCRQPGGSSAASEPLGVDSFDEWPCLGRQPWVRK", "text": "FUNCTION: Involved in oocyte maturation. It is possible that D7 is required at a certain point in the maturation process and that maturation cannot proceed beyond this point unless a threshold amount of D7 protein is provided. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0224 (FAM112) family."}
+{"protein": "MFNRPNRNDVDDGVQDIQNDVNQLADSLESVLKSWGSDAKGEAEAARSKAQALLKETRARMHGRTRVQQAARDAVGCADSFVRERPWCSVGTAAAVGIFIGALLSMRKS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ElaB/YgaM/YqjD family."}
+{"protein": "MDARTPEVPCGDLLQNAAENLLQEVEEHFQALTATLNLRMEEMGNRIEDLQRNVDDLMAQAGIENSIKEATT", "text": "SIMILARITY: Belongs to the HSBP1 family."}
+{"protein": "MKTLYSLRRFYHVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVLKALYFGGVYDTWAPGGGDVRKIANLTLSPSLIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICILGGIWHILTKPFAWARRAFVWSGEAYLSYSLGALSIFGFTACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLNRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFFFIGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN", "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 membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily."}
+{"protein": "MPSPKARSGSGRSGSVPCPGGNGRYEFISLNRTPPSPVPPQLLQRQGSDPTTARLRASESPVRRRGSGSSNSSTGGGGQQLPEEDCMRLNPSFFGIALSSLLAIDLWLSKRLGVCACEDSSWGSVRPLMKLIEVSGHGIPWLAGAAYCLYKSDSPAGQEVMLNLLMALVLDVVLVGVLKAVVRRRRPAHNRMDMFATFSVDSYSFPSGHATRAAMCARFLLNHLVLAAPLRVLVLLWATIVGFSRVLLGRHNVTDVAFGFFMGYWQYNLVEMLWLSPVMLQSAIGQLH", "text": "FUNCTION: Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates. May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway. May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins. Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols. May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine- 1-phosphate. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Nucleus envelope Nucleus inner membrane. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family."}
+{"protein": "MELGPEPPHRRRLFFACSPTPAPQPTGKMLFGASAAGGLSPVTNLTVTMDQLEGLGSDCEKMEVRNNSSLQRMGSSESTDSGFCLDSPGPLDSKENLEISLTRINSLPQKLLGCSPALKRSHSDSLDHDTFHLIDQDENKENEAFEFKKPIRPASRHIYEESKDPFTHRQNSAPARMLSSNESESGNFSPLFIPQSPVKATLSDEDDGFIDLLDGENMKNDEETPSCMASLWTAPLVMRRPANLADRCGLFDSPSPCGSSTRAVLKRADRSHEEPPRGTKRRKSVPSPVKAKADVPEPAQLPSQSLSLMSSPKGTIENILDSDPRDLIGDFSKGYLFNTVSGKHQDLKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFLKCQSHCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL", "text": "FUNCTION: Tyrosine protein phosphatase which functions as a dosage- dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro (By similarity). Phosphorylation by PIM1 leads to an increase in phosphatase activity (By similarity). SIMILARITY: Belongs to the MPI phosphatase family."}
+{"protein": "MELEVFAGQEKSELSMIEVARAILELRGRDHEMYFNDLVNEIQTYLEKSNSEIREALPLFYTELNVDGSFIPLGDNKWGLRSWYAIDEVDEEIIALEETDEEDNPKSRKKKRVNAFMDGDEDAIDYSDDDPEDEDSYEADPALNYDDENPDDEKNEADAYDAEINEIAPDDLDEDVDINEEDDEFSDDDAEGEEE", "text": "FUNCTION: Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling. SIMILARITY: Belongs to the RpoE family."}
+{"protein": "MSTDVSSAENEGGAPIRTARVPKYYRLKKHLLDMTETLPPGTPVPPERTLAAEFDTSRTTVRQALQELVVEGRLERIQGKGTFVAKPKVSQALQLTSYTEDMRAQGLEPTSQLLDIGYITADDTLAGLLDITAGGRVLRIERLRLASGEPMAIETTHLSAKRFPALRRSLVKYTSLYTALAEVYDVRLAEAEETIETSLATPREAGLLGTDVGLPMLMLSRHSLDKDGRPVEWVRSVYRGDRYKFVARLKRPQD", "text": "FUNCTION: Global regulator that is part of the nutrient-sensing system. In the absence of glucosamine 6-P (GlcN6P), represses the phosphotransferase system (PTS) specific for the uptake of N- acetylglucosamine (PTSNag), and genes involved in the metabolism of chitin, as well as several genes involved in development, thereby linking carbon availability to morphogenesis. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MSITLLCLIKGNTLANAFPVDIDKDQLVGHLKKVIKAEQPQTFANVDAKDLKLWRVPISDDHDDQLRNLSLEDSDELLAIRKISKYFPDSPPEECIHVLVEPPESTATSEVLKLREEVASLQALLNKSVAFDVVVSPKRTKGFKWTVNIEQATLDGLKEHIRKMEKPPALENDGAVLNIVNESGKYSPLNDQDLREMLQLFVSNKNLKFTVFIETPSKAFSDWTFSSVCQLYGLNGETEDPTMTVFPNFSCGNVKPSQESLEGLMAELKSRLDNTPISLLSVEATKSLYVYSYLLAGANNFKGKFEIRPQKVISGPNGHGPLDFAIDLCQTAKTVGVTEVKKDDFVKGVAQCAVQLESSLSYRKRKADEMEERTFGRVFGIVTDAEKFYFMECSMDDQDRPSFKLSKPVTVVYEDNDLQTKVEKVLEHIVWLLEEAQKPDSALDVKEREIKRVRSGELPKVTDLEGKTN", "text": "FUNCTION: Effector that participates in the arbuscule development step of the symbiosis. Arbuscular mycorrhizal (AM) symbiosis is one of the most prominent and beneficial plant-microbe interactions that facilitates mineral nutrition and confers tolerance to biotic and abiotic stresses (PubMed:30233541). Is not involved in cell death processes (PubMed:30233541). SUBCELLULAR LOCATION: Secreted Host nucleus Note=Localizes to host nuclear bodies. SIMILARITY: Belongs to the Crinkler effector family."}
+{"protein": "MYAATPETPFGSARSQPVITRSVSQRYNHPGQSNHHHLLHSLSFNHQNVLALPAAAREPPVDVKINDIAGNSIAGILYKWVNYGKGWRPRWFVLQDGVLSYYKIKGPDKIVVIHETEKGSRVIGEESTRMISRNKRHAATNNTNHQLRRKPFGEVHLKVSSIRESRSDDKRFSIFTGTKRLHLRAETREDREAWIEALQAVKDMFPRMSNCELMAPTNNLDISIEKLRLRLVEEGVSESAIQDCEQITRSEFSAIQSQLLLLKQKQWLLIDTLRQLETEKVDLENTVVDETQRQAGNGDSEETISESDDDNEQFDEAEEEMDTCDSLSSSSFKSIGSVFRTSSFSSDDDGLTNGFESENDDVDPSIKTIGFNYPHVKRRKKLPDPVEKEKSVSLWSMIKDNIGKDLTKVCLPVYFNEPLSSLQKCFEDLEYSYLLDQASEWGKRGNNLMRILNVAAFAVSGYASTEGRICKPFNPMLGETYEADYPDKGLRFFSEKVSHHPMIVACHCDGTGWKFWGDSNLKSKFWGRSIQLDPIGLLTLQFDDGEIVQWSKVTTSIYNLILGKLYCDHYGTMKIEGNGEYSCKLKFKEQSMIDRNPHQVQGIVEDKNGKTVARLFGKWDESIHYVMVDQGKVNESHLLWKRNKQPENPTKYNLTRFGITLNELTPGLKEKLPPTDSRLRPDQRYLEKGEYEMGNAEKLRLEQRQRQAREMQERGWKPKWFRKEKGSETYRYIGGYWEARDSGSWDDCPDIFGQVHQSIK", "text": "FUNCTION: May be involved in the transport of sterols. SIMILARITY: Belongs to the OSBP family."}
+{"protein": "MAKLLSCVLGPRLYKIYRERDTDRAATSVPETPTAVPAASSSSWDSYYQPRALEKHADSILALASVFWSISYYSSPFAFFYLYRKGYLSLSKVVPFSHYAGTLLVLLAGVACLRGIGRWTNPQYRQFITILEATHRNQSAENKRQLANYNFDFRSWPVDFHWEEPSSRKGSRGGPSRRGVALLRPEPLHRGTADTFLNRVKKLPCQITSYLVAHTLGRRMLYPGSVYLLQKALMPVLLQGQARLVEECNGRRAKLLACDGNEIDTMFVDRRGTAEPQGQKLVICCEGNAGFYEVGCVSTPLEAGYSVLGWNHPGFAGSTGVPFPQNEANAMDVVVQFAIHRLGFQPQDIVIYAWSIGGFTATWAAMSYPDISAVILDASFDDLVPLALKVMPDSWRALVTRTVRQHLNLNNAEQLCRFQGPVLLVRRTKDEIITTTVPEDIMSNRGNDLLLKLLQFRYPRVMTEEGLRAVRQWLEASSQLEEASIYSRWEVDEDWCVSVLRSYQAEHGPDFPWSVGEDMSVDGRRQLALFLARKHLHNFEATHCTPLPAQHFQMPWCL", "text": "FUNCTION: Phosphatidylserine (PS) lipase that mediates the hydrolysis of phosphatidylserine to generate lysophosphatidylserine (LPS). LPS constitutes a class of signaling lipids that regulates immunological and neurological processes (By similarity). Has no activity towards diacylglycerol, triacylglycerol or lysophosphatidylserine lipase (By similarity). Also has monoacylglycerol lipase activity, with preference for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy- Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD16 family."}
+{"protein": "MILSSFLKIERMSSMHELKFRDLNVEVNEEDTVLLSMTESEIIVLTKKEIDYGAKYINHIVLYCNTDGRFLNSFSIQTNEQVINVQKVDDSFLFLIDKEYEDSVRDVEPNIYLWNPIEGFHQSFYAGRYINSMIIDQNKNLWVGYDETGIFSCVDQEISTRGINKFVLKNGKYELYFHGVSSYVIDQYFSTFVSEDAIYLYYRSMGEDYLQKLNLLGETLERVEVGIECSSCIKNGSSIYLFSRDDDSYNIEKVFKTNDMQNYVEQKISNENNGESLCFTQVASYKDKVAGIDHNNKLFLLNNQSL", "text": "FUNCTION: Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. Neutralizes the tRNase activity of cognate toxin WapA upon expression in E.coli. Does not inhibit WapA from other strains of B.subtilis. The WapA C-terminus cannot be expressed on its own in E.coli, however it can be cloned in the presence of its cognate immunity protein gene. Cell contact is probably necessary for growth inhibition."}
+{"protein": "MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIEKKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS", "text": "FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:29301961). 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). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homomer. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Nucleus Nucleus speckle Cytoplasm, Stress granule Cytoplasm, Cytoplasmic ribonucleoprotein granule Cell projection, dendrite Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:15166247). In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (PubMed:17652158). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). SIMILARITY: Belongs to the CASC3 family."}
+{"protein": "MKIRIPDQKKAKNLEKIKWFFITAIFITSFFINNFFDKIGYFTRISIITLLVVFAISIALYTKKVKNVFVYINASKNEMKKITWPQYKETLYTTFIIISVTILISLLLWGLDSIIFRLIAFIISVRF", "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 inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecE/SEC61-gamma family."}
+{"protein": "AFHYAQLADVDSNAQAFLKSNMQAKYVKDCGIMCRHYKRAQQQQMNMKQWIK", "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": "MHRAAAVDTTPKIVFYYKCLLNKNWNEPINNIFWGEFFLLQPRLEVLSQLLRECPKQELTVNGPKFHSMYLYISEILKSKAESLRIRNSLATLQTFLAELSVRKPTDVNFTIFLLLGNIDSIDIQFSAFIKNLCQLVKDSEDVQSVEISLRFVLHFVSFLYNSSFISHIYGNYDVFSTLYTVILKRKFGFETAVYAIGLLSACDKFETVNTFRLGLSKIVDEEFFSSVLSSSAQQLISLRDFYVSIKPDNPLTGSFFNLFSLRSSSNNPDSDQESQFSRLPDERATMFFTIYELCCCNKLFLKKLVEGGEKNGEAPLEALLSLLSYINTHQRQSERSHHFSILSLILFHIIIDDRSLLYRLTDKKFKISVRVCSQRYPYPPNATKPATPLGYMLDICCIGIQHNMKLNLSATMYFLYFSFVYRAMTSLVQDGIRMEYHWLELWRVLFSFLDFVSVLINTSPTEDVTRLLELILDVLAYIISNGDALVIRSDELVDLFYKLLHSSKNFSSFSSKIPDERLGALNYLLEVTEYLTSKTVDLPRSTADEVESVIKLELESIPVAKQNAFGGVPPFKESQYRLFHKRASRGMADLLRRKSEAAN", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0588 family."}
+{"protein": "MTASGTHGGYDVLILYASDAAEWCQYLQNLFLSTRHIRKHHIQSYQLEGESAISDQELDLFNRSRSIIILLSAELVQNFYCPPVLQSLQEALWPPHKVVKLFCGVTDCDDYLTFFKDWYQWQELTYDDEPDAYLEAVKKAISEDSGCDSVTDTETEDEKTSVYSCQLAMNEEHESSKSTGEHLVVQPDHIRCGVQTTVYIIMKCRLDDKVKTEVEFSPENSSSVRVLAELENEYTISVEAPNLTSGTVPLQIYSGDLMVGETSVTYHTDMEEISSLLANAANPVQFMCQAFKIVPYSIEALDKLLTESLKKNIPASGLHLFGINQLEEDDMTTNQRDEELPTLLHFSARYGLKNLTALLLTCPGALQAYSVANKYGHYPNTIAEKHGFKDLRQFIDEYVETADMLKSHIKEELMQGEEDESVYESMAHLSTDLLMKCSLNPGSDEELYESMAGFVPGAPEDLYVEMLQSKPDTPISGDEISLTVKDSMLRKFLEGGSTDAPDSGEGVSQQYGEDLYYSVEKDTFPQEMASRPPVPVPRPESSSPQPDNELYISKVFAQKAQRPENLYVPRGKVRKETIVRPVRDLSQSSIYDPFAGMKTPGQRQLITLQEQVKMGILNVDEAVLHFKEWQLNQKKRSESFRFQQENLKRLRDSITRRQMEKQKSGKSADLEITVPIRRSHNTLGKPECGIYEYAPRKNIFPPKKELKRGDWKTESTSSTTSSASNRSSTRSILSVSSGMEGDSEDNEVSEASRSRSPIPSQAERLPLPLPERPPRVPPRGASRPVNCEGFYPPPVPPRGR", "text": "FUNCTION: Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3- kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll- like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein."}
+{"protein": "MRILKIQTLRGPNYWSIRRHKLIVMRLDLETLAETPSNEIPGFYEGLVEALPSLEGHYCSPGCHGGFLMRVREGTMMGHIVEHVALELQELAGMHVGFGRTRETATPGIYQVVIEYLNEEAGRYAGRAAVRLCQSIVDRGRYPKAELEQDIQDLKDLWRDASLGPSTEAIVKEAEKRGIPWMQLSARFLIQLGYGVNHKRMQATMTDKTGILGVELACDKEATKRILAASGVPVPRGTVINFLDDLEEAIEYVGGYPIVIKPLDGNHGRGITIDIRSWEEAEAAYEAARQVSRSIIVERYYVGRDHRVLVVDGKVVAVAERVPAHVIGNGRSTVAELIEEINQDPNRGDGHDKVLTKIELDRTSYQLLERAGYTLNSVPPKGTICYLRATANLSTGGTAVDRTDEIHPENVWLAQRVVKIIGLDIAGLDIVTTDISRPLRELDGVIVEVNAAPGFRMHVAPSQGIPRNVAGAVMDMLFPNEQSGRIPILSVTGTNGKTTTTRLLAHIYKQTGKVVGYTTTDGTYIGDYLVESGDNTGPQSAHVILQDPTVEVAVLETARGGILRSGLGFESANVGVVLNVAADHLGIGDIDTIDQLANLKSVVAESVYPDGYAVLNADDRRVAAMAEKTKANIAYFTMNSESELVRKHIQKGGVAAVYENGYLSIVKGDWTHRIERAEQIPLTMGGRAPFMIANALAASLAAFVQNVSIEQIRAGLRTFRASVSQTPGRMNLFNLGNYHALVDYAHNPASYEAVGAFVRNWTSGQRIGVVGGPGDRRDEDFVTLGKLAAEIFDYIIVKEDDDTRGRPRGSASELITKGITQVKPDARYESILDETQAINKGLDMAPANGLVVILPESVSRAIKLIKLRGLVKEEIQQQNSSTTVIDNQNGVASSSVINTLL", "text": "FUNCTION: Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer). SIMILARITY: In the C-terminal section; belongs to the MurCDEF family."}
+{"protein": "MNSFSAFSEMFGSDYESPVSSGGDYSPKLATSCPKKPAGRKKFRETRHPIYRGVRQRNSGKWVCELREPNKKTRIWLGTFQTAEMAARAHDVAAIALRGRSACLNFADSAWRLRIPESTCAKEIQKAAAEAALNFQDEMCHMTTDAHGLDMEETLVEAIYTPEQSQDAFYMDEEAMLGMSSLLDNMAEGMLLPSPSVQWNYNFDVEGDDDVSLWSY", "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": "MHIHKLKAKIKKKHQEKYLTKKKIQKKLFLNESEFRRLCIFKGIYPKDYKDIPLKFRNKFYKNKVYYTRNDYKKLSNEKIIQDFRKIKTSLKRYKKYKITLEDNERCKNIIKNFPKYKLDHIIKERFPILVYAVEQLNDALTAIIAYSFLPSNENIGIKNNLINQSIILRNHVKGYYLQAEILQKKITWLIPHIFTPYFDKSIDFKIITNFIEYYVTLLRFILYKLYRLDGMSYPPKEYKDLKNEKLNHLSFDKNYITKELSNELETKESTEDNIIEENEKKTKNGKTENCEKNDQENEKKTKNDKTKNCEKNDQKNDQKNDQKNDQKNDQKNEMKQIEHDIIXNDNTKSVKNLFKNHIFYIHSNMPFDVLSIIILSCGGTICWNSLYSPYKYDDKSITHEILEVSEENKNTQDSNKINNINEYTYKRSFIQPQYIFDCLNSNMILSCEDYNINKTLPVHLSPFIDDDNYKDLVKKDEYTINKMLSEDPQYNKSIQKNKTNSENKXNNYNDNENDMSEDEYNNAIRQKLRNDALNNQMEAENENNYNPQNDLKQENDLLNVQKINNQENIKRNKLALSKKKRKLYNKIEQAENRQKLTIEKFIKKSKNKKKQK", "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": "ERTHTGEKPFECPECHKRFTRDHHLKTHMRLHTGEKPYHCSHCDRQFVQVANLRRHLRVHTGERPYACELCAAK", "text": "FUNCTION: Krueppel is a gap class segmentation protein. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MYTCAKFVSTPSLIRRTSTLLSRSLSAVVVRRPETLTDESHSSLAVVPRPLTTSLTPSRSFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM", "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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family."}
+{"protein": "MSCIKMKDKCRNFSLSKWQDTRKPWLILIIVTIGLTCIAHFLFQEYLFMKPCEQCVYIRFDMLVMAIGGMIALINPANNIIKIFSYSLAFYGIWLGLEHCLTLNHIHEVVHSENPFAGVDGCREIPIYPFNLPLYKWASSWFLPTGECGMDTPVVPENAYNHLNAFQKFFIGTPPDFENGLYSNGWYLIPSLKFMNMAICCLIAFLCCFVVLFAMFIAYVLDKNKPNAKIFALVIVALVLVLKFIGESKNPNQNIASLNQVVLRYS", "text": "FUNCTION: Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. DsbI subfamily."}
+{"protein": "MATDSSMPGTVIGKAEFSDTKAASEFGTDLSRWRLNVDNGRHMWEYLESEDEARKRPQSFLEKYWLGLPYELPARPRATCALEAVENGWEFFKRLQTADGHWGCNDDGPLFVTSGMVIARYIVGIPIDSHMKQEMCRYLLNVVNEDGGWGLFIQSPSTVFGTVMNYCMLRILGLGPEHPAMAKARNTLHRLGSARATPTWGKFWLCVLGVYEWEGMVPLPPEPLLVPASLPFNPGKWWVHTRNVYISMSYLYGHRFSMPPNKLVQALRDELYDIPYQQINWPAQRTNVSAADRLTDPTWIQRSFTSALTMYETFKIPFLRRRALNEALFQIETETRNTHYLCIAPVSFASNMLALYHAHGRDSHWIRGMRDRFIDPMWLCREGLAASGTNGTSLWDTALTVQATIDAGLAARPENQAILRKALEFIDNSQIREDPLGVHHVYRQPTRGAWPFSTRDQSYAVSDTTAEAVKVIVLLQRIEGFPSRISDERLQQAIDLILGMENAGGGFSAYEPVRGPKFLELLNITELYENVMTDNLYPECTSSVIMCLTTFAREYPTYRPRDIQACLSRSIDYLLRSQYPNGGWFASWGVCFTYATMFALQGLACMGWNESNCAACQRACSFLLQHQNPDGGWGESLDTVRFKQYLPHPDGSQVTNTAYAVIGLLAARCGNHEAIRRGVAYLVKEQQDTGEWLPGPLEGVFAPPGGMRYPNYKFHFTLMALGRYVAIHGNECLAI", "text": "FUNCTION: Protostadienol synthase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)- oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:19951700, 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). FUNCTION: Protostadienol synthase which cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol), the biosynthetic precursor of helvolic acid, a secondary metabolite which promotes virulence. SIMILARITY: Belongs to the terpene cyclase/mutase family."}
+{"protein": "MGEIAPEMEISQYTKDKASCTRISIESYYSKRVTQCAERENRLKKLEEDISARGLSDEEKEEKRKIHHSKETDYLRLKRTRLTVNDFESLKVIGRGAFGEVRLVQKHDTGHIYAMKILRKSEMVEKEQTAHVRAERDILSEADCDWVVKMYYSFQDYSNLYLVMEFLPGGDMMTLLIKKDTLTEEATQFYIAEAALAIQFIHSLGFIHRDIKPDNLLLDARGHVKLSDFGLCTGLKKFHRTDHYRNWPSTLPPDFISKPFESKRKAETWKRNRRAYAYSTVGTPDYIAPEVFQPNGYTKSCDWWSLGVIMYEMLIGYPPFCSELPQETYRKVINWQQTLVFPSDVPISIEAKATIKRFCCEAERRLGNHGGLDEIKQCPFVKRIDWNHIRERPPPIRVTVKSIDDTSNFDDFPDEDLTWPTSTLIRPEEQPGRRGEFVDFTYKRFDGLTQKMRYSDLKKFQQAKKNKKGGQQGTSD", "text": "FUNCTION: Acts with sax-2 to restrict the growth of both primary and secondary neurites. Regulates mechanosensory tiling by controlling the termination point of sensory dendrites. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family."}
+{"protein": "MQSFRKIWNKPRPDDWMPLARFYYADSALNDIASELDSFDGRRDPDRCNALVTRLRVAQDRVLHIITEMLIHLYPREQDRACRDFRVKFPDEILHDTLPGQLWFGAECLSAGSNIIDHETESDLIRPLAKDVTKQLDFLRDLLKNQSLRDPSAYNPVIKENLLKFDKLFAEFEYQYVSAMVPVKSVKEHDSQLDVAVLFSEVLSLALVKDLITQDLIDYCDPSVMIAIPRLGIVWGLLVYSNGALNVDVPAENLSEMFRPFYSLLVKIRNLLRILTPTELTKLETVLCKGESAVPEDTSSTLTMSDFRTNATDEEKAKNNQRVWMCDMPSDSTSSLDSSVQDSSSETTSLASSALASPHSGSEENVSQIENEEGDDEAIGTNSNSSNEVTESPETIEEPDNVDMEESSESEVDTHIDETRNESDDEITDDVQASDVLQVETKKCKSSRLLEQKKFDKSVKTIIPMQTDPRSQIDPKNLRSRFRSSEDLVHRLFVCIAGVADQLQTNYSSEIRKVLKLILQPSEIIPVYEVVNAQVANSQTEGEETGVEAQETLPLPAFMGVRWVPDEDCEQCTACSMPFNFVRRRHHCRNCGRIFCHKCSCNTISIPEHGYDRKVRVCNLCYVHRLNSFGCNEPMSQVNENGATVPSVTEQQSAQTASASS", "text": "FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR) signaling. SIMILARITY: Belongs to the lst-2 family."}
+{"protein": "MTVVLDSKDLARIDEEYKADSQVWSYLTGGNGVSAADFVGANEVRINKLSGFVDAAAYQRGQDNARHTISVDKETVKLTHEDWFGYDLDQFDMDENGAYTVENVVREHNKMITIPHRDKVAVQKLFDSAAKKATDSITKDNALDAYDTAEAYMFDNEVPGGFVMFVSSAYYTALKQSAAVTRTFSTDGTMAINGIDRRVAQLDGGVPIVRVSSDRLKGLGITDHVNFILTPLSAIAPIVKYDSVSVIDPSTDRSGNRWTIKGLSYYDAIVLDNAKKGIYVAATAGA", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the Lactobacillus delbrueckii bacteriophages Gp34 family."}
+{"protein": "MPTIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQWCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTCKTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK", "text": "FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1- RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2 (By similarity). FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1- RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) direct ubiquitination of BCL2. SIMILARITY: Belongs to the SKP1 family."}
+{"protein": "MAKEGGRTAPCCSRPKVAALTVGTLLFLTGIGAASWAIVTILLRSDQEPLYQVQLSPGDSRLLVLDKTEGTWRLLCSSRSNARVAGLGCEEMGFLRALAHSELDVRTAGANGTSGFFCVDEGGLPLAQRLLDVISVCDCPRGRFLTATCQDCGRRKLPVDRIVGGQDSSLGRWPWQVSLRYDGTHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVARTSPHAVQLGVQAVIYHGGYLPFRDPTIDENSNDIALVHLSSSLPLTEYIQPVCLPAAGQALVDGKVCTVTGWGNTQFYGQQAVVLQEARVPIISNEVCNSPDFYGNQIKPKMFCAGYPEGGIDACQGDSGGHFVCEDRISGTSRWRLCGIVSWGTGCALARKPGVYTKVIDFREWIFQAIKTHSEATGMVTQP", "text": "FUNCTION: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2. Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Apical cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MARKYVPHTTELCENSLKKFKSLVGTVDKLLIITGAGISTESGIPDYRSKDVGLYTKTALEPIYFQDFMKSKKCRQRYWSRSYLNWPRFAQALPNFNHYALSKWEAANKFHWLITQNVDGLHLKAGSKMITELHGNALQVKCTSCEYIETRQTYQDRLNYANPGFKEQFVSPGQQELDADTALPLGSEQGFKIPECLNCGGLMKTDVTLFGENLNTDKIKVCGKKVNECNGVLTLGTSLEVLSGYQIVNHAHMQNKPIFIVNIGPTRADQMATMKLDYRISDVLKEM", "text": "FUNCTION: NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues. Plays a role in oxidative stress resistance (PubMed:23438705). Might promote neuronal cell death under ischemic conditions and cell death in touch neurons induced by mec-4 channel hyperactivation, possibly downstream of the insulin-like receptor daf-2 (PubMed:28820880). Might attenuate the reactive oxygen species (ROS) scavenging system, that eliminates ROS in ischemic conditions, under dietary deprivation and when glycolysis is blocked (PubMed:28820880). SUBCELLULAR LOCATION: Mitochondrion matrix Mitochondrion. SIMILARITY: Belongs to the sirtuin family. Class II subfamily."}
+{"protein": "MKLLILGNHTCGNRGDSAILRGLLDAINILNPHAEVDVMSRYPVSSSWLLNRPVMGDPLFLQMKQHNSAAGVVGRVKKVLRRRYQHQVLLSRVTDTGKLRNIAIAQGFTDFVRLLSGYDAIIQVGGSFFVDLYGVPQFEHALCTFMAKKPLFMIGHSVGPFQDEQFNQLANYVFGHCDALILRESVSFDLMKRSNITTAKVEHGVDTAWLVDHHTEDFTASYAVQHWLDVAAQQKTVAITLRELAPFDKRLGTTQQAYEKAFAGVVNRILDEGYQVIALSTCTGIDSYNKDDRMVALNLRQHISDPARYHVVMDELNDLEMGKILGACELTVGTRLHSAIISMNFATPAIAINYEHKSAGIMQQLGLPEMAIDIRHLLDGSLQAMVADTLGQLPALNARLSEAVSRERQTGMQMVQSVLERIGEVK", "text": "SIMILARITY: Belongs to the polysaccharide pyruvyl transferase family."}
+{"protein": "MGSSSLSEDYRLCLERELRRGRAGVCGDPSLRAVLWHILVEDFDLHGALQDDALALLTDGLWGRADLAPALRGLARAFELLELAAVHLYLLPWRKEFTTIKTFSGGYVHVLKGALSEDLLIQSFQKMGYVRRDAHRLMVAALPPARQLVQVALGCFALRLECEILGEVLAQLGTSVLPAEELLQARRASVDVASCVAWLQQRLAREEEPPPLPRRGSPTGCQARLDLYRDVQEDEGSDEASLYGGPSPGPDSPTSELACQPRFWEQSARLWGAGGGPWEPAEVSSPTSGASEEEEPQPEAFSFLSLRRELLSRPGDLAPPHAPRSPEQASPPPIPEPPGYQMHTCLAPGALPALCCDTCRQLHAAHCAALPSCHPGHSLRTLRGNSQRRLWLQRAQVDALLYDSPAAGP", "text": "SIMILARITY: Belongs to the SPATA2 family."}
+{"protein": "MTKSVDTLLIPGPIILSGAVQKALDVPSLGHTSPEFVSIFQRVLKNTRAVFKSAAASKSQPFVLAGSGTLGWDIFASNFILSKAPNKNVLVVSTGTFSDRFADCLRSYGAQVDVVRPLKIGESVPLELITEKLSQNSYGAVTVTHVDTSTAVLSDLKAISQAIKQTSPETFFVVDAVCSIGCEEFEFDEWGVDFALTASQKAIGAPAGLSISLCSSRFMDYALNDSKNGHVHGYFSSLRRWTPIMENYEAGKGAYFATPPVQLINSLDVALKEILEEGLHKRWDLHREMSDWFKDSLVNGLQLTSVSRYPSNMSAHGLTAVYVADPPDVIAFLKSHGVVIAGGIHKDIGPKYIRIGHMGVTACNKNLPYMKNCFDLIKLALQRKK", "text": "FUNCTION: Has alanine:glyoxylate aminotransferase activity. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MHKNNTTFLSRVFGINSRNIDVHNPLFADDSVIPLYDQNQSAYYDNAYSDYSSDEEDSKPRTSRQTDSNLHMTDHSGDGNDPFNQMDNSSRFSNSSSFHYNNTDQEDDNPELLLLQDEDSSLNRKNLDNSDFQSFAKKTFNQIPKIKFQLPKKEDYPTSHRQPPDIENQNGTLKSSVKKQIHFLDPMDKALWMWSNVSNLDTFLHQVYDYYTGNGFNCIMMNKFTELFTVVFIVWLFSFMGNCIDYDKLMNDRNVYQFSQVKIDKCYSKIGFFPQKLIYWLFFIGLCLKLYQIFLDYLVLKDMKLFFNLLLGLSDDELQTISWGLVVKRIMILRDKNINAIVSQNTDLTSRKRMNAHDIANRILRKENYMIAMYNKSILDLDIELPLIGKVQLLTNTLQWNLNIAILDYFFDSETGQINLPALKERNRHTISTELKKRLIFCGIINIVLAPILSIYFIMYYFLKFFYDFKTNPADISSREYSPYARWKLREFNELPHIFNRRLNISTESSNKYINQFPKETTTALLKFIMFISGSIVGVLVIVTILDPEFFLNFELTPGRTVLFYVSTLGAIFTICKNSIPDDTLVFDPEVSLRYLSQFTHYLPQEWEGKYHTEEVKNDFCKLYTLKLYLVGKEILSWLFLPYILCYKLPECADTISDFFREFSVHVDGLGYVCTFAMFQFNNQHNENGNANVHQNGNGNGGVPSAKSKSKKVPNPNRFTTKPSMRDMENDDKMIKSYMYFLESYGNDEIVQHQQALNRSLIYSTEISPTSGDDLNDSNILGLRQRNVATTGKRQNSIGNGLIYNGQNKRLSIGEAKTNVYSNPIASTVLDKDLQYKLANSYILNGMPGLNEANQPADRKNERKYSNDSPGVMKLVDKISQQHKA", "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 (By similarity). Essential for the formation of the sequestering membranes and assembly of the micropexophagy-specific membrane apparatus (MIPA) which mediates the fusion of the sequestering membranes and incorporation of the peroxisomes into the vacuole during micropexophagy (PubMed:11533052, PubMed:16079180). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=The peripheral pool of ATG9 partially colocalizes with mitochondria and it has been speculated that ATG9 resides either in the mitochondria or within vesicles in very close to the mitochondria. During methanol growth, localizes to multiple structures situated near the plasma membrane referred as the peripheral compartment (Atg9-PC). During glucose-induced micropexophagy, traffics from the Atg9-PC to unique perivacuolar structures (PVS) that contain ATG11, but lack ATG2 and ATG8. SIMILARITY: Belongs to the ATG9 family."}
+{"protein": "MEHFDASLSTYFRALLGPRDTRVKGWFLLDNYIPTFVCSAIYLLIVWLGPKYMKNRQPFSCRGILVVYNLGLTLLSLYMFYELVTGVWEGKYNFFCQGTRSAGESDMKVIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHATMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSSVPSMRPYLWWKKYITQGQLVQFVLTIIQTSCGVIWPCSFPLGWLYFQIGYMISLIALFTNFYIQTYNKKGASRRKEHLKGHQNGSMTAVNGHTNNFASLENSVTSRKQRKD", "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) (PubMed:22216341, PubMed:23873268). 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": "SDDKKAKAATSSVLTKFTQNQIQEMKEAFTMIDQNRDGLIDVSDLKEMYSNLGTAPQDSVLQAMVKEAPQMNFTGFLSLFSEKMSGTDPEETLRNAFQMFDSDNTGYIPEEYMKDLLENMGDNFSKDEVRQTWKEAPIAGGKVDYNAFVSKIKGKEQDDA", "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": "MSASALSSIRFPGSISEYLQVASVLSLLLLLFKTAQLYLHRQWLLSSTQQFPSPPSHWLFGHKILKDQDLQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLVFSRVRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLHLKKLQ", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins) (PubMed:17112342). 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:17112342). Catalyzes predominantly the oxidation of the terminal carbon (omega- oxidation) of saturated and unsaturated fatty acids (PubMed:17112342). May act as a major omega-hydroxylase for dodecanoic (lauric) acid in kidney (PubMed:17112342). Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20- hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Further catalyzes successive omega-oxidations of 20-HETE to the corresponding dicarboxylic acid, and may contribute to the degradation of PUFA by chain shortening (PubMed:17112342). Acts as an omega-hydroxylase and epoxidase toward (5Z,8Z,11Z,14Z,17Z)- eicosapentaenoc acid (EPA). Catalyzes stereoselective epoxidation of the last double bond of EPA, displaying a strong preference for the (R,S) stereoisomer (PubMed:17112342). Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency (PubMed:17112342). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MKKVIIRKTEEIENWRRNINSEINFIPTMGNLHDGHIKLISTAKNDNSNVNLVSIFINPLQFDNKLDLENYPQTIDNDIKISFSNGADAIFIPSYEDIYPPNNKNIKFLKAPKELSSALCGLNRIGHFDGVCTVVYRLLNLIKPKNLYLGEKDWQQLLILKNLVLRKNLNVAIRSIPTQRDFDGIPLSSRNVHLSKNERKLISFFSSELLEAKKIFQQDKKINLNQIIKKLSAKKISVEYLEHLHPHTLQKARPEDNISLLAGAIRCGETRLIDHVFLMKRRPIIAIDGPAGSGKSTVTKLIAKKLNLLYLDTGAMYRALSWLIIKESVDYKIEKKLQNILKDISIFFKSNTNSHQDVYVNNYCVTKEIRSQKISSIVSKISSIKEVRKFLVAEQRKIGESGGLVAEGRDIGTTVFPHAELKIFLTASIDERAKRRKYDKNSKDSQEIDLYTLKELIKKRDFEDSNREISPLIKANDAIEIITDGYTIDEVVDKIIDLYNDRIPKETEIK", "text": "FUNCTION: Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively. FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the pantothenate synthetase family. SIMILARITY: In the C-terminal section; belongs to the cytidylate kinase family. Type 1 subfamily."}
+{"protein": "MDSDLDRILPIASRALLCEGNRDWAGAYVSYCKVLEEMKKSSAARDRMGLGPLTGAEACSWNGLYDNCLSKASKLRKTILESEMERQNYQLAAKLSKKAPVDLHPLRPVRSQTPAYTPMTTRMMYRQTRGAQSEVNLSTPKQIYSKHSPPSTSTSSIVSSSYGDAPSYLAPSKPNRSPPLKPEDPFASFNSSASAIAAASKSAAASASALSSDTGRSATMNSTTFPTAMKSQSTTKPTLSNSVSSPSIQVSNNQNANNSTPLSFHAPIPPLHVPAVPLTSASHSSSDGKSRKHPSPYKPYLNSSHDTLGSSTRPSSADTAGSPATSPPATADSKTIVSKTISASTTQQTEPLQQTTPSSDFEYAIMNEIISNHEPVYWSDIAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHESSRRLKTEFLIQWSSLTNAAPDKQTGHSPRVLVLAATNLPWCIDEAARRRFVKRTYIPLPEKETRYKHLSHLLHNQVHCLTEEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDALLTTSAEMIPPISLNHFKASLRTIRPSVSQEGIHRYEEWNKQFGSQR", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AAA ATPase family."}
+{"protein": "MALSGHVLIDPARLPRDTGPELMWAPSLRNSLRVSPEALELAEREAERARSERWDRCAQVLKNRLLRVELDGIMRDHLARAEEIRQDLDAVVAFSDGLESMQVRSPSTGGRSAPAPPSPSPAQPFTRLTGNAQYAVSISPTDPPLMVAGSLAQTLLGNLYGNINQWVPSFGPWYRTMSANAMQRRVFPKQLRGNLNFTNSVSLKLMTEVVAVLEGTTQDFFSDVRHLPDLQAALILSVAYLLLQGGSSHQQRPLPASREELLELGPESLEKIIADLKAKSPGGNFMILTSGNKEARQSIAPLNRQAAYPPGTFADNKIYNLFVGAGLLPTTAALNVPGAAGRDRDLVYRIANQIFGEDVPPFSSHQWNLRVGLAALEALMLVYTLCETANLAEAATRRLHLSSLLPQAMQRRKPAMASAGMPGAYPVQTLFRHGELFRFIWAHYVRPTVAADPQASISSLFPGLVLLALELKLMDGQAPSHYAINLTGQKFDTLFEIINQKLLFHDPAAMLAARTQLRLAFEDGVGVALGRPSPMLAAREILERQFSASDDYDRLYFLTLGYLASPVAPS", "text": "FUNCTION: Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. Participates in the interaction between the capsid and the tegument through interaction with the large tegument protein/LTP. SUBCELLULAR LOCATION: Virion Host nucleus. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae CVC2 protein family."}
+{"protein": "MTSESTLPPVVPPLHSPKSPVWPTFPFHREGSRIWERGGGIAPRDLPSPLPTKRTRTYSATARASAGPVFKGVCKQFSRSQGHGFITPENGSEDIFVHVSDIEGEYVPVEGDEVTYKICPIPPKNQKFQAVEVVLTQLAPHTPHETWSGQVVGS", "text": "FUNCTION: RNA-binding factor which binds specifically to the very 3'- UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=PIPPin-RNA complexes are located to the nucleus."}
+{"protein": "MAETDQPGKIFIGGLNIKTRQKTLQEIFGRFGPVARVILMRDRETKKSRGFAFLTFRRPADAKNAVKEMNGVILDGKRIKVKQARRPSSLESGSKKRPPSFSRTRGASRILKCGRGGRSRARSGPSCEGNLGGDRYTPNFNVSSSGRHFAVKRNPSSKRDGPPSKRSATSAQTRSNTGLRGREPHRREISRNMPRGEPASSRRDEYPLPRDYGQSSNDRKYESTSRGYCDYGNYHSREESASKVFSDHAGYLGGRDRDFSEYLSGNSYRDTYRSYGRFHEAPSARGGNNRYDDYSNSQDGYGGRGEPYISNRSNIYSSDYERSGRQEVLPPPIDREYFDREGRQERGHSPKDGLYSASRESYSSNTKIWGIPWRSWRKQI", "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": "MDNRNTQMYTEGRIKVPGTQPSPGLRITIKRAGVEPTIPGVSQVMFPDASEVGSRKQLSSASGGPEKGPRYRDTFKEGPSELRTQEQRPPAKPGKKQSSWVPQEGSQELQAGQDQSELGLLPSWVPEGPEGLQQLGSGKEIEGQQRRQRNRGTGEDEPPESCQGPGYQSTLGHQADVVQPAEPCCPLAGRGQPLGDKRPKEADVPHIRPQEAPPEPSPGAHGDSSQEAMPPTSTVAPEEKTASSFLPSMPGPTKTKGGGEAVETQPAPGPLPPPEVRDIGERREPDRVQQQPQKPVVAAGTQNLRKFRQGFMKCLLEMEKVEASHRRALKARSLTAQKSPRTLTPVPTSSPSLPQTPASAPASGPSWARLSAPGPEPAPVGASVPTSTPCPVLLCPALDLGWRRMELSHHSSERTLSYAKARQEPEEQSLQKLYQNREKSEEQLTLKQEEAFRSYFEIFNGPGEVDAQSLKNILLLMGFSVTPAQVEDALMSADVNGDGHVDFKDFLAVMTDTRRFFCSVEQNALTDMAPHNPHTLLFEILPLLVEMLALPEAVLEEITNYYQKKLKAGTCKAQEMEAAIGRLRLQKQLPYNPQQEESSEVPERKVLSILSRLKQQNYAPNLQSPYAQVPCIPLCPRMDKKMVRRKPTNHYVQDQCTTPGLAPDIRSPFFQSRSQGNREHNSDSRKWPSSVPSRTH", "text": "FUNCTION: Involved in the differentiation of haploid spermatids."}
+{"protein": "MCDKEMCDKEMCEKKEEVDEDIYIASFDIGKVNFAYCIEKCFLKDIKKRTETTIDEMCSKGKIEIIDNVRLVSFPKNIVTRRRGPRKGTTYKPSGKYTFESLLLFLEERKTFWNKCHIFVIEQQMSQNKEGLKISYHLEAYFKTCYGTFKEVVLFPSYHKTQVFEAEKWINLDPLTRKTDKYGKPFYTKMSYNNRKKSCISKALEILEQRHDTDTIWKLERSQKKDDMCDVICQLQAYKWLYLFEK", "text": "SIMILARITY: Belongs to the IIV-6 170L family."}
+{"protein": "MRRCPCRGSLSEAEAGALPAEARMGLEALRGGRRRQPGLQRPGPGAGGPTGRPEGGGPRAWIEESSLHSEAERTDLEPAPCPNGPQAESCGDGHAECEAAGLVVASEKPRQNKELDGSNLQTHPRRNSPLVEMEMAGSWTDGFRTDLHRSDLQSRPKRASLCTQPGFDESWTELDRSDMWQTLPERDNKPRVDNLRTHHGVSKLQTHPVCLSPESSADNSGKELSADASRTPHDTDGFWIESQTDDSLKGPSTQTACRQPGSDGFSSKDTESALTQPGTDGLRDDSVLGESNGNDPLDLSEPGELVTNLCSHLECSSLCPVPRLIITPETPEPEAQPVGPQSRIEGGTGGFSSASSFDESEDDLVAGGGGTSDPEDRAGSKPWKKLKTVLKYSPFVVSFHKHYYPWVQLSGHAGNFQAGEDGRILKRFCQCEQRSLELLMGDPLRPFVPAYYGMVQRDGQAFNQMEDLLADFEGPSIMDCKMGSRTYLEEELVKARERPKPRKDMYEKMVAVDPGAPTPEEHAQGAITKPRYMQWRETLSSTSTLGFRIEGIKKADGTCNTNFKKTQALEQVTKVLEDFVNGDLGILRKYVARLEDLRETLENSPFFKTHEVVGSSLLFVHDHTGLAKVWMIDFGKTVALPDHQMLSHRLPWTEGNREDGYLWGLDNLICLLQGLAQS", "text": "FUNCTION: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5- trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis (By similarity). Can phosphorylate inositol 2,4,5-triphosphate to inositol 2,4,5,6-tetraphosphate (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles actively between nucleus and cytoplasm with both nuclear import and nuclear export activity. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family."}
+{"protein": "MASEIHMSEPMCLIENTEAQLVINQEALRILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKRTGFSLGSTVQSHTKGIWMWCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAVLLSSTFIYNSIGTINQQAMDQLHYVTELTDLIKSKSSPDQSDVDNSANFVGFFPIFVWTLRDFSLDLEFDGESITPDEYLETSLALRKGTDENTKKFNMPRLCIRKFFPKRKCFIFDRPGDRKQLSKLEWIQEDQLNKEFVEQVAEFTSYIFSYSGVKTLSGGITVNGPRLKSLVQTYVSAICSGELPCMENAVLTLAQIENSAAVQKAITYYEEQMNQKIHMPTETLQELLDLHRTCEREAIEVFMKNSFKDVDQKFQEELGAQLEAKRDAFVKKNMDMSSAHCSDLLEGLFAHLEEEVKQGTFYKPGGYYLFLQRKQELEKKYIQTPGKGLQAEVMLRKYFESKEDLADTLLKMDQSLTEKEKQIEMERIKAEAAEAANRALAEMQKKHEMLMEQKEQSYQEHMKQLTEKMEQERKELMAEQQRIISLKLQEQERLLKQGFQNESLQLRQEIEKIKNMPPPRSCTIL", "text": "FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:18025219, PubMed:21551061, PubMed:24739961, PubMed:24715728). Hydrolyzes GTP to GMP in two consecutive cleavage reactions: GTP is first hydrolyzed to GDP and then to GMP in a processive manner (By similarity). Following infection, recruited to the pathogen-containing vacuoles or vacuole-escaped bacteria and promotes both autophagy and inflammasome assembly (PubMed:21551061, PubMed:24739961, PubMed:24715728). Promotes host defense against bacterial infections by regulating bacteriolytic peptide generation via its interaction with ubiquitin-binding protein SQSTM1, which delivers monoubiquitinated proteins to autolysosomes for the generation of bacteriolytic peptides (PubMed:21551061). Also 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). Confers protection to several pathogens, including the bacterial pathogens L.monocytogenes and M.bovis BCG as well as the protozoan pathogen T.gondii (PubMed:18025219, PubMed:21551061). Exhibits antiviral activity against influenza virus (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Lipid- anchor; Cytoplasmic side Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm Secreted Note=Localizes to pathogen-containing vacuoles or to the cell surface of bacteria that escaped vacuoles. Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of IFNG induction. Golgi membrane localization requires isoprenylation and the presence of another IFNG- induced factor. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. GB1 subfamily."}
+{"protein": "MSEFSQTVPELVAWARKNDFSISLPVDRLSFLLAVATLNGERLDGEMSEGELVDAFRHVSDAFEQTSETIGVRANNAINDMVRQRLLNRFTSEQAEGNAIYRLTPLGIGITDYYIRQREFSTLRLSMQLSIVAGELKRAADAAEEGGDEFHWHRNVYAPLKYSVAEIFDSIDLTQRLMDEQQQQVKDDIAQLLNKDWRAAISSCELLLSETSGTLRELQDTLEAAGDKLQANLLRIQDATMTHDDLHFVDRLVFDLQSKLDRIISWGQQSIDLWIGYDRHVHKFIRTAIDMDKNRVFAQRLRQSVQTYFDEPWALTYANADRLLDMRDEEMALRDEEVTGELPEDLEYEEFNEIREQLAAIIEEQLAVYKTRQVPLDLGLVVREYLSQYPRARHFDVARIVIDQAVRLGVAQADFTGLPAKWQPINDYGAKVQAHVIDKY", "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. 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. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. Note=Restricted to the nucleoid region. SIMILARITY: Belongs to the MukF family. SIMILARITY: Belongs to the MukF family."}
+{"protein": "MAISSFKHEHPLEKRQAEAARIREKYPDRIPVIVERAEKSDVPDIDRKKYLVPADLTVGQFVYVVRKRIKLSPEKAIFIFVKNILPPTAAIMSAIYEEHKDEDGFLYMSYSGENTFGIFF", "text": "FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation. May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor Vacuole membrane; Lipid-anchor Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the ATG8 family."}
+{"protein": "MSALQLTPQAASLAERLADLAVDALIAEADLSPKPALVDRRGSGAHTDLHLGLMHSSALSLWPTFKLMADAAGQFNTVGQPLREALGRLGRDGEATMLRTTQGVNTHRGAIWALGLLVTAAALDARNCAPEAVLARAASLAQIKDRQVLVQGSHGNEVVRRYGVMGAREQAQQGFPAVRDFALPQLQRSRAAGSGEQNARLDALLAIMTTLSDTCVLHRAGIEGLHTMQRGAQHVLDVGGSASLAGRRALNQLDQQLLALNASPGGAADLLAACLFIDGLEPALGRVSRSV", "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": "MLWAFIVWLGALCIYGSAFDILIYAPRMMQSHVYFTARIANVLAARGHKVTVIDNVFRYDVDNELSSDIHEIISVEPSPEVTKLLNTGSLPTILWNSKASPEEQRTIMEGLGHVHRLQCTHLIENSTLIPKLQEIKFDFAIHEVFDSCGVGILEVIGVQKTVIVSSTGPMDVVPITLGISDTLNTPSLLSDYGSYLSFFEKRRNLKFLSGMLNFHEMQDSMISPLFKKYYGLKKPTGEIMRQANLLFYNIHEGSDGMRMRGRRSFDIGGIAFKDQKNLTMEYQTLLSDPRPKVLVSFGTAATSSHMPQNLKNSLMTAMKQMNNVLFIWKYEMEDNFTKQEELTTNIIFKKFLPQTDLLASSKIDLFVTHCGQNSLLEAFNSGVRVLAVPLFGDQHRNAKLAFENGLIEILPKSDIETPAKIVKAVKTGLEPNAKLDQNIVLISSLLRNSKENAENLLISTIEATYSTEFPPNFSKFPKNYHPNTLVRLIDSSIALVFMLFIFVFVNHFRKNYVGFKYPLSFSTK", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MLQQQESPIPRLGVGEEGVVGRHVFGEVWGVNDKLLQDDEYLKNLVIKAAEVANMHLVDVKVWRFGGGDKGGVSVIALVLESHIAIHTWPAYNYATIDVYTCGEHSRPWDAYDYIIKQLNPKTFTKTIVDRSSK", "text": "FUNCTION: Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity. SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily."}
+{"protein": "MNAPLRGQVYRCDLGYGAKPWLIVSNNARNRHTADVVAVRLTTTRRTIPTWVAMGPSDPLTGYVNADNIETLGKDELGDYLGEVTPATMNKINTALATALGLPWP", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an endoribonuclease on single-strand RNA, cleaving between the first and second bases in the sequence UCGCU. Neutralized by coexpression with cognate antitoxin MazE1. FUNCTION: Residues 29-56 inhibit ssDNA cleavage by DNA topoisomerase. This fragment does not have mRNA cleavage activity but it inhibits growth upon overexpression in M.smegmatis. FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an endoribonuclease (mRNA interferase) on single-strand mRNA, cleaving between the first and second bases in the sequence UCGCU. Overexpression in M.smegmatis but not E.coli inhibits growth, this effect is neutralized by coexpression with cognate toxin MazE4. FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an endoribonuclease on single-strand RNA, cleaving between the first and second bases in the sequence UCGCU. Neutralized by cognate antitoxin MazE4. SIMILARITY: Belongs to the PemK/MazF family."}
+{"protein": "MWLLLALLSIFQETPAFSLEASEEMEQEPCPAPISEQQEQVLTVALGQPVRLCCGRTERGRHWYKEGSRLASAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMTVVHNLTLIMDDSLPSINNEDPKTLSSSSSGHSYLQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIRYSYLLDVLERSPHRPILQAGLPANTTAVVGSNVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTTDINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPAEEEDLAWTTATSEARYTDIILYVSGSLALVLLLLLAGVYHRQAIHGHHSRQPVTVQKLSRFPLARQFSLESRSSGKSSLSLVRGVRLSSSGPPLLTGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEALGMDSSRPDQTSTVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPNNGDASSTCSSSDSVFSHDPLPLEPSPFPFPEAQTT", "text": "FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down- regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endosome Endoplasmic reticulum Note=Internalized from the cell membrane to recycling endosomes, and from there back to the cell membrane. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily."}
+{"protein": "MITKRKKKSYTSVYALGQYISMSAHKARRVIDQIRGRSYEEALMILELMPYRGCYPIFKLVYSAAANASHNKGFKETNLVISKAEVNQGNTVKKLKPRARGRSYPIKRSTCHITIVLEDISFYQQYEEYLMYLKKPGCSNENRNLTCYDTYSSGGLWDKK", "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": "MATFTDAEIDELFETSGTVIDNIITAQGKPAETVGRSAIPQGKTKVLSAAWEKHGSIQPPASQDNPDRQDRSDKQPSTPEQTTPHDSPPATSADQPPTQATDEAVDTQLRTGASNSLLLMLDKLSNKSSNAKKGPMVEPPRGESPTSDSTAGESTQSRKQSGKTAEPSQGRPWKPGHRREHSISWTMGGVTTISWCNPSWSPIKAEPKQYPCFCGSFPPTCRLCASDDVYYGGDFPKSK", "text": "FUNCTION: Protects the virus against cell antiviral state by blocking host interferon signaling. Mechanistically, targets host phosphorylated STAT1 (phospho-STAT1) for degradation, thereby inhibiting the interferon alpha signaling pathway (PubMed:12885886, PubMed:26859759). Plays a role in the inhibition of host apoptosis (PubMed:30290847). Interacts with and down-regulates the expression of host TXNL1. In turn, inhibits TXNL1-induced apoptosis through the BCL2-BAX-caspase 3 pathway (PubMed:30290847). Inhibits host apoptosis also by negatively regulating host CacyBP/SIP (PubMed:30234028). Promotes viral replication by activating the extracellular signal-regulated kinase (ERK) pathway (PubMed:30213106). SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the paramyxoviruses V protein family."}
+{"protein": "MNFKYIVAVSFLIASGYARSVKNDEQSLSQREVLEEESLREIRGIGGALLSVGKSALKGLAKGFAEHFGKRTAEDHEVMKRLEAVIRDLDSLDHPEEASEREARGFNQEEIANLFTKKDKRILGPVLSLVGNALGGLIKKIG", "text": "FUNCTION: Maximin-H16 shows antimicrobial activity against bacteria and against the fungus C.albicans. Shows strong hemolytic activity (By similarity). FUNCTION: Maximin-y 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": "MVSIHNSFILLMLMISICFCEKCLTNEECDLKWPDAICVRGRCRCSENTIRKKSASREWVCLATNDATGNSGPPLTCPTPEGAGYQVMYRKDGEPVKCSSKKKPDTCPEGFECIQGLSILGALDGVCCPDRAKTCVHPIFDHPDDGYLSRWGFDGEQCIEFKWNPERPSSANNFKTRAHCEDYCIGSINGITNYHQSNFHLF", "text": "FUNCTION: Appears to lack serine protease inhibitor activity in vitro when tested with bovine pancreatic alpha-chymotrypsin and elastase (PubMed:19716386). Involved in cuticle biosynthesis (PubMed:16500660, PubMed:19716386)."}
+{"protein": "MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLRSRTLTRTSQETADVKASVLLGSRGLDISHISQRLESLSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQESEPSYISDAGPPGRSSLDSIEMAYARQIYIYNEKIVNGHLQPNLLDLCASVTELDDKNISDMWAMVKQMTDVLLVPATDALKSRNSVEVRMEFVRQALGYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPLPGLQDGEVEGHPVWALIYYCMRCGDLLAASQVVNRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDVTDNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAIAFLFRMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCMRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDSQGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLELMNKLLSPIVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIDRLKLVPLNQESVEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSATRPQRVIEDRDSQLRSQARALITFAGMIPYRTSGDTNARLVQMEVLMN", "text": "FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling. SUBCELLULAR LOCATION: Nucleus membrane; Peripheral membrane protein Nucleus, nuclear pore complex Nucleus envelope 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": "MAPTKRKGECPGAAPKKPKEPVQVPKLLIKGGVEVLEVKTGVDAITEVECFLNPEMGDPDDNLRGYSQHLSAENAFESDSPDRKMLPCYSTARIPLPNLNEDLTCGNLLMWEAVTVKTEVIGITSMLNLHAGSQKVHENGGGKPVQGSNFHFFAVGGDPLEMQGVLMNYRTKYPQGTITPKNPTAQSQVMNTDHKAYLDKNNAYPVECWIPDPSRNENTRYFGTYTGGENVPPVLHVTNTATTVLLDEQGVGPLCKADSLYVSAADICGLFTNSSGTQQWRGLARYFKIRLRKRSVKNPYPISFLLSDLINRRTQKVDGQPMYGMESQVEEVRVFDGTEQLPGDPDMIRYIDRQGQLQTKMV", "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 VP2 or VP3 proteins. Interacts with gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated 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. SUBCELLULAR LOCATION: Virion. Host nucleus. SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family."}
+{"protein": "MWKEKVSVTPPYHFDRVLDRLSLDPLNAVDREAREVRVPIRNQAGDVCIVKVQALGHAGEPEFLVSGETDQGEMMKEIKRIFQWENHLQHVLDHFSKTSLSAIFEEHAGTPLVLDYSVYNCMMKCIIHQQLNLSFAYTLTERFVHAFGEQKDGVWCYPKPETIAELDYQDLRDLQFSMRKAEYTIDTSRMIAEGTLSLSELPHMADEDIMKKLIKIRGIGPWTVQNVLMFGLGRPNLFPLADIGLQNAIKRHFQLDDKPAKDVMLAMSKEWEPYLSYASLYLWRSIE", "text": "FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions. SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family."}
+{"protein": "MYALKRELWCVLLLCGAICTSPSQETHRRLRRGVRSYRVTCRDEKTQMIYQQHQSWLRPLLRGNRVEHCWCNDGQTQCHSVPVKSCSEPRCFNGGTCLQAIYFSDFVCQCPVGFIGRQCEIDARATCYEDQGITYRGTWSTTESGAECVNWNTSGLASMPYNGRRPDAVKLGLGNHNYCRNPDKDSKPWCYIFKAEKYSPDFCSTPACTKEKEECYTGKGLDYRGTRSLTMSGAFCLPWNSLVLMGKIYTAWNSNAQTLGLGKHNYCRNPDGDTQPWCHVLKDHKLTWEYCDLPQCVTCGLRQYKEPQFRIKGGLYADITSHPWQAAIFVKNRRSPGERFLCGGILISSCWVLSAAHCFQERFPPHHVRVVLGRTYRLVPGEEEQAFEVEKYIVHKEFDDDTYDNDIALLQLKSDSLTCAQESDAVRTVCLPEANLQLPDWTECELSGYGKHEASSPFYSERLKEAHVRLYPSSRCTSKHLFNKTITNNMLCAGDTRSGGDNANLHDACQGDSGGPLVCMKGNHMTLVGVISWGLGCGQKDVPGVYTKVTNYLNWIRDNTRP", "text": "FUNCTION: Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MNAHAALTLYTDGACLGNPGPGGWAFALVPSDVPFLETGQXAPEAAAFTRSGSAYPSTNNRMELCAVINALQEAHGRAAEAVVVVTDSQYVRKGITQWIHTWKHNGWKTAAKQPVKNKDLWEALSALADALSVEWRWVKGHAGDPYNELCDRLATDAARRAAQSTADCP", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase H family. SIMILARITY: Belongs to the RNase H family."}
+{"protein": "MKKVGTAFLTTLFIFSSFTSAHAEEKKDSKAFIDVSAATLWTAPDSLRPIDVPSATNPVDLWKWTKSMTLDEKLWLTNANKLETQALLGQEVTVVDKKGDWVKVLVHGQPTPRNEEGYPGWMPEKQLTYNQEFADKTNEPFVLVTKPTAILYINPSEKHKSLEVSYNTRLPLLSEDTISYRVLLPNGQKAWLRKNDGTFYRSQNDIPTPAADDLINTGKMFLGLPYIWAGTSGFGFDCSGFTHTIYKSHGITIPRDSGPQSRNGVAVDKEHLQKGDLIFFAHDQGKGSVHHVAMYIGDGNMIHSPRAERSVEIIPLNTPGYIEEYAGARRYLP", "text": "FUNCTION: Specifically hydrolyzes gamma-D-glutamyl-L-lysine bonds in murein peptides, releasing L-Ala-D-Glu. SIMILARITY: Belongs to the peptidase C40 family."}
+{"protein": "MEVPGANATSANTTSIPGTSTLCSRDYKITQVLFPLLYTVLFFAGLITNSLAMRIFFQIRSKSNFIIFLKNTVISDLLMILTFPFKILSDAKLGAGHLRTLVCQVTSVTFYFTMYISISFLGLITIDRYLKTTRPFKTSSPSNLLGAKILSVAIWAFMFLLSLPNMILTNRRPKDKDITKCSFLKSEFGLVWHEIVNYICQVIFWINFLIVIVCYSLITKELYRSYVRTRGSAKAPKKRVNIKVFIIIAVFFICFVPFHFARIPYTLSQTRAVFDCNAENTLFYVKESTLWLTSLNACLDPFIYFFLCKSFRNSLMSMLRCSTSGANKKKGQEGGDPSEETPM", "text": "FUNCTION: Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Required for normal platelet aggregation and blood coagulation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MGLPALLASALCTFVLPLLLFLAALKLWDLYCVSSRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGAGCLSNLHDSSHKQRKKVIMQAFSREALQCYVLVIAEEVSSCLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPGPAGGGEDEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGVKARNLIHARIEENIRAKIRRLQATEPDGGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREEIKSKGLLCKSNQDNKLDMETLEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFTNKEEFNPDRFIVPHPEDASRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPARFTYFQGDI", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:9250660, PubMed:9442090, PubMed:15911617). RAs exist as at least four different isomers: all- trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (PubMed:9250660, PubMed:9442090, PubMed:15911617). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity). Involved in the convertion of atRA to all-trans-4-oxo-RA (PubMed:15911617). Able to metabolize other RAs such as 9-cis, 13-cis and 9,13-di-cis RA (PubMed:9250660). Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans- 5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (Probable). May play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MSLSVSRRLAAVTAFAVAGLFASAVPAALAAPSAVAAAPTPPDIPLANVKAHLSQLSTIAANNGGNRAHGRAGYKASIDYVKGKLDAAGFTTTLQTFTSSGATGYNLIADWPGGDPNSVLMAGSHLDSVTSGAGINDNGSGSAAVLETALAVSRAGLQPTKHLRFGWWGAEELGLIGSKYYVNNLPAAEKAKISGYLNFDMIGSPNPGYFVYDDDPTIEQTFKNYYAGLGVPTEIETEGDGRSDHAPFKNAGIPVGGLFSGADYTKTAAQAQKWGGTSGQAFDRCYHSSCDSLTNINDTALDRNSDAVAYAIWTLGAGTPVPPGQSFENTADVNVPDSPAAAVSSPITVSGVTGNAPATTKVDVNIVHTYRGDLVVDLVAPDGTVYNLHNRSGGSADNLVQTYTVNASSEVANGVWNLRVKDTAAQDVGYINSWKITF", "text": "FUNCTION: A leucine-specific metalloprotease that plays a role in controlling the amount of leupeptin during colony development. Degrades leupeptin into three components, acetyl-leucine, leucine and argininal. Has a strict preference for leucine at the P1 site. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily."}
+{"protein": "MLCFFVLFFCCGTVLLEGADIDEIEHADKRRPIWNMGHMVNAVYQIDEFVDLGANAIETDVTFTKSANAEYTYHGVPCDCHRWCKKWEYVNDFLKALRRATTPGDAKYRSQLILVVFDLKTDYLTASTAYDAGKDFAKRLLQHYWNGGSNGGRAYIILSIPDLAHYKFINGFKEQLKTQGHEDLLAKVGYDFWGNEDLSSTRAAFQKAGVQDKEHIWQSDGITNCWLRTLKRVREAVANRDSSNGYINKVYYWTVDKYASVRDAINAGADGIMTNYPNVIVDVLKENDFKGKFRMATYNDNPWETFK", "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) with high activity (PubMed:18082635). 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, massive inflammatory response, platelet aggregation, increased vascular permeability, and causes edema and death in mice (PubMed:18082635). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the arthropod phospholipase D family. Class II subfamily. Class IIa sub-subfamily."}
+{"protein": "MAATTANPEMTSDVPPLGPAIASGNPGPGIQGGGAIVQRAIKRRPGLDFDDDGEGNSKFLRCDDDQMSNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGTYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGNSSVDSVSMNRLSFVRNRCRNGLGSAKDGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNVCQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRSKNREWLWVRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPSLSNTIQRPQLGPTANLSLEMGSGQLAPRQQQQQTELDVVPGRDGLTSCNHSQVSVQPVTTTGPEHSKPLEKSESLFAQDRDPRFSEIYSNISTDQSKGISSSTVPATQQLFSQGNTFPPTPRPAENFRNSGLAPPVTIVQPSTSAGQMLAQISRHSNPTQGAAPAWTPSTRPGFSAQQVVTEATAKTRSSQFGVGSFQTPSSFSPMSLPGASTASPGAAAYPSLTNRGSNFAPETGQTAGQFQTRTAEGVGVWPQWQGQQSHHRSSSNEQHVQQPSAQQPGQPEVFQEMLSMLGDQSNSYNNEEFPDLTMFPSFSE", "text": "FUNCTION: Required for activity of the AHR. Upon ligand binding, AHR translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Not required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex initiates transcription of genes involved in the regulation of a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (By similarity). The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (By similarity). The heterodimer ARNT:AHR binds to core DNA sequence 5'- TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKDFKKKIIMKISRIEYKHTAFSAEYKDVEKVYKKLRDNMDKVATGINNLMTYEHGGSAMKKIYHGLSMVSSASRMNYFSDADIFEGFARINKDLTDSDLDEGVREVGRKTAEAYENISKAKEKFNEQCGREMEVLMSMKKRAETTDKERENAKIYRYDLEKAKQSNNPEDQEEVDRLSELFENSQTRTIEMMRDFIGADGLQGVLTRVRDLNIEFHQESVKALERTK", "text": "SUBCELLULAR LOCATION: Spore wall. SIMILARITY: Belongs to the SWP12 family."}
+{"protein": "GKPICGETCFKGKCYTPGCTCSYPICKKN", "text": "FUNCTION: Probably participates in a plant defense mechanism (Potential). Binds to and induces leakage in phospholipd membranes, particularly ones containing 1-palmitoyl-2-oleophosphatidylethanolamine (POPE) (PubMed:26322745). In vitro, displays cytotoxicity against cultured cells (PubMed:26322745). Not active against Gram-negative bacterium E.coli ATCC 25922 or Gram-positive bacterium S.aureus ATCC 25923 up to a concentration of 64 uM (PubMed:26322745). SIMILARITY: Belongs to the cyclotide family. Moebuis subfamily."}
+{"protein": "MIESCFNVGIWATGLALLMNQGQSPLLSNVGLSVLAYKATAMFIPRVGPSFIKRGFSGKDMNKVEKYVIPETMGAVSALVYFMCMIIFIPVLFYKYLVPNHNPNLPSDGSVAEVAKSQFPHDLLGAYLSALLSILSVSLLGILDDLFDIRWRHKFFLPAIAAIPLLVVYYVDYGVTYVSVPSIVRPFLKRSLINLGFLYYFYMAAVAIFCPNSINIIAGVNGVEAGQSLVLALVIACNDLFYVLSPKNKDALRAHLLSLYLVLPLIGVTAGLLKYNWWPSRVFVGDTFCYFAGMVMAVVGILGHFSKTLMLFFIPQIFNFALSVPQLFGLVECPRHRLPKLNVKTGLLENSYTEFSLNEHPLPKKTLLTISIFEKLRLIRVEYDPSTGRPLRCTNFTIINFVLYHLGPMREDHLTICIMGLQLLTGIFGLIIRHFVAPLVYPEDNI", "text": "FUNCTION: Catalyzes the initial step in the synthesis of dolichol-P-P- oligosaccharides. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family."}
+{"protein": "MSEKSREEEKLSFKEQILRDLEKVKGYDEVLKEDEAVVRTPANEPSAEELMADSLSTVEEIMRKAPTVPTHPSQGVPASPADEIQRETPGVPSHPSQDVPSSPAEESGSRPGPGPVRPKKLEREYNETPTRVAVSYTTAEKKAEQAGPETPTPATETVDIIRDTSRRSRREGAKPAKPKKEKKSHVKAFVISFLVFLALLSAGGYFGYQYVLDSLLPIDANSKKYVTVGIPEGSNVQEIGTTLEKAGLVKHGLIFSFYAKYKNYTDLKAGYYNLQKSMSTEDLLKELQKGGTDEPQEPVLATLTIPEGYTLDQIAQTVGQLQGDFKESLTAEAFLAKVQDETFISQAVAKYPTLLESLPVKDSGARYRLEGYLFPATYSIKESTTIESLIDEMLAAMDKNLSLYYSTIKSKNLTVNELLTIASLVEKEGAKTEDRKLIAGVFYNRLNRDMPLQSNIAILYAQGKLGQNISLAEDVAIDTNIDSPYNVYKNVGLMPGPVDSPSLDAIESSINQTKSDNLYFVADVTEGKVYYANNQEDHDRNVAEHVNSKLN", "text": "FUNCTION: Mutations in this gene suppress deletion of PBP2b (penA); truncation at residue 168, undefined changes between residue Ile-447 and Ala-505, and mutation of Ala-505 suppress the penA deletion. Probably part of the elongasome which synthesizes peripheral peptidogylcan. FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Localizes to midcell in the presence and absence of khpB (also called eloR/jag). SIMILARITY: Belongs to the transglycosylase MltG family."}
+{"protein": "MAIALAEADKYEVLEKIGCGSFGIIRKVKRKSDGFILCRKEINYIKMSTKEREQLTAEFNILSSLRHPNIVAYYHREHLKASQDLYLYMEYCGGGDLSMVIKNLKRTNKYAEEDFVWRILSQLVTALYRCHYGTDPAEVGSNLLGPAPKPSGLKGKQAQMTILHRDLKPENIFLGSDNTVKLGDFGLSKLMHSHDFASTYVGTPFYMSPEICAAEKYTLRSDIWAVGCIMYELCQREPPFNARTHIQLVQKIREGKFAPLPDFYSSELKNVIASCLRVNPDHRPDTATLINTPVIRLMRREVELNNLSRAARKREEATMQKAKDVEQAFAKLEKEKQQIRSELENSIRREWEVKARLEIDRQVQNELDKLRKRFECEVQDRVAQEVEKQRRNANYREDASLRSSGHSSQMSSSNSEDSDFPSSTDISQLSLESPTNKAAKLPKKESRTPFTRSKTVVDSPMDIQMAEPSPISIASLSLSPRRTSATYSGKNIFAEGERKRPKFEPTLAYSDDEDDTPELPSPTRPKVKPDPFKAPSRPLLRQNTTALMQKLSTQPPIFPANPSRLPQMSAPDVRESKSRSPHRRLSKIPSSANLAADAGSPTRKNGVKSSPSKMNGGDEMFKAVMQRNMGGRTLVELAQARAGGRPIDEVKRCASDSRSGCSVPMKSADRDPPAVWDPERDEMPSPFLARGRKVIRNLR", "text": "FUNCTION: Protein kinase that plays an important role in mitotic regulation. Seems to be phosphorylated and thereby activated by CDC2/cyclin B during mitotic activation. It is also required for spindle formation and for nuclear envelope breakdown. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
+{"protein": "MKTIILLGLLGATMSAPLIPQRLMSASNSNELLLNLNNAQLQPLPFQGPFNSWIPPFSGILQQQQQAQIPGLSQFSLSALDRFAGLFPNQTPFPGRVSFAQGTQVGQQDPSQPQTPPQTQQSPNHVMPYVFSFKMPQEQAQMLQYYPVYMLLPWEQSQQTAPQSPPQTGQQQFEEQMPFYTQFGYVPVQVEPVMPGGQQQLALDPVLGTAPETVVMPAGVIPYLRKEVINFKHANGGIFVPSTSQTPSTTNYFAPAIDPTITPELMEKKAKTDYLKEP", "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": "MTTSFYDLECKDKKGESFKFDQLKGKVVLIVNVASKCGFTPQYKELEELYKKYQDKGFVILGFPCNQFGKQEPGSDEQITEFCQLNYGVTFPIMKKIDVNGSNADSVYNYLKSQKAGLLGFKGIKWNFEKFLVDSNGKVVQRFSSLTKPSSLDQEIQSLLSK", "text": "FUNCTION: Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Plays an important role in the oxidative stress-induced response in the presence of Ca(2+). Has peroxidase activity using preferentially thioredoxin as a reducing power. The redox state of the mitochondrial GPX2 is regulated by TRX1 and TRX2 (cytoplasmic thioredoxin), and by TRX3 (mitochondrial matrix thioredoxin) (PubMed:16251189). Involved in sporulation (PubMed:21763276). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the glutathione peroxidase family."}
+{"protein": "MLQLCDSECDGLSSLMECGGAVNSPGDTLGQSPAHLAACGGQAFFLLWQLQTGVDVNQQDCFGEAPIHKAARSGSMECLSLLIASDARIDMCNKDGHTAEDVALSCGFLDCARYLATIKLTQDTFSRAQSSLHNLKETAAGVKRGQCCQSISHGKRRRSDGFV", "text": "SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MIKQLYKNITICSLTISTALTVFPATSYAKINSEIKAVSEKNLDGDTKMYTRTATTSDSQKNITQSLQFNFLTEPNYDKETVFIKAKGTIGSGLRILDPNGYWNSTLRWPGSYSVSIQNVDDNNNTNVTDFAPKNQDESREVKYTYGYKTGGDFSINRGGLPGNITKESNYSETISYQQPSYRTLLDQSTSHKGVGWKVEAHLINNMGHDHTRQLTNDSDNRTKSEIFSLTRNGNLWAKDNFTPKNKMPVTVSEGFNPEFLAVMSHDKKDEGKSKFVVHYKRSMDEFKIDWNRHGFWGYWSGENHVDKKEEKLSALYEVDWKTHDVKFVKVLNDNEKK", "text": "SIMILARITY: Belongs to the aerolysin family."}
+{"protein": "MSQRMQQGQPMIIMGEDAQRVKDRDAQEYNIRAARAVAEAVRSTLGPKGMDKMLVDSMGDVTITNDGVTILKEMDIDNPTAEMIVEVAETQEDEAGDGTTTAVAIAGELLKNAEDLLEQDIHPTAIIRGFNLASEKAREEIDDIAERVDPDDEELLKKVAETSMTGKSSELNKELLADLIVRAVRQVTVEANDGSHVVDLENVSIETQTGRSASESELLTGAVIDKDPVHDDMPVQFDEADVLLLNEPVEVEETDIDTNVSIESPDQLQKFLDQEEAQLKQKVDQIVDSGADVVFCQKGIDDLAQHYLAKQGILAVRRTKKSDIRFLKNITGAAVVSDLDSIEAAVLGRASVRRDEAGELFYVEGIGDDVHGVTLLLRGSTDHVVDELERGVQDALDVVASTVADGRVLAGGGAIEVELASRLRNYADSVSGREQLAVEAYADALELVPRVLAENAGLDSIDTLVDLRAAHEDGQVRAGLNVFTGEVEDAFDAGVVETAHAKEQAVASASEAANLVLKIDDIIAAGDLSTGGDDDEEGGAPGGMGGMGGMGGMGGAM", "text": "FUNCTION: Molecular chaperone that assists in the folding or refolding of nascent or denatured proteins along with ATP hydrolysis (Probable). ATPase activity is highest in thermosome assemblies containing CCT1:CCT2, followed by assemblies containing CCT1:CCT2:CCT3. Seems to contribute to thermosome ATPase activity. Not required for growth. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
+{"protein": "MNMKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNNEVAAAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKAVSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETATQQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNTNNTNTNTPSKNTNTNSNTNTNTNSNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFGRV", "text": "FUNCTION: This major extracellular protein may be involved in the invasion of non-professional phagocytic cells by Listeria. SUBCELLULAR LOCATION: Cell surface Secreted. SIMILARITY: Belongs to the peptidase C40 family."}
+{"protein": "MLIADDLEKLLEILPHFVREPLKQHSNRKNLIEVVMDLGRRPEARFPGNPEYLSQRSISWQDLDYCVKKVGNFSGDNRAGIEKTLHRISSMRNREGSIIGLTCRVGRAVFGTISIIRDLLEQGDSILLLGKPGVGKTTAVREIARVLSDEMEKRVVIIDTSNEIAGDGDIPHPAIGRARRMQVAQPDLQHQVMIEAVENHMPEVIIIDEIGTELEALAARTIAERGVQLVGTAHGNYLESLIKNPTLADLIGGIQYVTLGDDEAKRRGTQKSILERKAAPAFQIAIEIHDRKAWIVHEKVEETIDQILQGHQPFVQKRQIQDNGRILIKCYPSQSTEVLSTNSSSLQKMSSLKQKTHFLQQREVKNKTFDLNKLENRDTSLLSTTINTPVNINNHSFQVEASIQYLYAYSLSWQHITSVISALDLPIILTKEIEKSDAILALRSQVKQNTKLRQIAKSRQIIIYTIQNSTVPQITRALRKILNINTSSDLNWVKLCKSKKFYEIQALQEAKLAIEIIILNENSIVQLTPRSAYIRKMQHNLIDNYQLRARSFGEEPYRKLRIYPE", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf45 family."}
+{"protein": "MRLDRFLANLPELSRRDAQMLIAGGHLRVDGQVVRDGTHEVRVFSRVELDERLLQAGKPARYYMLHKPMGCVSATRDPQHPTVLDLFPEDLRDDLHIGGRLDYNTTGLMLLTNDGQWSRRLTLPGSRRDKVYYVETEAPIDQRYVDAFAAGLHFRFEDLVTLPAQLEPIGPRCARLTLHEGRYHQVKRMFGHFDNKVLRLHRERMGDICLDPQLPPGAWRPLNAEEICSV", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RsuA family."}
+{"protein": "AEIKVRDGYIVYPNNCVYHCGLNPYCNDLCTKNGAKSGYCQWLTKWGNACYCYALPEKVPIKDPSYKCYS", "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 against rat Nav1.2/SCN2A and B.germanica Nav1. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
+{"protein": "MAFLKKSLFLVLFLGLVSLSVCEEEKRESEEEKNEQEEDDRDERSEEKRLLGMIPLAISAISALSKLG", "text": "FUNCTION: Antimicrobial peptide active against Gram-positive bacteria and fungi but inactive against Gram-negative bacteria. Also inhibits growth of B.dendrobatidis zoospores at high concentrations. Shows anticancer activities. Shows hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Medusin subfamily."}
+{"protein": "MKALLLTFSLSLLAALQAQAFPTTEENQDVSGTWYLKAAAWDKEIPDKKFGSVSVTPMKIKTLEGGNLQVKFTVLISGRCQEMSTVLEKTDEPGKYTAYSGKQVVYSIPSAVEDHYIFYYEGKIHRHHFQIAKLVGRNPEINQEALEDFQNAVRAGGLNPDNIFIPKQSETCPLGSN", "text": "FUNCTION: Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MQRSEGGSETPSTVALRTSTSAQAPVVQPVPASQQRVLVQATGSSQKGAQVQQLPVPRVQQVPQQVQQVQHYHSQQVQYVEGAEAVYPNGTIRAAYSYNPESQLYGQGSGSAYFDSQAGGAQVTTVVSSGGVPTHGMVGIAMDVGGSQIISSGSAYLIHGGMEGGRHHTSHSSRSSSAMLEMAIENLQKSEGIATHKSSLLNSHLQWLLDNYETAEGVSLPRSSLYNHYLRHCQEQKLDPVNAASFGKLIRSVFMGLRTRRLGTRGNSKYHYYGIRLKPDSPLNRMQEDTQYMAMRQTPVHQKQRFKPFHKMDGMGDSLNSGSQHLSSTPEQSVAAQCQHHQQYIDVSHVLPPFPSLDLGSCPLPESISMTDVKKLQSSYRIHCEATLDVVMNLQFHLIEKLWQTFWHSTAPSSDGATTIPNSEEDVEDIRGFPRDKLITLCKYEPIKQWMRSCDHILYQALVEILIPDVLRPVPSTLTQAIRNFAKSLEGWLTSAMTNFPPEIISTKAAVVSAFAQTLRRYTSLNHLAQAARAVLQNTSQINQMLSDLNRVDFANVQEQASWVCQCDESVVQRLELDFKATLQQQSSLDQWAAWLDNVVNQVLKPYDGSLSFPRAARQFLLKWSFYSSMVIRDLTLRSAASFGSFHLIRLLYDEYMFYLVEHRVAQATGETPIAVMGEFSDLSSLMPSLKEQDTSFSDDMTSDGDMSRMSERSLTEPAVKRERIEIPHSLQEI", "text": "FUNCTION: Transcription factor that acts as a key regulator of ciliogenesis (PubMed:22233545). Specifically regulates expression of genes required for cilium assembly and function (PubMed:22233545). Recognizes and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on promoters (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mainly expressed in the nucleus and at lower level in cytoplasm. SIMILARITY: Belongs to the RFX family."}
+{"protein": "MAKYLAQIVVMGMQVVGRAFTRALRQEFAASKVAAEARGRAGTESAAVSSLSGISLQEAQQILNVSKLTPEEIQKNYEHLFKVNDKGLGGSFYLQSKVVRAKERLDQEMEIQSKTHKPKEETTQT", "text": "FUNCTION: Regulates ATP-dependent protein translocation into the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the TIM16/PAM16 family."}
+{"protein": "MSVFIDKNTKVMVQGITGSTALFHTKQMLDYGTQIVAGVTPGKGGQVVEGVPVYNTVEEAKNETGANVSVVYVPAPFAADSIIEAADADLDMVICITEHIPVVDMVKVKRYLQGRKTRLVGPNCPGVITADECKIGIMPGYIHKKGHVGVVSRSGTLTYEAVHQLTEEGIGQTTAVGIGGDPVNGTNFIDVLKAFNEDSETKAVVMIGEIGGTAEEEAAQWIKENMNKPVVGFIGGQTAPPGKRMGHAGAIISGGKGTASEKIKTLNDCGVETADTPSEIGTTLIDAAKKAGIYEELLTIKK", "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 nucleotide specificity is provided by the beta subunit. SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family."}
+{"protein": "MTDLPFTLDQLRILKAIASEGSFKKAAESLYISQPAVSLQIQNLEKQLNIPIFDRANRKAVFTEEGDTLLRYGNRVLSLCDETCRAIEDLKTLQGGTLIIGASQTTGTYLMPRLIGLFRHKYPQIAVQLQVHSTRRVAWSVANGQVNLAVVGGKVPDELRSKLQITPYVDDELALILPKLHPFSKLEVIQKEDLYRLRFITLDKQSTIRRVIDTVLNEHGIDSARFKIEMELNSVEAIKNAVQSGLGAAFVSISAIAKELELGLLHWVKIEGVVIKRTLSIITNPSRYQAKASEIFSKEILTLFVTPYEI", "text": "FUNCTION: Trans-acting transcriptional regulator of RuBisCO genes (rbcL and rbcS) expression. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MLITKNQAEKWFDNSLGKQFNPDLFYGFQCYDYANMFFMIATGERLQGLYAYNIPFDNKARIEKYGQIIKNYDSFLPQKLDIVVFPSKYGGGAGHVEIVESANLNTFTSFGQNWNGKGWTNGVAQPGWGPETVTRHVHYYDDPMYFIRLNFPDKVSVGDKAKSVIKQATAKKQAVIKPKKIMLVAGHGYNDPGAVGNGTNERDFIRKYITPNIAKYLRHAGHEVALYGGSSQSQDMYQDTAYGVNVGNNKDYGLYWVKSHGYDIVLEIHLDAAGESASGGHVIISSQFNADTIDKSIQDVIKNNLGQIRGVTPRNDLLNVNVSAEININYRLSELGFITNKNDMDWIKKNYDLYSKLIAGAIHGKPIGGLVAGNVKTSAKNQKNPPVPAGYTLDKNNVPYKKETGYYTVANVKGNNVRDGYSTNSRITGVLPNNATIKYDGAYCINGYRWITYIANSGQRRYIATGEVDKAGNRISSFGKFSTI", "text": "FUNCTION: Has weak lytic activity toward S.aureus cells. Full-length protein has no activity, but fusion of the Peptidase C51 domain to the lysostaphin SH3 cell wall binding domain yields an active chimeric enzyme, suggesting that PH may be functional."}
+{"protein": "MSVSKIAFVLSAIASLAVADTSAAETAELQAIIGDINSHLSDYLGLETGNSGFQIPSDVLSVYQQVMTYTDDAYTTLFSELDFDAITKTIVKLPWYTTRLSSEIAAALASVSPASSEAASSSEAASSSKAASSSEATSSAAPSSSAAPSSSAAPSSSAESSSKAVSSSVAPTTSSVSTSTVETASNAGQRVNAGAASFGAVVAGAAALLL", "text": "FUNCTION: Seems to have esterase activity. Prefers ester of fatty acids from 4 to 16 carbon atoms. SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI- anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP) found only in mother cells. SIMILARITY: Belongs to the SRP1/TIP1 family."}
+{"protein": "MIATSRAVNMNKESKHKKAVAKPCRERQTSVTRAMRPAVARDPRRLSTSSSPSSSPMSAQRRLSREEIINEMEKEQDAIVVRLLREIETLKEENSRLKNQLHHPVPARRSSPFFEGESAILDDDDCNYGYTLDTPKLKLTDGASRHTVLPLTPKDSMTHISHSARRSSRNASISNGTSISDTIFPIETKIHSAPTTNRNLPSADLPHHTLLPRSLSGISSSDLTESGALLHDRRRRSSNYSLDGSNSLKADLMAKRFQTGSLK", "text": "FUNCTION: May be a component of a protein phosphatase type 2A (PP2A) complex. Negatively regulates SIT4 phosphatase, a modulators of caffeine sensitivity. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "WFSFIREAYQGAEDMWRAYSDMKEANWRDSDKYFHARGNYDAAKRGPGGVWAAEVISDAREGIQSLMGRGHEDSMADQEANRWGRSGNDPNHYRPAGLPDKY", "text": "FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL complex. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SAA family."}
+{"protein": "MPKQVIIPPGTTTPIAPFVPGTLADGVVYVSGTLPFDKQNNVVHIGDPKAQTRHVLETIKSVIETAGGSMADVTFNSIFITDWTNYAAINEVYAEFFPGDKPARFCIQCGLVKPDALVEIASVAHIGAPT", "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": "MSPPGSAAGESAAGGGGGGGGPGVSEELTAAAAAAAADEGPAREEQRPIQPSFTKSLCRESHWKCLLLSLLMYGCLGAVAWCHVTTVTRLTFSSAYQGNSLMYHDSPCSNGYVYIPLAFLLMLYAVYLVECWHCQARHELQHRVDVSSVRERVGRMQQATPCIWWKAISYHYVRRTRQVTRYRNGDAYTTTQVYHERVNTHVAEAEFDYARCGVRDVSKTLVGLEGAPATRLRFTKCFSFASVEAENAYLCQRARFFAENEGLDDYMEAREGMHLKNVDFREFMVAFPDPARPPWYACSSAFWAAALLTLSWPLRVLAEYRTAYAHYHVEKLFGLEGPGSASSAGGGLSPSDELLPPLTHRLPRVNTVDSTELEWHIRSNQQLVPSYSEAVLMDLAGLGTRCGGAGGGYAPSCRYGGVGGPGAAGVAPYRRSCEHCQRAVSSSSIFSRSALSICASPRAGPGPGGGAGCGGSRFSLGRLYGSRRSCLWRSRSGSVNEASCPTEQTRLSSQASMGDDEDDDEEEAGPPPPYHDALYFPVLIVHRQEGCLGHSHRPLHRHGSCVETSL", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM151 family."}
+{"protein": "MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK", "text": "FUNCTION: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway (PubMed:8135828, PubMed:29915090, PubMed:30850536). 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 (PubMed:29915090). Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long- chain fatty acids (PubMed:30850536). Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3- ketoacyl-CoA thiolase activity (PubMed:8135828, PubMed:29915090, PubMed:30850536). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane Mitochondrion outer membrane Endoplasmic reticulum Note=Protein stability and association with membranes require HADHA. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
+{"protein": "MTMMDMNFKYCHKIMKKHSKSFSYAFDLLPEDQRKAVWAIYAVCRKIDDSIDVYGDIQFLNQIKEDIQSIEKYPYEHHHFQSDRRIMMALQHVAQHKNIAFQSFYNLIDTVYKDQHFTMFETDAELFGYCYGVAGTVGEVLTPILSDHETHQTYDVARRLGESLQLINILRDVGEDFENERIYFSKQRLKQYEVDIAEVYQNGVNNHYIDLWEYYAAIAEKDFRDVMDQIKVFSIEAQPIIELAARIYIEILDEVRQASYTLHERVFVYKRKKAKLFHEINSKYHRI", "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 head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid 4,4'-diapophytoene (dehydrosqualene). SIMILARITY: Belongs to the phytoene/squalene synthase family. CrtM subfamily."}
+{"protein": "MKIWSSEHVFGHPWDTVIQAAMRKYPNPMNPSVLGVDVLQRRVDGRGRLHSLRLLSTEWGLPSLVRAILGTSRTLTYIREHSVVDPVEKKMELCSTNITLTNLVSVNERLVYTPHPENPEMTVLTQEAIITVKGISLGSYLESLMANTISSNAKKGWAAIEWIIEHSESAVS", "text": "FUNCTION: In vitro, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space. Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the slowmo family."}
+{"protein": "MRNVKGGVWKNTEDEILKVAIMKYGLNQWARISSLLTRKSPAQCKARWHEWLDPSIKKTEWSKEEEEKLLHLAKIFPSQWKTIAPLVGRTASQCLERYNRLLDEVQRQQDNENGGGSGGGGTTTTTTTTTGENDPRRLRMGDIDPTPETKPAKPDPIDMDEDEKETLSEAKARLSNTQGKKEKRKFREKQLEEARRLAFLQKKRELKAAGINYNPKKKGKEKSWDISKEIPFYLKPKAGFYDVPDEELRDEPNKDASFIGKRVDQIENPNYLQRQEKLNKLEDIKKSKKEIFNLPQLISETSKSNDVEHSIKRTKLQLPEPQLTDDDIQEISDYEKLNGSGSGGGSGGVGVGEFPLPAPRTASISSTAANNNTNNIRTPMKQDTIMSEAQNLLALSNAQTPLKGGAGPNVSQTPLPKSVNNSTPFRTPNPLANQTPTQHNKKQSLNDSNEFAIEDKFKRQQGKNQLLSNLKNLPSPTIEYKLELPSELPTIEDDTTLELDNSEIHIREQQQLKHKEQFKLRNRSTVLKRNLPRSRNLFPINKNNNNNNNNNINQDELRILKEINRIISHDNKTFPNDSITPSSTFDDDDDDDNHHHHHDDIDNNSINDNDEKYENYDYFTNTELEFADKLIRDEIEQIKQELKQPLPSSNEILEEIDQIRSQFIYLPKENQFIEKSNANQTQLIENLQFEYDKTLNKIKNSSMKSVNLEKKLNIYNGGYQNRSNTIIKNIDDMFDQLEQSEIEYQCFVALKNNESIQMEKRLKSIENQVYDQCEIESRLQQKYAQLLNEKNLLKKKLSIF", "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. May also play a role in the response to DNA damage (DDR). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=May shuttle between cytoplasm and nucleus. SIMILARITY: Belongs to the CEF1 family."}
+{"protein": "MPKTASRRREITQLLGKVDINFEDDIHMSIANDLFEAYGIPKLDSAEECINTAFPSLDQGVDTFRVEYLRAEILSKFDGHPLGIDTEAAAWEKFLAAEEGCRQTNERLSLVKYHDNSILSWGERVIHTARRKILKLIGESVPFGDVALRCRFSGGATTSVNRLHGHPSWKHACPQDVTKRAFKYLQAFKRACGDVVDLRVNEVRTSNKAVTVPKNSKTDRCIAIEPGWNMFFQLGVGAVLRDRLRLWKIDLNDQSTNQRLARDGSLLNHLATIDLSAASDSISLKLVELLMPPEWYDLLTDLRSDEGILPDGRVVTYEKISSMGNGYTFELESLIFAAIARSVCELLEIDQSTVSVYGDDIIIDTRAAAPLMDVFEYVGFTPNRKKTFCDGPFRESCGKHWFQGVDVTPFYIRRPIRCLADMILVLNSIYRWGTVDGIWDPRALTVYEKYLKLLPRNWRRNRIPDGYGDGALVGLATTNPFVIVKNYSRLYPVLVEVQRDVKRSEEGSYLYALLRDRETRYSPFLRDADRTGFDEAPLATSLRRKTGRYKVAWIQDSAFIRPPYLITGIPEVKLAS", "text": "FUNCTION: This is the catalytic subunit of the viral RNA-dependent RNA polymerase complex. This complex is involved in viral RNA replication that produces (+)-stranded genomes via a complementary, (-)-stranded intermediate. Binds RNA cooperatively with the host ribosomal protein S1."}
+{"protein": "MCRRPDCGFSFSPGPVILLWCCLLLSIVSSAAVSVAPTAAEKVPAECPELTRRCLLGEVFQGDKYESWLRPLVNVTGRDGPLSQLIRYRPVTPEAANSVLLDDAFLDTLALLYNNPDQLRALLTLLSSDTAPRWMTVMRGYSECGDGSPAVYTCVDDLCRGYDLTRLSYGRSIFTEHVLGFELVPPSLFNVVVAIRNEATRTNRAVRLPVSTAAAPEGITLFYGLYNAVKEFCLRHQLDPPLLRHLDKYYAGLPPELKQTRVNLPAHSRYGPQAVDAR", "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": "MIMSSTMSTEAALVPNESVFDTVSSFNEDDANYSVLDLYDDDDEGDDSSTVERKEILTTRELEKAKAFTSLIMADPENFDRYGFSKKGYFISQEEYDKWWTEYNRYTERRKKKWENFLLKNKIELHNDNPLVYPARTDELSKFVRKGIPAEWRGNAWWYFAGGQRQLDANVGVYDRLKSDCREGAVSGKDMEAIERDLYRTFPDNIHFHKESFQNGEPAIIRSLRRVLMAFSVYDKTIGYCQSMNFLVGLLLLFMEEEKAFWMLVIITGKYLPGVYESDLEGANVDQGVLVLCIKEYLPEIWSHIESSYMNGNGSTDQISGPASGEEYLCRLPTLTLCTASWFMSCFVGVVPIETTLRIWDCLFYEESHFLFKVALGILKLSESEFLESKSQKLFRQYSSYTFGGSNDSDSTFKRLKNKIKTQEEADMEILQVIQNFPKRLLNPNDIFEKVLMKKKVALNGITQEKIDRGREYVAMARNRQRASSRPKERRK", "text": "FUNCTION: Regulates exocytosis by functioning as a GAP for SEC4. 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": "MKQLKLTGFVIFFFFLTESLTLPTQPQDVDDVRITQKFIDDNIGYITIIAFAQYIQEASFEEVEMLVKAMTEYRDKCLADRTLPECSKLANEVLLENICAMEGLPQKYNFSHCCHKVDFERRLCFFHNKKADIGLLPPLPTLDPEEKCQTYKNNRESFLNNYVYEVSRRNPFVFAPTLLTVAARFEEMTKTCCEEQEKANCFQTKAEPFIYYLKALSSYQKNACRALMKFGRQILQSINIAILSQKFPKIGFKQLTSLLEDVSSKYDGCCEGDVVQCIRGRSKVMSHICSKQDSISSKIKDCCEKKIPERGECIIYSNKDDRPNDLSLREAKFIESDNVCEKRDADQANFMAEFLYEYSRRHPELSTPELLRIAKVYKDLLKECCNMENPPECYRHAENRFNETTEKSLKIVQRECEHFQNLGKDDLKYHYLINLTKLAPQLSTEELTFLGKEMVMALTTCCTLSEEFACVDNLVDLVLGELCGINENRNINPAVDHCCKTNFAFRRSCFESLEADKTYVPPSTSQGLFTFHADLCQAHNEELQRKKDRFLVNLVKLKPELAGEELWSLLADFTNVVEKCCKAQEPEACFKEESPKLAAKSQAA", "text": "FUNCTION: Functions as carrier for hydrophobic molecules in body fluids. Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (PubMed:26902720). Binds vitamin E. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient. May be involved in the transport of vitamin E across the blood-brain barrier (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ALB/AFP/VDB family."}
+{"protein": "VYPHFKTPIQCRFLTSDSISIRRRTAVSRWRSPTFSANYNGVNAQVLGVLKQEQKEIEEEKRSSSLAEKLRLGSLTEDGLSYKEKFIVRCYEVGINKTATVETIANLLQEVGGNHAQSVGFSTDGFATTPTMRKLHLIWVTARMHIEIYRYPAWSDVVEIETWCQSEGRIGTRRDWIIKDFATDEVIGRATSKWVMMNQDTRRLQKVSDDVRDEYLVFCPKTPRLSFPEENNKSLKKISKLEDPAQHSRLGLSPRRADLDMNQHVNNVAYIGWVLESIPKEVLYTHELETITLDYRRECQHDDVVDSLTSPEVDEDTAVTKIIGTNGHAAAATEARDDSLKFLHFLRVSGQGLEINRGRTEWRKKSEKR", "text": "FUNCTION: Plays an essential role in chain termination during de novo fatty acid synthesis. High thioesterase activity for oleoyl-ACP versus other acyl-ACPs. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the acyl-ACP thioesterase family."}
+{"protein": "MPTYYLALHGGQSYNLIVDTDMSGNPSLSVIPTNPYQEQLSNNPLIQLQIVVGENTGAPAPPQPPPPPPPPPPPERRDAWTQEPLPLDMNPLGSDASQGPLASSIRMLCMAQYLLRNARGQQGLLRPLGPQTRSQVTLERQPVHNPRQEAPIILLQSPAPPRFTPVPMVALGHTLQPTPPPRPTLPQPRIPLIIPPRHTNQPATTPPTAPQRLTLGHQLSLPPHPPPHQSTPHCSSDSTGLPPPPTSYSIPSMTLSPEPLPPPAAPAHPLPGVIYDQQALPPTPGPPWWPPVRDPTPTTQTPPTNTKQGPDQGQGRGRWRGRGRSKGRGRMHKLPEPRRPGPDTSSPSMPQLSPVVSLHQGQGPENSPTPGPSTAGPVCRVTPSATPDISPIHEPESSDSEEPPFLFPSDWYPPTLEPAELDESWEGIFETTESHSSDEENVGGPSKRPRTSTQ", "text": "FUNCTION: Plays a key role in the activation of the host resting B-cell and stimulation of B-cell proliferation. Acts by up-regulating the expression of viral EBNA1-6, LMP1, LMP2A and LMP2B genes, as well as several host genes including CD21, CD23 and MYC. Activates transcription by acting as an adapter molecule that binds to cellular sequence-specific DNA-binding proteins such as host CBF1, SMARCB1 and SPI1. Once EBNA2 is near promoter sites, its acidic activating domain recruits basal and activation-associated transcription factors TFIIB, TAF40, TFIIH components ERCC2 and ERCC3, and CBP in order to promote transcription. Alternatively, EBNA2 can affect activities of cell cycle regulators and retard cell cycle progression at G2/M phase. It also induces chromosomal instability, by disrupting mitotic checkpoints, multi-nucleation and formation of micronuclei in infected cells (By similarity). SUBCELLULAR LOCATION: Host nucleus matrix. Note=Associated with the nuclear matrix. SIMILARITY: Belongs to the herpesviridae EBNA2 family."}
+{"protein": "MKFYIDDLPILFPYPRIYPEQYQYMCDLKHSLDAGGIALLEMPSGTGKTISLLSLIVSYQQHYPEHRKLIYCSRTMSEIDKALAELKRLMAYRTSQLGYEEPFLGLGLTSRKNLCLHPSVRREKNGNVVDARCRSLTAGFVREQRLAGMDVPTCEFHDNLEDLEPHSLISNGVWTLDDITEYGEKTTRCPYFTVRRMLPFCNVIIYSYHYLLDPKIAERVSRELSKDCIVVFDEAHNIDNVCIESLSIDLTESSLRKASKSILSLEQKVNEVKQSDSKKLQDEYQKLVRGLQDANAANDEDQFMANPVLPEDVLKEAVPGNIRRAEHFIAFLKRFVEYLKTRMKVLHVIAETPTSFLQHVKDITFIDKKPLRFCAERLTSLVRALQISLVEDFHSLQQVVAFATLVATYERGFILILEPFETENATVPNPILRFSCLDASIAIKPVFERFRSVIITSGTLSPLDMYPKMLQFNTVMQESYGMSLARNCFLPMVVTRGSDQVAISSKFEARNDPSVVRNYGNILVEFSKITPDGLVAFFPSYLYLESIVSSWQSMGILDEVWKYKLILVETPDPHETTLALETYRAACSNGRGAVLLSVARGKVSEGVDFDHHYGRAVIMFGIPYQYTESRVLKARLEFLRDTYQIREADFLTFDAMRHAAQCLGRVLRGKDDHGIMVLADKRYGRSDKRTKLPKWIQQYITEGATNLSTDMSLALAKKFLRTMAQPFTASDQEGISWWSLDDLLIHQKKALKSAAIEQSKHEDEMDIDVVET", "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 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. The ATP-dependent helicase activity of XPD/rad15 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 TFIIK controls the initiation of transcription. XPD/rad15 acts by forming a bridge between TFIIK and the core-TFIIH complex. Involved in the maintenance of the fidelity of DNA replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily."}
+{"protein": "MEAYEQVQKGPLKLKGVAELGVTKRKKKKKDKDKAKLLEAMGTSKKNEEEKRRGLDKRTPAQAAFEKMQEKRQMERILKKASKTHKQRVEDFNRHLDTLTEHYDIPKVSWTK", "text": "FUNCTION: Isoform 1, but not isoform 2 or isoform 3, may induce G2 arrest and apoptosis. May also increase cell sensitivity to apoptotic stimuli. FUNCTION: May induce G2 arrest and apoptosis. May also increase cell sensitivity to apoptotic stimuli. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. SIMILARITY: Belongs to the FAM32 family."}
+{"protein": "MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW", "text": "FUNCTION: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (PubMed:9218461, PubMed:8663431, PubMed:10770950, PubMed:9572851, PubMed:9485382, PubMed:18629440, PubMed:23590222, PubMed:24648509, PubMed:24343571, PubMed:32110987, PubMed:23659204, PubMed:29748552). Mediates calcium- dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (PubMed:27206388, PubMed:17567603). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (PubMed:26745724). May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes (PubMed:15308695). Acts as an attachment receptor for HCV (PubMed:21806988). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Cell membrane; Lipid-anchor; Cytoplasmic side. Nucleus Cytoplasm Cytoplasm, perinuclear region Note=Localizes to the perinuclear region in the presence of RELT (PubMed:22052202). Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus (PubMed:12564925). SIMILARITY: Belongs to the phospholipid scramblase family."}
+{"protein": "ATGWSAFFIDGKWTEAKK", "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 (By similarity). SIMILARITY: Belongs to the type IA topoisomerase family."}
+{"protein": "MINSFKKLIILISLVIILLSSNNIFIDSFKIPVNQKNVKSSGDSSYQIGAGIYDITGASAEVNLMGYANPLQVGAGIHFRQRARAFVFVDSNGNRAVYVSTDSCMIFQEVKIHVVELLQDIFGPNVYTEANVLLSGTHTHSGPAGFSQYALYGITSLGFYKKNFDTICNGIVQAIVKAHKSVQPANMFTETGELWNTNINRSPFAYDNNPEEEKAMYDSNVDKNMTVLRIEDMNGNPFAAISFFAVHCTSMNNTNHLISGDNKGYASYLWEKQVNGPGTAGKGPFVAAFGQSNEGDVSPNTRGPTCRDGSPCDYKTSTCNGRNEECWSLGPGKDGDMFESTQIIGGNQFNKALELFNNASIQVSGPVQYRHSWVQFTNVSVEPPYNSGVDNATTCRGAMGYSFAAGTTDGPGAFNFVQSDNNTSGNPFWNFIGDFIAKPTPDQIRCQSPKPILLDVGMVEPIPWVPDVMPIQIVTIGQIVLVAVPGEFTTMSGRRLRNSVREIIGESIENPIVLIAGLSNTYSGYIATFEEYQVQRYEGASTVFGPHTLGSYMQEFGKLAQSIVDGTTVPAGPTPRNLTGHTLFFLPPVIVDAAPDFDDFGEVSIDVNLNYSVNETVSCVFYGGNPRNDFMIESSFLSVDLLTGTDQWTTVLDDGDWDTKFKWKMHDLGFSLITIEWVIAPDTTPGTYRITHSGFAKKNPFSSNLTPYQGISRNFVVQ", "text": "FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neutral ceramidase family."}
+{"protein": "SVAFSRAVFAEFLATLLFVFFGLGSALNWPQALPSVLQIAMAFGLGIGTLVQALGHVSGAHINPAVTVACLVGCHVSFLRAAFYVAAQLLGAVAGAALLHEITPPHVRG", "text": "FUNCTION: Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Note=Shuttles from vesicles to the apical membrane. Vasopressin-regulated phosphorylation is required for translocation to the apical cell membrane. PLEKHA8/FAPP2 is required to transport AQP2 from the TGN to sites where AQP2 is phosphorylated. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
+{"protein": "MAETSRELPLSTLTASTRRALRIRARQAREAKLSVLSKVCYAIGGAPNQVSGSASAFFLQIYLLDVALISPYQASLVLSLGKTWGGITDPIVGYCISKSKWTRIGRLMPWMLGCTPFLVVSYFLLWFVPTFETGRVLWYLAFFSCFQALSTAYHVPYTTLTMFLSTDQMERDSATAYRMTVEVLGTLIGAAVQGQIVASAHTGSHCNVTNMTGNLTADFLYEPTEYITSARQVYMIAAGIIGCLYLLCISVLFLGVKERDDPYALVAGKVIPFFKGFRETMQFGPYLNLISSFLLISAAVQIQQSNFVLFCTHAADLQDHFQNLVLTILIAAVLSIPFWQWFLQKFGKKMAAFGISLMIPFSIMLVTISSLVVAYVVAVASGLSIAASLLLPWSMLPDVVDNFRLTNPQGKGLEAIFYSSFVFFTKLSAGIALGISTLSLQFADYNTSLCKQSYSVVLTLKLLIGAAPALMIIIGLTILAFYPITEDTRKETELALDVIRMRTRRSTLIVI", "text": "FUNCTION: Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets. Sphingosine- 1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology. Sphingosine-1-phosphate export from platelets is required for platelet aggregation and thrombus formation. In addition to export, also able to mediate S1P import. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes to the cell membrane and intracellular membranes. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MVVKIGIIKCGNIGMSPVVDLALDERADRKDIAVRVLGSGAKMDPESVEEVTKKMVEEVKPDFIIYIGPNPAAPGPKKAREILSQSGIPAVIIGDAPGLRVKDEMEQQGLGYIIIKCDPMIGARREFLDPVEMALFNADVIRVLAGTGALRIVQEAIDKMIDAVKEGKEIELPKIVITEQKAVEAMEFTNPYAKAKAMAAFTIAEKVGDVDVKGCFMTKEAEKYIPIVASAHEMIRYAAKLVDEARELEKAMDAVSRKPHHPEGKRLSKKALMEKPE", "text": "FUNCTION: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT. SIMILARITY: Belongs to the MTD family."}
+{"protein": "MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSPTCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGCAFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL", "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. Preferentially eliminates organic peroxides rather than hydrogen peroxide (PubMed:10391912, PubMed:9988687, PubMed:10681558). Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation (PubMed:20145245). Involved in cellular Mn(2+) homeostasis (PubMed:10635552). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily."}
+{"protein": "MEIENTRDSDSMRGSRVGFSGSLVSGKKSARFKDDESYVEITLDVRDDSVSVQNIKGADHEAALLASRLEKRPNNTLGSQLSFHLRQVSKELKRMTSSNKFQKIDRSKSGAARALRGLQFMNKNVGTEGWSEVESRFDQLAVNGMLTKSLFGQCIGMKESSEFAEELFDALARKRCITSPAVTKDELREFWEQITDTSFDARLQTFFDMVDKDADGRITQEEVKEIISLSASANKLSKIQDNSDEYAALIMEELDPGNVGYIELYNLETLLLQAPSHSMNLSTNSRVLSRMLSQKLKPTKERNPFKRCKRRLDYFIEDNWKRIWVMALWLSICAGLFTWKFIQYKRRAVFDVMGYCVSVAKGGAETTKFNMALVLLPVCRNTITWLRSRTKLGKIIPFDDNINFHKVIAFGIAVGVGLHAISHLTCDFPRLLHATDEEYEPMKPFFGDERPNNYWWFVKGTEGWTGVVMVVLMIIAYVLAQPWFRRNRLNLPSTIKKLTGFNAFWYSHHLFVIVYVLFIIHGYFLYLSKKWYKKTTWMYIAVPMILYACERLLRAFRSGYKAVKILKVAVYPGNVMAVHMSKPQGFKYTSGQYIFVNCSDVSSFQWHPFTISSAPGDDYLSMHIRTLGDWTSQLKTLFSKVCEPPTGDQSGLLRADVAKADYKPRLPKLLIDGPYGAPAQDYKKYDVVLLVGLGIGATPLISIVKDVLNNIKQQKNIEDGTKGSKRSPFATKRAYFYWVTREQGSFEWFKGVMDEVSENDQEGLIELHNYCTSVYEEGDARSALITMLQSIQQAKSGVDIVSGTRVKTHFARPNWRQVFKRVTINHPDQRIGVFYCGPQGLVGELRHLSQDFSHKTGTKFEFHKENF", "text": "FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. Involved in the massive phase II oxidative burst induced by pathogen infection. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family."}
+{"protein": "MDCGIITSKTILLLLSLIFWAAGAALAYVGSYVIKSYNNFEDFMSDRHTLIPAAIIIGVAVVMFIIGFVGCCATLRESKVGLGLFLIIIMLIFAAEVTAFVFGIIYRGRIRGDLEKSMNDVFLKYDGLNSETHAVDYLQSQLECCGVKNQTDWTLTSWFAQHNNTVPQSCCKANMTQCTGQLSQPDLLNTQGCEAKLEQVLQDVLSYAMLVILGFAIIKFFGMLSVCVITCKSKKNEYQPLYA", "text": "FUNCTION: Plays a role in migration and segregation of pigment cells (melanophores and xanthophores). Contributes to pigment stripe patterning in the epidermis. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Mainly found in the Golgi apparatus. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MKILWAALVLTLLAGCRADVEPEVEVRETAVWQSGQPWELALSRFWDYLRWVQTLSDQVQEELLSSQVTQELTLLMEDTMKELKAYKSELEKEVGPMAEDTKARLSKELQGAQARLAGDMEEVRNRLSQYRSEVQAMLGQSSEELRARLASHLRKLRKRLQRDAEELQKRLAVYKAGAQEGAERGVSAIRERLGSLMEQGRLQALTSHPLRERAQAWGEQVRGRLEKVGSQARDRLEEVREQMEEVRVKVEEQTEAFQARLKSWFEPMVEDLRRQWAELIEKVQVAVGASTSPPSQKS", "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, 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. 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. A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes. 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. By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis. 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. First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues. Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes. APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting. 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": "MKKLSLSLMLNVSLALMLALSLIYPQSVAVNFVAAWAILATVICVVAGGVGVYATEYVLERYGRELPPESLAVKIVTSLFLQPVPWRRRAAALVVVVATFISLVAAGWIFTALIYLVVSLFFRLIRKACRQRLEGREPCQG", "text": "FUNCTION: Involved in lysis inhibition. Interacts with and inhibits the holin thereby delaying the host cell lysis timing. SUBCELLULAR LOCATION: Host cell inner membrane; Multi- pass membrane protein."}
+{"protein": "MENFSLLSISGPPISSSALSAFPDIMFSRATSLPDIAKTAVPTEASSPAQALPPQYQSITVRQGIQNTALSPDCSLGDTQHGEKLRRNCTIYRPWFSPYSYFVCADKESHPEAYDFPEVQQDEGKWDNCLSEDMAESICSSSSSAENTCPREATKKSRHGLDSITSQDILMASRWHPAQQNGYKCAACCRMYPTLDFLKSHIKRGFREGFSCKVYYRKLKALWSKEPKAWLGDRLSSGSCQAFNSPAEHLR", "text": "FUNCTION: Plays a role in spermiogenesis and fertilization. SUBCELLULAR LOCATION: Nucleus membrane Note=Located throughout the subacrosomal area."}
+{"protein": "MEGCVSNLMVCNLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKRMVEG", "text": "FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis. FUNCTION: Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MEPRPGTSSRADPGPERPPRQTPGTQPAAPHAWGMLNDMQWLASSDSEEETEVGISDDDLHRDSTSEAGSTDTEMFEAGLMDAATPPARPPAERQGSPTPADAQGSCGGGPVGEEEAEAGGGGDVCAVCTDEIAPPLRCQSFPCLHPFCIPCMKTWIPLRNTCPLCNTPVAYLIVGVTASGSFSTIPIVNDPRTRVEAEAAVRAGTAVDFIWTGNPRTAPRSLSLGGHTVRALSPTPPWPGTDDEDDDLADVDYVPPAPRRAPRRGGGGAGATRGTSQPAATRPAPPGAPRSSSSGGAPLRAGVGSGSGGGPAVAAVVPRVASLPPAAGGGRAQARRVGEDAAAAEGRTPPARQPRAAQEPPIVISDSPPPSPRRPAGPGPLSFVSSSSAQVSSGPGGGGLPQSSGRAARPRAAVAPRVRSPPRAAAAPVVSASADAAGPAPPAVPVDAHRAPRSRMTQAQTDTQAQSLGRAGATDARGSGGPGAEGGPGVPRGTNTPGAAPHAAEGAAARPRKRRGSDSGPAASSSASSSAAPRSPLAPQGVGAKRAAPRRAPDSDSGDRGHGPLAPASAGAAPPSASPSSQAAVAAASSSSASSSSASSSSASSSSASSSSASSSSASSSSASSSAGGAGGSVASASGAGERRETSLGPRAAAPRGPRKCARKTRHAEGGPEPGARDPAPGLTRYLPIAGVSSVVALAPYVNKTVTGDCLPVLDMETGHIGAYVVLVDQTGNVADLLRAAAPAWSRRTLLPEHARNCVRPPDYPTPPASEWNSLWMTPVGNMLFDQGTLVGALDFHGLRSRHPWSREQGAPAPAGDAPAGHGE", "text": "FUNCTION: Evades nuclear antiviral defenses triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML and SP100. Prevents antiviral response to viral DNA induced by IFI16 by degrading it. Additionally, inhibits host IRF3 nuclear signaling to prevent interferon production by the infected cells."}
+{"protein": "MFGKTDKMDVRCHSDTEAARVSKNAHKESREIKGAEGSLPAAFLKEPQGAFSASGASEDCNKSKSNSSADPDYCRRILVRDAKGSIREIILPKGLDLDRPKRTRTSFTAEQLYRLEMEFQRCQYVVGRERTELARQLNLSETQVKVWFQNRRTKQKKDQGKDSELRSVVSETAATCSVLRLLEQGRLLSPPGLPALLPPCATGALGSALRGPSLPALGAGAAAGSAAAAAAAATAPGPAGAASQHPPAVGGAPGPGPAGPGGLHAGAPTASHGLFSLPVPSLLGSVASRLSSAPLTMAGSLAGNLQELSARYLSSSAFEPYSRTNNKEGAEKKALD", "text": "FUNCTION: Transcription factor that may function in dorsoventral specification of the forebrain. Required for axon guidance and major tract formation in the developing forebrain. May contribute to the differentiation of the neuroretina, pigmented epithelium and optic stalk (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EMX homeobox family."}
+{"protein": "MAKNRRDRNSWGGFSEKTYEWSSEEEEPVKKAGPVQVLIVKDDHSFELDETALNRILLSEAVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMYNQESVDWVGDYNEPLTGFSWRGGSERETTGIQIWSEIFLINKPDGKKVAVLLMDTQGTFDSQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTEYGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNFDGKLKEIDDEFIKNLKILIPWLLSPESLDIKEINGNKITCRGLVEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVATAKDTYNKKMEEICGGDKPFLAPNDLQTKHLQLKEESVKLFRGVKKMGGEEFSRRYLQQLESEIDELYIQYIKHNDSKNIFHAARTPATLFVVIFITYVIAGVTGFIGLDIIASLCNMIMGLTLITLCTWAYIRYSGEYRELGAVIDQVAAALWDQGSTNEALYKLYSAAATHRHLYHQAFPTPKSESTEQSEKKKM", "text": "FUNCTION: GTPase tethering membranes through formation of trans- homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis (PubMed:27619977). May also regulate Golgi biogenesis. May regulate axonal development. FUNCTION: GTPase tethering membranes through formation of trans- homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cell projection, axon Note=Localizes to endoplasmic reticulum tubular network. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cell projection, axon Note=Localizes to endoplasmic reticulum tubular network (PubMed:27619977). SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. GB1 subfamily."}
+{"protein": "MQELIACVDHIRFDLELAVEQQLGAQPLPFPGMDKSGAAVCEFFLKSACGKGGMCPFRHISGEKTVVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYSKFGECSNKECPFLHIDPESKIKDCPWYDRGFCKHGPLCRHRHTRRVICVNYLVGFCIEGPNCKFMHPRFELPMGTTEQPPLPQQTQTQQKQNNNQVLQRSSSLIQLTSQNSPVSQQRSPQTIGVMQSQSGNQGNRGPRPLDQVTCYKCGEKGHYANRCTKGHLAFLSGQ", "text": "FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Cpsf4 binds RNA polymers with a preference for poly(U) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CPSF4/YTH1 family."}
+{"protein": "MSYTWLITRASSGRGAAIALAALEAGHKVIAGARNPAKASQVRPEIQNQGGTWLRLDDSTADVRHVIAKAAKEHGLNVLVNNAGGYALRGVLEDFSETELYQQMETNFFGPIRAIQGALPWSRAQKPGTIFNISSTSDITGFTGFSLYAASKAALEGASEALYGELALFGIRVLVVQPGASRTKFQSAGPRPAVSEACVGTTVDAILQRAVGMAAERR", "text": "FUNCTION: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress (PubMed:24465762, PubMed:27274078). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG (PubMed:27274078). This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB (PubMed:27274078). The cytochrome P450 monooxygenase claM then catalyzes the dimerization of nataloe-emodin to cladofulvin (PubMed:27274078). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MRLGSPGLLFLLFSSLRADTQEKEVRAMVGSDVELSCACPEGSRFDLNDVYVYWQTSESKTVVTYHIPQNSSLENVDSRYRNRALMSPAGMLRGDFSLRLFNVTPQDEQKFHCLVLSQSLGFQEVLSVEVTLHVAANFSVPVVSAPHSPSQDELTFTCTSINGYPRPNVYWINKTDNSLLDQALQNDTVFLNMRGLYDVVSVLRIARTPSVNIGCCIENVLLQQNLTVGSQTGNDIGERDKITENPVSTGEKNAATWSILAVLCLLVVVAVAIGWVCRDRCLQHSYAGAWAVSPETELTGHV", "text": "FUNCTION: Ligand for the T-cell-specific cell surface receptor ICOS. Acts as a costimulatory signal for T-cell proliferation and cytokine secretion; induces also B-cell proliferation and differentiation into plasma cells. Could play an important role in mediating local tissue responses to inflammatory conditions, as well as in modulating the secondary immune response by co-stimulating memory T-cell function (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family."}
+{"protein": "MAAELEYESVLCVKPDVSVYRIPPRASNRGYRASDWKLDQPDWTGRLRITSKGKTAYIKLEDKVSGELFAQAPVEQYPGIAVETVTDSSRYFVIRIQDGTGRSAFIGIGFTDRGDAFDFNVSLQDHFKWVKQESEISKESQEMDARPKLDLGFKEGQTIKLSIGNITNKEGGASKPRTARGGGLSLLPPPPGGKVTIPPPSSSVAISNHVTPPPIPKSNHGGSDADILLDLDSPAPVTTPAPTPVSASNDLWGDFSTASSSVPNQAPQPSNWVQF", "text": "FUNCTION: Involved in endocytosis. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane Cell membrane Note=Colocalizes with AP-2 at the plasma membrane. SIMILARITY: Belongs to the NECAP family."}
+{"protein": "MSNQAQDQPERRDSSSENSSPFKDDEVAADQSVSAHGNTSLNKKDRVSAVRDADASSAREGQQPGVTRIEALYRIFPRNSPIVYTVYASLAAVTICFALDQSTTAAYQLYATRTLGSHAKLFGVIATVEAILNAVSKPFIAKICDIFSRQTAYFLVAVFYTIGFVVVASAQTPAAFAVGRIITEVGQAGFDLVTDIVVADLSPLEWRGVVTALTSSPFIVLPWVGNLIQARLNTGRPEGWRWGYGMFAIMAPVCVAPIILVLMYVDRKAQKAGELSFASSRLETRRAQEQGTVKVQRDSLRDRFANLVQLCKEMDLVGLFLLALSFSLLLVPFSIYKDADKQWRNPSIIAMFVCGGVILGMFLAWEILLASHPVMNKRVWYNRTFLLAVTIDIFYFMGGNARSTYYGSFVLVGTNLSTANWGYVVNALATCALSVFGLAAGFYLRIFHRYKFLQIGGLVIRIVAMGLYLYGRNGNLTTMVVAWSQILNSLGGACSVVGTRVASQASVPHQDLASIISQLALWTRLGGAIGSAIAAGIWTGTLPDYLAATNLTPAQQSRAYNSPTTIKTSYPWNTPLRNQINQAFSKTMKPIFIVALVLAFIPLFAGLLMPNYYLGKTQNAVDGTDNSGRVIESAEDNPNAEINRKNVKYAKGTRLSWLW", "text": "FUNCTION: Siderophore transporter; part of the gene cluster that mediates the biosynthesis of siderophore ferrichrome A which is contributing to organismal virulence (PubMed:17138696, Ref.4). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MAGLKVEWNDWCPGCGNFGILSAEQQAIQELGLDPKKVVLVSGIGCSGKIPHFIRLPASGVHTLHGRALTFAIGIKLANPSLEVIVNGGDGDQLGIGVGHFVSAGRRNVDLTVIVHNNGVYGLTKGQASPTLKLGVKTKSLPKPNINSDINPIALAISSGYTFVARGYAYDVKHLKEIIKKAIKHKGLAMIDVLQPCPTYNDIHTKEYYDKRVYKLDEDPSWDPIVKKPEEMDDKMSKAILKSMEWGDRTPIGIFYQNELVSTYEQRIAERSPSYLDNPPAHDVIEFEGKPTTDVEDILKERRVT", "text": "FUNCTION: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2- oxobutyrate to form their CoA derivatives."}
+{"protein": "MNIMKRQLCTSSKRFFSTAKNVVKYNTIQDIRNKYFTGTPLSMCTAYDFITATWVNKANCDLLLVGDSLAMTSLGYDSTITLSLNEFKYHVASVCRAEGSSMVVVDMPFGTFESGISDGLKNAIDIMKLDSKVTSVKVEVGSYTKDKYAMKFIEELCSRGIPVMAHIGLTPQKVHSLGGYKVQGSKSLLQMQELYETAMQLQKIGCWSILIECVPHKMAQFITSKLSVPTIGIGAGNGTSGQVLVISDLLGMQGDSVPKFVKQAVNMTDIATQGLKEYIASVEDRTFPERGTHTFKVKEDLWNEFLSSINEK", "text": "FUNCTION: Probable 3-methyl-2-oxobutanoate hydroxymethyltransferase required for pantothenic acid biosynthesis (PubMed:11154694). Acts downstream in the pantothenic acid pathway (PubMed:11154694). SIMILARITY: Belongs to the PanB family."}
+{"protein": "MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRARELGSRRLSDLQKNTEDLSRPLYKKPPADSRALGEWGKASKLQLNEDELKQQEELIERYAINIYLSDRISLHRHIEDKRMYECKSQKFNYRTLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRVYLKTQLETYISNLDRVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNSGWLEPLLERIGRDETAVVCPVIDTIDWNTFEFYMQIGEPMIGGFDWRLTFQWHSVPKQERDRRISRIDPIRSPTMAGGLFAVSKKYFQYLGTYDTGMEVWGGENLELSFRVWQCGGKLEIHPCSHVGHVFPKRAPYARPNFLQNTARAAEVWMDEYKEHFYNRNPPARKEAYGDISERKLLRERLRCKSFDWYLKNVFPNLHVPEDRPGWHGAIRSRGISSECLDYNSPDNNPTGANLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPEQKNYVGMQNCPKDGFPVPANIIWHFKEDGTIFHPHSGLCLSAYRTPEGRPDVQMRTCDALDKNQIWSFEK", "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 a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily."}
+{"protein": "MATAASNPYSILSSSSLVHADSAGMQQGSPFRNPQKLLQSDYLQGVPSNGHPLGHHWVTSLSDGGPWSSTLATSPLDQQDVKPGREDLQLGAIIHHRSPHVAHHSPHTNHPNAWGASPAPNSSITSSGQPLNVYSQPGFTVSGMLEHGGLTPPPAAASTQSLHPVLREPPDHGELGSHHCQDHSDEETPTSDELEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSSTGSPTSIDKIAAQGRKRKKRTSIEVSVKGVLETHFLKCPKPAAQEISSLADSLQLEKEVVRVWFCNRRQKEKRMTPPGDQQPHEVYSHTVKTDASCHDL", "text": "FUNCTION: Probable transcription factor which exert its primary action widely during early neural development and in a very limited set of neurons in the mature brain. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the POU transcription factor family. Class-3 subfamily."}
+{"protein": "MTLDLDAHKKDDKLLITTIQQEYKILAEYKMIESEKLSGIYVIPSYANSLQWFGVFFGRQGLYAESVFRFTILLPDRFPDDKSLPTIIFQQDVIHPHVCPYTHSLDVSHAFPEWRCGEDHLWQLLKYLQVIFSDPLDSIRGIEVDKLKNREAAELLMNNKEEYVARVQENIKESKEHIFDTPPTEDPHYIVFEKFQQDVHGPVLERIKAGRSKQTEPSAQQGNGGHATGLSWVKEGEFKPLSIE", "text": "SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily."}
+{"protein": "MAEFHPTAFLLPAAVTMIAGYFLCTALYNVYFHPLAKFPGPRLYAASQIPITIKRLLGDEVATFHKLHAKYGQFVRVAPGELSTINPAASRDVYGHRNPAKSIPKDFKAYYMKNQRRDGTEGLMTADDDLHRRQRKIFSPAFSDRAIREQEPLLKKYTDLLVEKAGVASDADGKVDMVMMFNFATFDFIADCVFGDSLHLLEKMEYNPFLANISAVVKFSAMRRAIRSFPYMDETFEKLIPASMKRKRMEHVKFCDDLVDRRLEKAVTNHPDFWTLVLRANEKGEGLTLGEMHQNSFLFLTAATETTSSLMSALTYLLCQNPDKMKKLVDEIRGRFKSTEEMTTVSLPPLEYLQMCIEEGLRVYPPVPGGLPRRVTADGASLDGRELPPDTVVYYAHYASYHSAAHFARPDEFHPERWASVPPSEFANDCRDAVIPFSAGPRDCIGKNLAYHEARLLLAKFLWTYDVELCEESKDWIKQKSFIVGVKRPLYVKLHRVVREK", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of radicicol, a resorcylic acid lactone (RAL) that irreversibly inhibits the HSP90 molecular chaperone, an important target for cancer chemotherapy (PubMed:19101477). The cluster encodes only two apparent post-PKS enzymes, a cytochrome P450 monooxygenase (radP) and a non-heme halogenase (radH) that introduce the epoxide and the chlorine, respectively (PubMed:19101477). If this cluster includes all the genes required for radicicol biosynthesis, the remaining structural features of radicicol are presumably generated by the PKSs rads1 and rads2 (PubMed:19101477). The C-2' ketone could arise if the R-PKS rads1 and NR-PKS rads2 each carry out four iterations, in contrast to the five iteration-three iteration split for the hypothemycin PKSs (PubMed:19101477). The origin of the cis 5',6' double bond is not known (By similarity). The radicicol R-PKS rads1 ER domain may catalyze either double bond isomerization or reduction in the third iteration (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MKSTGLLLGYFLMKVLVCDAEGEPGKSLDGAVTASGSNDSRDGENGLSETPHTEDRCRGYYDVMGQWDPPFVCRTGSYLYCCGTCGFRFCCEFKNSRLDQTTCKNYDTPPWSMTGRPPPKMMDQHDPTKDKTNLIVYIICGVVAIMALVGIFTKLGLEKAHRPHRENMSRALAQVMRQTAPGEHVEREESLAVHGQPYENLQARATGNNLQSAQMNSVGPSSSMMQAMTPYPALGQVPVAHPYEPSPAAKELNKYASLKAVAEKANENFYTNRRHLADLAAKGTLPMHSVSLEQEPTNPYSPELPCQKQNGHKSKSTKVHSSHPLAYGSNTIANPGRMSSWETTETLGRRHTYGPKKHSATMEQMNELTSAQSQHYLPPHPYFVTNSKTEVTV", "text": "FUNCTION: Regulator of short-term neuronal synaptic plasticity in the dentate gyrus. Associates with AMPA receptors (ionotropic glutamate receptors) in synaptic spines and promotes AMPA receptor desensitization at excitatory synapses (By similarity). SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane; Single-pass type I membrane protein Synapse. SIMILARITY: Belongs to the shisa family. SHISA9 subfamily."}
+{"protein": "MTSIIKLHTISGAMDESPPCYILQIDDVRILLDCGWDEKFDANFIKELKRQVHTLDAVLLSHPDAYHLGALPYLVGKLGLNCPIYATIPVFKMGQMFMYDLYMSHFNMGDFDLFSLDDVDTAFEKITQLKYNQTVSLKDKGYGISITPLNAGHMIGGTIWKIVKVGEEDIVYATDFNHKKERHLSGCELDRLQRPSLLITDAYNAQYQQARRRARDEKLMTNILQTVRNNGNVLIAVDTAGRVLELAHMLDQLWKNKESGLMAYSLALLNNVSYNVIEFAKSQIEWMSDKLTKAFEGARNNPFQFKHIQLCHSLADVYKLPAGPKVVLASTPDLESGFTRDLFVQWASNANNSIILTTRTSPGTLAMELVENCAPGKQIELDVRRRVDLEGAELEEYLRTQGEKLNPLIVKPDVEEESSSESEDDIEMSVITGKHDIVVRPEGRHHSGFFKSNKRHHVMFPYHEEKVKCDEYGEIINLDDYRIADATGYEFVPMEEQNKENVKKEEPGIGAEQQANGGIVDNDVQLLEKPTKLISQRKTIEVNAQVQRIDFEGRSDGESMLKILSQLRPRRVIVIHGTAEGTQVVARHCEQNVGARVFTPQKGEIIDVTSEIHIYQVRLTEGLVSQLQFQKGKDAEVAWVDGRLGMRVKAIEAPMDVTVEQDASVQEGKTLTLETLADDEIPIHNSVLINELKLSDFKQTLMRNNINSEFSGGVLWCSNGTLALRRVDAGKVAMEGCLSEEYYKIRELLYEQYAIV", "text": "FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Required for the cotranscriptional processing of 3'- ends of polyadenylated and histone pre-mRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily."}
+{"protein": "MSDREESGSPEPRSKIEEDLESDEEVKTIKSEEVDKTQDNVEDEDDEEEEEEEEEEEEEDDDEEDVRQRKKPRRERRNQFLDVEAEVDEDEEDLEEDEDGLIGEDGFVAEPDADEPDASDDRFHREMDRRREAIAEEDAERLADEYREKYGRSTANKYRGDSGVIPQHLLLPSVNEPSIWGIRCKPGKEKELVRQCLRKKLSLQKSRNPLEIMSVFQRDTFTGYIYMEARNQQAVTVALKGLVNVYPQNMILVPIKEYVDLLRATKSAETELVPGAYVRLKRGKYGGDLAIVENLSENGLEVRLKLVPRLDYGRNAEAGIDGKRKRVARIPPPRLFSEQEASQYDPRNLQKRGPNAYVYAGDEYIGGFLYKDFKITLVNAENVAPKLEELTRFNSEETDGIDLASLAQSLRKSAAAVQFQGGDVVEVSEGEQTGVQGTVISTHGDIVTVEATTAPLVGKRIDLPSRSLRKKFAIGDHVRVISGNFLDDTGLIVGLEDDSVTLLSDLNKKEVTVFAKDLKKVSDIGGSHQVGDYELHDFVQLDALHVGCIVKVERDSLKVLDQEGTVRSVTPSSITMKLTRNMEGLATDSNGSEIKIGDTVRETVGEGRQGAVLHIYKNTLFLSSRSLGVFVAKAFKVNTIVAKGARTQSNSQATGPDLTKMNPAVYNARPGQMAPPVMPKQGGFDRLKGKHVAIGPGSQHKGCKGIVKETTDDIARVELHAPCKVVNVLKHQLRIYDDYKKTYLSYMEFATPRGMRSGGGRPGGPPGPGGPGSGGQTPSWGGGGKTPSWGAGGKTPSWGSKTPSWGGAKTSSWGSRTPAANAGGAQTPAWGAMGNKTPSWGASESRTPAWGGAKTPAWGAAGAGSKTPAFGVARTPSWKSSSAGTYGGSSSRNKGWEDLGSGNSAPTPGYAAATPGEMMGAPTPGAAHHPWEDSAPTPAAYNDARTPGVYDPRGSGPAQAETPAAWSTDDAPRYDDSPTP", "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. SIMILARITY: Belongs to the SPT5 family."}
+{"protein": "MGKSGGRKKKSGGSNSNSSQVNSSETSGLSKPSTIVNGGVDFDASIFLKRAHELKEEGNKKFQARDYVGALEQYENGIKLIPKSHPDRAVFHSNRAACLMQMKPIDYESVISECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVLLGSDPNHKDAGEISKRLKTALGPHQDLQSRPSPAALGASAALGGPIAGLGPCLPSRNVHKKGVTSPVGSVSLPNASNGKVERPQVVNPVTENGGSVSKGQASRVVLKPVSHSPKGSKVEELGSSSVAVVGKVQEKRIRWRPLKFVYDHDIRLGQMPVNCRFKELREIVSSRFPSSKAVLIKYKDNDGDLVTITSTAELKLAESAADCILTKEPDTDKSDSVGMLRLHVVDVSPEQEPMLLEEEEEEVEEKPVIEEVISSPTESLSETEINTEKTDKEVEKEKASSSEDPETKELEMDDWLFDFAHLFRTHVGIDPDAHIDLHELGMELCSEALEETVTSEKAQPLFDKASAKFQEVAALAFFNWGNVHMCAARKRIPLDESAGKEVVAAQLQTAYEWVKERYTLAKEKYEQALSIKPDFYEGLLALGQQQFEMAKLHWSYLLAQKIDISGWDPSETLNLFDSAEAKMKDATEMWEKLEEQRMDDLKNPNSNKKEEVSKRRKKQGGDGNEEVSETITAEEAAEQATAMRSQIHLFWGNMLFERSQVECKIGKDGWNKNLDSAVERFKLAGASEADIATVVKNHCSNEAAATEGDEKKVPAP", "text": "FUNCTION: Required for plastid separation and partitioning during cell division (PubMed:22025705). Not involved in plastid constriction or in the organization of cytoplasmic actin cables (PubMed:22025705). Contributes to polar growth of root hairs (PubMed:28096376). SUBCELLULAR LOCATION: Cytoplasm Note=Localized to distinct foci in the cytoplasm, which frequently colocalize with the cell periphery and with chloroplasts."}
+{"protein": "INWLKLGKAIIDAL", "text": "FUNCTION: Antibacterial peptide (PubMed:30974767). Inhibits biofilm formation of A.baumannii and Staphylococcus spp. bacteria (PubMed:30974767). Also shows potent mast cell degranulation activity and potent hemolytic activity of rat erythrocytes (PubMed:15052574, PubMed:15225564). Does not show chemotaxis for polymorphonucleated leukocytes (PMNL) (PubMed:15052574, PubMed:15225564). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MCD family. Mastoparan subfamily."}
+{"protein": "MAKIVILFDFDRTLIDGDSDNWVVTEMGLTEIFHQLRFTLPWNRLMDRMMMELQSQGRSIDDIKSCLKKMPIDSHIIEAIKSAKSSGCDLKIVSDANQFFIEKILEHHDLVDCFSEIYTNPTSLDDNGNLRILPYHSDALPPHSCNLCPSNLCKGLVMDHLRASSSNDQIPRRFIYLGDGGGDFCPTLKLRECDFVMPRTNYPLWKKISDNPLLIKAEVKEWSSAEEQQRILLQLVSTITKEEDS", "text": "FUNCTION: HAD-like hydrolase that has a thiamine monophosphate phosphatase activity in a heterologous system (PubMed:26537753). Does not contribute to thiamine monophosphate phosphatase activity in planta (PubMed:27677881). SIMILARITY: Belongs to the HAD-like hydrolase superfamily."}
+{"protein": "MSTRVLTLTLLKKRHLMQCFWSTVGSVHLRSIASDKIPSHAVEASLYVHWPYCLKRCSYCNFNKYISRSENHDTMTECLQKETETLLKLSQVSRITSVFFGGGTPSLAQPSTIAAVLETVTKNSNLSDLAEVTLEVNPTPAGKARLKDFTLAGVNRFSIGVQSLNADHLRILGRDHSVQHALQTVSEARKLCPGRVSVDIMFALPGQSVSCWQKQLEELLYVCDDHISLYQLTLERGTQLFKQVESGKLSVPGDEVTAIMYKTACRVLEESGFHQYEVSNFARNNAVSEHNMGYWRGHQYIGVGPGAHGRFVPHGDGGVQREARTQTLEPDVWIKEVQSRGRGTRRRITLHHLQLLEEVLVMGLRMNEGITHQHWELFSPEANLQQVFGKSANIQELQGGRFLILDDRGLRCSWEGLVLLDSILPTILLELEMFFHSRGIKRTQ", "text": "FUNCTION: May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl- L-methionine (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily."}
+{"protein": "MFLNKCEGDLGELRKPGDSEGTPPAAAEEEQPKKKHRRNRTTFTTYQLHELERAFEKSHYPDVYSREELAMKVNLPEVRVQVWFQNRRAKWRRQEKMEASSMKLHDTPMLSFNRPPMTANVGPMSNSLPLDPWLTSPISSATPVHSIPGFMGAPQALQPPYGGHSFLNTPPGMAQGMQPMAPAPYQCGTPFVDKYPLEDVDQRSSSIASLRMKAKEHIQTIDKTWQPI", "text": "FUNCTION: Plays a critical role in eye formation by regulating the initial specification of retinal cells and/or their subsequent proliferation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily."}
+{"protein": "MALKDYVLEKDKVKKFLQEFYQDDESGKKQFKYGNQLVQLAHREQVAMYVDLDDIAEDDPELVDSICENTKRYARLFADAVQELLPQYKEREVVNKDVLDVYIEHRLMMEQRSRDPGAARSPQNQYPPELMRRFELYFQGPSSNKPRVIREVRADSVGKLVTVRGIVTRVSEVKPRMVVATYTCDQCGAETYQPIQSPTFMPLIMCPSQECQTNRSGGRLYLQTRGSKFIKFQEMKMQEHSDQVPVGNIPRSITVLVEGENTRIAQPGDHVSVTGIFLPILRTGFRQMVQGLLSETYLEAHRIVKMSKSEEDESGAGELTREELRQITEEDFYEKLAASIAPEIYGHEDVKKALLLLLVGGVDQSPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVLRDSVSGELTLEGGALVLADQGVCCIDEFDKMAEADRTAIHEVMEQQTISIAKAGILTTLNARCSILAAANPAYGRYNPRRSLEQNIQLPAALLSRFDLLWLIQDRPDRDNDLRLAQHITYVHQHSRQPPAQFEPLDMKLMRRYIAMCREKQPAVPESLADYITAAYVEMRREAWASKDATYTSARTLLAILRLSTALARLRMVDTVEKEDVNEAIRLMEMSKDSLLGDKGQTARTQRPADVIFATVRELVSEGQSVRFSEAEQRCISRGFTPAQFQAALDEYEELNVWQVNTARTRITFV", "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. Required for S-phase checkpoint activation upon UV-induced damage. 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": "METGRQTGVSAEMLAMPRGLKGSKKDGIPEDLDGNLEAPRDQEGELRSEDVMDLTEGDSEASASAPPAAKRRKTHTKGKKESKPTVDAEEAQRMTTLLSAMSEEQLSRYEVCRRSAFPRARVAGLMRAITGSSVSENAAIAMAGIAKLFVGEVVEEALDVCEMWGETPPLQPKHLREAVRRLKPKGLFPNSNCKRIMF", "text": "SIMILARITY: Belongs to the TAF11 family."}
+{"protein": "MRNENVAGLLAERASEAGWTDQPAYYAPDVVTHGQIHDGAARLGAVLANRGLCRGDRVLLCMPDSPELVQVLLACLARGILAFLANPELHRDDHAFQERDTQAALVITSGPLCDRFAPSTVVDAADLFSEAARVGPADYEILGGDAAAYATYTSGTTGPPKAAIHRHCDVFAFVEAMCRNALRLTPADIGLSSARMYFAYGLGNSVWFPLATGSSAVVNPLPVGAEVAATLSARFEPSVLYGVPNFFARVVDACSADSFRSVRCVVSAGEALEVGLAERLTEFFGGIPILDGVGSTEVGQTFVSNTVDEWRPGSLGKVLPPYQIRVVAPDGAAAGPGVEGDLWVRGPSIAESYWNWPEPLLTDEGWLDTRDRVCIDDDGWVTYACRADDTEIVGAVNINPREIERLIVEEDAVAEVAVVGVKEATGASTLQAFLVPASAEGIDGSVMRDIHRRLLTRLSAFKVPHRFAVVERLPRTANGKLLRSALRGQTPAKPIWELASAEHRSGAPGQLDDQSASALVSGSREVSLKERLAALQQERHRLVLDAVCGETAKMLGEPDPRSVNRDLAFSELGFDSQMTVELCHRLAAATGLRVPETVGWDYGSISGLAQYLEAELSGADRRVTPQSARSGARALPLIEAQLNKVEELTAAIADGEKPRVAERLRALLGTITEGQEHWGQRIAAASTPDEIFQLIDSEFGES", "text": "FUNCTION: Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. This intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MKIKSALLTLVGALTVFSSSAHSKDLKIGLSIDDLRLERWQKDRDIFVNKAESMGAKVFVQSANGDDSAQISQIENMINKNIDVLVIIPHNGEVLSNVISEAKKEGIKVLAYDRLINNADLDFYVSFDNEKVGELQAKSIVAVKPEGNYFLMGGSPVDNNAKLFRKGQMKVLDPLIASGKIKVVGDQWVDSWLAEKALQIMENALTANKNNVDAVVASNDATAGGAIQALSAQGLSGKVAISGQDADLAAIKRIVNGSQTMTVYKPITKLADKAAEIAVELGKNEKIEANAELNNGLKNVPAYLLDPIAVDKRNINETVIKDGFHTKESIYH", "text": "FUNCTION: Involved in the high-affinity D-xylose membrane transport system. Binds with high affinity to xylose (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 2 family."}
+{"protein": "MRAVRAETRARELFRDAAFPASDSSLFYNLSTPLAQFREDITWRRPQDICATPQLFPDNPWEGQVKQGLLGDCWFLCACAALQKSRHLLDQVFPPGQPGWSDQEYQGFFTCRIWQFGHWEEVTIDDRLPCLAGRLCFSRCQREDVFWLPLLEKAYAKVHGSYEHLWAGQVADALVDLTGSLAERWSLKDIRKASGQQDRPSGGEHRACQQLLRLKDQCLLSCSVLSPRAGARELGEFHAFIISDLQELRSQTGQGILLLRIHNPWGRRCWQGLWREGGEGWNQVEPAKESELLAQLQEGEFWVEEEEFLREFDEVTIGYPVTEAGHLQSLYTEKVLCHTRALPGAWVTGQSAGGCRNNSCFPCNPKFWLRLLEPSEVCVAVLQRPRRRLVGQTRALAGASPAPVNLPGKDYQAVGLHIWKVEKRKISLPRVLSAPPVAGTACHAYDREIHLRCELSPGYYLAVPSTFLKDVPGQFLLRVFSTGKISLSAVRLATKGASPGAALPAGEWETVQLQGSWRAGQTAGGSRNFASYPCNPCLPFSVPEGAGPRYIRITLQQHCRLSDSQLHPIGFHVFQVPADGEKQDACSLLLQEPLLSCVPHCYAQEVSRLCLLSAGNYRIVPSTYLPDTEGTFTVTIATRIDRQSIHSQEMLGQLLQEVSFMAVMKA", "text": "FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin- stimulated glucose uptake (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the peptidase C2 family."}
+{"protein": "MQFTIAVALLCCAIASTLAYPMPDDMTMKPTPPPQYPLNLQGGGGGQSGDGFGFAVQGHQKVWTSDNGRHEIGLNGGYGQHLGGPYGNSEPSWKVGSTYTYRFPNF", "text": "FUNCTION: Required to resist Gram-negative bacterial infections, regulated by Dredd. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the attacin/sarcotoxin-2 family."}
+{"protein": "MPVIAGGILAALLLLIVVVLCLYFKIHNALKAAKEPEAVAVKNHNPDKVWWAKNSQAKTIATESCPALQCCEGYRMCASFDSLPPCCCDINEGL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FAM24 family."}
+{"protein": "MCDPTSESQLWRSSSQIPSPCLICRLDHIVMTVKNIEDTTMFYSKILGMEVTTFKGNRKALCFGDQKFNLHEVGKEFDPKAAHPVPGSLDVCLITEAPLEEVIERLKAFDVPIEEGPVFRTGAKGPILSIYFRDPDRNLLEVSSYVTS", "text": "SIMILARITY: Belongs to the glyoxalase I family."}
+{"protein": "MSRLSQLLNSKKAKQKPPSEHPIGLSSILKQDSSSSSDSPNFFPSSSTNDHQERDTINDTNFVVPEKQKTSKLALLAAERKKLHSSFPSTQQQPPKTEKEKEKEPIQAKHKKNVENDFLLQRFRKVRIAEKKDSEQPSSHEIHLTDDDDKTTLQKQMVESDQLKKNPQEVKLAPPSSFAKCLTGAKKRVFEDQIEIHLSKSSLLGFNAPSPDDIVLMAQSKSKSFQKHKRLDEQLLNSVKSMKKVSQQLKPQKNTNDSNNDHTLLSQDQLIELSKLVKPRTKLLLLGPPKSGKKTLLSRLFFQIGSFDPKTMQKCTVLNAKKESLSSVLKSTKTKWYDFETFSNSYSSTIIDFPLGIFTTNASSRDNFLKHSSLFQVMNTAIFTIDCLNPLEGLDGISSILQLMNGLSISSYMFAITKMDEIEWDENKFINLVNSIQSFLKESCGIIEKSKFIPISGLKGTNLTSISQEKLSQWYKSDTLLGKIDKEADTNHGTWNFLLNLPLSLTISHITPLPENQSHIYCSIHSGMLQDSQKLYVGTGRLETQITGLSSDENPKGFNVAGDMIQAKIPTLPNLCPGILIADSIDAFTSSKTAYVNATWFHGSLEKGKSMHVIALFGCHAVLTKLYCFTDSQEKAPNAIGNDLERNRTSLVKIELENAFPLVKESYINTLSRVLFVSEKWNSLIAFGTVLSLHD", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family."}
+{"protein": "MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSYSWGMAVNVYSTSITQETMSRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFPGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIPPPDPGEQIFNLPKKSHHANSPTAGAAKSSPAAKPGSTPSRPSSAKRASSSGSASKSDKDLETQVIQLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQEHGQENDDLVQRLMDILYASEEHEGHTEEPEAEEQAHEQQPPQQEEY", "text": "FUNCTION: May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Associated with the microtubule network. Accumulates at the plus end of microtubules. SIMILARITY: Belongs to the MAPRE family."}
+{"protein": "MSYTKLLTQLSFPNRISGPILETSLSDVSIGEICNIQAGIESNEIVARAQVVGFHDEKTILSLIGNSRGLSRQTLIKPTAQFLHTQVGRGLLGAVVNPLGEVTDKFAVTDNSEILYRPVDNAPPLYSERAAIEKPFLTGIKVIDSLLTCGEGQRMGIFASAGCGKTFLMNMLIEHSGADIYVIGLIGERGREVTETVDYLKNSEKKSRCVLVYATSDYSSVDRCNAAYIATAIAEFFRTEGHKVALFIDSLTRYARALRDVALAAGESPARRGYPVSVFDSLPRLLERPGKLKAGGSITAFYTVLLEDDDFADPLAEEVRSILDGHIYLSRNLAQKGQFPAIDSLKSISRVFTQVVDEKHRIMAAAFRELLSEIEELRTIIDFGEYKPGENASQDKIYNKISVVESFLKQDYRLGFTYEQTMELIGETIR", "text": "FUNCTION: ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:26947936, PubMed:27770024, PubMed:29595954). Acts as a molecular motor to provide the energy that is required for the export of proteins (Probable). Required for type III secretion apparatus (T3SA) formation, proper protein secretion, host cell invasion and virulence (PubMed:26947936, PubMed:27770024, PubMed:31162724). May play a critical role in T3SS substrate recognition, disassembly of the effector/chaperone complex and unfolding of the effector in an ATP-dependent manner prior to secretion (By similarity). FUNCTION: ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (By similarity). Acts as a molecular motor to provide the energy that is required for the export of proteins (By similarity). Required for type III secretion apparatus (T3SA) formation, proper protein secretion, host cell invasion and virulence (By similarity). May play a critical role in T3SS substrate recognition, disassembly of the effector/chaperone complex and unfolding of the effector in an ATP-dependent manner prior to secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase subfamily."}
+{"protein": "MILNKKNIHSKSVMLFCAGIVSLMPLHAIAYLQGEVRTNGGPNIFYAVLDHTTFPNNKAGELATVNFSLPDRYDGTVYCPNSRIYDRALTYFKATTDLPPVGNNFYQLNEYVDIKINFEIWGPNPLPTVPFSDIPNNRNNQQGCRVPSSPKPHISSGSSGQLTFRLRKPIINGVSLNGQSLAQMYAMVSHSGAPKTYGSEPISKLVITSGIITTKDKCIFNNGSPITFDFGNVGNTSDYLNGQNYKITRNIPIKCEGGSFTDPNSRIMFKVQTGSSGIASFDSNYLGTTGSVDRSNLGIVLRDKSGTIIPPNQYFSVGKLNNFNGNWEVSAAPIAKAGSKITEGEFSAHATLIAEFM", "text": "SUBCELLULAR LOCATION: Fimbrium."}
+{"protein": "MAPPKAASHRPAVRRKKSGTLVDSILDKYLNVRFFKYLLLEPAALPIVGLFVLLAELVINVVVIQRVPYTEIDWVAYMQECEGFLNGTTNYSLLRGDTGPLVYPAAFVYIYSALYYVTSHGTNVRLAQYIFAGIYLLQLALVLRLYSKSRKVPPYVLVLSAFTSYRIHSIYVLRLFNDPVAVLLLYAALNLFLDRRWTLGSTFFSLAVGVKMNILLFAPALLLFYLANLGLLRTILQLAVCGVIQLLLGAPFLLTHPVEYLRGSFDLGRIFEHKWTVNYRFLSRDVFENRTFHVSLLGLHLLLLLAFAKPIWTFFQSYVRLRRIEDQLQPQITQQNLQLKAQKRPKKVEKDKDKDQKKFTTEQQSFLKAFEKSLQKASGGKATPAPAQAEPERYGIHFDRCTQLALLPFFLCNLVGVACSRSLHYQFYVWYFHSLPYLAWSTPYSLGVRCLILGLIEYCWNTYPSTNFSSAALHFTHIILLAGVAKQLIQTMRINNAAKREQQEQQKKLQ", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 58 family."}
+{"protein": "MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRANSLFEEFKSGNIERECIEERCSKEEAREAFEDDEKTETFWNVYVDGDQCSSNPCHYGGTCKDGIGSYTCTCLSGYEGKNCEYVLYKSCRVDNGDCWHFCKPVQNGIQCSCAESYLLGEDGHSCVAGGDFSCGRNIKTRNKREANLPDFQTDFSDDYDEIDENNFVETPTNFSGLVLTVQSQNATLLKKSDNPSPDIRVVNGTDCKLGECPWQALLLNDEGDGFCGGTILSPIYVLTAAHCINQTKYITVVVGEIDISSKKTGRLHSVDKIYVHQKFVPATYDYDIAIIQLKTPIQFSENVVPACLPTADFANQVLMKQNFGIVSGFGRTRERGKTSNTLKVVTLPYVDRHTCMLSSNFPITQNMFCAGYDTLPQDACQGDSGGPHITAYRDTHFITGIVSWGEGCAQTGKYGVYTKVSKFILWIKRIIRQKQPSTESSTGRL", "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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MSPLLRRLLLAVLLQLAPAQAPVSQPDAPGHQKKVVSWIDVYARATCQPREVVVPLNMELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIQYPSSQLGEMSLEEHSQCECRPKKRESAVKPDRASTPHHRPQPRSVPGWDPAPGAPSPADITHPTPAPGPSAHAAPSAASALTPGPATAAADAAASSVVKGGA", "text": "FUNCTION: Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted but remains associated to cells or to the extracellular matrix unless released by heparin. SIMILARITY: Belongs to the PDGF/VEGF growth factor family."}
+{"protein": "AASGLEAAMKAAGKQYFGTALTVRNDQGEIDIINNKNEIGSITPENAMKWEAIQPNRGQFNWGPADQHAAAATSRGYELRCHTLVWHSQLPSWVANGNWNNQTLQAVMRDHINAVMGRYRGKCTHWDVVNEALNEDGTYRDSVFLRVIGEAYIPIAFRMALAADPTTKLYYNDYNLEYGNAKTEGAKRIARLVKSYGLRIDGIGLQAHMTSESTPTQNTPTPSRAKLASVLQGLADLGVDVAYTELDIRMNTPATQQKLQTNADAYARIVGSCMDVKRCVGITVWGISDKYSWVPGTFPGEGSALLWNDNFQKKPSYTSTLNTINRR", "text": "FUNCTION: Catalyzes the hydrolysis of the internal glycosidic bonds in heteroxylans, releasing mainly xylobiose and xylotriose. Most active on oat-spelt xylan. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family."}
+{"protein": "MEEGGGSGVGGMQGAASNLLDAGAQAFYPAVGAPFPFQQLPHQLYCPQPPPPPYQVMPVPPPPPPVGLPVPPLPATMAPQPGYCVPAAATVVDGPASRAVVLSLVPPHAPEDEIARAMAPFGAVRAVDASAVASEGVATVYFFDLRSAEHAVTGVREQHIRQQCRLGQLYAAAAAAAASSPTWPPPAWDWPHDDNRGLVLGQAVWAHFAAASTVPDDGASRGSLVVLNSLPAMSVFELREIFQAYGDVKDVRESALRPSNKFVEFFDTRDADRALHELNGKELFGRRLVVEYTRPSLPGPRRRGHVSHQPLAPTPPRLQAAWRPAPAPSQSAQPSSSGSGKAREGVVLLRRSSGKGSSGSQSKGGGNAGHERKSKGGKSAAAACSTAASASSSTATAPSKQSQKGGGGGGGRGGSWRGQKSGWEARFLFKEPEAAAAAAGDAAASETHEPASCKDTRTTVMIRNIPNKYSQKLLLNMLDNHCILSNQQIEASCEDEAQPFSSYDFLYLPIDFNNKCNVGYGFVNLTSPEAAVRLYKAFHKQPWEVFNSRKICQVTYARVQGLDALKEHFKNSKFPCDSDEYLPVVFSPPRDGKLLTEPVPLVGRSPAPSSASGASSPPKSCAASVDPLAQELMTAPSSSGDGASSASSSNAHADEDDVHGETGGDRGDDAGLDLELQRLGYTD", "text": "FUNCTION: Probable RNA-binding protein. Involved in the regular timing (plastochron) of lateral organs formation. May regulate the rate of leaf initiation and the duration of vegetative phase. Seems to be redundant to the function of PLASTOCHRON1, but to act in an independent pathway."}
+{"protein": "FNRXSPGLQGVSSVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASRGIELSEVRLNLEKMMEQKSSAVKALTGGIAHLFKQNKVVHVNGFGNITGKNQVTATKADGSSQVIGTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGAEVTAVEFLGHVGGIGIDMEISKKFQRILQKQGFKFKLNPKVPGATKRSDGKIDVSVEAAPGGKAEVIPCDVLLVCIGRRPFTQNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFR", "text": "FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched- chain amino acid-dehydrogenase complex) (PubMed:15888450). The 2- oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (PubMed:14645106, PubMed:15888450). SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Cell projection, cilium, flagellum Cytoplasmic vesicle, secretory vesicle, acrosome Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2- oxoglutarate dehydrogenase complex is required for histone succinylation. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MSEQQVQELEKKWYALQVEPGKENEAKENLLKVLELEGLKDLVDEVIVPAEEKVVIRAQGKEKYRLSLKGNARDISVLGKKGVTTFRIENGEVKVVESVEGDTCVNAPPISKPGQKITCKENKTEAKIVLDNKIFPGYILIKAHMNDKLLMAIEKTPHVFRPVMVGGKPVPLKEEEVQNILNQIKRGVKPSKVEFEKGDQVRVIEGPFMNFTGTVEEVHPEKRKLTVMISIFGRMTPVELDFDQVEKI", "text": "FUNCTION: Participates in transcription elongation, termination and antitermination. SIMILARITY: Belongs to the NusG family."}
+{"protein": "MSLSGVPLSAGLAPSPSNKPTNGKGQNIVRRSGNYKPALWDYDYLQSLPTLYAGEAHVEKLNKLKGEVRIMLEKTVTENPLAQLEQIDTLYRLGISYHFQDEIKALLNTIHNNNNNNNNNDDVYATALEFKLLRLYGYTVHSEVFNVFKDEIDKGFKAISLCGDYVKGMLSLYEASFYSFKGETILDEARDFSTKHLQKYVMMRHNNNSKDQSVDDDDDLVILVEYALELPMHWRMIRLEAKWFIDVYSKRRDDMNPTFLELAQIDFNLLQSTYQEDLKHVSRWWSTCKLGERLPFCRDRLVEVFLLAVALKYEAEFGYARRLLTKIGVLVTLMDDIYDVYGTLDELKLLEDAIERWNINELDQLPEYMNIFFVAMYNVVNGIAYDVLKENEILIVKYLKRAWMDACKSYMVEAKWYYSGYTPSLEEYLENGLISITIPLDLIFLYCLTTSPITEDSMEYLLQYPTILGLSGTLFRLVDDLATSSDELKRGDNPKSIQCYMHESGVCENDSREYIKNLISETWKQMNEVRVAKSPLFSQAFIESAVDFVRGAMLLYQKGDGFGTKHDGDAKDKLVSLFFNPIPTP", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily."}
+{"protein": "MIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREGAESLEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQALLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSPPSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPSADILEPSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYPEGGQLLDEKFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERNLKVYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT", "text": "FUNCTION: Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex (PubMed:18692468, PubMed:25263562, PubMed:25457612, PubMed:26449471, PubMed:26612684, PubMed:26586190, PubMed:31586034, PubMed:35114100). In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling (PubMed:18692468, PubMed:25263562, PubMed:25457612, PubMed:26449471, PubMed:26612684, PubMed:26586190, PubMed:31586034, PubMed:35114100). Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway (PubMed:26449471, PubMed:26586190, PubMed:35114100). This stress- inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via TORC1 (PubMed:24947615). May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1 (PubMed:23274085). May also mediate TP53 inhibition of TORC1 signaling upon genotoxic stress (PubMed:18692468). Moreover, may prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (PubMed:26612684). Was originally reported to contribute to oxidative stress resistance by reducing PRDX1 (PubMed:15105503). However, this could not be confirmed (PubMed:19113821). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sestrin family."}
+{"protein": "MTLQKDKVIKWVRFTPPQVLAIGFFLTIIIGAVLLMLPISTTKPLSWIDALFTAASATTVTGLAVVDTGTQFTVFGQTVIMGLIQIGGLGFMTFAVLIVMILGKKIGLKERMLVQEALNQPTIGGVIGLVKVLFLFSISIELIAALILSIRLVPQYGWSSGLFASLFHAISAFNNAGFSLWPDNLMSYVGDPTVNLVITFLFITGGIGFTVLFDVMKNRRFKTFSLHTKLMLTGTLMLNAIAMLTVFILEYSNPGTLGHLHIVDKLWASYFQAVTPRTAGFNSLDFGSMREGTIVFTLLLMFIGAGSASTASGIKLTTFIVILTSVIAYLRGKKETVIFRRSIKYPIIIKALAVSVTSLFIVFLGIFALTITEQAPFLQIVFETFSAFGTVGLTMGLTPELTTAGKCIIIVIMFIGRIGPLTFVFSFAKTEQSNIRYPDGEVFTG", "text": "FUNCTION: Integral membrane subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TrkH potassium transport family. Ktr (TC 2.A.38.4) subfamily."}
+{"protein": "MNVFFMFSLLFLAALGSCADDRNPLEECFRETDYEEFLEIAKNGLTATSNPKRVVIVGAGMSGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKEDWYANLGPMRLPTKHRIVREYIKKFGLELNEFFQENDNAWYFIKNIRKRVQEVKNNPGLLKYPVKPSETGKSAGQLYEESLRKVVEELRSTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDREATVTYQTSANEMSSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDEGIHGGKSTTDLPSRSIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHQLPKEDIQTFCHPSKIQRWSLDRYAMGGITTFTPYQFQHFSEALTAPFNRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEF", "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. 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. 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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
+{"protein": "MAEWHKIIEDISKNNKFEDAAIVDYKTTKNVLAAIPNRTFAKINPLITNRNILKPLIGQKYCIVYTNSLMDENTYAMELLTGYAPVSPIVIARTHTALIFLMGKPTTSRRDVYRTCRDHATRVRATGN", "text": "FUNCTION: More likely to influence phosphoinositide metabolism than actin assembly. SIMILARITY: Belongs to the profilin family."}
+{"protein": "MAMALQIIASSSSSPTITKSHLFSYPPLQSRYKASKPNLSSWFSLLGSSRFSPYIGLKHLGISISPKSSNPEKKRRCKSMMIRASLFGVGAPEALVIGVVALLVFGPKGLAEVARNLGKTLRTFQPTIRELQDVSRDFKSTLEREIGLDDISTPNVYNQNRTNPVQPPPPPPPPSVPSTEAPVTANDPNDSQSPKAYTSEDYLKFTEEQLKALSPAESQTEDQTQTQEPPQPTTVQTPTGESQPNGTARETTAASPPRQD", "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 the thylakoid membrane. Involved in delta pH-dependent protein transport required for chloroplast development, especially thylakoid membrane formation. TATC and TATB mediate precursor recognition, whereas TATA facilitates translocation (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein Note=The C- terminus is located in the stroma. SIMILARITY: Belongs to the TatB family."}
+{"protein": "MSFRKRGEILNDRGSGLRGPLLRGPPRTSSTPLRTGNRRAPGNVPLSDTTARLKKLNIADESKTKMGLDSSHVGVRPSPATSQPTTSTGSADLDSILGHMGLPLGNSVLVEEQSTTEFHSILGKLFAAQGIVHNRISDSSADKTRNGDTHVIVLSLNQMFAKELPGIYKGSRKQMKKNLISEEESKVTVQNLNETQRSTPSRYKDLKIAWKYKLADEKRLGSPDRDDIQQNSEYKDYNHQFDITTRLMPAPIASELTFIAPTQPVSTILSQIEQTIKRNDKKLIRIVIPSLLHPAMYPPKMFESSEIIGLMHGVRSLVKKYYERVVLFASISIDIITPPLLVLLRNMFDSVINLEPFNQEMTEFLERVYKSQPGKIQHGLVHILKLPVFTDRGEMRVLKSEWAFKNGRKKFEIEQWGIPVDDAEGSAASEQSHSHSHSDEISHNIPAKKTKISLDY", "text": "FUNCTION: Component of the elongator complex, a multiprotein complex which is required for multiple tRNA modifications, including mcm5U (5- methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2- thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, PubMed:18755837). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) (PubMed:11296232). May also be involved in sensitivity to Pichia inositovora toxin (PubMed:13680368). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the ELP4 family."}
+{"protein": "MIKSELFERIAEQKINISNKMIERAAKEMLEHMIISLANGKRIEIRGFGSFSLHYRSSRIGRNPKTGKSVKLNEKYVPYFKPGKKLRDRANIHK", "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": "MNPTLVVELSGDKTLEPHRLGGKAHSLNHLIHAGLPVPPAFCITAQAYRQFIEFAVPGALLDTGAPGNVRDMILSAAIPAPLDLAIRHACKQLGDGASLAVRSSALEEDGLTHSFAGQYDTYLHVRGDDEVVRKVQSCWASLWAERAAQYSRTSAAQSDIAVVLQIMVDADAAGVMFTQDPLTGDANHIVIDSCWGLGEGVVSGQVTTDSFILDKASGEIRERQIRHKPHYCQRDPQGRVTLLQTPEARRDAPSLTPEQLQQLARLARQTRMIYGAELDIEWAVKDDRVWLLQARPITTQAKPVQMLYANPWESDPTIKERAFFSRMDTGEIVTGLMTPLGLSFCQFYQKHIHGPAIKTMGLADIGDWQIYMGYLQGYVYLNISGSAYMLRQCPPTRDEMKFTTRYATADIDFSGYKNPYGPGVQGWAYLKSAWHWLKQQRHNLRSAGATVDAMIALRQRETRRFLALDLTTMTHQELERELSRIDGYFLDSCAAYMPFFLQSFALYDALALTCERYLKGRGNGLQNRIKASMNNLRTIEVTLGILSLVETVNRQPALKALFERHSAQELVTVLPTDPESRAFWQSDFSAFLFEFGARGRQEFELSLPRWNDDPSYLLQVMKMYLQHPVDLHTKLRETERLRHEDSAALLKAMPWFGRMKLKFITKLYGVMAERREATRPTFVTETWFYRRIMLEVLRRLEAQGLVKSADLPYVDFERFRAFMAGEQSAQEAFAADLIERNRHQHLLNLHAEEPPMAIVGGYQPRMKAPTAENAAGMLSGLAASPGKVVAKARVITDLLAQAGELQPNEILVARFTDASWTPLFALAAGIVTDIGSALSHSCIVAREFGIPAAVNLKNATQLINSGDTLILDGDSGTVIIQRGERADG", "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 transfer of 2-methyl-3- n-amyl-pyrrole (MAP) to 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) to yield prodigiosin. It is able to use substrates with a variety of monocyclic rings in place of the pyrrolic ring A of its natural substrate. SIMILARITY: Belongs to the PigC family."}
+{"protein": "MFLATLYFALPLLDLLMSAEVSGGDRLDCVKASDQCLKEQSCSTKYRTLRQCVAGKETNFSLTSGLEAKDECRSAMEALKQKSLYNCRCKRGMKKEKNCLRIYWSMYQSLQGNDLLEDSPYEPVNSRLSDIFRAVPFISDVFQQVEHISKGNNCLDAAKACNLDDTCKKYRSAYITPCTTSMSNEVCNRRKCHKALRQFFDKVPAKHSYGMLFCSCRDIACTERRRQTIVPVCSYEERERPNCLSLQDSCKTNYICRSRLADFFTNCQPESRSVSNCLKENYADCLLAYSGLIGTVMTPNYVDSSSLSVAPWCDCSNSGNDLEDCLKFLNFFKDNTCLKNAIQAFGNGSDVTMWQPAPPVQTTTATTTTAFRVKNKPLGPAGSENEIPTHVLPPCANLQAQKLKSNVSGSTHLCLSDSDFGKDGLAGASSHITTKSMAAPPSCSLSSLPVLMLTALAALLSVSLAETS", "text": "FUNCTION: Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Golgi apparatus, trans-Golgi network Endosome Endosome, multivesicular body Note=Localizes mainly to the plasma membrane. In the presence of SORL1, shifts to vesicular structures, including trans-Golgi network, endosomes and multivesicular bodies. SIMILARITY: Belongs to the GDNFR family."}
+{"protein": "MIQKSRPALLQHQDVGDRVETLMLQPVIKAFLCGSISGTCSTVLFQPLDLLKTRLQTLQPSAHGSRRVGMLALLLTVVRTESLLGLWKGMSPSIVRCVPGVGIYFGTLYSLKQYFLRGHPPTALESVILGAGSRSVAGVCMSPITVIKTRYESGRYGYQSIYAALRSICHSEGFRGLFSGLTATLLRDAPFSGIYLMFYSQTKNVVLHSTDQLDAVLVPVVNFSCGIFAGILASLVTQPADVIKTHMQLSPVKFRWIGQSVTLIFKDYGLRGFFQGSVPRALRRTLVAAMAWTVYEEMMAKMGLKS", "text": "FUNCTION: Plays a role as pro-apoptotic protein that induces caspase- dependent apoptosis. 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. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily."}
+{"protein": "MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFLSIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKEKKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW", "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": "MVGSGISALGLLLLMQGSVDANGIQGFFYPWSCEGDVWDRESCGGQAAIENPNLCLRLRCCYRDGVCYHQRPDENMRRKHMWALGWTCGSLLFLITSICLFWWARRQDMLHLPRFLHRKCSKLSKTVSSLSKDRRSANKSTTVLQSPGGEVETAAAVSGEDTGGEE", "text": "SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein Note=Localizes in the intracellular space in testicular germ cells and sperm. Detected also on the cell surface in post-meiotic round spermatids. In cauda epididymal sperm relocates during the acrosome reaction from the inner-acrosomal membrane onto the equatorial segment surface, on which sperm-oocyte fusion occurs. Colocalizes with IZUMO1 at the inner-acrosomal membrane."}
+{"protein": "MAEAGTGEPSPSVEGEHGTEYDTLPSDTVSLSDSDSDLSLPGGAEVEALSPMGLPGEEDSGPDEPPSPPSGLLPATVQPFHLRGMSSTFSQRSRDIFDCLEGAARRAPSSVAHTSMSDNGGFKRPLAPSGRSPVEGLGRAHRSPASPRVPPVPDYVAHPERWTKYSLEDVTEVSEQSNQATALAFLGSQSLAAPTDCVSSFNQDPSSCGEGRVIFTKPVRGVEARHERKRVLGKVGEPGRGGLGNPATDRGEGPVELAHLAGPGSPEAEEWGSHHGGLQEVEALSGSVHSGSVPGLPPVETVGFHGSRKRSRDHFRNKSSSPEDPGAEV", "text": "FUNCTION: Protein associated with the U5 snRNP, during its maturation and its post-splicing recycling and which is required for spliceosomal tri-snRNP complex assembly in the nucleus (PubMed:34131137, PubMed:35188580). Has a molecular sequestering activity and transiently hinders SNRNP200 binding sites for constitutive splicing factors that intervene later during the assembly of the spliceosome and splicing (PubMed:35188580). Together with its molecular sequestering activity, may also function as a molecular adapter and placeholder, coordinating the assembly of the U5 snRNP and its association with the U4/U6 di- snRNP (PubMed:34131137). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the cytoplasm and the nucleus, associated with the U5 snRNP. SIMILARITY: Belongs to the TSSC4 family."}
+{"protein": "MVEVRHSRVIILGSGPAGYSAAVYAARANLKPLLITGMQAGGQLTTTTEVDNWPGDVHGLTGPALMERMREHAERFETEIVFDHINAVDFAAKPYTLTGDSATYTCDALIIATGASARYLGLPSEEAFMGKGVSACATCDGFFYRNKPVAVVGGGNTAVEEALYLANIASTVTLIHRRETFRAEKILIDKLNARVAEGKIILKLNANLDEVLGDNMGVTGARLKNNDGSFDELKVDGVFIAIGHTPNTSLFEGQLTLKDGYLVVQGGRDGNATATSVEGIFAAGDVADHVYRQAITSAGAGCMAALDTERYLDGLQNASE", "text": "FUNCTION: Catalyzes the conversion of 2-amino-2-deoxy-D-gluconate (GlcNA) to 2-keto-3-deoxy-D-gluconic acid (KDGA) and ammonia. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELKEKFTAFCKAQGFTEDTIVFLPQTDKCMTEQ", "text": "FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation (PubMed:20667974). Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non- substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (PubMed:20667974, PubMed:9475419). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). SUBCELLULAR LOCATION: Rough endoplasmic reticulum Nucleus membrane Golgi apparatus Cytoplasm, perinuclear region Secreted Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MRKDTPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGSLLLGVSSLSGRCWVGSLWFFKDPSAAPNEGFCSAGVQTEAGVADLTWVGDKGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVTVLSSGTQAVSGSKDCCIKIWDLAQQVSLNSYRAHAGQVTCVAASPHKDSVFLSCSEDSRILLWDTRCPKPASQMACNASGYLPTALAWHPQQSEVFVFGDENGSVSLVDTKNASCTLSSAVHSQGVTRLVFSPHSVPLLTSLSEDCSLAVLDSSLSEVFRSRAHRDFVRDATWSPLNHSLLTTVGWDHQVIHHVVPLEPLPNPGPDSVVE", "text": "FUNCTION: Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones (By similarity). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles (By similarity). Might play a role in transcription regulation (By similarity). The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain- containing proteins and subsequent localization to the meiotic nuage (PubMed:19584108). FUNCTION: Substrate-recognition component of the DCX(WDR77) complex, which mediates ubiquitination and degradation of Irgm1 in intestinal cells. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MAEDDMVSLLFKLKVEDVTCSDDPEKHMKNASNERKPLIEPVENQLMDIGEEGGSLDYWLLYLYVDCLTMMCCFHRGSLPYNWMQGALLTNLPSYQHDVTLDEVNRGLKSASDFFGYVDPMRSDYFTAFSFPGRVTKLNEQMELTSTKGRCLKFDLYASTQLRFKPGELVRHGECKFAIG", "text": "FUNCTION: Hydrolyzes cytokinin glucosides thus liberating free cytokinins."}
+{"protein": "MARKQNRNSKELGLVPLTDDTSHAGPPGPGRALLECDHLRSGVPGGRRRKDWSCSLLVASLAGAFGSSFLYGYNLSVVNAPTPYIKAFYNESWERRHGRPIDPDTLTLLWSVTVSIFAIGGLVGTLIVKMIGKVLGRKHTLLANNGFAISAALLMACSLQAGAFEMLIVGRFIMGIDGGVALSVLPMYLSEISPKEIRGSLGQVTAIFICIGVFTGQLLGLPELLGKESTWPYLFGVIVVPAVVQLLSLPFLPDSPRYLLLEKHNEARAVKAFQTFLGKADVSQEVEEVLAESRVQRSIRLVSVLELLRAPYVRWQVVTVIVTMACYQLCGLNAIWFYTNSIFGKAGIPPAKIPYVTLSTGGIETLAAVFSGLVIEHLGRRPLLIGGFGLMGLFFGTLTITLTLQDHAPWVPYLSIVGILAIIASFCSGPGGIPFILTGEFFQQSQRPAAFIIAGTVNWLSNFAVGLLFPFIQKSLDTYCFLVFATICITGAIYLYFVLPETKNRTYAEISQAFSKRNKAYPPEEKIDSAVTDGKINGRP", "text": "FUNCTION: High-capacity urate transporter, which may play a role in the urate reabsorption by proximal tubules (PubMed:18327257, PubMed:28083649, PubMed:22647630, PubMed:18701466). May have a residual high-affinity, low-capacity glucose and fructose transporter activity (PubMed:18842065, PubMed:18327257, PubMed:18701466). Transports urate at rates 45- to 60-fold faster than glucose (PubMed:18842065). Does not transport galactose (PubMed:28083649). May mediate small uptake of adenine but not of other nucleobases (PubMed:22647630). SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily."}
+{"protein": "MDYRRDGQNDQHQTEPSHTEQQNTENQKLIGHSEQELLDAPVSYEAGRQETASALEMEKQETAVKKEKKRRAAWLSPILGGIIGGGLMLGIAPYLPSDQNQATETASANKQVQSDNFTTAPITNASNIADMVEDLEPTIVGISNIQTSQNNTFGTGGGSSSESESGTGSGVIFKKDSDKAYIITNNHVVEGANKLTVTLYNGETETAKLVGSDTITDLAVLEISGKNVKKVASFGDSSQLRTGEKVIAIGNPLGQQFSGTVTQGIISGLNRTIDVDTTQGTVEMNVLQTDAAINPGNSGGPLINASGQVIGINSLKVSESGVESLGFAIPSNDVEPIVDQLLQNGKVDRPFLGVQMIDMSQVPETYQENTLGLFGDQLGKGVYVKEVQANSPAEKAGIKSEDVIVKLNGKDVESSADIRQILYKDLKVGDKTTIQVLRKGKTKTLNATLTKQTESSSS", "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 (Probable). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S1C family."}
+{"protein": "MSQIHKHTIPANIADRCLINPQQYEAMYQQSINAPDTFWGEQGKILDWIKPYQKVKNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDASQSKHISYKELHRDVCRFANTLLKLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVDDALKNPNVTSVEHVVVLKRTGGKIDWQEGRDLWWHDQVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDSYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAIAMPS", "text": "FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs 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. FUNCTION: Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MTLEEKIGQMSQIDARRIGAATALEVRGFLISDSQGIDRHNLIPMSRIDDAVSRKSLVLLK", "text": "FUNCTION: Beta-glucosidase highly specific for the cleavage of C-26- bound glucose moiety of furostanol glycosides torvosides A and H. Hydrolyzes only p-nitrophenyl-beta-glucoside, but not p-nitrophenyl- beta-D-fucoside, p-nitrophenyl-beta-L-fucoside, p-nitrophenyl-beta-D- xyloside, p-nitrophenyl-beta-D-galactoside, p-nitrophenyl-beta-D-NAc- glucosamine, p-nitrophenyl-beta-D-mannoside or any of the p- nitrophenyl-alpha-glycosides tested. SIMILARITY: Belongs to the glycosyl hydrolase 3 family."}
+{"protein": "MKHLSIFFVFFCCICVMLCDAYGDCKKNSDCKAGECCVNTPPFARSTCQKYLQQGEFCAHMGKYNPLGKYINMCPCGKGLKCQLKDVSGPLALFRSRMLTCV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 20 family."}
+{"protein": "MSNGQLIYLMVAIAVILVLAYVVAIFLRKRNEGRLEALEEKKEELYNLPVNDEVEAVKNMHLIGQSQVAFREWNQKWVDLSLNSFADIENNLFEAEGYNHSFRFLKASHQIDQIESQITLIEEDIAAIRNALADLEKQESKNSGRVLHALDLFEELQHRVAENSEQYGQALDEIEKQLENIQSEFSQFVTLNSSGDPVEAAVILDNTENHILALSHIVDRVPALVTTLSTELPDQLQDLEAGYRKLIDANYHFVETDIEARFHLLYEAFKKNQENIRQLELDNAEYENGQAQEEINALYDIFTREIAAQKVVENLLATLPTYLQHMKENNTLLGEDIARLNKTYLLPETAASHVRRIQTELESFEAAIVEVTSNQEEPTQAYSVLEENLEDLQTQLKDIEDEQISVSERLTQIEKDDINARQKANVYVNRLHTIKRYMEKRNLPGIPQTFLKLFFTASNNTEDLMVELEQKMINIESVTRVLEIATNDMEALETETYNIVQYATLTEQLLQYSNRYRSFDERIQEAFNEALDIFEKEFDYHASFDKISQALEVAEPGVTNRFVTSYEKTRETIRF", "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. SIMILARITY: Belongs to the EzrA family."}
+{"protein": "MADKGSGGSRLPLALPPASQGCSSGSSGSSAGGSGNPRLPRNLQGLLQMAITAGSEEPDPPPEPMSEERRQWLQEAMSAAFRGQREEVEQMKNCLRVLSQATPPTAGEAELATDQQEREGALELLADLCENMDNAADFCQLSGMHLLVGRYLEAGAAGLRWRAAQLIGTCSQNVAAIQEQVLGLGALRKLLRLLDRDSCDTVRVKALFAISCLVREQEAGLLQFLRLDGFSVLMRAMQQQVQKLKVKSAFLLQNLLVGHPEHKGTLCSMGMVQQLVALVRTEHSPFHEHVLGALCSLVTDFPQGVRECREPELGLEELLRHRCQLLQQHEEYQEELEFCEKLLQTCFSSPTDDSMDR", "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": "MPKLEMMLLVLLILPLCYIDAVGPPPPWNMEDEIIEHWQKLHCHEISDLTPWILCSPEPLCGGKGCCAQEVCDCSGPVCTCPPCL", "text": "FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin D superfamily."}
+{"protein": "MSKSRRVFLSIQGDDDFWGNGDQLEGKTLSSIKQQESKKMDDSVEGMEEEKYFFRQSKLGRQNLERLHEKEEQECEEERLDWSEKVDSEEEEEDIQEQDEIITEGKETEMFDSGPETDQKMPVDPNEGFYNNYRSYFSGRPEMLFLIRSIDESATDYYEKPFIDLYETTRKRLEMYPNTELNQILRCACNPNAGGGADYRVRNKHAVVVSNFREPDRRLGRYSKYYYHHNVGPEVYSRKVFVGGLPACVKEMDILHFFSRYGRLQVDWPSKHYGCKSDSDPSVYNEPSFTPPTSHLGLSSPPFGQINPFMTDCPPAPSDLQMSRHGSVDGGGGGFPTHGMSMRNIGFGGGSGPRSTGEGEKKQQHLGYVFLLFEKERSVRDLVTECFEEEEGLFIILESAIEPIRVQIRPWLLADAEFLMDFNVPINTKMVAFIGGVPRPLKAVELAHFFEQTYGNVVCVGIDIDNKFKYPRGSGRVAFSNYHAYVQAITDRYIVLDHEDIHKRVEIKPYFFHNQSCEECSSRYHRQYAPFFCPSLECFQYYCEPCWHKMHARPSRFHHMPVVKGI", "text": "FUNCTION: Cytoplasmic polyadenylation element binding protein that binds to and regulates the translation of specific mRNAs."}
+{"protein": "MLFESFDLVSALATLAACLVSMALLLAVPQQLWQLRWTATRDKSCKLPMPKGSMGFPIIGETCHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFELSTRTFPRMISVPVVHPTDGLRVKFFGLDSNQNQIMAKSDEMLDATV", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:15661642). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (By similarity). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity). Involved in the convertion of atRA to all- trans-4-oxo-RA. Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4- hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (By similarity). Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints (PubMed:22019272). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MDAKIGQFFDSVGTFFSGSDKIPWCDGDVIAGCEREVREATDSGTEDLKKECLMRLSWALVHSRQTEDVQRGIAMLEASLESSAPPLEDREKLYLLAVGYYRSGNYSRSRQLVDRCIEMQADWRQALVLKKTIEDKITKDGVIGIGITATAFGAVGLIAGGIVAAMSRKK", "text": "FUNCTION: Component of the peroxisomal and mitochondrial division machineries. Plays a role in promoting the fission of mitochondria and peroxisomes. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FIS1 family."}
+{"protein": "MGTKKVKISSVKRAAHLKSKKTPLSKQQQQKQKQKRDQLKSKREQGQNIFSQKARKRDNLAQRKKHNKLASLGLDPLEEDNEDGDDEMLENVADMLDGDDLALLQANKRKRKAKTTGENDPDQGQSIGLERAYASDTKKEQDAQKIKLDLLPIKSRDGQIITRTTEVDYIPKPKQKKKNEEEEEDDSEEDGDTEYEDSDDDVVNDVEAATAAPVQKLISTTDLLIARQQEIERQKYRIGIICSGLLEKPEDKMRNFHALYELMDEINPASRQANLMAVRKLAIISVTEIFKDILPEYRVGQVDTKMQTLRKATLDRVTFENALLQQFKKFLQKLEQITAQVNRRGGLRTPQTVKLATVAVQCMCDLLVAHPYFNYVQNIAQLLVYMLNCNYAEMRTAVHQCFRTVFSNDKRLEMTLFIVRRINHLIKTKQNNVHVECITCLMGLKIKNVNLDAEKENELKQKKLESHRQRLLSLSKKERKRRKKLTEVNRELEETRAEENKQAKHQKLTEIIKMVFTIYFRVLKNDPTSRVLSAILEGLAEFAHVINLDFFSDLIDVLNRILEDQDELGYRERLHCVQTIFVILSGQGEVLNIDPIRFYQHFYRNMLAVQAGKNHDDFAIILRTLDEVLVKRRRNMSQQRLMAFMKRLLTGSLHLLHNGTLATLGTIKQTFQLTSVLDNLLDTDTTIGSGRYDPELDDPEYCNAASTALYELALLARHYHPTVRRMAVHIAHGVPATGEGALPTEIGKLTSHELFTQFDSTQMAFNPTIPLPKAGQPKLKRGKHLYIRSDFKQEYGKLLQQGKVSQTKDKQTLQIDFFSALQ", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the CBF/MAK21 family."}
+{"protein": "MRSRSFLVLVVVFLICGTLVAQAAGRIRRPKGKGTKKILALVKGQGPVRGKDQVKGQGPVKGQDLGKSQDPVKAQLPDKGQDLGKGEDSVKGQDPFKAQLPDKLQDPVKAQPAIKRLILLTKPGSCPRILIRCLMVNPPNRCLSDAQCPGLKKCCEGFCGKACMDPK", "text": "FUNCTION: Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis (By similarity)."}
+{"protein": "MAGSELRAELEQRLGALAIRTEVVEHPEVFTIEEMMPHIQHLKGAHSKNLFLKDKKKKNYWLVTVLHDRQINLNDLGKQLGVGSGNLRFADETAMLEKLKVGQGCATPLSLFCDDGDVKFVLDSAFLEGGHEKVYFHPMTNAATMGLSPEDFLIFVKATGHDPIILNFD", "text": "SIMILARITY: Belongs to the PRORSD1 family."}
+{"protein": "MDQPEAPCSSTGPRLAVARELLLAALEELSQEQLKRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQERRLQRLGLGSGTLLSVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPEEAMGPAEEPEPGRARRSDTHTFNRLFRRDEEGRRPLTVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVDFAFFMPCGELLERPGTRSLADLILDQCPDRGAPVPQMLAQPQRLLFILDGADELPALGGPEAAPCTDPFEAASGARVLGGLLSKALLPTALLLVTTRAAAPGRLQGRLCSPQCAEVRGFSDKDKKKYFYKYFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQQLELGRDLSRTSKTTTSVYLLFITSVLSSAPVADGPRLQGDLRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFLSKKELPGVLETEVTYQFIDQSFQEFLAALSYLLEDGGVPRTAAGGVGTLLRGDAQPHSHLVLTTRFLFGLLSAERMRDIERHFGCMVSERVKQEALRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCRFPELALQRVRFCRMDVAVLSYCVRCCPAGQALRLISCRLVAAQEKKKKSLGKRLQASLGGGSSSQGTTKQLPASLLHPLFQAMTDPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAWPQCRVQTVRVQLPDPQRGLQYLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGCGLQTLSLASVELSEQSLQELQAVKRAKPDLVITHPALDGHPQPPKELISTF", "text": "FUNCTION: Acts as the sensor component of the NLRP6 inflammasome, which mediates inflammasome activation in response to various pathogen- associated signals, leading to maturation and secretion of IL1B and IL18 (PubMed:30392956, PubMed:34678144). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:30674671). Acts as a recognition receptor (PRR): recognizes and binds specific pathogens and other damage-associated signals, such as lipoteichoic acid (LTA), a cell-wall component of Gram-positive bacteria, or double stranded RNA (dsRNA) (PubMed:30392956, PubMed:34678144, PubMed:33377178). May also recognize and bind lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria; however, LPS is probably not a major activator of the NLRP6 inflammasome (PubMed:31932628, PubMed:34678144). Following LTA- or dsRNA-binding, NLRP6 undergoes liquid-liquid phase separation (LLPS), enhancing multivalent interactions, an essential step for the formation of the NLRP6 inflammasome polymeric complex (PubMed:34678144). The NLRP6 inflammasome acts by promoting recruitment of effector pro-inflammatory caspases (CASP1 and/or CASP4) that catalyze maturation and secretion of IL1B and IL18 in the extracellular milieu (PubMed:30674671, PubMed:12387869, PubMed:30392956, PubMed:34678144). The NLRP6 inflammasome plays a central role in the maintenance of epithelial integrity and host defense against microbial infections in the intestine (PubMed:30392956). Required to restrict infection against Gram-positive bacteria by recognizing lipoteichoic acid (LTA), leading to recruitment of CASP4 and CASP1, and subsequent maturation and secretion of IL1B and IL18 (PubMed:30392956, PubMed:33377178). Involved in intestinal antiviral innate immunity together with DHX15: recognizes and binds viral dsRNA to restrict infection by enteric viruses through the interferon pathway and GSDMD-dependent release of IL18 (PubMed:34678144, PubMed:34161762). Required to prevent infection by the apicomplexan parasite Cryptosporidium in enterocytes by promoting GSDMD-dependent release of IL18 (By similarity). The NLRP6 inflammasome may also regulate the gut microbiota composition by acting as a sensor of microbiota-associated metabolites to form a PYCARD/ASC-dependent inflammasome for downstream IL18 release and secretion of antimicrobial peptides (By similarity). Essential for gut mucosal self-renewal and proliferation (By similarity). Regulate mucus secretion in an inflammasome- and autophagy-dependent manner to prevent invasion by enteric bacteria, (By similarity). During systemic bacterial infections, the NLRP6 inflammasome negatively regulates neutrophil recruitment and neutrophil extracellular traps (NETs) formation (By similarity). May promote peripheral nerve recovery following injury via an inflammasome-independent mechanism (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Inflammasome Cell membrane Nucleus membrane. SIMILARITY: Belongs to the NLRP family."}
+{"protein": "METSPISPMNEKNTAQPQQREENAQQILNTAIPFRQRSPGLLPEALKVGVRPDPANQIVETQEIEHPVAGFEGDSDQFQVSTNEMAEHLQASDLWYCPDGSFVKKIIVPGHGLDKPKLGSKCQVLALGFPFGSGMPEGWTELTIGIGQWREKMWGELMEKCLESMRQGEEAKIHLPGSSAPLAKLRLDSFTNGRDSWEMEAMEKEALAKEEHRRGTELFRAGNPQGAARCYGRALRLLLTLPPPGPPERTTLYANLAACQLLLGHPQLAAQSCDRVLEREPGHLKALYRRGVARAALGDLEKATADFKKVLAVDPKNRAAKEELGKVVIQGRKQDAGLARGLRKMFS", "text": "FUNCTION: May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21."}
+{"protein": "MASFPESDFQLCPLCKEMCVSTSSSSAGSAGGGTGLASAPPRRLHVLPCLHAFCRQCLEGRRSPGDSLQLRCPVCDHKVLISEAGMDALPSSTFLHLSNLLDAVVGAADEQQQSNGGRTASNRQRSASCSSSGLLRRAPPSQSEPRCSSCDDGNGASSHCLDCQENLCDNCLRAHQRVRLTKDHFIERFPASPCSSAASSAATTSSSSSSAFSLLPVYPERLYCQQHDEEVLHFYCDSCSVPICRECTMGRHAGHSFVYLQEALQDSRALTIQLLADAQQGRQAIQLSLEQAQALAEQVEMKAKVVQSEIKAVTSRHKKALEERECELLWKVEKIRQVKAKSLYHQVEKLHQALNKLDSTINAVQQVLEEGCTMDILIARDRVLAQVQDVKNARGLLQLQEDDRIMFTPPDQALYLAIKSLGLVSSGAFAALTKATGEGLKRALQGKVASFTVIGYDHDGEARLSGGDLITVLVMGPDGNLFAAEVSDQLNGTYLVSYRPQLEGEHLISVMVCNQHIENSPFKVNVKSGRCYLGIGLPTLSFGGEGDHDGKLCRPWGVCVDREGYIIVADRSNNRVQIFKPCGTFHHKFGSLGSRPGQFDRPAGVACDNSRRIVVADKDNHRVQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRVQLFGPDGTFLNKYGFEGALWKHFDSPRGVAFSQDGYLVVTDFNNHRLLIIKPDCQSAHFLGTEGTGNGQFLRPQGVAVDQEGRIIVADSRNHRVQIFEPNGSFLCKFGTQGSGFGQMDRPSGIAVTPDGTIVVVDFGNNRILAF", "text": "FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance. Binds to miRNAs and participates in post-transcriptional repression of transcripts. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development. SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the TRIM/RBCC family."}
+{"protein": "MSAAARVVAPVMMLSRFRGALVGSVLGDCIGGEFEGAVDVPLDRVLQHLSALEDDTRGDGILQYSDDTAMMRCVADSLLTRMTFDERDMAQRFAKEYSHSPGRGYGSGVVQVLRKLASPHLKDVFQPAQAQFGGRGSFGNGGAMRAVPFALAFRSRADVRKYSRFGAMLTHSCSLGYNGAALQALAVHLSLQGALALPKDFIDKLISEMEELEKDETAKHDAKALNLSEFPYCSRLHRVKELMDKTSVSIEEVISELGNGIAALQSVPTAIFCVLYCLEPQDGLPERFGGLERTIAYSLALGGDTDTIACMAGAIAGAHYGIDSIPLSWQVSCEGVDEADDLARRLYDLYCLPQHNEDRGNNQPHTTNTD", "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": "METQRASLCLGRWSLWLLLLALVVPSASAQALSYREAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDPGTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVKQCVGTVTLDQIKDPLDITCNEVQGVRGGRLCYCRRRFCICVG", "text": "FUNCTION: Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cathelicidin family."}
+{"protein": "MVKRNQRKKSAPKKRLTKAEVEKQRAIKRMILSVLMALLLIFAMLRLGVFGVTTYNMIRFLVGSLAYPFMFAWLIYLFCFKWLRQKDGMIAGVVIAFLGLLVEWHAFLFAMPRMLDQDIFLGTARLITRDLLALRVTEFVGGGMLGALLYKPIAFLFSNIGSYFIGFLFILLGLFLMTPWDIYDVSHFVKEAVDKLAVAYQENKEKRFIKREEHRLQAEKEALEKQAQEEEKRLAELTVDPETGEIVEDSQSQVSYDLAEDMTKEPEILAYDSHLKDDEASLFDQEDLAYAHEEIGAYDSLSALASSEDEMDMDEPVEVDFTPKTHLLYKLPTIDLFAPDKPKNQSKEKNLVRKNIKVLEDTFQSFGIDVKVERAEIGPSVTKYEIKPAVGVRVNRISNLADDLALALAAKDVRIEAPIPGKSLIGIEVPNSEIATVSFRELWEQSDANPENLLEVPLGKAVNGNARSFNLARMPHLLVAGSTGSGKSVAVNGIISSILMKARPDQVKFMMIDPKMVELSVYNDIPHLLIPVVTNPRKASKALQKVVDEMENRYELFSKIGVRNIAGYNTKVEEFNASSEQKQIPLTLIVVIVDELADLMMVASKEVEDAIIRLGQKARAAGIHMILATQRPSVDVISGLIKANVPSRMAFAVSSGTDSRTILDENGAEKLLGRGDMLFKPIDENHPVRLQGSFISDDDVERIVNFIKDQAEADYDDAFDPGEVSDNDPGFSGNGGAAEGDPLFEEAKALVLETQKASASMIQRRLSVGFNRATRLMDELEEAGVIGPAEGTKPRKVLQTN", "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": "MFNQTQFFVLLAVFTTSSVLGNNNDVKDGAASGAHSDRLGLWFGPRLGKRSLRISTEDNRQAFFKLLEAADALKYYYDQLPYEMQADEPETRVTKKVIFTPKLGRSLAYDDKSFENVEFTPRLGRRLSDDMPATPADQEMYRQDPEQIDSRTKYFSPRLGRTMNFSPRLGRELSYDMMPNKIRVVRSANKTRST", "text": "FUNCTION: A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pyrokinin family."}
+{"protein": "MTTVKFKYKGEEKQVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK", "text": "FUNCTION: Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family."}
+{"protein": "MKTGMFTCGHQRLPIEHAFRDASELGYDGIEIWGGRPHAFAPDLKAGGIKQIKALAQTYQMPIIGYTPETNGYPYNMMLGDEHMRRESLDMIKLAMDMAKEMNAGYTLISAAHAGYLTPPNVIWGRLAENLSELCEYAENIGMDLILEPLTPYESNVVCNANDVLHALALVPSPRLFSMVDICAPYVQAEPVMSYFDKLGDKLRHLHIVDSDGASDTHYIPGEGKMPLRELMRDIIDRGYEGYCTVELVTMYMNEPRLYARQALERFRALLPEDE", "text": "FUNCTION: Catalyzes the reversible interconversion of fructoselysine with its C-3 epimer, psicoselysine. Allows E.coli to utilize psicoselysine for growth. Does not act on psicose or fructoselysine 6- phosphate. SIMILARITY: Belongs to the FrlC family."}
+{"protein": "MASAATTTHFPSSRIPSEPCASSGPLFPDDVLFTTEASSASSSSCHVENDSRPLSPTMFTDGRTPVNISAKHLKDHPLHEPTGTSEVLTFYPTMREFKNFSQYIKKIEQNGGHLKAGIAKIVAPEGWTPRPTRKDFSDVDDYEITQPARETIEATEKPGAYFKRNVTCRRKMPVREFRTLANSAQYRNPRPDLKGSEIEKHYFDNILHGEPIYGADTEGSFYDAQVEEWNMNRLGTILEDTNYEIKGVNTVYLYFGMYKTTFPWHAEDMDLYSINFLHFGAPKYWFAISSEHADRFERFMSQQFSYQNEYAPQCKAFLRHKTYLVTPELLRQAGIPYATMVQRPNEFIITFPRGYHMGFNLGYNLAESTNFASQRWIDYGKDAVLCDCNKDSVKIDMTHFMAKYRPDEYTTWWTYWYGGGRELWIPKKKKEVPKKRRQSLADASKIAKRARLGASSTATDSDGSSGSSGSEEATEGSSFMRALPAGYTVHNWQLRPDYDELLRKYKKETKLLRSDTRIDFYQEREFNHARRAEWPHCAVCQYFQPPHMNAINHTVPNSSRRLIPKWCFSKTDTKKHEDHHEPPPPLDRLLTCSNCHVTVHSHCCSGGGGGGGDDDDVTSSGEPWRCPRCRNRTDVEIRTTSCQLCELRGGALIPCQIGTDSTWAHVACALFNRRAIFDCPNRPGACFVEPSPRQQSETPRMPPRRLSEEYRAELGDLYENSRWECVVCHRTDEGLAPCVLCIEEQATTSLPTLAHVTCARRVGFVCEVRDYPRGVVMICHKHEHSYLVNKTTQQQAYTNVKVGDFVFVEDVVEPPQKLFTRGAIVRADKKETVVVDFLDNSCSRDNHVEDIISCECLFCENGDHQYGARVKVVWDDKQVYDAYFRGKGQMIEYTVRLEDGREVRHPRNRLKTKRELNAYLKK", "text": "FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed:16603238, PubMed:24685137). Demethylation of Lys residue generates formaldehyde and succinate. Involved in the negative regulation of lifespan in a germline-dependent fashion (PubMed:22212395). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the JHDM3 histone demethylase family."}
+{"protein": "MSTPAYLTKLESIPKEKFLFGPSPISYLPNLTAVLGGKVKLYAKREDCNSGLAYGGNKVRKLEYLVADAKAKGCNTLVSVGGVQSNHTRAVTAVAVASGLKAVTVQEKWVPIDPPLYSETGNILLSRLMGGDVRLNQETFDIRHKKATEDAFKDVEAKGGKPYYIPAGASDHPLGGLGFTNWVVELAKQEKELGVFFDVVIVCSVTGSSHAGTVVGAVAEGRKRKIIGIDASGKPEATRNQVLKIARNTAALLDERLEIKEEDVILDDRFHAGIYGIPDDETIAAMKLAAQTDAFITDPVYEGKSMAGMIRLVKEGAIKEGSNVLYIHLGGQPALNAYSSYFPHA", "text": "FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase family."}
+{"protein": "MTRDQKFALVTGCGKGGIGEALILEYTRRGIYAIATVLPTENSDHLTAAGITWFPLDVTDEQSVVDLKKSIASVTDGYLDFLVNNAGICYTMTAIDTDVSAVKRMFDVNVFGPMRMVHHFHDMLIQATGTIVNIGSIGGVVPYMYGASYNASKAALHHYSNTLRLEMSPFNVKVLTVISGEVGTNILKNDVHRNLPEGSYYSPLAVEFRDHVQRTPKTTSRFEYAENVVAQSLKSSPAAWFWTGSATGIIRFLDMFAWRTIWDFFFYREFNLGKVKDAYLANLKKDM", "text": "FUNCTION: Short-chain dehydrogenase; 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 short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MAEPSLPLSFLCLLALSSACYIQNCPRGGKRALGDTALRQCLPCGPGNRGRCFGPGICCGAELGCYLGTAETRRCAEEDYMPSPCQAGGQPCGSDGRCAANGVCCSADTCAMDAVCLEEGSEQAEEAAEKNLTVLDGAAGDLLLRLMHLANRQQQGKQPGL", "text": "FUNCTION: Vasotocin is an antidiuretic hormone. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the vasopressin/oxytocin family."}
+{"protein": "MDISGAVKQKLLQFLGKQKKPELLATYLFYLEQALSLRPVVFVRDKIIFKTPEDAVRILEQDKKIWRETEIQISSEKPQVNENTKRIYICPFTGKVFADNVYANPQDAIYDWLSSCPQNMEKQGGVRIKRFLVSEDPDVIKEYAVPPKEPIIKTVFASAITGKLFHSLPPLLEDFISSYLRPMTLEEVQNQTKFQLESSFLSLLQDALVEDKIAAFIESLADDTAFHVYISQWVDTEE", "text": "SIMILARITY: Belongs to the chlamydial CPn_0658/CT_538/TC_0825 family."}
+{"protein": "MAAPPGEAPLTAATNIEPFYVLHKGGAAASSSSSSAPSLPSSGRARRRIDVSGLASPNPKPGKRSRDDDAAEDDDDDELYERLRLDAFHRVWSKIQSTINEVLRGISLKLFDQVLRWVQESFSAVRSIARPSAAEVRQPYPLLTDVICRKIPTAFVLTKNAEFVDDITTFRDLAEYLESNGCHLAKLSATELSEKNGVGCCFRSLLRQLLSDVPDVADIFALASWYSAAENYDQPIVVVIDDLEQCSGDVLGELVMMLSEWVIKIPIFFVMGIATTLDAPRKLLSSEDLQRLEPCKLTLGSPSDRMNALVEAILVKPCAGFCISHEVAVFLRNYFFKHDGTITSFISALKLACSKHFSVEPLSFLCMGMLEEDRENFWHDKFNALPQELRKYASGLPSCTREKDSTKSGDNMVDGLSELMNIQKDWSSVLLCLYEAGKHGKVQLLDIFCEAVNPDLHTQKAPNLPNEKSGTSRRFIDQVMDTIRYLPVETLFCLLEVWSIHLNGMDKITNKVKELQSTTISTDSVRITKDKWPRRSTNSTGNSTVALNDKVAMLLDDVTRKFLVSVECLPFHEIVCFKNVSILQSALIGNPRRMVQLDLVKSHKHLKCSCCRKNGIAVLASMHDTSIMCNLAQEYGDVINLHDWYISFDGIINSVHSKIKRKPHTSPSKKKSKPVAAESEAMIQARFCRAVTELQITGLLRMPSKRRPDLVQRIAFGL", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC3 family."}
+{"protein": "MSFGSEHYLCASSSYRKVFGDGSRLSSRLSGAGGSGSFRSQSLSRSNVASSAACSSASSLGLGLAYRRSPASDGLDLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRDLRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVDVAVAKPDLSSALREIRAQYESLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSAEVASYQDNIGQLENDLRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTSGLSISGLNPLPNPSYLLPPRILSSTTSKGSATGLSLKKEEEEEEASKIASKKTSQIGESFEEILEETVISTKKTEKSNIEETTISSQKI", "text": "FUNCTION: Class-IV neuronal intermediate filament that is able to self- assemble. It is involved in the morphogenesis of neurons. It may form an independent structural network without the involvement of other neurofilaments or it may cooperate with NEFL to form the filamentous backbone to which NEFM and NEFH attach to form the cross-bridges (By similarity). May also cooperate with the neuronal intermediate filament protein PRPH to form filamentous networks (By similarity). SIMILARITY: Belongs to the intermediate filament family."}
+{"protein": "MGLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMVAPVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVIEFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK", "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:3129430, PubMed:17158705). The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:2657735). The non-phosphorylated EIII-Glc is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, and glycerol. Phosphorylated EIII-Glc, however, may be an activator for adenylate cyclase. It is an important regulatory protein for cell metabolism (PubMed:789369). 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. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MPHTVATPPPLLQVRGISKQFSGVVVLKSIDFTLQPGQVHALLGGNGAGKSTLMKIIAGILPPDTGVIEMNGQPCFNLTPAKAHQLGIYLVPQEPMLFANLSVQENILFRLPKHQADKKKMAQLLKNLGCHLDLSVSAGSLEVADQQLVEIMRGLMRDSRILILDEPTASLTPAETHRLFSQIRMLLQQGVGVVFISHKLPEIRQLADWVSVMRDGGIALSGATADFSTEDMIQAMTPEAQKGALTDSQKLWLELPGNRRAQSRAQSQQPVIHVHDLSGEGFAHISFHVQAGEILGLAGVVGAGRTELAETLYGLRPASTGNVILEEVNITAMKTANRLAAGLVYLPEDRQASGLYLDAPLSWNVCALAHDRQGLWTQPAQEAAVLERYRRALNIKFSHLEQPVRTLSGGNQQKLLIAKCLEANPLLLIIDEPTRGVDVSARSDIYQLIRSIAEQQVAIIFISSDLEEVVQMADRVLVMHQGEINGALSGAAMNVDTIMHMAFGEHRSVSEPQGGTASSAENKGASC", "text": "FUNCTION: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. AI-2 autoinducer porter (TC 3.A.1.2.8) family."}
+{"protein": "MFSVLSCGRLVARAVFGGLSQTDSRDYSLVTASCGFGKDARKGILKKGMCYGDDACFIARHRTADVLGVADGVGGWRDYGVDPSQFSETLMRTCERLVKEGRFVPTNPVGILTSSYRELLQNKVPLLGSSTACLVVLDRTSHRLHTANLGDSGFLVVRAGEVVHRSDEQQHYFNTPFQLSIAPPEAEGAVLSDSPDAADSNSFDVQLGDIILTATDGLFDNMPDYMILQELKKLKNTNYESIQQTARSIAEQAHDLAYDPNYMSPFAQFACDYGLNVRGGKPDDITVLLSIVAEYTD", "text": "FUNCTION: Protein phosphatase which positively regulates biosynthesis of the ubiquinone, coenzyme Q (By similarity). Dephosphorylates the ubiquinone biosynthesis protein coq7 which is likely to lead to its activation (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the PP2C family."}
+{"protein": "MAGGAFIDESGHGGDYEGRVTAFVMITCIVAAMGGLLFGYDIGISGGVISMEDFLTKFFPDVLRQMQNKRGRETEYCKYDNELLTLFTSSLYLAALFASFLASTITRLFGRKVSMVIGSLAFLSGALLNGLAINLEMLIIGRLFLGVGVGFANQSVPLYLSEMAPAKIRGALNIGFQLAITIGILAANIVNYVTPKLQNGIGWRLSLGLAGVPAVMMLVGCFFLPDTPNSILERGNKEKAKEMLQKIRGTMEVEHEFNELCNACEAAKKVKHPWTNIMQARYRPQLTFCTFIPFFQQLTGINVIMFYAPVLFKTIGFGNDASLISAVITGLVNVLSTIVSIYSVDKFGRRALFLQGGFQMIVTQIAVGSMIGWKFGFNGEGNLSGVDADIILALICLYVAGFAWSWGPLGWLVPSEICPLEIRSAGQSLNVSVNMFFTFFIGQFFLTMLCHMKFGLFYFFAGMVLIMTIFIYFLLPETKGVPIEEMGKVWKEHRYWGKYSNNDDGDDVDDDAYF", "text": "FUNCTION: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport. Can transport glucose, galactose, mannose, xylose and 3-O-methylglucose, but not fructose and ribose. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
+{"protein": "MIFGHIAQPNPCRLPAAIEKALDFLRATDFNALEPGVVEIDGKNIYTQIIDLTTREAVVNRPEVHRRYIDIQFLAWGEEKIGIAIDTGNNKVSESLLEQRNIIFYHDSEHESFIEMIPGSYAIFFPQDVHRPGCIMQTASEIRKIVVKVALTALN", "text": "SIMILARITY: Belongs to the TabA/YiaL family."}
+{"protein": "MNSSYKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSSKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCSTFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY", "text": "FUNCTION: Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S.aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C47 family."}
+{"protein": "MSSNSSCLVTNQGGALPLTATCLEGFYCPNNSLENPPEICPPTPQCRLTRLQEYHNICDHAQGTYEPIVCQPGFYCPSGGKRQIPCPKGHFCPLGTVEPFKCFGLSSCAEGSEREIPLAGLLCSILLDIFLVIVVSWPFPFAWIRQLSRGKLRRGAGGNDSESGVISAGRREISFSESKYHVSQFFTSDGSHGTAAGIEVEFSGISMRPTRSGIETLCLQNGVIRAGSFVGVMGPSGSGKSTLVKVLTGRAQPTTGSVLINGDTCRAAELRDLLALVPQDDIILPDLTVQENILYSSRVRIGSSRKDSEIEQYVDHLIISLGLNKVRNRLIGEVGKRGLSGGERKRVNIALELAAVPGIIVLDEPTSGLDAMTALSVIELLKSLTKQGVIVICVIHQPRLEIFAALDDLLLLNHGRQVYFGSAAAAKQCFQDAGYTFPLNSNPTDTMMDIMSCHDNLHLTDYPRNKPALPKQNLRIVLQSVKKIRAPWYCQVLLAFMRGTKQQTRQYPSFVLEILTGAGCGILIGLSNYEFKGHLFQGLFHLPFQLLSSPVSYRLLTEQGMLLCLTIGCAAGPAGVKTFGEEKLVFLRESCSGYSEGAYFLGKALSTLIRIFLSALHFTSFYLILTTPIVSFPNQLIVNLLYFYCIYGAASMISAITSPKNGPLITMLTSVLFCALSGCAPRLASVKSWNLAWLWYICPAVWIAEANFNQYTDPLAYLYDIKPAAEDAIRAWDRLSLHSLFIV", "text": "FUNCTION: ABC-type transporter; 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). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family."}
+{"protein": "MSRKDDNQSGEVGRTLVDFMEVAITMIVYLKGFYPSAAFERRRYMNVVVQRARHPELRDYIHSAASGLLPFIEKGLVERVAVVFFSEDNVPVERFIFKITIKPSCAALVEEGQLEFALRSFLIKLSVSKSLVKPLPLNCRWEVTAYLRSLPQVGSSKEAELWIPTDTKQWQNPPVLTPVKSLNSEPLCLQLYLEHPSLSEPLNLVNPEDVAPHDP", "text": "FUNCTION: Regulatory subunit of the error prone DNA polymerase zeta. Involved in damage-tolerance mechanisms through translesion DNA synthesis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MAD2 family."}
+{"protein": "MKGSSESSSRGLNNTSGVSEFCTDGSKSLSHIDYVRSLLGSHKEANLGGLDDDSIVRALECEDVSLRQWLDNPDRSVDAFECFHVFRQIVEIVNAAHSQGIVVHNVRPSCFVMSSFNNVSFIESASCSDSGSDEDATTKSREIGSSRQEEILSERRSKQQEEVKKQPFPMKQILAMEMSWYTSHEEDNGSLCNCASDIYRLGVLLFELFCPVSSREEKSRTMSSLRHRVLPPQILLNWPKEASFCLWLLHPEPSCRPSMSELLQSEFINEPRENLEEREAAMELRDRIEEQELLLEFLFLIQQRKQEAADKLQDTISLLSSDIDQVVKRQLVLQQKGRDVRSFLASRKRIRQGAETTAAEEENDDNSIDEESKLDDTLESTLLESSRLMRNLKKLESVYFATRYRQIKAATAAEKPLARYYSALSCNGRSSEKSSMSQPSKDPINDSRQGGWIDPFLEGLCKYLSFSKLRVKADLKQGDLLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIKDGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARNQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSETGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHHKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSISGINETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAFPMPVLSYKFKTIDPVSELEVDDASQFISSVCWRGQSSTLVAANSTGNIKILEMV", "text": "FUNCTION: Repressor of photomorphogenesis in the light. Probably part of the COP1/SPA E3 ubiquitin-protein ligase complex. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MPEQVTDQENQAPQQQTTAVHAYNPEVLQDMLPVYYRRLFPHLPFYRWLSYGSSEDAIFSNREISFTLQDDIYIRYLCFDTQAELEKEICSRNPIKIDIGPVMHSKPKNHRSIPGGLTPVQRELVFDIDMTDYDEVRTCCSGAGVCLKCWKFMVLAARVLDVALREDFGFEHIIWIFSGRRGIHCWVCDYQARHLDGRGRYAVAEYLNIITYASFAGGNSPRCSMGDRPHHSLKRALKIVEPMFEEIVLEDQNLFGTPKGVTKLLNMVHDDAARGELESYMQKNLEDGAHSRLVWESFIKYANSMRTSTTSAWSRKLKNIVAEIQLGLLYPRLDINVTRGFNHLLKAPFCIHPATGKVCVPFSVSAVAKFDPTTVPTITQLLHEINAFDDKSKSYMEAPEDKSRIKDHKKTSMFKGVVVFEEFLRKLERSQKSASLQF", "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) which play an essential role in the initiation of DNA synthesis (PubMed:6773966, PubMed:6806812, PubMed:6812052, PubMed:6403945, PubMed:6409898). 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 (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 (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 (By similarity). Can add both ribo- and deoxynucleotides during elongation of the primers (PubMed:6812052). Binds single stranded DNA (By similarity). SIMILARITY: Belongs to the eukaryotic-type primase small subunit family."}
+{"protein": "MDLPCQDWVCHVEQKWAELRSEETERFSLLTDIDAIFNYGLSLICPEDLNILSRISEKFSVKKSPETASEFRQQGNLSFKVKDYPAAVLHYSKGVCHADKNTDELSLCYANRSAALFYQGLYQACLEDIRRSLEAGYPSHLQDKLQTRQTACQNQLRKAEKPNIPHTDHQLSPCQKTVNSTGHLSDGVSVYFSSDKGRHMLVMENKPAGEVVLEDEAYCSVLIPANIFNTGTNKAVETFGTEDRHCHHCLSQSLSFVPCPKCSYARYCGESCQKDAWDQWHQWECPVGADLLAIGVLGHLALRVVLKAGQTEVQMGIKNTKDHVTTYKNDSPVQLSLGGDCGKSLDHTDCFHGSSYMGIYSLLPHVAQHSPASRFLMAITMAVIYGKLQGGPPPNKWMSFKDEGVKASWQPEMSMLGATALRHMMQLRCNAQAITAVRVKEESGMAVQSSSEIRIATAIFPVLSLLNHSCSPNTSISFTTGFQPDPHNQLGCSEGHFDHPKGSRSGVTVTVRASKDLTAGQEILHCYGPHRSRMEVKERQRLLLEQYFFQCVCQACQRDLSEGSPNAKEHTAPGMKCVKCGKPLQSHTDGYTCSWSSCGHQISSADVQNRLQGFQLLLDEAVHLMEQDRLNEALHILQSAFSQANSILTETHPFQGELADALARLYASTGEWSLAASHLKRSLVAIQAQFGEDSIELGRQLFKLAQLHFNGRDGVASLSVIPRARRLLSLHCSPRCEELQELSEMEHCLQGLL", "text": "FUNCTION: Plays a critical role in cardiac development (PubMed:30110327). Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1 (PubMed:30110327). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
+{"protein": "MWFMYLLSWLSLFIQVAFITLAVAAGLYYLAELIEEYTVATSRIIKYMIWFSTAVLIGLYVFERFPTSMIGVGLFTNLVYFGLLQTFPFIMLTSPNFILSCGLVVVNHYLACQFFAEEYYPFSEVLAYFTFCLWIIPFAFFVSLSAGENVLPSTMQPGDDVVSNYFTKGKRGKRLGILVVFSFIKEAILPSRQKIY", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SVP26 family."}
+{"protein": "MTKHTLEQLAADLRRAAEQGEAIAPLRDLIGIDHAEAAYAIQHINVQYDVVQGRRVVGRKVGLTHPKVQQQLGVDQPDFGTLFADMCYGDNEIIPFSRVLQPRIEAEIALVLNRDLPATDITFDELYNAIEWVLPALEVVGSRIRDWSIQFVDTVADNASCGVYVIGGPAQRPAGLDLKNCAMKMTRNNEEVSSGRGSECLGHPLNAAVWLARKMASLGEPLRAGDIILTGALGPMVAVNAGDRFEAHIEGIGSVAATFSSAAPKGSLS", "text": "FUNCTION: Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid. SIMILARITY: Belongs to the hydratase/decarboxylase family. MhpD subfamily."}
+{"protein": "MTQLETRTEPMVVNFGPHHPSMHGVLRLVVTLDGEDVVDCEPVIGYLHRGMEKIAENRTNVMFVPYVSRMDYAAGMFYEAIVVNAPEKLANIPVPKRASYIRVLMLELNRIANHLLWLGPFLADVGAQTPFFYIFREREMIYDLWEAATGQRLINNNYFRIGGVAADLPWGWLEKCRDFCDWFGPKIDEYEKLITNNPIFRRRIEGLGRIEKEDAINWSLSGPMLRASGVPWDLRKVDHYECYDDFDWQVAWEKEGDCYARYRVRIEEMRQSLKILRQACDMIPGGPTENLEAKRLNEGKGSDAAGFDFQYVAKKVAPTFKIPNGELYTRLESGKGEIGVFIQGNNDVTPWRFKIRAADSNNLQILPHILKGHKVADIMAILGSIDVIMGSVDR", "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 49 kDa subunit family."}
+{"protein": "MSFASTLYKTVFKRNSVFVGTVFASAFVFQAAFDTGVTSWYENHNKGKLWKDIKGGIMNGGEEDEEDDE", "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; Single-pass membrane protein. SIMILARITY: Belongs to the UQCR10/QCR9 family."}
+{"protein": "MPGFLVRILPLLLPLLLLGPTRGLRNATRRVFEIAYSQDRFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNTIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKEAILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPIITVQVENEYGSYFACDFDYLRFLQKRFHHHLGDDVVLFTTDGAHETFLQCGALQGLYTTVDFGPGSNITDAFQIQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEVVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNVIQKFEKVPEGPIPPSTPKFAYGKVSLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQYYGFVLYRTTLPQDCSNSTPLSSPFNGVHDRAYVAVDGIPQGVLERNRVITLNITGKTGATLDLLVENMGRVNYGAYINDFKGLVSNLTLDSNILTGWTIFPLDTEDAVRSHLGGWEHRDSGRHDEAWAHSSSNYTLPAFYVGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELERAPCSSDGPELCAVEFVDRPVIGSSQIYDHLSKPVEQRLMAPPPKKTKIRGWSMYDDESL", "text": "FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
+{"protein": "MLSFILIQNRQGKTRLAKWYVPYSDEEKIKLKGEIHRLVAPRDQKYQSNFVEFRNHKVVYRRYAGLFFCACVDTNDNELAYLEAIHFFVEVLDSFFGNVCELDLVFNFYKVYAILDEVFLAGEIEETSKQVVLTRLEHLDKLE", "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 (By similarity). SUBCELLULAR LOCATION: Cell membrane Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side Note=Component of the coat surrounding the cytoplasmic face of the plasma membrane coated vesicles. SIMILARITY: Belongs to the adaptor complexes small subunit family."}
+{"protein": "MIQALLVAICLAVFPYQGSSIILESGNVNDYEVVYPQKVPALSKGGVQNPQPETKYEDTMQYEFHVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSSPVQDHCYYHGYIQNEADSSAVISACDGLKGHFKHQGETYFIEPLELSDSEAHAIYKDENVEEEEEIPKICGVTQTTWESDEPIEKSSQLTNTPEQDRYLQAKKYIEFYVVVDNVMYRKYTGKLHVITRRVYEMVNALNTMYRRLNFHIALIGLEIWSNGNEINVQSDVQATLDLFGEWRENKLLPRKRNDNAQLLTSTEFNGTTTGLGYIGSLCSPKKSVAVVQDHSKSTSMVAITMAHQMGHNLGMNDDRASCTCGSNKCIMSTKYYESLSEFSSCSVQEHREYLLRDRPQCILNKPSRKAIVTPPVCGNYFVERGEECDCGSPEDCQNTCCDAATCKLQHEAQCDSGECCEKCKFKGAGAECRAAKNDCDFPELCTGRSAKCPKDSFQRNGHPCQNNQGYCYNGTCPTLTNQCATLWGPGAKMSPGLCFMLNWNARSCGLCRKENGRKILCAAKDVKCGRLFCKKKNSMICHCPPPSKDPNYGMVAPGTKCGVKKVCRNRQCVKV", "text": "FUNCTION: Snake venom zinc metalloproteinase that inhibits platelet aggregation by cleaving platelet glycoprotein Ib alpha (GP1BA) at Glu- 298/Asp-299, and abolishes binding of von Willebrand factor (VWF) to GPIBA. Cleaves P-selectin glycoprotein ligand-1 (PSGL-1/SELPLG) at Tyr- 51/Asp-52, and completely abolishes the binding of PSGL-1 to P- selectin. Anionic amino acid sequences containing sulfated tyrosines are needed for cleavages. Inhibits the thrombin-induced platelet aggregation, and the thrombin-induced release of ATP and ADP. Has lectin activity (inhibited by heparin). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily."}
+{"protein": "MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLPPQQEWINQPVRVNVKREYDHMNGSRESPVDCSVSKCNKLVGGGEANPMNYNSYMDEKNGPPPPNMTTNERRVIVPADPTLWTQEHVRQWLEWAIKEYGLMEIDTSFFQNMDGKELCKMNKEDFLRATSAYNTEVLLSHLSYLRESSLLAYNTTSHTDQSSRLNVKEDPSYDSVRRGAWNNNMNSGLNKSPLLGGSQTMGKNTEQRPQPDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSANASCITWEGTNGEFKMTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQPHPTETSMYKYPSDISYMPSYHAHQQKVNFVPSHPSSMPVTSSSFFGAASQYWTSPTAGIYPNPSVPRHPNTHVPSHLGSYY", "text": "FUNCTION: Sequence-specific transcriptional activator. Recognizes the DNA sequence 5'-C[CA]GGAAGT-3'. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family."}
+{"protein": "MIETLITFIIIFGIIVAIHEYGHLWWAKRSGILVREYAVGMGPKIFAHQAKDGTLYTIRILPLGGYVRLAGWGDDKTEIKKGQAASLVVSKSEVVNPEAENSVSNIVRRINLSEHVELEEAIPMLITEYDFEKELFIEGEVFGEIKRYSVDHDATIIEEDGTEVRIAPLDVQYQSAGVFHKMLTNFGGPLNNFILGIIAFIVLTFVQGGVPSTTNAIGQVEKGTPAYNAGLKAGDKIEAVNGTKTADWNNVVTEISGSKGKELKLEVSRSGKSETLSVTPKKMDGSYRVGIMQSMKTGFFDKITGGFVQAGQSATAIFKALGSLIARPSLDKLGGPVAIYQLSGQAARAGFPAIVYLLAMLSINLGIVNLFPIPVLDGGKIVLNIIEAIRGKALSQEKESIITMVGVVFMLVLFVAVTWNDILRAFVN", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family."}
+{"protein": "MGKNWLTCVSVACLSPGKDKKNQKPEKPKRKWSFGKQKSRESFDFPLEETPPVDPSPSSVHRPYPPPPPLPDFAPQPLLPPPSPPPPPPAYTINTRIYGESKESKNRQALALASAVAAEAAVVAAHAAAEVIRLTTPSTPQIEESKEETAAIKIQNAYRCYTARRTLRALRGMARLKSLLQGKYVKRQMNAMLSSMQTLTRLQTQIQERRNRLSAENKTRHRLIQQKGHQKENHQNLVTAGNFDSSNKSKEQIVARSVNRKEASVRRERALAYAYSHQQTWRNSSKLPHQTLMDTNTTDWGWSWLERWMASRPWDAESIDDQVSVKSSLKRENSIKSSPARSKTQKSASQSSIQWPVNNDTKSRKIEVTNRRHSIGGGSSENAKDDESVGSSSSRRNSLDNTQTVKSKVSVETTSNVSNAQTVKPKANVGAKRNLDNTKTLKSKSSVGTTGNLANTEAVKSKVNVGTTSMPKKEVVADKKKPPQMVLPKKRLSSSTSLGKTKKLSDSDKATTGVANGEKKRRNGGSS", "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, nucleolus. SIMILARITY: Belongs to the IQD family."}
+{"protein": "MVLVITEPIKSQSKTVCVIGAGPSGLVSARELKKEGHKVVVMEQNHDVGGQWLYQPNVDEEDTLGKTKTLKVHSSVYSSLRLASPREVMGFSDFPFIAKEGRDSRRFPGHEELLLYLKDFCQVFGLREMIRFNVRVEFVGMVNEDDDDDDDVKKWMVKSVKKSGEVMEEVFDAVVVASGHYSYPRLPTIKGMDLWKRKQLHSHIYRVPEPFCDEVVVVVGCSMSGQDISIELVEVAKEVHLSTKSLDIPPGLSKVIEKHQNLHLHPQIESLEEDGRVIFEDGSCIVADTILYCTGYEYKFPFLESKGRVEIDDNRVGPLFEHTFSPSLSPFLSFVGIPRKLIGFPFFESQAKWIAKLLSGKTSLPSSDQMMQSISDFYLAREADGIPKRNTHDIADFNYSDKYADYIGFPHLEEWRKVLCLSAILNSIENLETYRDSWDDDDLLQETLQDPYFTQLSIPSV", "text": "FUNCTION: Catalyzes the conversion of methylthioalkyl glucosinolates of any chain length into methylsulfinylalkyl glucosinolates. SIMILARITY: Belongs to the FMO family."}
+{"protein": "FLPILINLIHKGLL", "text": "FUNCTION: Antibacterial activity against Gram-positive bacterium S.aureus. Weak activity against Gram-negative bacterium E.coli and C.albicans. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily."}
+{"protein": "MADAAATAGAAGSGTRSGSKQSTNPADNYHLARRRTLQVVVSSLLTEAGFESAEKASVETLTEMLQSYISEIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNVDTLPAYAKRSQRMVITAPPVTNQPVTPKALTAGQNRPHPPHIPSHFPEFPDPHTYIKTPTYREPVSDYQVLREKAASQRRDVERALTRFMAKTGETQSLFKDDVSTFPLIAARPFTIPYLTALLPSELEMQQMEETDSSEQDEQTDTENLPLHISPDDSGAEKENTSVLQQNPSLSGSRNGEESIIDNPYLRPVKKPKIRRKKSLS", "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. The TFIID complex structure can be divided into 3 modules TFIID- A, TFIID-B, and TFIID-C. TAF8 is involved in forming the TFIID-B module, together with TAF5. Mediates both basal and activator-dependent transcription. Plays a role in the differentiation of preadipocyte fibroblasts to adipocytes, however, does not seem to play a role in differentiation of myoblasts. Required for the integration of TAF10 in the TAF complex (By similarity). May be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localized in the cytoplasm and transported from the cytoplasm to the nucleus in some cells, possibly depending on the functional or developmental state of the cell. SIMILARITY: Belongs to the TAF8 family."}
+{"protein": "MSSDIKIKVQSFGRFLSNMVMPNIGAFIAWGIITALFIPTGWLPNETLAKLVGPMITYLLPLLIGYTGGKLVGGERGGVVGAITTMGVIVGADMPMFLGSMIAGPLGGWCIKHFDRWVDGKIKSGFEMLVNNFSAGIIGMILAILAFLGIGPIVEALSKMLAAGVNFMVVHDMLPLASIFVEPAKILFLNNAINHGIFSPLGIQQSHELGKSIFFLIEANPGPGMGVLLAYMFFGRGSAKQSAGGAAIIHFLGGIHEIYFPYVLMNPRLILAVILGGMTGVFTLTILGGGLVSPASPGSILAVLAMTPKGAYFANIAGVCAAMAVSFVVSAILLKTSKVKEEDDIEAATRRMQDMKAESKGASPLSAGDVTNDLSHVRKIIVACDAGMGSSAMGAGVLRKKIQDAGLSQISVTNSAINNLPPDVDLVITHRDLTERAMRQVPQAQHISLTNFLDSGLYTSLTERLVAAQRHTANEEKVKDSLKDSFDDSSANLFKLGAENIFLGRKAATKEEAIRFAGEQLVKGGYVEPEYVQAMLDREKLTPTYLGESIAVPHGTVEAKDRVLKTGVVFCQYPEGVRFGEEEDDIARLVIGIAARNNEHIQVITSLTNALDDESVIERLAHTTSVDEVLELLAGRK", "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 D-mannitol transport (PubMed:368051, PubMed:6427236, PubMed:2123863). Also able to use D-mannonic acid (PubMed:6427236). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MGCIKSKRKDNLNDDEVDSKTQPVRNTDRTIYVRDPTSNKQQRPVPEFHLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLSSKREGFIPSNYVAKVNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDYDPMHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQSDGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEFMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMSALSQGYRMPRMENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP", "text": "FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-96'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (PubMed:28098138). Phosphorylates CLNK (PubMed:12681493). Phosphorylates BCAR1/CAS and NEDD9/HEF1 (By similarity). SUBCELLULAR LOCATION: Cell membrane Nucleus Cytoplasm Cytoplasm, perinuclear region Golgi apparatus Membrane; Lipid-anchor Note=Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain- dependent but kinase activity independent manner and is mediated by exocytic vesicular transport (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily."}
+{"protein": "MSSATSPIILKWDPKSLEIRTLTVESLLEPLVTQVTTLVNTSNKGPSGKKKGRSKKAHVLAASVEQATQNFLEKGEQIAKESQDLKEELISAVEDVRKQGDTMRITSSEFADDPCSSVKRGTMVRAARALLSAVTRLLILADMADVMRLLIHLKIVEEALESVKNATNEQDLAHRFKEFGKEMVKLNYVAARRQQELKDPHCRDEMAAARGALKKNATMLYTASQAFLRHPDVAATRANRDYVFKQVQEAIAGIANAAQATSPTDEKQAHTGIGELAAALNEFDNKIILDPLTFSEARFRPSLEEKLESIISGAALMADSSCTRDDRRERIVAECNSVRQALQDLLSEYMNNCRYGTWMDESCKSGRKEKGDPLNIAIDKMTKKTRDLRRQLRKAVMDHISDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLVEVANLACSISNNEEGVKLVRMAATQIDSLCPQVINAALTLAARPQSKVAQDNMDVFKDQWEKQVRVLTEAVDDITSVDDFLSVSENHILEDVNKCVIALQEGDVDTLDRTAGAIRGRAARVIHIINAEMENYEAGVYTEKVLDATKLLCETVMPRFAEQVEFAIEALSANIPQPFEENEFIDASRLVYDGVRDIRKAVLMIRTPEELEDDSDFEQEDYDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEEKAKIAEQVEIFHQEKSKLDAEVAKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVINAAKKIAEAGSRMDKLARAVADQCPDSACKQDLIAYLQRIALYCHQLNICSKVKAEVQNLGGELIVSGTAVQSTFTTFYEVAGDVIAGGRDSQLSLDLLPSCTEGSLFGSGSRDSTMLDSATSLIQAAKNLMNAVVLTVKASYVASTKYQKVYGTAAVNSPVVSWKMKAPEKKPLVKREKPEEYQTRVRRGSQKKHISPVQALSEFKAMDSF", "text": "FUNCTION: May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Cytoplasm, cytoskeleton Cell junction, adherens junction Cell projection, axon Nucleus. SIMILARITY: Belongs to the vinculin/alpha-catenin family."}
+{"protein": "MAQIREIDVGEVRTRFARGWHCLGLSRTFKDGKPHAVEAFGTKLVVWADSNGEPKVLDAYCRHMGGDLSQGEIKGDSVACPFHDWRWGGNGKCTDIPYARRVPPLARTRSWITMEKHGQLFVWNDPEGNTPPPEVTIPEIEQYGSDEWTDWTWNQIRIEGSNCREIIDNVVDMAHFFYIHYAFPTFFKNVFEGHIAEQYLNTRGRPDKGMATQYGLESTLESYAAYYGPSYMINPLKNNYGGYQTESVLINCHYPITHDSFMLQYGIIVKKPQGMSPEQSDVLAAKLTEGVGEGFLQDVEIWKNKTKIENPLLCEEDGPVYQLRRWYEQFYVDVADVTEKMTGRFEFEVDTAKANEAWEKEVAENLERKKREEEQGKQEAEV", "text": "FUNCTION: In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4- androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4- androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 23,24-bisnorcholesta-4-ene-22-oate and 23,24- bisnorcholesta-1,4-diene-22-oate."}
+{"protein": "MPAPVPALLCLALALASAQPSPPPPPPFPVVATNYGKLRGVRAALPGDVLGPVTQFLGVPYAAPPTGERRFQPPEPPSSWAGVRDATRFAPVCPQHLDERALLRDCLPAWFAANLDAIAAYVQDQSEDCLYLNLYVPGGANGKKMADDVTGNDHGDDQDSRDPGVGGAAAAAARKPVMVYIHGGSYMEGTANIVDGSVLASYGDVIVVTVNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWVEENAGAFGGDPDRVTVFGSGAGASCVSLLTLSHYSEGLFQKAIIQSGTALSSWAVNYQPARYARALGERVGCATPDPGSPPGSPPGWDSASLVSCLRGKAAGELARARVTPATYHVAFGPTVDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGARFVDGLGGGHDGGYGGYGGGYGGGVEDDEVQDGGPDGAAGGVSAGEFDLAVSGFINDLYGRPEGRGDALRETVKFMYTDWADRDSPEARRKTLVALFTDHQWVAPAVATADLHARYGSPTYFYAFYHRCHGGGGGGGGVDGVAGGVAGGVGGEEARPAWADAAHGDEVPYVFGVHMAGPGDVFGCNFSRNDVMLSAVVMTYWTNFAKTGDPNQPVAQDTRFVHTRPNRFEEVAWAKYDPRGQLYLHIGLRPRVRDHYRAAKVAFWLELVPHLHGLAADPGAYLSAAATRAAPSGDPDRDPGGGGGGRRRPRPATRRPAVMTSSSMASGSGMTSSSGSGMTSSSGSSASAVLIETRRDYSTELSVTIAVGASLLFLNVLAFAALYYKKDKRRHETHRRPPPPRPPQAPPSAAAADRNPRPDPGPAGRRGGECGAVVTAMAAEASAGGLGHDGVGGVGVGGVIGGVAGLRLACPPDYALTLRRSPDDVPRAGAGPGTMTLIPGALGGGGGGAVHGFNTFGSGVGVAGVAGVATSQAGPGLPHGHSTTRV", "text": "FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in the formation or maintenance of synaptic junctions via its interactions (via the extracellular domains) with neurexin family members. Plays a role in synaptic signal transmission. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Postsynaptic cell membrane. Note=Detected at glycinergic postsynapses in retina. Detected on dendritic spines on cultured neurons. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
+{"protein": "MLGAIHLGVLAACFVLFVPMAMAGWHLSRNKMLFFSGALFISLAVCVHLTPYFPSVSDIVASVSSVVVYDHRISCINEVNQIVWDVKPVPNPESVRRNNGSTKLDYFVKNWDWMKSRKVLSCEFQKLDKFDVSDLLNGSWVVVAGDSQARFVALSLLNLVLGSDSKAMDSVRGDLFRRHSDYSIVVKEIGMKLDFVWAPYEKDLDDLVVSYKKMKKYPDVVIMGTGLWHMLHVNNASDFGFRLRQLSSHVESLVPLTPKEQEGGGSVSGRSVHLFWIGMPVLINGMLNTDEKKEKMSDTVWHEYDRSLGESKILRQMGGPLILLDIQSFTWNCGPQCTLDGMHYDSAVYDAAVHVMLNALLIESHQSL", "text": "FUNCTION: Component of the plant cell wall polysaccharide acetylation pathway (PubMed:25681330, PubMed:30083810). Does not directly catalyze O-acetylation of xyloglucan but exhibits weak acetylesterase activity in vitro (PubMed:30083810). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass membrane protein."}
+{"protein": "MNIRKNSKSVSKRFKVTSNKLILYKPASKSHLQEKKTVSRKKRLCRVKRIKVVDSKSIKLRYMF", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
+{"protein": "MASGDGGDDAGVKRVADRYLKREVLGEGTYGVVFKAVDTKTGNTVAIKKIRLGKYKEGVNFTALREIKLLKELKDSNIIELIDAFPYKGNLHLVFEFMETDLEAVIRDRNIVLSPADTKSYIQMMLKGLAFCHKKWVLHRDMKPNNLLIGADGQLKLADFGLARIFGSPERNFTHQVFARWYRAPELLFGTKQYGSAVDIWAAGCIFAELLLRRPFLQGSSDIDQLGKIFAAFGTPKSSQWPDMVYLPDYVEYQFVSAPPLRSLFPMASDDALDLLSRMFTYDPKARITAQQALEHRYFLSVPAPTKPSQLPRPPPKGDSGNNKIPDLNLQDGPVVLSPPRKLRRVTAHEGMEVHMHRADRTEEHPSGARHMDDMSSQSSRIPMSVDVGAIFGTRPAPRPTLNSADKSRLKRKLDMDPEFGYTE", "text": "FUNCTION: CDK-activating kinase that may control G1/S phase progression. May control the rate of cell differentiation to accomplish proper development of organs, or in response to a changing environment. Forms a complex with cyclin CYCH1-1 that phosphorylates CDKA-1 and the C-terminal domain (CTD) of the large subunit of RNA polymerase II. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "MNVIDLFSGCGGFSKGFLDENFRILGAIENFKPVVKTYLYNIKAPVWMDDIKRIPPKAFDEFIKNEKVDVIIGSPPCEPFTKANKLIKDNPLDRLYKDKVGRLVLYYIDYVNYFTQRNDDLIFVMENVPQIKEIKDELKKLFGDIGHKVYFNILRAEDYGNPSKRARMFISNIKLKPKKVDKLVVVEEALKDIPKDAKNHEIKKLSKEKVEMISKLKWGEALYRYRGKKKLMFNWYKLHPKKLAPTVKGRSRFIHPYEDRLLTVREQARLMSYPDDFVFFGGRDVQYNQIGESVPPILGRAIAKEIKKQL", "text": "FUNCTION: A putative methylase that may protect DNA from cleavage by an unknown endonuclease. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family."}
+{"protein": "MRLFLAIDIPENIKEEIAKFQEQFKMKGIKLVEKENLHITVKFLGEVDEEKLKEILNLDLSIQPIKIKLKYIGTFPNSNYIRVIWIGAYNNNLVEIFKEIDEKLSNLGFKKEREYVPHLTIGRVKFIDNKKKLKDRIEKYKDVDFGEFEAKHIKLYKSTLTPNGPIYEVIKEW", "text": "FUNCTION: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'- phosphomonoester. SIMILARITY: Belongs to the 2H phosphoesterase superfamily. ThpR family."}
+{"protein": "MASGQEKGRSELDSLAREGQTVVPGGTGGKSYEAQEKLAEGRSRGGQTRKEQMGEEGYSEMGRKGGLSTNDESGGERAAREGIDIDESKFKTKS", "text": "FUNCTION: It is thought to provide protection for the cytoplasm during the desiccation stage of embryo development. SIMILARITY: Belongs to the small hydrophilic plant seed protein family."}
+{"protein": "MAVLLALFGALVLSGGLCVNQEERLIHHLFEERGYNKEVRPVASADEVVDVYLALTLSNLISLKEVDETLTTNVWVEQSWTDYRLQWNTSEFGGVDVLRLLPEMLWLPEIVLENNNDGLFEVAYYCNVLVYNTGYVYWLPPAIFRSACPINVNFFPFDWQNCTLKFSSLAYNAQEINMHLKEESDPETEKNYRVEWIIIDPEGFTENGEWEIIHRPARKNIHPSYPTESSEHQDITFYLIIKRKPLFYVINIVTPCVLIAFMAILVFYLPADSGEKMTLVISVLLAQSVFLLLVSQRLPATSHAIPLIGKYLLFIMLLVTAVVVICVVVLNFHFRTPSTHVMSDWVRGVFLEILPRLLHMSHPAESPAGAPCIRRCSSAGYIAKAEEYYSVKSRSELMFEKQSERHGLASRVTPARFAPAATSEEQLYDHLKPTLDEANFIVKHMREKNSYNEEKDNWNRVARTLDRLCLFLITPMLVVGTLWIFLMGIYNHPPPLPFSGDPFDYREENKRYI", "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."}
+{"protein": "MGDWSFLGRLLENAQEHSTVIGKVWLTVLFIFRILVLGAAAEEVWGDEQSDFTCNTQQPGCENVCYDKAFPISHIRFWVLQIIFVSTPTLIYLGHVLHIVRMEEKRKEKEEELKKRGSVKDNNYPGAATSGGGSGGGNNFKDPPIKMGKEKLPIRDERGRIRMGGALLRTYIFNIIFKTLFEVGFIVGQYFLYGFELKPVYQCSRPPCPHTVDCFISRPTEKTIFIIFMLVVASVSLLLNMLEIYHLGWKKLKQGMTSQYSLEMPVTTLTPVMVTGESKPVSLPPPAPPVVVTTTAPAPVLPDTRAVTPLLAPVTMAPYYAAAAPRTRPPSNTASMASYPVAPPVPENRHRAVTPTPVSTPVTIPTPIPTPTPAIINYFNSKSNALAAEQNWVNMAAEQQGKAPSSSAGSSTPSSVRHPLPEQEEPLEQLLPLPAGPPITTTNSGSSTSLSGASGSKWDVEGEEELAEERPISATCTTVEMHEPPLLVDTRRLSRASKSSSSRARSDDLAV", "text": "FUNCTION: Structural component of lens fiber gap junctions (PubMed:7678009). Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore (PubMed:7678009). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell junction, gap junction. SIMILARITY: Belongs to the connexin family."}
+{"protein": "MSSRPANNQGPPNLPARDKSLVQRFMAVAKSLQFAWFTGHSVVLISSILYLLKMSEFYYRSAYLGVIESFGIIIYQQFFTRNEPLQTQDAAATKASIKSRVAGLLKSEDVLYLVLANFWLFTPRFSFSLIPFFAFAVFHVLIYVEKVLLPKVFHLSSKDSSKILSFIDKFVVQYNDLCMHWVGTAELLIFILVLFRAILCFQRSWIILVVYAIFIKLRYENSKYMKAAFAQWRVRMDGIISHPSIPPFVKRAYNAIKMSLIRLSEYRLSGAPQVTKKQN", "text": "FUNCTION: Contributes to proper distribution and/or efficient assembly of nuclear pores. Required for normal pore density in the daughter nucleus during telophase. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus, nuclear pore complex. SIMILARITY: Belongs to the PER33/POM33 family."}
+{"protein": "MLIAWLVLAATLSRSIRASTTISIPITTQDIIAGDVFFEILSPSELEYTYRLRPAKDFGSAFSERLEGVPLVITDPPGACQEIRNARDLNGGVALIDRGECSFLTKTLRAEAAGALAAIITEYNPSSPEFEHYIEMIHDNSQQDANIPAGFLLGKNGVIIRSTLQRLKRVHALINIPVNLTFTPPSKINHPPWLGW", "text": "FUNCTION: May be involved in iversification of muscle cell fates. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MPMTLGYWDIRGLAHAIRLFLEYTDSSYEEKRYTMGDAPDYDQSQWLNEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLGRKHNLCGETEEERIRVDILENQLMDNRMVLARLCYNADFEKLKPGYLEQLPGMMRLYSEFLGKRPWFAGDKITFVDFIAYDVLERNQVFEAKCLDAFPNLKDFIARFEGLKKISDYMKTSRFLPRPMFTKMATWGSN", "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. Mu family."}
+{"protein": "MTFTKACSVDEVPPGEALQVSHDAQKVAIFNVDGEFFATQDQCTHGEWSLSEGGYLDGDVVECSLHMGKFCVRTGKVKSPPPCEPLKVYPIRIEGRDVLVDFSRAALHA", "text": "FUNCTION: This protein seems to be a 2Fe-2S ferredoxin. SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin component family."}
+{"protein": "MWRFFYTSLLLICQPLILCFIGLLSVKSPRYRQRLAERYGFYGNASCPPPQGIFIHAASVGEVIAATPLVRQLQQDYPHLSITFTTFTPTGSERVKATFGDSVFHYYLPLDLPFSIHRFINFVQPKLCIVMETELWPNLIHQLFLRNIPFVIANARLSARSAHRYGKIKAHLQTMWSQISLIAAQDNISGKRYATLGYPKEKLNITGNIKYDLNTNDELLRKIDSLRTLWKQDRPIWIAASTHNGEDEIILKSHRALLAKYPNLLLLLVPRHPERFNVVADLLKKEKFQFIRRSTNELPNENTQVILGDSMGELMLMYGISDIAFVGGSLVKHGGHNPLEPLAFKMPVITGKHTFNFPEIFRMLVEVQGVLEVNSTADALERAVEALLNSKESRERLGNAGYEVLMENRGALQRLLDLLKPYLERNV", "text": "FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'- bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the acceptor lipid. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 30 subfamily."}
+{"protein": "MEVDINGVNRTNNSVPSTAEGSSPSKPDPEKPRCSSTPCSPIRRTVSGYQILHMDANFLVGFTTGGELLKLAQKCATTEETPGESLPAFRSKQLESGLSRSSRIYKARGRQFQPYDIPAVNGRRRRRMPSSGDKCNKAVPYEPYKAAHGPLPLCLLKGKRAHSKSLDYLNLDKMNIKESADTEVLQYQLQHLTLRGDRVFARNNT", "text": "FUNCTION: May play a role in immune regulation through regulation of the macrophage function (By similarity). May also play a role in trafficking of proteins via its interaction with unc119 family cargo adapters (By similarity). May play a role in ciliary membrane localization (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium. SIMILARITY: Belongs to the UNC119-binding protein family."}
+{"protein": "MSRNLRTALIFGGFISLIGAAFYPIYFRPLMRLEEYKKEQAINRAGIVQEDVQPPGLKVWSDPFGRK", "text": "FUNCTION: [Phoenixin-14]: Peptide involved in a broad spectrum of regulatory functions (By similarity). Is a ligand for GPR173 (By similarity). 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 (By similarity). Plays a protective role in memory retention through activation of GNRHR (By similarity). Regulates the secretion of AVP by hypothalamic neurons (By similarity). 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 similarity). 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 similarity). It also plays a cardioprotective role during ischemia, where it activates the SAFE and RISK pathways (By similarity). Stimulates the proliferation and differentiation of preadipocytes (By similarity). In pancreatic islet cells, it induces proliferation of islet cells as well as the production of INS (By similarity). FUNCTION: [Phoenixin-14]: Peptide involved in a broad spectrum of regulatory functions (By similarity). Is a ligand for GPR173 (By similarity). 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 (By similarity). Plays a protective role in memory retention through activation of GNRHR (By similarity). Regulates the secretion of AVP by hypothalamic neurons (By similarity). 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 similarity). In the ovary, it regulates follicular growth by stimulating granulosa cell proliferation by increasing the expression of GPR173, CREB1, CYP19A1, KITLG, FSHR, and LHCGR (PubMed:30933929). It also increases the production of estradiol (E2) (PubMed:30933929). In the heart, it regulates contractility and relaxation (By similarity). It also plays a cardioprotective role during ischemia, where it activates the SAFE and RISK pathways (By similarity). Stimulates the proliferation and differentiation of preadipocytes (By similarity). In pancreatic islet cells, it induces proliferation of islet cells as well as the production of INS (By similarity). 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/COX1 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). FUNCTION: [Phoenixin-20]: Peptide involved in a broad spectrum of regulatory functions (By similarity). Is a ligand for GPR173 (By similarity). 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 (By similarity). Plays a protective role in memory retention through activation of GNRHR (By similarity). Regulates the secretion of AVP by hypothalamic neurons (By similarity). 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 similarity). 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 similarity). It also plays a cardioprotective role during ischemia, where it activates the SAFE and RISK pathways (By similarity). Stimulates the proliferation and differentiation of preadipocytes (By similarity). In pancreatic islet cells, it induces proliferation of islet cells as well as the production of INS (By similarity). 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 (PubMed:26321642). Promotes the progression of complex assembly after the association of MT-CO1/COX1 with COX4I1 and COX6C (PubMed:26321642). Chaperone-like assembly factor required to stabilize newly synthesized MT-CO1/COX1 and to prevent its premature turnover (PubMed:26321642). FUNCTION: [Phoenixin-20]: Peptide involved in a broad spectrum of regulatory functions (By similarity). Is a ligand for GPR173 (By similarity). 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 (By similarity). Plays a protective role in memory retention through activation of GNRHR (By similarity). Regulates the secretion of AVP by hypothalamic neurons (By similarity). 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 similarity). In the ovary, it regulates follicular growth by stimulating granulosa cell proliferation by increasing the expression of GPR173, CREB1, CYP19A1, KITLG, FSHR, and LHCGR (PubMed:30933929). It also increases the production of estradiol (E2) (PubMed:30933929). In the heart, it regulates contractility and relaxation (By similarity). It also plays a cardioprotective role during ischemia, where it activates the SAFE and RISK pathways (By similarity). Stimulates the proliferation and differentiation of preadipocytes (By similarity). In pancreatic islet cells, it induces proliferation of islet cells as well as the production of INS (By similarity). SUBCELLULAR LOCATION: [Phoenixin-20]: Secreted. SUBCELLULAR LOCATION: [Small integral membrane protein 20]: Mitochondrion inner membrane; Single- pass membrane protein. SUBCELLULAR LOCATION: [Phoenixin-14]: Secreted. SUBCELLULAR LOCATION: [Small integral membrane protein 20]: Mitochondrion inner membrane; Single-pass membrane protein."}
+{"protein": "MAGARRTMALVALVAVVAAAVVAERASAAVSCGDVTSSIAPCLSYVMGRESSPSSSCCSGVRTLNGKASSSADRRTACSCLKNMASSFRNLNMGNAASIPSKCGVSVAFPISTSVDCSKIN", "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. May possess an antifungal activity and protect the plant against pathogens. SIMILARITY: Belongs to the plant LTP family."}
+{"protein": "MTTETLVSGTTPVSDNANLKQHLTTPTQEGQTLRDSVEKALHNYFAHLEGQPVTDVYNMVLCEVEAPLLETVMNHVKGNQTKASELLGLNRGTLRKKLKQYDLL", "text": "SIMILARITY: Belongs to the transcriptional regulatory Fis family."}
+{"protein": "MALKPLNNIWIRRQQCPCGDWKCYIRLEEDESTITKSEIESTPTPTSQYDTVFTPYVGQIFTTDDEAFEYYSTFARKSGFSIRKARSTESQNLGVYRRDFVCYRSGFNQPRKKANVEHPRERKSVRCGCDGKLYLTKEVVDGVSHWYVSQFSNVHNHELLEDDQVRLLPAYRKIQQSDQERILLLSKAGFPVNRIVKLLELEKGVVSGQLPFIEKDVRNFVRACKKSVQENDAFMTEKRESDTLELLECCKGLAERDMDFVYDCTSDENQKVENIAWAYGDSVRGYSLFGDVVVFDTSYRSVPYGLLLGVFFGIDNNGKAMLLGCVLLQDESCRSFTWALQTFVRFMRGRHPQTILTDIDTGLKDAIGREMPNTNHVVFMSHIVSKLASWFSQTLGSHYEEFRAGFDMLCRAGNVDEFEQQWDLLVTRFGLVPDRHAALLYSCRASWLPCCIREHFVAQTMTSEFNLSIDSFLKRVVDGATCMQLLLEESALQVSAAASLAKQILPRFTYPSLKTCMPMEDHARGILTPYAFSVLQNEMVLSVQYAVAEMANGPFIVHHYKKMEGECCVIWNPENEEIQCSCKEFEHSGILCRHTLRVLTVKNCFHIPEQYFLLRWRQESPHVATENQNGQGIGDDSAQTFHSLTETLLTESMISKDRLDYANQELSLLIDRVRNTAPANCLYQP", "text": "SIMILARITY: Belongs to the FHY3/FAR1 family."}
+{"protein": "MLLWIVATLLIFSLPVSTALDYNDFSLQRIARAPHPSSALLVPYPRVGKRSNILNNNSESQNSVQKRLYMARVGKRAFFYTPRIGK", "text": "FUNCTION: Encodes at least three neuropeptides: two of the periviscerokinin family (APHPSSALLVPYPRV-amide and LYMARV-amide) and one pyrokinin (AFFYTPRI-amide). FUNCTION: [AFFYTPRI-amide]: Putative ligand for neuromedin U receptor homolog nmur-2."}
+{"protein": "MYRKALLVWLLVYGIMRCTVHSSPTALKYPALRLEDEVYDEDGNTLPDFAFDNNPIGIGNPASVFDDMYSFYYPAEKRHADDLLNKAYRNLLGQLSARKYLHTLMAKHLGAVSSSLEDDSEPLSKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRIKNKGRRVAYL", "text": "FUNCTION: Primary role of GRF is to release GH from the pituitary. FUNCTION: PACAP plays pivotal roles as a neurotransmitter and/or a neuromodulator. Stimulates adenylate cyclase in pituitary cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family."}
+{"protein": "MTSLPCPLPDRGASNVVFPDLAPALSVVAAYPLGLSPGTAASPDLSYSQSYGHPRSYSHPGPATPGDSYLPRQQQLVAPSQPFHRPAEHPQELEAESEKLALSLVPSQQQSLTRKLRKPRTIYSSLQLQHLNQRFQHTQYLALPERAQLAAQLGLTQTQVKIWFQNKRSKYKKLLKQSSGEPEEDFSGRPPSLSPHSPALPFIWGLPKADTLPSSGYDNSHFGAWYQHRSPDVLALPQMM", "text": "FUNCTION: May play a role in determining the production of hemoglobin S. May act as a repressor. During embryonic development, plays a role in palatogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the distal-less homeobox family."}
+{"protein": "MTNPLNSTAANRSNQPSSDGISDGQITNEEAESLINKKNCSGHKLKEVTDSDTFSDNGKDDSDTKKRFHYHQDQRRMSLTSIVAVESPSSSNAPSRKTIDLGHGSDLIYIQRFLPFQQSWTFFDYLDKHIPWTRPTIRVFGRSCLQPRDTCYVASSGLTALVYSGYRPTSYSWDDFPPLKEILDAIYKVLPGSRFNSLLLNRYKGASDYVAWHADDEKIYGPTPEIASVSFGCERDFVLKKKKDEESSQGKTGDSGPAKKRLKRSSREDQQSLTLKHGSLLVMRGYTQRDWIHSVPKRAKAEGTRINLTFRLVL", "text": "FUNCTION: Dioxygenase that repairs alkylated DNA containing 1- methyladenine and 1-ethenoadenine by oxidative demethylation. Accepts double-stranded and single-stranded substrates, with a preference for dsDNA over ssDNA. Confers resistance to methylating agents such as methylmethanesulphonate (MMS). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the alkB family."}
+{"protein": "MASIAEMQKPHAICIPYPAQGHINPMMQFAKLLHFKGFHISFVNNHYNHKRLQRSRGLSALEGLPDFHFYSIPDGLPPSNAEATQSIPGLCESIPKHSLEPFCDLIATLNGSDVPPVSCIISDGVMSFTLQAAERFGLPEVLFWTPSACGFLAYTHYRDLVDKEYIPLKDTNDLTNGYLETSLDWIPGMKNIRLKDFPSFIRTTDINDIMLNYFLIETEAIPKGVAIILNTFDALEKDSITPVLALNPQIYTIGPLHMMQQYVDHDERLKHIGSNLWKEDVSCINWLDTKKPNSVVYVNFGSITVMTKEQLIEFGWGLANSKKDFLWITRPDIVGGNEAMIPAEFIEETKERGMVTSWCSQEEVLKHPSIGVFLTHSGWNSTIESISNGVPMICWPFFAEQQTNCRYCCVEWEIGLEIDTDVKREEVEAQVREMMDGSKGKMMKNKALEWKKKAEEAVSIGGSSYLNFEKLVTDVLLRK", "text": "FUNCTION: May glycosylate diterpenes or flavonols in leaves. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MLRLLRHARRHSTSSSSSAAAAAVPLTSPAFAVFGANTGVGKTLVSAGLVASLLASPSPSPSTVAYLKPLQTGFPDDSDARFVFDRAPALLRRLRLAGGGASTRLVASNHTLFPSPAVDPLPERQDTVVNYGGEEGVEEKALVCRTVYAWREPVSPHLAAEREGMPVEDEEVRWLVDRWLAEEDGGGEVWKVLETAGGVASPGPSGTLQCDLYRSSRLPAVLVGDGRLGGISSTLSAYETLLLRGYDVGSVILEDRGLSNDRFLLSYLRKRVPVHVLPPIPEDPKDDLTDWFSESSSAFSSLKDSLQSFHSRRVQRLNSMQRKSKYLLWWPFTQHDLVPVDSVTVIDSRFGENFSAYKVKDKTIVPQFDACASWWTQGPDSNLQIELARDMGYAAARYGHVMFPENVHEPALRCAELLLGGVGKDWASRVYFSDNGSTAIEIALKMAFRKYACDHGIIVDSEKDIRSEGSVHFKVLALNGSYHGDTLGAMEAQAPSAYTSFLQQPWYSGRGLFLDPPTVYIKNKSANLSLPPSIMHDQLSSCDTCFSSLTEVFCKTRDTSSAANVYVSYISQQLSQYAMSNNSEHIAALIIEPVIQGAGGMHLIDPLFQRLLVKECKNRKIPVIFDEVFTGFWRLGVESASELLGCFPDISCYAKLMTGGIVPLAATLATEPIFEAFRSDSKLTALLHGHSYTAHPMGCTAAVKAIQWYKDPSTNSNIDLDRMKLKELWDSALVNHLSSLPNVKRVVSLGTLCAIELKAEGSDAGYASLYASSLIRQLREEDNIYARPLGNVIYLMCGPCTTQDSCTRQLAKVHRRLQKLN", "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) to form an ureido ring. FUNCTION: Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor (By similarity). FUNCTION: Bifunctional enzyme that catalyzes two different reactions involved in the biotin biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: In the C-terminal section; belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. SIMILARITY: In the N-terminal section; belongs to the dethiobiotin synthetase family."}
+{"protein": "PDKYRVVYTDYQRLELEKEFHYSRYITMNRKAELAKSLDLTERQIKIWFQNRRAKERKINKKKDVMVKEP", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Caudal homeobox family."}
+{"protein": "MLPFAPVEDPWDQEDMEVFGSTSSSEPQVVFTMKNAATVMREHERKEVNDLKMVDEPMEEGEPVSCRREELVKEVPITQHVKEGYEKADPAQFDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRAHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSEGVEEVKRHAFFASIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFVATSIAEEYKITPVTSSNVLPIVQINGNAAQFSEAYELKEDIGIGSYSVCKRCIHSASNVEFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVECLHSQGVVHRDLKPSNILYMDESAHPDSIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQLPRHQPNSDEPPQEAVAAPYSVLARNPNRHHPILEPVTASRLAQRRNMKKRTSTGL", "text": "FUNCTION: Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Predominantly cytosolic. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily."}
+{"protein": "MHAIQFVEKGRAVLAELPVADLPPGHALVRVKASGLCHTDIDVLHARYGDGAFPVIPGHEYAGEVAAVASDVTVFKAGDRVVVDPNLPCGTCASCRKGLTNLCSTLKAYGVSHNGGFAEFSVVRADHLHGIGSMPYHVAALAEPLACVVNGMQSAGIGESGVVPENALVFGAGPIGLLLALSLKSRGIATVTMADINESRLAFAQDLGLQTAVSGSEALSRQRKEFDFVADATGIAPVAEAMIPLVADGGTALFFGVCAPDARISVAPFEIFRRQLKLVGSHSLNRNIPQALAILETDGEVMARLVSHRLPLSEMLPFFTKKPSDPATMKVQFAAE", "text": "FUNCTION: Involved in D-altritol catabolism. Catalyzes the oxidation of D-altritol to D-tagatose. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "METDCNPMELSGVSGFEEEAELNGFEGTDMKDMRLEAEAVVNDVLFAVNTMFVSKTLRCADDVAYINVETRERNRYCLELTEAGLRVVGYAFDQVDDHLQTPYHETVYSLLDTLSPAYREAFGNALLQRLEALKREGQS", "text": "FUNCTION: A-kinase anchoring protein for GSK3B and PKA that regulates or facilitates their kinase activity towards their targets. The ternary complex enhances Wnt-induced signaling by facilitating the GSK3B- and PKA-induced phosphorylation of beta-catenin leading to beta-catenin degradation and stabilization respectively. Upon cAMP activation, the ternary complex contributes to neuroprotection against oxidative stress-induced apoptosis by facilitating the PKA-induced phosphorylation of DML1 and PKA-induced inactivation of GSK3B. During neurite outgrowth promotes neuron proliferation; while increases beta- catenin-induced transcriptional activity through GSK3B kinase activity inhibition, reduces N-cadherin level to promote cell cycle progression (By similarity). May play a role in cleft palate formation and is required for postnatal life through modulation of the activity of GSK3B during development (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the GSKIP family."}
+{"protein": "MSNKEEHVDETSASGVKEVSSIAARHDNGYAPSLITSTSGMDSFQSHALLNDPTLIEDYSDIINNRPTSGSKLTLGNEDSESMGGSVVVTPTSNKSSPFNSKLNILSNAAEKGHDVLRNRDDDKELEEENVEKHMHSNSKRDQRHYKENSSELPDSYDYSDSEFEDNLERRLQEIETDSVDSADKDEVHFSVNNTMNPDVDDFSDGLKYAISEDEDEEENYSDDDDFDRKFQDSGFQGEKDDLEEENDDYQPLSPPRELDPDKLYALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRITDGKIGFAPAEILETFPERLARLNCWKNENMSSQSVASSDSKDDSISSGNKNQSDAESIIPTPALNGYGKGNKSVSFNDVVGYADRFIDDAIEDTSLDSNDDGGEGNGQSYDDDVDNDKETKVTHRDEYTEAKLNFGKFQDDDTSDVVSDVSFSTSLNTPLNVKKVRRQDNKNESEPKTSSSKDREDDYNANRYVGQEKSEPVDSDYDTDLKKVFEAPRMPFANGMAKSDSQNSLSTIGEFSPSSSEWTNESPSTPIVEESSSIPSSRAIKDISQYIHAKSKIEETTNVENTEGQIQASLGSSGGMANQTDAEQPKEELEKHHSTPEEEKQSTLSLHSSSEEDFYMDEQRAVSSASINSSLSGSRALSNTNMSDPASKPNSLVQHLYAPVFDRMDVLMKQLDEIIRK", "text": "FUNCTION: Important for bud site selection. Seems to be a regulatory subunit of the BUD14-GLC7 type-I phosphatase complex. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex."}
+{"protein": "MERSQSQRHGGEQSWWGSAPQYQYMPFEHCTSYGLPSENGGLQHRPRKDMGPRHNAHPTQIYGHQKEQYSYKAQDGGMPKKMGSSSTMDSLDEDHYSKCQDCVHRLGRVLRRKLGEDWIFLVLLGLLMALVSWCMDYVSAKSLQAYKWTYAQMKPSLPLQYLAWVTFPLILILFSALFCQLISPQAVGSGIPEMKTILRGVVLKEYLTLKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSMFSGVYEQPYYYTDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKHKCLSQFLAKHRLLYPGIVTFVIASLTFPPGMGQFMAGELMPREAISTLFDNNTWVKHIGDPQSLGQSAVWLHPQVNVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPEGILFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKFTIFVEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDSMILLGSVERSELQSLLQRHLCAERRLKAAQDMARKLSELPYNGKAQLAGDWHPGGRPESFAFVDEDEDEDLSRKMELPLTPAPPPPSPPPPPSQFPIAPSNPEEPNGPLPSHKQPPEASDSADQRSSTFQRLLHCLLGKAHSKKKKITQDSTDLVDNMSPEEIEAWEREQLSQPVCFDCCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIEGHTKSGVQLRPPLASFRNTTSIRKTPGGPPPPAEGWNVPEDGDGAPGREVMVPTMPETPVPPPSPEAPSCLAPARAEGELEELEMVGSLEPEEELADILHGPSLRSTDEEDEDELIL", "text": "FUNCTION: Voltage-gated chloride channel (By similarity). Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction (Probable) (PubMed:8119941). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC- 1/CLCN1 subfamily."}
+{"protein": "MTLRRASGCRQLTLTIGLALTLGLLQWPIGDVRGQDGASPAQVLQELLTRYGDNASISVPQLRSLLVRLNGGQSEDHDSKTQPTRTNASKCLAADTLAVYGMSEQSRIDERGLQQICPTMIQQLDSQACKTQPNQESESSPRPTEAEVWGYGLLCVTVISLCSLVGASVVPFMRKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFDPMEDYYVPKSAVVFGGFYLFFFTEKILKMILKPKDTGGHGHGHSHFPAERYANSNGDLEDGVMEKLQNGEAGGAALPRAEADGRGVGEDDKMLSTGQTVQDTQSSGGGGTGGCYWLKGRAYSDIGTLAWMITLSDGLHNFIDGLAIGASFTASVFQGISTSVAILCEEFPHELGDFVILLNAGMSIQQALFFNFLSACCCYLGMGFGILAGNNFSPNWIFALAGGMFLYIALADMFPEMNEVSREEEEAGGSGFLLTFALQNAGLLTGFAIMLVLTIYSGQIQLG", "text": "FUNCTION: Broad-scope metal ion transporter with a preference for zinc uptake. Also mediates cellular uptake of nontransferrin-bound iron. 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 (PubMed:27231142). Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions (By similarity). 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": "MKLFIILATATLLIAATQATYPRDEGFDLGETQMSSKCMRQVKMNEPHLKKCNRYIAMDILDDKYAEALSRVEGEGCKSEESCMRGCCVAMKEMDDECVCEWMKMMVENQKGRIGERLIKEGVRDLKELPSKCGLSELECGSRGNRYFV", "text": "FUNCTION: Seed storage protein. SIMILARITY: Belongs to the 2S seed storage albumins family."}
+{"protein": "MVSFKAILTLSLIGAAFATPIEQRAAEPVEDSGAVANSPEGSGMDLGGTDPTADAIEERGLLVRNILRQLLNNKQSGLTIISSTSNAITWLSRPPRRGRSLREYPVFQQHHKVYNYNSRPKENPGPFRLIATKDSRHFCGIISHDGIGHNPNAGLFHLCK", "text": "FUNCTION: This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ribonuclease U2 family."}
+{"protein": "MFRTLTVVPLLALGLSLSACADLGQPTVRADLLDQTGKVTGTATFSPSPIGTRVSIEVSGLKAGPHGLHIHENPNCNPGPDAQGQTIPFGAAGGHFDPGASHNHDGPHARNDQGHGGDLPMITVGEDGKGRLNFDTNRLKMTGPTGVLGRSIVIHADADDYQTNPAGNSGGRERCGVFQAIN", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
+{"protein": "MKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSMWCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLTVSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMKNISNHLVIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDIRKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS", "text": "FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=In discrete nuclear foci upon DNA damage. According to PubMed:11077446, localized also in the cytoplasm. DNA damage induces its nuclear translocation. Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the HUS1 family."}
+{"protein": "MYKLKTRKAAAKRYKAVGNKKISRRKAFRSHLLQKKSTNRKRQLSQVVIASPGDTKKIYLMLPYL", "text": "SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
+{"protein": "MKKLTFLLLCVLCTLSLQAQKQFTLASPDGNLKTTITIGDRLTYDITCNGRQILTPSPISMTLDNGTVWGENAKLSGTSRKSVDEMIPSPFYRASELRNHYNGLTLRFKKDWNVEFRAYNDGIAYRFVNQGKKPFRVVTEVSDYCFPSDMTASVPYVKSGKDGDYNSQFFNSFENTYTTDKLSKLNKQRLMFLPLVVDAGDGVKVCITESDLENYPGLYLSASEGANRLSSMHAPYPKRTVQGGHNQLQMLVKEHEDYIAKVDKPRNFPWRIAVVTTTDKDLAATNLSYLLGAPSRMSDLSWIKPGKVAWDWWNDWNLDGVDFVTGVNNPTYKAYIDFASANGIEYVILDEGWAVNLQADLMQVVKEIDLKELVDYAASKNVGIILWAGYHAFERDMENVCRHYAEMGVKGFKVDFMDRDDQEMTAFNYRAAEMCAKYKLILDLHGTHKPAGLNRTYPNVLNFEGVNGLEQMKWSSPSVDQVKYDVMIPFIRQVSGPMDYTQGAMRNASKGNYYPCYSEPMSQGTRCRQLALYVVFESPFNMLCDTPSNYMREPESTAFIAEIPTVWDESIVLDGKMGEYIVTARRKGDVWYVGGITDWSARDIEVDCSFLGDKSYHATLFKDGVNAHRAGRDYKCESFPIKKDGKLKVHLAPGGGFALKIK", "text": "FUNCTION: Galactosidase that is able to hydrolyze the alpha-1,6 disaccharide melibiose and the synthetic p-nitrophenyl alpha- galactoside substrate (pNP-Gal), with retention of the anomeric configuration. Does not hydrolyze DNP-Glc or pNP-Glc. SIMILARITY: Belongs to the glycosyl hydrolase 97 family."}
+{"protein": "MQTAYWVVVMMMMVWVTAPVSEGGKLSDVIWGLVPDDLTPQIILQILNASRHAYRRVRPRGQICIWKVCPPLPQWIHPLVKR", "text": "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. SIMILARITY: Belongs to the conotoxin C superfamily. Consomatin family."}
+{"protein": "MTDTTTTTTTDANKLVLEKSANSSGLEVDLHPLVLINISDHFTRTKVQSNYQDNCRVIGVILGVQNGRNVEICNSFEMVYATVDKQLVLDIEYLRKKYEQLFPLYDLLGWYSTGSQVSKDDILLHKQISEHNESPLYLMLDTDSPKSKDLPVIIYESELHIVNDEPTTIFVKTPYKIQTGEAERIGVNHIAKVTPSGSEGSGLTSHLFTMHNAISMLNIRVKALSDYLQAVKEKRLPYEQNILRKASSLCNQLPTIDTHDFKKSYLQEYNDVLLVTYLASITKTSASLNDTIDKYLVSNEKQSKRRFYQ", "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 E3 ligase complexes, leading to modify the Ubl ligase activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasmic vesicle, phagosome. SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily."}
+{"protein": "VTCFCKRPVCDSGETQIGYCRLGNTFYRLCCRQ", "text": "FUNCTION: Bactericidal activity, greater against Gram-positive bacteria. Low anti-fungi activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MAGDVEGFCSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQDKIHLKGLTATGFSHVLQFMYYGTIELSMNTVHEILQAAMYVQLIEVVKFCCSFLLAKICLENCAEIMRLLDDFGVNIEGVREKLDTFLLDNFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIELYEAVQSWLRHDRRRWRHTDTIIQNIRFCLMTPTSVFEKVKTSEFYRYSRQLRYEVDQALNYFQNVHQQPLLDMKSSRIRSAKPQTTVFRGMIGHSMVNSKILLLKKPRVWWELEGPQVPLRPDCLAIVNNFVFLLGGEELGPDGEFHASSKVFRYDPRQNSWLQMADMSVPRSEFAVGVIGKFIYAVAGRTRDETFYSTERYDITNDKWEFVDPYPVNKYGHEGTVLNNKLFITGGITSSSTSKQVCVFDPSKEGTIEQRTRRTQVVTNCWENKSKMNYARCFHKMISYNGKLYVFGGVCVILRASFESQGCPSTEVYNPETDQWTILASMPIGRSGHGVTVLDKQIMVLGGLCYNGHYSDSILTFDPDENKWKEDEYPRMPCKLDGLQVCNLHFPDYVLDEVRRCN", "text": "FUNCTION: Substrate-specific adapter for CUL3 E3 ubiquitin-protein ligase complex (PubMed:27561354, PubMed:14528312, PubMed:35219381). Acts as an adapter for CUL3 to target the serine/threonine-protein phosphatase 2A (PP2A) subunit PPP2R5B for ubiquitination and subsequent proteasomal degradation, thus promoting exchange with other regulatory subunits (PubMed:23135275). Acts as an adapter for CUL3 to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation (PubMed:27561354, PubMed:35219381). Through the regulation of RBBP8/CtIP protein turnover, plays a key 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) (PubMed:27561354, PubMed:35219381). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MEFQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKALCAEFKMKMKPDIVCIPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQDSIEPVPGQKGKKKAVEQRDFIGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIRFHTGLVDAHLYCLKKYIVDFLMENGSITSIRSELIPYLVRKQFSSASSQQGQEEKEEDLKKKELKSLDIYSFIKEANTLNLAPYDACWNACRGDRWEDLSRSQVRCYVHIMKEGLCSRVSTLGLYMEANRQVPKLLSALCPEEPPVHSSAQIVSKHLVGVDSLIGPETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKAKRVNEVIVGNDQLMEI", "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": "MAAGTSNYWEDLRKQARQLENELDLKLVSFSKLCTSYSHSGSRDGGRDRYSSDTTPLLNGSSQDRMFETMAIEIEQLLARLTGVNDKMAEYTHSAGVPSLNAALMHTLQRHRDILQDYTHEFHKTKANFTAIRERENLMGSVRKDIESYKSGSGVNNRRTELFLKEHDHLRNSDRLIEETISIAMATKENMTSQRGMLKSIHSKMNTLANRFPAVNSLIQRINLRKRRDSLILGGVIGICTILLLLYAFH", "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 (By similarity). 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. SIMILARITY: Belongs to the GOSR1 family."}
+{"protein": "MEESPLSRAPSRGGVNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRDYHTFVWSSVPESTADGSPIHTSVQFQASYLPKPGAQLYQFRYVNRQGRVCGQSPPFQFREPRPMDELVTLEEADGSSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHRLNLDLKEAKSWQKEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELATSSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNHVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEATAGLSCPAALTDSEDESPEDMRLPPYGLCEHGDPGSSPAGPREASPLVVISQPAPISPHLSGPAEDSSSDSEAEDEKSVLMAAVQSGGEEANLLLPELGNAFYDMASGFTVGPLSETSTGGPATPTWKECPICKERFPAESDKDALEDHMDGHFFFSTQDPFTFE", "text": "FUNCTION: Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N- terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER- activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions. In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma- globin promoter during erythroid differentiation of K562 erythroleukemia cells (By similarity). FUNCTION: Seems to enhance inorganic pyrophosphatase thus activating phosphogluomutase (PMG). Probably functions as component of the calphoglin complex, which is involved in linking cellular metabolism (phosphate and glucose metabolism) with other core functions including protein synthesis and degradation, calcium signaling and cell growth (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between nucleus and cytoplasm. SIMILARITY: Belongs to the CALCOCO family."}
+{"protein": "MVKEKKKADKKGEKSARSPSSLSDNLDFSKQDGNTTRQEMSPAGVPLLGMQLNEVKPKKDRQNVQQNEDASQYEESILTKLIVESYEGEKVRGLYEGEGFAAFQGGCTYRGMFSEGLMHGQGTYIWADGLKYEGDFVKNVPMNHGVYTWPDGSMYEGEVVNGMRNGFGMFKCSTQPVSYIGHWCNGKRHGKGSIYYNQEGTCWYEGDWVQNIKKGWGIRCYKSGNIYEGQWEDNMRHGEGRMRWLTTNEEYTGRWERGIQNGFGTHTWFLKRIRSSQYPLRNEYIGEFVNGYRHGRGKFYYASGAMYDGEWVSNKKHGMGRLTFKNGRVYEGAFSNDHIAGFPDLEVEFISCLDLSSGVAPRLSRSAELIRKLDGSESHSVLGSSIELDLNLLLDMYPETVQPEEKKQVEYAVLRNITELRRIYSFYSSLGCGHSLDNTFLMTKLHFWRFLKDCKFHHHKLTLADMDRILSANNDIPVEEIHSPFTTILLRTFLNYLLHLAYHIYHEEFQKRSPSLFLCFTKLMTENIRPNACQIKGNLFREQQRTLYSMSYMNKCWEIYLAYCRPSAAPPHEPTMKMRHFLWMLKDFKMINKELTAATFMEVIAEDNRFIYDGIDSNFEPELVFLEFFEALLSFAFICVTDQMTKSYTNVPADDVSGNKHETIYTILNQDAQNKSPSAVMSHESDAAHSDSARSSSSKLELSPDVNKIRKSEPKIKKSVSHERVSKMNFKLTGKGITFFSSESKKYERPKDDREEEFNTWVNNTYVFFVNTLFHAYKREEAIKEKIRADRLRSTAQAQQRKMEDDELEARLNIFILREEEAKRHDYEVDITVLKEPADVSSSHLILDPPKEDVTVSPSSKTITSKKKKK", "text": "FUNCTION: May function as part of the axonemal radial spoke complex 3 (RS3). Radial spoke complexes are important for ciliary motility. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme."}
+{"protein": "MDSPSSVSSYSSSSLSPSFSTSSVNSDFSFPSDNEREGKGTHELRPDTVGQRGGSRPSPGPIRCRHRPRVSSNQHTAPHLEQQGSEVKRSRDGEQETSLNTQGCTTEGDLLFAQKCKELQGFIRPLTDLLNGLKMGRFDRGLSSFQQSVAMDRIQRIVGVLQKPQMGERYLGTLLQVEGMLKTWFPHIAAQKSSSGGSRHQISKHFPSHHGDPGAASPAPLLEKMGQTQLGHLVLKPKQPWHLTGWPAMNLTWIHSTPICNPPLSSQGSASGHSPIGTGASIGVILVLQKGGQPFTHSAPGTPVPPTPLSPVVPGDLKKLPGEEPRCHSLPVTLPSDWSCILCPPVLPTTDREMTKGHPEPQMTSHPPVAPDPQP", "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. SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Co-localizes with the CLOCK-BMAL1 heterodimer in the PML body."}
+{"protein": "MEPPKAIVKKPRLVKLGPVDPGVRRGRGFSLGELAEAGLDAKKARKLGLHVDTRRRTVHPWNVEALKKYIERLREAGVEV", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family."}
+{"protein": "MVSFRFPFSFSQPPRATTSFSGFSISAVAVSVTVGAAAAGAAIAASRNPSHPILEWAFSSHRSSLSPWGSITLADESVVEPKTGFSFPASIGDSRRLLGVGLRKKSLLGLKNIDVYAFGVYADCDDVKKLVGDKYANLPASEIRGNKSFMDDLMEADIKMTIRLQIVYGKLNIRSVRNAFQESVGNRLKKFGGSDNDELLQSFTSLFKDEYKIPRNSTIDLTKDPGHVLSVAIEGNHVGSVKSHLLCRSILDLYIGEEPFDKNAREDFLDNAASLAFDN", "text": "FUNCTION: Fatty-acid-binding protein. Interacts preferentially with saturated fatty acid. May be involved in alpha-linolenic (C18:3) metabolism. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the chalcone isomerase family."}
+{"protein": "MVSIEDVYHTAELAKIEITEEQAEKFRKEFETILDYFNILDEVEEDVEPTFHVLPLTNVFREDEPGECLKQEEALSNAKHKEEGYFKGPRVVE", "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": "MLPPPPRQPPPQARAARGAVRLQRPFLRSPLGVLRLLQLLAGAAFWITIATSKYQGPVHFALFVSVLFWLLTLGLYFLTLLGKHELVPVLGSRWLMVNVAHDVLAAALYGAATGIMSDQMQRHSYCNLKDYPLPCAYHAFLAAAVCGGVCHGLYLLSALYGCGRRCQGKQEVA", "text": "FUNCTION: Microtubule-associated protein that exhibits cell cycle- dependent localization and can inhibit cell proliferation and migration. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasm, cytoskeleton Nucleus Note=Observed in the nucleus and at the perinuclear region during interphase, but localizes at the mitotic spindle and midbody at metaphase. A significant fraction of MARVELD1 translocates to the plasma membrane during anaphase or upon microtubule depolymerization (By similarity)."}
+{"protein": "MKLISFTGLALLLIVSLIDVEAQNEGACIPHGSVCTTNHAGCCSKLSCDCYRRFEKGVEKGQICWCIETGVTFSKE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 07 (U7-Lctx) subfamily."}
+{"protein": "MSFLNIFTFFSVLVSVATAVRFDLTNVTCNNLHGPHCGTYVMEVVGQNGTFLGQSTFAGADVLTESAGDAWARYLGQETRFLPKLTTIASNDTKNFSPLIFTTNIYTCNPQSFGDAMVPFANTVTGEIEYNSWADTADNASFITGLANQLFNSTQYGVQVASCYPNFASVILSTPTVNIFAANETLPDYCTAIQLKAVCPPDAGFA", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the VEL1 family."}
+{"protein": "MSTLGHQYDNSLVSNAFGFLRLPLNFQPYDSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLSAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRTEFDKDNGFTVLDACQVNDRGVDDIIAQVNQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYIQAAKKGE", "text": "FUNCTION: Catalyzes the formation of putrescine from agmatine. SIMILARITY: Belongs to the arginase family. Agmatinase subfamily."}
+{"protein": "MKKWLVTIAALWLAGCSSGEINKNYYQLPVVQSGTQSTASQGNRLLWVEQVTVPDYLAGNGVVYQTSDVKYVIANNNLWASPLDQQLRNTLVANLSTQLPGWVVASQPLGSAQDTLNVTVTEFNGRYDGKVIVSGEWLLNHQGQLIKRPFRLEGVQTQDGYDEMVKVLAGVWSQEAASIAQEIKRLP", "text": "FUNCTION: Component of a transport pathway that contributes to membrane integrity. FUNCTION: Component of a transport pathway that contributes to membrane integrity. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side."}
+{"protein": "MTAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQDHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFEHLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLSTCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKAAAQCYIDLIIKESDNNVKLIVLDRLIELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDNNEAAAADVLEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEIRRSLGEIPIVESEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATTLTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDIFNKECRQSLSHMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNTQRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVEKPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEFRQMWAEFEWENKVTVNTNMVDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVSIEKPIHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSI", "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. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Cell membrane Endoplasmic reticulum-Golgi intermediate compartment 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). Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (By similarity). Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack (By similarity). Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae (By similarity). Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (By similarity). Some association with high-density and low-density microsomes and mitochondria/nuclei fraction (By similarity). Very little found in plasma membrane fraction (PubMed:20362547)."}
+{"protein": "GRDGYIAQPENCVYHCFPGSSGCDTLCKEKGATSGHCGFLPGSGVACWCDNLPNKVPIVVGGEKCH", "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. As it competes neither with the classical alpha-toxin AaH2 nor the beta-toxin Css2, this toxin is an alpha-like toxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
+{"protein": "MNTFPKLNTIRNELKSVLDSDVIPLELTSLNRNRSIAKNPFLFEVTLNNTGQKNNGIEAFDPVTNQLPINLGSINSLNTGQILLEWTGLDINVTGTISSINDNEIIITFTSAFNNQYNYYRGLISVFSTGTWAHIIEYVFLGNNLGLFRFENLPSTLPTIGSSVTITFNGLLTSSGSNIFSVFIPKTMEHNALSGLLLYNETLNENKMISTYSSQRAEALISSGPVPTWTNAHTYSVRKEVPFVSSVSAAPPPTSTTVSLTPIPVGTGSPGDFIRNRSTGEIVTIVTIDNTTGAVTFSPSVNPVWVAGQTLEILTFNRDNFNYVTYSSLQREAPTGEYEATLISLNLPKERLDIDFPIEKMPFVYLEVRDTFNPSTNSFMSNNPGSKKALFKATLKSNKTDDKPFVKFSGDRAIRTLKFRPSAANFIFSILGPNGNPLMLWRQDTSSPYPPNRLLQTEAFLNIRKVSNSKYA", "text": "SIMILARITY: Belongs to the IIV-6 198R family."}
+{"protein": "MAMTPQLAFSRMPPGFRFQPTDEQLVVDYLQRRTAAQPCVTPDITDIDVYNVDPWQLPAMAMYGSDHDRYFFTMAAREAQARRTTPSGFWKPTGTKKTIFVVAGGHEVPTAVKRRFVFYLGHHQPSGSNNNNKTSWIMHEYRLMNSPRAAVPSSSSVNRLPTDDLTEEMVLCRISNKDLPKPPFIHNSLLQFSSVGLNGDGYNYLILDHLEPPAMEYPNVGIGNVDDAAAGTDDPGDLDEEIDDSMQRNHGG", "text": "FUNCTION: Transcription factor involved in the regulation of seed size (By similarity). Binds to DNA-specific sequences of CLPD1 and OAT promoters in vitro (PubMed:18813954). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MESYIQNLFAERIGGKSFGKEDVIYKFEKIKRAKQAAKLKYPDMELIDMGVGEPDEMADESVVEVLCEEAKKHVNRGYSDNGVQALKDEIPIYLEKIFGVKDLDPVNEVVHSIGSKPALAYITSVFINPGDVTLMTVPGYPVTATHTKWYGGSVETLPLLEKNNFLPELDAISKEVRENAKILYLNYPNNPTGAQATKKFYKEAVDFAFENDLIVIQDAAYAALTYGDKPLSFLSVKDAKEVGVEIHSFSKAYNMTGWRLAFVAGNELIVRGFAAVKDNYDSGQFIPIQKAGIHCLRHPEITEKTRAKYERRLSKMVKILKEAGFNAKMPGGTFYLYVKAPIGTKDGAKFANAEEFSQFMIKEKLISTVPWDDAGNFVRMAACFEAFKDGEISIEEEDRILNEVKRRLTEVEFVFE", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MQRICPAHCSVTHSLTMKSMRLSYIPPAASAAPQSPSYGRKKNASAAPPSAAASTTVLTSPLVTTTRTPKQTEQEDEQLVAKTKTTRTVIATTNGRAAPSQSRPRRRPAPAAAASAASLPMTFCNALEEVINTFIDPPALRPAVDPRNVLTSNFVPVDELPPTPCPVVRGAIPRCLAGGAYIRNGPNPQHLPRGPHHLFDGDGMLHSLLLPSPASSGDDPVLCSRYVQTYKYLVERDAGAPVLPNVFSGFHGVAGMARGAVVAARVLTGQMNPLEGVGLANTSLAYFAGRLYALGESDLPYAVRVHPDTGEVTTHGRCDFGGRLVMGMTAHPKKDPVTGELFAFRYGPVPPFVTYFRFDPAGNKGADVPIFSVQQPSFLHDFAITERYAIFPEIQIVMKPMDMVVGGGSPVGSDPGKVPRLGVIPRYATDESEMRWFEVPGFNIMHSVNAWEEAGGEELVLVAPNVLSIEHALEHMELVHSCVEKVRINLRTGVVTRTPLAAGNFDFPVINPAFLGRRNRYGYFGVGDPAPKIGGVAKLDFDRAGEGDCTVAQRDFGPGCFAGEPFFVADDVEGNGNEDDGYLVCYVHDEATGENRFVVMDARSPDLEIVAEVQLPGRVPYGFHGLFVTQAELQSQHQ", "text": "FUNCTION: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the carotenoid oxygenase family."}
+{"protein": "MPTQLEMAMDTMIRIFHRYSGKERKRFKLSKGELKLLLQRELTEFLSCQKETQLVDKIVQDLDANKDNEVDFNEFVVMVAALTVACNDYFVEQLKKKGK", "text": "SIMILARITY: Belongs to the S-100 family."}
+{"protein": "MPANSWPDNDSYKELDPLNSLLSDVSTTEESVVETRDLSLPSRFQGRRGKAALVLTIVWSGTIALHLVSWGSIFILGLTTVLGIHALGVVFARPRHYQKEIQGSLPFVSILVAAKNEEAVIAKLAKNLCNLEYPNGQYEVWIIDDNSTDKTPHILAELAKEYDKLKVLRRSAQATGGKSGALNQVLPLTQGEIIAVFDADAQVASDMLLHVVPLFQREKVGAVQVRKAIANAKENFWTKGQMAEMSLDIWFQQQRTALGGIGELRGNGQFVRRQALDSCGGWNEETITDDLDLTFRLHLDKWDIECLFYPAVQEEGVTTAIALWHQRNRWAEGGYQRYLDYWDLILKNRMGTRKTWDMLMFMLTMYILPTAAIPDLLMALTRHRPPMLGPVTGLSVTMSVVGMFAGLRRIRQEQKFQVHTPFVLLLQTMRGTLYMLHWLVVMSSTTARMSFRPKRLKWVKTVHTGTGE", "text": "FUNCTION: Glucosyltransferase involved in the biosynthesis of the non- bilayer-forming membrane lipid beta-monoglucosyldiacylglycerol which contributes to regulate the properties and stability of the membrane. Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding beta-glucosyl- DAG (1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor. Two types of DAG (dipalmitoyl-DAG (DPDAG) and 1-oleoyl-2-palmitoyl-DAG (OPDAG)) can be used as sugar acceptors, but OPDAG is preferred. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
+{"protein": "MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSLQKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQPSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWGSALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPEDEGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTTHNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFETIRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIEAWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCLA", "text": "FUNCTION: Calcium-independent phospholipase, lysophospholipase and O- acyltransferase involved in phospholipid remodeling with implications in endoplasmic reticulum membrane homeostasis and lipid droplet biogenesis (PubMed:19501189, PubMed:9705332, PubMed:10085124, PubMed:10358058, PubMed:28336330). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids with choline and ethanolamine head groups, producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:19501189, PubMed:9705332, PubMed:10085124, PubMed:10358058, PubMed:28336330). Transfers the sn-1 fatty acyl from one lysophospholipid molecule to the sn-2 position of another lysophospholipid to form diacyl, alkylacyl and alkenylacyl glycerophospholipids. Cleaves ester bonds but not alkyl or alkenyl ether bonds at sn-1 position of lysophospholipids (PubMed:19501189, PubMed:15944408). Catalyzes sn-2 fatty acyl transfer from phospholipids to the sn-2 position of 1-O-alkyl or 1-O-alkenyl lysophospholipids with lower efficiency (PubMed:19501189, PubMed:15944408). In response to dietary fatty acids, may play a role in the formation of nascent lipid droplets from the endoplasmic reticulum likely by regulating the phospholipid composition of these organelles (PubMed:28336330). FUNCTION: (Microbial infection) May facilitate human T-lymphotropic virus type 1 (HTLV-1) infection by promoting leukotriene B4 (LTB4) biosynthesis. LTB4 acts as a chemoattractant for HTLV-1-infected CD4- positive T cells and favors cell to cell viral transmission. FUNCTION: (Microbial infection) May play a role in replication and assembly of human hepatitis C virus (HCV) (PubMed:23015700, PubMed:28336330). In response to HCV infection, promotes remodeling of host endoplasmic reticulum membranes to form organelle-like structures called membranous web, where HCV replication occur (PubMed:23015700). Can further mediate translocation of replication complexes to lipid droplets to enable virion assembly (PubMed:23015700, PubMed:28336330). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Endoplasmic reticulum membrane; Lipid-anchor. Mitochondrion membrane; Lipid- anchor. Lipid droplet Note=Translocates from endoplasmic reticulum to lipid droplets in response to oleate."}
+{"protein": "MTISSAHPETEPKWWKEATIYQIYPASFKDSNNDGWGDMKGIASKLEYIKELGADAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEGKPIPPNNWRSYFGGSAWTFDEKTQEFYLRLFCSTQPDLNWENEDCRKAIYESAVGYWLDHGVDGFRIDVGSLYSKVAGLPDAPVIDENSKWQPSDPFTMNGPRIHEFHQEMNKFIRNRVKDGREIMTVGEMQHATDETKRLYTSASRHELSELFNFSHTDVGTSPKFRQNLIPYELKDWKVALAELFRYVNGTDCWSTIYLENHDQPRSITRFGDDSPKNRVISGKLLSVLLVSLSGTLYVYQGQELGEINFKNWPIEKYEDVEVRNNYDAIKEEHGENSKEMKRFLEAIALISRDHARTPMQWSREEPNAGFSGPNAKPWFYLNESFREGINAEDESKDPNSVLNFWKEALRFRKAHKDITVYGYDFEFIDLDNKKLFSFTKKYDNKTLFAALNFSSDSIDFTIPNNSSSFKLEFGNYPRSEVDASSRTLKPWEGRIYISE", "text": "FUNCTION: Alpha-glucosidase with specificity for isomaltase, methyl- alpha-glucoside, and palatinose. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MKLSCLLLTLAIIFVLTIVHAPNVKAKALADPESDAVGFADAVGEADPFDITKLNIKKLTKATCKVISKGASMCKVLFDKKKQE", "text": "FUNCTION: Shows activity against E.coli and S.aureus (MIC<6.25 uM), moderate activity against P.aeruginosa (MIC<25 uM), weak activity against B.subtilis (MIC<50 uM), and has no effect against L.garvieae, C.albicans, and S.cerevisiae. Has no hemolytic nor cytolytic activity. Causes an IgE-independent histamine release. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily. Ant pilosulin family."}
+{"protein": "MATRDLPHSVGDFCFGWVDQIRSEITLGKSQDQLIKEDVLEDDETVETKVEIKNLWPAFASGAGLFSDGYVNAGISTVLSCLKKIYGDEFTKSNAMNNIGSIGFVGTVVGQLSFGYISDNFDRKTGMLTANVMLIFFTLMCAVASWGTTVQGFFACLTVWRFFLGIAIGAEYPTSSVIASEFANQLPSGHRNRYFSWFTNAMIDFGFVVSSFVPLVLLWIFTPRHLRAVWRLSIGLGVIPPLILFFIRLKMDNSKSFKKMNMKRVNYSKYPWWLIIKFYWFRLTVVSLIWFIYDFSVYSFGTFNTIIIGEVIPNGTLYENWGWSVVFNLFYMPGAFLGAFIGDYLGPRLTLAIGVGAQGIIGIAMSACLKSLKKHVAGFVVVFGIFSTFGEFGPGNNTGLLASKTCASSIRGQYYGIAAAIGKIGAFVGTWVFPAIQKHYAYSEDLSLQVPFYVSSALCLFSAFLTIFFVPPVGQDAINKEDRLFKEYLEENGVDIRLLGDSGVVTQYQEDEDIGVISDEKDDTVKVQQKNV", "text": "FUNCTION: Glycerophosphodiester transporter that mediates uptake of glycerophosphocholine (GroPCho) with GIT3 (PubMed:24114876). Does not possess detectable glycerophosphoinositol (GroPIns) transport activity (PubMed:24114876). The expanded ability to utilize GroPIns and GroPCho results from the organism's pathogenic nature and its need to occupy a variety of environments within its host organism (PubMed:24114876). This possibility is buttressed by the fact that GroPIns and GroPCho are present and abundant in human fluids (PubMed:24114876). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
+{"protein": "MSIFIPKARRPTFELHLRIHDVVNIPLITGVIFVKWNIEGIHSRHANDQTEAEPVLEHRVTWEYETCVSVRMIIDNDNLLKDKFLILQVLCDSHTDSGVIRLGILKINLTEYVYVGQDTRKYLLADSKINATIRIGISLKQTSGNKDFRVSKTLGKPQVFSGLTGLLTDGKELKRRDDEVYTSTGLASAWAEKMLHSIKDFNQKTTVFHMHTRNNKYDTREIVDDIFFGGTGWAEPPKIADIVDAAGDTDLISLEIRQKSWVLPSEKVLNKRLP", "text": "SIMILARITY: To yeast YBL086c."}
+{"protein": "MSNKQNATLNITGMTCAACSNRIEKRLNKMDNVKAQVNLTTEKATIEYDTNDYAINDFVTTVQKLGYDVVIDKAELDITGMTCAACSNRIEKVLNKAPGVKDATVNLTTEQAMVTYYPGQTDLDTLIGRIRNLGYDAQPKQSEEDQATRKQQELKHKRNKLMISTILSLPLLMTMLVHLFNMHLPDILMNPWFQFILATPIQFIIGWQFYVGAYKNLRNGGFNMDVLVALGTSAAYFYSIYEMIKWFSGATNMPHLYFETSAVLITLILFGKYLEARAKSQTTNALSELLNLQAKEARLIDDNGMEKMVPLNQVNVDDILLIKPGEKIPVDGQIIKGETAIDESMLTGESMPVDKHVDDVVIGSTMNTNGVITIMATKVGKDTALSNIIKVVEEAQSSKAPIQRLADIISGYFVPIVIAIALLTFLIWITLVHPGQFEDALVAAISVLVIACPCALGLATPTSIMVGTGRAAENGILFKGGEYVERTHQVDTVVFDKTGTLTHGKPEVTYFEGDKDTLTLVASAENNSEHPLATAIVNYAKQHKVNLVNVTNYQTLPGHGIQAIIDDSMLFVGNQKLMLDHQINIQSIKQKMKQMEAEGHTVMLIAYDGKLRGMIAVADTVKASAKEAIQQLSSMNIRTVMLTGDNERTAKAIAKEVGIDQVIAGVLPEDKAHHITQLQEQKHNVAMVGDGINDAPALVKADIGIAMGTGTEVAIEAADITILGGDIQLVPKAIHASHKTIRNIKQNLFWAFGYNIAGIPIAAMGLLAPWIAGAAMALSSVSVVSNALRLKRMKL", "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": "MPFKAFDTFKEKILKPGKEGVKNAVGDSLGILQRKIDGTNEEEDAIELNEEGRPVQTSRAHRPVCDCSCCGIPKRYICDCSCCGIPKRYIIAVMSGLGFCISFGIRCNLGVAIVEMVNNSTVYVDGKPEIQTAQFNWDPETVGLIHGSFFWGYIVTQIPGGFISNKFAASRVFGAAIFLTSTLNMFIPSAARVHYGCVMGVRILQGLVEGVTYPACHGMWSKWAPPLERSRLATTSFCGSYAGAVVAMPLAGVLVQYIGWASVFYIYGMFGIIWYMFWLLQAYECPAAHPTISNAERTYIETSIGEGANLASLSKFNTPWRRFFTSLPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFAISKVGLLSAVPHMVMTIVVPIGGQLADYLRSRKILTTTAVRKIMNCGGFGMEATLLLVVGFSHTKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPLIVGAMTKHKTREEWQNVFLIAALVHYSGVIFYGVFASGEKQDWADPENLSEDKCGIIDQDELAEETELNHETFVSPRKKMSYGATTQNCEVQKTEWRQQRESAFDGEEPLSYQAEGDFSETS", "text": "FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, sodium and phosphate (PubMed:18215623, PubMed:18080752, PubMed:12384506). 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 (PubMed:18215623, PubMed:18080752, PubMed:12384506). 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 (PubMed:12384506). 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 (By similarity). The symporter activity is electrogenic (By similarity). Moreover, operates synergistically with SLC18A3/VACHT under a constant H(+) gradient, thereby allowing striatal vesicular acetylcholine uptake (PubMed:18278042). 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": "MSLTANDESPKPKKNALLKNLEIDDLIHSQFVRSDTNGHRTTRRLFNSDASISHRIRGSVRSDKGLNKIKKGLISQQSKLASENSSQNIVNRDNKMGAVSFPIIEPNIEVSEELKVRIKYDSIKFFNFERLISKSSVIAPLVNKNITSSGPLIGFQRRVNRLKQTWDLATENMEYPYSSDNTPFRDNDSWQWYVPYGGTIKKMKDFSTKRTLPTWEDKIKFLTFLENSKSATYINGNVSLCNHNETDQENEDRKKRKGKVPRIKNKVWFSQIEYIVLRNYEIKPWYTSPFPEHINQNKMVFICEFCLKYMTSRYTFYRHQLKCLTFKPPGNEIYRDGKLSVWEIDGRENVLYCQNLCLLAKCFINSKTLYYDVEPFIFYILTEREDTENHPYQNAAKFHFVGYFSKEKFNSNDYNLSCILTLPIYQRKGYGQFLMEFSYLLSRKESKFGTPEKPLSDLGLLTYRTFWKIKCAEVLLKLRDSARRRSNNKNEDTFQQVSLNDIAKLTGMIPTDVVFGLEQLQVLYRHKTRSLSSLDDFNYIIKIDSWNRIENIYKTWSSKNYPRVKYDKLLWEPIILGPSFGINGMMNLEPTALADEALTNETMAPVISNNTHIENYNNSRAHNKRRRRRRRSSEHKTSKLHVNNIIEPEVPATDFFEDTVSSLTEYMCDYKNTNNDRLIYQAEKRVLESIHDRKGIPRSKFSTETHWELCFTIKNSETPLGNHAARRNDTGISSLEQDEVENDVDTELYVGENAKEDEDEDEDFTLDDDIEDEQISEENDEEEDTYEEDSDDDEDGKRKGQEQDENDIESHIRKERVRKRRKITLIEDDEE", "text": "FUNCTION: Catalytic component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation. In vitro, SAS3 acetylates free histones H3 and H4. It is involved in silencing the HMR locus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MYST (SAS/MOZ) family."}
+{"protein": "MSARGINKVILVGRLGNDPEVRYIPNGGAVANLQVATSESWRDKQTGEMREQTEWHRVVLFGKLAEVAGEYLRKGAQVYIEGQLRTRSWDDNGITRYITEILVKTTGTMQMLGSAPQQNAQAQPKPQQNGQPQSADATKKGGAKTKGRERKAAQPEPQPQTPEGEDYGFSDDIPF", "text": "FUNCTION: May contribute to the conjugative processing of DNA. It has a functional relationship with Psi (plasmid-mediated sos inhibition) proteins."}
+{"protein": "MKNYLSFGMFALLFALTFGTVNSVQAIAGPEWLLDRPSVNNSQLVVSVAGTVEGTNQDISLKFFEIDLTSRPAHGGKTEQGLSPKSKPFATDSGAMSHKLEKADLLKAIQEQLIANVHSNDDYFEVIDFASDATITDRNGKVYFADKDGSVTLPTQPVQEFLLSGHVRVRPYKEKPIQNQAKSVDVEYTVQFTPLNPDDDFRPGLKDTKLLKTLAIGDTITSQELLAQAQSILNKNHPGYTIYERDSSIVTHDNDIFRTILPMDQEFTYRVKNREQAYRINKKSGLNEEINNTDLISEKYYVLKKGEKPYDPFDRSHLKLFTIKYVDVDTNELLKSEQLLTASERNLDFRDLYDPRDKAKLLYNNLDAFGIMDYTLTGKVEDNHDDTNRIITVYMGKRPEGENASYHLAYDKDRYTEEEREVYSYLRYTGTPIPDNPNDK", "text": "FUNCTION: This protein is not a protease, but it activates plasminogen by complexing with it. As a potential virulence factor, it is thought to prevent the formation of effective fibrin barriers around the site of infection, thereby contributing to the invasiveness of the cells."}
+{"protein": "MKIGPVLGIEGTAWNLSAALFDDDLIKLVSHPYKPVQGGIHPREAAQHHASVITSVIEEVLKGNPTPVAVAFSQGPGLGPCLRIVGTAARALALSFDVPLIGVNHCVAHVEIGRFASGFDDPVVLYASGANTQVLGYLQGRYRIFGETLDIGIGNAIDKFARSKGLPHPGGPEIERIAKNGSYIPLPYTVKGMDLAFSGLVSAAKDASAPLEDVCYSLQETAFAMCTEVTERALSQTGKEQLILVGGVGMNKRLQEMLSCMCEDRDAAFSVPNPQYLGDNGAMIAYTGRVMLESGSVLPVEESRVNPSYRADQVLVTWREEPSGSERHPDAYSARGAEAIVRFCDGAASKIRVSKRYRHPELDRRLIAERTRAEARLIAEARKAGVRTPIIREITQDTIIMEHIDGVKLKECLSPELLEETGRMVGKLHAAQIVHGDLTTCNFLVHDGKTWLIDFGLAGTSSDIEHRGVDIHVLFQVLESTSKDSDILKEAFIQGYREKMPLADEILNREHEIELRGRYL", "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": "MIGKLSLLLVCVAVASGNPAAGKPWHWKSPKPLVDPRIHVNATPRIVGGVEATPHSWPHQAALFIDDMYFCGGSLISSEWVLTAAHCMDGAGFVEVVLGAHNIRQNEASQVSITSTDFFTHENWNSWLLTNDIALIKLPSPVSLNSNIKTVKLPSSDVAVGTTVTPTGWGRPLDSAGGISDVLRQVDVPIMTNDDCDAVYGIVGNGVVCIDSEGGKGTCNGDSGGPLNLNGMTYGITSFGSSAGCEVGYPDAFTRVYYYLDWIEQKTGVTP", "text": "FUNCTION: Serine protease with chymotryptic and collagenolytic activities. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MKLTLFILIVFVVLANVYAAGISERNIIGGRVIKLCGGGAQKCCDREPRCDPCRKCVQSFHSGVYMCSDKKSNCS", "text": "FUNCTION: No toxicity is observed upon intracranial injection into mice and intrathorax injection into crickets. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MLPYIVLVLGCWSVLSQAAQTDDEERAGNRRPIWIMGHMVNAIGQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDCGRNCKKYENFNDFLKGLRSATTPGNSKYQEKLVLVVFDLKTGSLYDNQANDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTKDGHPELMDKVGHDFSGNDDIGDVGKAYKKAGITGHIWQSDGITNCLPRGLSRVNAAVANRDSANGFINKVYYWTVDKRSTTRDALDAGVDGIMTNYPDVITDVLNEAAYKKKFRVATYDENPWVTFKK", "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) with high activity (PubMed:16581177, PubMed:9790962, PubMed:21590705, PubMed:27233517). It also acts on lysophosphatidylcholine (LPC), and lyso-platelet activating factor (LPAF, an alkyl-LPC) but not on phosphatidylcholine (PC) (PubMed:21590705, PubMed:27233517). 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, it induces dermonecrosis, vascular permeability, platelet aggregation, inflammatory response, edema and cytotoxicity against renal epithelial cells (PubMed:16581177, PubMed:9790962, PubMed:17900646, PubMed:27233517). It causes direct nephrotoxicity (PubMed:16005484) and is directly toxic to liver (PubMed:18765244). It also induces hemolysis in a complement-dependent manner as well as in a complement-independent manner (PubMed:9790962, PubMed:17900646, PubMed:21590705, PubMed:27233517). The hemolysis provoked in a complement-independent manner is composed of several steps (PubMed:21590705). The toxin binds to erythrocyte membranes, hydrolyzes membrane phospholipids (SM and LPC) thus generating metabolism products that cause hemolysis, probably by provoking an increase of calcium inside cells (PubMed:21590705). The calcium influx is due to the opening of L-type calcium channels, since L-type calcium channel blockers inhibit calcium influx (PubMed:21590705). In vivo, is lethal to mice when intraperitoneally injected (PubMed:17900646). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the arthropod phospholipase D family. Class II subfamily. Class IIa sub-subfamily."}
+{"protein": "MHIGKKNYPNLITSFRMNLKKIILNHDRFSHPERWKTNALLRFTFVYIKFLFDLMIIKNPLRMVGKTYRDAVTALNSLQSNYANIMAIRQTGDRKNTMTLLEMHEWSRRIGYSASDFNKLNIVHITGTKGKGSTAAFTSSILGQYKEQLPRIGLYTSPHLKSVRERIRINGEPISEEKFAKYFFEVWDRLDSTTSSLDKFPHMIPGSKPGYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIEKPIVCGVTLLGIDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVEKQPPQGLTILKERAEERKTTLTEVPSFKQLENVKLGIAGEFQKSNASLAVMLASEILHTSNILEEKIKCSSNASIPEKFIIGLQNTKWEXRCQVLEKGKNVWYIDGAHTKDSMVAASTWFRDTVRLSKRKKILLFNQQSRDANALVNNLYSSVSPEITFDDVIFTTNVTWKSGSYSADLVSMNTSQEDVEKLKVQESLVKNWNKIDDNRAKTHVTASIEEANELIETLYDEPADIFVTGSLHLVGGLLVVFDRIDVK", "text": "FUNCTION: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Required for methionine synthesis and maintenance of intact mitochondrial DNA. Involved in telomere maintenance (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane Mitochondrion matrix Cytoplasm. SIMILARITY: Belongs to the folylpolyglutamate synthase family."}
+{"protein": "MPQFFLNKRLIILLISIIVLVALVGFSLRDRENASWPEQFVKDVVGFGENIVAKPTSFISGAVDGVVDLKNTYTENQHLKERLEELAQLESEVADLKKENKDLKESLDITDSIRDYDPLNASVISRNPTNWNDQVEIDKGSSDGVKPDMAVTTPSGLIGKVTTTGAKSATVELLTSSDVKNRVSAKVQGKENAFGIINGYDSDTKLLELKQLPYDMKFKKGQKVVTSGLGGKFPAGIFIGTIEKVETDKMGLSQTAFIKPGADMYDLNHVTVLKRSAEAGTTDDDTTSSDTTGGQ", "text": "FUNCTION: Involved in formation and maintenance of cell shape. SIMILARITY: Belongs to the MreC family."}
+{"protein": "MEYNKKLYEAIERVAIKNDALKKELETVVTDFKKIKEINIQLKKTTKIAEAFAKYKQKLDTGIAAEKILNTEKDLELIELAQMDLDEAKINIPIIENDLKIMLLPTDPNDDKNVIVEMRPAAGGDESSIFVGNLFDTYRAYAENNNWKMKIIEMTPNAVGFSFISFMISGEEVYSRMKFESGVHRVQRVPATESKGRVHTSTITVAVLPEQDEVDVVINPTELRIDTYRASGAGGQHVNRTESAVRITHIPTGVVAACQEGKSQIENRETAMKMLRAKLWEAAQEQQNAEFANLRKNQVGTGDRSEKIRTYNYPQNRVTDHRINLTLNKLDQIMMGELDEIIDALIADEQTGLMANLDI", "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": "MNGQLDLSGKLIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFVNGQPRPLESSQVKYLRRELIELRNKVNRLLDSLEPPGEPGPSTNIPENDTVDGREEKSASDSSGKQSTQVMAASMSAFDPLKNQDEINKNVMSAFGLTDDQVSGPPSAPAEDRSGTPDSIASSSSAAHPPGVQPQQPPYTGAQTQAGQIEGQMYQQYQQQAGYGAQQPQAPPQQPQQYGIQYSASYSQQTGPQQPQQFQGYGQQPTSQAPAPAFSGQPQQLPAQPPQQYQASNYPAQTYTAQTSQPTNYTVAPASQPGMAPSQPGAYQPRPGFTSLPGSTMTPPPSGPNPYARNRPPFGQGYTQPGPGYR", "text": "FUNCTION: Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules (PubMed:23479643, PubMed:27813252). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:21478858). SUBCELLULAR LOCATION: Endoplasmic reticulum Note=Localizes to endoplasmic reticulum exit site (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:27813252, PubMed:21478858)."}
+{"protein": "MAELREVQITEEKPLLPGQTPEVAKTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQPLFQFADMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCILQYLNFSTIIGIGVGAGAYVLSRYALTHPDTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSISEMILGHLFSQEELSGNSELIQKYRNIIAHAPNLDNIELYWNSYNNRRDLNFVRGGDTTLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLTSAASIDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC", "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 (By similarity). 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": "MMFEFYMAELLRHRWGRLRLYRFPGSVLTDYRILKNYAKTLKGAAA", "text": "SIMILARITY: To E.coli ylcG."}
+{"protein": "MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEESSEEKGPEVQEYREKVETELRGVCDTVLGLLDTHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPEEPQS", "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. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Secreted Note=May be secreted by a non-classical secretory pathway. SIMILARITY: Belongs to the 14-3-3 family."}
+{"protein": "VRDAYIAQNYNCVYACARDAYCNDLCTKNGARSGLFATFGPHGDACWCIALPNNVPLKVQGKCHRK", "text": "FUNCTION: Binds 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 (3 C-C) scorpion toxin superfamily."}
+{"protein": "MESGNVVNVQSELSGIIDGSKSYMYEQLWKLCAGPLCDIPKLGEKVYYFPQGHIELVEASTREELNELQPNCDLPSKLQCRVIAIHLKVENNSDETYVEITLMPDTTQVVIPTENENQFRPIVNSFTKVLTASDTSAQGEFSVPCKHAIECLPPLDMSQPIPAQELIAIDLHGNQWRFKHSYRVPRGDTTGWNAFTTSKKLVVGDVIVFARGETGELRVGIR", "text": "FUNCTION: Auxin response factors (ARFs) are transcriptional factors that binds 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": "MSATESSSIFTLSHNSNLQDILAANAKWASQMNNIQPTLFPDHNAKGQSPHTLFIGCSDSRYNENCLGVLPGEVFTWKNVANICHSEDLTLKATLEFAIICLKVNKVIICGHTDCGGIKTCLTNQREALPKVNCSHLYKYLDDIDTMYHEESQNLIHLKTQREKSHYLSHCNVKRQFNRIIENPTVQTAVQNGELQVYGLLYNVEDGLLQTVSTYTKVTPK", "text": "FUNCTION: Catalyzes the reversible hydration of CO(2) to H(2)CO(3). The main role may be to provide inorganic carbon for the bicarbonate- dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase. Involved in protection against oxidative damage. Encodes a substrate for the non- classical protein export pathway for proteins that lack a cleavable signal sequence. SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion intermembrane space. SIMILARITY: Belongs to the beta-class carbonic anhydrase family."}
+{"protein": "MASVTRAVFGELPSGGGTVEKFQLQSDLLRVDIISWGCTITALEVKDRQGRASDVVLGFAELEGYLQKQPYFGAVIGRVANRIAKGTFKVDGKEYHLAINKEPNSLHGGVRGFDKVLWTPRVLSNGVQFSRISPDGEEGYPGELKVWVTYTLDGGELIVNYRAQASQATPVNLTNHSYFNLAGQASPNINDHEVTIEADTYLPVDETLIPTGEVAPVQGTAFDLRKPVELGKHLQDFHLNGFDHNFCLKGSKEKHFCARVHHAASGRVLEVYTTQPGVQFYTGNFLDGTLKGKNGAVYPKHSGFCLETQNWPDAVNQPRFPPVLLRPGEEYDHTTWFKFSVA", "text": "FUNCTION: Mutarotase that catalyzes the interconversion of beta-D- galactose and alpha-D-galactose during galactose metabolism (PubMed:12753898). Beta-D-galactose is metabolized in the liver into glucose 1-phosphate, the primary metabolic fuel, by the action of four enzymes that constitute the Leloir pathway: GALM, GALK1 (galactokinase), GALT (galactose-1-phosphate uridylyltransferase) and GALE (UDP-galactose-4'-epimerase) (PubMed:30451973). Involved in the maintenance of the equilibrium between the beta- and alpha-anomers of galactose, therefore ensuring a sufficient supply of the alpha-anomer for GALK1 (PubMed:12753898). Also active on D-glucose although shows a preference for galactose over glucose (PubMed:12753898). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldose epimerase family."}
+{"protein": "MVSLISIVSVVFLLFTTFYHFGEARIINVGGSLDAWKVPESPNHSLNHWAESVRFQVGDALLFKYDSKIDSVLQVTKENYEKCNTQKPLEEHKDGYTTVKLDVSGPYYFISGAPSGNCAKGEKVTVVVQSPNHPKPGPAAVTPTLPPKPSTTPAAPAPAPPTPSPKSSTSTMAPAPAPAKSSAVGLVAGNGIFWASTLVAVIGLAFA", "text": "FUNCTION: May act as a carbohydrate transporter (PubMed:24470637). Required, together with ENODL11, ENODL12, ENODL13, ENODL14 and ENODL15, for male-female communication and pollen tube reception and burst at the synergid cell surface of the female gametophyte (PubMed:27524487). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the early nodulin-like (ENODL) family."}
+{"protein": "MTSSETTTDHPRTGKCPIDHSKFARSNEANPDAYINGIKKDQQSSSWWNSLWSRNTDVASEPDVAMLHKKPSTVDTHDHPLANPPPGCPMHKASNENSTGFFSNLFGREKQNSEATPAVQPPATCPMSNSNQKPAGVSEVLTGVDSKQQSYVPEGCPVATPKRGWFNWFGNNDDQKQEAYEVDKSNMMYKNIPQTAVDDQVVGLETTRTTSSIPKVDGKNWEYPSPQQMYNAMWRKGYRDSGENVPIMVQVHNFLNEGAWSEIKAWEREAGENTEPKLLRFEGNANKRTPRALWYMMLGRINPNRWGSGEGPFDRHDWYVQRKDNSIVRYVIDYYEAPDSADGKPVFSLDVRPAVDSFESVALRWKHWRAMRQMQQQ", "text": "FUNCTION: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome. SUBCELLULAR LOCATION: Mitochondrion inner membrane Mitochondrion intermembrane space. SIMILARITY: Belongs to the cytochrome c-type heme lyase family."}
+{"protein": "MARWQRKASVSSPCGRSIYRFLSLLFTLVTSVNSVSLPQSENPAFPGTLICDKDEVRIEFSSRFDMEKWNPSVVDTLGSEILNCTYALDLERFVLKFPYETCTIKVVGGYQVNIRVGDTTTDVRYKDDMYHFFCPAIQAETHEISEIVVCRRDLISFSFPQLFSRLADENQNVSEMGWIVKIGNGTRAHILPLKDAIVQGFNLLIDSQKVTLHVPANATGIVHYVQESSYLYTVQLELLFSTTGQKIVFSSHAICAPDLSVACNATHMTLTIPEFPGKLESVDFGQWSIPEDQWHANGIDKEATNGLRLNFRKSLLKTKPSEKCPFYQFYLSSLKLTFYFQGNMLSTVIDPECHCESPVSIDELCAQDGFMDFEVYSHQTKPALNLDTLLVGNSSCQPIFKVQSVGLARFHIPLNGCGTRQKFEGDKVIYENEIHALWENPPSNIVFRNSEFRMTVRCYYIRDSMLLNAHVKGHPSPEAFVKPGPLVLVLQTYPDQSYQRPYRKDEYPLVRYLRQPIYMEVKVLSRNDPNIKLVLDDCWATSSEDPASAPQWQIVMDGCEYELDNYRTTFHPAGSSAAHSGHYQRFDVKTFAFVSEARGLSSLIYFHCSALICNQVSLDSPLCSVTCPASLRSKREANKEDTMTVSLPGPILLLSDVSSSKGVDPSSSEITKDIIAKDIASKTLGAVAALVGSAVILGFICYLYKKRTIRFNH", "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. ZP2 may act as a secondary sperm receptor. SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 2]: Zona pellucida. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the ZP domain family. ZPA subfamily."}
+{"protein": "MMKYVFVALCLFAVVALATEVEQKESNTRVARLNVGGLVGCVVALVANIVGGLLRVIIGLVVTLSGVLQIVVGTVLGLVATVASLALDVVGSTVGGILNSLLGLGAILSLVEEVLHVLLSQALLTGLVNAIFALPLSLLVALSTLTDALASAACDCGASATGAGSSLAGCIAGPNGLLFTVGAGASV", "text": "SUBCELLULAR LOCATION: Membrane. SIMILARITY: To HAP-S protein."}
+{"protein": "MIDGEAYFEKNSTGKLGSWGWRDVNLQFIICTLPVPIYFVVVAIWTINGASNSYRFPFLQTYMILTDRFWLFFRCFTIVAWCGWCSNYIFFPCLMNAILYIISLSLSRDTTFILFIFYQMNKLITVIRDFSYSVYNWCYETVIGENTRKYKMTWKVPKESLKIIVNKNADARMQRELENRTAKDEANALTSRRRVFGSYALIGTQRAEFIQFRQIKHIDITNASLDFLYNLKQLKHDNLANFYGIQLNDDLNTMTILHALVERGTLEEFCLDRDFGMDETFKSAFMRDILKGLQYLHLSPVAYHGHLHAATCLIDINWVLKIALYGVTNFVCDNFDAENITMPDRSDYTISYAQYVCFPPEHIREYDATGKLPTRFVRGSKQGDIYCVGMIFYMMIEREDPYRLIHSVERPGSGLMMEILDHNLMPFISNNETQEDTLLDKCKECWNRDPEKRPTIENLRNAIAICYADSKGNLIDQMIRMNEKYADELETLVAARSADLALAQMQTMRLLNEMLPASIAKDLKNGVIAPARSYASATVMFVQICDFIVILKRRPPKEVIGFLNDIFDQFDTVIKRHDAYKVETTGETYMVASGVPNENEGRHVFEVAEMSLEIRAISLSYTLENDKNYKLRVRIGFHAGPIAAGVIGIKNPRYCLFGDTVNFASRMQSNCPPLQIQTSEITARMLLATHEYKLVKRGIVHVKGKGEVNCYWLNEHIHKDEEIEESGTISHPLES", "text": "FUNCTION: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). May be involved in sensitivity to quinine by regulating egl-4 activity through the production of cGMP (PubMed:23874221). Promotes the calcium flux to the cytoplasm in ASJ sensory neurons upon removal of a nitric oxide (NO) stimulus and is thereby involved in the behavioral avoidance response to NO-producing organisms like P.aeruginosa (PubMed:30014846). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase family."}
+{"protein": "MGAYKYMQELWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRATRPDKARRLGYKAKQGYVIYRVRVRRGGRKRPVPKGATYGKPVHHGVNQLKFARSLQSIAEERAGRHCGGLRVLNSYWVGEDSTYKFFEVILIDTFHKAIRRNPDMQWITKAVHKHREMRGLTSAGKKSRGLGKGHKFHLTIGGSRRAAWRRRNTLQLHRYR", "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": "MTKKVVTITLNPALDLTGSVNQLNVGSVSLVGQSSLHAAGKGVNVAKVLSELGAQVTVTGFLGRDNQELFCQLFEQLGVQDAFIRIAGATRINVKLVEQSGAVSDINFPGIQVTEADIEAFEATLQRLAQDHDYFVLAGSLPQGISPQRCAGWIAQLRSMNKKVLFDSSRDALLAGLDAKPWLIKPNDEELSQWCGRELTTLTDCQQAAAELAQKQIENIVISMGAEGVMWLHENQWLHAKPPKMQVVSTVGAGDTLVAGLCWGHMQRMEKESLLRFATALSALAVTQVGVGLGDREQLNTLQQQIQVSALYPTMGA", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l- phosphate to fructose-l,6-bisphosphate. SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
+{"protein": "MIPRNLISGLFLLPFVVAELNIYGYLDLKTLADGFHTTTACIAALNQTVDCDARTAVAAAVADTYYWTLDNVTTLCTSQCQQSLTSWTSAVDAACGNRPIVEDGIVKLASSTPLTYKEGFDLVCLKSGDSWCMIESQEWEGSDILKYPTDYCSTGDPEYDGPECFEKGFDQLAIEAGDERMTSLYEKDLLCSDCFLKVFRQRLLSPFLLKGGYTSYLVEQFQDMQSYCSTSMPYATSTSEVFMGTATRTMPTGSPPPTTTCGGPTIQPTDPPLSCEAITDKYNVTTGDSHSDLHGEFSLASKPRFLKANAIDRQHEPIEKLDHAICYAGTSEPPGGSYESQPPVHQPTGASEYYTTAIPPAPTSTGTTPSCGRYYEVVAGDQCNTIALHFGITVDAFLSLNTQIDERCSNLWIAYAYCVAPVDIVDQPMTIVDQDIATQGNVLPATELPSPRMGRVVLNIMIGSVVTQLLENAALSMDIAGVRRTSAQQGIVIRVPVIQTLAKRVLTVRADQALQETKHVPALNLAHVATWRDIVEMEPTTAHPGDAILERAKGPRIHSIALYVTVLYLDLWI", "text": "FUNCTION: Might have a role in sequestration of chitin oligosaccharides (breakdown products of fungal cell walls that are released during invasion and act as triggers of host immunity) to dampen host defense. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQSQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDNPNNPNNPDNPDNGDNNNSDNPDAA", "text": "FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1B family."}
+{"protein": "MALQLLTPSFSFQHSPSPHKLTTLRYTHHRIRCTASAPSYSDLVRRRSANYKPSKWDSNFVETLESDYKKENHEMYIEKLMGDVKHLMKEVVNPIEKMELVDTIQRLGLGYLFNKEIKEVLNTITTSKATLKTKKDLHAVALQFRLLRQHGYEVSPDAFHEFKDEKGGFKESLCMDIKGMLCLYEASHLSFQGEVVLDEAREFTSTHLKAIGGNIDPVLLKKVRHSLEMPLHWRMLRLEARWYIETYDEEDRKNPSLAELAKHDFNSVQTIYQRSLKRMSRWWRDLGLGERLEFSRDRLVECFFWTTGVIFDPQFERCRGVLTKVNQLVSTIDDVYDVYGSLEELELFTDAVDRWDIRAMEQLPEYMKICYLALYNTTNDIAYEALKEEGLDVIPYLKKVWTDLCKSYIVEARWYSNGYKPTLEEYLENAWTSIAGPVALVHAYFSFGQKMPFEALNYSNTSSLIKWSSMIFRLCDDLATSSDEVARGDVPKSIQCYMYEAGVSESVARDHIKYLIDEAWKKMNECLVYNTPFLQPLINAGLNLARMAHCMYERGDGHGFSNELDKKRVLLLLAEPFKFM", "text": "FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products used by traditional Chinese medicine to treat headache, inflammation and intoxication (Ref.1). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-thujene (Ref.1). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily."}
+{"protein": "MCGRTSCHLPREVLTRACAYQDRQGRRRLPQWRDPDKYCPSYNKSPQSSSPVLLSRLHFEKDADSSDRIIIPMRWGLVPSWFKESDPSKLQFNTTNCRSDTIMEKQSFKVPLGKGRRCVVLADGFYEWQRCQGTNQRQPYFIYFPQIKTEKSGGNDASDSSDNKEKVWDNWRLLTMAGIFDCWEAPGGECLYSYSIITVDSCRGLSDIHSRMPAILDGEEAVSKWLDFGEVATQEALKLIHPIDNITFHPVSPVVNNSRNNTPECLAPADLLVKKEPKANGSSQRMMQWLATKSPKKEVPDSPKKDASGLPQWSSQFLQKSPLPAKRGATSSFLDRWLKQEKEDEPMAKKPNS", "text": "FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites (By similarity). Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue (By similarity). The HMCES DNA-protein cross-link is then degraded by the proteasome (By similarity). Promotes error-free repair of abasic sites by acting as a 'suicide' enzyme that is degraded, thereby protecting abasic sites from translesion synthesis (TLS) polymerases and endonucleases that are error-prone and would generate mutations and double-strand breaks (By similarity). Has preference for ssDNA, but can also accommodate double-stranded DNA with 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction (By similarity). Also involved in class switch recombination (CSR) in B-cells independently of the formation of a DNA-protein cross-link: acts by binding and protecting ssDNA overhangs to promote DNA double-strand break repair through the microhomology-mediated alternative-end-joining (Alt-EJ) pathway (PubMed:31806351). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (PubMed:29020633). SUBCELLULAR LOCATION: Chromosome Note=Recruited to chromatin following DNA damage. Localizes to replication forks. SIMILARITY: Belongs to the SOS response-associated peptidase family."}
+{"protein": "MADSAGLDQPEPSPRPVLVVDFGAQYAQLIARRVREARVFSEVIPHTTSIEEITARDPLAIVLSGGPASVYTEGAPQLDPALFDLGLPVFGICYGFQAMAQVLGGTVARTKTSEYGRTELKVLGGDLHSGLPGVQPVWMSHGDAVTAAPDGFDVAASSSGAPVAAFENRDRRLAGVQYHPEVMHTPHGQQVLSRFLHDFAGLDADWTAANIAGVLVEQVRAQIGNGHAICGLSGGVDSAVAAALVQRAIGDRLTCIFVDHGLLRDGERGQVQRDFVAATGAKLVTVDAAETFLQALSGVTNPEGKRKIIGRQFIRAFEGAVRDLLGDSTFDSGIEFLVQGTLYPDVVESGGGSGTANIKSHHNVGGLPDNLRFKLVEPLRLLFKDEVRAVGRQLDLPEEIVARQPFPGPGLGIRIVGEVTAERLDTLRRADSIAREELTTAGLDYQIWQCPVVLLADVRSVGVQGDNRSYGHPIVLRPVSSEDAMTADWTWVPYEVLECISTRITNEVAEVNRVVLDITNKPPGTIEWE", "text": "FUNCTION: Catalyzes the synthesis of GMP from XMP. FUNCTION: Catalyzes the synthesis of GMP from XMP."}
+{"protein": "MDGVGLCANNKQKQNQMLPNKMRGEFTRNQRKDSEGLSEAPDLEFEYSDADKWTAELSELYSYTEGPEFLLNRKCFEEDFHTHLPDQKWTELDSVQRRAHAMRLLDGLEVIGRERRLKVARAILYMAQGTFGECSSELEVQHWMRYNVFLLLDVGAFTALVELLNMEIDNSAACSSAVRKPAISLADSTDLRVLLNIMYLMVETIQREEPTDSPEWRTIRETFKSELGSPLYNHEPVSVMLFGMVTKFCSGHAPHFPMKKVLLLLWKTILFTLGGFEQLQSCKISRRAALGLPPLPEDSIRVVRSMRAASPPASASDLIEQQQRRARREHKALIKQDNLDTFNEKDPYKADDSHEDEEENDDNDNSLEAEPFPLERDEVMPPPIPHPPTERMCFPKGLPWAPKVREKDIESFLESSRSKFIGYTLGNDTDTVVGLPRPIHESIKTLKQHKYVSIAEVQIAKEEAFQKTPLSGGEEELELCATELLYQGILPSLPQYMIALLKILLAAAPTSKAKTDSINILADVLPEEMPTTVLQSMKLGVDVNRHKEIIVKAISAILLLLLKHFKLNHVYQFEYMAQHLVFANCIPLILKFFNQNIMSYITAKNSISALDFPHCVIHELPELTAESLEAGDNNQFCWRNLFSCINLLRILNKLTKWKHSRTMMLVVFKSAPILKRALKVKQAMMQLYVLKLLKVQTKYLGRQWRKGNMKTMSAIYQKVRHRLNDDWAYGNDLDARPWDFQAEECALRANIERFNSRRYDKNQSNPEFLPVDNCLQSVLGQRIDLPEDFQMNYDLWLEREVFSKPISWEELLQ", "text": "FUNCTION: May play a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Enriched on the plasma membrane. SIMILARITY: Belongs to the STRIP family."}
+{"protein": "MSSLLSRSRVGWLLGFLLLPLLFWLPAPAWAATEVAPSTSPWQVIDLGTEKTILDIAFTSNKQHGWLVGTDLALYETLDGGQSWSERALDLDETYRLNSISFKGDEGWVVGQPSLMLHTTDGGKNWLRIPLSEKLPGSPLLVTALGKGEAEMATDVAAIYRSRDGGKSWQAQVPDAAGVARSVSRSRDGRYLAVSARGNFYSTWKPGDTTWTPHQRTSSRRLQLMGFGPDDRTWLIARGGRLQFSKTSQIDNWEEMLEESDAWGTAIEPERNAGWGFLDLAYRSKQEIWLSGGSGTLLVSEDGGEHWQRDRVIAKLPSNLYTIKFFAPKQGFVLGQRGLLLRYAPEAAA", "text": "FUNCTION: A factor required for optimal assembly of photosystem II (PSII), acting in the early stages of PSII assembly. Also plays a role in replacement of photodamaged D1 (psbA). Assists YidC in synthesis of chlorophyll-binding proteins. SUBCELLULAR LOCATION: Cellular thylakoid lumen Note=Associated with a PSII precusor complex on the lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the Ycf48 family."}
+{"protein": "MEAEGMLPPQSLSAKFEGSFAYLTVRDRLPTILTKVVDTLHRNKDNFYKEYGEEGTEAEKRAISFLSRLRNELQTDKPVLALTDNAEDTQAWNEYMERQQDLMENGQLVSWFKSPWLYVECYMYRRIQEALYMNPPMHNFDPFKEGKTQSYFESQQAIKYLCTYLQELITNMENMTEIQLRENFLKLIQVSLWGNKCDLSISAGQDNSQKLSPIDSLPDLQRFILVDDSSMVWSTLVASQGSRSSGMKHARVDIILDNAGFELVTDLVLADFLISSGLAKQIRFHGKSIPWFVSDVTKQDFEWTIKQTMAANHKWMSASGVQWKHFMKEGTWSYHDHPFWTLPHEFCDMTVDAANLYSTLQTSDLILFKGDLNYRKLTGDRKWEHTVRFDQALRGFQPAPLCSLRTLKADVQVGLQAGHAEKLSTQDPDWMTNGKYAVVQFSSPHREQ", "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": "MNILNVVRRFEFQLFLVNVIIALFFYFENSAYFSSNNITTIFQYLAEIGIIAIGEAMLMLCGEIDLSPPALANFVPLITLTIYNSIYQAISPTPAIVVSILLSLGLASLIGLMNGLITTKAKVNSLITTVGTLFLFNGIALIYSGGYPESFPYFRFLGGTVSILPVPFIWSLGALVFLILLLHYTKIGVWTIAAGSNPTGASEVGVPVDRVKIINFIIMANIGALVGIIQGSRVLTIGATNFTADVVLEGIAAAVIGGTSLVGGKGSLVGAFLGSVFISELLNGFNILGINAYEFDAILGGAIVVVMVLSYYAKRASYKLKSIATATSSSPEGKDRITKILKFKIQKIYRRVEENE", "text": "FUNCTION: Part of the ABC transporter complex XylFGH involved in the uptake of xylose and arabinose (PubMed:29150511). 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": "MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNSNRAFGVGDDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGAMELVGKTLAEVKALTTELTAENQEAAGLIMTAEPKTIVLKAGKNYIGYSGTGEGNHIENDPLKIKRVHARMAFTEIKVQMSAAYDNIYTFVPEKIYGLIAKKQSNLFGATLVNADANYLTGSLTTFNGAYTPANYANVPWLSRNYVAPAADAPQGFYVLENDYSANGGTIHPTILCVYGKLQKNGADLAGADLAAAQAANWVDAEGKTYYPVLVNFNSNNYTYDSNYTPKNKIERNHKYDIKLTITGPGTNNPENPITESAHLNVQCTVAEWVLVGQNATW", "text": "FUNCTION: Structural subunit of the major fimbriae. These long, 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 (PubMed:9786913, PubMed:12593606, PubMed:15165251, PubMed:17675496, PubMed:17526848, PubMed:20530728, PubMed:27062925). They play an important role in the invasion of periodontal tissues (PubMed:12593606). Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification (PubMed:23809984). The sequence-based classification correlates with pathogenicity (PubMed:17675496). FUNCTION: Structural subunit of the major fimbriae (PubMed:1987052). These long, 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. They play an important role in the invasion of periodontal tissues (PubMed:1987052, PubMed:11748193). Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence- based classification correlates with pathogenicity. SUBCELLULAR LOCATION: Fimbrium Cell outer membrane Note=Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein. SUBCELLULAR LOCATION: Fimbrium Cell outer membrane Note=Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein. SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily. FimA/Mfa1 family."}
+{"protein": "MTFQTLSSENNELLTIASESFLKRWAFSEQRLTVDLMTSDDDELTVYIETDLVQSSPIYLNEDLNICRLSIQDMHEILAVQHGYYVPPSRFGDLMKYSSECYSFFYGRKSDFKYLASFIGYEKYIACPIRFLEDISWRIR", "text": "FUNCTION: Putative immunity protein component of a toxin-immunity protein module, which may function as a cellular contact-dependent growth inhibition (CDI) system. Blocks the toxic effects of expression of the C-terminus (residues 1519-1658) of cognate toxin RhsC in E.coli."}
+{"protein": "MDFKKVFELGKFSDLELILVDKTNSLSINVHKVILYSAIPYFTTMFDNFKEKDCPSIKMEVIDVVVVSDIIKSFYGIETNNDPDWEYLLKEYISLDYLQLSCTLPDNIKVPDECFETLLDLVEIIGYNSKTIDMLANNLPNDFNLSTLPIELLREIESRYYDFYTMIIDRDNRMYSFNMCRKKLLQVTNKKYDDMYYFSVNDNLVLKASDKKIYTCNLSTKILKEHKENISMTDFHHHHLGETDIFIPENEAFKENIKNRIQKYLNNSSSNDGITEIYYSPDLTQIAVIFMLYQEESGEMYWLFIYDCKSDKLKKIYFKFDRISNVLFVPDGVIFYTHCSQKVIAWSNNKFQDVCCSLKHVKQITYDLGDNLLILTHNKFIVYSLNNKCVVNQVNCVLDKIEFVSKEIIIGYHKFYTNKSCVTNTKIIMYNILTGNETNKINVDLEIYKLVVVPDKARTKQKLKEYIESISTERISS", "text": "SIMILARITY: Belongs to the mimivirus BTB/WD family."}
+{"protein": "MEEFVIPVYSEDEIPYALLSRYPLAIQTNVKIEDVEGKHNVVKIPESDMIDIPKLTIVEAMNYKPARNDGIVVPRLLDITLRAYDDRKSTKSARGIEFMTNARWMKWAIDDRMDIQPLKVTLDHYCSVNHQLFNCVVKANAANADTIYYDYFPLEDYKKRCNHTNLDLLRSLTNMELFHALQGAAYSIKSSYELVAYSERGSLEETYVVGQPKWIHLTRGTRIGNSGLSYERFISSMVQVSVNGKIPDEIANEIAQLNRIRAEWITATYDRGRIRALELCSILSTIGRKMLNTHEEPKDEMDLSTRFQFKLDEKFNRADSEHVNIFGVRGPATDEGRFYALIAIAATDTQKGRVWRTNPYPCLRGALVAAECELGDVYSTLRRVYTWSLRPEYGQHERQLENNKYVFNRINLFDSNLAVGDQIIHWRYEVKASAETTYDSGYMCRHEAEEDELLCKINEDKYKEMLDRMIQGGWDQERFKLHNILTDPNLLTIDFEKDAYLNSRSELVLPDYFDKWISSPMFNARLRITKGEIGTSKKDDPWNNRAVRGYIKPLAESLDFVLGPYYDLRLLFFDETLSLKQEQSAVFQYLSQLDDFPALTQLRGDAVCPHSGGALYTFRKVALFLIGNYEKLSPDLHEGMEHQRYVHPSTGGTYQKRVLEMKDSCQLTCFVIDYIFEKREQLRDTKEARYIVYLIQSLTGTQRLSVLRSTFPNFFQRLLMLKEIKFVRDLNVINFLPLMFLVHDNISYWHRQWSIPMVLFDDTIKLIPVEVGAYANRFGFKSFMNFTRFHPGELKKKQIAEDIHKEFGVVAFEYYTNTKISQGNVHTPVMTTKMDVLRVHLSSLCAGLADSVVYTLPVAHPKKCIVLIIVGDDKLEPHTRSEQIVSRYNYSRKHICGIVSVTIGQNSQLRVHTSGIVKHRVCDKFILKHKCKVILVRMPGYVFGNDELMTKLLNV", "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": "EHPALYRRYSKEHTFCKTKNQXCN", "text": "FUNCTION: Possesses high activity against hyaluronan in vitro. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
+{"protein": "MTPWLGLVVLLGSWSLGDWGAEACTCSPSHPQDAFCNSDIVIRAKVVGKKLVKEGPFGTLVYTIKQMKMYRGFTKMPHVQYIHTEASESLCGLKLEVNKYQYLLTGRVYDGKMYTGLCNFVERWDQLTLSQRKGLNYRYHLGCNCKIKSCYYLPCYVTSKNECLWTDMLSNFGYPGYQSKHYACIRQKGGYCSWYRGWAPPDKSIINATDP", "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": "MAKIKKKGTSGQAKNYITRTQAVRKLQISLPDFRRLCIFKGIYPREPRNKKKASKTSTPNTTFYYTKDIQYLLHEPLLRKFRDQKAVAKKIARSLGRGEVGDASRLEKNHAPKLTLDHIIKERYPTFIDALRDLDDALSLLFLFANLPSTSHVPPKTIALCQRLCHEFQHYLITTNSLRKSFLSIKGIYYQATIQGQDIMWLVPYRFVQRVNGDVDYRIMATFVEFYTTLLGFVNFRLYSSIGLRYPPKFDTRSDENGAELAAFTLEGRAVANAAKTIEGSNKQSNNSSNQEVSRDVQAKVDKVIKTAGLDKTKDEQTVEATDENTDAIDRFEPAAPEADTLPQPDISGEEAGALFAPFTFYISREAPKAPLEFILRAFGCKRIGWDAVMGDGAFTHNEADTRITHQIVDRPSLPEGALPAVPAAKEGAVPAVRPGTRIPGRTYIQPQWVWDCINEGKLLRPDLYAPGETLPPHLSPWVKPSKGAYDPRATLAEQEEEGEAEMAGEEEEEESDEEMEEAPETKKADAKADESESEDEDESVDGGMDVADSDDDESESGQEEEDFGGFDDNEAASESEDEEEAARTQHQKELEAEAAGLPFSSNGATDDAKKKKSSQAKKIAAKKRKEEEELERQKMMMSRKKRKLLEKMMYSNKKQSEEAAKLRSKRRKLEKTGEK", "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": "MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILTFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDINKVVEYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLRRVNVQPELVS", "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": "MASFDGQGFMMVDNSWVQTKAIDVESTTDISPYLSKILEDSVWNGNRSIVFDVYWDVKSVSTKSEWRLCSVKFSTKNFCLFLRLPNPFCDNLKDLYRFFASKFVTFVGVQIQEDLALLKENHGIVIRSSLEIGKLAAKARGTPIVEFLGTRELAHKILWYDMSRLDSIQSKWDEASSNDRLEAAAIEGWLIFNVYDQLQQ", "text": "FUNCTION: 3'-to-5' exoribonuclease (RNase) specifically targeting single-stranded RNAs (PubMed:28463111). Triggers miRNA accumulation in RNA-induced silencing complex (RISC), composed of miRNAs and AGO proteins, by degrading uridylated cleavage fragments (PubMed:28463111). Required during plant growth and development (PubMed:28463111). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RICE family."}
+{"protein": "MGPVVERPAEPGTSSAAELELLKRRAAERIDEAAERLGALSRAIWSAPELAYEEHRAHGELTRFFECEPPAASWAVQPHFGLPTAFRAEWAPPESAAGPRALQVAFLCEYDALPALGHACGHNLIAEVGVAAALGLRAALESIAAPPPVKVIVLGTPAEEDGGGKIDLIEAGAFENLDVVFMAHPSQENAAYLPDVAEHDVTVKYYGKASHAAAYPWEGVNALDAAVLAYTNLSVLRQQMKPTWRVHGIIKNGGVKPNIIPSYSELVYYFRAPSMKELQVLTKKAEDCFRAAALATGCTVDIESEAHDYYNVIPNKTLCSAYTENGKKLGMEFISEDAVLNGPSGSTDFGNVSFVVPGIHPYFYIGTDALNHTEQYTEAAGSQAAQLYTLRTAKALAMTALDVIFKPALLEGVRKEFKCKLQEEQLLNTAA", "text": "FUNCTION: Catalyzes the peptide bond hydrolysis in dipeptides having basic amino acids lysine, ornithine or arginine at C-terminus. Postulated to function in a metabolite repair mechanism by eliminating alternate dipeptide by-products formed during carnosine synthesis. SIMILARITY: Belongs to the peptidase M20A family."}
+{"protein": "VALINNQFLPYPYYAKPVAVRSPAQTLQWQVLPNTVPAKSCQDQPTTMAHHPHPHLSFMAIPPKKDQDKTEIPAINTIASVEPTVHSTPTTEAVVNTVDNPEASSESIASAPETNAAQVTTTEV", "text": "FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kappa-casein family."}
+{"protein": "MAILIPASFGRLTITSRAQVRVRVSASANQRTIRRDSVDWVKETSSFFEEDKRPIMLFDGVCNLCNGGVKFVRDHDRNRSIRFEALQSEAGKKLLLRSGRAPDDISSVVLVENDRSYIKSEAVLKIMKYIDLPFPQLAFFLQFAPLFVRDFLYENVANNRYAMFGRSDSCEL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the DCC thiol-disulfide oxidoreductase family."}
+{"protein": "MEEGSSSPVSPVDSLGTSEEELERQPKRFGRKRRYSKKSSEDGSPTPGKRGKKGSPSAQSFEELQSQRILANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDEMDNKMTSCSYVAHERLSYAYSVWRMEGAWSMSASH", "text": "FUNCTION: Binds to the E-box consensus sequence 5'-CANNTG-3' as a heterodimer and inhibits transcriptional activation by MYOD1, MYOG, MEF2A and MEF2C. Also represses expression of pro-inflammatory cytokines such as TNFA and IL1B. Involved in postnatal glycogen storage and energy metabolism. Inhibits the premature or ectopic differentiation of preosteoblast cells during osteogenesis, possibly by changing the internal signal transduction response of osteoblasts to external growth factors (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mainly nuclear during embryonic development. Cytoplasmic in adult tissues."}
+{"protein": "MDMDAKQAVIAKLDELKINYTLIEHDPVYTIEEMEKIDIENVDYIVKNLFLRDAKGRQHYLVVADKDQKIDLKTLQDKIGSTKLSFASEDRLQKYLKLTKGAVSPFGVLNDETAEVEVVFDKNLVGRSCVAVHPNDNSATVVLSYEDLEKIVKANGNTFKAIEL", "text": "FUNCTION: Functions in trans to edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro). Has weak activity on correctly charged tRNA(Ala), tRNA(Gly) as well as tRNA(Cys), tRNA(Met), tRNA(Pro), tRNA(Ser) and tRNA(Leu). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRORSD1 family."}
+{"protein": "MTQRNAIVVGGGIGGLTAASALARQGWRVQLHERQPEIRAVGAGIYIWDNGLFALDAVHAYSEAIEGAHEPPSIDMRGQSGKTLMRIKINGESQPRCLTLLRDQLIKALVNAAKDAGVELVTNSSVVAVRPEGEVHFEHGDHSTTDLVVVADGVHSRLRDSVDLSYSRIRMSQGAARIMIPQSSHELPAEDRGRILESFHGSRRLLYTPCTPELVYLAFTCDSDDPAISGAYINTSEWSRSFPTLSDALRATEGVPATRWDTFEYVRLASWSRGKVAFLGDAAHAQPPYLGQGGGTAMTNAIALANAVSSDMELSEALATWERITRPGIESTQRTSYQQRLLNYVPDRVRNPLVRIAGLTSNVAKSQLKATEIRPTLGSTGGSR", "text": "FUNCTION: Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecule HHQ (2-heptyl-4-quinolone) to anthranilic acid. Probably catalyzes the hydroxylation of HHQ to PQS (2-heptyl-3-hydroxy-4-quinolone). SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family."}
+{"protein": "MATVTLNVKTVRPLGERVLVKVSQSEEKTAGGILLPDTVKEKPQIGEIIAEGPGRRNDDGSFQPLEVTVNSKVLYSKYAGTDIKLENEEYVLLSEKDILAIIA", "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: Plastid, cyanelle. SIMILARITY: Belongs to the GroES chaperonin family."}
+{"protein": "DADIAVWAPPVNAQN", "text": "FUNCTION: Has ribonuclease activity towards yeast tRNA and polyuracil, and decreasing ribonuclease activity towards polyadenine, polycytosine and polyguanine respectively. Lacks antifungal activity against M.arachidicola and P.piricola. Inhibits HIV-1 reverse transcriptase."}
+{"protein": "MSLVAEAFVSQIAAAEPWPENATLYQQLKGEQILLSDNAASLAVQAFLQMCNLPIKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKGHSLSDGLDEVQKAEMKAYMELVNNMLLTAELYLQWCDEATVGEITHARYGSPYPWPLNHILAYQKQWEVKRKMKAIGWGNKTLDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRIEQHYFEDHSKGSSSVRLS", "text": "FUNCTION: Involved in transport of proteins into the mitochondrion. SUBCELLULAR LOCATION: Mitochondrion outer membrane Mitochondrion. SIMILARITY: Belongs to the metaxin family."}
+{"protein": "MESADSTGKGSIEQSESQRQSQMDRLDREEAFYQFVNNLNEDDYRLMRDNNLLGTPGEITKEELLRRLQQIKEGPPQPSTEETRGDSVSTGGDPAEDSSNGDSIIDWLNSVRQTGNTTRSGQRGNQSWRAVSRTNPNSGDFRFSLEINVNRTSGNPSMPSLDQSAEMPGAEDMEVSSQGEAENEPEPIPIATRSAPAEVTVEEAPIQRGQRRARSRSPDQRRTRARTDRSRSPLHHAVDPPIRRAPHSSSQTVDTSNTEEAEGSSRTRHHVSSQVQNSSSSNETEGSSRTRQHIPARQQVLGTEGQSQSTVHLSNPETRSSSQTPQTDSSTNAETTGTGQRPPTIVLDLQVRRVRPGDYRQRDSIANRTRSRSQTPNNTVTYESERGGFRRTFSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLRQIMTGFGELSYFMYNDNDTDPNNPTAVSPTAAVPGEAQNNANAEVRAPSAEPTEPVAPVETDEGSNVSTTATRREGRNSRGAVTFEESGSLPFLSLAQFFLLNEDDDDQPRGLTKEQIDNLSTRNFGENDALKTCSVCITEYTEGNKLRKLPCSHEYHIHCIDRWLSENSTCPICRRAVLVASNRESIV", "text": "FUNCTION: Acts as an E3 ubiquitin-protein ligase specific for ldb1, mediating ubiquitination and proteasome-dependent degradation of excess ldb1 in a RING-dependent manner. Does not degrade ldb1 bound to lhx1/lim1, nor lim1 itself and thus contributes to the establishment of proper ldb1-lhx1/lim1 stoichiometry and the formation of a ldb1- lhx1/lim1 complex. Interferes with Spemann organizer function and suppresses secondary axis formation induced by ldb1 and lhx1/lim1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RNF12 family."}
+{"protein": "MKPSVILYKALPDDLLQRLQEHFTVHQVANLSPQTVEQNAAIFAEAEGLLGSNENVDAALLEKMPKLRATSTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTASIGPDWYGTDVHHKTLGIVGMGRIGMALAQRAHFGFNMPILYNARRHHKEAEERFNARYCDLDTLLQESDFVCLILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSMANVVAVPHIGSATHETRYGMAACAVDNLIDALQGKVEKNCVNPHVAD", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. 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": "MRTSNHLIGLVNFLTFLLSIPILGGGIWLSSRANSTDCLRFLQWPLIVIGISIMVVSLAGFAGACYRNKFLMWLYLVVMLLIIAALIGFIIFAYAVTDKGSGRTVLNRGYLDYYLEDYSGWLKDRVSDDSYWGKISSCLRDSGACRKIGRNFNGVPETADMFFLRRLSPVESGCCKPPTDCGFSYVNETGWDTRGGMIGPNQDCMVWSNDQSMLCYQCSSCKAGVLGSLKKSWRKVSVINIVVLIILVIFYVIAYAAYRNVKRIDNDEPAGEARMTKSHPSHFHL", "text": "FUNCTION: May be involved in the regulation of cell differentiation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MQFWRKQMSEIQHFSQQDIEILGEQTLYEGFFTLKRIQFKHKLFAGGQSGVVTRELLIKGAASAVIAYDPKEDSVILVEQVRIGAAYHPESHRSPWLLELIAGMVEKGEKPEDVALRESEEEAGIQVKNLTHCLSVWDSPGGIVERIHLFAGEVDSAQAKGIHGLAEENEDIKVHVVKREQAYQWMCEGKIDNGIAVIGLQWLQLNYAQLQQSWKRS", "text": "FUNCTION: Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process (By similarity). SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily."}
+{"protein": "MSESEVAGQRYRVGYALQGKKVESFIQPSLLDHAKQHSIDLVQIDPTAPLQQQGPFHCIIHKLHTQHWKNLLQQFSSKHPNTVIIDPPELVDRLHNRVSMLDAVTHLQFSLENATIGVPKQVVVNEPKSFDLHKFEEEQGLRFPVIAKPLAADGGAGSHELCLVFDEEGLHALSVPMVLQEFVNHGGVVFKIYVAGQRVNCVKRKSLGDITEEKLKVLRGSLPFSRVSSLGVEDEGGGAVEDAEMPPQSLVGELARGLREALGLNLFNVDVIRDGKEPTRYLVIDINYFPGYAKLPSYEPFITDFLLDIVRSKTA", "text": "FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). Barely able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting negligible InsP6 kinase activity (PubMed:35635723). Has also Ins(1,3,4,5,6)P5 phosphatase activity (PubMed:35635723). Probably involved in the regulation of drought and salinity tolerance by diverting the flux of inositol phosphate pool towards phytate biosynthesis (PubMed:29289899). SIMILARITY: Belongs to the ITPK1 family."}
+{"protein": "MPLHNLTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNALGALGYVESALEIAQQCEGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELELTASVEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAPALFAYHPHV", "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": "MRRYFIDDETPWEELGDGIKRKIITWSDDLMMVCVHFAKGAIGTPHKHDIHDQIAYVAAGSFEVVIEGEKRILKTGDAYMAVKNEMHGVVSLEEGSVLIDTFSPKRADFL", "text": "FUNCTION: May have a role in pathogenicity."}
+{"protein": "MGTKTHNSRGKIFMIYLILVSLSLLGLILPFKPLFRITSPSSTLRIDLPSPQVNKNPKWLRLIRNYLPEKRIQVGFLNIDEKERESYEARGPLVLKNIHVPLDHIPKNVTWKSLYPEWINEEASTCPEIPLPQPEGSDANVDVIVARVPCDGWSANKGLRDVFRLQVNLAAANLAVQSGLRTVNQAVYVVFIGSCGPMHEIFPCDERVMRVEDYWVYKPYLPRLKQKLLMPVGSCQIAPSFAQFGQEAWRPKHEDNLASKAVTALPRRLRVAYVTVLHSSEAYVCGAIALAQSIRQSGSHKDMILLHDHTITNKSLIGLSAAGWNLRLIDRIRSPFSQKDSYNEWNYSKLRVWQVTDYDKLVFIDADFIILKKLDHLFYYPQLSASGNDKVLFNSGIMVLEPSACMFKDLMEKSFKIESYNGGDQGFLNEIFVWWHRLSKRVNTMKYFDEKNHRRHDLPENVEGLHYLGLKPWVCYRDYDCNWDISERRVFASDSVHEKWWKVYDKMSEQLKGYCGLNKNMEKRIEKWRRIAKNNSLPDRHWEIEVRDPRKTNLLVQ", "text": "FUNCTION: May be involved in the substitutions of the xylan backbone in stem glucuronoxylan. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin subfamily."}
+{"protein": "MAASTDMAGLEESFRKFAIHGDPKASGQEMNGKNWAKLCKDCKVADGKSVTGTDVDIVFSKVKGKSARVINYEEFKKALEELATKRFKGKSKEEAFDAICQLVAGKEPANVGVTKAKTGGAVDRLTDTSRYTGSHKERFDESGKGKGIAGRQDILDDSGYVSAYKNAGTYDAKVKK", "text": "FUNCTION: Regulator of microtubule dynamic that has microtubule bundling activity (PubMed:17105200, PubMed:19633818). Required for embryo implantation; possibly by regulating beta-catenin (By similarity). Also required for decidualization via regulation of beta- catenin (PubMed:30667362). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TPPP family."}
+{"protein": "MTTFVKLRTKAKMPLVGLGTWKSPPGQVKEAVKAAIDAGYRHFDCAYVYQNESEVGEAIQEKIKEKAVRREDLFIVSKLWSTFFEKSLMKEAFQKTLSDLKLDYLDLYLIHWPQGLQAGKEFLPKDSQGKVLMSKSTFLDAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIAVIAYSPLGSPDRPYAKPEDPVVLEIPKIKEIAAKHKKTIAQVLIRFHVQRNVAVIPKSVTLSHIKENIQVFDFQLSEEDMAAILSLNRNWRACGLFVTSDEEDFPFHEEY", "text": "FUNCTION: Reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols (PubMed:21048316). Reduces prostaglandins (By similarity). May play a role in the metabolism of xenobiotic aromatic aldehydes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MAKNAMLCLLILSVVLALAFATNEKDDKEAGNLSTGIFGKAGRFVTVALAMSSRLGGAGASQGGGAVHGESLKSNQLQNAYRMALPPPMQIKSAEIDGWKPSPDEYLKKFAQEFRRNTGMKPQSYNEEKRVTPGGPDPLHNREKILEEQKRVTPGGPDPLHNREKTLEEQKRVTPGGPDPLHNREKTLEEQKRVTPGVPDRQHR", "text": "FUNCTION: [CLE1-1]: Mimics host plant CLE extracellular signal peptides that regulate cell fate. May play a role in the differentiation or division of feeding cells (syncytia) induced in plant roots during infection. SUBCELLULAR LOCATION: [CLE1-1]: Secreted Host cytoplasm Host extracellular space Secreted, extracellular space, apoplast Note=Present in secretory granules within the dorsal esophageal gland secretory cell and in the dorsal gland ampulla (collecting reservoir) at the base of the nematode stylet. Secreted into host root cells via the nematode stylet to transform the recipient cells into enlarged multinucleate feeding cells called giant-cells or syncytia. Secreted from the host cytoplasm to the host apoplasm via a plant secretory pathway. SIMILARITY: Belongs to the CLV3/ESR signal peptide family."}
+{"protein": "MKRKIIVACGGAVATSTMAAEEIKELCQSHNIPVELIQCRVNEIETYMDGVHLICTTARVDRSFGDIPLVHGMPFVSGVGIEALQNKILTILQG", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of GatA, GatB and GatC is involved in galactitol transport. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MGNSKSGALSKEILEELQLNTKFSEEELCSWYQSFLKDCPTGRITQQQFQSIYAKFFPDTDPKAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMITPEDVKLLPDDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEGTLANKEILRLIQFEPQKVKEKMKNA", "text": "FUNCTION: Acts as a calcium sensor and regulates phototransduction of cone and rod photoreceptor cells (By similarity). Modulates light sensitivity of cone photoreceptor in dark and dim conditions (By similarity). In response to high Ca(2+) levels induced by low light levels, prolongs RHO/rhodopsin activation in rod photoreceptor cells by binding to and inhibiting GRK1-mediated phosphorylation of RHO/rhodopsin (By similarity). Plays a role in scotopic vision/enhances vision in dim light by enhancing signal transfer between rod photoreceptors and rod bipolar cells (By similarity). Improves rod photoreceptor sensitivity in dim light and mediates response of rod photoreceptors to facilitate detection of change and motion in bright light (By similarity). SUBCELLULAR LOCATION: Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment Photoreceptor outer segment membrane; Lipid-anchor; Cytoplasmic side Perikaryon Note=Primarily expressed in the inner segments of light-adapted rod photoreceptors, approximately 10% of which translocates from photoreceptor outer segments upon light stimulation (By similarity). Targeting of myristoylated protein to rod photoreceptor outer segments is calcium dependent (By similarity). SIMILARITY: Belongs to the recoverin family."}
+{"protein": "MARKRTSKNDPLRMYLNYVRKLQTMGDAYDESAKYRIANFENGFKSLHMVENEFKQYLANVIDEAIKSGASPQDLPYVNEIKLALMKIFTSWLKYSNEKLGANEIAINVAGTATMTLTENLYGTRVSCEEAVSLINSIFAVWVGVEPFEAEEREGACLVTPRSPLPPVPISSPTGFSAPIQEVLQAKSPEEIIGVKGGA", "text": "FUNCTION: Self-assembles to form a helical, filamentous nucleocapsid (Probable) (PubMed:30135568). Together with capsid protein 1, wraps arounds the DNA and maintains it in an A-form (Probable) (PubMed:30135568). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable) (PubMed:30135568). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable). SUBCELLULAR LOCATION: Virion."}
+{"protein": "NKGLNPGMVVXLVVASFLLIFFVGNYALYXYAQKTLPPKKKKPVSKKKLKKEKLKQGVSAPGE", "text": "FUNCTION: DNA-binding protein that specifically recognizes a negative element (S1F) within the RPS1 promoter. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the S1FA transcription factor family."}
+{"protein": "MQSYKYDKAIVPESKNGGSPALNNNPRKGGSKRVLLICLDLFCLFMAALPFLIIETSTIKPYRRGFYCNDESIKYPLKVSETINDAVLCAVGIVIAILRIITGEFYRIYYLKEKSRSTIQNPYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCDPDFSQINCSEGYIQNYRCRGEDSKVQEARKSFFSGHASFSMFTMLYLVLYLQARFTWRGARLLRPLLQFTLLMMAFYTGLSRVSDYKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRREILSPVDIMDRSNHHNMV", "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": "MEKYHGLEKIGEGTYGVVYKAQNNYGETFALKKIRLEKEDEGIPSTTIREISILKELKHSNIVKLYDVIHTKKRLVLVFEHLDQDLKKLLDVCEGGLESVTAKSFLLQLLNGIAYCHDRRVLHRDLKPQNLLINREGELKIADFGLARAFGIPVRKYTHEVVTLWYRAPDVLMGSKKYSTTIDIWSVGCIFAEMVNGTPLFPGVSEADQLMRIFRILGTPNSKNWPNVTELPKYDPNFTVYEPLPWESFLKGLDESGIDLLSKMLKLDPNQRITAKQALEHAYFKENN", "text": "FUNCTION: Serine/threonine-protein kinase (PubMed:10722743, PubMed:12869562, PubMed:26094711). Involved in the control of the cell cycle (By similarity). Required for entry into S-phase and mitosis (By similarity). Probable component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (PubMed:12869562). In schizonts, phosphorylates ORC1 resulting in its dissociation from DNA, relocalization to the cytoplasm and likely its degradation (PubMed:26094711). FUNCTION: Serine/threonine-protein kinase (PubMed:8844681, PubMed:14604523). Involved in the control of the cell cycle (By similarity). Required for entry into S-phase and mitosis (By similarity). Probable component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity). In schizonts, phosphorylates ORC1 resulting in its dissociation from DNA, relocalization to the cytoplasm and likely its degradation (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "MHSCWKMKLQNEKTLGHSVSRSSNISKAGSPTSVSAPSSFPRTSVTPSSQDICRICHCEGDDESPLITPCHCTGSLHFVHQACLQQWIKSSDTRCCELCKFEFIMETKLKPLRKWEKLQMTASERRKIMCSVTFHVIAITCVVWSLYVLIDRTAEEIKMGQNNGILEWPFWTKLVVVAIGFTGGLLFMYVQCKVYVQLWKRLKAYNRVIYVQNCPETCKKKIFEKSVIIEPNLESKEALGIHHSDTNSSYYTEPEDCGAAILQV", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of cd86 and MHC class II proteins, such as hla-dr alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Early endosome membrane; Multi-pass membrane protein."}
+{"protein": "MGISMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSASLAVLPDNFPRYPVGKFFQYDTWRQSTQRLRR", "text": "FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3. FUNCTION: The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver. Acts as a ligand for integrin which is required for IGF2 signaling. Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity). Inhibits myoblast differentiation and metabolism via increasing the mitochondrial respiration rate (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
+{"protein": "MKVLEERNAFLSDYEVLKFLTDLEKKHLWDQKSLAALKKSRSKGKQNRPYNHPELQGITRNVVNYLSINKNFINQEDEGEERESSGAKDAEKSGISKMSDESFAELMTKLNSFKLFKAEKLQIVNQLPANMVHLYSIVEECDARFDEKTIEEMLEIISGYA", "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. The RPC25/RPC8-RPC17/RPC9 subcomplex may bind Pol III transcripts emerging from the adjacent exit pore during elongation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPC9 RNA polymerase subunit family."}
+{"protein": "MASELAMNNSDLPTSPLAMEYVNDFDLMKFEVKKEPVETDRIISQCGRLIAGGSLSSTPMSTPCSSVPPSPSFSAPSPASGSEQKAHLEDYYWMTGYPQQLNPEALGFSPEDAVEALISNSHQLQGGFDGYARGAQQLAAAAGAGAGASLGGSGEEMGPAAAVVSAVIAAAAAQSGGAPHYHHHHHHATGHHHHPTAGAPGAAGSASASASGAGGAGGGGPASAGGGGGGGGGGTAGAGGALHPHHAAGGLHFDDRFSDEQLVTMSVRELNRQLRGVSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHVLESEKNQLLQQVDHLKQEISRLVRERDAYKEKYEKLVSSGFRENCSSSDNPSSPEFFM", "text": "FUNCTION: Acts as a transcriptional activator or repressor. When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters. Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T-helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'- [GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT- rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells. It may interact with additional basic-zipper proteins that determine a subtype of Maf- responsive element binding (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Maf subfamily."}
+{"protein": "MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVNDTLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQLNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWANTYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVSYEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDHVFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKIILLCKISYVDTYPCRAAFI", "text": "FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer; paragloboside), resulting in the synthesis of Lc(3)Cer and neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family."}
+{"protein": "MKFQHTFIALLSLLTYANAYDYFTTTLANQNPVCASVDVIQNVCTEVCGRFVRYIPDATNTNQFTFAEYTTNQCTVQVTPAVTNTFTCADQTSSHALGSDWSGVCKITATPAPTVTPTVTPTVTPTVTPTPTNTPNPTPSQTSTTTGSASTVVASLSLIIFSMILSLC", "text": "FUNCTION: May bind F-actin and nucleates actin assembly. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the ponticulin family."}
+{"protein": "MPTDAKRPLQLNDQGQLRHFISLDGLPRELLTEILDTADSFLEVGARAVKKVPLLRGKTVCNVFFENSTRTRTTFELAAQRLSADVISLNVSTSSTSKGETLTDTLRNLEAMAADMFVVRHSDSGAAHFIAEHVSPNVAVINGGDGRHAHPTQGMLDMLTIRRHKGNFEQLSVAIVGDILHSRVARSNMLALKTLGCPDIRVIAPRTLLPIGLEEQYGVRVFTNADEGLKDVDVVIMLRLQRERMQGGLLPSEGEFFKLYGLTEKRLKLAKPDAIVMHPGPINRGVEIESAVADGAQSVILNQVTYGIAIRMAVLSMAMSGQNTQRQLEQEDAE", "text": "SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family."}
+{"protein": "GFFAFIPKIISSPLFKTLLSAVGSALSSSGEQE", "text": "FUNCTION: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis. SUBCELLULAR LOCATION: Secreted. Target cell membrane. Note=Forms a helical membrane channel in the prey. SIMILARITY: Belongs to the pardaxin family."}
+{"protein": "DLRANDLKRSQEIVESKSQRLDAGILDLEKRKFLVDQKEEYLIKLLEDVSGLTKYQAKELLIKQIKNKSEKELISILKNAELQAHSKAKIISNNILILAMERIKVELTSQRTTNIVKLPSDDLKGRIIGKDGRNMKTFEQIGGVDIVVDETPNVVVVSSFNPIRREIATRTLEQLIIDGRIQPVKIENELKKQEQELEYIIQETGLNTIKELNINDIDIELVKLIGKLKFRTSYGQNVLAHSIEVAKLSGAIASELGLDVEKAIRAGLLHDIGKAIDFEKQGSHVVLGAEIARKYNEDPIIINSIESHHEDKEKSSEIAAIVAIADSISASRPGARYNAIDEFILRMHEIEKIGNSIPGVAKTYALQSGRQIRLIVDPLVASDLDLALILEKMKEQIKNKVIIPGEITITVIREKKETDILK", "text": "FUNCTION: Endoribonuclease that initiates mRNA decay. SIMILARITY: Belongs to the RNase Y family."}
+{"protein": "MSDHFNFNEAFNSQTMRGRANVAKATWASLGLVYVLVKMHRRNTKRRETKLYCKGCQQAMLHG", "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. ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase required for dimerization of the ATP synthase complex and as such regulates ATP synthesis in the mitochondria. SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein."}
+{"protein": "MDKSGSPNASRTSRRRRPRRGSRSASGADAGLRALTQQMLKLNKTLAIGRPTLNHPTFVGSESCKPGYTFTSITLKPPEIEKGSYFGRRLSLPDSVTDYDKKLVSRIQIRINPLPKFDSTVWVTVRKVPSSSDLSVAAISAMFGDGNSPVLVYQYAASGVQANNKLLYDLSEMRADIGDMRKYAVLVYSKDDNLEKDEIVLHVDVEHQRIPISRMLPT", "text": "FUNCTION: Capsid protein. Probably binds RNA and plays a role in packaging (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the cucumovirus capsid protein family."}
+{"protein": "MSDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGDVMEGISVGTLFHAQATPLENRKRWIFGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDIAHGVSRYNSDALRRIAGHHSQEIDAILGYEYGPVAVHRDDMITR", "text": "FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. 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": "MRNALASFGQIVLAAVVASGVAAVSLIAIARVHWPAFPSSNQLHALTTVGQVGCLTGLLAVGGVWQAGRFRRLAQLGGLVFVSAFTVVTLGMPLGATKLYLFGISVDQQFRTEYLTRLTDSAALQDMTYLGLPPFYPPGWFWIGGRVAALTGTPAWEIFKPWAITSITIAVAITLVLWWQMIRFEYALLVTIATAAVTLVYSSPEPYAAMITVLLPPALVLTWSGLRAAEREADRTLGNKRGWATVVGAGIFLGFAATWYTLLLAYTAFTVVLMTLLLATALCRRAGFRATFDPLRRLAGIVVIAAAIGAITWLPFLARAAHDPVSDTGSAQHYLPADGAELAFPMLQFSLLGMICMLGTLWLIVRTSSSVRASALMISVLAVYLWSLLSILTTLARTTLLSFRLQPTLTVLLVTAGVFGFIETAQSLAKHNRAVLSVASAIGLAGAIAFSQDIPNVLRPDLTIAYTDTDGHGQRGDRRPPGSEKYYWAIDEAVLHITGKPRDQTVVLTADYSFLAYYPYWGFQGLTSHYANPLAQFDLRAAQIQQWSRLTTASELIHALDTLPWPPPTVFVMRHGAGNTYTLRLAKNVYPNQPNVRRYTVDLPAALFADQRFAVQDIGPFVLAIRKPMGNA", "text": "FUNCTION: Involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacterial cell wall. 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. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 85 family."}
+{"protein": "MCNFVFCFGSHNKKLLSDRIKSSKKGWYLYLGKKYRIGIKIITLSGRKYISVNFNKSIEFMKFLVRKNIHCNIFDQSHKCKSHNHYKNYLRYIIDNKCMDHIKIFYGKFFPLIRSQGRINNIIDIAKPLVLFENYTVDMDLGIDQETIMCIFKYGKMIDMASLLIHVLCTISDVTIEFLDDMLSIYRHKIIKLLTKEKHELDNDFNIMPMDVFLIPSFRNDDVDMFYFVVEEMFKLHDYIDTGNLTERELNVFNIFVYKLNADTINATINTHLIGLNHIHDFLVFYCPKIFNQLVLKLNDETSLNESIIFDILQLDFIEYMITVCETIGNNNPKILNKFLRYAKSTEMAQLLIDYDADYEKLYKSSKFHECNDCVKHFIENLVEETIDT", "text": "SIMILARITY: Belongs to the mimivirus L17x/L18x family."}
+{"protein": "MVFDPRTLDNPKEISAYRDQRYQGTVRDQETALRTSCTLYVGNLSYYTKEDQVYELFGRAGDVRRVIMGLDRFKKTPCGFCFVEYYTREDAELALQNISNTRMDDRVIRADWDAGFIEGRQYGRGKHGGQVRDEYRKDYDPERGGYNRAIAQKGGDRQ", "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 and is required for primary microRNAs (miRNAs) processing. In the CBC complex, ncbp-2 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires ncbp-1 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": "MVTTPRLVSLLLLLALCAAAAGALRLPPDASFPGAQAERLIRALNLLPKDSSSSSGRHGARVGEGNEDVAPGQLLERRVTLPGLPEGVADLGHHAGYYRLPNTHDARMFYFFFESRGKKEDPVVIWLTGGPGCSSELAVFYENGPFTIANNMSLVWNKFGWDKISNIIFVDQPTGTGFSYSSDDRDTRHDETGVSNDLYDFLQVFFKKHPEFIKNDFFITGESYAGHYIPAFASRVHQGNKKNEGTHINLKGFAIGNGLTDPAIQYKAYTDYALEMNLIQKADYERINKFIPPCEFAIKLCGTNGKASCMAAYMVCNTIFNSIMKLVGTKNYYDVRKECEGKLCYDFSNLEKFFGDKAVRQAIGVGDIEFVSCSTSVYQAMLTDWMRNLEVGIPALLEDGINVLIYAGEYDLICNWLGNSRWVHSMEWSGQKDFAKTAESSFLVDDAQAGVLKSHGALSFLKVHNAGHMVPMDQPKAALEMLRRFTQGKLKEAVPEEESSTTSFYAAM", "text": "SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm. SIMILARITY: Belongs to the peptidase S10 family."}
+{"protein": "MKFFIFTCLLAVALAKHKMEHVSSSEEPINIFQEIYKQEKNMAIHPRKEKLCTTSCEEVVRNANEEEYSIRSSSEESAEVAPEEIKITVDDKHYQKALNEINQFYQKFPQYLQYPYQGPIVLNPWDQVKRNAGPFTPTVNREQLSTSEENSKKTIDMESTEVFTKKTKLTEEEKNRLNFLKKISQYYQKFAWPQYLKTVDQHQKAMKPWTQPKTNAIPYVRYL", "text": "FUNCTION: Important role in the capacity of milk to transport calcium phosphate. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-casein family."}
+{"protein": "MQMGVAVLVLVIACGVVSVLFAIWAIRSVLAADQGTQRMQEIAEAIREGASAYLTRQYSTIAIVGVVVFLAAWYLLSISAAIGFLIGAVLSGVTGFIGMHVSVRANVRTAQAASLSLAGGLELAFKSGAITGLLVAGLALLGVSVYYFILTVWLGYSPSDRTVIDALVSLGFGASLISIFARLGGGIFTKGADVGGDLVGKVEAGIPEDDPRNPATIADNVGDNVGDCAGMAADLFETYAVTVVATMVLGAIFFNGSDILSSVMLYPLMICGACVITSIVGTFFVKLGVNGSIMGALYKGLIATGLLSIVGLAIANTLTVGWGEIGTVAGKSITGTNLFLCGLIGLIVTGLIVVITEYYTGTNKRPVNSIAQASVTGHGTNVIQGLAVSLESTALPAIVIVGGIISTYQLAGLFGTAIAVTAMLGIAGMIVALDAFGPVTDNAGGIAEMAGLDPEVRKATDALDAVGNTTKAVTKGYAIGSAGLGALVLFAAYSNDLAYFAANGQTYPYFADMGPVSFDLSNPYVVAGLIFGGLIPYLFGGMAMTAVGRAGGAVVQEVRRQFREKPGIMTGKERPDYARAVDLLTRAAIREMIIPSLLPVLAPIVVYFGVLLISGSKAAAFAALGASLLGVIVNGLFVAISMTSGGGAWDNAKKSFEDGFTDADGVKHLKGSEAHKASVTGDTVGDPYKDTAGPAVNPAIKITNIVALLLLAVLAHMS", "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 inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-insensitive subfamily."}
+{"protein": "MTAPPVHDRAHHPVRDVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTTTDVENYPGFRNGITGPELMDEMREQALRFGADLRMEDVESVSLHGPLKSVVTADGQTHRARAVILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFFRDQDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEFRASKIMLDRARNNDKIRFLTNHTVVAVDGDTTVTGLRVRDTNTGAETTLPVTGVFVAIGHEPRSGLVREAIDVDPDGYVLVQGRTTSTSLPGVFAAGDLVDRTYRQAVTAAGSGCAAAIDAERWLAEHAATGEADSTDALIGAQR", "text": "FUNCTION: Essential thiol-reducing enzyme that protects the cell from thiol-specific oxidizing stress. Plays a minor role in defense against oxidative and nitrosative stress. Is essential to establish and maintain infection in mice. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MAKKDGNQEEEISQMEEGNIHSASNSDSNVGFCSSVSVVVILQKLIAEAIGTYFVIFAGCGSVAVNKIYGSVTFPGICVTWGLIVMVMVYTVGYISGAHFNPAVTITFSIFGRFPWKQVPLYIIAQLMGSILASGTLALLFDVTPQAYFGTVPVGSNGQSLAIEIIISFLLMFVISGVATDDRAIGQVAGIAVGMTITLNVFVAGPISGASMNPARSIGPAIVKHVYTGLWVYVVGPIIGTLAGAFVYNLIRSTDKPLRELAKSASSLRS", "text": "FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. NIP (TC 1.A.8.12) subfamily."}
+{"protein": "MKRKMLKRLLTSAFACMFIANGLITTTVRAVGPKTGEENQVLVPNLNPTPENLEVVGDGFKITSSINLVGEEEADENAVNALREFLTANNIEINSENDPNSTTLIIGEVDDDIPELDEALNGTTAENLKEEGYALVSNDGKIAIEGKDGDGTFYGVQTFKQLVKESNIPEVNITDYPTVSARGIVEGFYGTPWTHKDRLDQIKFYGENKLNTYIYAPKDDPYHREKWREPYPENEMQRMQELIDASAENKVDFVFGISPGIDIRFDGEAGEEDFNHLIAKAESLYDMGVRSFAIYWDDIQDKSAAKHAQVLNRFNEEFVKAKGDVKPLITVPTEYDTGAMVSNGQPRTYTRIFAETVDPSIEVMWTGPGVVTNEIPLSDAQLISGIYNRNMAVWWNYPVTDYFKGKLALGPMHGLDKGLNQYVDFFTVNPMEHAELSKISIHTAADYSWNMDNYDYDKAWNRAIDMLYGDLAEDMKVFANHSTRMDNKTWAKSGREDAPELRAKMDELWNKLSSKEDASALIEELYGEFARMEEACNNLKANLPEVALEECSRQLDELITLAQGDKASLDMIVAQLNEDTEAYESAKEIAQNKLNTALSSFAVISEKVAQSFIQEALSFDLTLINPRTVKITASSEETSGENAPASFASDGDMNTFWHSKWSSPAHEGPHHLTLELDNVYEINKVKYAPRQDSKNGRITGYKVSVSLDGENFTEVKTGTLEDNAAIKFIEFDSVDAKYVRLDVTDSVSDQANGRGKFATAAEVNVHGKLKEAAEVTGSVSLEALEEVQVGENIEVGVGIDELVNAEAFAYDFTLNYDENAFEYVEAISDDGVFVNAKKIEDGKVRVLVSSLTGEPLPAKEVLAKVVLRAEAKTEGSNLSVTNSSVGDGEGLVHEIAGTEKTVNIIEGTSPEIVVNPVRDFKASEINKKNVTVTWTEPETTEGLEGYILYKDGKKVAEIGKDETSYTFKKLNRHTIYNFKIAAKYSNGEVSSKESLTLRTAR", "text": "FUNCTION: Binds carbohydrates. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O- glycosylated peptides from mammals. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates (in vitro). SIMILARITY: Belongs to the glycosyl hydrolase 84 family."}
+{"protein": "MAVDITLLFRASVKTVKTRNKALGVAVGGGVDGSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKDYINAYSHTMSEYGRMTDTERDQIDQDAQIFMRTCSEAIQQLRTEAHKEIHSQQVKEHRTAVLDFIEDYLKRVCKLYSEQRAIRVKRVVDKKRLSKLEPEPNTKTRESTSSEKVSRSPSKDSEENPATEERPEKILAETQPELGTWGDGKGEDELSPEEIQMFEQENQRLIGEMNSLFDEVRQIEGRVVEISRLQEIFTEKVLQQEAEIDSIHQLVVGATENIKEGNEDIREAIKNNAGFRVWILFFLVMCSFSLLFLDWYDS", "text": "FUNCTION: Syntaxin 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 Golgi apparatus membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the syntaxin family."}
+{"protein": "MHRLQVVLGHLAGRPESSSALQAAPCSARFPQASASDVVVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDDKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN", "text": "FUNCTION: Responsible for the thiolytic cleavage of straight chain 3- keto fatty acyl-CoAs (3-oxoacyl-CoAs) (Probable). Plays an important role in fatty acid peroxisomal beta-oxidation (Probable). Catalyzes the cleavage of short, medium, long, and very long straight chain 3- oxoacyl-CoAs (By similarity). SUBCELLULAR LOCATION: Peroxisome Note=Transported into peroxisomes following association with PEX7. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
+{"protein": "MSSPNIWSTGSSVYSTPVFSQKMTLWILLLLSLYPGLTRQKSDDDYEDYASNKTWVLTPKVPEGDVTVILNNLLEGYDNKLRPDIGVKPTLIHTDMYVNSIGPVNAINMEYTIDIFFGQTWYDRRLKFNSTIKVLRLNSNMVGKIWIPDTFFRNSKKADAHWITTPNRMLRIWNDGRVLYTLRLTIDAECQLQLHNFPMDEHSCPLEFSSYGYPREEIVYQWKRSSVEVSDTRSWRLYQFSFVGLRNTTEVVKTTSGDYVVMTVYFDLSRRMGYFTIQTYIPCTLIVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCFIFVFSALVEYGTLHYFVSNRKPSKDKDKKKKNPLLRMFSFKAPTIDIRPRSATIQMNNATHLQERDEEYGYECLDGKDCASFFCCFEDCRTGAWRHGRIHIRIAKMDSYARIFFPTAFCLFNLVYWVSYLYL", "text": "FUNCTION: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain (By similarity). Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel (By similarity). The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta2/gamma2 receptor, alpha2/beta2/gamma2 receptor and the alpha1/beta3/gamma2 receptor exhibit synaptogenic activity whereas the alpha2/beta3/gamma2 receptor shows very little or no synaptogenic activity (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine (By similarity). SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Cell projection, dendrite Cytoplasmic vesicle membrane. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRG2 sub- subfamily."}
+{"protein": "MKEYNIVITGVGGQGILTAANLLGWAALRAGYKVRVGEVHGMSQRFGSVIAYVRFGEDVYGAMVPEGKADVILSFEPVEALRYINYLKKGGLVFTNARPIPPVQVSMGLATYPTLDEMKKIVEEDFGGKFMAFDAEKLAMEAGNIVTTNVVLIGALSQTPGFPLSEEQIKEVIRISVPPKTIDVNMRAFELGVKAAKEMLGL", "text": "FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates."}
+{"protein": "MARLGALVCCLLAAWHCRPGLGLPLAPAGTGPAVGQFWHVTDFHLDPTYHITGDHTKVCASSKGAEASDPGPFGDVMCDSPYRLIFSALDFIKNSGQKVSFMIWTGDSPPHVPVLELSTDKVINVTANITTTIQRLFPNLQVFPALGNHDYWPQDQLPVVNSKVYNAVANLWKPWLTEDAITTLRKGGFYTQKVSNNPKLRIISLNTNLYYGPNSVTLNQTDPANQFEWLENTLNISQQNKEKVYIIAHVPVGYLPYARGISAMRKYHNEKLIDIFRKYSDIIAGQFYGHTHRDSIMVLSDKKGKPVNSLFVAPAVTPVRSVLERLTNNPGVRLFQYDPRDYKLLDMLQYYLNLTDANLKGESNWKLEYNLTQAYDIQDLQPKSLYKLAKQFAIQESKQFIKYYKYFFVSYDSSVICQGKCKIFQICAIMNLDVISYTDCFRQYHMKHRL", "text": "FUNCTION: Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP. Has in vitro activity with p- nitrophenyl-TMP. Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates. Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine. Does not have sphingomyelin phosphodiesterase activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the acid sphingomyelinase family."}
+{"protein": "MNHERILEKRETILQYCHRLTEMHRAALFDEEESPRNLSLQQLRKNIHICLKDLCRLNTWLTEQDGGFRKALGSLERYESKLAALLAKERQLGEERQAWEAAVPAGAGDDSGGVFTVHGGHQRHLNAYIESMGVDNTGLGKEPDALPRLSRQQALGHVAVLRLAQAAVSREISQAEGLLKSFRKDQTFIKAELAKLEAFVRAQKLAVERELEGVRRSQEHIFRKIGLLKLPAREREPLGLGRRPAADLESMKAQMEEFLHVRKSALKAMLSEHKQETQLLKSQQEVWKEVTTLVEDLEDRIRTRFATAAKVDPVELRRLITDAITQIKSLHYEESYPDVLTCIRDEIAALEKANDQLPFSKQKSITDKLVPVNTGAGFLVNSTSPPKVGLTKSIVPSSSMATNKKSV", "text": "FUNCTION: Required for cytoplasm to vacuole transport (Cvt) vesicle formation and efficient autophagy. Plays a role in ATG protein retrieval from the pre-autophagosomal structure (PAS) and is especially required for autophagy-dependent cycling of ATG9. Also plays a role in regulation of filamentous growth (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG23 family."}
+{"protein": "MTTWILDKSAHVRLVAGATPPAGIDLTDLAICDIGELEWLYSARSATDYDSQQTSLRAYQILRAPSDIFDRVRHLQRDLAHHRGMWHRTPLPDLFIAETALHHRAGVLHHDRDYKRIAVVRPGFQACELSRGR", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. The cognate antitoxin is VapB17 (By similarity). SIMILARITY: Belongs to the PINc/VapC protein family."}
+{"protein": "KKEGYLVGNDGCKYSCFTRPAQYCVHECELRKGTDGYCYAWLACYCYNMPDHVRTWSRATNRCGS", "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. This toxin is lethal to mice. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family."}
+{"protein": "MFQKLLLSVFIILLMDVGERVLTFNLLRHCNLCSHYDGFKCRNGMKSCWKFDLWTQNRTCTTENYYYYDRFTGLYLFRYAKLNCKPCAPGMYQMFHDLLRETFCCIDRNYCNDGTANLDTSSILIEDMNQKKELNDD", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the PATE family."}
+{"protein": "MKAKEVSLVALFVALTSVGAQISVSIGPVPLTLQVFFVILAGLVLGPKLGFLSILIYDILGALGIPVFAGFSGGIAHILGPTGGYIIAFPIATFIAGLGRGKVRYLTSLMGLLVIYLIGWMWLARFVGFNKAFILGVLPFIVPDIVKAATAVIIAERLQGNT", "text": "FUNCTION: Probable biotin transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BioY family."}
+{"protein": "MKFSELGLSDSLLKAIKRSGYEEATPIQEQTIPMVLEGKDVIGQAQTGTGKTAAFGLPIIENVDTENPNIQAIIISPTRELAIQTQEELYRLGKDKHVRVQVVYGGADIRRQIKSLKQHPQILVGTPGRLRDHINRHTVKLDHIKTLVLDEADEMLNMGFLEDIESIIKETPDDRQTLLFSATMPPEIKRIGVQFMSDPETVRIKAKELTTDLVDQYYVRARDYEKFDIMTRLIDVQDPDLTIVFGRTKRRVDELSKGLIARGYNAAGIHGDLTQDKRSKIMWKFKNNELDILVATDVAARGLDISGVTHVYNYDIPSDPDSYVHRIGRTGRAGHHGVSLTFVTPNEMDYLHEIEKLTRVRMLPLKPPTAEEAFKGQVASAFNDIDELIAQDSTDRYEEAAEKLLETHNATDLVAALLNNMTKEAASEVPVKITPERPLPRRNKRNNRNGNRNNSHGGNHYRRKNFRRHQHGSHRNDNHGKSHSSRHSFNIRHRKEN", "text": "FUNCTION: DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity (By similarity). Over-expression leads to cell aggregation. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Extracellular side. SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily."}
+{"protein": "MSKKFTMTLLSSSLAGLLVMSGGVSAQEEKYTVPYAIGEGKWGNTYEVVKTGGNGNFRYEVKEKNGKKRSLFTFDSKGDVIINGSGITYTIHDGALNDFAQTAEKKKNGQSQSHRMTDSVVRDVYNKVYSLQRTKITGFSVEDGENGKVSLGSDAKASGEFSVAVGTGARADKKFATAVGSWAAADGKQSTALGVGAYAYANASTAAGTAAYVDGSAIYGTAIGNYAKVDENATEGTALGAKATVTNKNSVALGANSVTTRDNEVYIGYKTGTESDKTYGTRVLGGLSDGTRNSDAATVGQLNRKVGGVYDDVKARITVESEKQKKYTDQKTSEVNEKVEARTTVGVDSDGKLTRAEGATKTIAVNDGLVALSGRTDRIDYAVGAIDGRVTRNTQSIEKNSKAIAANTRTLQQHSARLDSQQRQINENHKEMKRAAAQSAALTGLFQPYSVGKFNATAAVGGYSDQQALAVGVGYRFNEQTAAKAGVAFSDGDASWNVGVNFEF", "text": "FUNCTION: Binds (in a non-immune fashion) to the Fc portion of human IgG and less well to IgA; binding occurs on the cell surface. Confers the ability to survive exposure to human serum exposure (PubMed:10722621). Binds to the Fc portion of human IgG and IgA and to whole mouse antibodies also via Fc (PubMed:19303642). SUBCELLULAR LOCATION: Cell surface Cell outer membrane; Multi-pass membrane protein Note=The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface. SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family. Eib subfamily."}
+{"protein": "MNKKTLLVIFFVTMLIVDEVNSFRFGSFLKKVWKSKLAKKLRSKGKQLLKDYANKVLNGPEEEAAAPAERRR", "text": "FUNCTION: Amphipathic peptide that shows bradykinin potentiating activity and antimicrobial activities against bacteria and fungi. Has higher antibacterial activities against Gram-negative than against Gram-positive bacteria. Also inhibits NADPH oxidase-dependent superoxide production (IC(50) is 0.4 uM on granulocytes stimulated with PMA, IC(50) is 0.51 uM on HL-60 cells undifferentiated and IC(50) is 0.53 uM on HL-60 cells treated with DMSO). The C-terminal peptide shows a higher bradykinin potentiating activity than the complete peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Long chain multifunctional peptide (group 2) family."}
+{"protein": "MEFVFFLGCIAPNRYPGIEKATYITMEKLGIKLHPFEKASCCPAPGVFGSFDLKTWLTLAARNLCMAEEVEMDILTICNGCYGSLYEANHLLKENEKARKMVNEILSKYGLEYKGKVRVRHLPEVLYYDLGVDRIKEEITNPLNVNVAVHYGCHYLKPTDIKKLESSERPRSFDELVEALGAVSVNYKDKNMCCGAGGGVRARNLDVALKMTKTKLENIKEAKADCITEVCPFCHLQFDRGQVEIKEKFGEEYNIPVIHYSQLLGLAMGMSPKDVALDLHFIPTDEFIKKIDRH", "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 HdrB family."}
+{"protein": "MATEEDVKQRQIIESRARNISHNVRCTECGSQSIEDSQADIAILLRKLIRDEIKSGKSDKEIYKKLQADYGETILYTPKFDLQTAAIWLSPVIVGGVAAGVWAYKKHRQRTNVHIMALNLVRGVPLTPREKETMLDVLTPPPPANKWWWPGK", "text": "FUNCTION: Plays a role in mitochondrial cytochrome c maturation. Probable component of a heme lyase complex involved in the reduction of apocytochrome c. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CcmH/CycL/Ccl2/NrfF family."}
+{"protein": "MGYYSLTEVTAVQYAKEHGYFEKKANVVCHEIGDGNLNYVFKLDDGEKSIIIKQALPYAKVVGESWPLSIKRATIESKALQIFAKYVPEYVPVVYSHDEELAVTVIEDLSRLTITRKGLIDGEEYPLLSQHIGRFLANVLFYTSDFGLQSEEKRVLEGTFVNPDLCKITEDLVFTDPFGHYDTNDYEPELQLTIDELWSDKTLKLKVAQYKYKFLTRKEALIHGDLHTGSIFSSPSETKVIDPEFATYGPFGFDIGQFIANLLLNALSREEEQRGVLFFHIEKTWSYFVETFTKLWIGEGVEAYTKEKQWLPIILQNIFTDAVGFAGCELIRRTIGLAHVADLDEITNKETRIQAKKQALSLGKELIKYESKNADIQLFRTLFQQTVSGGIKA", "text": "FUNCTION: Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate. SIMILARITY: Belongs to the methylthioribose kinase family."}
+{"protein": "MMTKVGEVLLLLLLPAFVPHTDGTHYSLPGKPTEIKCRSPEKETFTCWWKPGSDGGLPTTYALYYRKEGSDVVHECPDYHTAGKNSCFFNKNNTLIWVSYNITVVATNALGKTYSDPQDIDVVYIVQPHPPEKLEVTVMKDQGWPFLRVSWEPPRKADTRSGWITLIYELRVKLEDEESEWENHAAGQQKMFNIFSLRSGGTYLIQVRCKPDHGFWSEWSSTSYVKVPEYLHREKSVWILVLVFSAFILLLLTWLIHMNSHSLKHCMLPPVPGPKIKGFDKQLLKSGKSDEVFSALVVSDFPPTTSNYEDLLVEYLEVYMPEQQELMVDKGKDHDGCLKSIGSASDSDSGRGSCDSDNLLMDKSGAPKEEQQQQNQEGDQIGKETQGPKEAWEKEAMPCANEDVVSPDASSEKVKTWPSVFSPVTPYSPLDPHNSLEMHKQHCLSNTQFPPGSPSSDHYIKEALQSSYWEVCFNNNQPYPQTEVHPQLQAHSDRNISAVNDRNAPTGLLLPTRMTEYVEVQRVNEENKVLLHPIPSGHSREKACPWVGQRDDYSKVKGVDSDNGLLLQREVVEEESMEMAGAAESCYTSSIAFTTPKQTACSPVALPVQDERVLAVSGYVDTATVFSVHT", "text": "FUNCTION: This is a receptor for the anterior pituitary hormone prolactin. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 1 subfamily."}
+{"protein": "MGNEFIASASISFIITLIGLTLGFALLKLQGE", "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 PetM family."}
+{"protein": "MKTPARRSKRVNQEESETNVTTRVVLRTRKTNCSKTRAARVRPDYPLTRTTSESEMKLMPPEFFQIDALDLAPRLLGKFMRRDNVVLRITEVEAYRPNDSACHGRFGVTPRTAPVFGPGGHAYVYLCYGLHMMLNIVADKEGVGAAVLIRSCSPVSGMETIQERRGLKTDKPVLLNGPGKVGQALGLSTEWSHHPLYSPGGLELLDGGEDVEKVMVGPRVGIDYALPEHVNALWRFAVADTPWISAPKNTLKPL", "text": "FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA glycosylase MPG family."}
+{"protein": "MAKTPSDHLLSTLEELVPYDFEKFKFKLQNTSVQKEHSRIPRSQIQRARPVKMATLLVTYYGEEYAVQLTLQVLRAINQRLLAEELHRAAIQEYSTQENGTDDSAASSSLGENKPRSLKTPDHPEGNEGNGPRPYGGGAASLRCSQPEAGRGLSRKPLSKRREKASEGLDAQGKPRTRSPALPGGRSPGPCRALEGGQAEVRLRRNASSAGRLQGLAGGAPGQKECRPFEVYLPSGKMRPRSLEVTISTGEKAPANPEILLTLEEKTAANLDSATEPRARPTPDGGASADLKEGPGNPEHSVTGRPPDTAASPRCHAQEGDPVDGTCVRDSCSFPEAVSGHPQASGSRSPGCPRCQDSHERKSPGSLSPQPLPQCKRHLKQVQLLFCEDHDEPICLICSLSQEHQGHRVRPIEEVALEHKKKIQKQLEHLKKLRKSGEEQRSYGEEKAVSFLKQTEALKQRVQRKLEQVYYFLEQQEHFFVASLEDVGQMVGQIRKAYDTRVSQDIALLDALIGELEAKECQSEWELLQDIGDILHRAKTVPVPEKWTTPQEIKQKIQLLHQKSEFVEKSTKYFSETLRSEMEMFNVPELIGAQAHAVNVILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVGDKTAWILGACKTSISRKGNMTLSPENGYWVVIMMKENEYQASSVPPTRLLIKEPPKRVGIFVDYRVGSISFYNVTARSHIYTFASCSFSGPLQPIFSPGTRDGGKNTAPLTICPVGGQGPD", "text": "FUNCTION: Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923, PubMed:16037825, PubMed:27030597, PubMed:28835462, PubMed:16785446, PubMed:17431422, PubMed:26347139). Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy (PubMed:16785446, PubMed:17431422, PubMed:26347139). Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation (PubMed:16785446, PubMed:17431422, PubMed:26347139). However, it can also have a positive effect in the inflammatory pathway, acting as an innate immune sensor that triggers PYCARD/ASC specks formation, caspase-1 activation, and IL1B and IL18 production (PubMed:16037825, PubMed:27030597, PubMed:28835462). Together with AIM2, also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). It is required for PSTPIP1-induced PYCARD/ASC oligomerization and inflammasome formation (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton Cell projection, ruffle Cell projection, lamellipodium Nucleus Cytoplasm Cytoplasmic vesicle, autophagosome Note=Associated with microtubules and with the filamentous actin of perinuclear filaments and peripheral lamellar ruffles (PubMed:11468188). In pre- apoptotic cells, colocalizes with PYCARD/ASC in large specks (inflammasomes) (PubMed:11468188). In migrating monocytes, strongly polarized at the leading edge of the cell where it colocalizes with polymerizing actin and PYCARD/ASC (PubMed:11468188)."}
+{"protein": "MDEAKEENRRLKSSLSKIKKDFDILQTQYNQLMAKHNEPTKFQSKGHHQDKGEDEDREKVNEREELVSLSLGRRLNSEVPSGSNKEEKNKDVEEAEGDRNYDDNEKSSIQGLSMGIEYKALSNPNEKLEIDHNQETMSLEISNNNKIRSQNSFGFKNDGDDHEDEDEILPQNLVKKTRVSVRSRCETPTMNDGCQWRKYGQKIAKGNPCPRAYYRCTIAASCPVRKQVQRCSEDMSILISTYEGTHNHPLPMSATAMASATSAAASMLLSGASSSSSAAADLHGLNFSLSGNNITPKPKTHFLQSPSSSGHPTVTLDLTTSSSSQQPFLSMLNRFSSPPSNVSRSNSYPSTNLNFSNNTNTLMNWGGGGNPSDQYRAAYGNINTHQQSPYHKIIQTRTAGSSFDPFGRSSSSHSPQINLDHIGIKNIISHQVPSLPAETIKAITTDPSFQSALATALSSIMGGDLKIDHNVTRNEAEKSP", "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."}
+{"protein": "MAAKAVDKLPVTFGSFVHQIPEGFYPGEDSTLPASVTIFPNVDLGGPLIQMSGVTGDGMISVDMNNDKRSLDFSYSSNYPLAPRTQPIAYMGKISIDHQYSGSGWNTEGIFNLVSAASLLGVPPSSCSSTSSSNASSGSPNLSCSMSHPQSDLEHIYSPPPYSSCNEIYQDPLRFPCGSPTAASLPPPPSYPSPKGASDGGMFPMIPDYSALFPPQCQRDLHSDRKPFPCPRHPSPLSTIRNFTLGGSSEGPRLASAYSPQNLPLRPILRPRKYPNRPSKTPVHERPYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDYCGRKFARSDERKRHTKIHLRQKERKNSATAAWRQHVARTSLKPQSGRDRQPCALLGPAAAHWDSIDPNRTG", "text": "FUNCTION: Sequence-specific DNA-binding transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family."}
+{"protein": "MAARSLMRILLVGLGLTLATIISGALVTISASATVCSSWPLCLEELVQSQNPLVWISLLHRLFVALALLAVFAGLVAVWRSSDTAGLPRITAGIAAAFFLLQALAGALLVWGVPAMVADVWHLSGALLAFGAQSLTIALIAVPTPATPERLAGRAAQMQRRLRSLAWWSAAAAGVAALAIGARSVVPGFGMMTAVPTNSVSAVGFAALLSVWMALEARRRLRPVAETPALALALPRYSLFLPALALLALLGAFIPVAGHLISLTAIALLWAATIIAAVILQRVPFSFATATAGVRSQPAWRTVVADYISLTKPKVISLLLVTTLTTMFITEAGLPSWWLVIWTMIGGYLAAGGAGAINCAFDSDIDINMGRTSRRPVPSGRISRRAAFIFGLILSVLSIIVLWVFTTPLAAFFALLGIIYYAWFYTGWLKRSTWQNIIIGGGAGAIPPLVGWTAVTGSVSLMAVVLFAIIFYWTPPHFWALALVKQKDYARAGVPMLPVVAGEAETRWQILVYSAIMVAVSLLPVAIGAMSWIYLIGAVVLGLRFMRDAWAVWRVGDQAAIWGLYKYSLLYLALVFAAMVADRLIIG", "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: In the C-terminal section; belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily."}
+{"protein": "MAEDAVVSDAVVVSDAMSSVAKGAPVTAQRPVRDDLEKHIPKPYLARALVAVDVNNPEGTKGGRHEHGQKSVLQQHVSFFDQNGDGIIYPWETFRGLRRLGFNLIVSFIVAIGIHTGLSYPTLPTWRPSLLFPVYIDRIHKAKHGSDTATFDTEGRFMPVNFENIFSKNARSQPDKLTLREIWMMTNDHRLAYDPFGWVANKGEWILLYMLAKDDEGYLPKEAIRGVYDGSLFEFLAEQRTKKAHGKQH", "text": "FUNCTION: Calcium-binding peroxygenase involved in cutin monomers biosynthesis. Can catalyze epoxidation of fatty acid and sulfoxidation reactions that can proceede competitively, although in favor of the sulfoxidation. Can only use unsaturated fatty acids with double bonds in the cis configuration as substrates. The preferred substrate is oleic acid and is inactive toward ricinoleic acid. Free fatty acid and fatty acid methyl esters are effective substrate forms, but not phospholipids and acyl-CoA. Hydroperoxy-trienoic (HPOT) acids are preferred over Hydroperoxy-dienoic (HPODT) acids as oxygen donors. SUBCELLULAR LOCATION: Microsome membrane. Lipid droplet. SIMILARITY: Belongs to the caleosin family."}
+{"protein": "MGCFNSKEAGAGRPKTTTQQQQQATPEPTVTTAEVRADEKISMDQDISQGNVEDFYVVGKELGRGAFSVVREGTRKTTSDKVALKYIEKKFVKKKHIEQLRREIDIMKKVKHENVLSLKEIFESDSHLTLVMELVTGGELFYKIVERGSFTEKGARNVVRQVCAGVEYLHSQGIAHRDLKPENLLCNGEGEDMTIKIADFGLSKIFGTGEALETSCGTPDYVAPEVLTGGSYDNAVDMWSIGVITYILLCGFPPFYASSQNLLFEKILTADYDFPEPEWTHVSEHAKAFIRNLIVKDPDQRHTAKQCLDDLWLSGSDQSIGSAADLHSHFAEKMKKYNDQRRGGQSSNN", "text": "FUNCTION: May phosphorylate a specific serine in the N-terminus of a myosin light chain. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily."}
+{"protein": "MASSSGNDDDLTIPRAAINKMIKETLPNVRVANDARELVVNCCTEFIHLISSEANEICNKSEKKTISPEHVIQALESLGFGSYISEVKEVLQECKTVALKRRKASSRLENLGIPEEELLRQQQELFAKARQQQAELAQQEWLQMQQAAQQAQLAAASASASNQAGSSQDEEDDDDI", "text": "FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NC2 beta/DR1 family."}
+{"protein": "MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPEVTLKAADLEDTTEEETAKDNGEVEDQEEKEDAEKENAEKDEDDVEQELANLDPTWVESPKANGHIENGPFSLEQQLEDEEDDEDDCANPEEYNLDEPNAESDYTYSSSYEQFNGELPNGQHKTSEFPTPLFSGPLEPVACGSVISEGSPLTEQEESSPSHDRSRTVSASSTGDLPKTKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS", "text": "FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing (PubMed:9446799). Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression (PubMed:19592491). This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (By similarity). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (By similarity). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (By similarity). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Nucleus speckle Chromosome Note=Shuttles between the nucleus and the cytoplasm (By similarity). KAT5/TIP60 inhibits its nuclear translocation (By similarity). Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation (By similarity). Preferentially localizes across the entire gene coding region (By similarity). During transcription, accumulates at chromatin loci where unscheduled R-loops form and colocalizes with paused 'Ser-5'-phosphorlyated POLR2A/RNA polymerase II and helicase DDX23 (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family."}
+{"protein": "MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSSLIALADKHATLSVCYRAGPGADTGEEGEVEEEVENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKDGEEDGRDQSKLETKVWEAHNPLVDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNSVKASVVNGTGTPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRNNMSPHGIPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYMPINSAAIKAECTARLPEASQSPLVLKQVVRKPLEAVLRYLETHPRPPKPDPVKSSSSVLSSLTPAKSAPVINNGSPTILGKRSYEQHNGVDGLANHGQTRHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPLRPPPPAPVNDEPIVIED", "text": "FUNCTION: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator (By similarity). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). In the NuRD complex, regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA (By similarity). In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A (By similarity). Acts as a transcriptional coactivator of BCAS3, and SUMO2, independent of the NuRD complex (By similarity). Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3 (). Regulates p53-dependent and -independent DNA repair processes following genotoxic stress (By similarity). Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair (By similarity). Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light- dark (LD) cycles (By similarity). Positively regulates the CLOCK-BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1 (By similarity). Regulates deacetylation of BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression (By similarity). With TFCP2L1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity). SUBCELLULAR LOCATION: [Isoform 2]: Rough endoplasmic reticulum Golgi apparatus Zymogen granule. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus Nucleus envelope Cytoplasm Cytoplasm, cytoskeleton Note=Associated with microtubules. Localization at the nuclear envelope is TPR- dependent (By similarity)."}
+{"protein": "MSAAQVSSSRRQSCYLCDLPRMPWAMIWDFSEPVCRGCVNYEGADRIEFVIETARQLKRAHGCFQDGRSPGPPPPVGVKTVALSAKEAAAAAAAAAAAAAAAQQQQQQQQQQQQQQQQQQQQQQQLNHVDGSSKPAVLAAPSGLERYGLSAAAAAAAAAAAAVEQRSRFEYPPPPVSLGSSSHATRLPNGLGGPNGFPKPTPEEGPPELNRQSPNSSSAAASVASRRGTHGGLVTGLPNPGGGGGPQLTVPPNLLPQTLLNGPASAAVLPPPPPHALGSRGPPTPAPPGAPGGPACLGGTPGVSATSSSASSSTSSSVAEVGVGAGGKRPGSVSSTDQERELKEKQRNAEALAELSESLRNRAEEWANKPKMVRDTLLTLAGCTPYEVRFKKDHSLLGRVFAFDAVSKPGMDYELKLFIEYPTGSGNVYSSASGVAKQMYQDCMKDFGRGLSSGFKYLEYEKKHGSGDWRLLGDLLPEAVRFFKEGVPGADMLPQPYLDASCPMLPTALVSLSRAPSAPPGTGTLPPAAPSGRGAAASLRKRKASPEPPDSAEGALKLGEEQQRQQWMANQSEALKLTMSAGGFAAPGHAAGGPPPPPPPLGPHSNRTTPPESAPQNGPSPMAALMSVADTLGTAHSPKDGSSVHSTTASARRNSSSPVSPASVPGQRRLASRNGDLNLQVAPPPPSAHPGMDQVHPQNIPDSPMANSGPLCCTICHERLEDTHFVQCPSVPSHKFCFPCSRESIKAQGASGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP", "text": "FUNCTION: Probable E3 ubiquitin protein ligase involved in the proteasome-mediated ubiquitin-dependent degradation of target proteins. Through the degradation of CTNNB1, functions downstream of FOXF2 to negatively regulate the Wnt signaling pathway. Probably plays a role in the development of the central nervous system and in neuronal maintenance (By similarity). Also acts as a transcriptional regulator of genes controlling female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IRF2BP family."}
+{"protein": "MGKKARFKEARRLQKRNLNNAIGSSSINSQNSLTNDKIGKGKNKGPTERYVLPFEKNNRFLLLGEGNFSFAFSLLLHHVSSEGFVLATSYDSKEDLKQKYPDAAEYISKIEINGGKVMHEIDATKLHLHKKLKTQKFDTIFWNFPHSGKGIKDQDRNILDNQKMLLAFFKASKFLLSEKGVIVITLAETKPYTLWNLKGLAKDAGYTSLMTEKFDSSFYPEYSHRRTIGWIDGISERSPWKGELRDSRHYCFVVNGSNIKPYNQRKEKRKRSELSDDSSDSS", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of a uridine in 25S rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. BMT5 family."}
+{"protein": "MKFSHSLQFNSVPEWSTKYLAYSQLKKLIYSLQKDKLYSNNKHHVVEPHDANDENLPLLADASPDDQFYISKFVAALNQELKKIDKFYISQETGLIANYNELKDDVMELENTNKATQLFNQQQQHQLQSVARNRKSKSQQRQRRFSSVSSTDSNPSLTDMSIDSAPVIHTQVSNTTNNGNSMQNLASASVSLSNSNPVYLSPFTQHRLSLKKRLISIYTQLSELKDFIELNQTGFSKICKKFDKSLNTNLKQNYLNYIKFHSHVFNPATINRIQHHITETILTYASLNKGTRRPSNTFNLDADRINNDENSSGNEEDEDGNRQEVLDFQDAERELSSHLRDHVVWERNTVWKDMMNLERKYQSAKTDNKKFSKLSSSQLRPNANITESMAMSSGGAGIIAPSTDSLTFRELMHLPPKQWLQFIMGQTSLLKFLLITSCFIALLTFNLTPFTQDSLQKNCFAILIYASLLWATETIPLFVTSLMIPLLIVVFPVIKDPITSQPMSPRDSSQFILSTMWSSVIMLLLGGFTLAAALSKYNIAKVLSTHILASAGTNPHFILLTNMFVALFVSMWVSNVAAPVLCYSIVQPLLRTLPRNCSYAKALILGIALASNIGGMSSPIASPQNIFSIGIMDPSPSWAEWFMIALPVCFICVMAIWVLLIITFPPEPNVKILQLHPSRDPFTLKQWFVTLVCIITIVLWCLSNQISGIFGEMGIISIIPIVVFFGTGLLTSDDFNNFMWTIVVLAMGGTTLGKAVSSSGLLSTMAQLIKAQVEHEPIFIIVLIFGLVILVMATFVSHTVAAMIIVPLMSEIGSNLPSGDHSRLLIVIAALLCSSAMGLPTSGFPNVTAISMIDEVGDRYLTVGTFITRGVPASLLSYAAIVTVGYGILKVMGF", "text": "FUNCTION: Vacuolar phosphate transporter that probably exports phosphate from the vacuolar lumen to the cytosol. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CitM (TC 2.A.11) transporter family."}
+{"protein": "MKSLFYLKLLLWVVLLSLCLLMAHRKTKVADKFRALRSRIQLRFNRHIRLNDSFADDLENGLHSRNFDIISENSNDVRGGLDDVSKNEIKQIMENDNVDFDKARLLYMERKFGQNGIAPDGTPIDPKAFTFDSR", "text": "SIMILARITY: Belongs to the UPF0357 family."}
+{"protein": "MPPLWALLALGCLRFGSAVNLQPQLASVTFATNNPTLTTVALEKPLCMFDSKEALTGTHEVYLYVLVDSAISRNASVQDSTNTPLGSTFLQTEGGRTGPYKAVAFDLIPCSDLPSLDAIGDVSKASQILNAYLVRVGANGTCLWDPNFQGLCNAPLSAATEYRFKYVLVNMSTGLVEDQTLWSDPIRTNQLTPYSTIDTWPGRRSGGMIVITSILGSLPFFLLVGFAGAIALSLVDMGSSDGETTHDSQITQEAVPKSLGASESSYTSVNRGPPLDRAEVYSSKLQD", "text": "FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER). SIMILARITY: Belongs to the uroplakin-3 family."}
+{"protein": "MASVEEFRNAQRAKGPATILAIGTATPDHCVYQSDYADYYFRVTKSEHMTELKKKFNRICDKSMIKKRYIHLTEEMLEEHPNIGAYMAPSLNIRQEIITAEVPRLGRDAALKALKEWGQPKSKITHLVFCTTSGVEMPGADYKLANLLGLETSVRRVMLYHQGCYAGGTVLRTAKDLAENNAGARVLVVCSEITVVTFRGPSEDALDSLVGQALFGDGSSAVIVGSDPDVSIERPLFQLVSAAQTFIPNSAGAIAGNLREVGLTFHLWPNVPTLISENIEKCLTQAFDPLGISDWNSLFWIAHPGGPAILDAVEAKLNLEKKKLEATRHVLSEYGNMSSACVLFILDEMRKKSLKGENATTGEGLDWGVLFGFGPGLTIETVVLHSIPTVTN", "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": "MSKEIPTPYMWSYQPQMGLAAGAAQDYSTRINYMSAGPHMISRVNGIRAHRNRILLEQAAITTTPRNNLNPRSWPAALVYQESPAPTTVVLPRDAQAEVQMTNSGAQLAGGFRHRVRSPGQGITHLTIRGRGIQLNDESVSSSLGLRPDGTFQIGGAGRPSFTPRQAILTLQTSSSEPRSGGIGTLQFIEEFVPSVYFNPFSGPPGHYPDQFIPNFDAVKDSADGYD", "text": "FUNCTION: [Hexon-linking protein-C]: Structural component of the virion that acts as a cement protein on the capsid interior and which glue the peripentonal hexons and group-of-nine hexons together. FUNCTION: [Hexon-linking protein-N]: Structural component of the virion that acts as a cement protein on the capsid interior and which glue the peripentonal hexons and group-of-nine hexons together. SUBCELLULAR LOCATION: [Pre-hexon-linking protein VIII]: Host nucleus. SUBCELLULAR LOCATION: [Hexon-linking protein-N]: Virion Note=Located on the inner side of the capsid shell. Present in 120 copies per virion. SUBCELLULAR LOCATION: [Hexon-linking protein-C]: Virion Note=Located on the inner side of the capsid shell. Present in 120 copies per virion. SIMILARITY: Belongs to the adenoviridae hexon-linking protein family."}
+{"protein": "MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK", "text": "FUNCTION: (Microbial infection) Kinase activity is required for SARS coronavirus-2/SARS-CoV-2 replication. FUNCTION: Catalytic 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 (PubMed:14617358, PubMed:7628435, PubMed:33637724). As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding (PubMed:32690950). Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20208530, PubMed:20643123). Involved in the transport of lysosomal enzyme precursors to lysosomes (By similarity). Required for transport from early to late endosomes (By similarity). SUBCELLULAR LOCATION: Midbody Late endosome Cytoplasmic vesicle, autophagosome Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes (PubMed:14617358). Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (By similarity). SIMILARITY: Belongs to the PI3/PI4-kinase family."}
+{"protein": "MGLLLLLLILTPLLAAYCHPDFRLLEKAQQLLQSTGSPYSTNCWLCTSSSSKTPGRAYPASSREWTTIEAELHISYQWDPNLKGLIRLANSLLSKVKQDFPDIRKEPPIFGPIFTNVNLIGIAPICVTAKRKDGTNVGTLPSTVCNVTLTVDPNQQTYQKYAHNQFHHQPRFPKPPNITFPQGTLLDKSTRFCQGRPSSCSTRNFWFQPADYNQCLQIPNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLSTSAVSEFSGTSVTSLFSFHISTCLKTQGAFYICGQSIHQCLPTNWTGTCTIGYVSPDIFIAPGNLSLPIPIYGNFHFPRVKRAIHLIPLLVGLGIVGSAGTGIAGIAKASFTYSQLSKEIANNIEAMAKTLTTVQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNRASTLQEQATQGWLNWEGTWKWFSWVLPFTGPLVSLLLLLLFGPCLLNLITQFVSSRLQATKLQMKLNKRVHPRNSQESPF", "text": "FUNCTION: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process (By similarity). FUNCTION: Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139). 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: Virion. SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily."}
+{"protein": "MPWLEALPYICGWLILRSCLLVGAQLDSDGTITIEEQIVLVMKAKMQCELNITAQFQEGEGNCFPEWDGLICWPRGTAGKTSAMPCPSYVYDFNHKGVAFRHCTPNGTWDFIHGSNKTWANYSDCFLQPDINIGKQEFFENLYILYTVGYSISFGSLAVAILIIGYFRRLHCTRNYIHLHLFVSFMLRAXSIFVKDRVAQAHLGVEALQSLVMQGDLQNFIGGPSVDKSQYVGCKIAVVMFIYFLATNYYWILVEGLYLHNLIFVSFFSDTKYLWGFILIGWGFPAVFVVAWAVARATLADTRCWELSAGDRWIYXXPILAAIGLNFILFLNTVRVLATKIWETNAVGHDMRKQYRKLAKSTLVLVLVFGVHYIVFICQPHSFSGLWWEIRMHCELFFNSFQGFFVSIVYCYCNGEVQAEVKKTWTRWNLSIDWKKAPPCGGHRYGSVLTTVTHSTSSQSQMGPSTRLVLISSKPAKTACRQIDSHVTLPGYVWSSSEQDCQPQSTPEETKKGHGRQEDDSPVGESSRPVAFTIDTEGCKGESHPI", "text": "FUNCTION: This is a specific receptor for parathyroid hormone. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. PTH2R may be responsible for PTH effects in a number of physiological systems. It may play a significant role in pancreatic function. PTH2R presence in neurons indicates that it may function as a neurotransmitter receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family."}
+{"protein": "MAGSHPYFNLPDSTHPSPPSAPPSLRWCQRCQPSDATNGLLVALLGGGLPAGFVGPLSRMAYQASNLPSLELLICRCLFHLPIALPLKLHGDPLLGPPDIRGRACFCALLNVLSIGCAYSAVQVVPAGNAATVRKGSSTVCSAILTLCLESQGLSGYDWCGLLGSILGLIIIVGPGLWTLQEGTMGVYTALGYVQAFLGGLALSLGLLVYRSLHFPSCLPTVAFLSGLVGLLGSVPGLFVLQTPVLPSDLLSWSCVGAVGILALVSFTCVGYAVTKAHPALVCAVLHSEVVVALILQYYVLHETVAPSDIMGAGIVLGSIAIITARNLSCERTGKVEE", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC35G solute transporter family."}
+{"protein": "MANNAAACAERATNDMLIGPDWAINIELCDIINMEPSQAKEAVKVLKKRLGSKNSKVQILALYALETLSKNCGESVYQLIVDRDILPDMVKIVKKKPDLTVREKILSLLDTWQEAFGGSGGRFPQYYNAYNELRSAGIEFPPRTESSVPFFTPPQTQPIVAQATASDEDAAIQASLQSDDASALSMEEIQSAQGSVDVLTDMLGALDPSHPEGLKEELIVDLVEQCRTYQRRVMALVNTTSDEELMCQGLALNDNLQRVLQHHDDKAKGNSVPATAPTPIPLVSINHDDDDDESDDDFLQLAHRSKRESARGTGQGNFNPILPPPPSSMRPVHVDSGAMDFLSGDVYKPQETFENVKPPSTSQSSNHDYSAPIFDEPVPQSKSPEHALFTKPVYDQTEQLPPAPWETQEPRKYPPSMSARTNKRPEYFQHNVPQHSSSASESSYDDLLGQSRNLSLNPTASAAPVTPPKKDDKPEDILFKDLMDFAKTRTSSSSSSKPNNQNNKPF", "text": "FUNCTION: Might contribute to the loading of the ESCRT machinery. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TOM1 family."}
+{"protein": "MKVSAALLCLLLTAAILTTQVPAQPDALSALFTCCFTFNNKKIPLQRLESYRITSSHCPRKAVIFSTKLAKAICADPKEKWVQDYVKHLDQRTQTPKT", "text": "FUNCTION: Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils, but not neutrophils. Signals through CCR2B and CCR3 receptors (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
+{"protein": "MLLKVSSCEPLVPIKQWIHTSQLDLSDSSSLVADLLYNIIKFNFSGLEDKRAIFTGYESIKRYTIGNEMFLQLAKDGFALPVSMSYGLFLEETDTLELRALPRSEGLHRGCEVLVLRLDSPNELKENIREWSSKFMNSKASQKQQMLSPETMQKVDLAGRASPRYQANDSWISKKRNAPLSSISQYANMPENYALNTKKSKISNENDTIFKANFQQNKYESLHAKQISASDLSLHQEFVSASIVQQPELNSLLTSQSKNSTPSESDSSSSESSSSVSDSSDLSSTSDSSSGDESSDTARQSSSDTISSNNVSVSVSLNTANEFSFPQGTFKAENEAVESEVAPSSSTPPTVEEISYLHYDEPSQYYFSSPSKLSSETTKVHRGCENTEKPSEEGKNFTTPLSDSVESENTWSNTLRSSVEDDNTGVSDDNKKSKLNAEFDGHVNNISVRPPGSGSSATKARNLRRKKARILKRLMQESNDTFSANESTVVANVPDSYLTKNDEEDSASLASLKVAPKYVSHPVSLSSNSFHTEFPIGSLMRFTVMDLNPVTCTPEISEKTGRVVDCSEEKVKIQLDLGDRLDLKFDVNGEVIRNRYGTTPDEELIEGIATYEWSSLSNVHKLELTN", "text": "FUNCTION: Has a role in sporulation. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MLGAECPKPCKGKWPTPPFDPRFPNQNQTRNCYQNFLDYHRCIKTMNRRGKSTQPCEYYFRVYHSLCPISWVQRWKEQIKDGTFAGKI", "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; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family."}
+{"protein": "MEFLLGNPFSTPVGQCLEKATDGSLQSEDWTLNMEICDIINETEEGPKDAIRALKKRLSGNRNYREVMLALTVLETCVKNCGHRFHLLVANRDFIDSVLVKIISPKNNPPTIVQDKVLALIQAWADAFRSSPDLTGVVHIYEELKRRGIEFPMADLDALSPIHTPQRSVPEMDPAATIPRSQTQPRTTAGTYSSPPPASYSTLQAPALSVTGPITANSEQIARLRSELDIVRGNTKVMSEMLTEMVPGQEDSSDLELLQELNRTCRAMQHRIVELISRVSNEEVTEELLHVNDDLNNVFLRYERFERYRSGRSVQNASNGVLSEVTEDNLIDLGPGSPAVVSPMVGSTAPPSSLSSQLAGLDLGTESVSGTLSSLQQCKPQDGFDMFAQTRGNSLAEQRKTVTYEDPQAVGGLASALDNRKQNSEMIPVAQPSVMDDIEVWLRTDLKGDDLEEGVTSEEFDKFLEERAKAAETVPDLPSPPTEAPAPASNTSTRKKPERSDDALFAL", "text": "FUNCTION: Acts as a MYO6/Myosin VI adapter protein that targets myosin VI to endocytic structures (By similarity). May also play a role in recruiting clathrin to endosomes (By similarity). May regulate growth factor-induced mitogenic signaling (By similarity). SIMILARITY: Belongs to the TOM1 family."}
+{"protein": "MGIRAFLDKIEHNFEKGGKYEKWYALYEAIDTFFYRPGSVTKTTAHVRDGIDLKRMMITVWLCTFPAMFFGMWNTGYQANLIFAQSPELLASQEGWRFALIGSLAGFDPNSLWDNFIQGAAYFLPVYAVTFIVGGFWEVLFASIRKHEVNEGFFVTSVLFALILPPSIPLWQVALGISFGVVIGKEVFGGTGKNFLNPALTGRAFLFFAYPAQMSGDAVWTAVDGFAGATSLSLAASGGIENVINNGITWMDAFIGTIHGSLGETSTLAIAIGGLVLLITKIASWRIVSGVMLGMIGLSLLLNLIGSNTNPMFAMPWYWHLVVGGFAFGMFFMATDPVSASMTNTGKWIFGALIGVMVVLIRVVNPAFPEGMMLAILFANLFAPLIDHFVVQANIKRRLARNV", "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": "MKIRASVRKICTKCRLIRRRGRIRVICSNPKHKQRQG", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
+{"protein": "MKKIIICVILLAIMLLAACQVNNVRDTGGGSVSPSSIVTGVSMGSDGVGNP", "text": "FUNCTION: Lysis proteins are required for both colicin release and partial cell lysis. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor."}
+{"protein": "MALASGNRLGSARGQTCADASGRVAPRLLSRACSGSPLALGVLACLGAASSVKPHPRLPATTSAASAPLPARGPAPCAAVPTVVTPDNATGVFEELAAGQQRKYIMISGKGGVGKTSLSASLAVKLAAAGHTTLVVSTDPAHSLSDSLAQDVSGGRPVLLQGTDLPLWGLEIDPEEAKREFFEGSGAGQDGEAGGPSAASQVSDFMNRMGMGFVIDQLKELKLGELLNTPPPGLDEAVAIAKVVQFVQAAEYARFSRIVFDTAPTGHTLRLLALPDFVDASLAKVIRLRKKLNGATSVVRGLFGAGESQDEAVEKLELLQQRVRMVKALFRDKTQTEFIIATIPTYLGVNESSRLLQALRAEQIPCKRIIVNQIVGPQQGDAYLRMKMKDQIAALEMVANDPGLRPLRKVIAPMVDVEVRGVPALSYFGNVVWKDVYDQMNQGADRKFFLLGGKGGVGKTSCSSSLAVHFANDGLPTLVVSTDPAHSLSDAFDQDLSGGSPVKITSPLGDELPLWGLQLDPEQAKAELRAVLADDGGKKLNETLDGLGLGVISDQLKDLQLGELLDTPPPGVDEAIAIAKVVQFLKAPEYSHFKRIVFDTAPTGHTLRLLSLPDFLDASIGKLVRLRQKLSAATSAVKNLFSGGQPGEEDVAVKRLEALQASMEDAKAMFRNQQTTEFIIVTIPTVMATAESCRLASALQHEGIPLKTIIVNQVVQANATDKFLTARRADQARALHHLEEDTGPDGLASLQLIKAPLCDLEVRGVPALSYFGNVVWK", "text": "FUNCTION: ATPase required for the post-translational delivery of tail- anchored (TA) proteins to the chloroplast. Required for the accumulation of TOC34, an essential component of the outer chloroplast membrane translocon (TOC) complex (PubMed:23167510, PubMed:28382961). Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to chloroplast, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis (PubMed:28382961). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the arsA ATPase family."}
+{"protein": "MAGLAGPAKPSLALNPQEDSQFEKALTQIQGRTKKPQQKKKEKLNRGVVYLGHLPSTLSESHIYNYCAQFGDISRFRLSRSKRTGNSKGYAFVEFESEDVAKIVAETMDNYLFGERLLSCKFMPRKKVHKDLFSQRNALFHRPSFPAVKRYNRKRGHLQMLKMEYRFKKKEKLLRKKLAAKGIDYSFPSLVLPKPKNIAVAHRDSEGNQVLPDQKEGLSGEPRRKEKMMKEDISNNIPKKRKRSRRKKSSVDSQGPTPVCTPTFLERRKSQVMEVGGDKDDEIILKLPVPPVKEDTQKTPTSASPGGKRPRKRKSKQ", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome Note=Localizes to mitotic chromosomes in conjunction with MKI67."}
+{"protein": "MGQEVSSVNNTKNEHHKTNKKSLKGGNERHEMKESSVGISKKIVENSFNNSKLRPGMFIQNSNVVFNEQYKGIKILGKGSFGEVILSRDKHTGHEYAIKVISKKHVKRKTDKESLLREVELLKMLDHINIMKLYEFFEDNNYYYLVSDVYTGGELFDEIISRKRFYEIDAARIIKQILSGITYMHKNNVVHRDLKPENILLETKNKEDMIIKIIDFGLSTHFEYSKKMKDKIGTAYYIAPDVLHGTYDEKCDIWSCGVILYILLSGCPPFNGSNEYDILKKVEAGKYTFDLPQFKKISDKAKDLIKKMLMYTSAVRISARDALEHEWIKMMTSKDNLNIDIPSLELSIANIRQFQSTQKLAQAALLYMGSKLTTIDETKELTKIFKKMDKNGDGQLDRNELIIGYKELLKLKGEDTSDLDNAAIEYEVDQILNSIDLDQNGYIEYSEFLTVSIDRKLLLSTERLEKAFKLFDKDGSGKISANELAQLFGLSDVSSECWKTVLKEVDQNNDGEIDFKEFRDMLVKLCNY", "text": "FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (PubMed:19307175, PubMed:19666141). Plays a central role in the host erythrocytes and hepatocytes infection cycles, sexual reproduction and mosquito transmission of the parasite. During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK1 and CDPK5. Involved in merosome egress from host hepatocytes, probably together with CDPK5. During the asexual blood stage, involved in merozoite invasion of host erythrocytes and motility by stabilizing the inner membrane complex, a structure below the plasma membrane which acts as an anchor for the glidosome, an acto-myosin motor. Required for cell cycle progression in the male gametocyte. During male gametogenesis in the mosquito gut, required to initiate the first round of DNA replication, probably by facilitating the assembly of the pre- replicative MCM complex, to assemble the first mitotic spindle and, at the end of gametogenesis, to initiate axoneme motility, cytokinesis and subsequent exflagellation. For each of these steps, may phosphorylate SOC1, SOC2 and SOC3, respectively. Together with CDPK1, regulates ookinete gliding in the mosquito host midgut (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily."}
+{"protein": "MALRMLWAGQAKGILGGWGIICLVMSLLLQHPGVYSKCYFQAQAPCHYEGKYFTLGESWLRKDCFHCTCLHPVGVGCCDTSQHPIDFPAGCEVRQEAGTCQFSLVQKSDPRLPCKGGGPDPEWGSANTPVPGAPAPHSS", "text": "FUNCTION: Acts as a ligand for C-C chemokine receptor CCR2 (PubMed:24442440). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (PubMed:24442440). Exhibits a chemotactic activity for monocytes and lymphocytes but not neutrophils (PubMed:24442440). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-microseminoprotein family."}
+{"protein": "GLWQKIKSAAGDLASGIVEAIKS", "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": "MIATLFIIFAFIRAFPWSRKRGRPALALTLMPEGGEDHRGDLNQKGENNNRPRPSISLANNGEAMAPRTRRKSSKFHEVTFSGSVGGGDSDGGGEAINGGNLDVSPSKRHSLSTTTSNSSSAPYRYLSGSSRSRGSRGDCHEYYQLQQHSSSLSNGNRGNRGLSQRSDTMATEAEGEEFDVDPMDEDDEDQTYDRETEEFYSNIQDAAGTGSSSRSKRSSLFSRSDSSATTTSSSGGGTFTGGKRRSAASILSSSMCSDLMTSDRRSSTATEYSVKSVTTGNTSQRRSSGRIRRYVSRMTIAGARRRTTGSFDVENGQGARSPLEGGSPSAGLVLQNLPQRRESFLYRSDSDFEMSPKSMSRNSSIASESHGEDLIVTPFAQILASLRSVRNNLLSLTNVPASNKSRRPNQSSSASRSGNPPGAPLSQGEEAYTRLATDTIEELDWCLDQLETIQTHRSVSDMASLKFKRMLNKELSHFSESSRSGNQISEYICSTFLDKQQEFDLPSLRVEDNPELVAANAAAGQQSAGQYARSRSPRGPPMSQISGVKRPLSHTNSFTGERLPTFGVETPRENELGTLLGELDTWGIQIFSIGEFSVNRPLTCVAYTIFQSRELLTSLMIPPKTFLNFMSTLEDHYVKDNPFHNSLHAADVTQSTNVLLNTPALEGVFTPLEVGGALFAACIHDVDHPGLTNQFLVNSSSELALMYNDESVLENHHLAVAFKLLQNQGCDIFCNMQKKQRQTLRKMVIDIVLSTDMSKHMSLLADLKTMVETKKVAGSGVLLLDNYTDRIQVLENLVHCADLSNPTKPLPLYKRWVALLMEEFFLQGDKERESGMDISPMCDRHNATIEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEENRDYYQSMIPPSPPPSGVDENPQEDRIRFQVTLEESDQENLAELEEGDESGGESTTTGTTGTTAASALSGAGGGGGGGGGMAPRTGGCQNQPQHGGM", "text": "FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (By similarity). Vital for female fertility. Required for learning/memory (By similarity). SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily."}
+{"protein": "MSGLRPALSTFIFLLLITGGVYPLLTTVLGQWWFPWQANGSLIREGDTVRGSALIGQNFTGNGYFHGRPSATAEMPYNPQASGGSNLAVSNPELDKLIAARVAALRAANPDASASVPVELVTASASGLDNNITPQAAAWQIPRVAKARNLSVEQLTQLIAKYSQQPLVKYIGQPVVNIVELNLALDKLDE", "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 (PubMed:2849541, PubMed:8499455, PubMed:23930894). 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 (PubMed:21711450). 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. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the KdpC family."}
+{"protein": "MTDDFAPDGQLAKAIPGFKPREPQRQMAVAVTQAIEKGQPLVVEAGTGTGKTYAYLAPALRAKKKVIISTGSKALQDQLYSRDLPTVSKALKYTGNVALLKGRSNYLCLERLEQQALAGGDLPVQILSDVILLRSWSNQTVDGDISTCVSVAEDSQAWPLVTSTNDNCLGSDCPMYKDCFVVKARKKAMDADVVVVNHHLFLADMVVKESGFGELIPEADVMIFDEAHQLPDIASQYFGQSLSSRQLLDLAKDITIAYRTELKDTQQLQKCADRLAQSAQDFRLQLGEPGYRGNLRELLANPQIQRAFLLLDDTLELCYDVAKLSLGRSALLDAAFERATLYRTRLKRLKEINQPGYSYWYECTSRHFTLALTPLSVADKFKELMAQKPGSWIFTSATLSVNDDLHHFTSRLGIEQAESLLLPSPFDYSRQALLCVLRNLPQTNQPGSARQLAAMLRPIIEANNGRCFMLCTSHAMMRDLAEQFRATMTLPVLLQGETSKGQLLQQFVSAGNALLVATSSFWEGVDVRGDTLSLVIIDKLPFTSPDDPLLKARMEDCRLRGGDPFDEVQLPDAVITLKQGVGRLIRDADDRGVLVICDNRLVMRPYGATFLASLPPAPRTRDIARAVRFLAIPSSR", "text": "FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase (By similarity). Involved in the repair of replication forks and tolerance of the chain- terminating nucleoside analog 3' azidothymidine (AZT). May unwind potentially damaged 3' nascent ends such as those terminated by AZT, promote repair and AZT excision (PubMed:26544712). SIMILARITY: Belongs to the helicase family. DinG subfamily."}
+{"protein": "MEESKTPHVAIIPSPGMGHLIPLVEFAKRLVHLHGLTVTFVIAGEGPPSKAQRTVLDSLPSSISSVFLPPVDLTDLSSSTRIESRISLTVTRSNPELRKVFDSFVEGGRLPTALVVDLFGTDAFDVAVEFHVPPYIFYPTTANVLSFFLHLPKLDETVSCEFRELTEPLMLPGCVPVAGKDFLDPAQDRKDDAYKWLLHNTKRYKEAEGILVNTFFELEPNAIKALQEPGLDKPPVYPVGPLVNIGKQEAKQTEESECLKWLDNQPLGSVLYVSFGSGGTLTCEQLNELALGLADSEQRFLWVIRSPSGIANSSYFDSHSQTDPLTFLPPGFLERTKKRGFVIPFWAPQAQVLAHPSTGGFLTHCGWNSTLESVVSGIPLIAWPLYAEQKMNAVLLSEDIRAALRPRAGDDGLVRREEVARVVKGLMEGEEGKGVRNKMKELKEAACRVLKDDGTSTKALSLVALKWKAHKKELEQNGNH", "text": "FUNCTION: Bifunctional O-glycosyltransferase and N-glycosyltransferase that can detoxify xenobiotics. Possesses high activity to metabolize the persistent pollutants 2,4,5-trichlorophenol (TCP) and 3,4- dichloroaniline (DCA). Also active on benzoates and benzoate derivatives in vitro. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MNGGHIQLIIGPMFSGKSTELIRRVRRYQIAQYKCVTIKYSNDNRYGTGLWTHDKNNFEALEATKLCDVLEAITDFSVIGIDEGQFFPDIVEFCERMANEGKIVIVAALDGTFQRKPFNNILDLIPLSEMVVKLTAVCMKCFKEASFSKRLGAETKIEIIGGIDMYQSVCRKCYIDS", "text": "FUNCTION: Phosphorylates thymidine and thymidine analogs, such as azidothymidine (AZT). Part of the salvage pathway for pyrimidine deoxyribonucleotide synthesis. SIMILARITY: Belongs to the thymidine kinase family."}
+{"protein": "MASSLIAKRFLSSSLLSRSLLRPAASASHRSFDTNAMRQYDNRADDHSTDIDRHSERSFPSTARRDDIFLRCVGSIFSDSEFEPGSEHDGPGHGQSVPLRVARDRSWRWSGRGWDARETEDALHLRVDMPGLAKEDVKISVEQNTLIIKGEGAKEGDEEESARRYTSRIDLPDKLYKIDQIRAEMKNGVLKVVVPKMKEEERKDVISVKVE", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MAVEIIVDREKCIGCGRCYDVCPKGPLIWTKDENGKYYAYDVEYCHNCKFCAGRCPTNAILIKVVKPKKKDENKNKK", "text": "FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons probably in the CO-dehydrogenase complex."}
+{"protein": "MKQQIQLRRREVDETADLPAELPPLLRRLYASRGVRSAQELERSVKGMLPWQQLSGVEKAVEILYNAFREGTRIIVVGDFDADGATSTALSVLAMRSLGCSNIDYLVPNRFEDGYGLSPEVVDQAHARGAQLIVTVDNGISSHAGVEHARSLGIPVIVTDHHLPGDTLPAAEAIINPNLRDCNFPSKSLAGVGVAFYLMLALRTFLRDQGWFDERNIAIPNLAELLDLVALGTVADVVPLDANNRILTWQGMSRIRAGKCRPGIKALLEVANRDAQKLAASDLGFALGPRLNAAGRLDDMSVGVALLLCDNIGEARVLANELDALNQTRKEIEQGMQIEALTLCEKLERSRDTLPGGLAMYHPEWHQGVVGILASRIKERFHRPVIAFAPAGDGTLKGSGRSIQGLHMRDALERLDTLYPGMMLKFGGHAMAAGLSLEEDKFKLFQQRFGELVTEWLDPSLLQGEVVSDGPLSPAEMTMEVAQLLRDAGPWGQMFPEPLFDGHFRLLQQRLVGERHLKVMVEPVGGGPLLDGIAFNVDTALWPDNGVREVQLAYKLDINEFRGNRSLQIIIDNIWPI", "text": "FUNCTION: Single-stranded-DNA-specific exonuclease. Required for many types of recombinational events, although the stringency of the requirement for RecJ appears to vary with the type of recombinational event monitored and the other recombination gene products which are available. SIMILARITY: Belongs to the RecJ family."}
+{"protein": "MAAYLLAVAILFCIQGWPSGTVQGEVRPFMEVYQRSVCQPRETLVSILEEYPDKISKIFRPSCVAVLRCGGCCSDESLTCTSVGERTVELQVMQVTPKTLSSKIKVMKFREHTACECRPRSGSRVNIGKHKRSPEEGEREPSSPLTPGSL", "text": "FUNCTION: Snake venom VEGFs that may contribute to venom dispersion and prey subjugation by inducing vascular permeability and hypotension. This protein induces an increase in capillary permeability after intradermal injection, as well as a drastic hypotensive effect after intravenous injection. The hypotension is mediated by nitric oxide (NO), which is produced by VEGF-activated endothelium NO synthase. Also induces angiogenesis in vitro, probably through VEGF receptor (KDR/VEGFR-2) signaling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the PDGF/VEGF growth factor family. Snake venom VEGF subfamily."}
+{"protein": "MGALRVLRYVSMIWRPELGSCARQRDAGFGTEARRPSQPHRSSKHKDLVEDQPFPGLLRTENLGLEELAHVLRAAVVDQKGPLVTLNKPQGLPVTGRPGELTLLSVLPQLSQALGLEHQELQVVRAPGKEASGLVLLSSCPQTASRLQKFFIHSRRAQRPTATYCAVTDGIPEPSEGTVCMPLKMEQMNDVDLAVPVMSPSRKDIQEGVKRTLSRFHVMATGRGCALVQLQPLTVFPNQLQVHMALQLCPILGDHTYAARVGTVLGQRFLWPAETTKPQRQVLDEALLRHLRLSPSQVAQMPLHLHLHRLLLPGTGSRDPPSELLAPLPPYFSRTLQCLRLSQQ", "text": "FUNCTION: Catalyzes uridine to pseudouridine isomerization (pseudouridylation) of specific mitochondrial mRNAs (mt-mRNAs), a post- transcriptional modification necessary for their translation. Acts at position 390 in COXI mt-mRNA and at position 697-699 in mitochondrial COXIII mt-mRNA. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and may play a role in mitochondrial ribosome biogenesis. 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 RluA family."}
+{"protein": "MKLLSITLTSIVISMVFYQTPITTEARSLRKTNDQDHFKAGFTDDFVPTSPGNSPGVGHKKGNVNVEGFQDDFKPTEGRKLLKTNVQDHFKTGSTDDFAPTSPGHSPGVGHKKGNVNVESSEDDFKHKEGRKLQQTNGQNHFKTGSTDDFAPTSPGNSPGIGHKKGHANVKGFKDDFAPTEEIRLQKMNGQDHFKTGSTDDFAPTTPGNSPGMGHKKGDDFKPTTPGHSPGVGHAVKNDEPKA", "text": "FUNCTION: Extracellular signaling peptide that represses primary root growth rate and significantly inhibits lateral root formation. Modulates leaf morphology (PubMed:24179096). Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways (PubMed:25324386). SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.5]: Secreted, extracellular space, apoplast Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.2]: Secreted, extracellular space, apoplast Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.4]: Secreted, extracellular space, apoplast Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.3]: Secreted, extracellular space, apoplast Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.1]: Secreted, extracellular space, apoplast Note=Accumulates in xylem sap. SIMILARITY: Belongs to the C-terminally encoded plant signaling peptide (CEP) family."}
+{"protein": "MELIVIIITLAFCILLYGTRWRAALDPREPRLISPTVPLIGHILGIATDGFGYFSKLNDKYGLPAFSLQMPLSRLYVITSSELVPAIQRQSQNIRFDTFEFTLAAERVGGVSGPGLKLLKGSIVDELQHAMHHALIGHGLDAMNLSMIEAIKPSIDELQSQKQAAFDLFAWCKRSITMASTDSVYGPMNPFRSIEVERAFWDFASNMNMIILNVLPFLTARKSLDDRRKVVDALTEYYNLGGHENSSEMTYGRWEVQYNKGITTQDIARMEIVNAIGVLSNTAPSTFWTLFEIYSRPSLLRDLRQELVASAVYTHPGTDGGIVRTIDLSAVRAKCSLLLGTFQEVLRMRSNAIVTRMVHEDTILNERVLFKKGSVIVIPARCVNREKSVWGETGDSFDAYRYLGQGKSGTSRSGRNVTRVAFQSFGTAPNICPGRHFASGEILAVVAMVILRFDMEPVLGEWIPPKANVKTLASSIQTPAGEFMVTLRERKEFKDDKWDFRVTEGDSKFPLLVG", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NA). Nodulisporic acid A (NAA) and its chemically modified derivatives are of particular significance because of their highly potent insecticidal activity against blood-feeding arthropods and lack of observable adverse effects on mammals, in particular the tremogenicity associated with the paspaline-derived IDTs is not observed (PubMed:29283570). The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (PubMed:29283570). Condensation of indole-3- glycerol phosphate with GGPP by the prenyl transferase nodC then forms 3-geranylgeranylindole (3-GGI) (PubMed:29283570). Epoxidation by the FAD-dependent monooxygenase nodM leads to a single-epoxidized-GGI that is substrate of the terpene cyclase nodB for cyclization to yield emindole SB (PubMed:29283570). The terminal methyl carbon, C28, of emindole SB is then oxidized by the cytochrome P450 monooxygenase nodW to produce nodulisporic acid F (NAF), the pentacyclic core of NAA (PubMed:29283570). NAF is converted to nodulisporic acid E (NAE) via prenylation. This step is probably performed by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). Several oxidation steps performed by the FAD-linked oxidoreductase nodO and one of the cytochrome P450 monooxygenase nodR, nodX or nodZ further convert NAE to nodulisporic acid D (NAD) (Probable). NAD is substrate of cytochrome P450 monooxygenase nodJ to produce the precursor of nodulisporic acid C (NAC), converted to NAC by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). The FAD- dependent monooxygenase nodY2 then oxidizes NAC to nodulisporic acid B (NAB) (Probable). Finally NAB is converted to NAA by one of the cytochrome P450 monooxygenases nodR, nodX or nodZ (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MGFRLPGIRKASNAVDAPKGYLAVYVGEKMKRFVIPVSYMNQPSFQDLLTQAEEEFGYDHPMGGLTIPCSEEVFQRITCCLN", "text": "SIMILARITY: Belongs to the ARG7 family."}
+{"protein": "EKIKICLQKQVNSSFSLHNGFGGNLYATEEKRMFELVKPKAGASVLNQSTWIGFGDSRTDKSNPNFPRSADVSVKTANKFRSLTGGSLMLSMFGPPGKVDYLYQGCGKHKVFYEGVNWSPHAAIDCYRKNWTDIKLNFQKNIYELASQSHCMSLVNALDKTIPLQATAGVAGNCNNSFLKNPALYTQEVTPPXXKCGKENLAFFTLPTQFGTYECRLHLVASCYFIYDSKEVYNKRGCDNYFQVIYDSSGKVVGGLDNRVSPYTGNSGDTPTMQCDMIQLKPGRYSVRSSPRFLLMPERSYCFDMKEKGPVTAVQSIWGKDRKSDYAVDQACLSTPGCMLIQKQKPYTGEADDHHGDQEMRELLSGLDYEARCISQSGWVNETSPFTEEYLLPPKFGRCPLAAKEESIPKIPDGLLIPTSGTDTTVTKPKSRIFGIDDLIIGLLFVAIVEAGIGGYLLGSRKESGGGVTKESAEKGFEKIGNDIQILRSSTNIAIEKLNDRISHDEQAIRDLTLEIENARSEALLGELGIIRALLVGNISIGLQESLWELASEITNRAGDLAVEISPGCWIIDNNICDQSCQNFIFKFNETAPVPTIPPLDTKIDLQSDPFYWGSSLGLAITAAISLAALVISGIAICRTK", "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 (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family."}
+{"protein": "MWFLTTLLLWVPVDGQVDTTKAVITLQPPWVSVFQEETVTLHCEVLHLPGSSSTQWFLNGTATQTSTPSYRITSASVNDSGEYRCQRGLSGRSDPIQLEIHRGWLLLQVSSRVFTEGEPLALRCHAWKDKLVYNVLYYRNGKAFKFFHWNSNLTILKTNISHNGTYHCSGMGKHRYTSAGISVTVKELFPAPVLNASVTSPLLEGNLVTLSCETKLLLQRPGLQLYFSFYMGSKTLRGRNTSSEYQILTARREDSGLYWCEAATEDGNVLKRSPELELQVLGLQLPTPVWFHVLFYLAVGIMFLVNTVLWVTIRKELKRKKKWDLEISLDSGHEKKVISSLQEDRHLEEELKCQEQKEEQLQEGVHRKEPQGAT", "text": "FUNCTION: High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses. Mediates IgG effector functions on monocytes triggering antibody-dependent cellular cytotoxicity (ADCC) of virus-infected cells. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Stabilized at the cell membrane through interaction with FCER1G. SIMILARITY: Belongs to the immunoglobulin superfamily. FCGR1 family."}
+{"protein": "MAKATGRYNLISPKKDLEKGVVLSDLCNFLVSQTIQGWKVYWAGIEFDVTHKGMALLHRLKTNDFAPAWSMTRNLFPHLFQNPNSTIESPLWALRVILAAGIQDQLIDQSLIEPLAGALGLISDWLLTTNTNHFNMRTQRVKEQLSLKMLSLIRSNILKFINKLDALHVVNYNGLLSSIEIGTQNHTIIITRTNMGFLVELQEPDKSAMNRMKPGPAKFSLLHESTLKAFTQGSSTRMQSLILEFNSSLAI", "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": "MRDFKTYLSVAPVLSTLSLGFFAGFLIEINRFFPDALTFPFFSF", "text": "FUNCTION: May help in the organization of the PsaE and PsaF subunits. SUBCELLULAR LOCATION: Plastid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaJ family."}
+{"protein": "MKTACFPVFRNRLPDLDRDLDRDTKRVCGIKLTHDGAIAVVEDGRLVFCTEQEKRNNNSRYQEINNLDAVVAALAENGVNARDVDQFVIDGWDGEAESRFKVLSGETPVILRGAPYVERHAEGLLDWIGGSGLTLGDRVFSYRSYPHVTSHVASAYCTSPFAKSGDPALCLVWDGCIFPQLYHVEGKRASFVKSLFPVTGQAYAAAGHYFGPYKQTSRGGWDLGVAGKLMAFVALGSVHVRIVAVFQKLYQEHFAGDTALACAFRANINNSESSLAAVHDFFAASALQLGQRRPKTCLHRLIFSSNVSSLTKWRTLQHHPLPGARNLCIAGGCGLNIKWNSALRQTGLFDSVWVPPFPNDSGSAIGAACCEIVAQQGFVPLDWSVYSGPSLQDRQVPAGWHASPCSISEVAAILASNKPVVFLSGRTELGPRALGGRSILAAATSPEMKDHLNEIKFREHFRPVAPICLEDRAPDIFSPGTPDPYMLFDHQTKMPWQDKVPAVVHLDGSARLQTISRNSQHKVAEVLVEYEKLTGIPLLCNTSANYHGRGFFPSAAAACEWGRVEHVWCDGMLYRKPSATA", "text": "FUNCTION: Involved in 6-O-carbamoylation of Nod-factors. SIMILARITY: Belongs to the NodU/CmcH family."}
+{"protein": "MDWQQLWLAFLLPMTVSGRALGPTEKEAVLDYLLQYGYLQKPLEGADDFRLEDITEALRTFQEASGLPISGQMDDATRARMKQPRCGLEDPFNQKSLKYLLLGHWRKKNLTFRIFNVPSTLSLPRVRAALHQAFKYWSSVAPLTFREVKAGWADIRLSFHGRQSLYCSNTFDGPGKVLAHADIPELGSIHFDKDELWTEGTYQGVNLRIIAAHEVGHALGLGHSRYTQALMAPVYAGYQPFFKLHPDDVAGIQALYGKRSPETRDEEEETEMLTVSPVTAKPGPMPNPCSGEVDAMVLGPRGKTYAFKGDYVWTVTDSGPGPLFQISALWEGLPGNLDAAVYSPRTRRTHFFKGNKVWRYVDFKMSPGFPMKFNRVEPNLDAALYWPVNQKVFLFKGSGYWQWDELARTDLSRYPKPIKELFTGVPDRPSAAMSWQDGQVYFFKGKEYWRLNQQLRVAKGYPRNTTHWMHCGSQTPDTNSSTGDVTPSTTDTVLGTTPSTMGSTLDIPSATDSASLSFSANVTLLGA", "text": "FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis (By similarity). Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the peptidase M10A family."}
+{"protein": "MASLFSSRLGSQSLSLLINIFFIFLIFLHFASQTPPPSGSIQTLNSFAGGDSDSCSGGLASLDDHRSKCSYIRSQSKCGPQGYIDYLKIFFCIFGQSPVLGHLVLSAWLFVLFYLLGDTAASYFCPSLDSLSKVLKLSPTMAGVTLLSLGNGAPDLFSSVVSFTRSNNGDFGLNSILGGAFFVSSFVVGTICVLIGSRDVAIDRNSFIRDVVFLLVALCCLGLIIFIGKVTIWVALCYLSIYLLYVGFLSVSHFFDRKKRMSDQILRSREDLAEMGVSLLGYIAEEKLALPEKTTQEFKIVFEDSPKRHRSCFSVLVSIIGLPLYLPRRLTIPVVCEEKWSKPCAVVSTAIAPVLLTELYCSHYSGSQRNLILYIISGSIGLIVGILAYLTTEKSHPPKKFSLVWLLGGFTMSVTWTYMIAQELVSLLISLGNIFGISPSVLGLTVLAWGNSLGDLIANVTVAFHGGNDGAQIALSGCYAGPLFNTVIGLGVPLVISSLAEYPGVYIIPSDNSLLETLGFLMVGLLWALVIMPKKKMRLDKLVGGGLLAIYLCFLSLRLARVFGVLDTDR", "text": "FUNCTION: Vacuolar membrane-localized H(+)-dependent K(+) and Na(+) transporter. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Cation/calcium exchanger (CCX) subfamily."}
+{"protein": "MFQQNQQSQNQQAQNLMHIQLNGNTQLGLGALQTINVKPIKLQSRAQSLNPNLRISERNKQTTQTSSNRQNISNKSPNNLQTSKSGGLQTQNANQKLSSSSAPKKISGNFSSRVIYRAKTKNEDEIIKKQSSQTSISTNGQEKKGEIIRFATESQINNENSTPNSKIQLPPIQEKNSYKFYINSQSSNNQVSQDQSPPLQGLQAFNINKNKENQFTKKRHFDFLERTKVKNQSEETDLLKMHRYFRCKVSNLITGSGKKQYYLQYLKDMKDLMTKVKQYERVAKQNLFINDVMNKLKKIVATRAKYKYKEKIDFTRSIIMRTLGYESRQIIQQLKENMALEEQEYEDLEDDADREYEELKKKQEQQALDKNQKKELISSEIIANWKKMRGYQPNQKVFICIGQYTDLKNYLKEQGWIENPNPESLVFDLKWVTKKKDVDKDLLLDQQITNHFQKNHNLTSKNGIALNLRNLIWYDSVDIDTFYPRCFDLSDVQEFEDFIEEFKFTQAESILKQYVENKLVIDQKAKQYEKYLRLKILLACVALKRRTFSIEKKISLISVNTLPIISPEEWSVLNRQDNNYLFLEQNPDVYHRLSQIITREMDSEESNAVDLSKLAQKYLEASKEYDPQYDLNEKNLWIVKPAGLSRGRGIRAFDQLEPLLNYIMGKDVMWVAQKYMENPLTIHKKKFDIRQWVLVTEWNPLTIYFYDTCYIRICFDEYDPSDLQNKFAHLANNCISKHADNFEEKVNDTMMYLEDFVEYIKKIEGKDMFYSKIQKEMMNIAINSIKSCKDSIEPRRNSLELYGYDFMVDQNYNTWLLEINSSPSMEYSTPVTTKLVKMGLEDTAKVIHHHFVEGEKRFNKNIEYGLWKNIYREQK", "text": "FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm, cytoskeleton, cilium axoneme Note=Mainly present in locomotory and oral cilia."}
+{"protein": "MKSLYFVAGLLVMLAQGSWQHSLQNTEEKSSSFPAPQTDPLGDPDQISEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVNIVEELRRRHADGSFSDEMNTVLDSLATRDFINWLLQTKI", "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": "MEDVVIAGIAGKLPESENLQEFWEKLLNGVDMVTEDDRRWKPGMYGLPKRNGKLKDISKFDASFFGVHPKQAHTMDPQLRLLLEVSYEAILDGGINPATLRGTDTGVWVGASGSEAGEAFSQDPEQLLGYSMIGCQRAMFANRISYFYDFKGPSLSIDTACSSSLMALENAYKAIRNGRCSAAVVGGVNLLLKPNTSVQFMKLGMLSPDGACKVFDASGDGYCRSEAVVVVLLTKKSMAKRIYATIVNAGSNTDGFKEQGVTFPSGDMQRQLVSSLHRECGIKPGDIEYVETHGTGTKVGDPQEVNGLADLFCQCEREPLLIGSTKSNMGHPEPASGLAALAKVVLSLEHGL", "text": "FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein."}
+{"protein": "MTRVPRGYIARRRRAKMRSFASNFRGAHLRLNRMITQQVRRAFVSSHRDRVRQKRDFRRLWISRINAATRIHKVFDNYSKLIHNLYKKELILNRKILAQVAVLNPNNLYTISNKIKIIN", "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. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family."}
+{"protein": "MFQRLSSLFFSTPSPPEDPDCPRAFVSEEDEVDGWLIIDLPDSYAAPPSPGAAPAPAGRPPPAPSLMDESWFVTPPACFTAEGPGLGPARLQSSPLEDLLIEHPSMSVYVTGSTIVLEPGSPSPLPDAALPDGDLSEGELTPARREPRAARHAAPLPARAALLEKAGQVRRLQRARQRAERHALSAKAVQRQNRARESRPRRSKNQSSFIYQPCQRQFNY", "text": "FUNCTION: Dual regulator of transcription and autophagy. Positively regulates autophagy and is required for autophagosome formation and processing. May act as a scaffold protein that recruits MAP1LC3A, GABARAP and GABARAPL2 and brings them to the autophagosome membrane by interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase class III complex, they trigger autophagosome development. Acts as a transcriptional activator of THRA. 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": "MQKLSEEMKQTIMDIFEHLHANPEVSWKEYETTSFLKQKLEDLGCRTRTFSDCTGVVGEIGSGSPVVAVRADIDALWQEVNGTFRANHSCGHDSHMTMALGTLMLLKKQPELPKGTIRFIFQPAEEKGGGALKMIEEGVLDDIDYLYGVHVRPIQETQNGRCAPSILHGSSQHIEGTIIGEEAHGARPHLGKNSIEIAAFLVHKLGLIHIDPQIPHTVKMTKLQAGGESSNIIPGKASFSLDLRAQTNEAMEALIAETERACEAAAAAFGAKIELHKEHSLPAATQNKEAEAIMAEAITEIIGAERLDDPLVTTGGEDFHFYAVKVPNLKTTMLGLGCGLQPGLHHPHMTFDRNAMFTGIHILANAVLKTFQKAESLAAANAS", "text": "SIMILARITY: Belongs to the peptidase M20 family."}
+{"protein": "MRVVVIGAGVIGLSTALCIHERYHSVLQPLDVKVYADRFTPFTTTDVAAGLWQPYTSEPSNPQEANWNQQTFNYLLSHIGSPNAANMGLTPVSGYNLFREAVPDPYWKDMVLGFRKLTPRELDMFPDYRYGWFNTSLILEGRKYLQWLTERLTERGVKFFLRKVESFEEVARGGADVIINCTGVWAGVLQPDPLLQPGRGQIIKVDAPWLKNFIITHDLERGIYNSPYIIPGLQAVTLGGTFQVGNWNEINNIQDHNTIWEGCCRLEPTLKDAKIVGEYTGFRPVRPQVRLEREQLRFGSSNTEVIHNYGHGGYGLTIHWGCALEVAKLFGKVLEERNLLTMPPSHL", "text": "FUNCTION: Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the DAMOX/DASOX family."}
+{"protein": "MGRTRKANVCRRLSRRALGFYARDAGVVQRTNLGILRALVCQESTKFKNVWTTHSKSPIAYERGRIYFDNYRCCVSSVASEPRKLYEMPKCSKSEKIEDALLWECPVGDILPDPSDYKSSLIALTAHNWLLRISATTGEVLEKIYLASYCKFRYLSWDTPQEVIAVKSAQNKGSAAARQAGTSPPVLLYLAVFRVLPFSLVGILEINKKVFENVTDATLSHGILIVMYSSGLVRLYSFQAIIEQFMQQKLDLGCACSQGGTTGTVGEAPFGIPCNVKITDSPPPLFEVSSLENAFQIGGHPWHYIITPNKKKQKGVFHICALKDNSLAKNGIQEMECCSLESDWIYFHPDASGRIIHVGPNQVKVLKLSEVENDSSQHQISEDFVIWAKREDRKENLITVTASGRVVKRNVSLLDDDPEQETFKIVDYEDELDLLSVVAVTQIDAEGKAHLDFHCNEYGTLLKSIPLVESWDVTYSHEVYFDRDLVLHIEQKPNRVFSCYVYQMVCDPGEEEEAVNRSG", "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=According to PubMed:19026396, it is a nucleolar protein, while sequence analysis programs clearly predict 2 transmembrane regions."}
+{"protein": "MRFYLTKLFAAAGALAWTTGLSTANAVTTPVSPLSRSSDHHQSDDSTQRRLRTLNGADEERMSPLTMTRLRAALAFELELVDFDSLAQNQFLARVREMLGIKVTGSTTAGLPKMIRRFGVKNSAKNVAKRVQDPAKQADLIAGLLIYPVKQRDLLGDELLRKWPYLTVSAIKKRVIAEKNRKVHKKPRPFAAHVHAPTIAAY", "text": "FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host nucleus. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MGLPKGFSSQRKRLSAVLNMLSLSLSTASLLSNYWFVGTQKVPKPLCGKGLPAKCFDVPVPLDGGGTNASSPEVVHYSWETGDDRFTFHAFRSGMWLSCAEIMEEPGERCRSFLELTPPTEREILWLSLGAQFAYIGLELISFILLLTDLLFTGNPGCSLKLSAFAAISSVLSGLLGMVGHMMYSQVFQATANLGPEDWRPHAWNYGWAFYTAWVSFTCCMASAVTTFNTYTRLVLEFKCRHSKSFRGAPGCQPHHHQCFLQQLACTAHPGGPVTSYPQFHCQPIRSISEGVDFYSELHDKELQQGSSQEPETKAAGSSVEEC", "text": "FUNCTION: May cause the redistribution of PAPOLB from the cytosol to the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Colocalizes with PAPOLB in the endoplasmic reticulum. SIMILARITY: Belongs to the GSG1 family."}
+{"protein": "MTNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVRAATEFALLLQNWTLSVIFSAGLVAFNNDFDTQLKIWLAWYALTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY", "text": "FUNCTION: Is the initiating enzyme for colanic acid (CA) synthesis. Catalyzes the transfer of the glucose-1-phosphate moiety from UDP-Glc onto the carrier lipid undecaprenyl phosphate (C55-P), forming a phosphoanhydride bond yielding to glucosyl-pyrophosphoryl-undecaprenol (Glc-PP-C55). Also possesses a weak galactose-1-P transferase activity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bacterial sugar transferase family."}
+{"protein": "MGVIEFLFALAQDMILAAIPAVGFAMVFNVPVRALRWCALLGAIGHGSRMILMTRGLNIEWSTFMASMLVGTIGIQWSRWYLAHPKVFTVAAVIPMFPGISAYTAMISAVKISQLGYSEPLMITLLTNFLTASSIVGALSIGLSIPGLWLYRKRPRV", "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": "MKRKMKMKLVRFGLAAGLAAQVFFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSPEELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTAHVKDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEFVVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK", "text": "FUNCTION: Extracellular zinc metalloprotease. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M4 family."}
+{"protein": "MALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWNPQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFAFAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFFFTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSAVFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING", "text": "FUNCTION: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. 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. SUBCELLULAR LOCATION: Cellular chromatophore membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family."}
+{"protein": "MENSERIKKWKEERAKVAQESRASRLQQKEDERALRQTEKSADAKSHHNPDAGWSATDADSVRRASLVIKERRVQQAKQSLRRLFLYIALPLLVIMLMSWILTSHFYSADATFIVQTDASQDNFSGTSFFGAGNKMSEGFQVREFILSKEMMDRMEKELGFLSYFAQDDIALFSRFHAPLGINDDPYRYYLSKVSVAVDIQQGMLRLNVKARSAKQAEFFAQRILSFAEQHVNTVSARMQKERILWLENDVKSAQENLGAARLELLKIQHIQKDIDPKETITAIYQLIAGFETQLAEAKAEYAQLMVNGLDQNPLIPRLSAKIKVLEKQIGEQRNRLSNKLGSQGSSESLSLFEDLRLQSEIAKARWESALQTLQQGKLQALRERQYLLIISQPMAESDTTRYADGTKWLLFFVLLGITYLVTSLLITIRRMRE", "text": "FUNCTION: May form an ATP-driven capsule polysaccharide export apparatus, in association with the VexA, VexB and VexC proteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BexC/CtrB/KpsE family."}
+{"protein": "MADNDNEDVIMDDLVEEYVETEEENFVDSEEESEDKSEDKDEIVESPSICEGFVQASSQTLVIIPDNERITSNVLTTFEATRLVAVRAQQLAINGSTMLKKKYSSPIDIAKQELFNRKIPLLVMRCIKVTPEGQKIVEIWNPREMGIPLLD", "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 archaeal RpoK/eukaryotic RPB6 RNA polymerase subunit family."}
+{"protein": "MVDTTKNTKLFTSYGVSTSKTVAPEMAAKLISKAKRPLLMVGTLALDPEILDRVVKISKTANIPIAATGSSLAALADKDVDAKYINAHMLGFYLTDPNWPGLDGNGNYDMVISIGFKKFYINQVLSAAKNFSNVKAIAIERGYIQNATMSFGNLSKAEHYAALDELVDFL", "text": "FUNCTION: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD- mediated CO oxidation. SIMILARITY: Belongs to the CdhB family."}
+{"protein": "MGFVDFFETYMVGSRVQFKQLDISDWLSLTPRLLILFGYFYLHSFFTAINQFLQFINTNSFCLRLHLLYDRFWSHVPIIGEYKIRLLSRALTYSKLKIIPTLDKVLEAIEIWFQLHLVEMTFEKKKNVQIFITEGSDDLNFFKDSKFQTTLMICNHRSVNDYTLINYLFLKSCPTKFYTKWEFLQKLRKGEDLAEWPQLKFLGWGKMFNFPRLDLLKNIFFKDETLALSSNELRDILERQNNQAITIFPEVNIMSLELSIIQRKLHQDFPFVINFYNLLYPRFKNFTTLMAAFSSIKNIKRKKNRNNIIKEARYLFHRELDKLVHKSMKMESSKVSDKTTPPMIVDNSYLLTKKEEISSGKPKVVRINPYIYDVTIIYYRVKYTDSGHDHTNGDLRLHKGYQLEQISPTIFEMIQPEMESENNIKDKDPIVVMVNVKKHQIQPLLAYNDESLEKWLENRWIEKDRLIESLQKNIKIETK", "text": "FUNCTION: Involved in the organization of the outer spore wall layers and especially in the assembly of the chitosan layer. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
+{"protein": "MAARSVDSRGLFREATKAVLGSWPVLQIAVENGFGGSHSQEKAEWMVGAIDQYFSSNADLEQYEVEDSIMGMMNDEFDTIVEDGSQALVAQQLCVLFSQCRQGETAAVQAKIAQLAQKKYDVRAKVQEVTPSDDEEESSDDEEEAMDCENTPGSSSAASLSGALGPSSAPKKEEEPEDDGWTVVRRKKK", "text": "FUNCTION: May be involved in 20S pre-rRNA processing. SIMILARITY: Belongs to the TSR2 family."}
+{"protein": "MSTDTGVSVRVRGIYSTALTKLFLDRGFRISQPSQKIAERLGIEKTYDEFDVDIYDKRDHHGVILVGTEVEKVKEVFEEEFIDVLFRKLPYQLYGIYKGLVIKRDERYVYVDIGNAIGTIPVEEGKNLHEGDEVLVQVKKHNLLPHLSTMLTIPGDYAVLIPKPVGVQRHVKISRKIRDSSERERLRILGLSIDMGEWGILWRTAAAYKDWNTLRDEIIRLSKIADRLKEAEKKSAPEQIVEGRNIYEVEFGGGAKKKLDEIRNRVVPTVEGHHMLKAYDVEFSFAVEIAEGILAKVPGQRIKVNQGFWEALLDSKGPKKGWLFFLEHNKPDGQRYKLGPGEIVEVTFNPLRITLRRNLKPGKFYDGLDLPIEFGDYAITEIEAGKWWFVHRYYDRNGNLKGEYYNINTPVEIYPDRARYIDLEIDIVKWPDGEKEIIDKDKLREHYEDGIISEKLYKAVLRITQEVYERI", "text": "FUNCTION: Probable RNase involved in rRNA stability through maturation and/or degradation of precursor rRNAs. Binds to RNA in loop regions with AU-rich sequences. SIMILARITY: Belongs to the FAU-1 family."}
+{"protein": "CCIARQICEGCICCI", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily."}
+{"protein": "MSQYTEKEPAAMDQESGKAVWPKPAGGYQTITGRRYGRRHAYVSFKPCMTRHERSLGRAGDDYEVLELDDVPKENSSGSSPLDQVDSSLPNEPIFEKSETEIPTCGSALNPTTESSQSFVAVHHSEEGRDTLGSSTNLHNHSEGEYTPGACNASGVQNGIALVHTDSYDPDGKHGEDNDRLQLSAEVVEGSRYQESSGNTLFELENREAEAYTGLSPPVPSFNCEVRDEFEGLDSVPLVKSSAGDTEFVHQNSQEIQRSSQDEMVSTKQQNNTSQERQTEHSPEDSACGPGRICSEQNTNDREKNHGSSPEQVVRPKVRKLISSSQVDQETGFNRHEAKQRSVQRWREALEVEESGSDDLLIKCEEYDGEHDCMFLDPPYSRVITQRETENNQVTPESGATAGRQEVDNPFWNGCGDYYQLYDKDEDSSECSDGEWSASLPHRFSGTEKDQSSSDESWETLPGKDENEPELQSDSSGPEEENQELSLQEGEQTSLEEGEIPWLQYNEVNESSSDEGNEPANEFAQPAFMLDGNNNLEDDSSVSEDLDVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDGLPETLVLEDHTAIGQEQCCPICCSEYIKDDIATELPCHHFFHKPCVSIWLQKSGTCPVCRRHFPPAVIEASAAPSSEPDPDAPPSNDSIAEAP", "text": "FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes. Through the ubiquitination of MFHAS1, positively regulates the TLR2 signaling pathway that leads to the activation of the downstream p38 and JNK MAP kinases and promotes the polarization of macrophages toward the pro-inflammatory M1 phenotype. Plays a role in ciliogenesis by ubiquitinating OFD1. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Endoplasmic reticulum membrane; Peripheral membrane protein Golgi apparatus membrane; Peripheral membrane protein Synapse Postsynaptic density Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes at the cytoplasmic side of endoplasmic reticulum and Golgi apparatus (By similarity). Expressed in the postsynaptic density region of synapses (By similarity). Colocalizes with PRKAR2A and PRKAR2B in the cytoplasm and the cell membrane (By similarity)."}
+{"protein": "TICTGADRPCAACCPCCPGTSCQGPEPNGVSYCRND", "text": "FUNCTION: This excitatory toxin inhibits insect calcium-activated potassium (KCa) channels (Slo-type). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 11 (kappa toxin) family."}
+{"protein": "MEKYQKATQNPLENVDNVKIESENAIPSNLQAFTKSLAVLDDNVSEFRKRMNHLSATKQILDNFNESFSSFLYGLQINAFCVDYENAPLSESFLLQAKKDQFKATLMTRTGHSISDPPYDGGVISHDPNFATADETFATNDTSFIERPETYSASR", "text": "FUNCTION: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore Note=Associates with the mitotic spindle and the kinetochore. Kinetochore association occurs only during mitosis. SIMILARITY: Belongs to the DASH complex DAM1 family."}
+{"protein": "MKFLYGIVFIALFLTVMFATQTDGCGPCFTTDANMARKCRECCGGNGKCFGPQCLCNRE", "text": "FUNCTION: Toxin with unknown function in healthy organisms. On glioma cells, interacts with chloride channels (probably ClC-3/CLCN3) and MMP2 at the surface of glioma cells. This complex is then internalized via caveolae, thus inhibiting the chloride channels necessary for cell shrinkage and tumor propagation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride channel inhibitor family."}
+{"protein": "MSTASAASSSSSSSASEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSDSGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIVATTAYTKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPARSLPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS", "text": "FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs); both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1). Independently of MAP2Ks and p38 MAPKs, acts as a key activator of NF-kappa-B by promoting activation of the I-kappa-B-kinase (IKK) core complex. Mechanistically, recruited to polyubiquitin chains of RIPK2 and IKBKG/NEMO via TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3, and catalyzes phosphorylation and activation of IKBKB/IKKB component of the IKK complex, leading to NF-kappa-B activation. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity (By similarity). Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily."}
+{"protein": "MNSMSSGHLLSRSLLKLPMSVLVKGTAIPSNPIQDLDIDTHKPVIYALPFRSNVDLLTLQTHAKEAGLPDPLEPLMLNGKAFQRYVFIASRPTLLSSDQHVPSDSIALFSELLTEHKLDSELDVQVIPATVLWGRKPGKEGQERPYLQALNGPEKALAVLASGRDCLVRFSPVVSMRYMADTHGTDASIAHKLARVARIHFSRQKLAASGPNLPQRAQLFARLMNSPAIEKAIADEAKSKQIPLEKARKEAHDILDEIAADFSYSLVKKGDRILGWLWNRIYQGLNINNAATVRRLAQDGHEIVYVPCHRSHMDYLLLSYVLYHEGMVPPHIAAGINLNFFPAGPIFRRGGAFFIRRSFKGAPLYSTIFREYLAELFAKGYSVEYFSEGGRSRTGRLLPAKTGMLAMTIQAMLRGLNRPVTLVPVYIGYEHVMEVGTYAKELRGKRKEKENAGLVLRTLRKLRNFGQGYVNFGEPIPLNQFLNETVPQWTQDIDPMGESKPQWMTPTVNKLANRMMTHINDAAAVNAMTLCATALLASRQRALARDNLIKQVDCYLSLLRNVPYSATSTLPSESAEKLVEHAESLDKFVVETDTMGDIISLDRNQSILMTYYRNNIIHLLALPSLIAQLLIRQQSVSLEKVQATVAQIYPFLKQELFLRFEAEELNDLVLRYVAELARQGLVTVEGKTVTLNQAQTQVLMLLGRIISETLQRYAIALNLLVSCPHLGKAELEEKSQEVAQRLGRLHGINAPEFFDKGVFASLFVTLQEQGYLDDQGRCVLETAKPLSRQLYALIYPEVRMTIQESLCQVDA", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family. SIMILARITY: Belongs to the GPAT/DAPAT family."}
+{"protein": "MAVWIQAQQLQGEALHQMQALYGQHFPIEVRHYLSQWIESQAWDSVDLDNPQENIKATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANNGSSPAGSLADAMSQKHLQINQTFEELRLVTQDTENELKKLQQTQEYFIIQYQESLRIQAQFGPLAQLSPQERLSRETALQQKQVSLEAWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNDYSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRSDRRGAESVTEEKFTILFESQFSVGGNELVFQVKTLSLPVVVIVHGSQDNNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNNSSSHLEDYSGLSVSWSQFNRENLPGRNYTFWQWFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSQERMFWNLMPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVYSKYYTPVPCESATAKAVDGYVKPQIKQVVPEFVNASADAGGGSATYMDQAPSPAVCPQAHYNMYPQNPDSVLDTDGDFDLEDTMDVARRVEELLGRPMDSQWIPHAQS", "text": "FUNCTION: Carries out a dual function: signal transduction and activation of transcription (PubMed:29844444). Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocated into the nucleus in response to phosphorylation. SIMILARITY: Belongs to the transcription factor STAT family."}
+{"protein": "MSSSSSSLAAAAARKRALTEQRFSELSPALSPEVVKALKGGGFRRCTPVQAAAIPLLLSHKDVAVDAATGSGKTLAFVVPVVEILRRRPSPPKPHEVLGIIISPTRELSSQIYNVAQPFFATLKGVSSMLLVGGFDIKAELKKLEEEGANILVGTPGKLFDVMERLDTLNYKNLEILILDEADRLLDLGFQKQITSIISKLPKLRRTGLFSATQTEAVKELAKAGLRNPVRVEVKTEVKPTGKDGAQQELGPSKTPLGLRLEYMICEASNKSSQLVDFLVQNNGKKIMVYFATCACVDYWAIVLPLLDSLKGSPIIPYHGKMKQGPREKALASFSALSSGILVCTDVAARGLDIPHVDLIVQYDPPQDPNVFIHRAGRTARYDQEGDAIVFLLPKEDTYVEFLKRRGVPLTERECSTNAVDIVPQIRSAALEDRNVMEKGLTAFVSFVRAYKEHHCSYIFSWKDLEIGRLGMEYGLLQIPSMPEVKHHSLSLEGFTPVKDVDVTKIKYKDKAREKQRQKTLKRKAEELALRPEIEKRRKAPEKPEKPKRKKTGKQRQAVQTKEDMDELANEYRLLKKLKRGVIDEDEYEKLTGFGESDDDDSSDGGDSDLDERKERGNKVLKKIKQKGKAKGSRRFEGRSKQKTRRR", "text": "SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4 subfamily."}
+{"protein": "MWCLAITGPPGAGKSTLARKVVEELKKAGLKVCGTSCPDVREGGRRVGFLIVDVEDGSRAWLARVDCEGPRVGRYKLCPGAEEVGVRALSKDCDVYLIDEIGPMELKLPKLREAMLRVVSGNKPFVAVYHARLRDEEFLRALSRCHKIFVTKDTREEAWKEALEALSSFSP", "text": "FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency. SIMILARITY: Belongs to the THEP1 NTPase family."}
+{"protein": "MTTSTPDIQPAVQHTAQVAIAGAGPVGLMMANYLGQMGISVLLVEKLDTLIDYPRAIGIDDESLRAMQAVGLVNDVLPHTTPWHAMRFLTPKGRCFADIQPMTDEFGWSRRNAFIQPQVDAVMYHGLQRFPQVRCLFSREVEAFSQNGDGVTLNLKGPDGERETVRADWLVACDGGASFIRRTLNVPFEGKTAPNQWIVIDIANDPLATPHVYLCCDPVRPYVSAALPHGVRRFEFMVMPGETEAQLSEPHNMRRLLSKVLPDPDRVELIRQRVYTHNARLAERFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWKLALVVNGKAGEALLDSYQQERRDHAKAMIDLSVTAGHVLAPPKRWQGAVRDGLSWLLNYLPPVKRYFLEMRFKPMPQYREGALLIDAAGKTSPVGKMFIQPQVTLESGESVLLDEVIGANFAIIGWGCNPQWGLDAGQIARWRAIGVRFIQVVPAVQIHREQDNAPGTLRVGDTQNRLKSWFAQHNTAIAVVRPDRFVAALAIPQTLGAQLTALAEKMTLATGDTARTEEKVA", "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": "MAAAKWLIASLAFASSGLAFTPEDFISAPRRGEAIPDPKGELAVFHVSKYNFDKKDRPSGWNLLNLKNGDISVLTTDSDVSEITWLGDGTKVVYVNGTDSVKGGVGIWISDAKNFGNAYKAGSVNGAFSGLKLAKSGDKINFVGYGQSTTKGDLYNEAAAKEAVSSARIYDSLFVRHWDTYVSTQFNAVFSGALTKNGDKYSFDGKLKNLVQPVKYAESPYPPFGGSGDYDLSSDGKTVAFMSKAPELPKANLTTSYIFLVPHDGSRVAEPINKRNGPRTPQGIEGASSSPVFSPDGKRIAYLQMATKNYESDRRVIHIAEVGSNKPVQRIASNWDRSPEAVKWSSDGRTLYVTAEDHATGKLFTLPADARDNHKPEVVKHDGSVSSFYFVGSSKSVLISGNSLWSNALYQVATPGRPNRKLFYANEHDPELKGLGPNDIEPLWVDGARTKIHSWIVKPTGFDKNKVYPLAFLIHGGPQGSWGDNWSTRWNPRVWADQGYVVVAPNPTGSTGFGQKLTDDITNDWGGAPYKDLVKIWEHVHNNIKYIDTDNGIAAGASFGGFMVNWIQGQDLGRKFKALVSHDGTFVGSSKIGTDELFFIEHDFNGTFFEARQNYDRWDCSKPELVAKWSTPQLVVHNDFDFRLSVAEGVGLFNVLQEKGVPSRFLNFPDETHWVTKPENSLVWHQQVLGWVNKWSGINKSNPKSIKLSDCPIEVVDHEAHSYFDY", "text": "FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini. Contributes to pathogenicity (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S9C family."}
+{"protein": "MKSLHVAANAGDLAEDCGILGGDADDTVLMDGIDEVGREIWLDDHGGDNNHVHGHQDDDLIVHHDPSIFYGDLPTLPDFPCMSSSSSSSTSPAPVNAIVSSASSSSAASSSTSSAASWAILRSDGEDPTPNQNQYASGNCDDSSGALQSTASMEIPLDSSQGFGCGEGGGDCIDMMETFGYMDLLDSNEFFDTSAIFSQDDDTQNPNLMDQTLERQEDQVVVPMMENNSGGDMQMMNSSLEQDDDLAAVFLEWLKNNKETVSAEDLRKVKIKKATIESAARRLGGGKEAMKQLLKLILEWVQTNHLQRRRTTTTTTNLSYQQSFQQDPFQNPNPNNNNLIPPSDQTCFSPSTWVPPPPQQQAFVSDPGFGYMPAPNYPPQPEFLPLLESPPSWPPPPQSGPMPHQQFPMPPTSQYNQFGDPTGFNGYNMNPYQYPYVPAGQMRDQRLLRLCSSATKEARKKRMARQRRFLSHHHRHNNNNNNNNNNQQNQTQIGETCAAVAPQLNPVATTATGGTWMYWPNVPAVPPQLPPVMETQLPTMDRAGSASAMPRQQVVPDRRQGWKPEKNLRFLLQKVLKQSDVGNLGRIVLPKKEAETHLPELEARDGISLAMEDIGTSRVWNMRYRFWPNNKSRMYLLENTGDFVKTNGLQEGDFIVIYSDVKCGKYLIRGVKVRQPSGQKPEAPPSSAATKRQNKSQRNINNNSPSANVVVASPTSQTVK", "text": "FUNCTION: Participates in abscisic acid-regulated gene expression during seed development. Regulates the transcription of SGR1 and SGR2 that are involved in leaf and embryo degreening. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly found in the nucleus."}
+{"protein": "MITVVKRNGRIEPLDITKIQKYTKDATDNLEGVSQSELEVDARLQFRDKITTEEIQQTLIKTAVDKIDIDTPNWSFVASRLFLYDLYHKVSGFTGYRHLKEYFENAEEKGRILKGFKEKFDLEFLNSQIKPERDFQFNYLGIKTLYDRYLLKDANNNPIELPQHMFMSIAMFLAQNEQEPNKIALEFYEVLSKFEAMCATPTLANARTTKHQLSSCYIGSTPDNIEGIFDSYKEMALLSKYGGGIGWDFSLVRSIGSYIDGHKNASAGTIPFLKIANDVAIAVDQLGTRKGAIAVYLEIWHIDVMEFIDLRKNSGDERRRAHDLFPALWVCDLFLKRVLEDAMWTLFDPYECKDLTELYGQDFEKRYLEYEKDPKIIKEYINAKDLWKKILMNYFEAGLPFLAFKDNANRCNPNAHAGIIRSSNLCTEIFQNTAPNHYYMQIEYTDGTIEFFEEKELVTTDSNITKCANKLTSTDILKGKPIYIATKVAKDGQTAVCNLASINLSKINTEEDIKRVVPIMVRLLDNVIDLNFYPNRKVKATNLQNRAIGLGVMGEAQMLAEHQIAWGSKEHLEKIDALMEQISYHAIDTSANLAKEKGVYKDFENSEWSKGIFPIDKANNEALKLTEKGLFNHACDWQGLREKVKANGMRNGYLMAIAPTSSISILVGTTQTIEPIYKKKWFEENLSGLIPVVVPNLNVETWNFYTSAYDIDAKDLIKAAAVRQKWIDQGQSLNVFLRIENASGKTLHDIYTLAWKLGLKSTYYLRSESPSIDEKSVLDRSVECFNCQ", "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 large chain family."}
+{"protein": "MLILLGYLVVIGTVFGGYVMTGGHLGALYQPAELVIIGGAGIGAFIVGNNGKAIKGTMKAIPLLFRRSKYTKSMYMDLLALLYRLMAKSRQQGMFSLERDIENPKESEIFASYPRILADAVMLDFIVDYLRLIISGNMNTFEIEALMDEEIETHESEAEVPANSLAMVGDSLPAFGIVAAVMGVVHALASADRPAAELGALIAHAMVGTFLGILLAYGFISPLATVLRQKSAETTKMMQCVKITLLSNLNGYAPPIAVEFGRKTLYSSERPSFIELEEHVRAVRNPNQQQTTEEA", "text": "FUNCTION: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MotA family."}
+{"protein": "MATQLPSPTATTSHSGNEPRRVIRESCNNCSAQKIRCGKQRPACARCVNKKLQCNYSYSQRSGRRSSSMNTQRGGPHIAFLPGIPDTPATMPDANAMSAMYGSLTTSSPGLQGTTLSPSIETSLEYDQNPFEDPNQYHDLTFDFLASPPNTEPLHSRSTSSNTGTDMGDTAMVDSEAFWHSFPSMPPQNLDALRSVSNHPIFDQDQVASFRRSLEKTVQHGHDCMALALQVVNDLSVTREPCLVATSNPMTGIETHQMQARDVDTVLFINRDAAQSVKKILDCSCSSDQAVSLACYLATSKIVDWYGAAIEAVGERTEDFSKNAGPKTSQGIMAERIIARPIYMGKYCLDPEVQRVVRAQVVLGELKEHVQPLLNSLPRFHITGLEAESDSSANGQQACILRNQLRNVIQSARDLNGTGSS", "text": "FUNCTION: Transcription regulator of the gene cluster that mediates the biosynthesis of elsinochrome C, a perelyenequinone phytotoxin structurally similar to cercosporin. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MTPGALLLLLLGVLGAHLAPGARGSEAEGRLREKLFSGYDSTVRPAREVGDRVWVSIGLTLAQLISLNEKDEEMSTKVYLDLEWTDYRLSWDPEEHEGIDSLRISAESVWLPDVVLLNNNDGNFDVALDINVVVSSDGSMRWQPPGIYRSSCSIQVTYFPFDWQNCTMVFSSYSYDSSEVSLQTGLSPEGQERQEVYIHEGTFIENGQWEIIHKPSRLIQPSVDPRGGGEGRREEVTFYLIIRRKPLFYLVNVIAPCILITLLAIFVFYLPPDAGEKMGLSIFALLTLTVFLLLLADKVPETSLSVPIIIKYLMFTMVLVTFSVILSVVVLNLHHRSPHTHQMPLWVRQIFIHKLPLYLGLKRPKPERDQMQEPPSIAPRDSPGSGWGRGTDEYFIRKPPNDFLFPKPNRFQPELSAPDLRRFIDGPNRAVGLPPELREVVSSISYIARQLQEQEDHDVLKEDWQFVAMVVDRLFLWTFIIFTSVGTLVIFLDATYHLPPADPFP", "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-1/CHRNB1 sub- subfamily."}
+{"protein": "MMAARMMAAGLAATALSAHAFRIPTPGEQDARIQTVPYHPEEVVLVRAWNGYVTRIVFDEQEKIIDVAAGFADGWQFSPEGNVLYIKAKSFPAQGSPAQAPEPGLWNTNLLVKTDRRLYDFDLVLASADAATPQALQRSRMAYRLQFRYPAAPQAASRASPVGPAVPAGALNRRYAMQVGNGSDGIAPIAAYDDGRHTWLTFRPGQPFPAVFAVAPDGTETLVNLHIDNQSLVIHRVAPVLMLRSGASVIRIVNQNGDASASPAFECHAEPAL", "text": "SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the TrbG/VirB9 family."}
+{"protein": "MVNWELLKNPINWLIVILMLTIAGMAATLVCNHFGKNAVTSE", "text": "FUNCTION: Together with P22, forms the internal part of the portal complex embeded in the virion internal membrane and which plays critical roles in genome packaging and genome ejection. Both proteins multimerize as a single ring-shaped heterdodecamer arranged around a central channel and interact with the P6/P9 external part of the portal. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein. Note=Part of the capsid inner membrane. Binds the portal complex at the capsid vertex."}
+{"protein": "MEIIFYHQTFDTPFWIRELEKQLPGARVREWKAGDNQPADYALVWHPPVEMLQGRALKAVFALGAGVDSILSKLRDHPDMLPLSIPLFRLEDTGMGRQMQEYAVSQVLHWFRRFDDYQALKLASRWQPLPEYRADEFTVGIMGAGVLGAKVAESLQPWGFPLRVWSRSRKSWPQVQSFAGQAELGEFLQGTRVLINLLPNTAETAGIINQTLLAQLPDESYVLNLARGVHVVEEDLLAALNSGKLKGAMLDVFSREPLPQESPLWAHPRVAMTPHVAAVTRPMEAITYIAETISRLERGEPVSGQVDRQRGY", "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. GhrA subfamily."}
+{"protein": "MAKEKARYFTFLLYPESIPSDWELKLETLGVPMAISPLHDKDKSSIKGQKYKKAHYHVLYIAKNPVTADSVRKKIKLLLGEKSLAMVQVVLNVENMYLYLTHESKDAIAKKKHVYDKADIKLINNFDIDRYVTLDVEEKTELFNVVVSLIRAYTLQNIFDLYDFIDENGETYGLTINLVNEVIAGKTGFMKLLFDGAYQRSKRGTKNEER", "text": "FUNCTION: Is essential for plasmid replication. Nicks the positive strand at the plus origin of replication. SIMILARITY: Belongs to the Gram-positive plasmids replication protein type 2 family."}
+{"protein": "MASLQQSRRLVTEIPGPASQALTHRRAAAVSSGVGVTLPVFVARAGGGIVEDVDGNRLIDLGSGIAVTTIGNSSPRVVDAVRTQVAEFTHTCFMVTPYEGYVAVAEQLNRITPGSGPKRSVLFNSGAEAVENAVKIARSYTGKPAVVAFDHAYHGRTNLTMALTAKSMPYKSGFGPFAPEIYRAPLSYPYRDGLLDKQLATNGELAAARAIGVIDKQVGANNLAALVIEPIQGEGGFIVPAEGFLPALLDWCRKNHVVFIADEVQTGFARTGAMFACEHEGPDGLEPDLICTAKGIADGLPLSAVTGRAEIMNAPHVGGLGGTFGGNPVACAAALATIATIESDGLIERARQIERLVTDRLTTLQAVDDRIGDVRGRGAMIAVELVKSGTTEPDAGLTERLATAAHAAGVIILTCGMFGNIIRLLPPLTIGDELLSEGLDIVCAILADL", "text": "SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MANFDLTRINCQFLDRHLTFPLLEFLCGKEIYNQQELLEYILETVNKTNMIDYTMDTRKRLNLSQEMPEELVQRKAEVLATLKQLQNEVAPIMKATDILKNGESMKDSKTFVNALQKDYNFKVEHLESAYKLAKYLYECGNYQESTSYLYFCLIVMSPNDKNYLNVLWGKLAAEILTLNWNTALEDLTRLRDYIDNANFSTIQALQQRTWLIHWSVLVFFNHPKGRDLIIEMFLYKPLYLNAIQTMCPHIMRYLATAVVINRTRRNALKDLIKVIQQESYTYRDPITEFLECLYVNFDFEGARLKLHECQTVILNDFFIVACLNEFVEDARLMIFETFCRIHQCITISMLADKLNMKPNEAECWIVNLIRNARLNAKIDSKLGHVVMGTQPLSPYQQLVEKIDSLSMRSEHLAGLIERKSKQKQNQESADSWKYY", "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. 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 (PubMed:18493598). In addition to its role in the eIF-3 complex, also functions in protein ubiquitination and degradation (PubMed:18493598, PubMed:28505193). During mitosis required for regulating mitotic microtubule growth and kinetochore formation, and consequently is required for satisfying the spindle assembly checkpoint (SAC) during metaphase to prevent delays in mitotic progression (PubMed:28505193). This is likely by promoting the ubiquitination and degradation of Klp67A, a kinesin-like protein that suppresses microtubule polymerization at plus ends (PubMed:28505193). Acts in the COP9 signalosome (CSN) mediated regulation of cullin neddylation by promoting Cul1 and Cul3 neddylation and negatively regulating the CSN complex subunit CSN5 (PubMed:18493598). SUBCELLULAR LOCATION: Cytoplasm Microsome Endoplasmic reticulum Note=Uniformly distributed in interphase and mitotic cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit E family."}
+{"protein": "MDKETNDNEYRRQSEHRTSAPKRKKKKKIRKLPIILLIVVILLIALVVYIVHSYNSGVEYAKKHAKDVKVHQFNGPVKNDGKISILVLGADKAQGGQSRTDSIMVVQYDFINKKMKMMSVMRDIYADIPGYGKHKINSAYALGGPKLLRKTLDKNLGINPEYYAVVDFTGFEKMIDELMPEGVPINVEKDMSKNIGVSLKKGNHRLNGKELLGYARFRHDPEGDFGRVRRQQQVMQTLKKEMVNFRTVVKLPKVAGILRGYVNTNIPDSGIFQTGLSFGIRGEKDVKSLTVPIKNSYEDVNTNTDGSALQINKNTNKQAIKDFLDED", "text": "FUNCTION: Involved in SarA attenuation. Affects resistance to oxacillin and teicoplanin, as well as the synthesis of virulence factors (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family."}
+{"protein": "MYHDYASKLLADYRSDPPLWESDLPRHNRYSDNILNSRYCGNKNGAAPVYNEYTNSPEKAEKGLQLSDLRNFSFMLNPQHKNIGYGDAQDLEPYSSIPKNKLFNHFKNHRPAFSTHTENLIRRNVVRTEKKTFPQVASLKGTQKNCLTQPSSLPSLKNPKNSSVPSTRFSEHTKFFSYEDIPKLKTKGTIKHEQHLGDQMPGQHYNGYIPHKDVYNILCLAHNLPASVEKGIAGRGIPLGNPHVKPNIEQELIKSTSTYTGVPMLGPLPPKDSQHGREYQEFSANRHMLQVANILHSVFANHSIKPQILEDIPVLNAQLTSIKPVSPFLNKAYQTHYMENIVTLVPRFKSIANYSSPIPNYSKRNSGQAEYFDTSKQTISRHNNYIPKYTGGIGDSKLDSTFPKDFNASSVPLTSAEKDHSLRGDNSACCISSISPSL", "text": "FUNCTION: Together with the penton and the other minor capsid proteins (M1249L, p17), forms a complicated network immediately below the outer capsid shell, stabilizing the whole capsid (PubMed:31624094). Plays an essential role in the formation of infectious virus particles. Especially required for the formation of the capsid vertices (PubMed:17005638). During virion assembly, associates with the membrane and probably mediates the docking of the penton complex to the inner membrane, where it recruits the capsomers to form the penton core (PubMed:31624094). SUBCELLULAR LOCATION: Virion Note=Localizes in close proximity to the capsid vertices. SIMILARITY: Belongs to the asfivirus p49 structural protein family."}
+{"protein": "MIPRIVVVLLSVLAVVTARRSYEGYKVYGIVPESPDEAEILYQIRQSNPDLDFWHLTKQPGDEARVLVAPKDQRSFLIKLIRHGLHYQEVISDVEGTLAPYNEPRTRGMSLDRDVSTSYLRHNEINEYLQTLSQKYPSLVSVEEAGTSYEGRSIKTITINKKPGNAVVFLDAGIHAREWIAPATALYAIEQLVEHSSENQEVLSNLTWVIMPVVNPDGYEFSHETDRFWRKTRKPTGKTCKGTDGNRNFDYHWGEVGASTQACADTFRGETAFSEPETRAVRDAVMKLKGSCKFYLSLHSYGNYILYPWGWTSKLPETWEAIDEVAQAGAEAIKQSTGSRYTVGSSTNVLYAAAGGSDDWAFAVAEVPISITMELPGGGNGGFNPPPSSIEKIVNESWVGIKAMALKVAQMF", "text": "FUNCTION: Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus (PubMed:34750241). During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut (PubMed:25521592). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the peptidase M14 family."}
+{"protein": "MSNSDIRSFFGGGNAQKKPKVSPTPTSPKPKRSLKKKRIVLSDDEDGTIENSKVPASKSKVQKRNESEDISHSLPSIVHEDDKLVGSDGVSTTPDEYFEQQSTRSRSKPRIISNKETTTSKDVVHPVKTENFANDLDTTSDSKPVVHQTRATRKPAQPKAEKSTTSKSKSHTTTATTHTSRSSKSKGLPRFSDEVSQALKNVPLIDVDSMGVMAPGTFYERAATTQTPGSKPVPEGNSDCLSGISFVITGILETLTRQEATDLIKQYGGKVTGAPSVRTDFILLGENAGPRKVETIKQHKIPAINEDGLFYLITHLPASGGTGAAAQAAQQKKEQEEKKILETVARMDDSNKKESQPSQIWTSKYAPTSLKDICGNKGVVQKLQKWLQDYHKNRKSNFNKPGPDGLGLYKAVLLSGPPGIGKTTAAHLVAKLEGYDVLELNASDTRSKRLLDEQLFGVTDSQSLAGYFGTKANPVDMAKSRLVLIMDEIDGMSSGDRGGVGQLNMIIKKSMIPIICICNDRAHPKLRPLDRTTFDLRFRRPDANSMRSRIMSIAYREGLKLSPQAVDQLVQGTQSDMRQIINLLSTYKLSCSEMTPQNSQAVIKNSEKHIVMKPWDICSRYLHGGMFHPSSKSTINDKLELYFNDHEFSYLMVQENYLNTTPDRIRQEPPKMSHLKHLELISSAANSFSDSDLVDSMIHGPQQHWSLMPTHALMSCVRPASFVAGSGSRQIRFTNWLGNNSKTNKLYRMLREIQVHMRLKVSANKLDLRQHYIPILYESLPVKLSTGHSDVVPEIIELMDEYYLNREDFDSITELVLPADAGEKLMKTIPTAAKSAFTRKYNSSSHPIAFFGSSDVLPMKGSAQREVPDVEDAIEAEDEMLEEASDSEAANEEDIDLSKDKFISVPKKPKKRTKAKAEASSSSSTSRRSRKKTA", "text": "FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 1 is essential for cell cycle progression. It may associate with components of the DNA replication machinery and serve to enhance the efficiency of DNA replication. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the activator 1 large subunit family."}
+{"protein": "MAGAAAAVASGISIRPVAAPKISRAPRSRSVVRAAVSIDEKAYTVQKSEEIFNAAKELMPGGVNSPVRAFKSVGGQPIVFDSVKGSHMWDVDGNEYIDYVGSWGPAIIGHADDKVNAALIETLKKGTSFGAPCALENVLAQMVISAVPSIEMVRFVNSGTEACMGALRLVRAFTGREKILKFEGCYHGHADSFLVKAGSGVATLGLPDSPGVPKGATVGTLTAPYNDADAVKKLFEDNKGEIAAVFLEPVVGNAGFIPPQPAFLNALREVTKQDGALLVFDEVMTGFRLAYGGAQEYFGITPDVTTLGKIIGGGLPVGAYGGRKDIMEMVAPAGPMYQAGTLSGNPLAMTAGIHTLKRLMEPGTYEYLDKVTGELVRGILDVGAKTGHEMCGGHIRGMFGFFFAGGPVHNFDDAKKSDTAKFGRFHRGMLGEGVYLAPSQFEAGFTSLAHTTQDIEKTVEAAEKVLRWI", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
+{"protein": "PQVGLIPFPRV", "text": "FUNCTION: Mediates visceral muscle contractile activity (myotropic activity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the periviscerokinin family."}
+{"protein": "MSIVTKSIVNADAEARYLSPGELDRIKSFVMSGQRRLRIAQILTDNRERIVKQAGQQLFQKRPDIVSPGGNAYGEEMTATCLRDLDYYLRLITYSVVAGDVIPIEEIGLVGVREMYNSLGTPLSGVAEGIRSMKSVVSGLLAGDDAAEASFYFDYAIGAMQ", "text": "FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a 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": "MIDGYSPVLQSLLGTLLTWGLTAAGSALVFIFSSGQRQILDGSLGFAAGVMLAASYWSLLAPAIEMAENSNQYGSFAFVPAAVGFLVGAGFVYLADQLMPALGFSEDPYSIATLNQDSKPIKEKDEGDLYEDKELSIRIGRGGFHQDKIENGDVYQRKRGTVSPLAEDFSMLNPREAAHKGGSSWRRIMLLILAITIHNIPEGLAVGVGFGAIGKTPSATFENARNLALGIGIQNFPEGLAVSLPLRGAGVSTWKAFWYGQLSGMVEPIAGLLGTIAISLAEPLLPYALAFAAGAMVYVVTDDIIPEAQACGNGKLASWTCIFGFIVMMSLDVGLG", "text": "FUNCTION: Functions as a cellular zinc transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Nucleus Cytoplasm Golgi apparatus. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
+{"protein": "MAMMPSDSSHHGIVENSPYRTTQGRNEETGELGASWYFSRKEIEENSPSRRDGIDLKKESYLRKSYCTFLQDLGMRLKVPQVTIATAIVFCHRFYLRQSHAKNDRRTIATVCMFLAGKVEETPRPLKDVILVSYEIIHKKDPAAGQRIKQKEVYDQQKELILLAERVVLATLGFDLNVHHPYKPLVEAIRKFKVAQNALAQVAWNFVNDGLRTSLCLQFKPHHIAAGAIFLAAKFLKVKLPSDGEKVWWQEFDVTPRQLEEVSNQMLELYEQNCAAQAQPSHGNEAEGSSASVPNQRVSVKSEETPLPHQSKQSSSQHSTGAPSHHGVEHSNLEKQTVDQKMLQNDNGDHGSNKTRSNQSGSRVDFGANDGLHHDKQSMTENKNLPSHGNSSEIRDVNRNGNDGTNVTSLMVNKIDKDKVKAQMEKQRKLKGDVARKVEVIDDDDDLERQLEHDIELAVEDNKIKQERKQSSPHVMHRGDHRNADQVTGNGHLGKQNTPETAQDAPMDDIKEQRNSHGSKHHDSHDTAHERGERDYKRPRPEG", "text": "SIMILARITY: Belongs to the cyclin family. Cyclin T subfamily."}
+{"protein": "MSAAPVVDAEYMAEVERARRDLRALIASKSCAPIMLRLAWHDAGTYDKATKTGGPNGSIRFPQEYSHAANAGIKIAIDLLEPMKQKHPKITYADLYQLAGVVAVEVTGGPTIDYVPGRRDSSDSPEEGRLPDAKKGAAHLREVFYRMGLSDKDIVALSGGHTLGKARPERSGFDGAWTKDPLKFDNSYFIELLKENSEGLLKLPTDKALVEDPTFRRYVELYAKDEDAFFRDYAESHKKLSELGFTPPRSAFIYKSCQKPKSLLMQTAAGVAVAAAVVAWAYLCESNKRLG", "text": "FUNCTION: Plays a key role in hydrogen peroxide removal. SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein Note=Targets to peroxisomes and to a reticular compartment circulating the nucleus. SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase subfamily."}
+{"protein": "MAEAKTCNMEVSCALPEGSVKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGAKKVIGIECSSISDYAIKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIYARDKWLNPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVSNACLIKEVDIYTVKVDDLTFTSPFCLQVKRNDYIHAMVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTISMKPNAKNNRDLDFTVDIDFKGQLCELSCSTDYRMR", "text": "FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in target proteins. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). Methylates ilf3 to regulate its DNA-binding activity (PubMed:18636753). Required for neural induction, playing a key role in the control of epidermal versus neural cell fate choice (PubMed:16214893). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Cytoplasm, cytosol Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family."}
+{"protein": "MLTLLNLLSAVALLVWGTHIVRTGVMRVFGARLRTVLSRSVEKKPLAFCAGIGVTALVQSSNATTMLVTSFVAQDLVALAPALVIVLGADVGTALMARILTFDLSWLSPLLIFIGVIFFLGRKQSRAGQLGRVGIGLGLILLALELIVQAVTPITQANGVQVIFASLTGDILLDALIGAMFAIISYSSLAAVLLTATLTAAGIISFPVALCLVIGANLGSGLLAMLNNSAANAAARRVALGSLLFKLVGSLIILPFVHLLAETMGKLSLPKAELVIYFHVFYNLVRCLAMLPFVDPMARFCKTIIRDEPELDTQLRPKHLDVSALDTPTLALANAARETLRIGDAMEQMMEGLNKVMHGEPRQEKELRKLADDINVLYTAIKLYLARMPKEELAEEESRRWAEIIEMSLNLEQASDIVERMSSEIADKSLAARRAFSLDGLKELDALYEQLLSNLKLAMSVFFSGDVTSARRLRRSKHRFRILNRRYSHAHVDRLHQQNVQSIETSSLHLGLLGDMQRLNSLFCSVAYSVLEQPDEDEGRDEY", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To B.subtilis YqeW."}
+{"protein": "MIMEALVALLRFPFYSFGKQSYQVRQSLLLPSPSALKGALAKGIILLGGKKGKSLDEIAKKTVEELENKLIYVGAKPYKSSIIKTPILLKRLRNLEDQKNPEKSDAMRREYVFAREILAIYVFRRKLSEEEKDLMLKAVYLIDQLGDTECVGNVIKTEWVEVKEEKAPLKTYVKFKKVSKMSINGGIIENMLETPNFGNKVKEEPYLLPLIEKRYRRSSYYVESDRIFDGNYKIIAFDEVIGLWI", "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 Cas5 family. Subtype I-A/Apern subfamily."}
+{"protein": "MPSVCHTSPIEKIIQQGHRIQNDSLIPSKRTKLAHTELTAHYATEDSHVEKHFLHNGSNFDGIDNVRYQNQPSPLTFITPNNTVDSSDWVPQFSSMKIDDSLEFSSEYKRLYSNYESQQRLNSSRQHLPFKNCMIRKTSCTYPPQKTLRQQRQGNRDNPTDAFQFDAEFQVLEREIQKERYEPITRRDEKWFDQDQSELQRIATDIVKCCTPPPSSASSSSTLSSSVESKLSESKFIQLMRNISSGDVTLKKNADGNSASELFSSNNGELVGNRHIFVKDEIHKDILD", "text": "FUNCTION: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7 (PubMed:12167700, PubMed:9864360, PubMed:23812376). 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 (PubMed:23812376). Acts as an activator of the seryl-tRNA synthetase SES1 by increasing its binding to tRNA (PubMed:12204379, PubMed:17451428). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome Note=Cycles between the cytosol and the peroxisome. SIMILARITY: Belongs to the peroxin-21 family."}
+{"protein": "MVGSVAGNMLLRAAWRRASLAATSLALGRSSVPTRGLRLRVVDHGPHSPVHSEAEAVLRPLYMDVQATTPLDPRVLDAMLPYLVNYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVARFYRSRKKHLVTTQTEHKCVLDSCRSLEAEGFRVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGQICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKLYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPLVVGLGAACELAQQEMEYDHKRISKLAERLVQNIMKNLPDVVMNGDPKQHYPGCINLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTAEKCIHHVKRLREMSPLWEMVQDGIDLKSIKWTQH", "text": "FUNCTION: Mitochondrial cysteine desulfurase, of the core iron-sulfur cluster (ISC) assembly complex, that catalyzes the desulfuration of L- cysteine to L-alanine, as component of the cysteine desulfurase complex, leading to the formation of a cysteine persulfide intermediate at the active site cysteine residue and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (PubMed:25597503). The persulfide is then transferred on the flexible Cys loop from the catalytic site of NFS1 to the surface of NFS1 (By similarity). After the NFS1-linked persulfide sulfur is transferred to one of the conserved Cys residues of the scaffold, a reaction assisted by FXN (PubMed:25597503). 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). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily."}
+{"protein": "MEYESVLIVKPEVFIYKIPPRASNRGYRAGDWNLKEPTWTGRMRLVAKGTAVVLKLEDKTSGALFANCPIDTYPGVAIEAVSDSSRYFVIRVQDDNGRSAFLGLGFGDRSDSFDLNVALQDHFKWVKNQEQIEKEKTEPKQELDLGFKEGETIKINMRITKKDGSEGSSRTGKNKGSSGVLPPPPGGLGKIAPPPAAAAANTTVRQSPGVSPAHRPAAGGSEWTDYASAGGNQGQQNSANANWVQF", "text": "FUNCTION: May be involved in endocytosis. SIMILARITY: Belongs to the NECAP family."}
+{"protein": "MAYHSFLLEPITCHAWNKDATQIAFCPNSHDVHIYKKDGDKWSKIHELKEHNGHVTGIDWAPESNRIVTCGTDRNAYVWTLKNNVWKPTLVILRINRAARCVKWSPKENKFAVGSGSRLISICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSSDFKSRIFSAYIKEVEERPAPTPWGSKMPFGELMFESSSSCGWVHSVCFSHSGDRMAWVSHDSTICISDATKKMRVTSLITDTLPLLCVTFITENSLVAAGHDCFPVLYIYDEAQGTLSFGGKLDIPKQSSQRGMTARERFQNLDKKASSDTNNITLDSLHKNSISQLSVLSGGKAKCSKFCTTGLDGGMCIWDVKSLESAMKDLKIK", "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 Nucleus. SIMILARITY: Belongs to the WD repeat ARPC1 family."}
+{"protein": "MNVTFDGIYNEIIENMHHFASEEKDFSKLTQYKDLISKTIDEVVEEVFNDIFSYEKTKTLFDESKRKELEEDFKNWIKGLFEISNDSDLNEFYKEIVKRGIKYVEKDFLPEYLTAIIIKIEDRLKNKLKEELKEDAQEIVDILDDLLKRVILLNVAAYMNFESKVLDYIGINQNLKKNAVKLGIKKMGL", "text": "SIMILARITY: To M.jannaschii MJ1461."}
+{"protein": "MFMNCRRVKKWHFLQLLSMCCVMSVLMVCWEHVDHHVVSHVKSYSYRYLINSYDFINKSLSVSPEEAARFGSFPYLLDRRDVCKNKDVLLLLFVKSSPGNFKRRQAIRSTWGNESYISQELGVVVKVVFAMGVRPDRSGHKTMQRELRKEHMAHHDLIQQDFLDTFHNLTVKLLLQFRWTHENCAHAHFLMSADDDVFIHVPNLVHYLQELKSQNVRNLWVGHVHRGAPPVRKRDSKYYMPFDMYQWSSYPDYTAGAGYVVSGDVAAKIYQATQSLNASMYIDDVFMGICAIAAGVSPQEHVYFSGEGKTPYHPCIYEKMITSHGHEGDIRYLWKAATGPQVEGISSGLLGKLYCAAVKMTLLCKPYFTNTYSCMAAFT", "text": "FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family."}
+{"protein": "MNVLQLMQQHDTMPETYKRLSVEEMEKRVARVKRELGTRLFIPGHHYQKDEVIQFADATGDSLQLAQVAAKNKEAEYIVFCGVHFMAETADILTSDEQIVILPDMRAGCSMADMAEIEQVERAWPILQQLFGDTILPLTYVNSTAAIKAFVGVHGGATVTSSNAKKMVAWAFTQKERIFFLPDQHLGRNTAYDLGVPLEQMAVWDPITNTLQYEGDVQQIKVILWKGHCSVHENFTVKHIEHIRKTKPDMKIIVHPECSWEVVQQADDAGSTKYIIETIANAPAGSKWAIGTEMNLVNRIIQQHPDKEIVSLNPYMCPCLTMNRIDLPHLLWALESLLEGKVVNRITVPKDVAEGAMLALERMLARA", "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": "MSFIKNLLFGGVKTSEDPTGLTGNGASNTNDSNKGSEPVVAGNFFPRTLSKFNGHDDEKIFIAIRGKVYDCTRGRQFYGPSGPYTNFAGHDASRGLALNSFDLDVIKDWDQPIDPLDDLTKEQIDALDEWQEHFENKYPCIGTLIPEPGVNV", "text": "SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily."}
+{"protein": "MSSSVPNSDRKIVTGPAGYILEDVPHFSDDFPDHPTYPNPLQDNAAYSVVKQYFVDEDDTVPQKIVVHPDSPRGTHFRRAGPRQRVYFESDDVLACIVTCGGLCPGLNTVIREIVCGLSYMYGVKRILGIDGGYRGFYARNTIHLDLKTVNDIHRSGGTILGTSRGGHNTTKIVDSIQDRGINQVYIIGGDGSQKGAAAIFEEIRKRKLKVAVAGIPKTIDNDIPIIDRSFGFDTAVEEAQRAINAAHVEATSFENGIGLVKLMGRYSGFIAMHATLASRDVDCCLIPESPFFLEGSGGLFEFIDKRLKESGHMVIVIAEGAGQDLLSESMKESTTLKDASGNKLLQDIGLWISQRIKDHFAKKMTLTLKYIDPTYMIRAVPSNASDNVCCTLLAQSAVHGVMAGYNGFTVGLVNGRHTYIPFNRITEKQNKVVITDRMWARLLSSTNQPSFMKQADKIHSNQLVGEPGTMKW", "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 Note=May be associated with the plasma membrane. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily."}
+{"protein": "MLSYGERLGSPAVSPLPVRGGHVMRGTAFAYVPSPQVLHRIPGTSAYAFPSLGPVALAEHTCPCGEVLERHEPLPAKLALEEEQKPESRLVPKLRQAGAMLLKVPLMLTFLYLFVCSLDMLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIIVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHITRLVVASFNIHGGRDAPDLLKIITEPFTKLIIQLDESVITSIATGDESLRNHSLIQIWCHPDSLQAPTSMSRAEANSSQTLGNATMEKCNHIFVDTGLPDLAVGLILLAGSLVLLCTCLILLVKMLNSLLKGQVAKVIQKVINTDFPAPFTWVTGYFAMVVGASMTFVVQSSSVFTSAITPLIGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSAFQIALCHFFFNISGILLWYPVPCTRLPIRMAKALGKRTAKYRWFAVLYLLVCFLLLPSLVFGISMAGWQVMVGVGTPFGALLAFVVLINVLQSRSPGHLPKWLQTWDFLPRWMHSLKPLDHLITRATLCCARPEPRSPPLPPRVFLEELPPATPSPRLALPAHHNATRL", "text": "FUNCTION: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane (PubMed:26047794, PubMed:8327470, PubMed:12324554, PubMed:20335586). The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Localized at the brush border membranes of the proximal tubules. Internalized from the cell surface upon PTH stimulation. SIMILARITY: Belongs to the SLC34A transporter family."}
+{"protein": "MTSNGLPVPAQNSNYMENGRWYHGFRRGLYMYPCDEPEKDRMDIYHQFFAVARRGQLHQAPVPSEPHLQPRILDVGCGTGIWAIDMADKYLNAEVLGLDLVNIQPEKIPPNLRFRVPRDYESPWTLGEDSWDLIHLRMACGSVESWPELYQKIYTHLKPGTGWIEHIEIDMEPRCDDYTLPPDSMLRKWYGWLADATQRAYRPIAYEHRTRQLLQAAGFIDIQETVIRVPYNTWPNDPHQKDIGRWYNLGLTEGLEALTFAPLTRVYHWDLNAHVRPIVEGVRRELCNRKIHAYNNIHIWTARRPQQ", "text": "FUNCTION: Methyltransferase that performs automethylation (By similarity). No other methyl-accepting substrate has been identified yet (By similarity). Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression (By similarity). Controls the expression of the T-toxin gene cluster (PubMed:22383877). Promotes oxidative stress tolerance and acts as a virulence factors during infection (PubMed:22383877). Negatively regulate mycelial pigmentation and controls sexual development, as well as asexual development during vegetative growth (PubMed:22383877). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the methyltransferase superfamily. LaeA methyltransferase family."}
+{"protein": "MVTEQEVEAIGKTLVDSTQPLQARFRALFTLRGLGGPDAISWISRGFEDSSALLKHELAYCLGQMRDPRAIPVLVSVLQDRNQEPMVRHEAGEALGAIGNPKVLGLLKQYSTDPVVEVAETCQLAVRRLEWLQQHPGEATCAGPYLSVDPAPPAAEGDVGRLRETLLDEAQPLFERYRAMFALRNVGGKEAALALAEGLKCGSALFRHEVGYVLGQLQHEAAVSELAATLARTTESPMVRHECAEALGAIARPACLAALREYITDPERVVRESCEVALDMYEYENGQDFQYADGLERLRPPP", "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": "MTDRSTLDDAPAQADFIIAGATLIDGGGGPARQGDLAVRGGRIVALGDFAHAPGVPVIDARGLALAPGFIDSHTHDDGYLLAHPEMLPKVSQGITTVVTGNCGISLAPLSRRQIPQPLDLLGPPELFRFATFRDWLRALAETPAAVNVIPLVGHTTLRVAVMDDTGRAATDAERAAMRALLDEALQAGAFGVSTGTFYPPASAAPTDEIIDVCQPLRGRAGAIYATHLRDEADHIVPAMEEALLIGRELDCRVVFSHHKLAGERNHGRSRETLDMISRAAATQRVCLDCHPYPATSTMLRLDRARLASRTLITWSKGYPEATGRDFSEVMAELGLDDEAAIARLAPAGAIYFLMDQADVNRIFSHPLTTVGSDGLPFDPHPHPRQWGTFTNVLRTMVREQRLLSLETAIHKMTGLAAAQYGLTERGLLRQGYHADLVLFDPANVTDTATFSAPIQVSQGIHAVWVNGRQVWDGERTGAERPGQVLAPGDAIPWSQQSE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. N- acyl-D-amino-acid deacylase family."}
+{"protein": "MLSILLSLLSLSGTHAAPISKDNGTVCYALNSSTTDESIFPLLNGQGPHYDYPQSFGIPVEVPDQCTVEHVQMLARHGERYPTASKGKLMIALWDKLKEFQGQYNGPMEVFNDYEFFVSNTKYFDQLTNSTDVDPSNPYAGAKTAQHLGKYIAYNYGDLFSDSNPVFTSSSGRVHQTAKYVVSSLEEELDIQLDLQIIQENETSGANSLTPADSCMTYNGDLGDEYFENATLPYLTDIKNRWMKKNSNLNLTLEHDDIELLVDWCAFETNVKGSSAVCDLFERNDLVAYSYYANVNNFYRRGAGNPMSNPIGSVLVNASYNLLTQADELDNKVWLSFSHDTDIQQFISALGLIDNGVTEYSLDQVDFQNIQQLSWVTPMGGRIFTEKLKCGNASYVRYIINDVIIPVPGCTSGPGFSCPIEDFDDYITNRLNGIDYVSSCEVQQVSNTTELTFYWDYNEVEYNGPVSNK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the histidine acid phosphatase family."}
+{"protein": "MRFTFTSRCLALFLLLNHPTPILPAFSNQTYPTIEPKPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDDTPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKLKNAYVLYYLAIVGHSLSIFTLVISLGIFVFFRSLGCQRVTLHKNMFLTYILNSMIIIIHLVEVVPNGELVRRDPVSCKILHFFHQYMMACNYFWMLCEGIYLHTLIVVAVFTEKQRLRWYYLLGWGFPLVPTTIHAITRAVYFNDNCWLSVETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRETHEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKMLGKIYDYVMHSLIHFQGFFVATIYCFCNNEVQTTVKRQWAQFKIQWNQRWGRRPSNRSARAAAAAAEAGDIPIYICHQELRNEPANNQGEESAEIIPLNIIEQESSA", "text": "FUNCTION: This is a receptor for calcitonin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The calcitonin receptor is thought to couple to the heterotrimeric guanosine triphosphate-binding protein that is sensitive to cholera toxin. FUNCTION: [Isoform 2]: Receptor for calcitonin but is unable to couple to G proteins and activate adenylyl cyclase (PubMed:7476993). Does not undergo receptor internalization following ligand binding (PubMed:7476993). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family."}
+{"protein": "MKLNKLFDSKTVVFKKSDKYGKSDCCKTKCVEGQIEFGVKIPTDFPAFNRALVTFLKTQKNQLNVDLDSFVELYKAENLCYKTALKVVVASITFCETTPFTMKTEPQKNVEVAVKCDSEHTSLIKEYEVVGNYVNMARQLQDTPSDQLYPEEFVKRFEKAATGLGVKITVLKQADLIKKKMGLLLGVNKGSEREARLLVISYNNNKKSSETLALVGKGITYDSGGMNIKTGDYMRGMKYDMSGAAIVCSTVLALAKNKVKTNVVAVAALTENLPGPHAQRPDDIQTAYNGKTVEIDNTDAEGRLVLADAISYAAKDLKATQIIDVATLTGLMSYILSTTYTGIFSTCDMAWDAFKKAACCAGEPVWRLPMHPDYLKPLESKLADLQNSTSVKGAGSSRAACFLAEFREGVPLIHCDIASTASIQDLGQGVLVRTLYERAAQQAKE", "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: Cytoplasm. SIMILARITY: Belongs to the peptidase M17 family."}
+{"protein": "MSVGIIGAGQLAYALARGFTAAGIVSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRCMTNTPVVVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTLTPSSPGKLLTRSLALGGKKD", "text": "FUNCTION: Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH (By similarity). Involved in cellular response to oxidative stress (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion. SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family."}
+{"protein": "MRLLPRLLLLFLLAFPAAVLLRGGPGGSLALAQDPTEDEEIVEDSIIEDEDDEAEVEEDEPTDLAEDKEEEDVSSEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTVIEREDGLDGETIFMYMFLAGLGLLVVVGLHQLLESRKRKRPIQKVEMGTSSQNDVDMSWIPQETLNQINKASPRRQPRKRAQKRSVGSDE", "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. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the TRAP-alpha family."}
+{"protein": "MDNTSFEKREFISVWVRDPQVHKEDFWHTYISYEICLHTNSMCFRKKTSCVRRRYSEFVWLRHKLQDNALLIELPKLPPWNPFFNLNNEFHITQRMQGLQQFLEAVLQTPLLLSDSRLHLFLQSQLSIAKMDACAQGHTHYTVAQAIQRCGGEARFPVEEQHQEDSKTCCDSDCDSTTSSGLGCSIEPATLVEQDLSHNERFAHEFQATNPEAELCSSLSSSPHGHSVI", "text": "FUNCTION: Probable phosphoinositide-binding protein involved in protein sorting and membrane trafficking in endosomes. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. SUBCELLULAR LOCATION: Cytoplasm Endosome membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "MLPVPLIQLQCGVNSYEWGKKGNSSRAAQFAAASLDDNEFKIDEEKPYAELWMGTHPSNPSKDKHTGRTLLELIQDNQALLSPAIAERYQNKLPFLFKVLSIQKALSIQAHPNKKLAEKLHARDPKNYPDDNHKPEMAIAISDFEGLCGFRPLKEIAHFLDNVPALRQLVGEDKAKAFVETVKRNDGNESDEATAENKKVLQSAFGALMASSEADMTAAADKLVQSAKSAGADFTGTAVPSPGGAKLSELVGRLHGQFGADYGLFVLFFLNFVEMKAGEAIYLRADDIHAYISGDIIECMASSDNVVRAGFTPKFKDVDNLVNMLTYDFAPIEQQKMEPTDYTQDVKNKREAGATLNQTAIDSQSEIVEYNPPIEEFSVVRSLLKSQGSKVTFKPIDGPSIIICTQGQGKISVGPKVQEIKKGHVFFVGATAECVLESEDDKFETFKAFCVLDEQSNGN", "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": "MAGGYGVMGDDGSIDYTVHEAWNEATNVYLIVILVSFGLFMYAKRNKRRIMRIFSVPPTEETLSEPNFYDTISKIRLRQQLEMYSISRKYDYQQPQNQADSVQLSLE", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMIM19 family."}
+{"protein": "NLYQFKNMVQCVGTQLCVAYVKYGCYCGPG", "text": "FUNCTION: Relatively highly potent phospholipase A2 that displays potent antimicrobial and hemolytic activities. It does not show cytotoxic effects on the three human cell lines tested. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn- phosphoglycerides. It shows similar potencies on both Gram-negative and Gram-positive bacteria: B.cereus (MIC>9 ug/ml), B.subtilis (MIC>12 ug/ml), E.faecalis (MIC>7 ug/ml), S.epidermidis (MIC>12 ug/ml), S.aureux (MIC>5 ug/ml), E.coli (MIC>7 ug/ml), K.pneumonia (MIC>8 ug/ml), P.aeruginosa (MIC>10 ug/ml), and S.enteric (MIC>9 ug/ml). It also shows antifungal activities: A.niger (MIC>15 ug/ml), B.cinerea (MIC>12 ug/ml), F.solani (MIC>15 ug/ml), and P.digitatum (MIC>10 ug/ml). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily."}
+{"protein": "MKWVTFISLLFLFSSAYSRGVFRREAHKSEIAHRFNDVGEEHFIGLVLITFSQYLQKCPYEEHAKLVKEVTDLAKACVADESAANCDKSLHDIFGDKICALPSLRDTYGDVADCCEKKEPERNECFLHHKDDKPDLPPFARPEADVLCKAFHDDEKAFFGHYLYEVARRHPYFYAPELLYYAQKYKAILTECCEAADKGACLTPKLDALEGKSLISAAQERLRCASIQKFGDRAYKAWALVRLSQRFPKADFTDISKIVTDLTKVHKECCHGDLLECADDRADLAKYMCEHQETISSHLKECCDKPILEKAHCIYGLHNDETPAGLPAVAEEFVEDKDVCKNYEEAKDLFLGKFLYEYSRRHPDYSVVLLLRLGKAYEATLKKCCATDDPHACYAKVLDEFQPLVDEPKNLVKQNCELYEQLGDYNFQNALLVRYTKKVPQVSTPTLVEISRSLGKVGSKCCKHPEAERLPCVEDYLSVVLNRLCVLHEKTPVSEKVTKCCSESLVDRRPCFSALGPDETYVPKEFNAETFTFHADICTLPETERKIKKQTALVELVKHKPHATNDQLKTVVGEFTALLDKCCSAEDKEACFAVEGPKLVESSKATLG", "text": "FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ALB/AFP/VDB family."}
+{"protein": "MEPQDRTKRPQEEDNGVPIDGHNGSNSEPAAKKIKLDSPSSADSRAKGVAPIKAEYLLFPPGQKAKPTQSEAEADDNDDDAAEGRTAPTPQETQQAPQKDGKRKSQRGQNKEREFGTFSDAQRLCNTIAWTPEFSPRPCKHGDRCNALHDLRKYLKEGRRPDITTFGGKCPVWEKYGKCPSGWRCLFVHSHMDEIKHEDGRSELVLVGDASKAPEGGEEAAGEIKPGVVNMVPVGIKYDLSKKRIPLEKSEQYLAWLAKDTKHLAKHYQKHKDDETNPNDYRAQYVEPPFKPSEKRRLYFGRETPVLAPLTTQGNLPFRRLCVELGAQVTYSEMALGLPLLQGLKADWTLMRAHESEIVPPRFNPGGPIVQGYDNSKDVKFGAQIAANAPWVAVKATEALSQLLPHLRLVDLNCGCPVDAVFKSGSGSALLDSHSKLERMIRGMNAVSGEVPITAKIRMGSRDGKLTAQKLVERLALGSEDLRDMIGAPGCAAVTLHGRTRLQRYTKAADWGYIAECAALIKQFNEKSNDLADTIREADENTLPNGGKMYFLGNGDCYSHVEYFDHVDNAKVDSVMIGRGALVKPWVFEEIEKGQYLDKSSSERLTYIEKFVRYGMEAWGSDELGLNYTRRFLLEFLSFFCRYVPIGLLERLPPNLNERPPAYRGRDDLETLFASKNYKDWIKISEMFLGPAPPGFKFQPKHKSNSYEIEAEG", "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": "MSFVPSKVFFTKGVGRHKEYLSSFELALRDAKIEKCNLVTVSSIFPPKCERVSVEEGVKMLTPGQITFAVMARNSTNEYNRLIAASIGVAIPADDTQYGYLSEHHPFGEDAEQSGEYAEDLAATMLATTLGIEFDPNKDWDEREGIYKMSGKIINSYNITQSAEGENGMWTTVISCAVLLP", "text": "SIMILARITY: Belongs to the PdaD family."}
+{"protein": "MVSMTFKRSRSDRFYSTRCCGCCHVRTGTIILGTWYMVVNLLMAILLTVEVTHPNSMPAVNIQYEVIGNYYSSERMADNACVLFAVSVLMFIISSMLVYGAISYQVGWLIPFFCYRLFDFVLSCLVAISSLTYLPRIKEYLDQLPDFPYKDDLLALDSSCLLFIVLVFFALFIIFKAYLINCVWNCYKYINNRNVPEIAVYPAFEAPPQYVLPTYEMAVKMPEKEPPPPYLPA", "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. SIMILARITY: Belongs to the LAPTM4/LAPTM5 transporter family."}
+{"protein": "MDTMRQRILVVDDDASLAEMLTIVLRGEGFDTAVIGDGTQALTAVRELRPDLVLLDLMLPGMNGIDVCRVLRADSGVPIVMLTAKTDTVDVVLGLESGADDYIMKPFKPKELVARVRARLRRNDDEPAEMLSIADVEIDVPAHKVTRNGEQISLTPLEFDLLVALARKPRQVFTRDVLLEQVWGYRHPADTRLVNVHVQRLRAKVEKDPENPTVVLTVRGVGYKAGPP", "text": "FUNCTION: Member of the two-component regulatory system MtrA/MtrB. FUNCTION: Member of the two-component regulatory system MtrA/MtrB. Binds direct repeat motifs of sequence 5'-GTCACAGCG-3', phosphorylation confers higher affinity. Overexpression decreases bacteria viability upon infection of human THP-1 macrophage cell line, due at least in part to impaired blockage of phagosome-lysosome fusion (upon infection bacteria usually remain in phagosomes). Infecting C57BL/6 mice with an overexpressing strain leads to an attentuated infection in both spleen and lungs. The level of dnaA mRNA increases dramatically. Binds the promoter of dnaA, fbpD, ripA and itself, as well as oriC, which it may regulate. Upon co-overexpression of MrtA and MtrB growth in macrophages is partially restored, dnaA expression is not induced, although mouse infections are still attenuated, suggesting that bacterial growth in macrophages requires an optimal ratio of MtrB to MtrA. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MSAPVPQLVNISHALQASTIQQIRLDMVDFNKDCKLSSIQLARIDKYIDSLQAALNQFTKDNLHIERKEKNVTEADIQLYSGLKSMYLDYLNQLIKLKHEKQHHSTPPIANDVSLDFFVNQLPKFSPEERKNYIDNLILNKNSHNRLSKMDGLVDAVINLCVLDTSVAENVRSYMKLLDTLGFQKGSNSTGTKANLKKKLASSKAKIKDSEKEKEKEKDKSKVKMKTKLKPSPLLNNDDKNSSPSPTASTSSMKKLKSGLFNKNEAKSTESLPTSSKKKLSFSKYLNKDDADMTKLGTKRSIDVDFKVNPEASTVASNIISSSTSGSSTTTVATPASSEEPLKKKTKISVQDSNVQSILRNGKPKKARISSIKFLDDSQLIKVYGDDLPNQGLQVSPTQLKKILKPFKEGEPKEIILFEDMSIKLKPLDLMFLKNTNSDDYMDISETKGGPIHCETRTPLIYRKNFNHFNPDLNKRPPREPIEFDLNGNTNSTPTIAKAFGKNSLLLRKDRGGLPYKHVPIVKRNKYPPRPVH", "text": "FUNCTION: RNA-binding 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. Negative regulator of poly(A) synthesis. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. REF2 is required for 3'-end formation of snoRNAs. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MTLHSNSTTSPLFPNISSSWIHSPSDAGLPRGTVTHFGSYNVSRAAGNFSSPNGPTDDPLGGHTVWQVVFIAFLTGILALVTIIGNILVIVSFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLAIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFVLWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAETENFVHPTGSSRSCSSYELQQQSMKRANRRKYGRCHFWFTTKSWKPSSEQMDQDHSSSDSWNNNDAAASLENSASSDEEDIGSETRAIYSIVLKLPGHSTILNSTKLPSSDNLQVPEEELGMVDLERKANKLQAQKSVDDGGSFPKSFSKLPIQLESAVDTAKTADVNSSVGKTTATLPLSFKEATLAKRFALKTRSQITKRKRMSLVKEKKAAQTLSAILLAFIITWTPYNIMVLVNTFCDSCIPKTFWNLGYWLCYINSTVNPVCYALCNKTFRTTFKMLLLCQCDKKKRRKQQYQQRQSVIFHKRAPEQAL", "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 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Colocalizes with TMEM147 in the endoplasmic reticulum (ER) membrane. TMEM147 impairs its trafficking to the cell membrane leading to its retention in the ER membrane. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM3 sub-subfamily."}
+{"protein": "MAAAVHGALKAVGEDFYRDAIEHCRSYNARLSAERSTRLPFLDAQTGVAQSDCYIWMERSHRGPGLSPGQIYSYPARCWRKKRRLNILEDPRLRPLCDAPQKKELGSAVAEGAVLEALLCAEPPKEPKEEEALLDCQKPPPGDFAHDAEGDEMEDDAPRRKNKAKGKTYGLGAVRKRQDAAALEDRDKPYVCDICGKRYKNRPGLSYHYTHTHLAEEEGEESAERHPLPFQRRNHHKQFYKELNWVPESQRRHAAAAGRRSEGPCDFCVGGAVRRAALGHEEMIACADCGRAGHPSCLQFTLAMAAAARSYRWQCIECKNCSLCGSAENDEQLLFCDDCDRGYHMYCISPPVAEPPEGTWSCHLCLRQLKDKAAAFITLT", "text": "FUNCTION: May have an important role in developing neurons by participating in regulation of cell survival, possibly as a neurospecific transcription factor. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex) and plays a role in neural development. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the requiem/DPF family."}
+{"protein": "MSDDSSSPLTTLKILIIGESGVGKSSLMLRFVDDVFDPEQAATIGVDFRVTSMTIDGNRVKLAIWDTAGQERFRTLTPSYYRGAQGVICVYDVTSRSSFEKLKHWMTEVDTYCTNDNVIKMMVANKIDMPNRTVTREEGLKFAKRHRTLFIEASAKTKEGVQCTFEELIEKIIQTPDLWDNDRPTFRLGQPTDTSSGNLCGC", "text": "FUNCTION: Plays a role in apical endocytosis/recycling. May be implicated in transport between the plasma membrane and early endosomes (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MAIQTTTGLAARLVAKRATFPASRRNFSASRSALKEIQEAYILSGARTPTAKFNGSFVSVSAPELGAVAIKSAVSKSGVPVEKITDVYMGNVLQGAVGQAPARQASMFAGLSPTVESMTVNKVCASGLKAVALAAQNIQLGLAEAQVAGGMENMSRVPYYLPRSTQLPPFGEIKLQDGLIQDGLWDVYNQFHMGICAEKTAKKYEISREEQDQYAIQSYQRAQAAWKENKFAEEIAPVTVKGKKGETVVERDEGYENLRIDKMATLKPAFLRDGTGTVTAGNASTMNDGASALVLGSKAIAREFAQGNRALARIVSTADAAIDPVDFPVAPAKAVPIALERAGITKDQVAVWEFNEAFAAVIKANEKILGLQNARVNPLGGAISLGHALGSSGSRILVTLLHQLQPGEYGVAAICNGGGAATAMVVQKLDRVD", "text": "FUNCTION: Mitochondrial acetyl-CoA acetyltransferase that catalyzes both the formation and degradation of acetoacetyl-CoA (PubMed:32005728). Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis (PubMed:32005728). Plays an important role in growth, morphogenesis and maintaining mitochondrial function including the response to oxidative stresses (PubMed:32005728). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
+{"protein": "MVLSLLSVMLLSGYKFLSKKEELVTILPLPQVENKFKPQKIWSYYIGSNNGGGDFYSNLQPTVQNTRVFVANRYGLVKALDADSGKELWAKDLSIYTGCFSRNRPAQLSGGVTAVGNRIYVASELAKVYAMEAKCGSLAWEVLVAGETLSPPVVSDGVILIHTSNGMLQALNEADGALKWTVNLEAKMLNIRGGSTPTTACGTAIVGSDNGLVSAVMLNIGQIIWQQRISQTGGVTEIARINDVQATPVVVNGYVYALAYNGNLAALDLFSGKLMWSREIGSFTNMLVENGIIYLVDQNDRVIAVDAKNGITSWYQSALLHRNLTSPVLNKDSIVIGDSGGYLHWINIDDGRLVAQKKIASALLVTPLFDGDKIIVQATNGEVHAIIR", "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 BamB family."}
+{"protein": "MEPNTPAIDPKKERLARWKQKKQQQDMLRQKSGASSKSSHDQAEDGDAARSTQPFEGLDKMAERRKRLELWKKKKKEQDEQKWKGDDAGQESATDIPVKGKAAPAEDAKAVPRGRKSRKGADPEKRQIWDDSDDELEAPKLKLFKPGSTIQTETPPDEDPEDTLDTYMNTIQEKNEVQLLAPREVFDQEDDETTAFDYNRTDNGTGSEFMRLAKLKAKKQLKPVIYSADELKPFIKNFYQEPEEISKLSEEEVADLRLSLDNVQVRGRDCPRPILKWSQLGLNSGIMNLLTRELEFTVPTPIQAQAIPAIMSGRDVIGISKTGSGKTVSFILPLLRQIKAQRPLGGDETGPLGLILSPTRELALQIHEEVTKFTSGDPSIRSLCCTGGSELKRQINDIKRGVEIVIATPGRFIDLLSLNSGNLINPKRIVFVVMDEADRLFDLGFEPQVNQIMKCIRPDKQCVLFSATFPNKLKSFASKILHDPVYITVNSKSLINENIEQKVEIFSNEEDKFKSLIHWLALTQQNLNDEKTIVFVSSQQICDILYNRLEANGFTTFAIHAGKIYTERAWNLKCFKETANGILICTEVLSRGLNVPEVSLVIIYNAAKTFAQYVHTTGRTARGSNKGTALTLLMNTELAASYILMKSMRDEELNKHHDATVSTLKQMSEKFNKGLKTGEYRLVKGFGGKGLDHLGKVYEEKHTEERNQLALEAGLAATEVSVSAPDGGLGDESTSVSIPKLDYTVKKRSNPDGTSTYFAHVQVNDLPQIVRWEATKYTTLSSIKHETGCSITNKGRYYPSGQGPQGPSDEPRLYLLVESATDQDISLAIDLLESKVRDGVRKSNMQEIRSNKYTI", "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": "MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTEKLKTLFLAVRVENEEGKCEVTEVNKLDGEASINNRKGKLIFFYEWTIKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEDGVKLLREAVGIYISTLKTEFTQGMILPTVNGESVDPVGQPALKTETCKAKSAPSKSQAKPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF", "text": "FUNCTION: Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co- chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). SUBCELLULAR LOCATION: Cytoplasm, cytosol Endoplasmic reticulum Note=May transiently interact with the endoplasmic reticulum. SIMILARITY: Belongs to the AHA1 family."}
+{"protein": "MSPAPRPSRSLLLPLLTLGTALASLGWAQGSNFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADLATMMAMRRPRCGVPDKFGTEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMILFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGSKSGSPTKMPPQPRTTSRPSVPDKPKNPAYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV", "text": "FUNCTION: Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (PubMed:10520996). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (By similarity). Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues (By similarity). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein; Extracellular side Melanosome Cytoplasm Note=Forms a complex with BST2 and localizes to the cytoplasm. SIMILARITY: Belongs to the peptidase M10A family."}
+{"protein": "MKSISTLGICLRASQDLAKTRPISLLSTRSFANLTQGTSTYHSLSIRSIRHNRLEARYTNILNRNILPYKNYSTGTAPPPPPPPPPPHDKNAKGKFLFNRIGRAFTFSLSSVIVLGATCISVLVVYLILSELFLPSGDTRTFNKAVRMLESNELAHEALGFKKGQRVKAHGEQHADKWARNRPAQSVRTRGADGKDYLFMKFQVESPSGKYGTVTLEQVDRTFWSSEFLYIALDMPGNKRIYIKEPKFQSKKYVPKVGSLASNDGFLGLKWGPKKDD", "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 keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM21 family."}
+{"protein": "MPQEQYSHHRSTMPSSEGPHIYKVGIYGWRKRCLYFFVLLLMILILVNLAMTIWILKVMNFTIDGMGNLRITEKGLKLEGDSEFLQPLYAKEIQSRPGNALYFKSARNVTVNILNDQTKVLTRLVTGPKAVEAYGKKFEVKTVSGKLLFSADDNEVVVGAERLRVLGAEGTVFPKSIETPNVRADPFKELRLESPTRSLVMEAPKGVEINAEAGNMEATCRSELRLESKDGEIKLDAAKIKLPRLPRGSYTPTGTRQKVFEVCICANGRLFLSQAGTGSTCQINTSVCL", "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. SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single- pass type II membrane protein Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family."}
+{"protein": "MRNKAHNFPNQNNNKLEGEPRAKAEYASKRADGTTNTHPQERMRASGERSDFF", "text": "SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspK family."}
+{"protein": "MESYDKVGSNKVPCLLILTCIIMSSFVNNNIVQAKVSWSLKAAEEAEAVANINCSGHGRAFLDGILSDGSPKCECNTCYTGADCSEKITGCSADVASGDGLFLEEYWQQHKENSAVLVSGWHRMSYFFNPVSNFISFELEKTIKELHEIVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTATPCAPQSKVVAHAPYYPVFREQTKYFDKKGYEWKGNAADYVNTSTPEQFIEMVTSPNNPEGLLRHEVIKGCKSIYYMVYYWPHYTPIKYKADEDIMLFTMSKYTGHSGSRFGWALIKDETVYNKLLNYMTKNTEGTSRETQLRSLKILKEVIAMVKTQNGTMRDLNTFGFQKLRERWVNITALLDKSDRFSYQKLPQSEYCNYFRRMRPPSPSYAWVKCEWEEDKDCYQTFQNGRINTQSGEGFEAGSRYVRLSLIKTKDDFDQLMYYLKIMVEAKRKTPLIKQLSNDQISRRPFI", "text": "SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the alliinase family."}
+{"protein": "MNNVISFIGNSSNKYFQINQLHFIRIINKNIHSKNNLINSNSSYNVFYNKYFIKNTFQNKNKLSSIYSKLNFSIKNMCKDKNEKKNYEHVNANEKNGYLASEKNELTKNKVEEHTYDYDYVVIGGGPGGMASAKEAAAHGARVLLFDYVKPSSQGTKWGIGGTCVNVGCVPKKLMHYAGHMGSIFKLDSKAYGWKFDNLKHDWKKLVTTVQSHIRSLNFSYMTGLRSSKVKYINGLAKLKDKNTVSYYLKGDLSKEETVTGKYILIATGCRPHIPDDVEGAKELSITSDDIFSLKKDPGKTLVVGASYVALECSGFLNSLGYDVTVAVRSIVLRGFDQQCAVKVKLYMEEQGVMFKNGILPKKLTKMDDKILVEFSDKTSELYDTVLYAIGRKGDIDGLNLESLNMNVNKSNNKIIADHLSCTNIPSIFAVGDVAENVPELAPVAIKAGEILARRLFKDSDEIMDYSYIPTSIYTPIEYGACGYSEEKAYELYGKSNVEVFLQEFNNLEISAVHRQKHIRAQKDEYDLDVSSTCLAKLVCLKNEDNRVIGFHYVGPNAGEVTQGMALALRLKVKKKDFDNCIGIHPTDAESFMNLFVTISSGLSYAAKGGCGGGKCG", "text": "FUNCTION: Catalyzes the transfer of electrons from NADPH to thioredoxins TRX1, TRX2 and TRX3, which in turn act as reductants of disulfide containing proteins (PubMed:9368022, PubMed:11013257, PubMed:16910770, PubMed:23845423). Able to reduce nitroglutathione (GSNO), a compound involved in the transport of nitric oxide (NO); however, TRX1 is more efficient in reducing GSNO (PubMed:11013257). Has no catalytic activity towards oxidized glutathione (GSSG) (PubMed:11013257). SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MAASTAAQVQLSEEALGLARIFENPKGSLEAASKLLQKNHDEFHVFWRDVGGHNHIPHSVLSILALGGGPAELQRAWDDGVAIQRPTPPLDEDVVKKLENPAEFRARIGSIPNYTNFLHFFRNQMDKKGWQAVVSEYAFSRTPLAETIFAQLFEGAYHPFIHIGFGIEFNLPSIIAEGLAQAATHDSAGIEGFFLEAERQAAQSKGPGKSLVQLLDEVRTTEKIKTAARLPDGPVRVRDGVIGRAGAEIAALASQFRVPADQLSRGAAESINISAYTAGAAQRAGKARKIDFFHMHNTTSSLFLTVFLNQPWISTEDKVRIVEWKGRLDLVWYAACSAPDLNVDHVIGYKPAQSAGWGWKELYEAINVAHDDGHLAKIVRALKNGEEVSRPFESGEGAEAFPIKGDSWLKLAQMSYDTTLDLPDDDKWIWGAGFLPLWNKVPSL", "text": "FUNCTION: Baeyer-Villiger oxidase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702). The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA (PubMed:24302702). As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain (PubMed:24302702). The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702). Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC (PubMed:24302702). Spontaneous decarboxylation of endocrocin occurs to generate emodin (PubMed:24302702). An O- methyltransferase (ptaH or ptaI) could methylate emodin to form physcion (PubMed:24302702). PtaJ could then catalyze the oxidative cleavage of physcion, and rotation of the intermediate could then afford desmethylisosulochrin (PubMed:24302702). PtaF, a putative NADH- dependent oxidoreductase, might also participate in the oxidative cleavage step (PubMed:24302702). Desmethylisosulochrin is then transformed by another O-methyltransferase (ptaH or ptaI) to form isosulochrin (PubMed:24302702). Chlorination of isosulochrin by ptaM in the cyclohexadienone B ring then produces chloroisosulochrin (PubMed:24302702). PtaE is responsible for the oxidative coupling reactions of both benzophenones isosulouchrin and chloroisosulouchrin to RES-1214-1 and pestheic acid respectively, regardless of chlorination. SIMILARITY: Belongs to the questin oxidase family."}
+{"protein": "MADVSVDQSKLPGVKEVCRDFAVLEDHTLAHSLQEQEIEHHLASNIQRNRLVQHDLQVAKQLQEEDLKAQAQLQKRYKALEQHDCEIAQEIQEKLTIEAERRRIQEKKDEDIARLLQEKELQEEKKRKKHTPEFSGGSASGDNYYYEDGGMKSRGINEAVSAPARVSHRDQEWYDAEIARKLQEEELLATHMDIRAAQVAQDEEIARLLMAEEKKAYKKAKDREKSSLDKRKHDYDCKSKAKSAHSKSKEGDETQRAKIDRPSRPPPPAAMAPEDVDPTHFTNQHSNTRHFSKSESSHKGFHNKQ", "text": "FUNCTION: Involved in EGFR signaling."}
+{"protein": "MTTVSYVTILLTVLVQVLTSDAKATNNKRELSSGLKERSLSDDAPQFWKGRFSRSEEDPQFWKGRFSDPQFWKGRFSDPQFWKGRFSDPQFWKGRFSDPQFWKGRFSDPQFWKGRFSDPQFWKGRFSDGTKRENDPQYWKGRFSRSFEDQPDSEAQFWKGRFARTSSGEKREPQYWKGRFSRDSVPGRYGRELQGRFGRELQGRFGREAQGRFGRELQGRFGREFQGRFGREDQGRFGREDQGRFGREDQGRFGREDQGRFGREDQGRFGREDQGRFGRELQGRFGREFQGRFGREDQGRFGREDQGRFGRELQGRFGREDQGRFGREDQGRFGREDLAKEDQGRFGREDLAKEDQGRFGREDIAEADQGRFGRNAAAAAAAAAAAKKRTIDVIDIESDPKPQTRFRDGKDMQEKRKVEKKDKIEKSDDALAKTS", "text": "FUNCTION: Not known but it could act as a transmitter at neuromuscular synapses. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
+{"protein": "MHAKVGDYLVVKGTTTERHDQHAEIIEVRSADGSPPYVVRWLVNGHETTVYPGSDAVVVTATEHAEAEKRAAARAGHAAT", "text": "SIMILARITY: To M.leprae U650M."}
+{"protein": "MNMKKFVKKPLAIAVLMLASGGMVNMVHAEPTVINSKDISATKTVKEGGSFSVEFKATENEIVSGKLDADTPAFHLVMSDSGEHKGWNVRPTGASEGGQMVSADGTRVDLHTNELSWDNDHWWIDDGSERVEATFFLAAGDEVKAGEYQFTGRVEEYVE", "text": "FUNCTION: Major pilus subunit. Expressed only in pathogenic serotypes, it is part of myf, a probable virulence factor. SUBCELLULAR LOCATION: Fimbrium."}
+{"protein": "MLLDENPGTLIHHTIGNFNIQPDKQAVTRINDSLSTLQQSRELRMREAESSLRKLSRHLHSLNAQHEEAVAAHDSSKHAADMVELDTKKFRIAKAATELEIESERLESELEMLKERLADLEAQGLEGDEATRRERELDDATILRLKIYRSLGVDIEADDAGNFNKAVIRNSRKGDVHVVNIDPKFSRFFYSNYFWSTMQG", "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 Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body Note=Associated with kinetochores. SIMILARITY: Belongs to the SPC24 family."}
+{"protein": "MITLKEALKYSKEELENLKKELNEKAKKEKKLGAYIEQFLDKDLSVSGEGVPVAIKDNISVKGWELTSASKILQGYIAPYDASAIVNLKANGFSPFGRCNMDEFAMGSSTASSCYGKTLNPLNFERVPGGSSGGSAAAVAGGLALASLGSDTGGSVRQPAAFCGCVGFKPSYGRVSRYGLASYSSSLDQIGVLTQNVEDAAILYDAIAGYDKMDSTSANIEFIKTVPNLNANKKLKIAVIENYVNDADSEVKNALLKTIDMLKANGHEIVYKNLLDSKFDIAAYYIIATAEASANLSRYDGVRYGKRSENIQNLKEMYVNTRSEGFGEEVKRRILLGTFVLSSGYYDAYYIKAQKARAFIKAKYEEILQDCDLIFMPVTPTTAFKFDTQKSPMQTYLEDVYTISVNLAGLGGISVPVAKDKEGLNISAQLICKAYDEQTLLDGALSLEQMIKN", "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). 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) (By similarity). SIMILARITY: Belongs to the amidase family. GatA subfamily. SIMILARITY: Belongs to the amidase family. GatA subfamily."}
+{"protein": "MKKTLLAIILGGMAFATTNASANTGTINFNGKITSATCTIDPEVNGNRTSTIDLGQAAISGHGTVVDFKLKPAPGSNDCLAKTNARIDWSGSMNSLGFNNTASGNTAAKGYHMTLRATNVGNGSGGANINTSFTTAEYTHTSAIQSFNYSAQLKKDDRAPSNGGYKAGVFTTSASFLVTYM", "text": "FUNCTION: FanC is the main component of the K99 fimbriae. 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. SIMILARITY: Belongs to the fimbrial protein family."}
+{"protein": "LWKT", "text": "FUNCTION: Specific inhibitor of store-operated non-voltage-gated calcium channels. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MARGLKKHLKRLNAPKHWMLDKLGGAFAPKPSSGPHKSRECLPLVLIIRNRLKYALTYREVISILMQRHIQVDGKVRTDKTYPAGFMDVVSIPKTNENFRLLYDTKGRFRLHSIKDEEAKFKLCKVRSIQFGQKGIPYLNTYDGRTIRYPDPLIKPNDTIKLDLEENKIVEFIKFDVGNVVMVTGGRNRGRVGVIKNREKHKGSFETIHIQDSTGHEFATRLGNVYTIGKGTKPWVSLPKGKGIKLTIIEEARKRLASQQAA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family."}
+{"protein": "MSKVSKRISEVRNKIENKPYKAIEALNLLKDTATAKFVESAEAHIALKLDTKYADQQLRTTLVLPKGTGKKIRIAVIAEGEKATEAINAGADLAGSTDLVQDIMKGMLDFDRLIATPDMMPLIAKLGKVLGPRGLMPSPKSGTVTSDVKSAIEEFKKGKLEYRADKSGIVHISFGKTNFSVNDLLLNLEAVQESIDKNRPAGVKGKYWKSFYICSTMGPSIQLDISEFRDKNFQ", "text": "FUNCTION: Binds directly to 23S rRNA. Might be involved in E site tRNA release (Potential). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL1 family."}
+{"protein": "MSESLQSVLIIGGSGFLGLHLIEQFYRHCPNVAITVFDVRPLPEKLSKYFTFDPSKIQFFKGDLTSDKDVSDAINQSKCDVIVHSASPMHGLPQEIYEKVNVQGTKNLLSVAQKLHVKALVYTSSAGVIFNGQDVINADETWPYPEVHMDGYNETKAAAEEAVMKANDNDQLRTVCLRPAGIFGPGDRQLVPGLRASAKLGQSKYQLGDNNNLFDWTYVGNVADAHVLAAQKILDKSTRDDISGQTFFITNDSPTYFWTLARTVWKNDGYIDKYYIKLPYPVALTLGYISEFVAKNILKKEPGITPFRVKVVCAIRYHNIAKAKKLLGYKPEVDLETGINYTLDWMNEDL", "text": "FUNCTION: Sterol-4-alpha-carboxylate 3-dehydrogenase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:12702354). ERG26 is a catalytic component of the C-4 demethylation complex that catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group (PubMed:12702354). 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; Peripheral membrane protein. SIMILARITY: Belongs to the 3-beta-HSD family."}
+{"protein": "MSKHHDAGTAFIQTQQLHAAMADTFLEHMCRLDIDSEPTIARNTGIICTIGPASRSVDKLKEMIKSGMNVARLNFSHGTHEYHEGTIKNVREATESFASDPITYRPVAIALDTKGPEIRTGLIKGSGTAEVELKKGAALKVTLDNAFMENCDENVLWVDYKNLIKVIDVGSKIYVDDGLISLLVKEKGKDFVMTEVENGGMLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQNVDMVFASFIRKAADVHAVRKVLGEKGKHIKIISKIENHEGVRRFDEIMEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPIICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHAIAREAEAAMFHRQQFEEILRHSVHHREPADAMAAGAVEASFKCLAAALIVMTESGRSAHLVSRYRPRAPIIAVTRNDQTARQAHLYRGVFPVLCKQPAHDAWAEDVDLRVNLGMNVGKARGFFKTGDLVIVLTGWRPGSGYTNTMRVVPVP", "text": "FUNCTION: Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. SIMILARITY: Belongs to the pyruvate kinase family."}
+{"protein": "QEAPKAFNQCQACHKVEAGEDGVGPSLFGLFGHKLGQAPGFKYSEAHLKFAQQTVDEPFLTKYLADPKASLPGNKMVFAGLKNPDDVKAVLAYLKTIK", "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": "MAAAIMAAEQEAAKGGGGRNRGGVQRVEGKLRASVEKGDYYEAHQMYRTLFFRYMSQGKHAEARELMYSGALLFFSHNQQNSAADLSMLVLESLEKSDAKVAEDLLENLAKLFSLMDPNSPERVAFVSRALKWSSGGSGKLGHPKLHQLLAITLWKEQNYSESRYHFLHSTDGEGCANMLVEYSSSRGYRSEVDMFVAQAVLQFLCLKNKTSASVVFTTYTQKHPSIEKGPPFVQPLLNFIWFLLLAVDGGKLTVFTVLCEQYQPSLKRDPMYNEYLDRIGQLFFGVPPKQTSSYGGLLGNLLNSLMGTGEDDDTEEGQEDSSPIELD", "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. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated and sorted to the proteasome. 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": "MDIKEHAEEVWFIVMLVLVLIFFSWNVYYLSTGKSFSLDYGLPTYSGLPEQAQKAVQYFDSHPPSPGQYSEVINGMLVVNLTATQYKWTPDLIVVNKSEPVVLIINSPQVDTGFYLRTPDGVINLNNVAGITSYAYFVINQPGNYTWRDAEYAGYNSSYMTGTVEVVG", "text": "FUNCTION: Subunit 2 transfers the electrons from caldariella quinol to the bimetallic center of the catalytic subunit 1 that is formed by heme A3 and Cu(B). FUNCTION: The terminal 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. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
+{"protein": "MTAREHSPRHGARARAMQRASTIDVTADMVGLSLAGNIQDPDEPILEFSLACSELHTPSLDRKPNSFVAVSVTTPPQAFWTKHAQTEIIEGTNNPIFLSSIAFFQDSLINQMTQIKLSVYDVKDRSQGTMYLLGSGTFVVKDLLQDRHHRLHLTLRSAESDRVGNITVIGWQMEEKSDQQPPVTRSLDTVNGRMVLPVDESLTEALGIRSKYASLRKDSLLKAVFGGAICRMYRFPTTDGNHLRILEQMAESVLSLHVPRQFVKLLLEEDAARVCELEELGELSPCWESLRRQIVTQYQTIILTYQENLTDLHQYKGPSFKASSLKADKKLEFVPTNLHIQRMRVQDDGGSDQNYDVVTIGAPAAHCQGFKSGGLRKKLHKFEEAKKHSFEECCTSSTCQSIIYIPQDVVRAKEIIAQINTLKTQVSYYAERLSRAAKDRSATGLERTLAILADKTRQLVTVCDCKLLANSIHGLNAARPDYIASKASPTSTEEEQVMLRNDQDTLMARWAGRSSRSSLQVDWHEEEWEKVWLNVDKSLECIIQRVDKLLQKERLHGEGGEDVFPCSSTCSSKKDCSPPPEESCPGEWSEALYPLLTTLTDCVAMMSDKAKAAMVFLLMQTAAPTIASYLSLQYRRDVVFCQTLTALICGFIIKLRNCLHDGGFLRQLYTIGLLAQFESLLSTYGEELAMLEDMSLGIMDLRNVTFKVTQATSNASSDMLPVITGNRDGFNVRIPLPGPLFDSLPREIQSGMLLRVQPVLFNVGINEQQTLAERFGDTSLQEVINVESLVRLNSYFEQFKEVLPEDCLPRSRSQTCLPELLRFLGQNVHARKNKNVDILWQAAEVCRRLNGVRFTSCKSAKDRTAMSVTLEQCLILQHEHGMAPQVFTQALECMRSEGCRRENTMKNVGSRKYAFNSLQLKAFPKHYRPPEGTYGKVET", "text": "FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate (PubMed:7608176). Catalyzes also inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate (PubMed:7608176). Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival (By similarity). May protect neurons from excitotoxic cell death by regulating the synaptic localization of cell surface N-methyl-D-aspartate-type glutamate receptors (NMDARs) and NMDAR-mediated excitatory postsynaptic current (By similarity). SUBCELLULAR LOCATION: Early endosome membrane Recycling endosome membrane Cell membrane Nucleus Cytoplasm Postsynaptic density Note=Translocates to the plasma membrane upon EGF stimulation (By similarity). Shuttles between the cytoplasm and the nucleus, depending on the cell cycle stage, with highest amounts detected in the nucleus during the G0/G1phase (By similarity). SIMILARITY: Belongs to the inositol 3,4-bisphosphate 4-phosphatase family."}
+{"protein": "MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEKMSKDGKKKKKKTKTKCIIM", "text": "FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation. May play a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MPRKGPAPK", "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": "MDYSHQTSLVPCGQDKYISKNELLLHLKTYNLYYEGQNLQLRHREEEDEFIVEGLLNISWGLRRPIRLQMQDDNERIRPPPSSSSWHSGCNLGAQGTTLKPLTVPKVQISEVDAPPEGDQMPSSTDSRGLKPLQEDTPQLMRTRSDVGVRRRGNVRTPSDQRRIRRHRFSINGHFYNHKTSVFTPAYGSVTNVRINSTMTTPQVLKLLLNKFKIENSAEEFALYVVHTSGEKQKLKATDYPLIARILQGPCEQISKVFLMEKDQVEEVTYDVAQYIKFEMPVLKSFIQKLQEEEDREVKKLMRKYTVLRLMIRQRLEEIAETPATI", "text": "FUNCTION: Potential tumor suppressor. Acts as a KRAS-specific effector protein. May promote apoptosis and cell cycle arrest. Stabilizes STK3/MST2 by protecting it from proteasomal degradation. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome, centromere, kinetochore Note=Translocates to the cytoplasm in the presence of STK3/MST2 and STK4/MST1."}
+{"protein": "MKIVAFTLVAFVALAGASCPYAAPAAAPAPAAPSGYPAPPCPTNYLFSCQPNLAPAPCAQEAPAYGSAGAYTEQVPQYVGNPSREQVQQFHQRIGMAALMEELRGLGQGIQGQQY", "text": "FUNCTION: Major early eggshell protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the vitelline membrane family."}
+{"protein": "MPVEENYQPLLQEEEERAYDSDEKVLIIGVDSDTESGGSTVLPPFSWKKLWLFTGPGFLMSIAFLDPGNLEGDLQAGAIAGYSLLWLLLWATAMGLLVQLLSARLGVATGRHLAELCREEYPTWASMVLWIMAELALIGADIQEVIGSAIAIKILSNGFVPLWAGVTITACDCFIFLFLENYGVRKLEAVFAVLIGIMAVTFGWMFADAKPSASELFLGILIPKLSSRTIQQAVGVVGCIIMPHNVFLHSALVQSREIDHNKKDRVQEALRYYSIESTTALVISFVINLFVTTVFAKGFYGTELANSIGLVNAGQYLQDKYGGGFFPILYIWGIGLLAAGQSSTITGTYAGQFIMGGFLNLRLKKWLRALITRSCAIIPTMIVALVFDTSEDSLDVLNEWLNVLQSIQIPFALIPLLCLVSKEQIMGTFKIGPILKMVAWLVAALVMVINGYLLLDFFFNEVTGVAFTTVVCGFTGAYVAFIIYLISRGFTCFSRCCPSKQIEVE", "text": "FUNCTION: Divalent metal transporter (PubMed:35700212). Can transport manganese (Mn) and iron (Fe) (PubMed:35700212). Involved in the release of metals stored in the vacuole (PubMed:35700212). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP (TC 2.A.55) family."}
+{"protein": "MPKSKVRKKNDFTISPVSRTPVKVKAGPSSVWFVALFVGLMLIGLIWLLVFQLAATNPVDAPGMLQWMADLGPWNYAIAFAFMITGLLLTMRWR", "text": "FUNCTION: Involved in cell division. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CrgA family."}
+{"protein": "MEDNQRSRFRKICVFCGSHSGHREVFSDAAIELGNELVKRKIDLVYGGGSVGLMGLISRRVYEGGLHVLGIIPKALMPIEISGETVGDVRVVADMHERKAAMAQEAEAFIALPGGYGTMEELLEMITWSQLGIHKKTVGLLNVDGYYNNLLALFDTGVEEGFIKPGARNIVVSAPTAKELMEKMEEYTPSHMHVASHESWKVEELGDYPGQENKPQ", "text": "FUNCTION: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the LOG family."}
+{"protein": "MVADNSEKSTKSVANGSLISTVSSKDDLPNAIIVTQVPEDVFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAKLIVQGFSFKGHELKAFFAQRIYMSANSQMLSPPPLEKQFLISPPCSPPVGWEQTKDMPPVVCNFDLMARLASFAIDEKYEVHNGDELTPAIIVHPCETPIDVPSAIEMPRTPRPSSPCEQ", "text": "FUNCTION: Inhibits tax-6/calcineurin A phosphatase activity and thereby negatively regulates calcineurin-mediated functions (PubMed:12684004, PubMed:26232604, PubMed:27871170). Plays a role in modulating temperature-dependent calcium responses in AFD neurons and in addition, also negatively regulates thermotaxis in a tax-6-dependent manner in AFD neurons (PubMed:26232604). In response to changes in intracellular calcium levels may also regulate nuclear translocation of transcriptional regulators such as crtc-1 (PubMed:26232604). May play a role in regulating body size (PubMed:27871170). Plays a role in male tail tip morphogenesis (PubMed:21408209). SIMILARITY: Belongs to the RCAN family."}
+{"protein": "MGAQLSTLGHVVLSPVWFLYSLIMKLFQRSTPAITLENPDIKYPLRLIDKEVISHDTRRFRFALPSPEHILGLPVGQHIYLSARIDGNLVIRPYTPVSSDDDKGFVDLVIKVYFKDTHPKFPAGGKMSQYLESMKIGDTIEFRGPNGLLVYQGKGKFAIRPDKKSDPVIKTVKSVGMIAGGTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNEHSARFKLWYTVDKAPEAWDYSQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLDRVGHPKERCFAF", "text": "FUNCTION: Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family."}
+{"protein": "MPGRTPTYKLPPLPRLKVKKPVIKQEANRCLVLMSNLLQCWSSNGHMNPVCEKLATDLKACTSQNVMGSNQKPRKSTINYHAARLYDRISGKPHD", "text": "FUNCTION: Involved in mitochondrial genome encoded proteins translation. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mS37 family."}
+{"protein": "MENEAGQLVDLYVPRKCSATNRIIQAKDHASVQINVCAVDAEGRQIPGEKTTYAISGFVRSKGESDDCINRLTTQDGLLEGVWSYQR", "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 (By similarity). eS21 is required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability (PubMed:14623272). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family."}
+{"protein": "MAVAVGRPSNEELRNLSLSGHVGFDSLPDQLVNKSTSQGFCFNILCVGETGIGKSTLMDTLFNTKFESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDDSYKPIVEYIDAQFEAYLQEELKIKRSLFNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNELHKFKSKIMSELVSNGVQIYQFPTDEETVAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVMRVKEKEAELKEAEKELHEKFDLLKRTHQEEKKKVEDKKKELEEEVSNFQKKKAAAQLLQSQAQQSGAQQTKKDKDKKNPWLCTE", "text": "FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity. FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Synapse. Cell projection, dendritic spine. Cell projection, axon. Note=Partly colocalizes with stress fibers. Association with microtubules not observed in embryonic fibroblasts. In cultured hippocampal neurons, localizes to 54% of GABAergic and 25% of glutamatergic synapses. Frequently present at the base of dendritic protrusions and at the bifurcation points of the dendritic branches. Expressed at low levels in the axons of mature cultured hippocampal neurons. In embryonic fibroblasts, associated with actin stress fibers. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Synapse Cell projection, dendritic spine Cell projection, axon. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
+{"protein": "MQPPELEIGMPKRHREHIRKNLNILVEWTNYERLAMECVQQGILTVQMLRNTQDLNGKPFNMDEKDVRVEQHRRLLLKITQRGPTAYNLLINALRNINCLDAAVLLESVDESDSRPPFISLNERRTSRKSADIVDTPSPEASEGPCVSKLRNEPLGALTPYVGVVDGPEVKKSKKIHGGDSAILGTYKMQSRFNRGVLLMVNIMDYPDQNRRRIGAEKDSKSLIHLFQELNFTIFPYGNVNQDQFFKLLTMVTSSSYVQNTECFVMVLMTHGNSVEGKEKVEFCDGSVVDMQKIKDHFQTAKCPYLVNKPKVLMFPFCRGDEYDLGHPKNQGNLMEPVYTAQEEKWPDTQTEGIPSPSTNVPSLADTLVCYANTPGYVTHRDLDTGSWYIQKFCQVMADHAHDTDLEDILKKTSEAVGNKRTKKGSMQTGAYDNLGFNKKLYFNPGFFNE", "text": "FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Effector of steroid-mediated apoptosis during insect metamorphosis. Overexpression promotes programmed cell death. Interaction with Diap1 is required to suppress Dronc-mediated cell death; via Diap1-mediated ubiquitination of Dronc. Rate-limiting caspase in rpr and hid death pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C14A family."}
+{"protein": "MWVPGFGSARLPQRRRSGLESSSVRPLWLLLLFLLAAVRPVRAWESGDLELFDLVEEVQLNFYEFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDVLINGLPDWRQPVFYYRRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLGRKKRERKKKTGSKSVDAAKLGASEKNERLLIKPQWHDLLPCKLGIWFCLTLKALPHLIQDAGQFYAKYKETKLKEKEDALARIEIETLQKQKKVKVKKPKPEFPVYMPLENTYIQSYDHGTSIEEIEEQMDDWLENRKRTQKRQAPEWTEEDLSQLTRSMVKFPGGTPGRWDKIAHELGRSVTDVTTKAKELKDSVTSSPGMTRLSELKSNGQNSRPIKIATALPDDIITQREDSAGAMEDEEHEAAEGEQESATTEARPRRRKSARAAEAVTRVEPEEKLRGKRQKDFDISEQNDSSDEEKQRKERTRAAEEAWTQSQQKLLELALQQYPKGASDRWDKIAKCVPSKSKEDCIARYKLLVELVQKKKQAKS", "text": "FUNCTION: May modulate protein synthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Microsome membrane; Single-pass type I membrane protein."}
+{"protein": "MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALDSYSVANLIREPLVIFVCATTGQGDPPDNMKNFWRFIFRKSLPSSSLCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWVGDLWEKIMVMYPVPLDIPEIPHGVPLPSKFIFQFLQEVPSIGAEELNIASSAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPGLPQPCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCDFPHTAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQAGPVRVPLWVRPGSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTGNFLFFGCRQRDQDFYWQTEWQKLEQKGWLTLVTAFSREQEQKVYVQHRLRELGPLVWELLDGQGAYFYLAGNAKYLPTDVSEALMSIFQEEGRLSTADASAYLARLQQTLRFQTETWA", "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 CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair (By similarity). In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Note=Concentrated in perinuclear structure. 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": "MLLFIILSVGVDAISYIQNDRSNDLCIVYEMTSFGTSFNNANDSLVKLHKHMGLKYEVCKIESNANALTQMQKCNCIYDDTPQIVVFTNFKKSSLKTLIGTENKCELLPQTTIYTPTVDIESEYFIYGNDVKICYLDKNLLGIGCDATDTTSWLDLDAGLPTNHALDIPEITSDGFKLFAKYSDSFLCQRLMDEPKKQIQFYAEVDNVPSNDVIESSRSWASVWKVVKTVLHFTYHILDLFYGNRRATARMIEHSPLG", "text": "FUNCTION: Outer capsid protein involved in attachment and possibly entry into the host epithelial cell. It is subsequently lost, together with VP4, following virus entry into the host cell. The outer layer contains 780 copies of VP7, grouped as 260 trimers. 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 (By similarity). SUBCELLULAR LOCATION: Virion Host rough endoplasmic reticulum membrane; Single-pass membrane protein; Lumenal side Note=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 (By similarity). SIMILARITY: Belongs to the rotavirus VP7 family."}
+{"protein": "MTVFNKFARSFKSHWLLYLSVIVFGITNLVASSGAHMVQRLLFFVLTILVVKRISSLPLRLLVAAPFVLLTAADMSISLYSWCTFGTTFNDGFAISVLQSDPDEVAKMLGMYSPYLCAFAFLSLLFLAVIIKYDVSLPTKKVTGILLLIVISGSLFSACQFAYKDAKNKNAFSPYILASRFATYTPFFNLNYFALAAKEHQRLLSIANTVPYFQLSVRDTGIDTYVLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFNQAISGAPYTALSVPLSLTADSVLSHDIHNYPDNIINMANQAGFQTFWLSSQSAFRQNGTAVTSIAMRAMETVYVRGFDELLLPHLSQALQQNTQQKKLIVLHLNGSHEPACSAYPQSSAVFQPQDDQDACYDNSIHYTDSLLGQVFELLKDRRASVMYFADHGLERDPTKKNVYFHGGREASQQAYHVPMFIWYSPVLGDGVDRTTENNIFSTAYNNYLINAWMGVTKPEQPQTLEEVIVHYKGDSLVVDANHDVFDYVMLRKEFTEDKQGNPTPEGQG", "text": "FUNCTION: There are several lipid A forms in this strain, including a phosphoethanolamine (1-O-P-pEtN) form; overexpression of this gene does not lead 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."}
+{"protein": "MGQRLSGGRSCLDVPGRFLPQPPPPPPPVRRKLALLFAMLCIWLYMFLYSCAGSCTAAPGLLLLGSGSRATHAQPALVTAPNETSPKMPFRAPPANSLAAGKDKTVGAGSQEEQSPEAPDSPSPISSFFSGAGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYHKGLAWYRDLMPRTLKGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQTLSKRPDIPSFESLTFRNRSAGLIDTSWSAIQIGLYAKHLEPWLRHFPLGQMLFVSGERLVSDPAGELRRVQDFLGLKRIITDKHFYFNQTKGFPCLKKAEGSGKPHCLGKTKGRAHPTIAREVLRQLRDFYRPFNRKFYQMTGRDFGWD", "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": "MPKSDTKQKKRRSNKNRLRIKRARLFGPKDIDQVKEDIESQKKIEYDPELPGGGHFYCCECDRHFITEKVLMEHKRSNPHRRRAKEVREVAHSQRDAEWAVGLT", "text": "FUNCTION: Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein family."}
+{"protein": "MKKPLVTRNEIAEAIALHTACMPTREIPGAIANYFMITRRFYTRTDKAVINRLLIAEIRDYLIEQGRLRYATVAAEIRKEAHRMTGNNLNVEKTAPVTSATPAPAVNIIPNTGDTIDSQTLLKMVNEARKLCGEPEVRNNKFIEKILDELEGEFYTKSAKSHGTRAGRSFEVITMTYKQALRVAARESKAVRRSLIDKLEELQQANSPAPSIPQTLPEALRLAAELAEQKMQLEQQLVAAAPKVDFADRVSVANGILIGNFAKVVGLKQNALFSWLRQNGILMAFGARKNVPRQQYINAGYFTVKEVVLDDENGYQIRLTPN", "text": "FUNCTION: Antagonist of the C1 repressor or repressor bypass function."}
+{"protein": "MDSDETGFEHSGLWVSVLAGLLLGACQAHPIPDSSPLLQFGGQVRQRYLYTDDAQQTEAHLEIREDGTVGGAADQSPESLLQLKALKPGVIQILGVKTSRFLCQRPDGALYGSLHFDPEACSFRELLLEDGYNVYQSEAHGLPLHLPGNKSPHRDPAPRGPARFLPLPGLPPALPEPPGILAPQPPDVGSSDPLSMVGPSQGRSPSYAS", "text": "FUNCTION: Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity requires the presence of KLB. Regulates systemic glucose homeostasis and insulin sensitivity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the heparin-binding growth factors family."}
+{"protein": "MAALASSLIRQKREVREPGGSRPVSAQRRVCPRGTKSLCQKQLLILLSKVRLCGGRPARPDRGPEPQLKGIVTKLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFENYYVLYASALYRQRRSGRAWYLGLDKEGQVMKGNRVKKTKAAAHFLPKLLEVAMYQEPSLHSVPEASPSSPPAP", "text": "FUNCTION: Probably involved in nervous system development and function. SIMILARITY: Belongs to the heparin-binding growth factors family."}
+{"protein": "MGVKLEIFRMIIYLTFPVAMFWVSNQAEWFEDDVIQRKRELWPPEKLQEIEEFKERLRKRREEKLLRDAQQNS", "text": "FUNCTION: Plays an essential role in mitochondrial complex IV maturation and assembly. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Mitochondrion Mitochondrion inner membrane. SIMILARITY: Belongs to the PET100 family."}
+{"protein": "MSTVVSEGRNDGNNRYSPQDEVEDRLPDVVDNRLTENMRVPSFERLPSPTPRYFGSCKWFNVSKGYGFVIDDITGEDLFVHQSNLNMQGFRSLDEGERVSYYIQERSNGKGREAYAVSGEVEGQGLKGSRIHPLGRKKAVSLRCFRCGKFATHKAKSCPNVKTDAKVCYTCGSEEHVSSICPERRRKHRPEQVAAEEAEAARMAAEKSSPTTSDDDIREKNSNSSDE", "text": "FUNCTION: Heterochronic protein which controls the choice of stage specific cell fates (PubMed:9054503, PubMed:6494891, PubMed:2702689, PubMed:2628162, PubMed:1916265, PubMed:7671811, PubMed:8625405, PubMed:8756295, PubMed:8756296, PubMed:9477318, PubMed:9649524, PubMed:10706289, PubMed:12871707, PubMed:15073154, PubMed:16139228). Regulates the timing of the second larval stage events (L2 events) in the hypodermis (PubMed:2702689, PubMed:2628162). May negatively regulate the larval to adult transition via the suppression of the microRNA (miRNA) let-7 during L3 (PubMed:10706289, PubMed:12871707, PubMed:16139228). Through this regulatory role, controls the timing of the sexual maturation of the nervous system (PubMed:31264582). Also has a role in the fox-1-sex-1-mediated determination of sexual fate (PubMed:21471153). Plays a role in governing the developmental timing of male tail tip morphogenesis (PubMed:26811380, PubMed:30956008). Plays a role in controlling the seam cell number during larval stages (PubMed:21471153, PubMed:28602583). Plays a role in vulval development (PubMed:28602583). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lin-28 family."}
+{"protein": "MFKVPVGLASRTRELMNSVTLNSLNNGKGFNMYLPGILRAFPKPVPSAITSPAIPKYRGESFQFRKLSCISSNYCSTTHQFLSSLKSSTSRLVGKRAFHSSRRAEIKFIFSSKSPKNGNKPFVKVYKVSPFFIIFATASIFTFILTSTIVVIPLIFHFFFPLLIMFFFFKQFKKWQKNIFYKDVLTSLPKTKLKITLPTMRSLQLQPMVQSWKEISSRMGIPNEFAKGLNVDLVKQEETRKQFLSFLQKRVLESFTKNELGIRSYFLGDSVEKWIKESYDLELDIDNCRSELRKFQTFIFSSVRYKLYLDSMKNLPLNPSKKLEGKKHIADVYVIILDESFPAIMFNGGAYSKADFFKILQESETSNSSKTLNTIIAIKSVNTLLSKHFVITTNGDSGEFFSKYNISKINDKNTEYTLKE", "text": "FUNCTION: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post- transcriptional gene expression. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion membrane; Multi-pass membrane protein."}
+{"protein": "MVSAGNHAIVALGWTTSEDGTLTRPLDLVENWLLARIQRANTPPGREAEGLTYKLKLRLPQDIDDPIPYLRRAWLVFRYVQPLIGAIYPPYSERDETGRYLVTVPPMDPEEWLRLSFHVNQGSQAVFRDVDDAGMIFRPRPTAMAYWFPPSSTLVIRSTHLRFDAVGLYKATNTFMLGLESVFRLGLDANLDCYTTDVKQPSLPPGIDYILGFPPQETPVSHRVGCAVDELMRHWHHGLYSLSLPVREGSEDAAPANTQHMVTLFDEPTLEAIVAGCKELGVSVSAAVHASIVRVWASFPQQQHTGARNMLIPLVANLRPLLDPKWVVPDYALSLCIFVVPFCLTGGFEDLTQRLGAVYSRDLSALPSDSAGDPVSFLELLPLYDSQEAAFLGSLPVAGCPPFRVPNLSSLGVLERYLARAYGQKGAQAPVCEIEDVALVNATTDPTIEFQLFTFRGTMRLYLYYNDAYYTEDFLASVMEMVRESLLQELGLDGSESSEGLDPKEA", "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": "MSRFVQDLSKAMSQDGASQFQEVILQELELSVKKELEKILTTAASHEFEHTKKDLDGFRKLFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGLPDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPIAKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYILNHLMNPPNGKRCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAIDMEIIVNPKTLDGGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSGNLRILDH", "text": "FUNCTION: UTP--glucose-1-phosphate uridylyltransferase catalyzing the conversion of glucose-1-phosphate into UDP-glucose, a crucial precursor for the production of glycogen. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UDPGP type 1 family."}
+{"protein": "MADQLSEEQISEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMRDTDSEEEIKEAFKVFDKDGNGYISAAELRHVMTNLGEKLTDNEVDEMIREADVDGDGQINYEEFVKMMLSK", "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 (By similarity). SIMILARITY: Belongs to the calmodulin family."}
+{"protein": "MGAKSMRSWCLCQICSCGSDYCPYEIVKQPRHVPEEYKPKQGKIDLGTTYKRDLNSYKVQPVAIVRPLERQVKKGKLDTVPTYKDDYRAWDLHKSELYKPEQTYHPPTVKFGNSTTFQDDFVPQEIKPRQSFKPSSVVKRSTAPFNGITSHRLDYIPHQLELKFERPKEVYKPTDQRFEDLTTHRCDFQGLIGETAKLCRPVHTRVTQNALFEGSTEFRESFQPWEIPPPEVKKVPEYVPPTGSMLLNSTSHLDYVPYQANHVVPIRPVSQKRSNNFPFQGKSIMKEDFPAWESCRQGLIKKQQQIPNPSGKFDGLSTFRSHYVPHELIPTESCKPLNIAFKSSVPFDDVTMYSVEYTPKRQEICPASYPSPPGYIFDNTNSQGHKFFRKIIPAVKAF", "text": "SIMILARITY: Belongs to the FAM154 family."}
+{"protein": "MDFDLTDEQRAIQDTFARFSDERIAPQAAALDEARAFPRALFRELAELGFFGMRYPESVGGSGLALSEFCLALSEVARGSMSLAGAVAMQSLMGTKFLQLLGNADIVERLFKPALRGDRIGAICMTEPNAGSDLESIATTATRVDGGYVINGQKTWITSAPVADFFTVFARAGDEKKLTIFLVEKDVPGITVGREIHKMGVWALPTSEVAFDGCFVPDSHRLSKEEGDGEGHLKKTLAEIRIITGAMALGVARAALFAAVRYAGERKQFGKPINRFQAIQLKLADMATGLEAATTLVHRAAWLCDMKRPHHKEAAMAKLFATETAAGICDDAARVLASYGYAMEYPVQRYLRDVRFTLIGGGTSEILKLVIAKEVSS", "text": "FUNCTION: Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones (PubMed:34059946). Catalyzes the irreversible oxidative decarboxylation of (2- aminobenzyl)malonyl-CoA to 2-aminocinnamoyl-CoA and CO(2) (Probable). In vitro, shows high catalytic efficiency with benzylmalonyl-CoA, a chemical analog of the physiological substrate, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities (PubMed:34059946). SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
+{"protein": "MSLFDFFKNKGSAATATDRLKLILAKERTLNLPYMEEMRKEIIAVIQKYTKSSDIHFKTLDGNQSVETIEVEIILPK", "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 (By similarity). SIMILARITY: Belongs to the MinE family."}
+{"protein": "MRRLRRWAIAALLLLPLLPPPGLGALGPRGALHWRSSAHVGSPESPEGSEVTEPSRLVRQSSGGEVRKPQLDTRVRQDPPRGTPVHLAQVSFVIPAFDSNFTLDLELNHHLLSSQYVERHFSREGTRQHSTGAGDHCYYHGKLRGNPQSFAALSTCQGLHGVFSDGNLTYIVEPKEIAGPWGPPQGPLPHLIYRTPLLPAPLGCREPGCLFAVPAQSALPNWPKLRRKRQVRRGHPTVHSETKYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRREGLPEPSDATHLFSGRTFQSTSSGAAYVGGICSLSRGGGVNEYGNMGAMAVTLAQTLGQNLGMMWNKHRSSAGDCKCPDIWLGCIMEDTGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKPLKLLDPPECGNGFVEAGEECDCGSVQECSRAGGNCCKKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPNLHKLDGYYCDHEQGRCYGGRCKTRDRQCQALWGHAAADRFCYEKLNVEGTERGNCGRKGSGWVQCSKQDVLCGFLLCVNISGAPRLGDLGGDISSVTFYHQGKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLPASAFNFSTCPGSGERRICSHHGVCSNEGKCICQPDWTGKDCSIHNPLPTSPPTGETERYKGPSGTNIIIGSIAGAVLVAAIVLGGTGWGFKNIRRGRSGGA", "text": "FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Required for localization of the potassium channel subunit proteins KCNA1/KV1.1 and KCNA2/KV1.2 at cerebellar cortex basket cell distal terminals, is thereby involved in ephaptic inhibitory synchronization of Purkinje cell firing and response to stress (PubMed:26269648). Plays a role in spatial learning and motor coordination (PubMed:16504143). Involved in the nociceptive pain response to chemical-derived stimulation (PubMed:16729981). SUBCELLULAR LOCATION: Presynaptic cell membrane; Single-pass type I membrane protein. Perikaryon Cell projection, axon Note=Localizes to basket cell terminals and pinceaux."}
+{"protein": "MRDPLTDCSYNKVYKSLKEFAQHGDNFCKQITSVLQQRANLEISYAKGLQKLAVRLSKALQSTKKNCLSTAWAWASESMKSAADLHQKLGKAIELEAIKPTHQVLSMQEKKRKSLDNEVEKTANLVINNWNQQIKAKKKLMMSTKKHEALFHLVESSKQSLTQKEKQKLLNKLKKSTEKLEKEDESYYQKNMAGYSTRLKWESTLENCYKSMLELEKERIQLLCNNLNQYSQHISLFGQTLTTCHTQIHCAISKVDVEKDIQALMEETAILSIENKSELLLADYFEEDPKNPMDKERRKSLLKPKLGRLQRDIEKASRDKEGLERKLKALASSSSFSDAKSQKDMETLMDENSLKLDLLQANSYKLSSVLADLEQRPKPCHPCSTCIFKWKEKEHSHTYVKISRPLLTKRLEKAESKAPAGGQNNPSSSPSGSTVSQASKHLCKALYTFQARQDDELNLEKGDIVTVHEKKEEGWWFGSLKGKRGHFPAAYVEELPPKAGNTATQA", "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": "MTNQILSNDDWGRYKKEGFLVTKFGDLTDYVMNWARSGSLWPMTFGLACCAVEMMHTASSRYDLDRYGIMFRASPRQSDVMIVAGTLTNKMAAALRKVYDQMADPKYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALLYGMLCLQNKIKRTRNG", "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). 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. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
+{"protein": "MPLRNQNRAPLPSPNVKKEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDTKGKIEQMTDIIKKLKVCVRWYQQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKKLHNTILELKGNIRVFCRVRPLLPDDGGRQEASVIAYPTSTESLGRGIDVVQSGNKHPFTFDKVFDHGASQEEVFFEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPETPEQKGLIPRSLEQIFKTSQSLSTQGWKYKMQVSMLEIYNESIRDLLSTSRTIAIESVRADSSTSGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNESTEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARVNACEIGIPRRQTSAKLLDSRLSYG", "text": "FUNCTION: Kinesin that supports microtubule movement in an ATP- dependent manner and that functions as a minus-end directed motor as well as a plus-end tracking protein. During mitosis, is involved in early spindle assembly. Participates in the capture of antiparallel interpolar microtubules and helps in generating force to coalign microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, phragmoplast. Note=In interphase, is enriched specifically at growing microtubule plus-ends. In dividing cells, accumulates in spindle midzones and phragmoplast leading edges. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-14 subfamily."}
+{"protein": "MELSETYACVPSTERGRGILISGNSKSDTILYTNGRSVVTLDLNNPLKVSIYGEHAYPATVARYSPNGEWIASGDVSGTVRIWGAYNDHVLKNEFKVLAGRIDDLQWSADGMRIVASGDGKGKSLVRAFMWDSGSNVGEFDGHSRRVLSCAIKPTRPFRIVTCGEDFLVNFYEGPPFKFKLSSREHSNFVNCVRFAPDGSKFITVSSDKKGIIYDGKTCEILGELSSDDGHKGSIYAVSWSPDGKQVLTVSADKSAKIWDISDNGSGSLNTTLNCPGSSGGVDDMLVGCLWQNDHIVTVSLGGTISIFSASDLDKSPFQFSGHMKNVSSLAVLKGNADYILSGSYDGLICKWMLGRGFCGKLQRTQNSQIKCFAAHEEEIVTSGYDNKISRISYKDDQCTNEESIDIGNQPKDLSLAPLSPDLLLVTFESGVVFLRDGKVVSTINLGFIVTALAVTPDGTEAVIGGQDGKLHLYSINGDSLTEEAVLERHRGAISVIRYSPDLSMFASADLNREAVVWDRVSREMKLKNMLYHSARINCLAWSPNSTMVATGSLDTCVIVYEVDKPASSRMTIKGAHLGGVYGLGFADDSHVVSSGEDACIRVWSFTPQ", "text": "FUNCTION: Binds actin. Enhances the F-actin depolymerization activity of actin-depolymerizing factor (ADF) proteins."}
+{"protein": "MALVVQKYGGSSLESAERIRNVAERIVATKKAGNDVVVVCSAMGDTTDELLELAAAVNPVPPAREMDMLLTAGERISNALVAMAIESLGAEAQSFTGSQAGVLTTERHGNARIVDVTPGRVREALDEGKICIVAGFQGVNKETRDVTTLGRGGSDTTAVALAAALNADVCEIYSDVDGVYTADPRIVPNAQKLEKLSFEEMLELAAVGSKILVLRSVEYARAFNVPLRVRSSYSNDPGTLIAGSMEDIPVEEAVLTGVATDKSEAKVTVLGISDKPGEAAKVFRALADAEINIDMVLQNVSSVEDGTTDITFTCPRADGRRAMEILKKLQVQGNWTNVLYDDQVDKVSLVGAGMKSHPGVTAEFMEALRDVNVNIELISTSEIRISVLIREDDLDAAARALHEQFQLGGEDEAVVYAGTGR", "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": "MACTEFSFHVPSLEELAEVLQKGLKDNFAHVQVSVVDCPDLTKEPFTFPVKGICGQTRIAEVGGVPYLLPLVNKKKVYDLNEIAKEIKLPGAFILGAGAGPFQTLGFNSEFMPIVQTASEHHQPVNGSYFARANPADGKCLLEKYSQKYPDFGCALLANLFASEGQPGKVIEVQAKKRTGEHNFVSCMRQTLEKHYGDKPVGMGGTFLVQKGKVKAHIMPAEFSSCSLNSDEAVNQWLNFYEMKAPLVCLPVFVSKDPGLDLRLEHTHFFSHHGEGGHYHYDTTPDTVEYLGYFSPAQFLYRIDQPKETHAFGRD", "text": "FUNCTION: Exhibits ester hydrolase activity on the substrate p- nitrophenyl acetate. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MTHLQAGLSPETLEKAKVELKENPDTLHQDIQEVRDMIITRPDIGFLRTDDAFILRFLRARKFNHFEAFRLLAQYFEYRQQNLDMFKNLKATDPGIKQALKDGFPGVLSNLDRYGRKILVLFAANWDQSRYTFVDILRAILLSLEAMIEDPELQVNGFVLIIDWSNFTFKQASKLTPSMLRLAIEGLQDSFPARFGGIHFVNQPWYIHALYTVIRPFLKDKTRKRIFMHGNNLNSLHQLILPEILPSELGGMLPPYDMGTWARTLLDHAYDEETDYCPESYTLSVKDLEKDLSPKTMKRSQSVVEPGVLKRPEKVKSEEENMQPLLSLD", "text": "FUNCTION: Required for normal morphology of late endosomes and/or lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Early endosome membrane; Peripheral membrane protein Cytoplasmic vesicle, clathrin-coated vesicle."}
+{"protein": "MQIQSFYHSASLKTQEAFKSLQKTLYNGMQILSGQGKAPAKAPDARPEIIVLREPGATWGNYLQHQKASNHSLHNLYNLQRDLLTVAATVLGKQDPVLTSMANQMELAKVKADRPATKQEEAAAKALKKNLIELIAARTQQQDGLPAKEAHRFAAVAFRDAQVKQLNNQPWQTIKNTLTHNGHHYTNTQLPAAEMKIGAKDIFPSAYEGKGVCSWDTKNIHHANNLWMSTVSVHEDGKDKTLFCGIRHGVLSPYHEKDPLLRHVGAENKAKEVLTAALFSKPELLNKALAGEAVSLKLVSVGLLTASNIFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGDLQTVKIKPDVAAFNVGVNELALKLGFGLKASDSYNAEALHQLLGNDLRPEARPGGWVGEWLAQYPDNYEVVNTLARQIKDIWKNNQHHKDGGEPYKLAQRLAMLAHEIDAVPAWNCKSGKDRTGMMDSEIKREIISLHQTHMLSAPGSLPDSGGQKIFQKVLLNSGNLEIQKQNTGGAGNKVMKNLSPEVLNLSYQKRVGDENIWQSVKGISSLITS", "text": "FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicles, which are essential to create a favorable environment where Salmonella can replicate and avoid immune defenses of the host cell. SUBCELLULAR LOCATION: Secreted Note=Secreted via the type III secretion system 1 (SPI-1 TTSS). SIMILARITY: Belongs to the phosphatase IpgD/SopB family."}
+{"protein": "MAALTMQFEGEKKNVSEVADVTLKQEDEQQERRSYSTPFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGDRERMPEPIVRAFGVLKKCAAKVNMEYGLDPMIGEAIMEAAQEVAEGKLNDHFPLVVWQTGSGTQSNMNANEVIANRAAEILGHKRGEKIVHPNDHVNRSQSSNDTFPTVMHIAAATEITSRLIPSLKNLHSSLESKSFEFKDIVKIGRTHTQDATPLTLGQEFGGYATQVEYGLNRVACTLPRIYQLAQGGTAVGTGLNTKKGFDVKIAAAVAEETNLPFVTAENKFEALAAHDACVETSGSLNTIATSLMKIANDIRFLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAVTIGGSNGHFELNVFKPVIASALLHSIRLIADASASFEKNCVRGIEANRERISKLLHESLMLVTSLNPKIGYDNAAAVAKRAHKEGCTLKHAAMKLGVLTSEEFDTLVVPEKMIGPSD", "text": "FUNCTION: Cytosolic fumarate hydratase that catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:29688630). Catalyzes the dehydration of L-malate to fumarate in the cytosol: required for the massive fumarate accumulation during the day in plants grown under high nitrogen (PubMed:20202172). Also required for acclimation of photosynthesis to cold: acts by mediating accumulation of fumarate at low temperature, leading to reduce accumulation of phosphorylated sugars (PubMed:27440755). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase subfamily."}
+{"protein": "MAEVEAALPVAATETPEVAAEGDAGAAEAKGPHKLQRQWTFWYDIQTKPKPGAAWGTSLKKGYTFDTVEEFWCLYDQIFRPSKLVGSADFHLFKAGVEPKWEDPECANGGKWTVISSRKTNLDTMWLETCMALIGEQFDESQEICGVVASVRQRQDKLSLWTKTASNEAVQVDIGKKWKEVIDYNDKMVYSFHDDSRSQKPSRGGRYTV", "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 (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). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the eukaryotic initiation factor 4E family."}
+{"protein": "MLLLINVILTLWVSCANGQEVKPCDFPEIQHGGLYYKSLRRLYFPAAAGQSYSYYCDQNFVTPSGSYWDYIHCTQDGWSPTVPCLRTCSKSDVEIENGFISESSSIYILNEETQYNCKPGYATAEGNSSGSITCLQNGWSTQPICIKFCDMPVFENSRAKSNGMWFKLHDTLDYECYDGYESSYGNTTDSIVCGEDGWSHLPTCYNSSENCGPPPPISNGDTTSFPQKVYLPWSRVEYQCQSYYELQGSKYVTCSNGDWSEPPRCISMKPCEFPEIQHGHLYYENTRRPYFPVATGQSYSYYCDQNFVTPSGSYWDYIHCTQDGWLPTVPCLRTCSKSDIEIENGFISESSSIYILNKEIQYKCKPGYATADGNSSGSITCLQNGWSAQPICIKFCDMPVFENSRAKSNGMRFKLHDTLDYECYDGYEISYGNTTGSIVCGEDGWSHFPTCYNSSEKCGPPPPISNGDTTSFLLKVYVPQSRVEYQCQSYYELQGSNYVTCSNGEWSEPPRCIHPCIITEENMNKNNIQLKGKSDIKYYAKTGDTIEFMCKLGYNANTSVLSFQAVCREGIVEYPRCE", "text": "FUNCTION: Involved in complement regulation. Can associate with lipoproteins and may play a role in lipid metabolism. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSMGIAARPPRAALLPPPSVPRSR", "text": "FUNCTION: This peptide is involved in the control mechanism of the synthesis of the macrolide-lincosamide-streptogramin B resistance protein."}
+{"protein": "MLVLYGHSTQDVPETNARVVGGTEARRNSWPSQISLQYLSGGKWYHTCGGTLIRQNWVMTAAHCVDRTMTFRVVIGEHNLSQNDGTEQSASVQKIVVHPYWNSNDVSAGYDIALLRLAQKVTLNSYVQLGVLPQEGAILANNSPCYITGWGLTKTNGQLAQVLQQAYLPTVDYAICSSSSYWGSIVKKSMVCAGGDGIRSGCQGDSGGPLHCSVNGKYTVHGVTSFVSSLGCNVSRKPTVFTRVSAYITWINNVIASN", "text": "FUNCTION: Acts upon elastin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily."}
+{"protein": "MSMLTVAMPKGRIFDEAVGLLRKAGYNLPAEFEASRKLIVDVPEENMRFILAKPMDVPTYVEHGVADVGVAGKDVMLEEERDVYEVLDLKISECYLAVAGLPNYEKKHDLNPKVASKYPHLATRYFKEQGEQVEIIKLNGSIELAPLIGLADRIVDIVSTGRTLRENGLVELEKMMTITSRLIVNPVSYRMKDERIDEMVERLLQVVEGDGA", "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": "MSNEVEQKKSIKTINDLPGISQTVINKLIEAGYSSLETLAVASPQDLSVAAGIPLSTAQKIIKEARDALDIRFKTALEVKKERMNVKKISTGSQALDGLLAGGIETRTMTEFFGEFGSGKTQLCHQLSVNVQLPPEKGGLSGKAVYIDTEGTFRWERIENMAKALGLDIDNVMNNIYYIRAINTDHQIAIVDDLQELVSKDPSIKLIVVDSVTSHFRAEYPGRENLAVRQQKLNKHLHQLTRLAEVYDIAVIITNQVMARPDMFYGDPTVAVGGHTLYHVPGIRIQLKKSRGNRRIARVVDAPHLPEGEVVFALTEEGIRDAEE", "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. SIMILARITY: Belongs to the eukaryotic RecA-like protein family."}
+{"protein": "MAMQREAGVQDFVLLDQVSMEKFMDNLRKRFQNGSIYTYIGEVCVSMNPYRQMNIYGPETIRKYKGRELFENAPHLFAIADSAYRVLKQRQQDTCILISGESGAGKTEASKIIMKYIAAVTNAQGQNEIERVKNVLIQSNAILETFGNAKTNRNDNSSRFGKYMDIEFDYKADPVGGIITNYLLEKSRVVQQQPGERNFHSFYQLLRGANDNELRQYELQKETGKYHYLNQGSMDILTEKSDYKGTCNAFKTLGFSTDEVQTIWRTIAAVLHLGNVEFQTIEDELVISNKQHLKSTAKLLQVTETELSTALTKRVIAAGGNVMQKDHNATQAEYGKDALAKAIYDRLFTWIISRINRAILFRGSKTQARFNSVIGVLDIYGFEIFDSNSFEQFCINYCNEKLQQLFIELVLKQEQEEYQREGIEWTNIEYFNNKIICDLVEQPHKGIIAIMDEACLSVGKVTDDTLLGAMDKNLSKHPHYTSRQLKPTDKELKHREDFRITHYAGDVIYNINGFIEKNKDTLYQDFKRLLHNSKDANLSEMWPEGAQDIKKTTKRPLTAGTLFQRSMADLVVTLLKKEPFYVRCIKPNDLKSSTVFDEERVEHQVRYLGLLENLRVRRAGFVHRQRYDKFLLRYKMISQYTWPNFRAGSDRDGVRVLIEEKKFAQDVKYGHTKIFIRSPRTLFALEHQRNEMIPHIVTLLQKRVRGWIVRRNFKKMKAAITIVRAYKAYKLRSYVQELANRLRKAKQMRDYGKSIQWPQPPLAGRKVEAKLHRMFDFWRANMILHKYPRSEWPQLRLQIIAATALAGRRPYWGQARRWVGDYLANSQENSGYEAYNGSIKNIRNHPADGETFQQVLFSSFVKKFNHFNKQANRAFIVSDSTIHKLDGIKNKFKDMKRTIKIRELTSISVSPGRDQLIVFHSSKNKDLVFSLESEYTPLKEDRIGEVVGIVCKKYHDLTGTELRVNVTTNISCRLDGKARIITVEAASNVEVPNFRPKEGNIIFEVPAAYCV", "text": "FUNCTION: Unconventional myosin that functions as actin-based motor protein with ATPase activity (PubMed:30467170). Binds to membranes enriched in phosphatidylinositol 4-5-bisphosphate, and can glide along actin filaments when anchored to a lipid bilayer (PubMed:30467170). Generates left-right asymmetry at the level of single cells, organs and the whole body via its interaction with the actin cytoskeleton, both in the embryo and the adult (PubMed:16598258, PubMed:16598259, PubMed:18521948, PubMed:26073018, PubMed:25659376, PubMed:30467170). Normal left-right asymmetry of the larval midgut and hindgut requires expression in the embryonic hindgut epithelium during a critical time period, 10 to 12.75 hours after egg laying (PubMed:18521948). This period corresponds to a late stage of germband retraction, and precedes left-right asymmetric morphogenesis (PubMed:18521948). Expression in segment H1 of the imaginal ring is required at 0 to 24 hours after pupation for changes of cell shape and orientation in the H2 segment, which then gives rise to normal, dextral looping of the adult hindgut (PubMed:16598258, PubMed:26073018). Required during a critical period, 126-132 hours after egg laying, for normal, dextral rotation of the adult male genitalia (PubMed:16598258, PubMed:16598259, PubMed:22491943, PubMed:26073018, PubMed:25659376). Has a double role by promoting dextral rotation in the posterior compartment of segment A8 of the male genital disk, and in repressing sinistral looping in the anterior compartment (PubMed:16598259). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cell cortex Cytoplasm, cytoskeleton Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction Cell junction, adherens junction Cell projection Note=Detected throughout the cytoplasm. Detected primarily in the basolateral cytoplasmic region of immature enterocytes. Detected also in the apical cytoplasmic region in midgut enterocytes and follicle cells (PubMed:7589814). Colocalizes with the actin cytoskeleton (PubMed:7589814, PubMed:16598258, PubMed:16598259, PubMed:25659376). Colocalizes with arm at adherens junctions (PubMed:16598259). Colocalizes with ds at cell junctions (PubMed:26073018). SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family."}
+{"protein": "MKLTPELLSRSSSSINTLRDRELDLRGLKIPAIENLGVTRDQNDAIDLTDNDIRYLGNFPLLQQLKTLQLANNLISRIDPRIGHSLPALHSLNLTNNCISDLSELVHLSKCRRLEYLCLMGTPASREAQYREFVIWKLPQVRVLDYQRIKDKERARAKDLMETEDGRPTALAANILKKLGASAMDVDVDVMVGKQKTFEPGRLNGSSRRLLTAEERKAIEDAIESSESLEEIRKLEEQLKMGHTFV", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the U2 small nuclear ribonucleoprotein A family."}
+{"protein": "MSLISAVEDRDIHNIGKTSGGGSRTSSITSSKKSLKHGSKSLRKPKVYQTTGELLSREALYKAKLKYGVYQSPAQSYSIGVSDAHAASDKAANLAHDNQTTVEAYKRMFIDPNATKAASKMGPKVVRNNSITSATSKTSXESQTKRKSKESPGAAASKAYSMTMETTSLSSQTNSRSYSITSASSVLSGASGSFNSTVNPKPKTLNLEKVLVGAEKKAESRIKERWEPEKTNFQYGVKTDEHGNLNQFSFSNEMMNNIMAKVDAPKAQDLQKVKKVSAEKEAKSMKFALGAANAVKDMHPGEDIDKSIALKAQKRETYLSQLTSQQVLTLARANVDRQLDIIEKSDMHRKLFTNMEYNKAAVAVAQSNHQKKTEFHNKINMGGGLFLSPEDITKIASGLISPVLGEVSERAEAQRAMDEEIAERTEAYNKSLNEWETMERSIISNDAKVLTTTANRHQTEKKTSQEKIKASFDALVARMDTKVAERETLLEDTKSKEIEFKKQMQQELKDEKARLDQDLEEWGKKCEQDITEARKEQEELLKPYHDDLANAEAEHKTLVEERDXINAEISRLQDAIVDHKRKISGYGNDLDAQKNRNIREDDKLLELGQTKESLESHLNDDVIILANKAKEQAELSTKEARLKQLEVDSLINERKSELNATXIELKKEKLXLLEAMKDVASARGDDKIDEEKVKKLIGMTSEEYLTQNKSVEKNVEDLPTQLEXIEEGDELKKEEIVGAETKNSGGDGVPVSTAAKEATETSSAVQTKEPEEKISIGNKSSGKEDANDCKSAEHSKEISVSQKAGNNKSLGVSPDSLEHTFSGFSQGSSIEDDQDAISNQEKK", "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": "MNHCQLPVVIDNGSGMIKAGVAGCREPQFIYPNIIGRAKGQSRAAQGGLELCVGDQAQDWRSSLFISYPVERGLITSWEDMEIMWKHIYDYNLKLKPCDGPVLITEPALNPLANRQQITEMFFEHLGVPAFYMSIQAVLALFAAGFTTGLVLNSGAGVTQSVPIFEGYCLPHGVQQLDLAGLDLTNYLMVLMKNHGIMLLSASDRKIVEDIKESFCYVAMNYEEEMAKKPDCLEKVYQLPDGKVIQLHDQLFSCPEALFSPCHMNLEAPGIDKICFSSIMKCDTGLRNSFFSNIILAGGSTSFPGLDKRLVKDIAKVAPANTAVQVIAPPERKISVWMGGSILASLSAFQDMWITAAEFKEVGPNIVHQRCF", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm Nucleus. SIMILARITY: Belongs to the actin family."}
+{"protein": "MQQNTSLYDSLNVTAAASTSEIKKAYRNAALKYHPDKNNHTEESKRKFQEICQAYEILKDNRLRALYDQYGTTDEVLIQEQQAQAQRQQAGPFSSSSNFDTEAMSFPDLSPGDLFAQFFNSSATPSSNGSKSSFNFSFNNSSTPSFSFVNGSGVNNLYSSSAKYNSNDEDHHLDRGPDIKHNLKCTLKELYMGKTAKLGLNRTRICSVCDGHGGLKKCTCKTCKGQGIQTQTRRMGPLVQSWSQTCADCGGAGVFVKNKDICQQCQGLGFIKERKILQVTVQPGSCHNQLIVLTGEGDEVISTKGGGHEKVIPGDVVITILRLKDPNFQVINYSNLICKKCKIDFMTSLCGGVVYIEGHPSGKLIKLDIIPGEILKPGCFKTVEDMGMPKFINGVRSGFGHLYVKFDVTYPERLEPENAKKIQNILANDKYIKAERSTMETADSDCYCDLEKSYDSVEEHVLSSFEAPNLNNEVIEDDDLGDLINERDSRKRNNRRFDESNINNNNETKRNKYSSPVSGFYDHDINGY", "text": "FUNCTION: Putative chaperone involved in protein folding. Interferes with propagation of [PSI+] prion when overproduced. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
+{"protein": "MSSLIRRVISTAKAPGAIGPYSQAVLVDRTIYISGQIGMDPSSGQLVSGGVAEEAKQALKNMGEILKAAGCDFTNVVKTTVLLADINDFNTVNEIYKQYFKSNFPARAAYQVAALPKGSRIEIEAVAIQGPLTTASL", "text": "FUNCTION: Also promotes endoribonucleolytic cleavage of some transcripts by promoting recruitment of the ribonuclease P/MRP complex (PubMed:8973653, PubMed:30930054). Acts by bridging YTHDF2 and the ribonuclease P/MRP complex (PubMed:30930054). RIDA/HRSP12 binds to N6- methyladenosine (m6A)-containing mRNAs containing a 5'-GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such transcripts lead to recruitment of the ribonuclease P/MRP complex and subsequent endoribonucleolytic cleavage (PubMed:30930054). FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'- phosphate-dependent dehydratases including L-threonine dehydratase. SUBCELLULAR LOCATION: Cytoplasm Nucleus Peroxisome Mitochondrion Note=Mostly cytoplasmic but, in less differentiated cells occasionally nuclear. SIMILARITY: Belongs to the RutC family."}
+{"protein": "QSHISKARRPYIL", "text": "FUNCTION: Smooth muscle-contracting peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotensin family."}
+{"protein": "MDSERIVFRVHNQVVSLKPEIISDQYEYKYPAITDGKKPGITLGRAPDLSTAYKSILSGMNAAKLDSDDVCSYLAAAMQLFEGVCPEDWISYGIHIATKGETITPDVLIDVTRTNVEGNWAQAGGTDMTRDPTIAEHASLVGLLLCLYRLSKIVGQNTANYKTNVADRMEQIFETAPFVKVVEHHTLMTVHKMCANWSTIPNFRFLAGTYDMFFARVEHLYSALRVGTVVTAYEDCSGLVSFTGFIKQINLSARDALLYFFHKKFEEEIKRMFEPGQETAVPHPYFIHFRALGVSGKSPYSSTAVGHHFNLIHFIGCYMGQVKSLNATVIQTCAPHEMSVLGGYLGEEFFGKGTFERRFFRDEKEMQDYADLEGARVEASLADDGTVDSDDEDFFSGETRSPEAVYSRIMMNNGRLKKSHIRRYVSVSSNHQARPNSFAEFLNKVYSESS", "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 lyssavirus nucleocapsid protein family."}
+{"protein": "MHYRFLRDSFVGRVTYHLSKHKYFAHPEEAKNYIIPEKYLADYKPTLADDTSINFEKEEIDNQGEPNSSQSSSSNNTIVDNNNNNNNDVDGDKIVVTWDGDDDPENPQNWPTLQKAFFIFQISFLTTSVYMGSAVYTPGIEELMHDFGIGRVVATLPLTLFVIGYGVGPLVFSPMSENAIFGRTSIYIITLFLFVILQIPTALVNNIAGLCILRFLGGFFASPCLATGGASVADVVKFWNLPVGLAAWSLGAVCGPSFGPFFGSILTVKASWRWTFWFMCIISGFSFVMLCFTLPETFGKTLLYRKAKRLRAITGNDRITSEGEIENSKMTSHELIIDTLWRPLEITVMEPVVLLINIYIAMVYSILYLFFEVFPIYFVGVKHFTLVELGTTYMSIVIGIVIAAFIYIPVIRQKFTKPILRQEQVFPEVFIPIAIVGGILLTSGLFIFGWSANRTTHWVGPLFGAATTASGAFLIFQTLFNFMGASFKPHYIASVFASNDLFRSVIASVFPLFGAPLFDNLATPEYPVAWGSSVLGFITLVMIAIPVLFYLNGPKLRARSKYAN", "text": "FUNCTION: Probable transporter. Confers resistance to benomyl and methotrexate. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family."}
+{"protein": "MGDLPGLVRLSIALRIQPNDGPVFFKVDGQRFGQNRTIKLLTGSSYKVEVKIKPTTLQVENISIGGVLVPLELKGKEPDGERVVYTGIYDTEGVAPTKSGERQPIQITMPFTDIGTFETVWQVKFYNYHKRDHCQWGSPFSVIEYECKPNETRSLMWVNKESFL", "text": "FUNCTION: Suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels. SIMILARITY: Belongs to the CNRIP family."}
+{"protein": "MGCDRNCGLITGAVIGAVLAVFGGILMPVGDLLIEKTIKREVVLEEGTIAFKNWVKTGTTVYRQFWIFDVQNPEEVAKNSSKIKVKQRGPYTYRVRYLAKENITQDPKDSTVSFVQPNGAIFEPSLSVGTENDNFTVLNLAVAAAPHIYTNSFVQGVLNSLIKKSKSSMFQTRSLKELLWGYKDPFLSLVPYPISTTVGVFYPYNNTVDGVYKVFNGKDNISKVAIIDTYKGKRNLSYWESYCDMINGTDAASFPPFVEKSQTLRFFSSDICRSIYAVFESEVNLKGIPVYRFVLPANAFASPLQNPDNHCFCTEKVISNNCTSYGVLDIGKCKEGKPVYISLPHFLHASPDVSEPIEGLNPNEDEHRTYLDVEPITGFTLQFAKRLQVNILVKPARKIEALKNLKRPYIVPILWLNETGTIGDEKAEMFRNQVTGKIKLLGLVEMVLLGVGVVMFVAFMISYCACRSKNGK", "text": "FUNCTION: Multifunctional glycoprotein that acts as receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor- ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (By similarity) (PubMed:8320718). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (By similarity) (PubMed:8320718). Mechanistically, binding of fatty acids activates downstream kinase LYN, which phosphorylates the palmitoyltransferase ZDHHC5 and inactivates it, resulting in the subsequent depalmitoylation of CD36 and caveolar endocytosis (By similarity). In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway (By similarity) (PubMed:16276419, PubMed:21610069). Involved in oral fat perception and preferences (By similarity) (PubMed:16276419). Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions (By similarity) (PubMed:16276419). In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract (By similarity). Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis (By similarity) (PubMed:23557700). Receptor for thrombospondins, THBS1 and THBS2, mediating their antiangiogenic effects (By similarity). As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid- beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B- dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome. Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B- dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Membrane raft Golgi apparatus Apical cell membrane Note=Upon ligand-binding, internalized through dynamin-dependent endocytosis. SIMILARITY: Belongs to the CD36 family."}
+{"protein": "MESLYRVPFLVLECPNLKLKKPPWVHMPSAMTVYALVVVSYFLITGGIIYDVIVEPPSVGSVTDEHGHQRPVAFLAYRVNGQYIMEGLASSFLFTMGGLGFIILDRSNAPNIPKLNRFLLLFIGFVCVLLSFFMARVFMRMKLPGYLMG", "text": "FUNCTION: Specific component of the STT3A-containing form 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. May be involved in N- glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1. SUBCELLULAR LOCATION: Endoplasmic reticulum Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OSTC family."}
+{"protein": "MKGPIKFNALSLQGRSVMSNQSNDTTITQRRDTMNELTEEQKLLMEMVRNLAVREIAPRAIEIDENHSFPVHARDLFADLGLLSPLVPVEYGGTGMDITTFAMVLEEIGKVCASTALMLLAQADGMLSIILDGSPALKEKYLPRFGEKSTLMTAFAATEPGAGSDLLAMKTRAVKKGDKYVINGQKCFITNGSVADILTVWAYTDPSKGAKGMSTFVVERGTPGLIYGHNEKKMGMRGCPNSELFFEDLEVPAENLVGEEGKGFAYLMGALSINRVFCASQAVGIAQGALERAMQHTREREQFGKPIAHLTPIQFMIADMATEVEAARLLVRKATTLLDAKDKRGPLIGGMAKTFASDTAMKVTTDAVQVMGGSGYMQEYQVERMMREAKLTQIYTGTNQITRMVTGRSLLFPS", "text": "FUNCTION: Mediates the conversion of cyclohex-1-ene-1-carbonyl-CoA into (E)-2-cyclohex-1,5-diene-1-carbonyl-CoA in biosynthesis of cyclohexane- 1-carboxylate, a by-product produced during fermentation of benzoate and crotonate to acetate. Also able to further convert (E)-2-cyclohex- 1,5-diene-1-carbonyl-CoA to benzoyl-CoA. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
+{"protein": "MSSEVETQQQQPDALEGKAGQEPAATVGDKKVIATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPEGVPVQGSKYAADRNHYRRYPRRRGPPRNYQQNYQNNESGEKAEENESAPEGDDSNQQRPYHRRRFPPYYSRRPYGRRPQYSNAPVQGEEAEGADSQGTDEQGRPARQNMYRGFRPRFRRGPPRQRQPREEGNEEDKENQGDETQSQPPPQRRYRRNFNYRRRRPENPKSQDGKETKAAETSAENTSTPEAEQGGAE", "text": "FUNCTION: DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing and transcription regulation (By similarity). Binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C) (By similarity). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and preventing mRNA decay (By similarity). Plays a role in the maternal-to-zygotic transition in early embryo by binding to m5C-containing maternal mRNAs and preventing their degradation (By similarity). Also promotes maternal-to-zygotic transition in oocytes and embryos by promoting translation repression; molecular mechanisms governing translation repression are unknown (By similarity). Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs (By similarity). Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs (By similarity). Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence- associated subset of cytokine mRNAs, possibly by binding to m5C- containing mRNAs (By similarity). Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection (By similarity). Also able to bind DNA and regulate transcription (PubMed:2247479). Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3') (PubMed:2247479). Promotes separation of DNA strands that contain mismatches or are modified by cisplatin (By similarity). Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair (By similarity). The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasmic granule Secreted Secreted, extracellular exosome. SIMILARITY: Belongs to the YBX1 family."}
+{"protein": "MPSLLSLVLTFLAVSSPSCCQNSDTASPKASNGASFPWNNMRLPEYITPIHYDLMIHANLSTLTFWGKTEVEITVSQPTSTIIMHSHQLQISKATLRRGAEEMLPEEPLKLMEYSAHEQVALLTAQPLLAGSVYTVIITYAANLSENFHGFYKSTYRTQEGERRILAATQFEPTAARMAFPCFDEPALKASFSIKIKRDPRHLAISNMPLVKSVTVAEGLIEDHFDITVKMSTYLVAFIISDFKSVSKMTKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLYDKEKSSASSKLGITMTVSHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVTVTHPELKVEEYFFGKCFNAMEVDALNSSHPVSTPVENPAQIREMFDEVSYEKGACILNMLRDYLSADTFKRGIVQYLQKYSYKNTKNEDLWNSMMHICPTDGTQTMDGFCSRNQHSSSTSHWRQEVIDIKSMMNTWTLQKGFPLITITVRGRNVHLKQEHYMKGSECFPETGSLWHVPLTFITSKSDSVQRFLLKTKTDVIILPEAVEWIKFNVGMNGYYIVHYGDDGWASLNGLLKEAHTTISSNDRASLINNAFQLVSIGKLSIEKALDLILYLKNETEIMPIFQGLNELIPMYKLMEKRDMVEVETQFKDFLLRLLKDLINKQTWTDEGSVSERMLRSQLLLLACVHRYQLCVQRAERYFREWKASNGNMSLPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCISQDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLKENWNKIVQKFELGSSSIAHMVMGTTNQFSTRARLEEVKGFFSSLKKNGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKERQELL", "text": "FUNCTION: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase M1 family."}
+{"protein": "MRFTFLRSTRIFLANHQNHLSSLQNIRTIPSSSSSPVAISSVSKLSASLDHLSDVKQEHGFMVKQGIYNSLFLQNKLLQAYTKIREFDDADKLFDEMPLRNIVTWNILIHGVIQRDGDTNHRAHLGFCYLSRILFTDVSLDHVSFMGLIRLCTDSTNMKAGIQLHCLMVKQGLESSCFPSTSLVHFYGKCGLIVEARRVFEAVLDRDLVLWNALVSSYVLNGMIDEAFGLLKLMGSDKNRFRGDYFTFSSLLSACRIEQGKQIHAILFKVSYQFDIPVATALLNMYAKSNHLSDARECFESMVVRNVVSWNAMIVGFAQNGEGREAMRLFGQMLLENLQPDELTFASVLSSCAKFSAIWEIKQVQAMVTKKGSADFLSVANSLISSYSRNGNLSEALLCFHSIREPDLVSWTSVIGALASHGFAEESLQMFESMLQKLQPDKITFLEVLSACSHGGLVQEGLRCFKRMTEFYKIEAEDEHYTCLIDLLGRAGFIDEASDVLNSMPTEPSTHALAAFTGGCNIHEKRESMKWGAKKLLEIEPTKPVNYSILSNAYVSEGHWNQAALLRKRERRNCYNPKTPGCSWLGDYSI", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PPR family. PCMP-E subfamily."}
+{"protein": "MSNAPEIVQRLIKMIMRAFYETRHIIFMDAILRHSALTDEQTALLMGIPIKECRFIAGKLREDRLLAIQSRTEMKEGQQRQYHTTYFYIDFCSTIDSIKWRMHQLVKTVEDRMRNDFDSKGYVCPFCNKKFSSLDVLSLVTNEGTFACNVCGTELKDDEESAEMMSSQKRLGKLMGQVNGIIDALKRVDEIVVPQNNFQSALEHAVPVSLDTQNLSQQNLSKSNSDVRLSTSSPSITVDFSADKETDEKRERNCDKQVKAAQNILPEWHATSTISGSITRAGAKDAALHSFRTETVNEVQDTKTDITSEKSALDAYYATLRAKQKEESEFMDSENVDDEEDDDFLDVTTATSLQNKSTDYGSVKRKTENLNSDSDIQNKRTKSIEENNSLPPIVSTNGITDGDTEMQESKKNVIINGFNEDDEDDEDEADFEDV", "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 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIE alpha subunit family."}
+{"protein": "MNVLLNPLNRRHRLRYDIPVMPGAFPLVGHLPAIVCDLPRLLRRAERTLGSHFWLDFGPAGHLMTCVDPHAFALLRHKDVSSALIEEIAPELLGGTLVAQDGGAHRQARDAIKAAFLPEGLTQAGIGDLFAPVIRARVQAWRDRGDVTILPETGDLMLKLIFTLMGVPAQDLPGWHRKYRQLLQLIVAPSVDLPGLPLRRGRAARDWIDAQLRQFVRDARAHAARTGLINDMVSAFDRSDDALSDDLLVANIRLLLLAGHDTTASTMAWMVIELARQPMLWDALVEEAQRVGAVPTRHADLEQCPVAEALFRETLRVHPATTLLPRRALQELQLGQRRIPAGTHLCIPLLHFSTSALLHEAPDQFRLARWLQRTEPIRPVDMLQFGTGPHVCIGYHLVWLELVQFSIALALTMHKAGVRPLLLSGVEKGRRYYPTAHPSMTIRIGFS", "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. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MATWALLLLAAMLLGNPGLVFSRLSPEYYDLARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYRTCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWRDVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPSTGPL", "text": "FUNCTION: Antimicrobial protein that kills intracellular pathogens. Active against a broad range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis. SUBCELLULAR LOCATION: Secreted. Note=Located in the cytotoxic granules of T-cells, which are released upon antigen stimulation."}
+{"protein": "MFDKKLLESSELYDKRYRNFSTLIILPLFILLVGGVIFTFFAHKELTVISTGSIEPTKIVAKIQSTNANPIIENNLKEGEAVKENSLLLKYNGTPEQTQLSELLTQKKQALDKKVQLDLLQRSLTNEKNEFPTADSFGYEKSFENYEAQVKSLEATIQKSNQAVEDQNKSTESQKQAIQNQVATLQQAIQNYSEIENAVSSGGGVSQDNPYLSQYNSYQAQQATLEADLKNQKNPDETAKQAAKSQEESLKSQFLSGLASSKDSLKSQIQSFNVQESSLTGSNAYDNSQSSQILTLKSQALSASNKEMTDLNSTLTDLETKISLQKQDDQYSQVFAEQAGVLHVLPDILGMKKIPIGTPIAEIYPLLKSETQVNLTSYIPSTQISGMKVGQKVRFTVQQNLPQPEILTGIINQIDSAPTAFKEGNAYKVSATTTINAKDLPNIRYGLQGKTVTIIGKKTYFNYFLDKIMGRGNQ", "text": "FUNCTION: Involved in the secretion of lactococcin A. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family."}
+{"protein": "MTDTHYDVVIVGAGHGGAQTAIALRQNGFAGTIAIIGAEPDLPYERPPLSKEYLAAEKGFERILIRPASFWNDRHIAMHLGCAVERVDPTQRLVFLADGRSMGYGDLVWCAGGSARRLDCTGHDLGGVHYVRTRADTDALAAELPGVSKVVIIGGGYIGLEAAAVMAKFGKNVTLIEALDRVLARVAGEPLSRFFEEKHRSRGVDVRLRTKVGCLLGQDGRVTHVELNDADPIPADLVIVGIGIIPAISPLVVAGAKASNGLLVDASGRTSIPHVYALGDCAAHVNSFAPNDIPIRLESVQNANDQAVVVARTICGTAAQYHAVPWFWSSQYDIRLQTVGLTAGYDQTFVRGDPATGSFTVVYGRDGRVIALDCVNATKDYVQGKRLVEAKALIEPGMTDPQYPLKNFMTPSPA", "text": "FUNCTION: Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. SIMILARITY: Belongs to the FAD-dependent oxidoreductase family."}
+{"protein": "MSSIVEHVVLFKLNDDDVDSGKINSMVNGINELVNLDQVLHLYCGSIHRLITTTASDFTHVLHSRYRSKEDLNAYAIHPDHVRVVKESESIREDIMAVDWIAEQAPEALAPPLGSIGKITLLKLKENVMEEAKLEIMEVMKEKFEGIDQITVGENFSPGRSKDFSIGSISYFRDLGEIEAVDDQMKLQNDKIRDYVDDTIVVEFNVPSSS", "text": "FUNCTION: Involved in defense against fungal pathogens. Possesses antifungal activity against diverse pathogenic fungi. SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
+{"protein": "MPCAMELPSTPDELAAQQADSAALKDLLKDPSRWHSIPLLNYTPLHKLKDQTLVRFRGMIQDMMDPEIYLERYEVKSADGSKRVQEGKYRDCLKIANGEVIDYNADGNVHGERRTMFVVSVPGLNDWSKEHEKLCCPQIDLASLGQSPSSAKKRTIVGEEEAMDVDVASETTFKRPCLKEIQKDSEPVGASKSSVLGSDYLINSPLPDRPSMACMVKVYEEFDTYQLNSLVDFVGFLSVDASLDAATLEIDDCENLSELQAAHPSPFLIPRLHAFGVQVLPHANPLLDKSLRQPTEICEETYPTHLAVHKDLRMLLKLCLFDDDLAAEYLLSHLISTVYSRSEMQSIGKFALNLCNLPKNCEAYATKLYQILELLLPASHYMPMTLVTLNTAAFAPKKDYETNKLVSGVLQLAPHTHLVLDETCMQQGKLEANGVHAVQHLAHLINNQELKCDFQYYQIDYQANIPVLVLSEGRSMLPSDFVLPINADSKAVELVDESLKAAHHYLQPSRLQQFRKYLTTARTSGFNVSEEHTEMIQQDFVDMRKANVKSNADDLHGLLVLSRLLGIARGKDTLDKETWQLATEFEAKRRQRIQSLPKSSAQLRN", "text": "FUNCTION: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and may act by promoting the disassembly of the MCM complex from chromatin (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MCMBP family."}
+{"protein": "MGLMWGLFSVIIASVAQLSLGFAASHLPPMTHLWDFIAALLAFGLDARILLLGLLGYLLSVFCWYKTLHKLALSKAYALLSMSYVLVWIASMVLPGWEGTFSLKALLGVACIMSGLMLIFLPMTKQRY", "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": "MEAEMLYSALALTFAIFMVYRILSNSQDKRSLTKLPPSPPGWLPVIGHAHLMKNLLHRTLYDFSQKLGPIFSIRFGSRLVVVVSSSSLVEECFTKYDIVLANRPQASVDRRSLGFSTTSVIGAPYGDHWRNLRKLCDLEVFAPTRLASFLSIRLDERDRMISALYKISSAGFAKVNLEAKIVELTFNNIMRMVAAKRYYGEEAEDDEEAKRFRDLTKEALELTSASNPGEIFPILRWLGCNGLEKKLAVHSRKTDEFMQGLLDEHRRGERQNTMVDHLLSLQESQPEYYTDEIITGLIVALIIAGTDASVVTTEWAMSLLLNHPKVLEKARKELDTLVGHERMVDEHDLPKLRYLHCIVLETLRLFPSVPTLVPHEPSEDCKIGGYNVPKGTMVLVNAWAIHRDPKVWDDPLSFKPDRFEIMEVETHKLLPFGMGRRACPGAGLAQKFVGLALGSLIQCFDWERTSPEKIDLNEGSGITLPKAKTLEAMCKPRHVMEKVLRQVSNV", "text": "FUNCTION: Involved in the biosynthesis of (+)-sesamin, a furofuran class lignan (PubMed:16785429). Functions in a dual catalytic mode (PubMed:16785429). Catalyzes the synthesis of (+)-sesamin from (+)- pinoresinol by formation of two successive methylenedioxy bridges on (+)-pinoresinol and (+)-piperitol, respectively (PubMed:16785429). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MHTGPRTMATSSVSKGCFVFKPDFKKRKVFVPIEDYFNNEELDSEDSKLRFETYSLLWQRMKSETEQLQEELNENLFDNLVDFLQKSHPEFQKNSRDWGSQMKFREIPTAALILGVNVTDHDVILRSLTETLQNNVTPYVVSLQAKDCPDVKHFLQKFTSQLMDCCVDRHSKEVTSGKALKKTNYSMDSLCSWYSAVTQKADHKVTIKKRTASGHWRSPPVVLILKSMESFTSKVLQDFITISSQHLHEFPLILIFGIATSPVIIHRLLPHSVSSLLCVELFQSLSCEQHLTVVLDKLLLTPQFPFKLSKKALQVLTNIFLYHDFSIQSFIKGIKLSLLEHFYSQPLSVLCCDLSEAKKRVNVFSVSQCENIRRLPSFRRYVENQPLGKQVALLTNETFLKEKTQSLLEDLHVYHINYFLVLRCLHNFTSSLPKYPLGRQIRELYCTCLEKKIWDSEEYKSALQLLRMLAKDELVSILQRCIEVLDSSTEKQLGNTTQKIKDFLTQFQNLDADSKEEEDACGSQPKGLQKTDLYHLQKSLLEMKELRRTKKPTKFEMLRENVMNFIDNLVRDYLLPPESQPLHEVVYFSAANTLREHLNAAPRIALHTALNNPYYYLKNEELEGCIPNTAPDICIAYKLHLECSLLINLVDWAEAFATVVTAAEKMDANSTVSEEMSEVIHARFIRAVSELELLGFIKPTKQKTDHVARLTWGGC", "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. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the ORC3 family."}
+{"protein": "MTSDEVRDGAGSPADSSKGNKCTAAGMFQAAKRSTVSAARNIPAFDDLPVPSDTANLREGANLNSTLLALLPLVGVWRGEGEGRGPNGDYHFGQQIVVSHDGGNYLNWEARSWRLNDAGEYQETSLRETGFWRFVSDPYDPTESQAIELLLAHSAGYVELFYGRPRNASSWELVTDALACSKSGVLVGGAKRLYGIVEGGDLAYVEERVDADGGLVPNLSARLYRFAG", "text": "SIMILARITY: Belongs to the nitrobindin family."}
+{"protein": "MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF", "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:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39 (PubMed:25783203). The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG (PubMed:24554770). SUBCELLULAR LOCATION: Cytoplasmic vesicle Late endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Early endosome Cytoplasmic vesicle, autophagosome Cytoplasmic vesicle, clathrin-coated vesicle. SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family."}
+{"protein": "MKKVITYGTFDLLHWGHIKLLERAKQLGDYLVVAISTDEFNLQKQKKAYHSYEHRKLILETIRYVDEVIPEKNWEQKKQDIIDHNIDVFVMGDDWEGKFDFLKDQCEVVYLPRTEGISTTKIKEEIAGL", "text": "FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to sn- glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylyltransferase family."}
+{"protein": "SAGLLTQEWSAVEDLLAQMSLPEADAQRDAEMVSTATGGGRMNQESIEPPNNLPPRERKAGCKNFYWKGFTSC", "text": "FUNCTION: Somatostatin inhibits the release of somatotropin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatostatin family."}
+{"protein": "MVDNTSIATKSALQAAFSSASSLPLLVSSPGAHGQSGGGGGMKLEAVMENLQRQQAARLALEEKLRQAEKEKDIRSMVESQIQQQALAFRHYQAAVRGAFAAGVPNSSSGHPLERRAESDIDDEDDEDDDPELDRGMDDEERDMDEDDSMNEGGGDEDLEGPLAHYPPRHAVYPGAGQSPKSTPIHLSRVQPPYPAPRQAESPSALAPQAQSQHHEWTYEEQFKQLYELDDDEKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYTLYKLVTEKGGLVEVINKKIWREITKGLNLPTSITSAAFTLRTQYMKYLYPYECEKRGLSSPGELQAAIDSNRREGRRQSYGSTLFNYSPVGTPTLLASPKLQMPHISMPTPNGGHMTQTPGIKKEDSMLSSCLTNRVGIPMSLAGHHSAAQAAAAAAVQAAALEQLREKLESGEPPEKKVMLMAEEQQRIMQHALQQNLFAMATQLPMNIKLNNRDDRQETALNLSTNGISSINMSIEINGVVYTGVLFARKPAIGFMPSSQRVHHQHSSQGKSNSPGLSSHIQPSSSASSSASSHGPATSP", "text": "FUNCTION: Transcription factor. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between nucleus and cytoplasm."}
+{"protein": "MMSTYKRATLDEEDLVDSLSESDVYPNHLQVNFRGPRNGQRCWAARTPVEKRLVVLVALLAAALVACLAVLGIQYQTRTPSVCLSEACISVTSSILSSMDPTVDPCQDFFTYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELKAKPLMELIEKLGGWNITGPWDKDNFQDTLQVVTSHYHTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGAEDTIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVIYDKEYLSKVSTLINSTDKCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENTLGFALGPMFVKATFAEDSKNIASEIILEIKKAFEESLSTLKWMDEDTRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPNALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKQQTACMVEQYGNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEQTLPTLGLTNNQLFFLSFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSISNSKEFSEHFHCPPGSPMNPHHKCEVW", "text": "FUNCTION: Converts big endothelin-1 to endothelin-1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase M13 family."}
+{"protein": "MAGVNQACIFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLQRRDEDYSLVRHMLSVGQQLLQKDAPQSIHRFGFHQPPFNSVDHLHLHCFALPYVPRWKAIKYKSLGPLGGFIEAETLLEKIRPLLSKV", "text": "FUNCTION: Possesses adenylylsulfatase activity in vitro, releasing AMP and sulfate from adenylyl sulfate. Possesses also adenosine 5'- phosphosulfate (APS) phosphorylase activity in vitro. Catalyzes the phosphorolysis of APS, leading to ADP and sulfate. SUBCELLULAR LOCATION: Peroxisome."}
+{"protein": "MNPIQSFHCKLRGLATTLDSETARLLRALDGEDSDFEDSPGRILHDLHSEVQTLKDNVNALLDEARLENQESTRFKKATKILMEKNSADVRKLREFFQKYGYQARDKEDSGCEHRVNNSTPELAVCKDIQKAGVKELSDPCVPSGSVSEEPLRSPQLSDFGLQRYIISQVPANPPQTAASLKEERVAETPPAKDPSVQVLKTPRCALRMDDFECETPKLEHFGISEHTMCLNEDYTMGLKNMKNIKSSLLSGVSGEAIGTGPVTSDNSFAIPGPIIQQMEENDVEYVSSPLPPKFCTPGLKIPSTMDRTDLVSIDYPLSKPNSSSTDLEIKDCVPLILNSDECYQSFAEPPSSAITSCENFATPSPPKVTAIPEDILQMITKHSSNLASPLDVKVMPRRKGTRGAANKENW", "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": "MRCLVVLLAVFALSQGAEITRIPLYKGKPLRKALKERGLLEDFLQKQQYGVSSEYSGFGEVASVPLTNYLDSQYFGKIYLGTPPQEFTVLFDTGSSDFWVPSIYCKSNACKNHQRFDPRKSSTFQNLGKPLSIRYGTGSMQGILGYDTVTVSNIVDIQQTVGLSTQEPGDVFTYAEFDGILGMAYPSLASEYSVPVFDNMMDRRLVAQDLFSVYMDRSGQGSMLTLGAIDPSYYTGSLHWVPVTLQKYWQFTVDSVTISGAVVACEGGCQAILDTGTSKLVGPSSDILNIQQAIGATQNQYGEFDIDCDSLSSMPTVVFEINGKMYPLTPYAYTSQEEGFCTSGFQGENHSHQWILGDVFIREYYSVFDRANNLVGLAKAI", "text": "FUNCTION: Chymosin is synthesized in the mucosa of the stomach. The enzyme hydrolyzes casein to paracasein. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MGQTGKKSEKGAVCWRKRVKSEYMRLRQLKRFRRADEVKSMFNTNRQKIMERTEILNQEWKQRRIQPVHIMTTVSSLRGTRECFVTSDLDFPKQVIPLKTLTAVASMPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALAQYSDYEDDEDGEDNQDDERDDITKDQDDNMEEKETLPLRKFPSDKIFEAISSVFPDKGTSEELKEKYKELTEQQLPGALPPECTPNIDGSNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNNEAANDGKLCGPYCYQLLEGAREFAAALTAEIIKTPPKRPSGRRRGRLPNNSSRPSTPTVNVLEAKDTDSDREAGTETGGESNDKEEEEKKDETDSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASLFRVLIGTYYDNFCAIARLISTKTCRQVYEFRVKESSIIAPVIAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSDCQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIYIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSLNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP", "text": "FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the prc2/eed-ezh2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. May regulate the circadian clock via histone methylation at the promoter of the circadian genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily."}
+{"protein": "MSVFTKSAFTMSALPSPNTSQPPSAAPSRRGSFANGLASGQLTPVTDPHIVSINVESVLFDMDGTLINSSPAVVKAWELFAEKYPLDLDDILRSAHGMRTIDVLKKWCKITDPELLASEVIRFETAILNSAEDIAKHSGKAGIEVLPGVAKLLADLGEEADKRDGEEKWAICTSSTYFYAGKAIPIAGLPTPKVFVTADSVTRGKPFPDPYLLGASGCNASPFESLVVEDAPTGIRSGKASGALVLATCTSHEREELERERPDFLVDDLSHVKASWDAATNTFNLIIEQPIDRYTPRPTPDVTPVITPAMSRSNSFSGVGQDRPSVRNTQTIMKGSDDLTGNDSVVGSPAASRPGSPGADDSVEKRAEMEFHRRASQSGQAGVTLDAFRRALAGNAAKRRAQSQGEMSQDE", "text": "FUNCTION: Probable phosphatase (Probable). Required for cell wall integrity and virulence (PubMed:29233914). SIMILARITY: Belongs to the HAD-like hydrolase superfamily."}
+{"protein": "MDQEIEIPSFFLCPISLDIMKDPVIVSTGITYDRESIEKWLFSGKKNSCPVTKQVITETDLTPNHTLRRLIQSWCTLNASYGIERIPTPKPPICKSEIEKLIKESSSSHLNQVKCLKRLRQIVSENTTNKRCLEAAEVPEFLANIVSNSVDTYNSPSSSLSSSNLNDMCQSNMLENRFDSSRSLMDEALSVLYHLDTSETALKSLLNNKKGTNLVKTLTKIMQRGIYESRAYAALLLKKLLEVADPMQIILLERELFGEVIQILHDQISHKATRSAMQILVITCPWGRNRHKAVEGGTISMIIELLMDDTFSSERRNSEMAMVVLDMLCQCAEGRAEFLNHGAAIAVVSKKILRVSQITSERAVRVLLSVGRFCATPSLLQEMLQLGVVAKLCLVLQVSCGNKTKEKAKELLKLHARVWRESPCVPRNLYDSYPA", "text": "FUNCTION: E3 ubiquitin-protein ligase that negatively regulates water stress response. May control in coordination with PUB23 a drought signaling pathway by ubiquitinating cytosolic RPN12a. Acts as negative regulator of the immunity triggered by the pathogen-associated molecular patterns (PAMPs), in association with PUB23 and PUB24. Regulates EXO70B2 ubiquitination and degradation via the 26S proteasome to attenuate PAMP-induced signaling (PubMed:23170036). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MHRPNFRPPTPPYPSPGIGGWGGGNNFRGALGGGPRPPSPRDGYGSPHHTPPCGPRARPYGSSQSPRHGGNFSGARFGSPSPGGYPGSYSRSPAGSQHQFGYSPGQQQTYPQGSPRTSTPFGSGRGREKRMSNELESYFKPSMLEDPWAGLEPVSVVDISQQYSNTQTFTGKKGRYFS", "text": "FUNCTION: May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=The subcellular location is regulated during cell cycle. During interphase located in the nucleus. During mitosis located at the centrosome and dispersed in the cytoplasm. During telophase located in the midbody. Colocalizes with PLK1 at the centrosome in M phase."}
+{"protein": "MFRRPVLQVFRQFVRQESEVASSLVLERSLNRVQLLGRVGQDPVMRQVEGKNPVTIFSLATNEMWRSGDNEAYQMGDVSQKTTWHRISVFRPGLRDVAYQYVKKGARIFVEGKVDYGEYMDKNNVRRQATTIIADNIIFLSDQAREKPLNG", "text": "FUNCTION: Binds preferentially and cooperatively to pyrimidine rich single-stranded DNA (ss-DNA). In vitro, required to maintain the copy number of mitochondrial DNA (mtDNA) and plays a crucial role during mtDNA replication by stimulating the activity of the replisome components POLG and TWNK at the replication fork. Promotes the activity of the gamma complex polymerase POLG, largely by organizing the template DNA and eliminating secondary structures to favor ss-DNA conformations that facilitate POLG activity. In addition it is able to promote the 5'-3' unwinding activity of the mtDNA helicase TWNK. May also function in mtDNA repair. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion matrix, mitochondrion nucleoid."}
+{"protein": "MTNILIVEDEQNLARFIELELTHENYTVDIENDGKAGLDKALSKPYDLYILDLMLPNINGLEICRQIRQKTTTPIIIITAKSETYDKVAGLDYGADDYIVKPFDIEELLARIRAVLRRQPDKDVLDINGIIIDKDAFKVTVNGHQLELTKTEYDLLYVLAENRNHVMQREQILDHVWGYNSEVETNVVDVYIRYLRNKLKPFNKEKSIETVRGVGYVIR", "text": "FUNCTION: Member of the two-component regulatory system ArlS/ArlR. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGTDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQYATTYINIVGKLFNECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNPRVVKAMLANMRDELSDALKR", "text": "FUNCTION: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure (PubMed:32871103). Involved in 30S ribosomal subunit biogenesis; thought to be required for loop formation between NusB/NusE (rpsJ, ribosomal protein S10) bound to boxA upstream of the rRNA operons and the elongating RNAP complex. This would promote correct co- transcriptional folding of rRNA. Plays a role in transcription antitermination in a plasmid context in vivo (PubMed:26980831). Required for rrn transcription antitermination; required for integration of NusB/NusE into the antitermination complex (PubMed:31020314). The Nus factor complex (NusA, NusB, NusE (rpsJ), NusG and SuhB) represses expression of suhB and possibly other genes via boxA; the Nus complex prevents or promotes Rho-mediated transcription termination depending on gene context (PubMed:29229908). Involved in post-transcriptional control of gene expression (Probable). Enzymatic activity is not required for complementation of the cold- sensitive phenotype of the dnaB121 mutation (PubMed:10747806) (Probable). FUNCTION: Has D,L-inositol-1-monophosphatase and beta- glycerophosphatase activity, has less to no activity against a number of other substrates (PubMed:8002619). 2.5-fold more active on 1D- inositol-1-monophosphate than L-inositol-1-monophosphate (1D-myo- inositol 3-phosphate). Specific activity increases significantly upon heating. Only beta-glycerophosphate and adenosine 2'-monophosphate are alternative substrates (PubMed:10747806). FUNCTION: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure. IMPase activity is not required for its Nus factor function. FUNCTION: Required for growth at low temperatures (PubMed:2138605, PubMed:6389495, PubMed:1847383, PubMed:8002619, PubMed:8589060, PubMed:17652087, PubMed:26980831). Identified as a suppressor (ssyA3) of a temperature-sensitive, protein export missense mutation of secY (secY24), allows growth at 42 but not 30 degrees Celsius (PubMed:6389495). Identified as a suppressor (suhB2) of an rpoH missense mutation (rpoH15), allowing growth at 37 and 40 but not 25, 30 or 34 degrees Celsius, increases expression of RpoH (PubMed:2138605). Identified as a suppressor of a dnaB helicase missense mutation (dnaB121), restores growth at 42 but not 30 degrees Celsius (PubMed:1847383). In both suhB2 and ssyA3 there is an insertion in the 5' region of the gene which prevents SuhB protein expression (PubMed:8002619, PubMed:8589060). Missense mutant suhB10 is suppressed by mutations in RNase III (rnc), showing genetic interaction between them (PubMed:8589060). Deletion of suhB is suppressed by mutations in RNase III, by a mutation in nusA or deletion of nusB, indicating that in the absence of SuhB the Nus complex inhibits growth (PubMed:26980831). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
+{"protein": "MTAEPATKKIKLELSDPSEPLTQSDVIAFQKEALFRCINRRRVDFEALRKQYELSRRECIDVSRKLANIMALIVTLARFIETFCTDANEKQLCREIAQGDETLIVQRSDSFMKLLTKYGKPNTTDSNTNSNASDHIQELTTELKNLRKSKEELFYENSQLTEEISALKEYYTNIIRKYDRDESFTIKRVFKEDKTDAVKELREDEKESNENNIKSGNKDSSAINGDNTSKKSEKGDELVQAEDERKEDAENEKLELDLKFSDLRAEINSLSSTIKDLENIRRENEEELIKTRSEVSNLKKQQIAAADQDPDFKSYDHESLLAKIQHLTEQNAELSEINSSFLSKFQVLAKEKEIYTKKVREEFQKSLDSLVEMNSSLEKDVVRIRTARDDLLSKIAILEAEKSKTEVLSDLQHAIDILKEQWTKIDQRSNDTKSSSTQDALIKEIQDLEKGFRELSDLTHKKYSEIINHESVISKLTVEKTKADQKYFAAMRSKDSILIEIKTLSKSLSKSNELILQLKDSDRLLQQKIGNLHKQLDLSQNNERRLIDSSKTETLKIIDLNNTSTKLKRSLEKLQEESNKSIADMTHLETKLNDTEIELKHFKQKASHLESKCEKLHDTLFRGNNKNKGSSDEALVEELANFRTLVYCSLCSKNWKNMAIKTCGHVFCENCCKERLAARMRKCPTCNKAFSSNDLLTVHL", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Also modulates the formation of double-strand breaks during meiosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BRE1 family."}
+{"protein": "MEIKTRRDTSETSVRKDDEEEVEEEQPLSPAARVFHAPEFNCYVISVIGIKKKIDPDVIIEGLKQTLIRHPRFSSKMVSTSVGNKKRQTQSWVRTNVVVTDHVIVSDIQTQNIENGNADAFLETYVSNLTTVPLDISKPLWQLHLLDLKTSDAENVAVLKFHHSLGDGMSLMALVLACMRKTSNPDELPSLPNQNRSSSRSSRLMAGSRGDSRFLWLVMVIWSAIMLVLNTVCDALEFIATTMFLKDTETPIKGDFRFSKSKRMCLVHRTVSLDDIKLIKNTMKMTVNDVVLGVSQAGLSQYLDRRYGEKKKKVGEDQDSKRKATDMPKRIRLRSALLVNLRPNTGIQDLADMMAKGSTCRWGNWIGYIVFPFSIGLRDDPLQHLRRAKRIIDRKKNSLEAALTFVAGKFILKTFGVQVAAKIINRALSNTTMSFSNLIGPIEEISFYGHPITYMAPSVYGHPHALTMHFQSYMNQMTISLTVDPTVISDPHRLLDDWEKSLQSIKAAVQERDSRSLD", "text": "FUNCTION: Bifunctional wax ester synthase/diacylglycerol acyltransferase that uses acyl-CoAs with 16, 18 and 20 carbons as substrates, preferably in combination with 16:0ol alcohol (PubMed:30729606). Involved in cuticular wax biosynthesis (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Endoplasmic reticulum membrane; Single-pass membrane protein Golgi apparatus membrane; Single-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the long-chain O- acyltransferase family."}
+{"protein": "MAEHVVYVGNKPVMNYVLATLTQLNEGADEVVIKARGRAISRAVDVAEIVRNRFMPGVKVKEIKIDTEELESEQGRRSNVSTIEIVLAK", "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": "MADKEATVYIVDVGRSMGECRNGRSVTDLEWAMQYVWDRITGTVATGRKTATMGVIGLRTDETSNELEDDVHFSHIAVLSNIKQFLMPDIRKLEDELKPSKTDKGDAISAIILAIQMIITHCKKLKYRRKIALVTNGQGRMSDEDLGEIVKKVKEDNIELVVMGIDFDDPEYGYKEEDKDPRKAENETLLRTLVEDCDGVYGTFEQAVAELDIPRVKSVRSVASFKGYLQLGNPEDYDSALRIPVERYYRTYPAKPPTASSFVLRSEPEAGQEEAESSEAAAATQKGSQSGDIGLTTVRTMRTYQVEDKSAPGGKIDIERDDLAKGYEYGRTAVHISETDENITILDTFAGLELMGFIQTDRYQRYMHMSNTNIIIAQRANDKAALALSSFIHALFELECYAVARLVVKENKPPVIVLLAPSIEPDYECLLEVQLPFAEDVRTYRFPPLDKVITVSGKVVTQHRNLPNDDLLDVMGKYVNSMELVDADEDGDPVETFPIDDSYSPVLHRIDAAIRARAIHPDQPIPPPSERLTKFSHPREDLIERSQKYLEKLIEIADVKKVPPKAKGRKRTRETEKPLSGLDVDALLHHEKRAKISPNNAIPEFKQTLAQAENIEAIKDATKQMMVIVEDQIKHSLGNANYDRVIEALGTMRDELVSYEEPASYNDFLGQLKDKLLQEKLGGDRQELWWLVRRNKLGLVTQRESDQSRVTDTEAKEVSLTKMKE", "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": "MAGLSNSQIPDGEFTAVVYRLIRDSRYSEAVQLLSAELQRSSRSRAGLSLLAYCYYRLQEFELAAECYEQLSQMHPELEQYRLYQAQALYKACLYPEATRVAFLLDNPTFYSRVLRLQAAIKYSEGDLPGARSLVEQLLSGEAGEDSGGENDPDGLVNMGCLLYKEGHYEAACSKFFAALQASGYQPDVSYNLALACYSNRHYAPALKHIANIIERGIRQHPELGVGMTTEGIDVRSVGNTVVLHQTALVEAFNLKAAIEYQLRNYEAAQEALTDMPPRAEEELDPVTLHNQALMNMDAKPTEGFEKLQFLLQQNPFPPETFGNLLLLYCKYEYFDLAADVLAENAHLTYKFLTPYLYDFLDAMITCQTAPEEAFIKLDGLAGMLTEQLRRLTKQVQEARHNRDDEVVIKAVNEYDETLEKYIPVLMAQAKIYWNLENYPMVEKIFRKSVEFCNDHDVWKLNVAHVLFMQENKYKEAIGFYEPIVKKNYDNILSVSAIVLANLCVSYIMTSQNEEAEELMRKIEKEEEQLSYGDPDKKIYHLCIVNLVIGTLYCAKGNYDFGISRVIKSLEPYHKKLGTDTWYYAKRCFLSLLENMSKHTIMLRDSVIQECVQFLEHCEIFGRNIPAVIEQPLEEERMHIGKNTVTYESRQLKALIYEIIGWNM", "text": "FUNCTION: Required for polyglutamylation of axonemal tubulin. 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": "MEKSNRSLKDLDLNALFIGDKAENGQLYKDLLNKLVDEHLGWRKNYIPSDPNMIGPEDQNSPAFKKTVGHMKTVLDQLSERIRTESVPWHSAGRYWGHMNSETLMPALLAYNYAMLWNGNNVAYESSPATSQMEEEVGQEFARLMGYDYGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVNPELVAGKSDWELLNMPTKEIMDLLENAGSQIDEVKKRSARSGKNLQRLGKWLVPQTKHYSWMKAADIIGIGLDQVVPVPIDSNYRMDIQALESIIRKYAAEKTPILGVVGVAGSTEEGAVDGIDKIVALRQKLQKEGIYFYLHVDAAYGGYARALFLDEDDQFIPYKNLQKVHAENHVFTEDKEYIKPEVYAAYKAFDQAESITIDPHKMGYVPYSAGGIVIQDIRMRDTISYFATYVFEKGADIPALLGAYILEGSKAGATAASVWAAHHTLPLNVTGYGKLEGASIEGAHRYYDFLKNLKFEVAGKRISVHPLISPDFNMVDYVLKEDGNDDLIEMNRLNHAFYEQASYVKGSLYGKEYIVSHTDFAIPDYGDSPLAFVESLGFSEVEWRHAGKVTIIRASVMTPYMNQRENFDYFAPRIKKAIQADLEKVYASVNQKENV", "text": "FUNCTION: Is also able to decarboxylate the Parkinson's disease medication levodopa (L-dopa) to dopamine in vitro. FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:24211777, PubMed:27292129). Cannot use other aromatic L-amino acids as substrates like L-phenylalanine, L-tryptophan and L- glutamate (PubMed:24211777). SIMILARITY: Belongs to the group II decarboxylase family. Tyrosine decarboxylase subfamily."}
+{"protein": "MNGRVQPRLMLGFLLILLVILALGSANMGALSLSFRTLWNTSTNDAMWHIWLNIRLPRVLLAVVVGCALAVSGTIMQGLFRNPLADPGLLGISSGAALCVGLIIVMPFSLPPLLALYSHMVGAFIGSLAISTIIFTLSRWGHGNLARLLLAGIAINALCGAAVGVLTYISDDQQLRQFSLWSMGSLGQAQWSTLLVASSLILPTCILGLLQARQLNLLQLGDEEAHYLGVNVRQAKLRLLLLSAILIGAAVAVSGVIGFIGLVVPHLIRMRIGADHRWLLPGAALGGACLLLTADTLARTLVAPAEMPVGLLTSLLGGPYFLWLILRQREQRSG", "text": "FUNCTION: Part of the binding-protein-dependent transport system for hemin; 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. FecCD subfamily."}
+{"protein": "MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQIMTAK", "text": "FUNCTION: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin- dependent protein kinase type II (CaMK2), and phosphatases. SIMILARITY: Belongs to the calmodulin family."}
+{"protein": "MNYRRNICLRIGWMLLFAFIPAYAGHSAEEWKRRSIYQIITDRFSLEEGATERIPCDPVRFMYCGGTWNGIRNHLDYIQGMGFDAIWISPIFENVEGNDIDGSSYHGYWTTNLYELNHHFGTKEEFMELIQELHKRDIWILLDVAINSMAINGPLEQMSFEKVIPFNDASFFHPHCWVDYESNDIESVQNCWLGDENLLLADVDTENEVVLSVLEKWIKNVVQEYDIDGIRFDAIKHAPIEFWLRMSKAADIFTIGEYFTGSPAEACDYQNSGLDSFLNFPLYWPITWAFNNTGLQCEALAIAINQINEECNDINVLGTFIGNHDLPRISHNNTDQARIMNAITFVMMWDGIPIIYYGTEQNFNSYHDPFNREALWLSNFDMENVYYKLIGILNRFRKSVQRQEENYVNTRSTILSVKIHHIVVQKLNVITVLNNYGIHNEERLSIVFKPLGASPKDTFFDIINNQKYVVNTDGTLKVVITNGFPIVLYPTSKIETSLPQFTATLLPEITFVPSITVTTHYVLPTLLAPLGYDIREHPGGQQFWNTLTAKSEAKTIRSFTKLKLFILLIAVPFALPMIILI", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MVRVEKIKTKKGKRVLVNRASKTVENDKKALFCRGAKTNEIISHAMMDLFDMKKPLTTKMDKHNPYHLFEDETPIVRAGSKFDTSLFVLGSNSKKKPNCLTFGRTYDGQLLDMAELRITSYKSSSNFEAAKMTLGSKPCVILEGAAFESDGDMKRIGNLMVDWFRGPKVDTVRLEGLETVIVFTALDETNLALRVYRPMLKKSATATPRVELAEMGPSISFEVMRKKLADDALFKLACKKPKALMKKRRKNLSEDVFGNQLARVHVGKQRTDDIQTRKVKALRKTPLVEAAPENAIE", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RPF2 family."}
+{"protein": "MEKIKKQNNIGSYSSDKDGEYKKFRFSKTSIRGFLLKEYEREVPIIVKIQSYRNKFLDFYFKMASILGEEVFFILALPISTWCVATQLGVELCVVLALTIGGGNILKNTFTLPRPPPNIVWTNTAHQKDHGLPSTHTASAFGLTFYFLIYTYFLFPTIGESFNISLLSMFFIVLFWSTSVMFSRLYNGHHTPMDVIAGLIVAITSILATTYQLRYFIEGMVLSETFLFGPMLYIAILSAILFFHPQANTGPTPAYPETGLVCGASLGSLISLWLHAQHPCPLMNQELLLLEANYDSIVSTIHSIPLLLHGSRILIGLVLVGIAKVFSKKFFFFAYDLVIRANTNNEQSQPITTVSFDPNKKIIVTPTIEAFSKLFVYTCVSFTIVSMPYLFYYLNIQTSADVTRYY", "text": "FUNCTION: Has enzymatic activity against both sphingosine 1 phosphate (S1P) and dihydro-S1P. Regulates intracellular and extracellular S1P levels (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family."}
+{"protein": "MGPCSGSRLGPPEAESPSQPPKRRKKRYLRHDKPPYTYLAMIALVIQAAPSRRLKLAQIIRQVQAVFPFFREDYEGWKDSIRHNLSSNRCFRKVPKDPAKPQAKGNFWAVDVSLIPAEALRLQNTALCRRWQNGGARGAFAKDLGPYVLHGRPYRPPSPPPPPSEGFSIKSLLGGSGEGAPWPGLAPQSSPVPAGTGNSGEEAVPTPPLPSSERPLWPLCPLPGPTRVEGETVQGGAIGPSTLSPEPRAWPLHLLQGTAVPGGRSSGGHRASLWGQLPTSYLPIYTPNVVMPLAPPPTSCPQCPSTSPAYWGVAPETRGPPGLLCDLDALFQGVPPNKSIYDVWVSHPRDLAAPGPGWLLSWCSL", "text": "FUNCTION: Transcriptional activator. Recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. Required for induction of the goosecoid (GSC) promoter by TGF-beta or activin signaling. Forms a transcriptionally active complex containing FOXH1/SMAD2/SMAD4 on a site on the GSC promoter called TARE (TGF-beta/activin response element). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MDRFVWTSGLLEINETLVIQQRGVRVYDGEEKIKFDAGTLLLSTHRLIWRDQKNNECCMAIPLSQIVFIEEQAAGIGKSAKIVVHLHPAPSNKEPGPFQSSKNSYIRLSFKEHGQIEFYRRLSEEMTQRRWETVPVSQSLQTNKGPQPGRVRAVGIVGIERKLEEKRKETDKNISEAFEDLSKLMIKAKEMVELSKSIANKIKEKQGDVTEDETIRFKSYLLSMGIANPVTRETYGSGTQYHMQLAKQLAGILQAPLEERGGIMSLTEVYCLVNRARGMELLSPEDLVNACKMLEALKLPIRLRVFDSGVMVIELQTHKEEEMVASALETVSERGSLTSEEFAKLVGMSVLLAKERLLLAEKMGHLCRDDSVEGLRFYPNLFMTQN", "text": "FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3. SUBCELLULAR LOCATION: Cytoplasm Endosome Late endosome Membrane Nucleus Note=Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membrane to participate in vesicle formation. SIMILARITY: Belongs to the VPS36 family."}
+{"protein": "MEEHDYDSNSNPPLMSTYKHLFVEQHRLDMDMGAIDVDECELPVIDLAGLMEAEQVCRADMVRAASEWGFFQVTNHGVPQALLRELHDAQVAVFRRPFQEKVTERLLGFSPESYRWGTPTAKCLEQLSWSEAYHIPMTTPRPSTSIRARAVIEEVSRAMYELAQKLAEILMRGLPGAGEGETMVTTREETCFLRLNRYPPCAMAMGGFGLCPHTDSDLLTIVHQQQDTVGGLQLLKGGRWVAVKPSPSTLIVNVGDLLQAWSNDVYKSVEHRVMANATLERFSMAFFLCPSYHTLIIPSSSHVHDDDAHYRSFTFGEYRKQIMEDVRSTGRKIGLHRFRTR", "text": "FUNCTION: Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins (GAs), leading to the homeostatic regulation of their endogenous level (PubMed:18952778, PubMed:24475234). Catabolism of GAs plays a central role in plant development (PubMed:18952778, PubMed:24475234). In vitro, converts GA12 and GA53 to the corresponding 2-beta-hydroxylated products GA110 and GA97, respectively (PubMed:18952778). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family. GA2OX subfamily."}
+{"protein": "MAHTVKIYDTCIGCTQCVRACPTDVLEMVPWDGCRANQIASAPRTEDCVGCKRCESACPTDFLSIRVYLGAETTRSMGLGY", "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 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, cyanelle thylakoid membrane; Peripheral membrane protein; Stromal side."}
+{"protein": "MKKPDIQQLKDIVNNSNQIVFFTGAGVSVASGIPDFRSMGGLYDEISKDGQSPEYLLSIDHLHDNKESFINFYHERLLIADKKPNIVHQWIAQLENQQKSLGVITQNIDGLHEDAGSHNIDELHGTLNRFYCINCYEEYSKSYFMTHHLKYCEKCGNVIRPDIVLYGEMLNQKTVFKALDKIQHADTLIVLGSSLVVQPAAGFVSEFKGDNLVIINRDATPYDHTASLVIHDDMTSVIEEIVNSNS", "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": "MENGAVYSPTTEEDPGPARGPRSGLAAYFFMGRLPLLRRVLKGLQLLLSLLAFICEEVVSQCTLCGGLYFFEFVSCSAFLLSLLILIVYCTPFYERVDTTKVKSSDFYITLGTGCVFLLASIIFVSTHDRTSAEIAAIVFGFIASFMFLLDFITMLYEKRQESQLRKPENTTRAEALTEPLNA", "text": "FUNCTION: Master regulator of recycling and plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Associates with both constitutive and IFNG-induced PD-L1/CD274 at recycling endosomes, where it protects PD-L1/CD274 from being targeted for lysosomal degradation, likely by preventing its STUB1-mediated ubiquitination. May stabilize PD-L1/CD274 expression on antigen presenting cells and potentiates inhibitory signaling by PDCD1/CD279, its receptor on T-cells, ultimately triggering T-cell anergy. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Note=Co-localizes with PD-L1/CD274 in the plasma membrane and in recycling endosomes. SIMILARITY: Belongs to the chemokine-like factor family."}
+{"protein": "MPAQRMRSVIPPYMLRALLTRYAPQRDCALHTLNHVQSLLGNKPLRSPTEKNARAGERSAISTTPERHPTARQTGAQGGAAQQPRRAVDEAYDHLGVTYDFFWQAYRRNSVDNKGLPLVQRALRQGLPEQLSGTASRWCSETATARSSTVSPSPSTLVGHELTHGSDRERSRLIYYQQSGALNESLSDVFGSLVKQFHLQQTADKADWLIGAGLLAKGIKGKGLRSMSAPGTAYDDPLLGKDPQPASMKDYIQTKEDNGGVHLNSGIPNRAFYLAATVLGGFAGKKPVTSGMTRCATKRCRKTPTSDHLRPRHGETRAGLRTKRGDKVQQAWASGWQWSNETAADAQSGYGH", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M4 family."}
+{"protein": "MAACRALKAVLVDLSGTLHIEDAAVPGAQEALKRLRGTSVIVRFVTNTTKESKQDLLERLRKLEFDISEDEIFTSLTAARSLLEQKQVRPMLLVDDRALPDFKGIQTTDPNAVVMGLAPEHFHYQILNQAFRLLLDGAPLIAIHKARYYKRKDGLALGPGPFVTALEYATDTKATVVGKPEKTFFLEALRGTGCEPEEAVMIGDDCRDDVGGAQDVGMLGILVKTGKYRASDEEKINPPPYLTCESFPHAVDHILQHLL", "text": "SIMILARITY: Belongs to the HAD-like hydrolase superfamily."}
+{"protein": "MALNFNAIASKSQKLPCFALPPKATLRSPKFSMISTIPSGSKEVGNLKKPFTPPKEVPVQITHSMPPHKIEIFKSLEGWAENNILTHLKPVEKCWQPADFLPDPNSDGFHEQVKELRERAKEIPDDYFVVLVGDMITEEALSTYQTMLNTLDGTRDETGASLTPWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIERTIQYLIGSGMDPHTENSPYRGFIYTSFQERATFISHGNTGRLAKEYGDINLAQICGSIASDEKRHETAYTKIVEKLFEIDPDETVLAFADMMKKKIAMPAEFIYDGRDYNLFDHYSAVAQRIGVYTAKDYVDIVEHLVDRWKVKELAGLSAEGRKAQDYLCSLPSRIRRLEERAQEKAQGSTPVSPFSWIFDREVKL", "text": "FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 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": "MLPLPSLRRSLLSHAWRGAGLRWKHTSSLKVTNEPILAFSQGSPERDALQKALKDLKGQMEAIPCVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKAFARIKKWLEHARSSPSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKYRETLQLVDSTTSYGLTGAVFAQDKAIVQEATRMLRNAAGNFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWRYSYMQ", "text": "FUNCTION: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma- semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
+{"protein": "MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPVGDDEFIPEDVLNFDDLTADTLSALKVSQIKKVRLLIDEAIQKCDGERLKLEAERFENLREIGNLLHPSVPISNDEDADNKVERIWGDCTVRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYTPIYTPFFMRKEVMQEVAQLSQFDEELYKVIGKGSEKSDDSSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMIGTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKGIIVPEKLREFMPPGLQELIPFVKPAPIDQEPSKKQKKQHEGSKKKAKEVTLESQLQNMEVTEA", "text": "FUNCTION: Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). Is probably 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). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC. Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). Thereby, inhibits the production of VEGFA and sprouting angiogenesis mediated by VEGFA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic, but a minor proportion is also found in the nucleus. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily."}
+{"protein": "MPLISIQNAFLAFSDLEILKNAVLYINKKERISLIGKNGAGKSTLLKVINKNQELDHGSIIYQKNIKISYLKQDNPKNLDISIYDFIKNQLKKENNKEININTIVEIKKIIKTFQIDKHSLLSELSGGSLRKVVLGSALLSQPDVLLLDEPTNHLDINTIAWLEKFLKKFSGTTLFISHDRSFIQNLCTRIIDLDRGKLTSFPGDYKEFIKLKKENNRIEKTKKKLFDQHLEKEEIWIRKGIKARTTRNEGRVRNLKVLRKEYKNYKKIENFNNVIINEIKNYSGKIIFKLKNISFFIEKKTIIQSFSSIIQYGDKIGLIGNNGSGKSTMIKILMGEKKIQKGSIHFGTKLNIAYFDQDRSTLDSNKSILENVNNGREKIVLNGKEQHLIGYLKKFLFKPNQMKCLVKNLSGGECNRLLLAKLFLKPSNVLILDEPTNDLDLDTLELLENIIIKYSGTVLIVSHDRNFIENTVNKYWIFKGDGLINTHFSSHNNIIKEKNKKIQKKYVLNPIKSNISFLKTKQNQVKKELKKVLNEIEKIENSIKTLKIQMNEPDFFKQHIKNQLPIVKQFNIEEKKLEKILIYWENLEKKL", "text": "FUNCTION: Probably plays a role in ribosome assembly or function. May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds DNA and has ATPase activity. SUBCELLULAR LOCATION: Cytoplasm Note=Associates with ribosomes. SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. Uup subfamily."}
+{"protein": "MADRDRPHPHQIQVHPQHPHRYEGGVKSLLPQKGPSTTQILAIITLLPISGTLLCLAGITLVGTLIGLAVATPVFVIFSPVLVPAAILIAGAVTAFLTSGAFGLTGLSSLSWVLNSFRRATGQGPLEYAKRGVQEGTLYVGEKTKQAGEAIKSTAKEGGREGTART", "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": "MAAPKLESFRRGSMFDGSFRRGSMFDGSFRQSMRDRLILQSRGYSNVNDDDKTSVRCCSYSYFSDKITGVVKKLKDVLVTAWEMGTADPRKMIFSAKMGLALTLTSILIFFKIPGLELSGHYLWAILTVVVIFEFSIGATFSKGCNRGLGTLSAGGLALGMSWISEMTGNWADVFNAASIFVVAFFATYAKLYPTMKPYEYGFRVFLLTYCYVIVSGYKTGEFMETAVSRFLLIALGASVGLIVNTCIYPIWAGEDLHNLVAKNFVNVATSLEGCVNGYLECVAYDTIPSRILVYEAVAEDPVYSGYRSAVQSTSQEDTLMSFASWEPPHGPYKSFRYPWALYVKVGGALRHCAIMVMALHGCILSEIQAAEDRRREFRNELQRVGIEGAKVLRYIGESLKKMEKLNPIEDILYEIHQAAEELQSKIDKKSYLLVNAKNWEIGNRPRVRDLTDEQKISNLDSDLSRILAHKSQSEATLRPPKNWDDVTTAANLSSATMLPYLQSRTMIHKQPSWPSRISITPGSMLQPPLGEPGKMYESASNLSLATFASLLIEFVARLENLVNAYDELSVKANFKEAVSE", "text": "FUNCTION: Malate transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic acid exporter (TC 2.A.85) family."}
+{"protein": "MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIPADNPEVVVSLAWDESLAPKHPGSRKNVACYCRIPACLAGERRYGTCIYQGRLWAFCC", "text": "FUNCTION: Effector molecule of the innate immune system that acts via antibiotic-like properties against a broad array of infectious agents including bacteria, fungi, and viruses or by promoting the activation and maturation of some APCs. Interacts with the essential precursor of cell wall synthesis lipid II to inhibit bacterial cell wall synthesis. Inhibits adenovirus infection via inhibition of viral disassembly at the vertex region, thereby restricting the release of internal capsid protein pVI, which is required for endosomal membrane penetration during cell entry. In addition, interaction with adenovirus capsid leads to the redirection of viral particles to TLR4 thereby promoting a NLRP3-mediated inflammasome response and interleukin 1-beta (IL-1beta) release. Induces the production of proinflammatory cytokines including type I interferon (IFN) in plasmacytoid dendritic cells (pDCs) by triggering the degradation of NFKBIA and nuclear translocation of IRF1, both of which are required for activation of pDCs. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MFPTRVLRSTLQKLPHRETVPMAYDLHMPQRSLFQNLNEKHTEPIVFLHGIFGSKKSYELDSKMIAHGTHTPVYTVDIRNHGQTSHAMPFNYDTLAQDVKEFCHVQGLKSVKLVGYSLGAKISMLAALKYPELVKSAVIIDNAPVKQPYIELYMKQYVKSMLHVLEEAKIKTTDKDWKNKASDAMKKFLPNGVIRKNLLVNLVNKKPDGFESPVVNFDEGLIQFLNPIRQMEEAAVKDVTDWPEESTEGLKYNGPVKFIKGLKSPFINEEGMTKIQDIFPNNEFANVNSSHDILDQRPTEYVKIICDFFNAHRYESAPSNTIIGHKDFKTTIDMRV", "text": "FUNCTION: Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA (PubMed:28356220). Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AB hydrolase superfamily."}
+{"protein": "MQTSETVSDTGSTVTLQTSVAGQAAVPTQVVQQVPVQQQVQQVQTVQQVQHVYPAQVQYVEGSDTVYTNGAIRTTTYPYTETQMYSQNTGGNYFDTQGGSAQVTTVVSTHSMVGTGGIQMGVTGGQIISSTGGTYLIGNAMENSGHSVSHTTRASPATIEMAIETLQKSDGLSSHRSSLLNSHLQWLLDNYETAEGVSLPRSTLYNHYLRHCQEHKLDPVNAASFGKLIRSIFMGLRTRRLGTRGNSKYHYYGIRVKPDSPLNRLQEDMQYMAMRQQPMQQKQRYKPMQKVDGVGDGFAGSGQSGASVEQTVIAQSQHHQQFLDASRALPEFAEVEISSLPDGTTFEDIKSLQSLYREHCEAILDVVVNLQFSLIEKLWQTFWRYSPSSPADGSTITESGNLSEIESRLPKSKLILFCKNESIVKWMCNCDHMMYQSLVEILIPDVLRPIPSALTQAVRNFAKSLEGWLSSAMSNIPQRMIQTKVAAVSAFAQTLRRYTSLNHLAQAARAVLQNTSQINQMLNDLNRVDFANVQEQASWVCQCDDSMVQRLETDFKMTLQQQSTLEQWAAWLDNVVTQALKPYEGRPSFPKAARQFLLKWSFYSSMVIRDLTLRSAASFGSFHLIRLLYDEYMFYLVEHRVAQATGESPIAVMGEFGDLNDASPGNMEKDEGSDVESEIEEELDDSVEPPAKREKTELSQAFQVGCMQPSLEGSVQQSLVLNQLHSEHIVTSTQTIRQCSATGNTYTAV", "text": "FUNCTION: Transcription factor required for ciliogenesis and islet cell differentiation during endocrine pancreas development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RFX family."}
+{"protein": "MLLLINVILTLWVSCANGQVKPCDFPDIKHGGLFHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDYIHCTQNGWSPAVPCLRKCYFPYLENGYNQNYGRKFVQGNSTEVACHPGYGLPKAQTTVTCTEKGWSPTPRCIRVRTCSKSDIEIENGFISESSSIYILNKEIQYKCKPGYATADGNSSGSITCLQNGWSAQPICINSSEKCGPPPPISNGDTTSFLLKVYVPQSRVEYQCQPYYELQGSNYVTCSNGEWSEPPRCIHPCIITEENMNKNNIKLKGRSDRKYYAKTGDTIEFMCKLGYNANTSILSFQAVCREGIVEYPRCE", "text": "FUNCTION: Might be involved in complement regulation. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MESLKEMRKAQMSEGPAAILAIGTANPDNVYMQADYPDYYFKMTKSEHMTELKDKFRTLCEKSMIRKRHMCFSEEFLKANPEVCKHMGKSLNARQDIAVVETPRLGNEAAVKAIKEWGQPKSSITHLIFCSSAGVDMPGADYQLTRILGLNPSVKRMMIYQQGCYAGGTVLRLAKDLAENNKGSRVLVVCSELTAPTFRGPSPDAVDSLVGQALFADGAAALVVGADPDSSIERALYYLVSASQMLLPDSDGAIEGHIREEGLTVHLKKDVPALFSGNIDTPLVEAFKPLGISDWNSIFWIAHPGGPAILDQIEEKLGLKEDKLRASKHVMSEYGNMSSSCVLFVLDEMRSRSLQDGKSTTGEGLDWGVLFGFGPGLTVETIVLRSVPIEA", "text": "SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family."}
+{"protein": "MNYNIRGENIEVTPALKDHVERKIGKLERYFDHSVDADVNVNLKFYNDKESKVEVTIPMTDLALRSEVHNEDMYNAIDLATNKLERQIRKHKTKVNRKFREQGSPKYLLANGLGSDTDIAVQDDIEEEESLDIVRQKRFNLKPMDSEEAILQMNMLGHNFFVFTNAETNLTNVVYRRNDGKYGLIEPTE", "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. May not be the only factor implicated (PubMed:22950019). Might negatively regulate the activity of the sigma-54 factor (SigL) (PubMed:9852014). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family. Long HPF subfamily."}
+{"protein": "MTMTLDAARGGEMVESPFLAQLVAVIRAEDSHGLWDDKTNSEILREFIVTAEERRSMPIIGDPDPELIWRMTKFYDAIGLLVEKRTGCMASQMQKMHHEGFGRVVLIAGKLVVVSKHLRDVHRFGFETWAKLAEAGEKLVESAVATINEFPEAARA", "text": "SIMILARITY: Belongs to the UPF0460 family."}
+{"protein": "MPLLRRPPAAPHRTPIHHDKRLHLFSTHNTRHRATVSSLPVTCLRIRYSSSNPVRHLCGIPSSRCHAAADPAPSKIPGGGSGALEAGVVGWRDLLLQVGEVLSLGFPVWVASACAVALWRPPAFLWVSPMAQIVGISFTMLGMGMTLTLDDLKTALLMPKELASGFLLQYSVMPLSGFLISKLLNLPSYYAAGLILVSCCPGGTASNIVTYLARGNVALSVLMTAASTFAAAFLTPLLTSKLAGQYVAVDPMGLFVSTSQVVLAPVLLGALLNQYCNGLVQLVSPLMPFIAVATVAVLCGNAIAQNASAILSSGLQVVMSVCWLHASGFFFGYVLSRTIGIDISSSRTISIEVGMQNSVLGVVLASKHFGNPLTAVPCAVSSVCHSVYGSLLAGIWRSLPPNDKGQ", "text": "FUNCTION: May function as sodium-coupled metabolite transporter across the chloroplast envelope. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Plastid, chloroplast envelope. SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family."}
+{"protein": "FTCFTTPSDTSETCPIGNNICYEKRWSGHGMQIEKGCVASCPSFESHYKFLLCCRIENCNQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Orphan group VI sub-subfamily."}
+{"protein": "MIRFILDTSIFVNPDVRKKFGNTPTEAMKTFLKYAEKLFGKVEFYMPPGIYKEVKNFLEDIPPEMELYIIKKPPNVHDIKIPAFVVYELIEDIRRRVDKGLRVAEKAVRESVIDTNNVDKIIQKLRRNYRKALREGIVDSTEDFELILLAKEIDGIIVSADVGILTWAEKMGIKWVDAFKFKELLDELVEKVESEKERK", "text": "FUNCTION: RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. SIMILARITY: Belongs to the HARP family."}
+{"protein": "MEKRPYSVAWLSESSQRKPLCTNVDLLGYKSGNPDLPPNREYNVSLPSRVILPTPDYREKENYCGRNVHNGERSPPVRDQLHFHPAPQELTTSRRTSIEVSAESSTDQRVIGMTDTNKKTISVCDEDAASRARTKFTAEQLEELEKSFKENRYIGSSEKRRLSKVLKLSENQIKTWFQNRRMKFKRQTQDARVEAFFSGLYLPYYGYPDLPTPGYSVQSEFPVLAPQTMAASSIPFGPLHSTVMSPGLHPAIPSANLGSYPCSSMLVRPILNEPTRQRYSPY", "text": "FUNCTION: Transcriptional repressor. Acts in a ventral signaling pathway downstream of bmp4 to antagonize the Spemann organizer and ventrally pattern the embryonic mesoderm. Represses transcription of the dorsal genes gsc and otx2 (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MTVDEQVSNYYDMLLKRNAGEPEFHQAVAEVLESLKIVLEKDPHYADYGLIQRLCEPERQLIFRVPWVDDQGQVHVNRGFRVQFNSALGPYKGGLRFHPSVNLGIVKFLGFEQIFKNSLTGLPIGGGKGGSDFDPKGKSDLEIMRFCQSFMTELHRHIGEYRDVPAGDIGVGGREIGYLFGHYRRMANQHESGVLTGKGLTWGGSLVRTEATGYGCVYFVSEMIKAKGESISGQKIIVSGSGNVATYAIEKAQELGATVIGFSDSSGWVHTPNGVDVAKLREIKEVRRARVSVYADEVEGATYHTDGSIWDLKCDIALPCATQNELNGENAKTLADNGCRFVAEGANMPSTPEAVEVFRERDIRFGPGKAANAGGVATSALEMQQNASRDSWSFEYTDERLQVIMKNIFKTCAETAAEYGHENDYVVGANIAGFKKVADAMLAQGVI", "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": "MDEIQEPLALTVHLLADTGNGLLLQQALDQLLECICPEVRLFLVSERARPVNYHEKYHPRRARFPGMSVLLFLQESLGQERLFRVLDFLRRSPWQGFPTQHAQGRSCSYLPANQEFYSLHNQMPVWGMRPVNCGTDILRVTLYCSFDNYEDAIRLYEMLLQRDATVQKSDFCFFVLYATEGFSLQLSLKQLPLGMSVDPKESSVLQFRVQEIGQLVPLLPNPCVPISSARWQTQDYDGNKILLQVHPKPGVGIKNGEHPFLNGCLRGDTHPQDSSLNSVSTQRTLEPRSRRRSRSRRFKVHSLELPQPSGSWENSTDPLWRRLGWSTLADSSASGMQQRRLSIPIEPKMGRNVLREDGFEKLEAETNVDTGFTIINSEPRRSFPSRFPRDFQSSQPPRCLSGSSLEVTVSPNQGVFKDRLHPLSLPSQRDFGAKKVISKCSHHLQAQGEEKEEFFI", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FAM124 family."}
+{"protein": "MEKIFQNVEIKPLLIDFSNPFIKNAAKKLFQLEEQLPLVPVNVVMDFKGINRAAVHGLSRVLQDEIPNYMLDIKPGGYKIEDSTDLFMTEQFIRNRINFIPIYAENESLVFALRSLNNSCEVKTIYTRDLIQVAGPKLKYPIFNPTFEIGFLQPGKSLIIEDIYIKKGIGRKHAAFNLAVKTHFSHLDIEQYPTDKKEYMALSGYKQSSMTSDPRHHRLGLCFPAVPMPRINKAVRTYLKNACRVIIGRIQSIQKIYENFEEPQPELVLFSMDEEKTKAIITIKDETHTIGNLLKTCIYEMIPDISFVGYQCVPHKQEMVLTIIHKASQEDLITLLEKSIQNIIQMFQTLEKNIDELIA", "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: In the N-terminal section; belongs to the archaeal RpoD/eukaryotic RPB3 RNA polymerase subunit family. SIMILARITY: In the C-terminal section; belongs to the archaeal RpoL/eukaryotic RPB11/RPC19 RNA polymerase subunit family."}
+{"protein": "MAKRLVLFVAVVVALVALTVAEGEASEQLQCERELQELQERELKACQQVMDQQLRDISPECHPVVVSPVAGQYEQQIVVPKGGSFYPGETTPPQQLQQRIFWGIPALLKRYYPSVTSPQQVSYYPGQASPQRPGQGQQPGQGQQSGQGQQGYYPTSPQQPGQWQQPEQGQPGYYPTSPQQPGQLQQPAQGQQPGQGQQGRQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQGQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPEQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQPGQGQQPGQGQPGYYPTSPLQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQKGQQPGQGQQPGQGQQGQQPGQGQQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSPLQPGQGQPGYDPTSPQQPGQGQQPGQLQQPAQGQQGQQLAQGQQGQQPAQVQQGQQPAQGQQGQQLGQGQQGQQPGQGQQPAQGQQGQQPGQGQQGQQPGQGQQPGQGQPWYYPTSPQESGQGQQPGQWQQPGQWQQPGQGQPGYYLTSPLQLGQGQQGYYPTSLQQPGQGQQPGQWQQSGQGQHGYYPTSPQLSGQGQRPGQWLQPGQGQQGYYPTSPQQSGQGQQLGQWLQPGQGQQGYYPTSLQQTGQGQQSGQGQQGYYSSYHVSVEHQAASLKVAKAQQLAAQLPAMCRLEGGDALSASQ", "text": "FUNCTION: Glutenins are high-molecular weight seed storage proteins of wheat endosperm. Thought to be responsible for the visco-elastic property of wheat dough. SIMILARITY: Belongs to the gliadin/glutenin family."}
+{"protein": "MSDKLKERKRTPVSHKVIEKRRRDRINRCLNELGKTVPMALAKQSSGKLEKAEILEMTVQYLRALHSADFPRGREKAELLAEFANYFHYGYHECMKNLVHYLTTVERMETKDTKYARILAFLQSKARLGAEPAFPPLGSLPEPDFSYQLHPAGPEFAGHSPGEAAVFPQGSGAGPFPWPPGAARSPALPYLPSAPVPLASPAQQHSPFLTPVQGLDRHYLNLIGHAHPNALNLHTPQHPPVL", "text": "FUNCTION: Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGCG-3'. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HEY family."}
+{"protein": "MAENSNGALGCVVRCLSSESELQELCREEQLCCAELGVTRKNLSDFEVEYLWNYKKVQDQELYLVKWKYYPDSESTWEPRHHLKCNNLLKQFHLDLERELLRRAKAAGTKKTAVRCPRRLDQSLSHYLVLKAKQRKRLRQWAQQLNAKRSHLGLILVENEVDLEGPPRDFVYINEYRVGEGVTINRISAGCKCRDCFSDEGGCCPGAFQHKKAYNNEGQVKVKPGFPIYECNSCCRCGPSCPNRVVQKGIQYKFCIFRTSDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGTTYLFDLDYVEDVYTVDAARYGNISHFVNHSCKPNLQVYNVFIDNLDERLPRIAFFATRTIRTGEELTFDYNMQVDPVDVESSKMDSNFGIAGLPASPKKRVRVECKCGVSSCRKYLF", "text": "FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Associates with centromeric constitutive heterochromatin. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily."}
+{"protein": "MDSRIPYDDYPVVFLPAYENPPAWIPPHERVYHPDYNNELTQFLPRIVTLKKPPGAQLGFNIRGGKASQLGIFISKVIPDSDAHRAGLQEGDQVLAVNDVDFQDIEHSKAVEILKTAREISMRVRFFPYNYHRQKERTVH", "text": "FUNCTION: Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10- binding protein TSPAN33. SUBCELLULAR LOCATION: Cytoplasm Cell junction, adherens junction Cell membrane."}
+{"protein": "MALKQLSSNKCFGGLQKVFEHDSVELKCKMKFAIYLPPKAETGKCPALYWLSGLTCTEQNFITKSGYHQAASEHGLVVIAPDTSPRGCNIKGEDESWDFGTGAGFYLDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICTLKNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDESKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLSDGQLLPDNFIAACTEKKIPVVFRSQEGYDHSYYFIATFITDHIRHHAKYLNA", "text": "FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle. SIMILARITY: Belongs to the esterase D family."}
+{"protein": "MSKNIVVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKAGADIISVHVEHNASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRQMCDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVRNSKRPEPQLATV", "text": "FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate. SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family."}
+{"protein": "MLEHLSSLPTQMDYKGQKLAEQMFQGIILFSAIVGFIYGYVAEQFGWTVYIVMAGFAFSCLLTLPPWPIYRRHPLKWLPVQDSGSEDKKPGERKIKRHAKNN", "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 (PubMed:3511473). Dispensable for SPC enzymatic activity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SPCS1 family."}
+{"protein": "MQSMTIFNIITQLVFLSKTLNGNLSVQPVFQTLDGYEYTSQSFSQNLQSESQLEIVYEWKYLDFLYSTFVQRQQSILNGDFVPKNNLPLGIDVHNNRLFVTTPRWKNGVPASLGTLPFPPKESSPAIKPYPNWEAHGNPNNPDCSKLMSVYRTAVDRCDRIWLIDSGIVNATINLNQICPPKIVVYDLKSDELIVRYNLEASHVKQDSLHSNIVVDIGEDCDDAHAIVSDVWRFGLLVYSLSKNRSWRVTNYNFYPDPFASDFNVYGLNFQWLDGVFGMSIYYNKKIMERVLYFHPMASFKEFMVPMNILLNESVWQTNTQEYAKYFIPIGDRGYNSQSSTSGVTRNGIMFFTQVHQDDIGCWDTSKPYTRAHLGKFHNMENSNLIQFPNDLKVDKEKDQNVWLISNRLPIFLYSNLDYGEVNFRILKANVNKIIRNSVCNPDNSYINTSKSAFVLIEEGQCF", "text": "FUNCTION: Catalyzes the conversion of dopaminechrome to 5,6- dihydroxyindole in the eumelanin biosynthetic pathway originating from dopamine (PubMed:34388859). Catalyzes tautomerization of dopaminechrome to 5,6-dihydroxyindole during eumelanin biosynthesis (PubMed:34388859). Acts both dopaminechrome and N-methyl dopaminechrome but not on dopachrome or other aminochromes tested (PubMed:34388859). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the major royal jelly protein family."}
+{"protein": "MIVVGIDHGTSGITSCIMENGLIKSIFKIRRTEFEKLSFLDELKKHINLSEIDLIGVCYSMGDGINKITDISRVKNRGVRNLEGIGKKIGGGTKVYDEIKESKIPAVVIPGLHKGIDCMDKRFNALFSHTASPEKISICYNAYKTFNLENFILSDISSNTVTLLIRNGKIFGGFDACIGAVGILHGPIDLELIKKIDLREITANEAFSKAGAVKITDSYKGVEDTKSEIIEKYEKDEKCKLAVDSLVLSVSMEINSLMFLNPENNVVIAGSVGVCKNPDISKMIKENTNGNFFVLDGESGAIGSAMIANDILYGKKDILGISVDFNIE", "text": "SIMILARITY: Belongs to the UPF0285 family."}
+{"protein": "MSDNDALRALTAQMAQEGIRRLLVLSGDVSWCRERALALREALAGDWLWVATDAPAAPHCTPQALQTLLGREFRHAVFDAQLGFDASAFAALSGTLRAGSWLVLLTPPYSAWESRPDADSLRWSDCPQPVATPHFIQHLKRVMARDEQTLHWQQSQPFSWPRFPARPHWQPATGEPQPEQAAILRHLLRMPPGVAAVTAARGRGKSALAGQLISRMSGTAIVTAPSKAATDVLAQFAGEKFRFLAPDALLAGTETADWLIVDEAAAIPAPLLHRLASRFSRILLTTTVQGYEGTGRGFLLKFCARFPHLRRFELRQPVRWAQGCPLEQWVGEALIFDDETFAHAPQGAIRFSAFTQALWHTGPAQPLAVYQLLSGAHYRTSPLDLRRMMDAPGQHFLGAFTAERVAGAAWLVEEGRLSAALSQAVWAGYRRPRGNLVAQSLAAHGGDPLAATLTGRRVSRIAVHPARQREGIGQQLIAEAYGGASRCDYLSVSFGYTAELWRFWQRCGFVLVRMGNHKEASSGCYTAMALLPISEAGARLAHREHQRLRRDAEILARWNGEAIPVIPLKASTLNDDDWDELAGFAFAHRPLLTSLGSLSRLLERCELALPALRGRLEEKCSDANLCIRLGLPGRKALLVAQRREVAHALTALDDERAQRLRERVLQWQFFH", "text": "FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA subfamily."}
+{"protein": "MNQEDNTGGGGIFGLFKWTKDALFGTDISPSMKYKDQEERRDRSRYAQDDTNFSMKFGNDSNRRSTNLSRSNSWSGLDSTLHRKYELLPEYNENGFNSIVNGDHHSKERIRSLRSPAPIVPREPLRNEPTDTFGHRLHTKRRTINELSNSQIPFIPPQEDDPLLSKLFNKDGVNEVRRSPYKLSVKDIPGKFPSPLTKRDEIDNYYVRDEDACHKNREYKKAYFDLFAQMDLNSRDLEDLCEDVREQREQFHRNEQTYKQAYEEMRAELVNELKKSKTLFENYYSLGQKYKSLKKVLDQTISHEAELATSRERLYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNYESEIHDLLLQLSLRNNERKDTSAGSNIFSTGQ", "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. 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": "MRFRQQVETCLNYWPAEGPVQRELILGTVGAYRRPIDSRPVLIQDVRGQEGTFTLDIHGFQFIKHISQHVASFDEASVLKDNMTALEAEHLLKTRWAIVNIWRPLKPVPRDPLAVSDARSFHDKDLLEIYGRVPGRQAKKDYDAATKGSGFGMLYGKYSPGQQWFYMSDMKPDEALLIKCYDSKDDGRTARRTPHTAFVDPRTRDVKVARESLELRCLVFFEDQPLA", "text": "FUNCTION: Hydroxylase/desaturase; part of the gene cluster that mediates the biosynthesis of aspergillic acid, a hydroxamic acid- containing pyrazinone with aliphatic side chains that originates from leucine (Leu) and isoleucine (Ile) (PubMed:29674152). Aspergillic acid has antibiotic properties and was shown to be lethal to mice (PubMed:29674152). The first step in the pathway is the production of deoxyaspergillic acid via a condensation between the Ile amine and the Leu carboxylic acid, followed by a reductive release from the protein forming the dipeptide aldehyde NH(2)-Leu-Ile-CHO, which could undergo an intermolecular cyclization resulting in a dihydropyrazinone (PubMed:29674152). As the NRPS asaC lacks a condensation domain, it is improbable that it is responsible for condensation of Leu and Ile (PubMed:29674152). One possibility is that asaC acts on a previously condensed dipeptide and functions as a Leu-Ile reductase to yield deoxyaspergillic acid (PubMed:29674152). After asaC forms deoxyaspergillic acid, the cytochrome P450 asaD oxidizes the pyrazinone to the hydroxamic acid-containing bioactive metabolite aspergillic acid (PubMed:29674152). The hydroxylase/desaturase asaB can then convert aspergillic acid to hydroxyaspergillic acid (PubMed:29674152). Both aspergillic acid and hydroxyaspergillic acid can form complexes with iron producing ferriaspergillin analogs (PubMed:29674152). SIMILARITY: Belongs to the asaB hydroxylase/desaturase family."}
+{"protein": "MTRRPVSRKRRATHGTGPGEQSDWDHSAHKRKRLQPEKKSLVFYLKSRELKPHNDSTYLHLLRGHAACTLPGILSEREFHLGNLNKVFASQWLNHRQVVCGTKCNTLFVVDIQTGQITKIPILKDREPISGSHQSCGIHAIEINPSRTLLATGGENPNSIAVYRLPTLDPVCVGDGGHNDWIFSIAWISDTMAVSGSRDGFMALWEMTDEVVNKRDFQHGLSRVPVYSHISHKALKDIPKESSNPVNCKVRALAFNGNNKELGAVSLDGFFHLWKAEQTLSKLLSTKLPFCRENVCLAYGLEWSLYAVGSQAHVSFLDPREPPQCAKSVYCREQGSGIRSVSFYEHIVTVGTGQGALLFYDIRAQRFLEDLTGSCREGDLLKLNTGKGWLNHNEMWMNYFSDIDSCPNAVYTHCYDSSGTKLFVAGGPLPTGLHGNYAGLWS", "text": "FUNCTION: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) 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 DCX(DCAF12) complex specifically recognizes proteins with a diglutamate (Glu-Glu) at the C-terminus leading to their ubiquitination and degradation. Also directly recognizes the C-terminal glutamate-leucine (Glu-Leu) degron as an alternative degron in proteins leading to their ubiquitination and degradation. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus. SIMILARITY: Belongs to the WD repeat DCAF12 family."}
+{"protein": "MGKDEEEMRGEIEERLINEEYKIWKKNTPFLYDLVITHALEWPSLTVEWLPDREEPSGKDYSVQKMILGTHTSESEPNYLMLAQVQLPLDDTESEARQYDDDRSEFGGFGCATGKVQIIQQINHDGEVNRARYMPQNPFIIATKTVNAEVYVFDYSKHPSKPPLDGACNPDLKLRGHSSEGYGLSWSKFKQGHLLSGSDDAQICLWDINATPKNKSLDAQQIFKAHEGVVEDVAWHLRHEYLFGSVGDDQYLLIWDLRSPSASKPVQSVVAHSMEVNCLAFNPFNEWVVATGSTDKTVKLFDLRKLSTALHTFDSHKEEVFQVGWNPKNETILASCCLGRRLMVWDLSRIDEEQTVEDAEDGPPELLFIHGGHTSKISDFSWNPCEDWVISSVAEDNILQIWQMAENIYHDEDDAPGEEPSKAS", "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, and the fertilization independent seed (FIS) complex, a polycomb group protein complex which is required to maintain the transcriptionally repressive state of homeotic genes throughout development. Required for several aspects of plant development including normal leaf expansion, correct development of flowers, normal endosperm development, repression of parthenogenetic seed development and repression of floral homeotic genes in leaf tissue. Also required for the recruitment of chromosomal DNA into heterochromatic chromocenters. Also involved in regulation of imprinted genes. Acts together with RBR1 to repress the expression of MET1 during female gametogenesis. This in turn activates expression of the imprinted genes FIS2 and FWA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."}
+{"protein": "MENRENLVEIPIEEEVKQAYIDYAMSVIVGRAIPDVRDGLKPVQRRILYSMYEMGLLPDKPFKKSARIVGETLGKYHPHGDQAVYEALVRMAQDFTMRYPLIIGQGNFGSIDGDPAAQMRYTEAKLSPLAVEMLTDIDKDTVDFQPNFDDTLMEPEVLPSKFPNLLCNGTSGIAVGLATSIPPHNLTEVGNALVKLAQNPQISVDEIMEILKGPDFPTGGVIENFAQVKEIYKTGRGIIKVKGKAHVEKVQGGRERIVITEIPYQVNKAELIKKIADNVRNGKIKEISDIRDETDKEGIRIVVELKRDAKGEEVLKKLYKYTPLEKGFPVNLVVLIDKEPKLVDIKTLLREFIKHRLEVILRRSKYFLKKVQDRLHIVEGLLKAINFIDDIIERIRRSKDASEARNYLMEEFGLSEKQAQAVLDLRLQRLTSLEREKLLEEEKELREKIEYYKKLVASEGERIKVFIEETEELVKKYGDKRRTFIGGVKEVKEGSITVAVLQDGSIIPVEELPLEKAPVVNILRVPFTEGLFLVSNRGRVYWIAGSQALQGSKVSLKSREEKIVGAFIREKFGNRLLLATKKGYVKKIPLAEFEYKAQGMPIIKLTEGDEVVSIASSVDETHILLFTKKGRVARFSVREVPPSTPGARGVQGIKLEKNDETSGLRIWNGEPYLLVITAKGRVKKISHEEIPKTNRGVKGTEVSGTKDTLVDLIPIKEEVELLITTKNGKAFYDKINQKDIPLSTKKSIPRTRWKLEDDEIIKVVIKKSE", "text": "FUNCTION: A type II topoisomerase. Despite its similarity to DNA gyrase, this enzyme is not able to supercoil DNA, and instead acts like topoisomerase IV. Relaxes both positively and negatively supercoiled DNA in an ATP-dependent fashion, decatenates interlocked circles. This the first bacteria shown to not contain DNA gyrase, although it has 2 copies of a reverse gyrase that introduces positive supercoils. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP- dependent manner (PubMed:21076033). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit family."}
+{"protein": "MEKYENLGLVGEGSYGMVMKCRNKDSGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLKLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDIWAIGCLVIEMLMGQPLFPGESDIDQLHHIMTCLGNLIPRHQELFYKNPVFAGVRLPEVKDAEAEPLESRYPKLPEAVISLAKKCLHIDPDKRPFCADLLRHDFFQMDGFAERFSQELQLKIEKDARNNSLPKKSQNRKKEKDDALGEERKTLVVQDTNADPKIKDSKVFKVKGSKIDVEKMEKGSRASNANCLHDNGTNHKGLASTSLRDCSNVNIDHSRNPGTAIPPLTHNLSAVAPGINAGMGTIPGVQNYRVDEKTKKYCNPFVKPNQPPPAGIYNMNVSTSVSGEKYLLQANKKRKEYPKADVRLPELNYNHLPELRALEGIARNSRLIKKENKCLSESRIPSLAAIDLHVSSVASHQGAGSPLSDDSEADLPRMEHQH", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "MLRRLGVRHFRRTPLLFVGGDGSIFERYTEIDNSNERRINALKGCGMFEDEWIATEKVHGANFGIYSIEGEKMIRYAKRSGIMPPNEHFFGYHILIPELQRYITSIREMLCEKQKKKLHVVLINGELFGGKYDHPSVPKTRKTVMVAGKPRTISAVQTDSFPQYSPDLHFYAFDIKYKETEDGDYTTLVYDEAIELFQRVPGLLYARAVIRGPMSKVAAFDVERFVTTIPPLVGMGNYPLTGNWAEGLVVKHSRLGMAGFDPKGPTVLKFKCTAFQEISTDRAQGPRVDEMRNVRRDSINRAGVQLPDLESIVQDPIQLEASKLLLNHVCENRLKNVLSKIGTEPFEKEEMTPDQLATLLAKDVLKDFLKDTEPSIVNIPVLIRKDLTRYVIFESRRLVCSQWKDILKRQSPDFSE", "text": "FUNCTION: RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RNA ligase 2 family."}
+{"protein": "MSLKHFLNTQDWSRAELDALLTQAALFKRNKLGSELKGKSIALVFFNPSMRTRTSFELGAFQLGGHAVVLQPGKDAWPIEFNLGTVMDGDTEEHIAEVARVLGRYVDLIGVRAFPKFVDWSKDREDQVLKSFAKYSPVPVINMETITHPCQELAHALALQEHFGTPDLRGKKYVLTWTYHPKPLNTAVANSALTIATRMGMDVTLLCPTPDYILDERYMDWAAQNVAESGGSLQVSHDIDSAYAGADVVYAKSWGALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNGVFSHCLPLRRNVKATDAVMDSPNCIAIDEAENRLHVQKAIMAALVGQSRP", "text": "FUNCTION: Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to produce N(2)-acetyl-L-citrulline. This is a step in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. AOTCase family."}
+{"protein": "MENGATSQSEGKDPSGFLSEIIGNPVTVKLNSGVVYKGELQSVDGYMNIALEKTEEFINGVKRRSYGDAFVRGNNVMYISAD", "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": "MDIVSLAWAALMVVFSFSLSLVVWGRSGL", "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. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetN family."}
+{"protein": "MALARANSPQEALLWALNDLEENSFKTLKFHLRDVTQFHLARGELESLSQVDLASKLISMYGAQEAVRVVSRSLLAMNLMELVDYLNQVCLNDYREIYREHVRCLEERQDWGVNSSHNKLLLMATSSSGGRRSPSCSDLEQELDPVDVETLFAPEAESYSTPPIVVMQGSAGTGKTTLVKKLVQDWSKGKLYPGQFDYVFYVSCREVVLLPKCDLPNLICWCCGDDQAPVTEILRQPGRLLFILDGYDELQKSSRAECVLHILMRRREVPCSLLITTRPPALQSLEPMLGERRHVLVLGFSEEERETYFSSCFTDKEQLKNALEFVQNNAVLYKACQVPGICWVVCSWLKKKMARGQEVSETPSNSTDIFTAYVSTFLPTDGNGDSSELTRHKVLKSLCSLAAEGMRHQRLLFEEEVLRKHGLDGPSLTAFLNCIDYRAGLGIKKFYSFRHISFQEFFYAMSFLVKEDQSQQGEATHKEVAKLVDPENHEEVTLSLQFLFDMLKTEGTLSLGLKFCFRIAPSVRQDLKHFKEQIEAIKYKRSWDLEFSLYDSKIKKLTQGIQMKDVILNVQHLDEKKSDKKKSVSVTSSFSSGKVQSPFLGNDKSTRKQKKASNGKSRGAEEPAPGVRNRRLASREKGHMEMNDKEDGGVEEQEDEEGQTLKKDGEMIDKMNG", "text": "FUNCTION: Inhibits autoprocessing of CASP1, CASP1-dependent IL1B secretion, PYCARD aggregation and PYCARD-mediated apoptosis but not apoptosis induced by FAS or BID (By similarity). Displays anti- inflammatory activity (By similarity). Required for immunity against C.albicans infection (PubMed:23071280). Involved in the innate immune response by contributing to pro-inflammatory cytokine release in response to invasive bacterial infection (By similarity). Contributes to T-cell-mediated inflammatory responses in the skin (PubMed:27221772). Plays a role in protection against periodontitis through its involvement in induction of IL1A via ERK activation in oral epithelial cells infected with periodontal pathogens (By similarity). Exhibits both ATPase and GTPase activities (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Note=Cytoplasmic protein which is recruited to the cell membrane by NOD1 following invasive bacterial infection. SIMILARITY: Belongs to the NLRP family."}
+{"protein": "MYLIGEALVGDGAELAHIDLIMGNKEGAVGQAFANSISQLSKGHTPLLAVVRPNLPTKPSTLIIPKVTLKKEYQVNQMFGPVQAAVAKAVADSIEEGVFEGVDIEDTVIMASVFVHPTAQDYNKIYRFNYGAMKLALRRALDRFPDVETLLHEKDRAAHAVMGFKVQRLWDPPYLQVAMDLVDRNHMNRVLDELPQNDHLIIEAGTPLIKKFGLSIISEIRERRPNAFIVADLKTLDTGNLEARMTADAGADAVVISGLAPISTIEKAIEDTRKTGIYTVIDMLNVKDPVAVVKQLKVKPDVVELHRGIDVEDTAYAWGDIPAIKKAGGERLLVATAGGIRQGVVKDARKAGADILVVGRAITASKNIQHAAEEFLEELSTEEIDQFRIMTDF", "text": "FUNCTION: Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H(4)MPT) to 5,10- methylenetetrahydromethanopterin. FUNCTION: Catalyzes the reversible formation of ribulose-5-phosphate and formaldehyde from 3-hexulose-6-phosphate. SIMILARITY: In the C-terminal section; belongs to the HPS/KGPDC family. HPS subfamily. SIMILARITY: In the N-terminal section; belongs to the formaldehyde- activating enzyme family."}
+{"protein": "MNSLLFLALVGAAVAFPVDDDDKIVGGYTCRENSIPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKTRIQVRLGEHNINVLEGNEQFVNSAKIIKHPNFNSRTLNNDIMLIKLASPVTLNARVATVALPSSCAPAGTQCLISGWGNTLSFGVNNPDLLQCLDAPLLPQADCEASYPGKITNNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCALKDNPGVYTKVCNYVDWIQDTIAAN", "text": "FUNCTION: Serine protease capable of autoactivation. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MVVFSKVAAAAFGLSAVASAMPAAPPRQGFTINQLTRAIPKRTINLPAIYANALSKYGGNVPPHIQDAMAHGSAVTTPEQYDVEYLTPVAVGGTTMNLDFDTGSADLWVFSNELPSSQTTGHSVYKPSDNGTRMSGYSWEISYGDGSSAGGDVYRDTVTVGGVTAPGQAVEAASHISEQFTRDQNNDGLLGLAFSSINTVQPKSQTTFFDSVKSQLESPLFAVTLKHQAPGSYDFGYIDQSKYTGELTYTDVDNSQGFWMFSATAGETDFDAIADTGTTLIMIDQSIAEDYYSQVPLAFNNFFYGGWTFPCSAELPSFTVTINGYDAVVPGEHIKYAPVTDGSSTCFGGIQDNQGLPFSILGDVFLKSQYVVFDSEGPQLGFAPQA", "text": "FUNCTION: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MVSLDDILGIVYVTSWSISMYPPIITNWRHKSASAISMDFVMLNTAGYSYLVISIFLQLYCWKMTGDESDLGRPKLTQFDFWYCLHGCLMNVVLLTQVVAGARIWRFPGKGHRKMNPWYLRILLASLAIFSLLTVQFMYSNYWYDWHNSRTLAYCNNLFLLKISMSLIKYIPQVTHNSTRKSMDCFPIQGVFLDVTGGIASLLQLIWQLSNDQGFSLDTFVTNFGKVGLSMVTLIFNFIFIMQWFVYRSRGHDLASEYPL", "text": "FUNCTION: Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from vacuoles/endodomes. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cystinosin family."}
+{"protein": "MVRVMVVIRIFGTGCPKCNQTYENVKKAVEELGIDAEIVKVTDVNEIAEWVFVTPGVAFDDVIVFEGKIPSVEEIKEELKSYLEGK", "text": "FUNCTION: Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity). SIMILARITY: Belongs to the glutaredoxin family."}
+{"protein": "MAHSVKIYDTCIGCTQCVRACPTDVLEMIPWNGCKANQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGSETTRSMGLAY", "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": "LVKDDMSLILSSFSLFRSSRSSPASASLAGSGHPRTTPPKIASLQSPMVEETKERIAKLFKKKEVSRSTYDTAWVGMVPSPFSSEEPCFPDCLFWLLQNQCPDGSWAQPHHHSLSPSLLNKDVLSSTLASILALQKWGLGQRHIAKGLHFLELNFASATDNSQITPLGFDIVFPAMLDYAADLSLNLRLDPTTLNDLMNRRDSELKRCTENGSAETEVYLAYIGEGMGKLHDWETVMKYQRKNGSLFNSPSTTAAAFIALGNSDCLKYLNSALKKFGSAVPAVYPLDIYSQLCIVDNLERLGISRFFSTEIQSVLDDTYRCWLQGDEEIFMDASTCGLAFRTLRMNGYKVTSDSFIKVVQDCFSSSSPGHMRDVNTTLELYRASELMLYPHEIELEKQNSRLRSLLEQELSGGSIQSSQLNAEVKQALDYPFYAVLDRMAKKKTIEHYNIDDSRILKTSFCLPSFGNKDLLSLSVQDYNRCQAIHREELREFDRWFVENRLDELEFARHKSAYYYCYFAAAATFFAPELSDARMSWAKNALMTTMVDDLFDVTGSVEEMKNLIQLVELWDVDVSTECRSHKVQILFSALKRTICEVGDRAHQLQGRSIRSHIIVIWLDLLHSMMKEVEWSRDKFVPTMDEYVSNAYVSFALGPIVLPALYLVGPKLSEEMVNHSEYHNLFKLMSMCGRLLNDIRGYEREHDDGKLNAMSLYIMNNGGEITPEVAIMEIKSWNDRQRRELLRLVLEEKSVIPKACKDLFWHMCSVVHLFYNKDDGFWSQELIEVVNQVIHQPILLSHF", "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 (By similarity). Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-atiserene (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MKITTKVLIIGSGPAGLSAAIYTARSALKPILINGMQPGGQLTMTTDVENYPGFAETIQGPWLMEQMSMQAKNVGTEIISDYVERVDLSKRPFKIFTGTGNEYEADSIIICTGAESKWLGIASEQEFRGFGVSSCAICDGFFFKNQEIVVVGGGNSALEEALYLTNHANKVTVVHRRNSFRAEKILQDRLFKNPKISVIWDHIIDEIVGSNKPKAVTGVKIQNVYTNEINLVNCSGVFIAIGHAPNTALFKGQIAIDDDNYIVTQSGSTRTNVEGVFAAGDVQDKIYRQAVTAAASGCMAALEVAKFLNK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MRVKRAVHAKKKRKKYLKAAKGYRGALSRRYKLAKQMYVRSKWYSYVGRKQKKRDMRKLWITRINIAARNEGLKYSELIHGLKLAGVSINRKMLSELAVNDPEAFKEYVKIAKEALAS", "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": "MNRLIVLCLFVAMIYATIALPKKEDISNDERSISVSKVPVKKSVAIAGAVIEGAKLTFGILEKILTVLGDINRKIAIGVDNESGREWTAQNAYFFSGTSDVVLPASVPNTKAFLYNAQKDRGPVATGVVGVLAYSLSNGNTLGILFSVPYDYNLYSNWWNIKLYKGIKRADRDMYNDLYYYAHPHKGDNGWHENSLGFGLKSKGFMTSSGQTILQIRVSRA", "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": "MQLGLSVSDSDASPFTPLAVLELAHDTKAEAIAWLLNRIRDKQRNGGAELLVDQLLFPAQDGQKPNPNVFVVGSTLQRLLSGAEDVGLFKEFQDGTMRGFTYANRESFKDFEGDGEGFLGDAECQYIVKHELDTLRAKNEEYIPGYPKYKLYPGKSIVRRLQSKGVLVQYFPLHNKEDLKRLSFSWYKKIKLSFQPLDDIRSYFGEGLGLYFGFLEYFTFALIPMALIGIPYYLFDWEDYDKYVLFAVFNLVWSTVFLEVWKRCSATLAYSWGTLGRKKAFEEPRAGFHGPLGLNPVTGREEPIYPSSKRHLRIYLVSVPFVLLCLYLSFYVMMVYFDMEFWAISIYHENPNFATSVLLFVPSIIYAVVIEIMNLLYRYAAEFLTDWENHRLESSFQNHLVPKVLVFNFVNCFASLFYIAFVMQDMVLLRQSLATLLITSQILNQVMEAFLPYWLQRRRNKRVYKRMRRLMGDKELPLLEQIQLETEMNTYLGTFDDYLEQFLLFGYVSLFSCVHPLAAVLVVLNNITEVYSDAFKMCHVFKRPFSEPAANIGVWQLAFETMSIIAVVTNCALIALSPQVKAYFPESDAQLILTVVAIEHVLLAFKFILAFVIPDVPKHIQVKLSKLDFESLEALKKRKILEVAET", "text": "FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1 (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. SIMILARITY: Belongs to the anoctamin family."}
+{"protein": "MSAFFLPSSSHALFLVLMLFFLTNISAQPLYISETNFTCPVDSPPSCETYVAYRAQSPNFLSLSNISDIFNLSPLRIAKASNIEAEDKKLIPDQLLLVPVTCGCTKNHSFANITYSIKQGDNFFILSITSYQNLTNYLEFKNFNPNLSPTLLPLDTKVSVPLFCKCPSKNQLNKGIKYLITYVWQDNDNVTLVSSKFGASQVEMLAENNHNFTASTNRSVLIPVTSLPKLDQPSSNGRKSSSQNLALIIGISLGSAFFILVLTLSLVYVYCLKMKRLNRSTSSSETADKLLSGVSGYVSKPTMYEIDAIMEGTTNLSDNCKIGESVYKANIDGRVLAVKKIKKDASEELKILQKVNHGNLVKLMGVSSDNDGNCFLVYEYAENGSLEEWLFSESSKTSNSVVSLTWSQRITIAMDVAIGLQYMHEHTYPRIIHRDITTSNILLGSNFKAKIANFGMARTSTNSMMPKIDVFAFGVVLIELLTGKKAMTTKENGEVVILWKDFWKIFDLEGNREERLRKWMDPKLESFYPIDNALSLASLAVNCTADKSLSRPTIAEIVLCLSLLNQPSSEPMLERSLTSGLDAEATHVVTSVIAR", "text": "FUNCTION: Involved in resistance to oomycetes (e.g. Aphanomyces euteiches) and to fungi (e.g. Colletotrichum trifolii). FUNCTION: During nodulation, plays a central role in nodule organogenesis (PubMed:22874912). Involved in the perception of Nod factors, the first step of recognition of rhizobia prior to nodulation (PubMed:12753588). Necessary in epidermal cells to induce cortical cell divisions leading to nodule primordia formation (PubMed:22874912). Required during root nodule symbiosis with Sinorhizobium meliloti by triggering infection threads and release of bacteria into the cytoplasm of cells in the infection zone of developing nodules, especially in cells derived from the meristem (PubMed:25351493, PubMed:16844829, PubMed:22087221). Promotes plant fitness (e.g. fruit weight and leaf number) (PubMed:23173081). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Vacuole lumen Note=Removed from the plasma membrane upon the release of rhizobia into the host cytoplasm. Vacuolar localization is observed in cells undergoing breakdown of the receptors. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family."}
+{"protein": "MSQTYNVTLLPGDGIGPEIMAVAVAVLGKVADQFGFAFNFQEALIGGAAIDATGQPLPEATLAQAKDSDAVLLAAIGGYAWDNLPRSQRPETGLLAIREGLGLFANLRPATIFPQLIDASSLKREVVEGVDIMVVRELTGGIYFGKPKGIFETETGEKRGVNTMAYTVGEIDRIAKVAFETARKRRGQLCSVDKANVLDVSQLWRDRVMAIAVDYPDVELSHLYVDNAAMQLVRSPRQFDTIVTGNLFGDILSDIAAMLTGSIGMLPSASLGSDGPGLFEPVHGSAPDIAGQDKANPLAQVLSAAMMLRYGLDQPQAADRLEDAVKKVLEQGYRTGDILSPGTQLVGCRQMGEQLLSILDEM", "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": "MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGVYASPIF", "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": "MFPIDIRPDKLTQEMLDYSRKLGQGMENLLNAEAIDTGVSPKQAVYSEDKLVLYRYDRPEGAPEAQPVPLLIVYALVNRPYMTDIQEDRSTIKGLLATGQDVYLIDWGYPDQADRALTLDDYINGYIDRCVDYLREAHGVDKVNLLGICQGGAFSLMYSALHPDKVRNLVTMVTPVDFKTPDNLLSAWVQNVDIDLAVDTMGNIPGELLNWTFLSLKPFSLTGQKYVNMVDLLDDPDKVKNFLRMEKWIFDSPDQAGETFRQFIKDFYQNNGFLNGGVVLGGQEVDLKDITCPVLNIFALQDHLVPPDASRALKGLTSSPDYTELAFPGGHIGIYVSGKAQKEVTPAIGKWLNER", "text": "FUNCTION: Polymerizes D(-)-3-hydroxybutyryl-CoA to create polyhydroxybutyrate (PHB) which consists of thousands of hydroxybutyrate molecules linked end to end (PubMed:7957260). This subunit has catalytic activity that is enhanced 100-fold by PhaE, the non-catalytic subunit (PubMed:9888824). SUBCELLULAR LOCATION: Cytoplasm Note=Associates with the exterior of poly(3-hydroxybutyric acid) granules (PHB) when grown under 'storage' conditions. SIMILARITY: Belongs to the PHA/PHB synthase family. Type III PhaC subfamily."}
+{"protein": "HPITESAEMPYPGPASLEERGVGSLDDLSLSEQNYPPQRGAGLRYATLEVLLEKQSLLNPFSRVFGIRKQFAGTTECFWKYCV", "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 urotensin-2 family."}
+{"protein": "MNIKTIKIVTIGDYGVGKTTLLMTYTASGSFPQEYVPTALDNFIHEATINGKKASLSIWDTAGGEYYHELRPLIYPETDILLLLFAIENRESFLHIKTNWITEINQYIPGIPIILVGTKIDLRDSDLIKDKSNFVKYKEGLALSKEIGASHFCECSSRMNLGLEELFKKVIKLTNNNNNNNNNNKCIIL", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
+{"protein": "MNRQESINSFNSDETSSLSDVESQQPQQYIPSESGSKSNMAPNQLKLTRTETVKSLQDMGVSSKAPVPDVNAPQSSKNKIFPEEYTLETPTGLVPVATLHSIGRTSTAISRTRTRQIDGASSPSSNEDALESDNNEKGKEGDSSGANDEAPDLDPEIEFVTFVTGDPENPHNWPAWIRWSYTVLLSILVICVAYGSACISGGLGTVEKKYHVGMEAAILSVSLMVIGFSLGPLIWSPVSDLYGRRVAYFVSMGLYVIFNIPCALAPNLGSLLACRFLCGVWSSSGLCLVGGSIADMFPSETRGKAIAFFAFAPYVGPVVGPLVNGFISVSTGRMDLIFWVNMAFAGVMWIISSAIPETYAPVILKRKAARLRKETGNPKIMTEQEAQGVSMGEMMRACLLRPLYFSVTEPVLVATCFYVCLIYSLLYAFFFAFPVIFGELYGYKDNLVGLMFIPIVIGALWALATTFYCENKYLQIVKQRKPTPEDRLLGAKIGAPFAAIALWILGATAYKHIIWVGPASAGLAFGFGMVLIYYSLNNYIIDCYVQYASSALATKVFLRSAGGAAFPLFTIQMYHKLNLHWGSWLLAFISTAMIALPFAFSYWGKGLRHKLSKKDYSIDSIE", "text": "FUNCTION: Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Recognizes spermine, but not spermidine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily."}
+{"protein": "MDRTLESLRHIIAQVLPHRDPALVFKDLNVVSMLQEFWESKQQQKAAFPSEGVVVYESLPAPGPPFVSYVTLPGGSCFGNFQCCLSRAEARRDAAKVALINSLFNELPSRRITKEFIMESVQEAVASTSGTLDDADDPSTSVGAYHYMLESNMGKTMLEFQELMTIFQLLHWNGSLKALRETKCSRQEVISYYSQYSLDEKMRSHMALDWIMKERDSPGIVSQELRMALRQLEEARKAGQELRFYKEKKEILSLALTQICSDPDTSSPSDDQLSLTALCGYH", "text": "SIMILARITY: Belongs to the LIX1 family."}
+{"protein": "MDKKPCNSQDAEVRKGPWTMEEDLILINYIANHGEGVWNSLAKSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQAETMNGQAASSEQNDHQEACTSQMSNGPNDNTIDQTYSPTSYSGNVDTFQAGPNFLTEANDNMWSMEDIWSMQLLNGD", "text": "FUNCTION: MYB-type transcription factor controlling the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) by regulating the expression of ODO1 and EOBI, key regulators of the shikimate pathway, and of several biosynthetic floral scent-related genes including IGS, PAL2 and CFAT (PubMed:21585571, PubMed:20543029, PubMed:23275577). This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:21585571, PubMed:20543029). Binds to and activates the ODO1 and EOBI promoters via MYB binding sites (MBS) 5'-AAACCTAAT-3' and 5'- CTAACT-3' (PubMed:21585571, PubMed:22499185, PubMed:20543029, PubMed:23275577). Regulates the promoters of IGS1, CFAT and PAL2 (PubMed:20543029). Controls flowers petal opening by modulating a global transcriptomic switch (PubMed:21464473). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKLKSVLYLLMLLNCLGLKSAHAATLVHGISTSWHSFSNSVSQTWNEPQTFDLYMPALTWHNRWTYDADKIDRYNERPWGAGGGMSRYDEKGNWNGIYLMAFKDSFNKWEPIGGYGWEKTWRPLNDPDFHFGLGYTAGVTMRDNWNYIPIPLLLPLASIGYGAANFQMTYIPGTYNNGNVYFAWLRWQF", "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. SIMILARITY: Belongs to the lipid A palmitoyltransferase family."}
+{"protein": "MNYTESSPLRESTAIGFTPELESIIPVPSNKTTCENWREIHHLVFHVANICFAVGLVIPTTLHLHMIFLRGMLTLGCTLYIVWATLYRCALDIMIWNSVFLGVNILHLSYLLYKKRPVKIEKELSGMYRRLFEPLRVPPDLFRRLTGQFCMIQTLKKGQTYAAEDKTSVDDRLSILLKGKMKVSYRGHFLHNIYPCAFIDSPEFRSTQMHKGEKFQVTIIADDNCRFLCWSRERLTYFLESEPFLYEIFRYLIGKDITNKLYSLNDPTLNDKKAKKLEHQLSLCTQISMLEMRNSIASSSDSDDGLHQFLRGTSSMSSLHVSSPHQRASAKMKPIEEGAEDDDDVFEPASPNTLKVHQLP", "text": "FUNCTION: Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells (PubMed:16188940). Plays a role in VAMP3-mediated vesicular transport and recycling of different receptor molecules through its interaction with VAMP3. Plays a role in the regulation of cell shape and movement by modulating the Rho-family GTPase activity through its interaction with ARHGEF25/GEFT. Induces primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. Also involved in striated muscle regeneration and repair and in the regulation of cell spreading (By similarity). Important for the maintenance of cardiac function. Plays a regulatory function in heart rate dynamics mediated, at least in part, through cAMP-binding and, probably, by increasing cell surface expression of the potassium channel KCNK2 and enhancing current density (PubMed:26642364). Is also a caveolae-associated protein important for the preservation of caveolae structural and functional integrity as well as for heart protection against ischemia injury. SUBCELLULAR LOCATION: Lateral cell membrane Cell junction, tight junction Membrane; Multi-pass membrane protein Cell membrane, sarcolemma Membrane, caveola Note=Colocalizes with VAMP3 at the cell-cell contact in cardiac and skeletal muscle (By similarity). Its movement from the cytoplasm to membrane is an early event occurring concurrently with cell-cell contact. Colocalizes in epithelial cells with OCLN and TJP1 in an apical-lateral position within the z axis. Detected at cell-cell contact but never observed at the free surface of epithelial cells. SIMILARITY: Belongs to the popeye family."}
+{"protein": "MSKAGASLATCYGPVSTHVMTKAENIRLLILDVDGVLSDGLIYMGNNGEELKAFNVRDGYGIRCALTSNIEVAIITGRKAKLVEDRCATLGIVHLYQGQSNKLIAFSDLLEKLAIAPENVAYVGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTHIAGGRGAVREVCDLLLLAQGKLDEAKGQSI", "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 in vitro. Also catalyzes the dephosphorylation of phospho- tyrosine in vitro. SIMILARITY: Belongs to the KdsC family."}
+{"protein": "MDAAAQESLILELHAIEAIKFGTFVLKSGITSPIYLDLRALVSHPGLLSSIATLLHTLPATRPYDLLCGVPYTALPIASVLSVHRSVPMVMRRKEAKAHGTAKSIEGAFRAGEAVLIIEDLVTSGASVLETAAPLRDQGLVVADAVVVVDREQGGRENLAANGITLHSLMTLTEVLAVLLKHGKVTEEKAREVRQFLDANRKVTVPGAAGAVKPKAVRKGFAERAGLAKNPMGKRLFEVMEAKQSNLCVAADVGTAKELLELAEKVGPEICMLKTHVDILSDFTPDFGAKLCSIAEKHNFLIFEDRKFADIGNTVTMQYEGGIFRILDWADIVNAHIIPGPGIVDGLKLKGLPKGRGLLLLAEMSSAGNLAHGEYTAAAVKIAEQHSDFVIGFISVNPASWSVAPSSPAFIHATPGVQMVSGGDALGQQYNTPHSVINDRGSDIIIVGRGIIKASNPAETAREYRIQGWGAYQSSLP", "text": "SIMILARITY: In the C-terminal section; belongs to the OMP decarboxylase family. SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family."}
+{"protein": "MRYAIMVTGPAYGTQQASSALQFAHALLNEGHELASVFFYREGVYNANLLTSPASDEYDLVRVWQKLNTQHGVALNICVAAALRRGIIDETEAGRLELPSANLQPGFTLSGLGALAEASLTCDRVVQF", "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": "MEPSKMAPLKNAPRDALVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPPRDFLLDIARQKNQTPLPLIKPYAGPRLPPDRYCLTAPNYRLKSLVKKGPNQGRLVPRLSVGAVSSRPTTPTVAPPQAVSVPNKVATPVSVTSQRFAVQIPTSQSTPAKPAPAATSVQNVLINPSMIGSKNILITTNMVSSQSTATDSNPLKRKHDDDDDDDDDDDDNDTM", "text": "FUNCTION: Essential for cell viability. TAF9 and TAF9L are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF9 family."}
+{"protein": "MKLVRKDIEKDNAGQVTLVPEEPEDMWHTFNLVQVGDSLRASTIRKVQTESSTGSVGSNRVRTTLTLCVEAIDFDSQACQLRVKGTNIQENEYVKMGAYHTIELEPNRQFTLAKKQWDSVVLERIEQACDPAWSADVAAVVMQEGLAHVCLVTPSMTLTRAKVEVNIPRKRKGNCSQHDRALERFYEQVVQAIQRHINFEVVKCVLVASPGFVREQFCDYMFQQAVKTDNKVLLENRSKFLQVHASSGHKYSLKEALCDPTVASRLSDTKAAGEVKALDDFYKMLQHEPDRAFYGLKQVERANEALAIDTLLISDELFRHQDVATRSRYVRLVDSVKENAGTVRIFSSLHVSGEQLGQLTGVAAILRFPVPELSDQEDDSSSEED", "text": "FUNCTION: Component of the Pelota-HBS1L complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway. In the Pelota-HBS1L complex, PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel. Following mRNA extraction from stalled ribosomes by the SKI complex, the Pelota-HBS1L complex promotes recruitment of ABCE1, which drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway. As part of the PINK1-regulated signaling, upon mitochondrial damage is recruited to the ribosome/mRNA-ribonucleoprotein complex associated to mitochondrial outer membrane thereby enabling the recruitment of autophagy receptors and induction of mitophagy. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota subfamily."}
+{"protein": "GLLDTLKGAAKNVVGSLASKVMEKL", "text": "FUNCTION: Antibacterial peptide that ihibits reference strains of both Gram-negative bacteria (E.coli, E.cloacae, K.pneumoniae, P.aeruginosa) and Gram-positive bacteria (S.aureus, S.epidermidis, E.faecalis, Streptococcus group B) with relatively low potencies (MIC=25-200 uM). The peptide shows very low hemolytic activity against human erythrocytes. Wheel projection demonstrates the amphipathicity of the alpha-helices is low which may explain the low antibacterial potency. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Ocellatin subfamily."}
+{"protein": "MSCTIEKILTDAKTLLERLREHDAAAESLVDQSAALHRRVAAMREAGTALPDQYQEDASDMKDMSKYKPHILLSQENTQIRDLQQENRELWISLEEHQDALELIMSKYRKQMLQLMVAKKAVDAEPVLKAHQSHSAEIESQIDRICEMGEVMRKAVQMDDDQFCKIQEKLAQLELENKELRELLSISSESLQARKENSMDTASQAIK", "text": "FUNCTION: Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3- mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and RIGI. Does not inhibit NF- kappa-B activation pathways (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIKE family."}
+{"protein": "MATMENKVICALVLVSMLALGTLAEAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFYPNTIDVPPEEECEF", "text": "FUNCTION: Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. May inhibit the growth of calcium oxalate crystals in urine. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MAAAEEGCGVGVEDDRELEELLESALDDFDKAKPSPEHAPTISAPDASGPQKRAPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDASSQQEFTSCLKETLSGLAKNATELQNSGMSEEELMKAMEGLGMDEGDGEASILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHQDSTPPEQFEKYQQQHSVMVKICEQFEAETPTDSEATQRARFEAMLDLMQQLQALGHPPKELAGEMPPGLNFDLDALNLSGPPGANGEQCLIM", "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 membrane-associated to the outer surface of peroxisomes. SIMILARITY: Belongs to the peroxin-19 family."}
+{"protein": "MEAIAKLIKVQLPNYLQKLPVPSSLSGFAELSPSDAIAVVFPFAVVSWLIGYSTYKFFQPKAVELPPSPKAKDTNCVNKCIDKTCKKVVHTVDIEDVGEKLVFCRCWRSKKFPYCDGSHNNHNEQEQDNVGPLIVKGKAN", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CISD protein family. CISD2 subfamily."}
+{"protein": "MSTPFGLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGETGKNKQTSNIKNTVANLKRIIGLDYHHPDFEQESKHFTSKLVELDDKKTGAEVRFAGEKHVFSATQLAAMFIDKVKDTVKQDTKANITDVCIAVPPWYTEEQRYNIADAARIAGLNPVRIVNDVTAAGVSYGIFKTDLPEGEEKPRIVAFVDIGHSSYTCSIMAFKKGQLKVLGTACDKHFGGRDFDLAITEHFADEFKTKYKIDIRENPKAYNRILTAAEKLKKVLSANTNAPFSVESVMNDVDVSSQLSREELEELVKPLLERVTEPVTKALAQAKLSAEEVDFVEIIGGTTRIPTLKQSISEAFGKPLSTTLNQDEAIAKGAAFICAIHSPTLRVRPFKFEDIHPYSVSYSWDKQVEDEDHMEVFPAGSSFPSTKLITLNRTGDFSMAASYTDITQLPPNTPEQIANWEITGVQLPEGQDSVPVKLKLRCDPSGLHTIEEAYTIEDIEVEEPIPLPEDAPEDAEQEFKKVTKTVKKDDLTIVAHTFGLDAKKLNELIEKENEMLAQDKLVAETEDRKNTLEEYIYTLRGKLEEEYAPFASDAEKTKLQGMLNKAEEWLYDEGFDSIKAKYIAKYEELASLGNIIRGRYLAKEEEKKQAIRSKQEASQMAAMAEKLAAQRKAEAEKKEEKKDTEGDVDMD", "text": "FUNCTION: Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "DECFSPGTFCGFKPGLCCSARCFSLFCISLEF", "text": "FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process. This toxin acts on Nav1.2/SCN2A, Nav1.3/SCN3A and Nav1.6/SCN8A (EC(50)=1.7 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
+{"protein": "MSGEMDKPLISRRLVDSDGSLAEVPKEAPKVGILGSGDFARSLATRLVGSGFSVVVGSRNPKRTAGLFPSLAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLADQLAGKILVDVSNPTEKERLQHRQSNAEYLASLFPACTVVKAFNVISAWALQAGPRDGNRQVLICGDQLEAKHTVSEMARAMGFTPLDMGSLASAREVEAIPLRLLPSWKVPTLLALGLFVCFYAYNFIRDVLQPYIRKDENKFYKMPLSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFFAMLHALYSFCLPLRRSHRYDLVNLAVKQVLANKSRLWVEEEVWRMEIYLSLGVLALGMLSLLAVTSIPSIANSLNWKEFSFVQSTLGFVALMLSTMHTLTYGWTRAFEENHYKFYLPPTFTLTLLLPCVIILAKGLFLLPCLSHRLTKIRRGWERDGAVKFMLPAGHTQGEKTSHV", "text": "FUNCTION: Endosomal ferrireductase required for efficient transferrin- dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Also mediates reduction of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP (By similarity). May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the STEAP family."}
+{"protein": "MGSDDLSAGDKIQKGFQINYMILRDADTGKVIWQENKDFSAPDVEHEARVPVKILDMRAVSREINFSTIESMENFRLDQKVLFKGRIMEEWFFEMGFVGANTTNTWQSTIEAAPESQMMPAKVLNGNVTIQTSFYDNEILITKSVVRLYYI", "text": "SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the PDE6D/unc-119 family."}
+{"protein": "MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAAMSLLQQLEAIESTLLEKEADRNSRQKRCNGENVPCGPNHSTCCSGLSCEETFGYGWWYDTPFCVKPSKG", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 06 (ICK-Trit) subfamily."}
+{"protein": "MSDSKEPRLQQLGLLEEEQLRGLGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLLVQVSKVPSSISQEESRQDVIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKMQEIYQELTRLKAAVGELPEKSKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCRRCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNEEGTWQWVDGSPLLPSFNQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA", "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": "MLSPNDKMLGKLDPFYQPSVSKQKTSAEIISEARNALRTVRTQRPFTPQEAQRKLFGPASSRTSENRPPSSFSLHASSFESSDSRPISGTRLSPLELKPKVPASPTREEDSCFSFPKPPVDPAKIRRVSNARARLFRAASQRALLPDRSLPPSDSKKTVESKETVMMGDSMVKINGIYLTKSNAICHLKSHPLQLTDDGGFSEIKEQEMFKGTTSLPSHLKNGGDQGKRHARASSCPSSSDLSRLQTKAVPKADLQEEDAEIEVDEVFWNTRIVPILRELEKEENIETVCAACTQLHHALEEGNMLGNKFKGRSILLKTLCKLVDVGSDSLSLKLAKIILALKVSRKNLLNVCKLIFKISRNEKNDSLIQNDSILESLLEVLRSEDLQTNMEAFLYCMGSIKFISGNLGFLNEMISKGAVEILINLIKQINENIKKCGTFLPNSGHLLVQVTATLRNLVDSSLVRSKFLNISALPQLCTAMEQYKGDKDVCTNIARIFSKLTSYRDCCTALASYSRCYALFLNLINKYQKKQDLVVRVVFILGNLTAKNNQAREQFSKEKGSIQTLLSLFQTFHQLDLHSQKPVGQRGEQHRAQRPPSEAEDVLIKLTRVLANIAIHPGVGPVLAANPGIVGLLLTTLEYKSLDDCEELVINATATINNLSYYQVKNSIIQDKKLYIAELLLKLLVSNNMDGILEAVRVFGNLSQDHDVCDFIVQNNVHRFMMALLDAQHQDICFSACGVLLNLTVDKDKRVILKEGGGIKKLVDCLRDLGPTDWQLACLVCKTLWNFSENITNASSCFGNEDTNTLLLLLSSFLDEELALDGSFDPDLKNYHKLHWETEFKPVAQQLLNRIQRHHTFLEPLPIPSF", "text": "FUNCTION: Required for sperm flagellum axoneme organization and function (By similarity). Involved in axonemal central pair complex assembly and/or stability (By similarity)."}
+{"protein": "MLDFAQLPPEVNSALMYAGPGSGPMLAAAAAWEALAAELQTTASTYDALITGLADGPWQGSSAASMVAAATPQVAWLRSTAGQAEQAGSQAVAAASAYEAAFFATVPPPEIAANRALLMALLATNFLGQNTAAIAATEAQYAEMWAQDAAAMYGYAGASAAATQLSPFNPAAQTINPAGLASQAASVGQAVSGAANAQALTDIPKALFGLSGIFTNEPPWLTDLGKALGLTGHTWSSDGSGLIVGGVLGDFVQGVTGSAELDASVAMDTFGKWVSPARLMVTQFKDYFGLAHDLPKWASEGAKAAGEAAKALPAAVPAIPSAGLSGVAGAVGQAASVGGLKVPAVWTATTPAASPAVLAASNGLGAAAAAEGSTHAFGGMPLMGSGAGRAFNNFAAPRYGFKPTVIAQPPAGG", "text": "SIMILARITY: Belongs to the mycobacterial PPE family."}
+{"protein": "MSGSHAPEGDCCLRQCRAQDKEHPRYLIPELCKQFYHLGWVTGTGGGISLKHGNEIYIAPSGVQKERIQPEDMFVCDINEKDISGPPPSKNLKKSQCTPLFMNAYTMREAGAVIHTHSKAAVMATLVFPGKEFKITHQEMIKGIKKCTSGGYYRYDDMLVVPIIENTPEEKDLKERMARAVNDYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDVAVSMKQAGLDPAQLPAGENGIV", "text": "FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily."}
+{"protein": "MPKRAAEDQKHPAETSSEDEYDESYLEEDSYAPDSPDDPTMEDDEEVPDTIDVDFEYFDFNKDIDYHAIGNLLRQLLDSDSTSFNLSELSDMILEQESCGTTIKTDGKESDPFAILTVINMSKHKDNKKGVIAALIDYFVARTQDLPELHKQMRKLLGPSSTSKVGLIISERLINMPVQVVPPMYKMLLDETKDQDFDYFLVLSKTFTEAETSVDEEDERPSKKNKKGPGYKPETYYFHPEDEVIQEKSTQYGSYAFKKASQEADSKRAFQEYGIFPQGHLMLFKAKDLEAIVAKMEVEFAP", "text": "FUNCTION: Involved in nuclear export, actin cytoskeleton organization and vesicular transport. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the BCP1 family."}
+{"protein": "MATVPKSNMGPTKAVPTPFGCIGCKLPKPDYPPALIIFMFCAMVITVVVDLIGNSMVILAVTKNKKLRNSGNIFVASLSVADMLVAIYPYPLMLYAMSVGGWDLSQLQCQMVGLVTGLSVVGSIFNITAIAINRYCYICHSLQYKRIFSLRNTCIYLVVTWVMTVLAVLPNMYIGTIEYDPRTYTCIFNYVNNPAFTVTIVCIHFVLPLIIVGYCYTKIWIKVLAARDPAGQNPDNQFAEVRNFLTMFVIFLLFAVCWCPVNVLTVLVAVIPKEMAGKIPNWLYLAAYCIAYFNSCLNAIIYGILNESFRREYWTIFHAMRHPILFISHLISDIRETWETRALTRARVRARDQVREQERARACVAVEGTPRNVRNVLLPGDASAPHSDRASVRPKPQTRSTSVYRKPASIHHKSISGHPKSASVYPKPASSVHCKPASVHFKPASVHFKGDSVYFKGDTVHYRAASKLVTSHRISAGPSTSHPTSMAGYIKSGTSHPATTTVDYLEPATTSHSVLTAVDLPEVSASHCLEMTSTGHLRADISASVLPSVPFELAATPPDTTAIPIASGDYRKVVLIDDDSDDSDCSDEMAV", "text": "FUNCTION: Does not bind melatonin. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MSQTAAHLMERILQPAPEPFALLYRPESSGPGLLDVLIGEMSEPQVLADIDLPATSIGAPRLDVLALIPYRQIAERGFEAVDDESPLLAMNITEQQSISIERLLGMLPNVPIQLNSERFDLSDASYAEIVSQVIANEIGSGEGANFVIKRTFLAEISEYGPASALSFFRHLLEREKGAYWTFIIHTGSRTFVGASPERHISIKDGLSVMNPISGTYRYPPAGPNLSEVMDFLADRKEADELYMVVDEELKMMARICEDGGHVLGPYLKEMAHLAHTEYFIEGKTHRDVREILRETLFAPTVTGSPLESACRVIQRYEPQGRAYYSGMAALIGSDGKGGRSLDSAILIRTADIDNSGEVRISVGSTIVRHSDPMTEAAESRAKATGLISALKNQAPSRFGNHLQVRAALASRNAYVSDFWLMDSQQREQIQADFSGRQVLIVDAEDTFTSMIAKQLRALGLVVTVCSFSDEYSFEGYDLVIMGPGPGNPSEVQQPKINHLHVAIRSLLSQQRPFLAVCLSHQVLSLCLGLELQRKAIPNQGVQKQIDLFGNVERVGFYNTFAAQSSSDRLDIDGIGTVEISRDSETGEVHALRGPSFASMQFHAESLLTQEGPRIIADLLRHALIHTPVENNASAAGR", "text": "FUNCTION: Involved in the biosynthesis of the antibiotic, phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control."}
+{"protein": "MKIIHTADWHLGKILNGKQLLEDQTYILDMFVEKMKEEEPDIIVIAGDLYDTTYPSKDAIMLLEQAIGKLNLELRIPIIMISGNHDGKERLNYGASWFEHNQLFIRTDFTSINSPIEINGVNFYTLPYATVSEMKHYFEDDTIETHQQGITRCIETIAPAIDEVAVNILISHLTVQGGKTSDSERPLTIGTVESVQKGVFDIFDYVMLGHLHHPFSIEDDKIKYSGSLLQYSFSEAGQAKGYRRVTINDGIINDVFIPLKSLRQLEIISGEYNDVINEKVHVKNKDNYLHFKLKNMSHITDPMMSLKQIYPNTLALTNETFNYNEENNTIEISEKDDMSIIEMFYNHITDKKLSDIQSKKIKNILENELRKED", "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": "MLTYGAPFNFPRWIDEHAHLLKPPVGNRQVWQDSDFIVTVVGGPNHRTDYHDDPLEEFFYQLRGNAYLNLWVDGRRERADLKEGDIFLLPPHVRHSPQRPEAGSACLVIERQRPAGMLDGFEWYCDACGHLVHRVEVQLKSIVTDLPPLFESFYASEDKRRCPHCGQVHPGRAA", "text": "FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. SIMILARITY: Belongs to the 3-HAO family."}
+{"protein": "MKAESSNESFIIGQRVHSLNDSRRVGTVKYVGDVEGYSGTWIGVDWDQDGDGKHNGSVNGVFYFNGRSQSSASFVRSQNLSRGITLLQALELRYRTISTKDEEDEMYVLSAGNRRVSIQLLGGDKIQDKLSRFEELTSASLSYLGVSSLGVSSDLGSILPNLKLLDLTGNLISDWEEIGALCEQLPALTTLNLSCNSLSSDIKSLPQLKNIRVLVLNNSGLSWTQVEILRRSLPGIEELHLMGNMISTITSTSSSDDQAFNSLRLLNLDDNCISDWSEVLKLSQLPCLEQLYLNKNKLSRIFQSVNGTESSEKGSDPFPSLSCLLLGANNIGDLASVDALNGFPQLVDIRLSENPISDPVRGGVPRFVLVARLTKVQVLNGSEVRAREKKDSEIRYVRMVMSKLNDKSGEIELLHPRFYELKKLHGIEDERASAENSGPKNIASGLISITLKCVGPSMGEKPHLTKKLPGSITVGKLKILSENFFKLKSIKPRLFLQEEGSPFPTALDDETATLLDVGICDGSTLLVDEES", "text": "FUNCTION: Essential tubulin-folding protein involved in the tubulin folding pathway. Not essential for cell viability. Probably involved in the binding of alpha-tubulin in the multimeric supercomplex. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TBCE family."}
+{"protein": "MARGVSYVSAAQLVPMLRDPRIAVVDVRDEERIYDAHIAGSHHYASDSFGERLPELAQATKGKETLVFHCALSKVRGPSCAQMYLDYLSEADEDSDVKNIMVLERGFNGWELSGRPVCRCKDAPCKGVCS", "text": "FUNCTION: Possesses phosphatase activity towards p-nitrophenyl phosphate in vitro. FUNCTION: Possesses arsenate reductase activity in vitro. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. May play a role in arsenic retention in roots."}
+{"protein": "MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLRMERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCRKGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRIALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRNGGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHLVAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAFWNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLLWDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS", "text": "FUNCTION: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone (PubMed:18238778). Active against both saturated and unsaturated long-chain fatty acyl- CoAs (PubMed:18238778). Protects cells against lipotoxicity (PubMed:30846318). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family."}
+{"protein": "MRIGVDYYPEHWDRQLWEKDAQLMKEIGVKVVRLAEFAWCKLEPIEGQYDFKWLDDVIEIFSVRNIEIVLGTPTNTPPLWLYEKYPDAIQVNESGERQFIGIRGHRCYNSSSMRKYTKAIVEAMTERYANNKAVIGWQIDNELDATHCCCDNCTEKFRGWLKNKYSTLENINKEYGNVVWSGEYSAWSQVTAPLGGSPFLNPSYLLDYNRFASDSMVEYIDFQREIIRKNCPSQFITTNTWFTGNLPNFYDAFENLDFVSYDNYPTTNEITDEEELHSHAFHCDLMRGIKKKNFWIMEQLSGTPGCWMPMQRTPKPGMIKGYSFQAIGRGAETVVHFRWRNAIIGAEMFWHGILDHSNVKGRRFYEFAELCREVNKINEEIPDYKINNEVAILYSSDQDFAFKIQPQVEGLYYLQQLKAFHNALIRLGVGTDIINWSESLNKYKVVIAPTLYLTDDNVTTELYRFVEAGGTLILTNRTGVKNMNNVCLMEQMPSNLKECAGVVVKEYDPIGHSIHTIKDEAGKVYQCKQWCDILEPTTAKVIATYNDDFYIDEAAVTVNKYKKGNVYYLGTVFNSDYYIELLSKILDEKELPYYKKLPYGLELSVLENENGKYLMVFNNSNEIKCFEGKHEGKSIIRNELDGKSFTLEPYGIEVLQLVE", "text": "FUNCTION: Involved in plant cell wall degradation in cooperation with cellulosome. Hydrolyzes both p-nitrophenyl-alpha-L-arabinopyranoside (pNPAp) and p-nitrophenyl-beta-D-galactopyranoside (pNPGp), with higher activity for pNPAp. Shows hydrolysis activity against p-nitrophenyl- beta-D-fucopyranoside (pNPFp), but not against p-nitrophenyl-alpha-L- arabinofuranoside (pNPAf), o-nitrophenyl-beta-D-galactopyranoside (oNPGp), p-nitrophenyl-beta-D-xylopyranoside (pNPXp), p-nitrophenyl- beta-D-glucopyranoside (pNPGLp), p-nitrophenyl-beta-D- cellobiopyranoside (pNPCp), p-nitrophenyl-beta-lactopyranoside (pNPLp) or p-nitrophenyl-alpha-galactopyranoside (pNPalphaGp). No detectable activity against arabinan or arabinoxylan, but activity against arabinogalactan can be detected. Increases degradation activity of alpha-L-arabinofuranosidase (ArfA) and endo-1,4-beta-xylanase (XynA) when corn fiber gum and corn stem powder are used as substrates. SIMILARITY: Belongs to the glycosyl hydrolase 42 family."}
+{"protein": "MAENNSKNVDVRPKTSRSRSADRKDGYVWSGKKLSWSKKSESCSESEAIGTVENVEIPLRSQERQLSCSSIELDLDHSCGHRFLGRSLKQKLQDAVGQCFPIKNCSGRHSPGLPSKRKIHISELMLDKCPFPPRSDLAFRWHFIKRHTVPMSPNSDEWVSADLSERKLRDAQLKRRNTEDDIPCFSHTNGQPCVITANSASCTGGHITGSMMNLVTNNSIEDSDMDSEDEIITLCTSSRKRNKPRWEMEEEILQLEAPPKFHTQIDYVHCLVPDLLQISNNPCYWGVMDKYAAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYSRSLHARIEQWNHNFSFDAHDPCVFHSPDITGLLEHYKDPSACMFFEPLLSTPLIRTFPFSLQHICRTVICNCTTYDGIDALPIPSPMKLYLKEYHYKSKVRLLRIDVPEQQ", "text": "FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. 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. Inhibits EGF signaling by mediating the degradation of the Tyr-phosphorylated EGF receptor/EGFR (By similarity)."}
+{"protein": "MDEDLVLALQLQEEWNLQVSEREPAQEPLSLVDASWELVDPTPDLQGLFVLFNDRFFWGQLEAVEVKWSVRMTLCAGICSYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINRLTGANITVYHTFHDEVDEYRRHWWRCNGPCQNSKPYYGYVKRATNRAPSAHDYWWAEHQKTCGGTYIKIKEPENYSKKGKGKTKLRKQPVSEAENKDKPNRGEKQLLIPFTGKGYVLGETSNFSSGKCITSHAINESQEPLSQDHSANALRPHSKTEVKFEQNGPSKKTSVASPVLSTSHQNVLSNYFSKVSVASSKAFRSVSGSPVKSLTVGDSTTKSVSAGSQRRVTSSRTSLRNSLKAMESTYVTVPQDAGGPEGKLPSKRPRIEDKTFFDLFFIKKEQAQSGGGDVTSSSHPPAAAQSPSGASGQSRVVHCPVCQDEVSETQINEHLDWCLERDSTQVKS", "text": "FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed- forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress following deubiquitination. CHEK1 stimulates recruitment to chromatin. SIMILARITY: Belongs to the Spartan family."}
+{"protein": "MATFPHFGTAAIHVGQEPEQWDMNQVVPPISLSSTYKQDNPGEPKGHDYSRAGNPTRDVLQKNLAALEDAKHCQVFSSGLAATSAIINLLKYGDHIVCSDDVYGGTQRYIRRVAVPNHGLEVDSVDLTDVQNLEKAIKPNTKMVWFESPSNPLLKVVDIAAVVQTAKKANPEIVVVVDNTFMSPYFQRPISLGADVVVHSITKYINGHSDVVMGAVITDNDEFQQHLFFMQLAVGAVPSPFDCFLVNRGLKTLHIRMRAHYENALAVAKYLEANDRIESVLYPALPSHPQHEVHEKQTKGMSGMISFYLKGELQESRAFLSALKVFTLAESLGGYESLAELPSIMTHASVPAETRIVLGITDNLIRISVGIEDLDDLVADLDQALKIAIPKV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
+{"protein": "MIQPISGPPPGQPPGQGDNLPSGTGNQPLSSQQRTSLESLMTKVTSLTQQQRAELWAGIRHDIGLSGDSPLLSRHFPAAEHNLAQRLLAAQKSHSARQLLAQLGEYLRLGNNRQAVTDYIRHNFGQTPLNQLSPEQLKTILTLLQEGKMVIPQPQQREATDRPLLPAEHNALKQLVTKLAAATGEPSKQIWQSMLELSGVKDGELIPAKLFNHLVTWLQARQTLSQQNTPTLESLQMTLKQPLDASELAALSAYIQQKYGLSAQSSLSSAQAEDILNQLYQRRVKGIDPRVMQPLLNPFPPMMDTLQNMATRPALWILLVAIILMLVWLVR", "text": "FUNCTION: Acts as a regulator of flagellar gene expression by modulating the protein level of the anti sigma factor FlgM upon sensing ring completion or hook elongation. Flk could inhibit FlgM secretion by acting as a braking system for the flagellar-associated type III secretion (T3S) system. Plays a role in hindering to flip the flagellar T3S specificity switch from the rod and hook-type substrates to filament-type substrates prior to hook-basal body (HBB) completion possibly by preventing interaction of FliK with FlhB (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the flk family."}
+{"protein": "MSRLVIVSNRVPVPDKGGIAPAGGLAVALKVALEEQGGGIWMGWSGKSSGEDEPAPLAQLQQGNITYALTDLTDTDVEEYYHGFANRVLWPICHYRLDLAEYGRKEMAGYFRVNRFFAHRLAPLVKPDDVIWVHDYPLIPLAAELRQMGLENRIGFFLHIPWPPADVLFTMPVHEEIMRGLSHYDVVGFQTDHDLENFASCLRREGIGDALGGGRLSAYGRIFKGGVYAIGIETAAFAEFAKKASTNSTVKKARESIERRSLIIGVDRLDYSKGLTQRIEAFERFILANPAQRGRVTYLQITPKSRSEVPEYEAMQRTVAEQAGRVNGALGAVDWVPMRYINRSVGRRVLAGLYRLGKVGLVTPLRDGKNLVAKEYVAAQDPDDPGVLVLSRFAGAARELQGALLVNPYDIEGTANAMARSLSMPLEERQERWTTMMDQLLEHDVSRWCRDFLNDLTASSDRCG", "text": "FUNCTION: Probably involved in the osmoprotection via the biosynthesis of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D- glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose- 6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. SIMILARITY: Belongs to the glycosyltransferase 20 family."}
+{"protein": "MQHNTFLPNDAVEEQKQNPYYGILRAVETDLRLGQRWCELKVHVLDIDLKTKRPLLSGIPVNGQLKDKLQYVLPLYLQETISIEFLSSVFDSMKKLSLPLVKDARGLSGDEFFLYLGIMCSDSTIVYYKITDGLIKPRQNDEE", "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 (By similarity). SIMILARITY: Belongs to the SEN15 family."}
+{"protein": "MANAGLQLLGFILASLGWIGSIVSTALPQWKIYSYAGDNIVTAQAIYEGLWMSCVSQSTGQIQCKVFDSLLNLNSTLQATRALMVIGILLGLIAIFVSTIGMKCMRCLEDDEVQKMWMAVIGGIIFVISGLATLVATAWYGNRIVQEFYDPMTPVNARYEFGQALFTGWAAASLCLLGGALLSCSCPRKTTSYPTPRPYPKPTPSSGKDYV", "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": "MNAIKTAVAAVTAAASLVAFSPAEAATATANLNVTANVGGACSIGSGAGGGTLNFGTYDPVVVNSALGVDLFGTGSLSVQCTLLSTAVITLGQGLYPAAGSTAAVPLRRMRNAASTDYLSYFLYMDVTRLIAWGNTSGTGLPFLGLGLPVPVQVYGTVPRGQNVPSGTYNDTVVATITF", "text": "FUNCTION: A late-developmental spore coat protein. SUBCELLULAR LOCATION: Secreted. Spore, perispore. Note=Secreted across the membrane to assemble on the spore surface."}
+{"protein": "MMQTVLAKIVADKAIWVEARKQQQPLASFQNEVQPSTRHFYDALQGARTAFILECKKASPSKGVIRDDFDPARIAAIYKHYASAISVLTDEKYFQGSFNFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDDQYRQLAAVAHSLEMGVLTEVSNEEEQERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSALMAHDDLHAAVRRVLLGENKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAPLQYVGVFRNHDIADVVDKAKVLSLAAVQLHGNEEQLYIDTLREALPAHVAIWKALSVGETLPAREFQHVDKYVLDNGQGGSGQRFDWSLLNGQSLGNVLLAGGLGADNCVEAAQTGCAGLDFNSAVESQPGIKDARLLASVFQTLRAY", "text": "FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. SIMILARITY: In the N-terminal section; belongs to the TrpC family. SIMILARITY: In the C-terminal section; belongs to the TrpF family."}
+{"protein": "MSRVEPIKKVSVVIPVYNEQESLPALLERTTAACKQLTQPYEIILVDDGSSDNSADMLTAAAEQPGSCVIAVLLNRNYGQHSAIMAGFNQVSGDLVITLDADLQNPPEEIPRLVKVAEEGYDVVGTVRANRQDSWFRKSASRIINMMIQRATGKSMGDYGCMLRAYRRHIIEAMLNCHERSTFIPILANTFARRTTEIEVLHAEREFGDSKYSLMKLINLMYDLITCLTTTPLRLLSVVGSVVALSGFLLAVLLIALRLIMGPEWSGGGVFTLFAVLFTFIGAQFVGMGLLGEYIGRIYTDVRARPRYFVQKVVGEQPNHNTQEEE", "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": "MNKALLPLLLCCFIFPASGKDAGWQWYNEKINPKEKENKPVPAAPRQEPDIMQKLAALQTATKRALYEAILYPGVDNFVKYFRLQNYWAQQAGLFTMSARKAMLAHPELDYNLQYSHYNGTVRNQLAADQAQQRQAIAKLAEHYGIMFFYRGQDPIDGQLAQVINGFRDTYGLSVIPVSVDGVINPLLPDSRTDQGQAQRLGVKYFPAMMLVDPKQGSVRPLSYGFISQDDLAKQFLNVSEDFKPNF", "text": "FUNCTION: Involved in F pilus assembly. SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MPRLCSSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLACIRACKPDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNGSSSSGVGGAAQKREEEVAVGEGPGPRGDDAETGPREDKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAQAFPLEFKRELTGERLEQARGPEAQAESAAARAELEYGLVAEAEAEAAEKKDSGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ", "text": "FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol. FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate. FUNCTION: [Met-enkephalin]: Endogenous opiate. SUBCELLULAR LOCATION: Secreted Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. SIMILARITY: Belongs to the POMC family."}
+{"protein": "MAKPLTDGERRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATRRDYYLALAHTVRDHLVGRWIRTQQRYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHSPEGVRWLDTQVVLAMPYDTPVPGYKNDTVNTMRLWSAKAPNDFKLHDFNVGGYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTSFETFPDKVAIQLNDTHPALAIPELMRILVDVEKVDWGKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLDIIYAINQRHLDHVAALFPGDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVRQSVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLAETIVERIGEDFLTDLSQLKKLLPLVGDEALIRDVAQVKQENKVKFSAFLEKQYGVKVNPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKKDPTQAFVPRTVMIGGKAAPGYHMAKKIIKLVTSIGDIVNHDPIVGDRLKVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVEALDRKGYNAHEYYNHLPELQQAVDQINSGFFSPREPDCFKDVVNMLLNHDRFKVFADYEAYVACQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYARDIWGAEPPALQTPPPSLPRD", "text": "FUNCTION: Glycogen phosphorylase that regulates glycogen mobilization. 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. SIMILARITY: Belongs to the glycogen phosphorylase family."}
+{"protein": "MTSRDLGSHDNLSPPFANSRIQSKTERGSYSSYGRENVQGCHQSLLGGDMDMGNPGTLSPTKPGSQYYPYSSNNARRRPLHSSTMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYSSSKPAASTFSSSFFMQDGHHSSDPWSSSSGMNQPGYGGMLGNSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGTGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAVPGGHGDMHGIIGPSHNGAMGSLGSGYGTGLLSANRHSLMVGAHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITRSRSSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDTANHMGQM", "text": "FUNCTION: Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'- CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Interacts with the CCAAT displacement protein (CDP2) to bind the tyrosine hydroxylase enhancer. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLLSKFGSLAHICSPASMDHLPVKILPPVKVEKEPFDKVYQVGSVLGSGGFGTVYAGSRTADGLPVAVKHVVKERVTEWGTIGGVMVPLEIVLLKKVGSGFRGVIKLLDWYERPDGFLIVMERPELVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYGCGVVHRDIKDENLLVDLRTGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLYFRRRISPECQQLIKWCLSLRPSDRPTLEQIFDHQWMHKSEVVKSEDCDIRLRTLDTDVSSTSSSNESL", "text": "FUNCTION: Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis and promote cell survival and protein translation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily."}
+{"protein": "MGKKRTKGRSAPDTVASESAEPVCRHLRKGLEQGNLKKALVNVEWNICQDCKTDNKVKDKPEEEAEDPSVWLCLKCGHQGCGRDSQEQHALKHYTTPRSEPHYLVLSLDNWSVWCYKCDEEVKYCSSNRLGQVVDYVRKQAGVRTSKPAEKNNGHIELENKKLEKESKNEQEREKSENLAKETIPMDSASQITVKGLSNLGNTCFFNAVMQNLSQTPVLRELLKEVKMSGTIVKIEPPDLALTEPLEVNLEPPGPLTLAMSQFLSEMQENKKRVVTPKELFSQVCKKATRFKGYQQQDSQELLRYLLDGMRAEEHQRVSKGILKAFGNSTEKLDEEVKNKVKDYEKKKAIPSFVDRIFGGELTSTIMCDECRTVSLVHESFLDLSLPVLDDQSGKKSINDKNVKMTMEEEDKDSEEEKDDSYMKSRSDLPSGTSKHLQKKAKKQAKKQAKNQRRQQKIQERFLHFNELCATDYTEDNEREADTALAGEVEVDTDSTHGSQEEATQIELSVNQKDLDGQESMIERTPDVQESPEDLGVKSANTESDLGIVTPAPECPRDFNGAFLEERTSGELDIINGLKNLNLNAAVDPDEINIEIPNDSHSAPKVYEVMNEDPETAFCTLANREAFSTDECSIQHCLYQFTRNEKLQDANKLLCEVCSRRQCNGPKANIKGDRRHVYTNAKKQMLVSLAPPVLTLHLKRFQQAGFNLRKVNKHIKFPEILDLAPFCTLKCKNVAEESTRVLYSLYGVVEHSGTMRSGHYTAYAKERTASCHLSNLVLHGDIPQDCEMESTKGQWFHISDTHVQAVPITKVLNSQAYLLFYERIL", "text": "FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes (PubMed:24034696). Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. Also deubiquitinates non-histone proteins, such as ribosomal protein RPS27A: deubiquitination of monoubiquitinated RPS27A promotes maturation of the 40S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the peptidase C19 family. USP16 subfamily."}
+{"protein": "MSSLEPATTAKVALITTKGPIEIELWAKEVPNITRVFIQNCLDKKYIGTTFNKVIKDYLVQTSKIKEPATLKLKDEFHSRLKFNKRGLVGAVHDDKRNSNNVDSLFITLKPTPEFNNNYVLFGKIMGDSIYNVVKINESELKSEETPMYPAEITDIKILVQYFDDLVESKEHIAEPAKKKAKKAKKPRVKLDYTLEDEEDTGFKMKSAHDLLSDSKLSNKLYANKKKGPSENNEKQKTIEKAQDSSMETKKIVPERPDYKGSEEIENETKITSSENMNHETKQDKPNYKAKLDRNPNIDSDYDSDLDLSSSESIDLFAFKQSNFQSS", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in pre-mRNA splicing (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27 subfamily."}
+{"protein": "MACRLFWASRVASHLRISVAQRGFSSVVLKDLKYADSHEWVKIDGNKATFGITDHAQDHLGDVVYVELPDVGHSVSQGKSFGAVESVKATSDINSPVSGKVVEVNEELTESPGLVNSSPYEQGWIIKVELSDAGEAEKLMDSDKYSKFCEEEDAKH", "text": "FUNCTION: The glycine decarboxylase (GDC) or 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 (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvH family."}
+{"protein": "MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPANKKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSKNYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSTHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKHNISQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKELKQKIAEVMAVMPSITYSAATSPLSPVSPHYSSKFVETSPSGLDPNASVYQPLKK", "text": "FUNCTION: Plays a role in the regulation of neuronal activity. SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Multi-pass membrane protein Nucleus membrane; Multi- pass membrane protein Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells. SIMILARITY: Belongs to the macoilin family."}
+{"protein": "MTSRRPLKDHLFNHLFRYHYPSWDQILQELDTLSVATLNPDCHVPALNVEKTLYLAKTIQILVQHRQSEPYLVPAARANLAYSLQQLYKLGNDKIRGVINGMLPLVDAGCIGFERELIKGLPRVLTLQYPHTAPLESEPPTADCTEWCLSHFVGASGRLRSEVRDILTTHNGTCAPSFQWMASVVKKFFLVETVIYEDFQDTDFNVQLNLCFFWTAVVQMYQRCIYEQKLVHIISTSLTLLKSTARSFFAWYDLYRPNLGSAALVKYTEHLIRALTPDCSDVELGELCSHLHHCKHALFSIQ", "text": "FUNCTION: Plays a role in the activation the host JNK/p38 pathways necessary for KSHV reactivation from latency and for viral replication. Induces transcriptional activation through host JUN of several ORF50- responsive promoters. SIMILARITY: Belongs to the herpesviridae BBRF1 family."}
+{"protein": "MALMLVLLFLAAVLPPSLLQDTTDEWDRDLENLSTTKLSVQEEIINKHNQLRRTVSPSGSDLLRVEWDHDAYVNAQKWANRCIYNHSPLQHRTTTLKCGENLFMANYPASWSSVIQDWYDESLDFVFGFGPKKVGVKVGHYTQVVWNSTFLVACGVAECPDQPLKYFYVCHYCPGGNYVGRLYSPYTEGEPCDSCPGNCEDGLCTNSCEYEDNYSNCGDLKKMVSCDDPLLKEGCRASCFCEDKIH", "text": "FUNCTION: This protein is supposed to help spermatozoa undergo functional maturation while they move from the testis to the ductus deferens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
+{"protein": "MNPNDNNLFGDIEQDNNPSFYGNQSFLRDPYGKSKQTCPPSVTSNGDPSITNDDNNSAHNNDLVSNSIVLSKKIEQMVNDPNLQINVISSERMINSSVVAYSIELSSFDDNRMIVKRRYSEFKSLRDNLQILFPTLVIPPIPEKHTLFTYLINSIDNSKELNIIETRKRCFANFLKDIIFDSNVALKSCVLVHKFLDPNYELCWNNAVNEPPVSLIPNNLLLANPVNPTDQNGLYSLLPIVNGFELNSNIDNISSLHKLNEDLHKLNEQVHVFELRKEQNERRHPSEPTTSLFTEIPISLIDFEKNFHQNIKVLTELNKLNSRSVKNFKSIINTLIELGGNLNNFSLQIHELNTDSNALSSLIEKFGSTIDSNFLGYEAFLMNDIIPEWQEPISQLVQYYLTSLQLIKFYKFKIIQYKLVYKLKFNKYQELANISTNFESQSKLKDLRNLDIDSPSINEAIKKIELNQKRLKNRKISSKKSWYGLFGGNSKPTFNLREDLPASTIPSEGTGIRRERTPLVSDENMSYPVNPSANLENTNIDINSHYKHKINQIEKELTKLDQLIDLTNTDISTLTQELNLNFNDFLVRVEKKWLVIMLEFIKNGKQLFKDNLQNWNECKVFINDL", "text": "FUNCTION: Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity). SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "MAQSEVNSVCVASDRAGDTGDQSDDSSDGSLFKTQCAPSPIQKQRHPTVKRVTLPASVETDSSSDSSIEPRPLTLKAIFERFKKKKRKKRKKRKYEPKLRPRGRPRGKPSGTRITRRSQIDAKQIKDKGAVFPFLESESGRKPLPWKKILTYEQAVARGFFHHIEKLKYEHHLKECLKQMHAGEDLEKEDLDSRRHKYMDDDGSLSPIEEPLTEDEATNPQAECDIKLVEDSCFIISSEFSRKRNLEQEKIKKESTFSKKAKDATHREKGHRRTLKGNEHVTIEEDSRPQPRPFAHLQSKVMKKGELEYLEVHHLCGLSQPL", "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": "MALPYLEAVLCFMILMYIFETYLDIRQHRALKLPTLPKPLVGVISGEKFERSRAYSLDKSKFHFIHEAVTILMDTTILYYRVLPWVWKKSGELATNAGLNAENEILHTLAFLAGVMIWSQITDLPFSLYSTFVIEAKHGFNKQTIWLFIRDMIKGILLSILLGPPIVAAIIIIVQNGGPYLAIYLWGFMFALSLVMMTIYPIVIAPLFNKFTPLPEGVLREKIEKLAASLSFPLKKLFVVDGSTRSSHSNAYMYGFFKNKRIVLYDTLIQQCSSEDEIVSVIAHELGHWKLNHTVYSFVAVQLLMFLQFGGYTLVRNSKDLFESFGFEDQPVIIGLIIFQHTIIPVQHLLSFCLNLVSRAFEFQADAFAKNLGYAPQLRAALVKLQEENLSAMNTDPWYSAYHYSHPPLVERLSALEDADSKKEN", "text": "FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48A family."}
+{"protein": "MERGMESEAFYGLSARGWDGSEVSLGSFRGCVIMIANVASSCKFAESNYKSFAGLLDKFYRKGLRILLFPCNQYLGQESRPIEEIRGEVSKKYSDRFVVFDKVDVFGKGAHPVFRHLVNTKNGKGRLGNFIKWNFTKFLVDRKGCVVKRFGPSDIVKEDDENLLRSIEDGENGMQNS", "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": "MFRLLSSCCSCLRTTEETRRNVTIPIIGLNNSGKTVLVEAFQKLLPSKTDHCMKSELTTLLLDEYELSIYDLNGDLKGREAWPNYYAQAHGLVFVLDSSDIRRMQEVKIILTHLLSDKRVAGKPILILANKQDKKKALMPCDIIDYLLLKKLVKENKCPCRVEPCSAIRNLERRNHQPIVEGLRWLLAVIDTCQLPPTSSISISKNNTGSGERCSSHSFSTRTGMSKEKRQHLEQCSIEAKPLKSILQKEGTRLWSKKNMSVTFALDEPMKEGECSRRMRAQNTTKLCYN", "text": "SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
+{"protein": "MFKPLLSAELFFNWTAKDFKDKTSFLKQACRVLQDKNCIKEEQIALTALKEREAQITTGIMSKLALPHMQSATVLKPFVAVFKVNNVDWQSLDNQPVKLIFLIGVPKDQGNLHLEFISQFSKLMLQDEFANKVPNIRSFNGLINLIDSFQQTAVASQPVVNEAAAQTEEPKDTNTQYDFVAVTACPTGIAHTFMAKEALEKFARDHNLKVKVETQGTDGIQNQLTESDLNNTKGIILACDRLIDLTRFYGHANVVEVSTTKAIKTPQTVYDQVVKKEGKLLGNKSSDSASQTELKETTEQLSFKDFHKRIYRAILSGVSYMLPFVVFGGILIAIAFLIDINNAGNAGKQFGSKDPIANWFKTLGGLSFGLIVPILSAYIAFALVGRQGLLPGFIVGLISAGKFLLNIDIVTGKIDWATESKVSSGFFGAIFGGLLAAVLIIVQQRYIYRKLPQALQGIKNILFIPLLGTLVTAALFWVINIPLIYLNYGLSKFLQIMDKPYLAPLLGLVIGLMMCFDLGGPVNKAAYVFGVVSLESQNSGTVAMASAILSGMVPPLGIAIAATIRKQCFDKEELPAAYACYVMGLSFISEGAIPFVAKRPKIMLAANLIGGAVCGVLTGAFALTIRAPHGGVFVFALLKTNLEGIAGNTLQIGAGVGLALLALIVSSFISAGIIIGHNLLVVRKKTKQLVNTNA", "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 fructose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MTCRVGLTEWRLAPSGAAAIRLAAAVGADGIQLDFGGPGRGVLVDGPGRAGQLRAVADEAGVDLLALAGNLLNDIGLTSQPAVVQPVLARLADTATELGVPLLIVPSFRRSAITDAMSFTRTAAALRWAVSLAEARGIVLASENVLPPARARQLVEEVGSPAFRLLLDTFNPVRYGLDPAWLATELRPWWADQIHLKDGPPDTGPSPLLGAGQGGVRRTLTALRGSPAPVRALVLENDYRDGHGARLRADLEWARRAAVNARESEKGKLT", "text": "FUNCTION: Involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose. Catalyzes the 2-epimerisation of 2-epi-5- epivaliolone 7-phosphate to yield 5-epi-valiolone 7-phosphate. SIMILARITY: Belongs to the hyi family."}
+{"protein": "MICEEAYHQQPQIQKEQMMTMDQRNNHQRKRSPLSSPSSPSSPSSPSSPKSPSFNNNEEERLEVVNLSGMALESLPNPSLNLAQICKLDLSNNHLQTIPESLTARLLNLIALDVHSNQIKALPNSIGCLSKLKTLNVSGNFLVSFPKSIQHCRSLEELNANFNKLIRLPDSIGFELTNLRKLSINSNKLISLPISITHLTSLRVLDARLNCLMILPDDLENLINLEILNVSQNFQYLSALPSSIGLLMNLIELDVSYNKITVLPESIGCMRRLRKLSVEGNPLVSPPIEVMEQNLQVVREYLTQKMNGGSPRSPSKKKSWGFGKLVKYGTFNGGSRSWNREEREGFIMPEYRSIDSLASPRYSGMFSPRRLFSPRTYFSR", "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": "MTMDGDSSTTDASQLGISADYIGGSHYVIQPHDDTEDSMNDHEDTNGSKESFREQDIYLPIANVARIMKNAIPQTGKIAKDAKECVQECVSEFISFITSEASERCHQEKRKTINGEDILFAMSTLGFDSYVEPLKLYLQKFREAMKGEKGIGGAVSATDGLSEELTEEAFTNQLPAGLITADGQQQNVMVYTTSYQQISGVQQIQFS", "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": "MGEQQQQVERQPDLPPGFRFHPTDEEIITFYLAPKVVDSRGFCVAAIGEVDLNKCEPWDLPGKAKMNGEKEWYFYCQKDRKYPTGMRTNRATEAGYWKATGKDKEIFRNHHMLIGMKKTLVFYKGRAPKGDKTNWVMHEYRLADASPPQPPPPPSSAEPPRQDDWAVCRIFHKSSGIKKPVQVPMQMPMQMQMPVAHQVPAANYQQQMAMASASIIQVPMQMQMPSMSDQLQMLDDFSTGSLMAPPPPPPSYSTLPGFPLQINGGAQQFVGNPSMYYQQQQQQQQQQMDMAAGGFVVSEPSSLVVSPQDAADQNNAADISSVACNMDATIWKY", "text": "FUNCTION: Transcription factor that acts redundantly with NAC20 to regulate the expression of genes involved in the biosynthesis of starch and storage proteins in grain. Directly binds to the promoters of starch synthase 1 (SS1), pullulanase (PUL), glutelin A1 (GLUA1), glutelins B4 and B5 (GLUB4 and GLUB5), alpha-globulin and 16 kDa prolamin, and activates their expression (By similarity). Possesses transactivation activity in yeast (PubMed:27872632). FUNCTION: Transcription factor that acts redundantly with NAC20 to regulate the expression of genes involved in the biosynthesis of starch and storage proteins in grain (PubMed:32989010). Directly binds to the promoters of starch synthase 1 (SS1), pullulanase (PUL), glutelin A1 (GLUA1), glutelins B4 and B5 (GLUB4 and GLUB5), alpha-globulin and 16 kDa prolamin, and activates their expression (PubMed:32989010). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLNLVLMMIERVGLIVILGFLLSHIKTFRRLLHKQDGYVDKLKLICIFSVFTIVSNYTGIEIAGNTIMNENWLQGVSSSSTIANTRIMGVGISGLLGGPIVGIGVGSIAGIHRYMLGGTTALSCAISSILAGVITGYIGYIFKKYNRTITPKFSAILSVFIVSLEMIMILLIVEDGMSIVKTIAIPMILVNSFGSFILLSMIQAILRQEENAKALQTHKVLRIADKTLPYFRQGLTEESCKHVAQIIHRFPGTDAVSLTDTEKILAHVGLASDHHIPSHSLITGLSKEVLHTGQIMKAKSREVINCQHEGCPLQAAIVIPLTSHGNTIGTLKLYFKNPNQLSRVEEELAEGLAKIFSTQLELGEAELQSKLLQDAEIKALQAQINPHFLFNAINTVSALCRTDVEKARKLLLQLSVYFRCNLQGARQLLIPLEQELNHVQAYLSLEQARFPNKYEVKMYIEDELKTTLVPPFVLQLLVENALRHAFPKKQPVCEVEVHVFEKEGMVHFEVKDNGQGIEEERLEQLGKMVVSSKKGTGTALYNINERLIGLFGKETMLHIESELNEGTEITFVIPKKVGEEEQIVKSISS", "text": "FUNCTION: Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MTEGIRARGPRSSSVNSVPLILDIEDFKGDFSFDALFGNLVNDLLPSFLDEEADSGDGHGNIAGVDGLTNGHLRGQSAPLSSAPFFPEVDGLLSLFKDACKELVDLRKQVDGRLNTLKKEVSTQDSKHRKTLTEIEKGVDGLFESFARLDGRISSVGQTAAKIGDHLQSADAQRETASQTIDLIKYLMEFNGSPGDLMELSALFSDDSRVAEAASIAQKLRSFAEEDIGRQGASAAAGNATPGRGLEVAVANLQDYCNELENRLLSRFDAASQRRDLSTMSECAKILSQFNRGTSAMQHYVATRPMFIDVEVMNSDIRLVLGDHGSQPSPSNVARGLSALFKEITDTVRKEAATITAVFPTPNEVMAILVQRVLEQRVTGILDKILAKPSLMSPPPVQEGGLLLYLRMLAVAYERTQELAKDLRAVGCGDLDVEDLTESLFSSHKDEYPEHERASLKQLYQAKMEELRAESQQVSESSGTIGRSKGASISSSLQQISVTVVTDFVRWNEEAITRCTLFSSQPATLAANVKAIFTCLLDQVSVYITEGLERARDSLSEAAALRERFVLGRRVAAAAASAAEAAAAAGESSFKSFMVAVQRCGSSVAIVQQYFANSISRLLLPVDGAHAASCEEMSTALSKAEAAAYKGLQQCIETVMAEVDRLLSSEQKSTDYRSTDDGIASDHRPTNACIRVVAYLSRVLESAFTALEGLNKQAFLTELGNRLEKLLLTHWQKFTFNPSGGLRLKRDLNEYVGFVKSFGAPSVDEKFELLGIIANVFIVAPDSLPTLFEGSPSIRKDAQRFIQLREDYKSAKLATKLSSLWPSLS", "text": "FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. SUBCELLULAR LOCATION: Cytoplasm, cytosol Secreted, extracellular exosome Note=Shuttles from the cytoplasm to the exocyst-positive organelle (EXPO) in the presence of EXO70E2. SIMILARITY: Belongs to the SEC10 family."}
+{"protein": "MKYQFNVAMACDGCKNAIDRVLTRLGVEDKSISVEKQEVIVTTDKPYELVEQTIKKTGKEVRSGKVLE", "text": "FUNCTION: Shuttles copper to the transport ATPase ccc2. Protects against oxygen toxicity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ATX1 family."}
+{"protein": "MNQKGRGLEILINEKQDGQWLFSVLKTALKASKPVIQDWMSHQQIKVNHESVLNNMIVKKGDRVFIDLQESEASSVIPEYGELDILFEDNHMLIINKPAGIATHPNEDGQTGTLANLIAYHYQINGETCKVRHVHRLDQDTSGAIVFAKHRLAHAILDQQLEKKTLKRTYTAIAEGKLRTKKGTINSPIGRDRSHPTRRRVSPGGQTAVTHFKVMASNAKERLSLVELELETGRTHQIRVHLASLGHPLTGDSLYGGGSKLLNRQALHANKVQAVHPITDELIVAEAPFPADMKNLCRTYFS", "text": "SIMILARITY: Belongs to the pseudouridine synthase RluA family."}
+{"protein": "MSGSNPKAATAGSQAGPGGLVAGKEEKKKAGGGVLNRLKARRQGPPHTPDDGSGAAVTEQELLALDTIRPEHVLRLNRVTENYLCKPEDNVYSIDFTRFKIRDLETGTVLFEIAKPCISDQDQDAEEESVDVDISVGRFVRYQFTPAFLRLRTVGATVEFTVGDRPVTGFRMIERHYFRERLLKTFDFDFGFCIPSSRNTCEHIYEFPQLSEDVIRLMIENPYETRSDSFYFVDNKLVMHNKADYAYNGGQ", "text": "FUNCTION: Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells (By similarity). SUBCELLULAR LOCATION: Cell projection, cilium Note=Enriched at the transition zone and extended into the proximal end of the cilium. SIMILARITY: Belongs to the PDE6D/unc-119 family."}
+{"protein": "MDETATSSEVTETFVSDPTTRQFEEDGHPPLETRHLNMIHEELEKLNISTDVINKMEVQLDLARADFRETQVQWSEKLKELSKQYSSQIAKARPFYELKIKERSLREESQKAAERFERATSILGIAKQQVSLTQESLSRQTSVLPECLEVLNHHIQRVREVEEERTAAESLHASKAHAMLHLAEKIRAMEKDNRYAIKKSRLYFEKRLEFTKILEAQKATILCLEAEVRQKKNDYTTSLRNLERISERIHEERSTGSLESAVSSDQEDQKSDFKSSESLPGNPPPYAPTAPPPYEDKYIIDKDDDSIVLNMIKTEQEEEGEKRNSRSLGSGVILLAQQLIGNGNSTEKHNITPPRHGEEADISYHTRPVGLSDGSDNSEVSSLASFNIGDDDTVSKMLMSHSELIKDIELATDRVGHILKPNIKSVSNAHE", "text": "FUNCTION: Guanine nucleotide exchange factor for Rab GTPase Rab-11.1 (By similarity). May spatially and temporally regulate the distribution of Rab-11.1 to target membranes during embryogenesis (PubMed:26506309). May play a role in cytokinesis, probably by targeting rab-11.1 to the cleavage furrows (PubMed:26506309). SIMILARITY: Belongs to the SH3BP5 family."}
+{"protein": "MFKPHVTVACVVHAEGKFLVVEETINGKALWNQPAGHLEADETLVEAAARELWEETGISAQPQHFIRMHQWIAPDKTPFLRFLFAIELEQICPTQPHDSDIDCCRWVSAEEILQASNLRSPLVAESIRCYQSGQRYPLEMIGDFNWPFTKGVI", "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), and hydrolysis of thiamine pyrophosphate (TPP) to thiamine monophosphate (TMP). Can hydrolyze other substrates such as MeO-HMP-PP, CF(3)-HMP-PP and MeO-TPP. Is also a non-specific nucleoside tri- and diphosphatase that releases inorganic orthophosphate. SIMILARITY: Belongs to the Nudix hydrolase family. NudJ subfamily."}
+{"protein": "MQFSGEGLFFHSPFNSPKKHMFSSSKGLFRGHPCPSIAAGQFCRLLCCPFDHPERVKRESENGSDSAEMVKRRKLEVGQGVARVAGDSSGGKLELPGARQALNQRDRPEIEGVGASPKTEGGRAEGAEKKEFASSQSSQKEQQETPHASATPQASVSPQTSAPPQHVSSSVSEDVLKQGKNGITSKSEKSSVKQPGSRDIYQPSSSREPPVSSIDTRTSSSPKSALEAVMTTSASPSQSRDGSRNTSASPSSSRDAEHLMPTTIFPCPATVPQRIAYLKAIHSALTDKRKLKFPKRAAILEELAAAKRSAGNYMVYTNECRVLVKSIKDGSWRGGKAGGTKTDSKTSGHITSSISNQLDMLASKTKPLLAQNGYPVNPDPLKSGLPSNIGIQHCDRCDKAFDVPKVDNYGSCKYHWARARMGGNSTMPEKFYPCCNQPVGMSEGCEEAPRHVYKLHDLNDLAFVIPFRTVSTSESLDTSTSTSTSTSATTSAPSAKSTKTASRPASTPTKSLTSSLDLEKSRQPFNKARRPRTIFNGPAVNQREPDITLETMKRGIGESRGQADSQERSSEPRERSARVREQPSGSCDQAGSLQTSVVAVDCEMLYTSLGMELCRVTCIDYHGKKTLDRVVRPTGRILDYNTRFSGISDINEPIITESGEKGDSISFEEAHRLILKLINKQTILVGHGLENDLIAMRLIHDRIIDTSILYPDFNPRYKTALKTLALKYLKRTIQTGEHDSMEDALAALDVVKCHLKG", "text": "FUNCTION: 3' to 5' exoribonuclease required for proper 3' end maturation of MRP RNA and of the U5L snRNA. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the REXO1/REXO3 family."}
+{"protein": "MIVVLKPGSTEEDIRKVVKLAESYNLKCHISKGQERTVIGIIGDDRYVVADKFESLDCVESVVRVLKPYKLVSREFHPEDTVIDLGDVKIGNGYFTIIAGPCSVEGREMLMETAHFLSELGVKVLRGGAYKPRTSPYSFQGLGEKGLEYLREAADKYGMYVVTEALGEDDLPKVAEYADIIQIGARNAQNFRLLSKAGSYNKPVLLKRGFMNTIEEFLLSAEYIANSGNTKIILCERGIRTFEKATRNTLDISAVPIIRKESHLPILVDPSHSGGRRDLVIPLSRAAIAVGAHGIIVEVHPEPEKALSDGKQSLDFELFKELVQEMKKLADALGVKVN", "text": "FUNCTION: Catalyzes the 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": "MATVTELKAVLKDTLEKRGVLGHLKARIRAEVFNALDDDREPRPSLSHENLLINELIREYLEFNKYKYTASVLIAESGQPVVPLDRQFLIRELNAFEESKDNSIPLLYGILAHFLRGPPDGAQNVLLTESTLHPATKHLSWKPSRRPDDDHVRKDTGPRTTTEELPAAAQAVSR", "text": "FUNCTION: Involved in the biogenesis of cilia (By similarity). Required for the recruitment of PLK1 to centrosomes and S phase progression (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasmic granule Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Note=Localization to centrioles and pericentriolar satellites may be mediated by KIAA0753/OFIP. SIMILARITY: Belongs to the CEP43 family."}
+{"protein": "MNKKIIILIYLIFIKSIVGQNPVWIGGSGCNLFTDSSCWSPSTSPLTTDIVTMGVDSTQTVVDGDITITTLINNNLTLGGVEMSSTISLEIIDTSLIVSGAFSMATNSRLSLSLSDSYANSLVSGSATRNAVNVLMNLQSMQTLMVGSSFTMTGNSVLDVNRSISTINGVFTMNDDTSLFMYSKQNGDSKFTVGNSVLNDASSLNFQGQSFIFFNQTNLPSGLVLNDQSKIVAIDADNVKISGVVTLNDQSSIQLTSSRLYLDSLVTATTSSILVNNSTLSILQSIPTTFSPASAVFKGSVFTIKSNCTIQSPITMIDSVYSFNQSHTLASQFTGSNVYMIMDAAILNAGNYYDCSGCSLSMRNSIANFDSYENQGDLILSSSKLNSNAPITSNTGSIFGYYGELNQALTVESGSLGVYNEKTRLFVNGNVIVESGAKIQFYLSSPLDFSWLNTSGSLDVQSGTIIEIYVYIEILNNGSMEVIKTSNGFVTPLSTDNVKLYTYDPDNDVITDFSTTGGCEYSISITNTSVLVHTDYACQQAIITLGTDGISKGSLAGISVSMVALACFVSLGVWWKTSKKNDQRNDSQVLTNFSQNKSDDIDVERKL", "text": "FUNCTION: Component of a complex that acts as a quorum sensing protein regulating discoidin gene expression during growth and development. Its function in the complex is unclear as it has no ability to induce discoidin during growth and development by itself. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Secreted."}
+{"protein": "MVDKTHETEFSKKQLEASSSGHGGVLIDAEENGIHDQAEQRSCLICGDRATGLHYGIISCEGCKGFFKRSICNKRVYRCSRDKNCEMSRKQRNRCQYCRLLKCLQMGMNRKAIREDGMPGGRNKSIGPVQISDEEIERIMSGQEFKDEANMPEHTWGNNGDSDHSSPGNGVSDGNQPSPVSTLSSNRSVELNGYTTALREQYIGNAMAQHYQFLPHLFGYAAQPRSLYPQSHTLIGQLVAAEDLAPLGTPMLIEDGYRVTQVELFALLCRLADELLFRQISWIKKLPFFCDLSIEDYTRLLSATWQELILLACLTVYSAQVLGDLANVTHKYTPSDDELHSFSEDGMEVMEKLIYLFRKFHQLKVSNEEYACMKAINFLNQDIRGLTNVTQLEQLNKRYWYVCQDYTEYKYPHQPKRFPEIMMCLPEIRCIAGKLVNIPLEQLPLLFKAVLHSCKSSLSSYRTSSSPCVTKGTAPAN", "text": "FUNCTION: Probable orphan nuclear receptor. Binds to a response element containing repeats of the motif 5'-AGGTCA-3' (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR6 subfamily."}
+{"protein": "MACSRFEYVKSFEQDDSILPNVWIVIRIDGKKFHKFSKTHDFEKPNDENALNVMNAAATAVMQEFRDIVLAYGQSDEYSFVFRKETAAFKRRSAKLLTYVTSLFSSSYVMQWSKWMNLPLAYAPCFDGRVVLYPSEQNLKDYLSWRQADVHVNNLYNTAFWKLVLEKGLTNQQAEAKLRGTFSADKNELLFQEFGINYNNLPAMYRKGTILLRKRVILGEKSRQAVVPLHEDLISSQFWKEHTEILGKYVPGTYDAPQTFPRLVEMQINGKDDNEAEEPQNLAGTS", "text": "FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family."}
+{"protein": "MGQIVTFFQEVPHVIEEVMNIVLIALSVLAVLKGLYNFATCGLVGLVTFLLLCGRSCTTSLYKGVYELQTLELNMETLNMTMPLSCTKNNSHHYIMVGNETGLELTLTNTSIINHKFCNLSDAHKKNLYDHALMSIISTFHLSIPNFNQYEAMSCDFNGGKISVQYNLSHSYAGDAANHCGTVANGVLQTFMRMAWGGSYIALDSGRGNWDCIMTSYQYLIIQNTTWEDHCQFSRPSPIGYLGLLSQRTRDIYISRRLLGTFTWTLSDSEGKDTPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNKQAIQRLKAEAQMSIQLINKAVNALINDQLIMKNHLRDIMGIPYCNYSKYWYLNHTTTGRTSLPKCWLVSNGSYLNETHFSDDIEQQADNMITEMLQKEYMERQGKTPLGLVDLFVFSTSFYLISIFLHLVKIPTHRHIVGKSCPKPHRLNHMGICSCGLYKQPGVPVKWKR", "text": "FUNCTION: [Glycoprotein G2]: Forms the virion spikes together with glycoprotein G1 (PubMed:26849049, PubMed:35173332). The glycoprotein spike trimers are connected to the underlying matrix (PubMed:26849049). Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification (PubMed:31004664). FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP- C) (PubMed:35173332). Helps to stabilize the spike complex in its native conformation (PubMed:35173332). The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH- dependent glycoprotein-mediated cell fusion (PubMed:14555961). FUNCTION: [Glycoprotein G1]: Forms the virion spikes together with glycoprotein G2 (PubMed:26849049, PubMed:35173332). The glycoprotein spike trimers are connected to the underlying matrix (PubMed:26849049). Interacts with the host receptor. Mediates virus attachment to the host primary receptor alpha-dystroglycan DAG1 (alpha-DG) at the cell surface (PubMed:11967329, PubMed:27147735). This attachment induces virion internalization apparently through macropinocytosis (Probable) (PubMed:27147735). Following endocytosis, there is a pH-dependent switch from binding DAG1 to the host lysosomal receptor LAMP1 (PubMed:24970085, PubMed:27605678, PubMed:28448640). This latter binding triggers the dissociation of GP1, exposing the fusion subunit, GP2, such that fusion can occur (PubMed:24970085). Down-modulates host DAG1 (PubMed:17761532). SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane; Peripheral membrane protein Host endoplasmic reticulum membrane; Peripheral membrane protein Host Golgi apparatus membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane; Single-pass type II membrane protein Host endoplasmic reticulum membrane; Single-pass type II membrane protein Host Golgi apparatus membrane; Single-pass type II membrane protein Host cell membrane; Single-pass type II membrane protein. SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane; Single-pass membrane protein Host endoplasmic reticulum membrane; Single-pass membrane protein Host Golgi apparatus membrane; Single-pass membrane protein Host cell membrane; Single-pass membrane protein Note=Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly. SIMILARITY: Belongs to the arenaviridae GPC protein family."}
+{"protein": "MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALFEDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAETEAFLTYIEGVCVVWFTFEFLMRVVFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGAQPNDPSASEHTHFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPHHSTQSDTCPLAQEEILEINRADSKLNGEVAKAALANEDCPHIDQALTPDEGLPFTRSGTRERYGPCFLLSTGEYACPPGGGMRKDLCKESPVIAKYMPTEAVRVT", "text": "FUNCTION: Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient (PubMed:10482766, PubMed:14679187). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well (PubMed:10482766, PubMed:14679187). Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons (PubMed:10482766). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, axon Presynaptic cell membrane Note=Localizes in parallel fiber membranes, distributed on the perisynaptic and extrasynaptic membranes away from the active zones. SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC 1.A.1.2) subfamily. Kv3.1/KCNC1 sub-subfamily."}
+{"protein": "MLARLAAKRLLEIRQVFRQPTSQVTRSLSTALNYHLDSPDNKPDLPWEFSEANQSKVKEILSYYPSNYKQSAVIPLLDLAQQQNGGWLPVSAMNAVAKVIEVAPIRVYEVATFYSMFNRAKVGKYHLLVCGTTPCMIRGSRDIESALLDHLGVKRGEVTKDGLFSVGEMECMGCCVNAPMITVADYSNGSEGYTYNYFEDVTPEKVVEIVEKLRKGEKPPHGTQNPKRIKCGPEGGNKTLLGEPKPPQFRDLDAC", "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 Note=Matrix and cytoplasmic side of the mitochondrial inner membrane. SIMILARITY: Belongs to the complex I 24 kDa subunit family."}
+{"protein": "MPPPLQAQRLLLSHRRLPSPHRRRFTAVSSLPSSPAKTVAAAAAHAPSSILSIRESLLSGERTAAEITAEYLSRLRRTEPSVRSFIHVADAAAEREAEELDRRIATEGLDAVGPLAGVLVGVKDNLCTANMPSTGGSRILDGYQPAYDATAVRRLREAGAIVVGKTNLDEFGMGSTTEGSGFQVTTNPWDDSRVPGGSSGGSASAVSARQCVVSLGSDTGGSVRQPASFCGVVGLKPTYGRVSRFGLMAYASSLDVVGCFGSSVVDTATILSVIAGHDKMDSTSSSHDVSDYKSELVPLDLLESKPLNGMRIGIIQETLGEGVETGVISSIKDAASHLEQLGSVVEEVSLPSFSLGLPAYYILASSEASSNLSRYDGIRYGRQVSGDDLNELYGGSRANGLGHEVKMRILMGTYALSAGYYDAYYKRAQQVRTLVKKSFKEALERYDILVSPAAPSAAYKIGEKINDPLAMYAGDTMTVNVNLAGLPALVVPCGFVEGGSAGLPVGLQMIGSPFSEGNLLRIGHIFEQTLQNYSFVPPLLAES", "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 stroma. SIMILARITY: Belongs to the amidase family. GatA subfamily."}
+{"protein": "MELDDASRHGFGRMGFGCKHYRRRCRIRAPCCNDVFHCRHCHNESTKDGHELDRHAVESVICLVCDTEQPVAQVCYNCGVCMGEYFCSACKFFDDDVDREHFHCQDCGICRVGGKDNFFHCEKCGSCYSVSLRDKHCCIENSMKNNCPICYEYLFDSLRETSVLRCGHTMHLQCFHEMLKHDKFSCPICSMPIFDMDKFLRALDAEIEANMLHIDYMGKGWIVCNDCRDTTQVYARVAGHKCCHCQSHNTCRVAAPVLPA", "text": "FUNCTION: Possesses E3 ubiquitin-protein ligase activity in vitro. Possesses transactivation activity in yeast cells. May modulate abiotic stress responses by negatively regulating antioxidant enzymes-mediated reactive oxygen species (ROS) removal. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localizes predominantly in nucleus."}
+{"protein": "MVADEEAQLHAQAWDHALSYIKPTALSAAVELEIPDILENHGGPMTLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTTENLGPYMLMQATPVTRCPTGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMTAHARLTAAAIVRNYPAAFDGVQSVVDVGSRHGTAIGKLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPANIGKVMIVDAIINEDGEGDEFSGTRLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKHTIKNIKAMEFVIEAYP", "text": "FUNCTION: Flavonoid 4'-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:22923679). Catalyzes S-adenosylmethionine-dependent regioselective 4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and, with a lower efficiency, cirsimaritin (CIRM), sakuranetin (NAR7Me), ladanein (LAD) and genkwanin (GENK) (PubMed:22923679). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
+{"protein": "MAAQGAAAAVAAGTSGVAGEGEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPKHKQVKLSKK", "text": "FUNCTION: Histone acetyltransferase which may be involved in transcriptional activation (PubMed:12397079, PubMed:22020126). May influence the function of ATM (PubMed:15923642). As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac (PubMed:16227571, PubMed:16543150, PubMed:21217699, PubMed:22547026, PubMed:22020126). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852, PubMed:22547026). That activity is less specific than the one of the MSL complex (PubMed:20018852, PubMed:22547026). Can also acetylate TP53/p53 at 'Lys-120'. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the MYST (SAS/MOZ) family."}
+{"protein": "MSSTLREASKDTLQAKDKTYHYYSLPLAAKSLGDITRLPKSLKVLLENLLRWQDGNSVTEEDIHALAGWLKNAHADREIAYRPARVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDRFGDDEAFEENVRLEMERNHERYVFLKWGKQAFSRFSVVPPGTGICHQVNLEYLGKAVWSELQDGEWIAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAVTLDYMRLSGRSEDQVELVEKYAKAQGMWRNPGDEPIFTSTLELDMNDVEASLAGPKRPQDRVALPDVPKAFAASNELEVNATHKDRQPVDYVMNGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLAKAKLTPYLDELGFNLVGYGCTTCIGNSGPLPDPIETAIKKSDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYALAGNMNINLASEPIGHDRKGDPVYLKDIWPSAQEIARAVEQVSTEMFRKEYAEVFEGTAEWKGINVTRSDTYGWQEDSTYIRLSPFFDEMQATPAPVEDIHGARILAMLGDSVTTDHISPAGSIKPDSPAGRYLQGRGVERKDFNSYGSRRGNHEVMMRGTFANIRIRNEMVPGVEGGMTRHLPDSDVVSIYDAAMRYKQEQTPLAVIAGKEYGSGSSRDWAAKGPRLLGIRVVIAESFERIHRSNLIGMGILPLEFPQGVTRKTLGLTGEEKIDIGDLQNLQPGATVPVTLTRADGSQEVVPCRCRIDTATELTYYQNDGILHYVIRNMLK", "text": "FUNCTION: Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript. SIMILARITY: Belongs to the aconitase/IPM isomerase family."}
+{"protein": "MSDPEGETLRSTFPSYMAEGERLYLCGEFSKAAQSFSNALYLQDGDKNCLVARSKCFLKMGDLERSLKDAEASLQSDPAFCKGILQKAETLYTMGDFEFALVFYHRGYKLRPDREFRVGIQKAQEAINNSVGSPSSIKLENKGDLSFLSKQAENIKAQQKPQPMKHLLHPTKGEPKWKASLKSEKTVRQLLGELYVDKEYLEKLLLDEDLIKGTMKGGLTVEDLIMTGINYLDTHSNFWRQQKPIYARERDRKLMQEKWLRDHKRRPSQTAHYILKSLEDIDMLLTSGSAEGSLQKAEKVLKKVLEWNKEEVPNKDELVGNLYSCIGNAQIELGQMEAALQSHRKDLEIAKEYDLPDAKSRALDNIGRVFARVGKFQQAIDTWEEKIPLAKTTLEKTWLFHEIGRCYLELDQAWQAQNYGEKSQQCAEEEGDIEWQLNASVLVAQAQVKLRDFESAVNNFEKALERAKLVHNNEAQQAIISALDDANKGIIRELRKTNYVENLKEKSEGEASLYEDRIITREKDMRRVRDEPEKVVKQWDHSEDEKETDEDDEAFGEALQSPASGKQSVEAGKARSDLGAVAKGLSGELGTRSGETGRKLLEAGRRESREIYRRPSGELEQRLSGEFSRQEPEELKKLSEVGRREPEELGKTQFGEIGETKKTGNEMEKEYE", "text": "FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Plays an essential role for the assembly of ODA-DC and for the docking of ODA in ciliary axoneme. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme."}
+{"protein": "MSDTASSPFIDRPRSMLDEDSEFNSRQLISNLQFQISSLKTEKSLLQQNKESMAEKYEALLITKNEEVVSLQNDFDYVFKQRDELQSKYDNSQQINGKTVESLQVQLKDITERYDELKEEHEYLNSDFKKFCRDNNQVKSDLEFHINSKDQMNEKITSLQDENKSLCKTNDELIEKLNSISEQLVSNTQDKFSRNLQEQNSKLQRTNNQLQLKVDSLLQHRTSVELLRQKNITLTNKLSSLANLEEKCCKLEIENLELSNKFDTFFKTIEDSVNDDTSRTNESVVIEFMNKYKRLQNLNLVLQDKYNQSVTGVKNMQTELSNMQQKYSEAISKVESLNETVSTKTEFIDKLERQKLLNVKEIEYLRDSLKKLEELNLKRSKEETNDKSTEQYMTNLEKLVDEYRTEINTLQKQMSSQEIQSNVQSGSKRPRIIDNGIQNDFKSQVSVLEKENLKLLSTIKNLEYNNKTLGEKLQNLESLDNKKKELHILQLKSNPASQDQLIKQQTLDLLSKENQEMIETFVKNKSAHDMIPKSLFERQENDKLQLQTKIDQLNKRISRLRDIYSQKSRDILSVISKFFGYTIEFLPSPINSNDLSSRIKLVSKYMNNKDESNSAYLILDVNSKSLKANGSLEFKTLCEDLVTNWIREKDQIPCFLSALNLSIYDKYVS", "text": "FUNCTION: Central component of the spindle assembly checkpoint. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MAD1 family."}
+{"protein": "MLTRKIKLWDINAHITCRLCSGYLIDATTVTECLHTFCRSCLVKYLEENNTCPTCRIVIHQSHPLQYIGHDRTMQDIVYKLVPGLQEAEMRKQREFYHKLGMEVPGDIKGEACSAKQHLDPRNGETKADDNSNKETAEEKQEEDNDYHRSDEQVSICLECNSSKLRGLKRKWIRCSAQATVLHLKKFIAKKLNLSSFNELDILCNEEILGKDHTLKFVVVTRWRFKKAPLLLHYRPKMDLL", "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 (PubMed:28596365). 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 (PubMed:28596365). 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": "MKAFTYERVNTPAEAALSAQRVPGAKFIAGGTNLLDLMKLEIETPTHLIDVNGLGLDKIEVTDAGGLRIGALVRNTDLAAHERVRRDYAVLSRALLAGASGQLRNQATTAGNLLQRTRCPYFYDTNQPCNKRLPGSGCAALEGFSRQHAVVGVSEACIATHPSDMAVAMRLLDAVVETITPEGKTRSITLADFYHPPGKTPHIETALLPGELIVAVTLPPPLGGKHIYRKVRDRASYAFALVSVAAIIQPDGSGRVALGGVAHKPWRIEAADAQLSQGAQAVYDTLFASAHPTAENTFKLLLAKRTLASVLAEARAQA", "text": "FUNCTION: Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage. SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR", "text": "FUNCTION: This toxin binds to the surface of glioma cells, and inhibits their proliferation without having effects on normal brain cells. In this context, this toxin has been described as a chloride channel inhibitor (probably ClC-3/CLCN3) by causing its internalization via caveolae (PubMed:16520829). It has also been described to selectively interact with MMP2 (in complex with MT1-MMP (MMP14) and TIMP2), to inhibit its enzymatic activity and to decrease its presence at the cell surface (PubMed:12454020). Additionnally, annexin A2 that is expressed on the surface of multiple human tumor cell lines and vascular endothelial cells in culture may be another molecular target, since surface binding of this peptide to the pancreatic tumor cell line Panc- 1 is dependent on the expression of annexin A2 using siRNA-mediated specific knockdown of annexin A2 levels (PubMed:20018898). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride channel inhibitor family."}
+{"protein": "MEDAGTPCAPPPPAGSQTGAPPANLSSAPHNCSAEGYIYQDSIALPWKVLLAILLALLTLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYAVTGRWTLGQVVCDLWLSSDITCCTASILHLCVIALDRYWAITDAVEYSAKRTPKRAAVMIALVWVFSISISLPPFFWRQAKAEEEVSDCVVNTDHILYTVYSTVGAFYFPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSVNSRAPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCAS", "text": "FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. 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 inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MPKNSHHHRSSSVNSTKSRSTESTNKWKIPHYYRRSASGSTQASPDRNSSTGSCSTPVLPTMNVMSSPKKVLLEDPRDNHTKAKKSSRKKSGEMVFVNYTVQDTANENDTDLQTQPVSVPAPKAKLKKKSSKRRMLKIFGSSKNEHIEDIVEEQPMVLQMDSESKPLSGTPISESGIDASSLTTKRSYNSFLKHNRLNGKTPFSGNLSFPSLNMMGNTTDLPIDNNDFCSEKEVVPKSTHDPSLAKPPSRFTESETNSTPNLSSIPLMNTKNTRLKYNKVAPQSSDRQKSQESGLYHSTESFNFKDQNYSNNKSSLSLNSDLSTPHFAKHSPDSPRTSRSFNCGDSQSKVKLPEENDASIAFSKMFTRKRANTGGSTCSLASPTIAQTIQQSNIKVNKLPTQRTTSVGSLSSMSNRYSPIRVASPGRARSATRGSSLYRLSRDLNSLPSVTDLPEMDSTTPVNEIFLDGQPQHKSGSVKGGHRKKQESISDAQRIQHSNSYITTPSSSLVTPPYYMTGYTLPSSASASSTPNVLETHNMNFVPSTSTVTSYRPSSNFSSFDKEYSNENDASGEFSAFNTPMENIPALKGIPRSTLEENEEEDVLVQDIPNTAHFQRRDIMGMDTHRKDDSLDFNSLMPHGSTTSSSIVDSVMTNSISTTTSNATGNYFQDQDKYTLVNTGLGLSDANLDHFIRSQWKHASRSESNNNTGNRVSYSGSTPNNVDTTKTNLQVYTEFDFENPESFFHEQSKLLGEMGHSNNNSNSAINMNEPKSADTYIGNISPDTSATVSLGDLMGSNVSNNSERNFYDGHTFVPQYQANSSVENSNNQNAAPIANNDIDNNLQSFYFDNSN", "text": "FUNCTION: Dosage dependent suppressor of PKC1 deletion and MPK1 deletion. Involved in cell lysis."}
+{"protein": "MFVRSLFLALLLATIVAADIDFSTCARMDVPILKKAAQGLCITSCSMQNCGTGSCKKRSGRPTCVCYRCANGGGDIPLGALIKRG", "text": "FUNCTION: Exhibits antimicrobial activity against the Gram-positive bacteria B.subtilis IFO 3134, K.varians MAFF 118076 and S.aureus ATCC 6538P, the Gram-negative bacteria A.tumefaciens MAFF 1001, B.bacteriovorus MAFF 106101 and K.pneumoniae MAFF 519002, and the yeasts C.krusei MAFF 114085, K.thermotolerans MAFF 113848 and T.delbrueckii MAFF 113811. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MKCVLVATEGAEVLFYWTDEEFAESLRLKLQQSEDEEEELPVLEDQLSTLLAPVIISSMTMLEKLSDTYTCFSTENDNHLYVLHLFGEYLFVAINGDHSESEGDLRRKLCVLKYLFEVHFGLVTVDGQLIRKELRPPDLEERARVWKHFQRLLGTYSYLRDREQSFAVEAVERLIHPQLCEQSIETLERHVVQAINASPERGGEEVLHAFLLVHCKLLAFYSGHGASTLRPADLLALILLVQDLQPSPGTTEEEEEEEDSDSPQRRPKSSQNIPVQQARSQSTSVPTRSSRETDTDSISLPEEYFTPAPSPGDQSSGSLVWLDGGTPPSDALQMAEDTPEGLASHSPELPSPRRIFLDANIKENYCPLVPHTMYCLPLWPGINMVLLTKSPSTPLALILYQLLDGFSLLEKKLKEGQEAGSALRSQPFVADLRQKMDKFIKNRVGQEIQNTWLEFKSKAFSRSEPGSSWELLQVCGKLKRQLCVIYRLSFLVTAPSRGGPHLPQHLQDRAQKLMKERLLDWKDFLLVKSRRNVTMVSYLEDFPGLVHFIYVDRTTGQMVAPSLSPNEKMSSELGKGPLAAFVKAKVWALVRLARRYLQKGCTTLLFQEGDFRCSYFLWFENDMGYKLQMIEVPVLSDDSVPIGVLGGDYYRKLLRYYSKSHPSEPVRCYELLTLHLSVIPTDLLVQQASQLARRLGEASRVTLP", "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": "MGPNDHGFAYILIFLLLSPPTHANRDANRLFEDLIADYNKLVRPVSENGETLVVTFKLKLSQLLDVHEKNQIMTTNVWLQHSWMDYKLRWDPVEYGGVEVLYVPSDTIWLPDVVLYNNADGNYQVTIMTKAKLTYNGTVEWAPPAIYKSMCQIDVEFFPFDRQQCEMKFGSWTYGGLEVDLQHRDKHLEKEIEEDVEGVDGPTKEIVWVVDRGIDLSDYYPSVEWDILNVPGKRHSKRYPCCESPFIDITYEIHLRRKTLFYTVNLIFPSVGISFLTALVFYLPSDGGEKISLCISILISLTVFFLLLVEIIPSTSLVIPLIGKYLLFTMVLVTLSVVVTVVTLNVHYRSPTTHTMPKWMKRLFVDFLPKYLLMTRPQPPGHHSKPNRKFDSRASTFSIGVNHVLGQNSELLSPGLNSNREESSFTLPRDNSPVRSAVESVAYIADHLKNEEDDKQVIEDWKYISVVMDRIFLITFTFACAFGTVVIIARAPSIYDNTPALA", "text": "FUNCTION: Alpha subunit of nicotinic acetylcholine receptor (nAChR) (PubMed:15280391, PubMed:15990870, PubMed:20027209). Probably acts in cholinergic motoneurons to regulate presynaptic neurotransmitter release, thereby ensuring normal level of excitation of cholinergic motoneurons during locomotion (PubMed:20027209). Involved in nAChR sensitivity to nicotine and levamisole (PubMed:15280391, PubMed:15990870). 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."}
+{"protein": "MDGPDQIGPDVRPRRTFGDRVRRAARAFTTRDGLIGDYDYGFLFTPRLPFVKQKRRAAPFFGLEDKIPLVLALLLGLQHALAMLAGVITPPILLAGSSGANFGADESQYLVSTSLIVSGLLSAVQMFRLHVYKTRYYVGTGLVSVVGTSFATITVATGTFNQMYSTGYCPVDGSGNRLPCPKGYGALLATSCLCSLLEIGLSFMSSRLLKALFPPIVTGPTVFLIGASLIGNAMKDWAGGSGTCSSNPGNGALCPSADAPHPLPWGSAEFIGLGFLVFATIILCERFGSPIMKSCAVIVGLLVGCIVAAACGYFDRSGIDAAPVASFIWVKTFPLTIYAPLILPLLAVYMVIMMESIGDITATCDVSRLQVEGATFDSRIQGGVLGNGITCLLAGLCTITPMSVFAQNNGVIALTRCANRKAGYCCCFFLVVMGIFAKFAAALVAIPSSVLGGMTTFLFSSVAISGVRIMCSVDWTRRNRFILTASFAVGMAATLVPDWFSYFFTYSGDNHALEGLLQAVELVMANGFAVTGFLGLLLNLILPEDMEEDVVESEEDYEATTVVGMQGGSEPGSSGQNVKA", "text": "FUNCTION: Able to transport with low efficiency all natural purines as well as purine analogs. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family."}
+{"protein": "MRRLNGVDALMLYLDGGSAYNHTLKISVLDPSTDPDGWSWPKARQMFEERAHLLPVFRLRYLPTPLGLHHPIWVEDPEFDLDAHVRRVVCPAPGGMAEFCALVEQIYAHPLDRDRPLWQTWVVEGLDGGRVALVTLLHHAYSDGVGVLDMLAAFYNDTPDEAPVVAPPWEPPPLPSTRQRLGWALRDLPSRLGKIAPTVRAVRDRVRIEREFAKDGDRRVPPTFDRSAPPGPFQRGLSRSRRFSCESFPLAEVREVSKTLGVTINDVFLACVAGAVRRYLERCGSPPTDAMVATMPLAVTPAAERAHPGNYSSVDYVWLRADIADPLERLHATHLAAEATKQHFAQTKDADVGAVVELLPERLISGLARANARTKGRFDTFKNVVVSNVPGPREPRYLGRWRVDQWFSTGQISHGATLNMTVWSYCDQFNLCVMADAVAVRNTWELLGGFRASHEELLAAARAQATPKEMAT", "text": "FUNCTION: Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Upon expression in E.coli functions weakly as a triacylglycerol synthase, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Has no wax synthase activity. SIMILARITY: Belongs to the long-chain O-acyltransferase family."}
+{"protein": "MKSLLLTVTLSSLVATLQTYDDLPFISEEDKLSGVWFIKATVSQRREVEGETLVAFPIKFTCPEEGTLELRHTLASKGECINVGIRLQRTEEPGQYSAFWGHTLFYIYDLPVKDHYIIYCESHPFQKISQFGYLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRDRCIPIHDSAHQDHKC", "text": "FUNCTION: Transport of lipophilic molecules, possible pheromone- carrier. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MSGMIENGLQLSDNAKTLHSQMMSKGIGALFTQQELQKQMGIGSLTDLMSIVQELLDKNLIKLVKQNDELKFQGVLESEAQKKATMSAEEALVYSYIEASGREGIWSKTIKARTNLHQHVVLKCLKSLESQRYVKSVKSVKFPTRKIYMLYSLQPSVDITGGPWFTDGELDIEFINSLLTIVWRFISENTFPNGFKNFENGPKKNVFYAPNVKNYSTTQEILEFITAAQVANVELTPSNIRSLCEVLVYDDKLEKVTHDCYRVTLESILQMNQGEGEPEAGNKALEDEEEFSIFNYFKMFPASKHDKEVVYFDEWTI", "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. Involved in recruitment of Pol III to the preinitiation complex. Involved in the configuration of an initiation-competent form of RNA polymerase. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPC34/RPC39 RNA polymerase subunit family."}
+{"protein": "MHFLGLVVAFAPAALAQSAIWGQCGGTGWSGSTTCQSGLKCEKINDFYYQCIPGSDNGGGTTPDPGTPSPGNGNADATGLDAKIRAKGKIYFGTEIDHYHLSNNPLINIVKKDFGQVTNENSMKWDAIEPSRGQFTFSNADKVVDFAQANGKKIRGHTLLWYSQLPQWVKNIRDRATMTSVIENHVKTVVTRYKGKILHWDVVNEIFAEDGNMRNSEFYQVLGEDFVGIAFRAARAADPAAKLYINDYNLDIANYAKVTRGMVDHVNKWVSQGIPIDGIGSQAHLAKPGGWNPASGFPAALKVLAGANVKEVAITELDIDGAAANDYVTVVNSCLTTPKCVGITVWGVSDKDSWRSESNPLLFDRNYQPKAAYTAVSNALN", "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. Plays an important role in causing fusarium head blight (FHB) on cereal crops. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family."}
+{"protein": "MMSKLGVLLTICLLLFPLTAVPLDGDQPADQPAERKQNEQHPLFDQKRGCCRWPCPSRCGMARCCSS", "text": "FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin specifically inhibits mammalian Nav1.8/SCN10A sodium currents (IC(50)=2.11 uM) without inducing a shift in the current-voltage relationship of this channel (PubMed:32758497). In vivo, shows potent analgesic activity in a mice hotplate analgesic assay (PubMed:28219625). In addition, this toxin has better analgesic effects than Ziconotide, an analgesic drug (PubMed:28219625). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily."}
+{"protein": "MIIQTPSRIHMGLIDLNGSIGRVDGGIGLALEEPNIKIEGKESDDISIEFDKKLIEKYGEDYIKSVRDRVYNTAIKVLDVIGGEGVDLKILSLFPAHSGLGSGTQLSLAVGKLISKIYNKEMNAYNIAKITGRGGTSGIGIGAFEYGGFLIDGGHSFGKGKDKEDFRPSSASKGVKPAPIIFRHDFDWETILIIPKGEHVYGKKEVDIFKKYCPVPLNEVEKICHLVLMKMMPAVVEKNLDDFGEVINKLQYLGFKKVELSLQSDIVKDLINELHKDVYAGLSSFGPTIYAFGDKKLIVEKANDIFDKYGVYGEIIITKANNVGHKIW", "text": "FUNCTION: Catalyzes the condensation of 4-hydroxybenzoate (HB) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylphenol 5'-phosphate (beta-RFH-P) (PubMed:21634403). Also catalyzes the condensation of 4-aminobenzoate (pABA) with PRPP to produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P) (PubMed:15262968, PubMed:21634403). Only 4-hydroxybenzoate is known to be biosynthesized by methanogenic archaea, but 4-aminobenzoate can be used as substrate by growing methanogens when it is present in the growth medium (PubMed:21634403). SIMILARITY: Belongs to the beta-RFA-P synthase family."}
+{"protein": "MIRLNWLFRSSSVLLRSQVRLLHVGDANVLHSEVDKQSAEYKENAREMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHELYGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPDKLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYLARQIVSNLNLSATNSYNDQLMHSSQVNFQTATPPSAVEEPRYDAEELYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRKRAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQETKFGVFRM", "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 (By similarity). Vital for adult survival. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the AccD/PCCB family."}
+{"protein": "MGQLHFFFFPVMAHGHMIPTLDMAKLFASRGVKATIITTPLNEFVFSKAIQRNKHLGIEIEIRLIKFPAVENGLPEECERLDQIPSDEKLPNFFKAVAMMQEPLEQLIEECRPDCLISDMFLPWTTDTAAKFNIPRIVFHGTSFFALCVENSVRLNKPFKNVSSDSETFVVPDLPHEIKLTRTQVSPFERSGEETAMTRMIKTVRESDSKSYGVVFNSFYELETDYVEHYTKVLGRRAWAIGPLSMCNRDIEDKAERGKKSSIDKHECLKWLDSKKPSSVVYVCFGSVANFTASQLHELAMGIEASGQEFIWVVRTELDNEDWLPEGFEERTKEKGLIIRGWAPQVLILDHESVGAFVTHCGWNSTLEGVSGGVPMVTWPVFAEQFFNEKLVTEVLKTGAGVGSIQWKRSASEGVKREAIAKAIKRVMVSEEADGFRNRAKAYKEMARKAIEEGGSSYTGLTTLLEDISTYSSTGH", "text": "FUNCTION: Glucosyltransferase acting preferentially on aromatic substrates of the phenylpropanoid types. The best substrates are scopoletin and esculetin. Required for full resistance to virus. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "GLLDFVTGVGKDIFAQLIKQI", "text": "FUNCTION: Has hemolytic activity against human erythrocytes (HC50=14.3 uM). Has antibacterial activity against the Gram-positive bacterium S.aureus ATCC 25923 (MIC=64 uM) and the Gram-negative bacterium E.coli ATCC 25922 (MIC=64 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Ocellatin subfamily."}
+{"protein": "QELVDVEGKTVRNGGTYYLVPQLRPGGGGMEAAKVGNEDCPLTVVKSLDENSNGEPIRIASRLRSTFIPEYSLVNLGFADPPKCAPSPFWTVVKDQSERLPSIKLGEYKDSELDYPFKFERVYAASKMYAYKLLYCGSEDEEEEMMCKDIGVYRDQEGYQRLVVSKHNPLVVGFKKAESSTT", "text": "SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz- type inhibitor) family."}
+{"protein": "MQYTYQHIQDLVPGPTPQNFYGKIIFIKKKINQIVVLIKDETQSIYLRVIPKEDQELEFQLRQVVRVHRCKIQSILNSKEGIAQIGLFGCHLIAWSQSGKVDNPVIISSRSWTKSDEDSERLQTLRKLGKSRRKSGRKTSVDTMANKLIERREAMFADTFIKSLFNKIALSRKEHLSRNARELFYHRPGDIVETQNLLEIDDSWFNDENSEQFVQYVLNCTTCHVEYNHVEYAQNNIPTNCRFCQEAMESFHAAFRIRISIETYGVFLTIPLELIKTELDICEDWDSESNIVEEEEKVTRFKKNIQEKVRDASIVHIKGISSLLLIIMLNINSISLVNNITENKRILLQKSNVPSSLQLKILITPFVIVVVRFFGITWIYSGSSCIEEVLNLIDNCSRRR", "text": "FUNCTION: Telomeric DNA-binding protein, which binds to single-stranded C-rich repeat sequences, with high specificity to the 5'-GCCTAA-3' sequence (PubMed:18329362, PubMed:23390606). Repeat sequence binding can be at the 5' or 3' telomeric end (PubMed:18329362). May have a role in protecting the 5' end of the C-rich strand of the telomere (PubMed:23390606). Acts redundantly with pot-2 to negatively regulate telomerase-mediated telomere extension (PubMed:18329362, PubMed:23390606, PubMed:24297748). Also regulates telomere length by the telomerase-independent telomere maintenance pathway called ALT (alternative lengthening of telomeres) (PubMed:23390606, PubMed:22547822, PubMed:24297748). Through sun-1, anchors telomeres to the nuclear envelope in embryos (PubMed:24297748). SUBCELLULAR LOCATION: Nucleus Nucleus envelope Chromosome, telomere Note=More highly expressed in meiotic pachytene nuclei than in diakinesis-stage oocyte nuclei (PubMed:23390606). Also expressed in mitotic nuclei (PubMed:23390606). SIMILARITY: Belongs to the telombin family."}
+{"protein": "MKLVTIFLLVTISLCSYSATAFLINKVPLPVDKLAPLPLDNILPFMDPLKLLLKTLGISVEHLVEGLRKCVNELGPEASEAVKKLLEALSHLV", "text": "FUNCTION: Secreted cytokine-like protein (PubMed:12847263). Binds to the scavenger receptor MARCO (PubMed:12847263). Can also bind to pathogens including the Gram-positive bacterium L.monocytogenes, the Gram-negative bacterium P.aeruginosa, and yeast (PubMed:12847263). Strongly inhibits phospholipase A2 (PLA2G1B) activity (PubMed:24213919). Seems to have anti-inflammatory effects in respiratory epithelium (By similarity). Also has anti-fibrotic activity in lung (PubMed:24213919). May play a role in fetal lung development and maturation (PubMed:24213919). Promotes branching morphogenesis during early stages of lung development (PubMed:24213919). In the pituitary, may inhibit production of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the secretoglobin family. UGRP subfamily."}
+{"protein": "MDDERRVLCPENRGLAAYVLQKKQEYAEKPKGLSENLERTFVKGYRSVCDAKDPINTLKDLSQIKGFGKWMVKLMKGYFDTAVESSEQEDLPDNRAGKKANGKKRYIPQRNSVGYALLITLHRRTTNGKEFMRKQELIDAADANGLSHAPVGPEKGKGKAGLGHSKREWYSGWSCMTTLIQKGLVVKSSNPAKYMLTVEGREVANECILRSGLPDSVDILSVDEMDPTPQAKKTPNQNPTCSFTMREELPYVDPRCRAQSAIPSDILEKFTPFGYSKEQVVAAFREVSDGSGDKDPSTLWLSVMCHLRQAEVYNSCPDSRNSKKDSSGPFKSQIRQVDLEGSRAKKFRSCNDGSTLNPCSSGSSHAVKACSSSLASDGTKGITNIPRLPPLQFGETFEEAYDVILILDDREKFATKGSRSRNIVENICSEFNIKIEVRRLPVGDCIWIARHKYLETEYVLDFIAERKNVDDMRSSIRDNRYRDQKLRLQRSGFKKLIYILEGDPNHSDAAESIKTACFTTEILEGFDVLRTHGLGETLRKYGYLTKSIYQYYKLRVNDNDQSKGAASCPSFDSFVKRCQDLDKMTISDVFAIQLMQVPQVTEEIAIAVLDMYPTLLSLASAYSHLEADVSAQEEMLRNRSNNVICASASKNIFKLVWGE", "text": "FUNCTION: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks, nicked Holliday junctions and also intact Holliday junctions with a reduced efficiency. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. Plays a role in DNA repair and in genotoxic stress-induced homologous recombination (HR) in somatic cells. Mediates a subset of meiotic recombination events that are insensitive to crossover interference. Together with SEND1, essential for the resolution of toxic replication structures to ensure genome stability, and to maintain telomere integrity and replication (PubMed:26704385). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus. SIMILARITY: Belongs to the XPF family."}
+{"protein": "MCRFVDAIKSLLDESDITTLVALANRLSPFRVDYRRVVVGDALSVKPILVLEHEQPPCDGAWRSAAHINLGLGAAQQQHHPVPTRAVHGAAVGGVQCDGLASPPVSNNVMSDGTVDGDDDDLGYDQDTLYNQGTDYENEGGAVGQDGLPAPDAGLFQECMFSHRSASTPRAGGHGESYCQEVAQSSHAITCRELLERCILPNFEINHLENCESSTSGGIHHCLPDEHSGMTGLARNTPSASPVENSITVELDGALEIATDVRTGKFNTLRAAKRHRRNTSSLRLSSHDAGCVGDARSSAGVVKSPARRSTAVSDAALRKVKYAARTCIRADYFQFLEANLPRWVRDGIWGKEWSPNQTANVDGYENLQKAYWHVCRLDRQMRDDAIRSRMAMVLLHLEYENTCLSWKTCAHSGKKPVTKVGRGNISSLIDNIIENTHPEWRTADPGERSELRAKFHDRKRYGKRWWMLVKPLGSSILMLCSSKFAGMIKNTTVTAAMINEIKLAIQRSETGLMSLLSLANPIAESLFLDQGYDGHNAEQVLKALRAARLEVAPGEGVA", "text": "FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of aurovertins, fungal polyketides that exhibit potent inhibition of adenosine triphosphate synthase (PubMed:26340065). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the POU transcription factor family. Class-3 subfamily."}
+{"protein": "MDAQIENAIEIAWDPTSDQALKGQAFEFLNQLRTDPQAWQVCIAIFTRTPRTSPVVRLVCLEIVNHAVSSQILDGQGLGFLKQSLLEYVGRVYSGDAQDQVDPAHLQNKLTQTLTYLFVGLYKEGWESFIDDFLALAQKENNLPGVVMYLRILGSIHDEIADLMLSRSDNEARRNNDLKDLIRERDMQKIAQSWQDLLARYSHQNDGVVETTLKTIGKWVSWIDIHLVINQEMISLVLPLVGRTHAAGSGDKVRDAAVDTFTEIVAKKMKPSDKAEMITFLNLREIVSQLLASPPLNEWKGTPRYDTDLAEAVAKLVNTLVADVVRVLEDGKVDNDTRGKAEQLLRDFLPSLLRLFSDEYDEVCSTVIPSLTDLLTFLRKVGQLPPTYSEMLPPILNAIVSKMRYDETSNWGNEDEQTDEAEFQELRKKLQILQKSVASVDENLCIDLLSNLVANMFSTLEQQGSQMDWRDLDLALHEIYLFGELALPNTGLAQKSQPNPLAAERLAVMMSKMVESGIANYHHPAILLQYMEICTRYYSFFEDQQRYIPQVLENFVRLVHHDHVRIRTRSWYLFHRFVKTLRAQVGNVAKTVIESISDLLPIKAEVPGNDADDDMSSDESDHSADAVFSSQLFLYEAIGCISSTSATPPADQGLYARSVMEPLFSDMSVHIERAKAGDPQAVLQVHHIIMALGTLANGFADAHAAQQGKRPQPHEAVSNEFSRAAEAILIALNELNAIGDVRAACRSAFSRLLGVLGAAVLPQLPQWIEGLLSRSSSNDEMAMFLRLLEQVVYNFKSEIYNILDVLLTPLLQRVFSGLSDPINGTDDEIQLQELRREFVSFVQVILHNELGGVLVSASNQGTFESLISSIIDIAKTLTHGNLVASRVAFNVLSRMASQWGGPDVATIGENPMTTGAPAPAIPGFDQFMIEHFHGLCWTVLQDGGFRPNTDAQSRQILNEIAGIQQVIYSKTGDAFVNHLQGVTFPQLGIDGTEYLRLLTTSREKKPVVTWLLGLLKGRR", "text": "FUNCTION: tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Involved in pre-tRNA splicing, probably by affecting the interaction of pre-tRNA with splicing endonuclease (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the exportin family."}
+{"protein": "MKKDSTIISTCNEFSLSSVKTKRVYKNNHLLCSVSGGQDSIVSFFFLVNFLYLSKNFKLIKSKLSSFSVASKSAEKKRCFDCFFSLKKNKKINALINKEKKLSRLDLVFCQHFWQTQNFFCVEFLFQLTFFFDIPYTFVLSKNILVSENRARGWRKKTFSRLLKIQKLSTIVTGQTKTDTAEKSITNLLRGTSPKSFSLITKANSKTTSSFFCFRLFRPKTFYLTLTGNKRERKVNRRISFSFYRTQKKDSKKLRETRAPFFIEMASFSAFFGNTFQKKKSSNSFLLYKTRLSFSFCFSGETREHSINSLKPLQNRNRYHISKLVKFYKFPLTIDATNFSLNFSRNKIRHLFIPFIRFLFKLKFETLLLNFLYLVNLEHEQIENENLELKRVLNFLRINYLKKNFFSSNRRSFFVIQTGHKNNNVFPTKKKEKRWFYCNEIGISKIRKQCKIHEDPILETSLVIYFTSVLTTSRKYSLLQNLLYNYREIEINFRQISKLENSFW", "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: Plastid, chloroplast. SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family."}
+{"protein": "MKRRTFLAMSLALTFLPSVALADNIPVRVGYIADYWGTSITAIASEKGLWEKHGLDADTRVFTNGPIQVQALGAGSLDFGYIGPGALWLPASGKAKIVAINSVGFSDRVIAQEGFKSMADLKGKKIGVPEGTSGDMLLRLALGKAGMKLDDVQVIKMDPSTVVSAFASKQIDAAGIWYPLIGTIKEHVPGMVELAANSDFFPDKTFPSAFIARNEIVAENPEAVKRMIAVIEEAEDFRTANPEQSVDITAKFLKVDKANLETEAKNGKSLTSEELVKLTRDGSVNGWLSGMADMFVTFGKLKSPLDPKDYYLADYFTAK", "text": "FUNCTION: Probably part of an ABC transporter complex. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein SsuA/TauA family."}
+{"protein": "MAELGLNEHHQNEVINYMRFARSKRGLRLKTVDSCFQDLKDSRLVEETFTIDEVSEVLNGLQAVVHSEVESELINTAYTNVLLLRQLFSQAEKWYLKLQTDISELENRELLEQVAEFEKAEFVSSSKKPIIDITKPKLVPINEGGTTELLNKEILRLQQENEKLKSRLKTIEIQAVNALDEKSKLERVLQDLQLDQENQQDLLKAQDLDDLENTVATLRSEFQKTLNDKTENQKSLEENLAAAKHDLLRVQEQLSMAEKELEKKFQQTAAYRNMKEILTKKNDQIKDLRKRLAKYESED", "text": "FUNCTION: Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LZTFL1 family."}
+{"protein": "MTTPAGSGNGFGTVSWWGLSPALDLQAESPPVDPDSQSKTEHKIPELDALLLGSVDGRHMLRTLARAMLWPLRRFNFYVLENNLEAVARHMLIFSLALEEPEKMGLQERSETFLELWGNALLRPSVAAFLRAQASHLSNLVPEPDRLEELLPWLSLRPLKFRERDALEAVFRFWSGGEKGPEVFPMSRLWDSRLRHYLGSRYDARRGVADWDLRMKLHDRGAQVIHFHEFRRWRDTGVAFELRDLSAYHVPNRTMASGRLLSHRGERVAARGYWGDIATGPFVAFGIEADDKSLLRTSNGQPVKTASEITQHNVTELFRDVAAWRGPRAIKGNVEETKSPEPDAPAQEPFTIHFLPLDSSQTLHHKTCYRGRFQLLYVSCGMIHLLSPELGACVAPGGNLVVELARYLVDLRPKELKAFSDRVVEIAQAAGFAPHTGTKPSETFARFYKLGDSTRGGGDSAVESGPVPSKVLAPTPESINPPQADQAPSLEVMSPPKVDQTPPLEAMSPPEADQAPPLEAMSPPRADQIPPLEAMSPLQAEVVLPLEAISPPQADLAPPPEVISPVQEALAMSSAIAPLKHVT", "text": "FUNCTION: Required for the assembly of axonemal inner and outer dynein arms. Involved in preassembly of dyneins into complexes before their transport into cilia (By similarity). SUBCELLULAR LOCATION: Cytoplasm Dynein axonemal particle. SIMILARITY: Belongs to the DNAAF3 family."}
+{"protein": "MTRSSVLADALNAINNAEKTGKRQVLLRPSSKVIIKFLQVMQKHGYIGEFEYIDDHRSGKIVVQLNGRLNKCGVISPRFNVKIGDIEKWTANLLPARQFGYVILTTSAGIMDHEEARRKHVSGKILGFVY", "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 uS8 family."}
+{"protein": "MAAPESLRPRLCRLVRGEQGYGFHLHGEKGRRGQFIRRVEPGSPAEAAALRAGDRLVEVNGVNVEGETHHQVVHRIKAVEGQTQLLVVDKETDEELCRRQLTCTEEMAHRGLPPAHNPWEPKPDWACSGSLGSDTGHKDVNGPPRELRPRLCHLRRGPQGYGFNLHSDKSRPGQYIRSVDPGSPASLSGLRAQDRLIEVNGQNVEGLRHAEVVARIKAQEDEARLLVVDPETDEHFKRLRVVPTEDHVEGPLPSPVTNGTSLAQLNGGSVCSSRSDLPGSEKDNEDGSAWKRDPFQESGLHLSPTAAEAKEKARATRVNKRAPQMDWNRKREIFSNF", "text": "FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus. SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Nucleus. Apical cell membrane. Note=Nuclear, in a punctate pattern. Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes."}
+{"protein": "MIERYSRPEMSAIWTDENRFQAWLEVEILACEAWAELGVIPKEDVKVMRENASFDINRILEIEKDTRHDVVAFTRAVSESLGEERKWVHYGLTSTDVVDTALSYLLKQANDILLKDLERFVDIIKEKAKEHKYTVMMGRTHGVHAEPTTFGLKLALWHEEMKRNLERFKQAKAGIEVGKISGAVGTYANIDPFVEQYVCEKLGLKAAPISTQTLQRDRHADYMATLALIATSIEKFAVEIRGLQKSETREVEEFFAKGQKGSSAMPHKRNPIGSENMTGMARVIRGYMMTAYENVPLWHERDISHSSAERIILPDATIALNYMLNRFSNIVKNLTVFPENMKRNMDRTLGLIYSQRVLLALIDTGLTREEAYDTVQPKAMEAWEKQVPFRELVEAEEKITSRLSPEKIADCFDYNYHLKNVDLIFERLGLA", "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 (PubMed:15182182). Influences the affinity of glutamyl-- tRNA ligase for its substrates and increases its thermostability. SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily."}
+{"protein": "MKILVTGGGGFLGQALCRGLVERGHQVLAFNRSHYPELQVMGVGQIRGDLADPQAVLHAVAGVDAVFHNGAKAGAWGSYDSYHQANVIGTDNVIAACRAHGIGRLVYTSTPSVTHRATHPVEGLGADEVPYGEDFQAPYAATKAIAEQRVLAANDASLATVALRPRLIWGPGDQQLVPRLAERARQGRLRLVGDGSNKVDTTYIDNAALAHFLAFEALAPGAACAGKAYFISNGEPLPMRELVNQLLAAVGAPRVDKAISFKTAYRIGAICERLWPLLRLRGEPPLTRFLAEQLCTPHWYSMEPARRDFGYVPQVSIEEGLRRLKASSAA", "text": "FUNCTION: Involved in olefin biosynthesis. Catalyzes the reversible stereospecific NADPH-dependent reduction of 2-alkyl-3-oxoalkanoic acids to 2-alkyl-3-hydroxyalkanoic acids. In the oxidative direction, syn-2- decyl-3-hydroxytetradecanoic acid is the preferred substrate. In the reductive direction, (2R/S)-2-hexyl-3-ketodecanoic acid is accepted as substrate. SIMILARITY: Belongs to the 3-beta-HSD family."}
+{"protein": "MELSWETKSAIILITVTFGLVYAWRVLNWMWLKPKKIEKLLREQGLQGNPYRLLLGDAKDYFVMQKKVQSKPMNLSDDIAPRVAPYIHHAVQTHGKKSFIWFGMKPWVILNEPEQIREVFNKMSEFPKVQYKFMKLITRGLVKLEGEKWSKHRRIINPAFHMEKLKIMTPTFLKSCNDLISNWEKMLSSNGSCEMDVWPSLQSLTSDVIARSSFGSSYEEGRKVFQLQIEQGELIMKNLMKSLIPLWRFLPTADHRKINENEKQIETTLKNIINKREKAIKAGEATENDLLGLLLESNHREIKEHGNVKNMGLSLEEVVGECRLFHVAGQETTSDLLVWTMVLLSRYPDWQERARKEVLEIFGNEKPDFDGLNKLKIMAMILYEVLRLYPPVTGVARKVENDIKLGDLTLYAGMEVYMPIVLIHHDCELWGDDAKIFNPERFSGGISKATNGRFSYFPFGAGPRICIGQNFSLLEAKMAMALILKNFSFELSQTYAHAPSVVLSVQPQHGAHVILRKIKT", "text": "FUNCTION: Catalyzes the carboxylation of oleanolic acid at the C-23 position to form gypsogenic acid. Involved in the hemolytic saponin biosynthetic pathway. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MMNKVDQIIGYKKYEVKLPKDRQVKKNKSKGGNVDQIDTKREKDKMRAFGEERKKFLDKMAKNKKKNTSRKDREKPKEVEKENYKREDKRLKEQKKLSLAKEFRFKEPNSEAINQNTAAENGKPKPQTGLDFDIDHQTVSKIMIDQAIQTSSPLNVQLTELFNDNVLDVSKDSQFVLQDMEFTSWERRWSNCSTTSNATTVSSVPDPKYNINYNDITSFNSVALITEDLNISASSNGLHERGKKLLQQEMEYSNKVKNVTIGLERLCMDEKPVPDAGITMQQASRWSEFPTCCDQAAI", "text": "FUNCTION: Component of the MIS complex, a complex that mediates N6- methyladenosine (m6A) methylation on some mRNAs during meiosis and is required for sporulation. In the complex, mediates the entry of the MIS complex in nucleolus, where methylation takes place. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Mediates localization of the MIS complex to the nucleolus during the period of m6A mRNA accumulation."}
+{"protein": "MFLLLPFDSLIVSLLGISLTVLFTLLLVFIIVPAVFGVSFGIRKLYMKTLLKIFAWATLRMERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCRKGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCLLLSLRIALAFTGISLLVVGTTMVGYLPNGRFKEFLSKHVHLMCYRICVRALTAIITYHDRKNRPRNGGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHLVARRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAFWNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTRQAEEDAVQFANRVKSAIARQGGLVDLLWDGGLKREKVKDTFKEEQQKLYSKMIVGNHEDRSRS", "text": "FUNCTION: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone. Active against both saturated and unsaturated long-chain fatty acyl-CoAs. Protects cells against lipotoxicity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family."}
+{"protein": "MSFGTLYTHNPTPRSTTLIALAKLHNLDVKIIHAEKKNKEAFEELCRYNPLGQVPTFVGADGFVLSECIPLTLYCNDERSSLRILQWMSFANSDLFPAVGGVFLPRIGQRQIIQQDDGDSLRAMLQRCKYLDEHLKRSRYLVGESITIADFFAASLLMGAFAAFRRSMQERFGALCSWYDGVLEIGWFKKVAGGVPDLGLELEIPEDIKW", "text": "FUNCTION: Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213). SIMILARITY: Belongs to the GST superfamily."}
+{"protein": "MSFSVDELARIAIDLQSDIGHTDRFSRLITTLRQILGCDASALLRYEAHQFVPLAIDGLAQDVLGRRFALEGHPRLEAIARAGDVVRFPADSDLPDPYDGLIPGHESLKVHACVGLPLFAGQTLIGALTLDGMDADRFDSFSDEELRLIAALVAGALNNALLIARLEAQNVLPAQAVNYPLPERQEIIGLSGPMLQLKKEIDIVAASDLNVLISGETGTGKELVAKAVHQGSPRAANPLVYLNCAALPESVAESELFGHVKGAFTGAISNRSGKFEMADNGTLFLDEIGELSLALQAKLLRVLQYGDIQRVGDDRSLRVDVRVLAATNRDLRQEVVEGRFRADLYHRLSVFPLSVPPLRERESDVVLLAGYFCEQCRLRMGLARVILAEAARNRLQQWSWPGNVRELEHAIHRAVVLARATQAGDEVVLEPQHFQFAVAAPMLPTETAAAAPATGNINLREATDSFQREAISRALEANQGNWAATARALELDVANLHRLAKRLGLKGSPPGKSSAG", "text": "FUNCTION: Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54."}
+{"protein": "MKLLLLLTISASMLIEGLVNADGYIRGGDGCKVSCVINHVFCDNECKAAGGSYGYCWGWGLACWCEGLPADREWDYETDTCGGKK", "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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
+{"protein": "MATTSLASAFCSMKAVMLARDGRGMKPRSSDLQLRAGNAQTSLKMINGTKFSYTESLKKLPDWSMLFAVITTIFSAAEKQWTNLEWKPKPNPPQLLDDHFGPHGLVFRRTFAIRSYEVGPDRSTSIVAVMNHLQEAALNHAKSVGILGDGFGTTLEMSKRDLIWVVKRTHVAVERYPAWGDTVEVECWVGASGNNGRRHDFLVRDCKTGEILTRCTSLSVMMNTRTRRLSKIPEEVRGEIGPAFIDNVAVKDEEIKKPQKLNDSTADYIQGGLTPRWNDLDINQHVNNIKYVDWILETVPDSIFESHHISSFTIEYRRECTMDSVLQSLTTVSGGSSEAGLVCEHLLQLEGGSEVLRAKTEWRPKLTDSFRGISVIPAESSV", "text": "FUNCTION: Plays an essential role in chain termination during de novo fatty acid synthesis. High thioesterase activity for myristoyl-ACP. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the acyl-ACP thioesterase family."}
+{"protein": "MFNLYRSSLKNLKLPNINNNIKSNLVIRSYTTNINGNIKNDDDNNKFYSLSQFPYPSGALHMGHVRVYTISDCIARLKRMQGYDVIHPMGWDAFGLPAENAAIDKQVSPSEWTNLNISSMRDQLKLLNFQFDWDRELSTCNKEYYRWTQEIFLRLLKSGLAYRKSATVNWDPIDQTVLANEQVDAQGRSWRSNAIVEKKEMKQWFYKITSMADRLTDDLDQLPGWSDEIKNMQKEWIGRSYGHLIEFQSCAQKPLSNITVFTTRAETIYGVSFLAISPHHSEINQIRANLINDEKRLELDQYLKEIQEIKNKMGTQEDVENLKTFNTGLTFYQPITKKYIPLILSNFVHADYGTGAVMGVPSHNRSDYQVAKQQNLKLLPVLGIEREQQQQQQQQQQQQQLEIEEECYDYSNTGKLINSGQDTGIEFKEFIKRLEDQQLIKRQTNYRIHDWLISRQRYWGTPIPIIVCEKCGDVPVPSDQLPVELPIDIQFTGKGNLLNQLDHWKNVKCPCCGSQATRETDTMDTFVDSSWYFLRFLDSKNSQSIFSSELVNRFMPIDVYVGGIEHAILHLLYSRFITKFLKDQQLIDHSEPFKVLLAQGLVKSPTYRDSITNKPIHPSNVEFKTIKSNESGKSQQQTINKLTGNQVSVTIEKMSKSKLNGIDPKEIIDKYGSDTLKTYILFKAPPEKSLDWDTQGIEGCKKWLTRINVSIQSFLNQFDVIEGKEQHQHQQQQHQQPLPSSEFNEQQSKEVKDILFETHLTMNKVTESIDKHSFNTGIAALMELSNTLQKSSPQIKLTKEYYQSLRALTLMLFPFSPIFSQIHWKSLIDDLPQSCKSFYSENYSSFEQQSYGNSNDNDVFNQRWPKPTPSALVRDFNSLVIQFDGKTKGVESIPTSITDFSNFVQSNSKYLNRFKDKTIDQIFIGTTKTGNSINFTFKKK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
+{"protein": "MSLPVNFKIYNPLEALEASHGGGGGITPGSVTGGPGGSIAPGTITSFNLSPGTAASNINSGPDAAVLGSKISKADNTNFGVIEFDPTGDLVQTAAGSGVALLKPGSAANNINSGPPGSINSSQINGGPFLPLSGGTLTGNLVMGPGANITSNPPLNPTDVANKQYVDLSGQKAFAGWTLSSGAFAVSVPAGSTVNAFATTTAPIGNQVWTGADGVTITINGAGIITINNTNTFDTYYVCYFRGNGLLCSNASASPAVYFRFYDETNAANITVEQSLRLISPTIVPAVGGQPFNNYIDFSAFIKVLASSSLNISVKARNPGVDNCLLSTNVSSDVCQVMVIRQG", "text": "SIMILARITY: Belongs to the IIV-6 219L family."}
+{"protein": "MARLGRLLSVLGLVLCGATGLGLSAPPAPTPKKPIIGILMQKCHNKNMRALGKYYIAASYVKFLESAGARVVPVRLDLKNEEYEKLFKSINGVLFPGGSVNLMRSGYARVAKMFYNLSIKSFGEGDYFPVWGTCLGFEELIYLVSGESLLTLTDTVGIKLPLNFSRGTLQSRMFQNFPADLLLSLAVEPLTAHFHKWSLSVMNFTKNEKLKAFFSILTTNTDGNIDFISTMEGYRYPIYGVQWHPEKAPYEWGQLRGISHAPNAVKAAFYLAEFFVAEARKSNHHFESDVEETKALIYQYRPTYTGNVSSFQQSYIFD", "text": "FUNCTION: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Exhibits either endo- or exopeptidase activity depending upon the tissue of origin. When secreted, it acts primarily as an endopeptidase (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space Lysosome Melanosome Note=While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted. SIMILARITY: Belongs to the peptidase C26 family."}
+{"protein": "MEEPGATPQPYLGLVLEELRRVVAALPESMRPDENPYGFPSELVVCAAVIGFFVVLLFLWRSFRSVRSRLYVGREQKLGATLSGLIEEKCKLLEKFSLIQKEYEGYEVESSLEDASFEKAAAEEARSLEATCEKLNRSNSELEDEILCLEKDLKEEKSKHSQQDELMADISKSIQSLEDESKSLKSQIAEAKIICKTFKMSEERRAIAIKDALNENSQLQTSHKQLFQQEAEVWKGEVSELNKQKITFEDSKVHAEQVLNDKENHIKTLTGHLPMMKDQAAVLEEDTTDDDNLELEVNSQWENGANLDDPLKGALKKLIHAAKLNVSLKSLEGERNHIIIQLSEVDKTKEELTEHIKNLQTQQESLQSENIYFESENQKLQQKLKIMTEFYQEDEMKLYRKLTVEENYRIEEEEKLSKVEEKLSRATEQLETYRKLAKDLEEELERTVHFYQKQVISYEKRGHDNWLAARTAERNLSDLRKENAHNKQKLTETELKFELLEKDPNALDVSNTAFGREHAPNGPAPLGQRSSETRAFLSPQTLLEDPLGLSPVLPEGGGRGPRGPGNPLDHQITNERGEPSCDRLTDPHRAPSDTGSLSSPVEQDCKMMFPPPGQSYPDSALPPQREDRFYSNSERLSGSAEPRSFKMTSLDKMDGSMPSEMESSRNDAKDDLGNLNVPDSSLPAENEATGPGFIPPPLAPVRGPLFPVDTRGPFMRRGPPFPPPPPGTMFGASRGYFPPRDFPGPPHAPFAMRNIYPPRGLPPYFHPRPGFYPNPAF", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cTAGE family."}
+{"protein": "MINCGDVYKVIEAMVPLYVALILGYGSVKWWHIFTRDQCDAINRLVCYFTLPLFTIEFTAHVDPFNMNYRFIAADVLSKVIIVTVLALWAKYSNKGSYCWSITSFSLCTLTNSLVVGVPLAKAMYGQQAVDLVVQSSVFQAIVWLTLLLFVLEFRKAGFSSNNISDVQVDNINIESGKRETVVVGEKSFLEVMSLVWLKLATNPNCYSCILGIAWAFISNRWHLELPGILEGSILIMSKAGTGTAMFNMGIFMALQEKLIVCGTSLTVMGMVLKFIAGPAAMAIGSIVLGLHGDVLRVAIIQAALPQSITSFIFAKEYGLHADVLSTAVIFGMLVSLPVLVAYYAALEFIH", "text": "FUNCTION: Auxin transporter regulating intracellular auxin homeostasis and metabolism (PubMed:19506555, PubMed:20439545). Mediates the auxin transport from the cytosol into the lumen of the endoplasmic reticulum (PubMed:19506555). May also act as an auxin efflux carrier when located to the cell membrane (PubMed:24692422). PIN5 and PIN8 may have an antagonistic/compensatory activity (PubMed:22760640, PubMed:22990451). Involved in unfolded protein response (UPR) activation (PubMed:24180465). Involved in the control of vein patterning (PubMed:24304505). Promotes vein formation (PubMed:26560462). PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells (PubMed:26560462). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Along the root developmental zones, the localization gradually shifted from cell membrane localization in the meristematic epidermal cells to internal localization in the older elongating epidermal cells. Localizes to the cell membrane in the pavement and guard cells of the cotyledon and to internal compartments in the vascular tissues. SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family."}
+{"protein": "MIKLHEVPPEPVDPASLPHDVNAHSPEGDGNPDKRKKIFGIPYPFSRSSCRRFLWNCQKISVLPMALYFPLHAANTLITPAVSPDSAPDDVLMMVREILPSITTKLLVAGITLHVSAGVLLRIVNNWNKPRRNRHRHLKISAEQDLSQDSIGLTGGISGYLFGLYKTFRIPPQVISGYILVPVLIYHLLIMKWVPNSISTEVDFASIKQLLSSKNRWWKWLGGLVPLAILLESGVYHIGSGLCRYFGVRKMTSRKKWSTAINLLTLVGFVSLIRLMKEDSTKLGPNQFESIFKKIRLLLHVN", "text": "FUNCTION: Recruits the lipid transfer protein Vps13 to mitochondria thereby promoting vacuole-mitochondria contacts (PubMed:28864540, PubMed:30018089, PubMed:34830155). Involved in mitochondrial lipid homeostasis (PubMed:23781023, PubMed:28864540). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein."}
+{"protein": "MAEGHGDANGATAHTAADGGHKAPFPPFQKDTFASQLVSLLIAFVALYLIVSKIALPRVGSVLDERAKRIEDDFAAAQRLKGESDDALKAYETELAQARARAQAIGAETRERLNAASEAERKSLEEKLAVKLAEAEKTIAATRETAMSNVRGIAADAAAAIVQQLSGLVPDGKALDRAVDATLKGSQA", "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: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
+{"protein": "MEQANPLRPDGESKGGVLAHLERLETQVSRSRKQSEELQSVQAQEGALGTKIHKLRRLRDELRAVVRHRRASVKACIANVEPNQTVEINEQEALEEKLENVKAILQAYHFTGLSGKLTSRGVCVCISTAFEGNLLDSYFVDLVIQKPLRIHHHSVPVFIPLEEIAAKYLQTNIQHFLFSLCEYLNAYSGRKYQADRLQSDFAALLTGPLQRNPLCNLLSFTYKLDPGGQSFPFCARLLYKDLTATLPTDVTVTCQGVEVLSTSWEEQRASHETLFCTKPLHQVFASFTRKGEKLDMSLVS", "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. Modulates the kinetochore-bound levels of NDC80 complex. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. Note=The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex. SIMILARITY: Belongs to the CENP-O/MCM21 family."}
+{"protein": "MIKDDVVTGRVVRVSGPIVYAEGLSACSVYDVVDVGEASLIGEIIRLDESKAVVQVYEDDTGMRVGEKVTSLRRPLSVRLGPGLIGTIYDGIQRPLERLFQEDGAFLRPGARSQPLDGSVRWDFRPHCNERGEALCAGIPIAPGSVLGTVQETPSVVHTIMVPPDIRGSVLSSFKGAGAYTIDEEIGRTDLGEPLFLSQYWPVRRARPFSKKLAVCEPLVTGQRAIDVFFPLSKGGTAAIPGGFGTGKTMTQHAVAKWCDADIIVYIGCGERGNEMTDVLSEFPKLIDPRTGRSLMERTILIANTSNMPVSAREVSLYSGITLAEYYRDMGMHVAIMADSTSRWAEALRELSGRMEEMPAEEGFPAYLPTRLAEFYERAGRVETCVAREGSVSIIGAVSPLGGDFSEPVTQHTKRFIRCFWALDRELAHARHYPAIGWIDSYSEYAQEVSAWWSKYDPRAGALRAAALDLLRKEQRLQQIVRLVGPDALPGEDRLVLMVCEMIKGGFLQQNAFDPTDVFSCPEKQVQILRTIVDFHERAVVLLRAGISLSALSQLSCRELIVRMKTTYGNEDVHKMQKVYDTMCTEFDQLSVCAAARTQGGEKVE", "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 (By similarity). SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
+{"protein": "MAGNFWQSSHYLQWILDKQDLLKERQKDLKFLSEEEYWKLQIFFTNVIQALGEHLKLRQQVIATATVYFKRFYARYSLKSIDPVLMAPTCVFLASKVEEFGVVSNTRLISAATSVLKTRFSYAFPKEFPYRMNHILECEFYLLELMDCCLIVYHPYRPLLQYVQDMGQEDMLLPLAWRIVNDTYRTDLCLLYPPFMIALACLHVACVVQQKDARQWFAELSVDMEKILEIIRVILKLYEQWKNFDERKEMASILSKMPKPKPPPNSDGEQGTNGSQSSGYSQS", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in regulated gene 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. Binds to and activates cyclin- dependent kinase cdk8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily."}
+{"protein": "MAYELSTLQLSCVAFVAFMAVLVFRTRTRNLKQNVPPGPRPLPIIGNFFDLPPKGQPEYLHWFKHKDAYGPVSSINVMGTTLVIFHDKDAAHAVMGKKAQKTSARPQLNFAQLCGFENFLITHQYNDKYRLHRKMVHQEIGTKGLSAGFRPIQEQESIRFILQTFNRPDDILQHLKTLAAAIVLKITYGYSIERKGQDPLVELIEHAMENLSQAFVPLAWAVDSVPAIKYLPDWFPGMSYRKTARKWRAINEAAAELPYDFVKRQMAHKAHQPSYVSNLLEKHMIKSEDNKINVSAADEEAIKWTAVSLYAAGSDSTVAIIHSVICGLVMFPEVVTRAQEEIDRVVGSDRLPNFDDRTNLPYVDGIIKEAWRWNPVGPMGLTHKSEEDLVCGEYLIPKGSYLLPSLWWFLNDPKEYPEPRVFKPERYMEPFNHPDPSEIAFGYGRRSCAGRYFADASVYITVVQLLAVFNVRKARDDQGNEIPVTLQAIPGMVNRPAPFQFKVEPRSQHHIDLLRRIESEQIPEVSHASLLKPSTV", "text": "FUNCTION: Multifunctional cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283). Within the pathway, the multifunctional cytochrome P450 monooxygenase af510 acts as a 2,4,6- trichlorophenol monooxygenase that first performs the C-H hydroxylation at the bridgehead C5 position to yield 5R-hydroxyl-beta-trans- bergamotene (PubMed:24568283). Subsequently, a four electron oxidation initiated at C-9 coupled to cleavage of the cyclobutane C5-C8 bond of the bicyclo[3.1.1] core yields the epoxyketone intermediate 5-keto- cordycol (PubMed:24568283). An additional epoxidation reaction also catalyzed by af510 then furnishes the characteristic bisepoxide ketone 5-keto-demethoxyfumagillol (PubMed:24568283). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans- bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto- fumagillol, which is then stereoselectively reduced by the keto- reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy- seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MSTFRLALIQLQVSSIKSDNLTRACSLVREAAKQGANIVSLPECFNSPYGTTYFPDYAEKIPGESTQKLSEVAKESSIYLIGGSIPEEDAGKLYNTCSVFGPDGSLLVKHRKIHLFDIDVPGKITFQESKTLSPGDSFSTFDTPYCKVGLGICYDMRFAELAQIYAQRGCQLLVYPGAFNLTTGPAHWELLQRARAVDNQVYVATASPARDDKASYVAWGHSTVVDPWGQVLTKAGTEETILYSDIDLKKLAEIRQQIPILKQKRADLYTVESKKP", "text": "FUNCTION: Has omega-amidase activity (PubMed:19596042, PubMed:28373563). The role of omega-amidase is to remove potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively (PubMed:19596042). Can also hydrolyze gamma-monomethyl-alpha- ketoglutarate in vitro (PubMed:19596042). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family."}
+{"protein": "MLLSLLIIIPFLSSFFSFFSPRLHNNFPRWIALSGIIATLLVVIQIFFQENYHIFQIRHYPNWNCQLIVPWISRFGIEFNIALDGLSIIMLIFSSFLSIIAIICSWNEIKKNEGFFYFNFMLVFTGIIGVFISCDLFLFFCFWEIMLIPMYFLIALWSDKTEKKKNFLAANKFFLYSQTSGLILLSSILLLVFSHYYSTNILTFNYNLLINKPINIYVEYIVMIGFFLSFAIKMPIVPFHGWLPDIHSRSLSCGSVEIIGVLLKTAPYALLRYNLVLFPDSTKSFSLIAVFWGIISIFYGAWIAFSQTNIKRLIAYSSVSHMGLILIGIYSNNERALQGVVIQMLSNSLTVAALCILSGQIYKRFKTQDMSKMGGLWSCIYWIPGFSLFFSLANLGVPGTGNFIGEFLILSGVFEVFPLVSILATIGIVFSSIYSLNVIQKIFYGPCKQNIKVFFINKQEVWTIIALVFTLVFLGLNPQKIIDVSYNSIHNIQKEFNNSILKIRS", "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 4 family."}
+{"protein": "MATPGPGDPVDAKSGKAPLAQRIDPTREKLTPAQLQFMRQAQLAQWQKTLPQRRTRNIVTGLGIGALVLAIYGYTFYSVSQERFLDELEDEAKAARARALERASGH", "text": "FUNCTION: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the COA3 family."}
+{"protein": "MKLLLLLCLGLTLASSHKEAGQDVVTSNFDASKIAGEWYSILLASDAKENIEENGSMRVFVEHIRVLDNSSLAFKFQRKVNGECTDFYAVCDKVGDGVYTVAYYGENKFRLLEVNYSDYVILHLVNVNGDKTFQLMEFYGRKPDVEPKLKDKFVEICQQYGIIKENIIDLTKIDRCFQLRGSGGVQESSAE", "text": "FUNCTION: Binds pheromones, the pheromones are released from the saliva of males and affect the sexual behavior of females. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MARKTKPLTDTEIKAAKPKDADYQLYDGDGLTLLIKSSGSKLWQFRYYRPLTKQRTKQSFGAYPAVSLSDARKLRAESKVLLAKDIDPQEHQKEQVRNSQEAKTNTFLLVAERWWNVKKTSVTEDYADDIWRSLERDIFPAIGDISITEIKAHTLVKAVQPVQARGALETVRRLCQRINEVMIYAQNTGLIDAVPSVNIGKAFEKPQKKNMPSIRPDQLPQLMHTMRTASISMSTRCLFMWQLLTITRPAEAAEARWDEIDFNASEWKIPAARMKMNRDHTVPLSDGALAILEMMKPLSGGREFIFPSRIKPNQPMNSQTVNAALKRAGLGGVLVSHGLRSIASTALNEEGFPPDVIEAALAHVDKNEVRRAYNRSDYLEQRRPMMQWWADLVKAADSGSIVLTHLSKIRLVG", "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. Part of the cryptic P4-like prophage CP4-57, it excises the prophage when overexpressed, which also requires integration host factor (encoded by ihfA and ihfB) (PubMed:7511583). Overexpression of AlpA leads to excision of the CP4-57 prophage, which inactivates ssrA (the gene upstream of the prophage) that encodes tmRNA which is required to rescue stalled ribosomes in a process known as trans-translation (PubMed:7511582). SIMILARITY: Belongs to the 'phage' integrase family."}
+{"protein": "MTVVIPEYITPLIPWVRGIVGLVLIGVIFMGAMGAVWLERKLSADIQTRMGPCRVGKYGLLQLVADAIKLFTKEDLKPLNADSLLFNNANIFMLGSVFLMLVALPVGAVFINGVEYPLAVTQMDISVLYIEAVSALSIFGIFMVAYGSNNKYSLLGAFRNFARMVGYEVPLGITVISVAAMTGSLNIVDISTAQGLHWNIFLQPLGCFVFFVSLMADMGRLPFDQNESEEELIAGWITEYCGMRFGLGFFAEYIHMILGSFLVALLFLGGWNVPGFIANNSFFGIIVPTGFLIVKVVFVLMVIIGLRWAVPRFRIDQVVDLSWKKLLPLALLNLVWAVGLGLYLGA", "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": "MVVADAHTQGFSLAQYLQEQKTIVETALDQSLVITEPVTIYEAMRYSLLAGGKRLRPILCLAACEMLGGTAAMAMNTACALEMIHTMSLIHDDLPAMDNDDLRRGKPTNHKVYGEDIAILAGDALLSYAFEYVARTPDVPAERLLQVIVRLGQAVGAEGLVGGQVVDLESEGKTDVAVETLNFIHTHKTGALLEVCVTAGAILAGAKPEEVQLLSRYAQNIGLAFQIVDDILDITATAEELGKTAGKDLEAQKVTYPSLWGIEKSQAEAQKLVAEAIASLEPYGEKANPLKALAEYIVNRKN", "text": "FUNCTION: Catalyzes the sequential condensation of three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to yield geranylgeranyl diphosphate (GGPP). Thereby, is a key enzyme for the biosynthesis of terpenenoids. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MALKNKVQLITYPDSLGGNLKTLNDVLEKYFSDVFGGVHILPPFPSSGDRGFAPITYSEIEPKFGTWYDIKKMAENFDILLDLMVNHVSRRSIYFQDFLKKGRKSEYADMFITLDKLWKDGKPVKGDIEKMFLRRTLPYSTFKIEETGEEEKVWTTFGKTDPSEQIDLDVNSHLVREFLLEVFKTFSNFGVKIVRLDAVGYVIKKIGTSCFFVEPEIYEFLDWAKGQAASYGIELLLEVHSQFEVQYKLAERGFLIYDFILPFTVLYTLINKSNEMLYHYLKNRPINQFTMLDCHDGIPVKPDLDGLIDTKKAKEVVDICVQRGANLSLIYGDKYKSEDGFDVHQINCTYYSALNCDDDAYLAARAIQFFTPGIPQVYYVGLLAGVNDFEAVKKTKEGREINRHNYGLKEIEESVQKNVVQRLLKLIRFRNEYEAFNGEFFIEDCRKDEIRLTWKKDDKRCSLFIDLKTYKTTIDYINENGEEVKYLV", "text": "FUNCTION: Catalyzes the reversible phosphorolysis of sucrose 6(F)- phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6- phosphate. May be involved in a new pathway for the degradation of sucrose, which could become phosphorylated on its fructose moiety during uptake via a PTS system. To a lesser extent, can also reversibly act on sucrose in vitro (PubMed:24599311). Is also able to catalyze transglycosylation reactions in vitro (PubMed:26074151). SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose phosphorylase subfamily."}
+{"protein": "MFWVLVLLSFIVLIGDGMISEGAGLRPRYVDVGAIFSLGTLQGEVTNIAMKAAEEDVNSDPSFLGGSKLRITTYDAKRNGFLTIMGALQFMETDAVAIIGPQTSIMAHVLSHLANELSVPMLSFTALDPSLSALQFPFFVQTAPSDLFLMRAIAEMISYYGWSEVIALYNDDDNSRNGITALGDELEGRRCKISYKAVLPLDVVITSPREIINELVKIQGMESRVIIVNTFPKTGKKIFEEAQKLGMMEKGYVWIATTWLTSLLDSVNPLPAKTAESLRGVLTLRIHTPNSKKKKDFVARWNKLSNGTVGLNVYGLYAYDTVWIIARAVKRLLDSRANISFSSDPKLTSMKGGGSLNLGALSIFDQGSQFLDYIVNTNMTGVTGQIQFLPDRSMIQPSYDIINVVDDGFRQIGYWSNHSGLSIIPPESLYKKLSNRSSSNQHLNNVTWPGGTSETPRGWVFPNNGRRLRIGVPDRASFKEFVSRLDGSNKVQGYAIDVFEAAVKLISYPVPHEFVLFGDGLKNPNFNEFVNNVTIGVFDAVVGDIAIVTKRTRIVDFTQPYIESGLVVVAPVTKLNDTPWAFLRPFTPPMWAVTAAFFLIVGSVIWILEHRINDEFRGPPRKQIVTILWFSFSTMFFSHRENTVSTLGRAVLLIWLFVVLIITSSYTASLTSILTVQQLNSPIRGVDTLISSSGRVGFQVGSYAENYMIDELNIARSRLVPLGSPKEYAAALQNGTVAAIVDERPYVDLFLSEFCGFAIRGQEFTRSGWGFAFPRDSPLAIDMSTAILGLSETGQLQKIHDKWLSRSNCSNLNGSVSDEDSEQLKLRSFWGLFLVCGISCFIALFIYFFKIVRDFFRHGKYDEEATVPSPESSRSKSLQTFLAYFDEKEDESKRRMKRKRNDDLSLKPSRPI", "text": "FUNCTION: Glutamate-gated receptor that probably acts as non-selective cation channel (Probable). May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells (Probable). Could play a role in calcium unloading from the xylem vessels (PubMed:11158446). Acts as negative regulator of lateral root initiation and development (PubMed:23590882). May restrict primordia numbers and position along the root axis by a signaling process originating in the phloem (PubMed:23590882). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes to the plasma membrane. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family."}
+{"protein": "MVSKDQTSFNKRWTLGLLMLGLVIILWVLSSFLINLIFEDDSYRKPFFITYTNTAAFIFYLFPTAKAVVVNYKDTGRANVHRELIMEEEGTGSDSNRSVDMTSPLLTNLEAGTHANQKKRLTLYETIKLSAEFCILWFTANLVTNASLAFTSVASQTILSTTSSFFTLFIGAICHVESLSKSKVLGSFISFVGIIMVTKSDSHQRYQRHIADVSGDDNDAVQVLIGNLLALAGAVLYGVYSTLLKREVGDETRVNMKIFFGFVGLFNLLFLWPSLIVLDFFGWEPFSLPKDPKVVVIIFVNCLITFVSDFCWAKAMLLTSPLTVTVGLSITIPLAMFGDVIFKHKTMSALYLFGATLILGSFFIINKSSEEEHFENSITASNYESVEVPAANN", "text": "SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family."}
+{"protein": "MSASNVSLLHETSRQVAAGGSAGLVEICLMHPLDVVKTRFQVQRSVTDPQSYRTVRGSFQMIFRTEGLFGFYKGIIPPILAETPKRAVKFSTFELYKKFLGYMSLSPGLTFLIAGLGSGLTEAVVVNPFEVVKVGLQVNRNLFKEQPSTFAYARQIIKKEGLGFQGLNKGLTATLGRHGIFNMVYFGFYHNVKNIIPSSKDPTLEFLRKFGIGFVSGTMGSVFNIPFDVAKSRIQGPQPVPGEIKYRSCFKTMEMIYREEGILALYKGLVPKVMRLGPGGGVMLLVYEYTYAWLQENW", "text": "FUNCTION: Transports dicarboxylates across the inner membranes of mitochondria by a counter-exchange mechanism. Can transport 2- oxoadipate (2-oxohexanedioate), 2-oxoglutarate, adipate (hexanedioate), glutarate, and to a lesser extent, pimelate (heptanedioate), 2- oxopimelate (2-oxoheptanedioate), 2-aminoadipate (2-aminohexanedioate), oxaloacetate, and citrate. Plays a central role in catabolism of lysine, hydroxylysine, and tryptophan, by transporting common metabolite intermediates (such as 2-oxoadipate) into the mitochondria, where it is converted into acetyl-CoA and can enter the citric acid (TCA) cycle. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MSSPPPARKGFYRQEVTKTAWEVRAVYQDLQPVGSGAYGAVCSAVDSRTGNKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDESLDDFTDFYLVMPFMGTDLGKLMKHETLSEDRIQFLVYQMLKGLKYIHAAGVIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKILFKGNDHLDQLKEIMKITGTPPPEFVQKLQSAEAKNYMEGLPELEKKDFASVLTNASPQAVNLLERMLVLDAEQRVTAAEALTHPYFESLRDTEDEPKAQKYDDSFDDVDRTLEEWKRVTYKEVLSFKPPRQLGARVPKETAL", "text": "FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 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. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down- regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12- signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion Note=Mitochondrial when associated with SH3BP5. In skeletal muscle colocalizes with SNTA1 at the neuromuscular junction and throughout the sarcolemma. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
+{"protein": "MFVPCGESVPDLTNFTLLMPAVSVGNVGQLAIDLIISTLNMCKIGYFYTDCLVPMVGNNPYATEEENSNELSINTEVYSLPSKKLVVLQLRSIFIKYKSKSFCEKLLAWVESSGCARIIVLSSSHSYHRNDAQLRSTPFRYLLTPCLQKSVQNKIKSLNWLEMEKSRCIPEMSDSEFCIRIPGGGITKTLYDESCSKEIQMAVLLKFVSEGDNIPDAVSLVEYLNEWLQIIKPCNDGPMASALPWKIPSSWRLLFGSGLPPALF", "text": "FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. 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: Nucleus. SIMILARITY: Belongs to the PSMG2 family."}
+{"protein": "MKKSIALVLSIVLLAALFAVPASAGEQNTIRVIVSVDKAKFNPHEVLGIGGHIVYQFKLIPAVVVDVPANAVGKLKKMPGVEKVEFDHQAVLLGKPSWLGGGSTQPAQTIPWGIERVKAPSVWSITDGSVSVIQVAVLDTGVDYDHPDLAANIAWCVSTLRGKVSTKLRDCADQNGHGTHVIGTIAALNNDIGVVGVAPGVQIYSVRVLDARGSGSYSDIAIGIEQAILGPDGVADKDGDGIIAGDPDDDAAEVISMSLGGPADDSYLYDMIIQAYNAGIVIVAASGNEGAPSPSYPAAYPEVIAVGAIDSNDNIASFSNRQPEVSAPGVDILSTYPDDSYETLMGTSMATPHVSGVVALIQAAYYQKYGKILPVGTFDDISKNTVRGILHITADDLGPTGWDADYGYGVVRAALAVQAALG", "text": "FUNCTION: Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
+{"protein": "MEVVEAAAQLQTLKFGGSGQGSAAPQPPEDRREAPPPGVQPPPPAPSGRPPPPPAPSSDPGGRPPPPPAPNWDAGGRPPPPPAPNSDPPPGGAWVTGRNAAEPPPVLQASDSSDSDSDSETDSDSSSSSSSSSSSSSSCVSFPPVLSDGDEDFQLEKENKNFPLKTKDELLLNELPSVEELTVILPEDIALKPLGKVSSIIEQLVIIESVTNIPPVNEDTVIFKSDRQAAGKIFEIFGPVAHPFYVLRFNSSDHIESKGIKINDTMYFAPSMKDFTQYIFTEKLKQDRGSDASWKNDQEPPPEVLDFSDDEKEKEAKQRKKSQIQGRKKLKSELNESGEDFGEVHENWNAYSSSEHSKGYHHREFSRGFARGRYSRRSHGRPPPQQYYNSDHMASQESLGFTPQRQDNPVMPHYPFPPPMFDMHNFPLPPPPPPPPPPPPSMGWAAPSMASHPVLNLPYSMPPPPLPPPPPPPPPSPGENNSSHFGPYF", "text": "FUNCTION: RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by NOLA1/GAR1 to yield mature H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding with DKC1/NOLA4 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the cytoplasm and the nucleus. Absent from the nucleolus (By similarity). SIMILARITY: Belongs to the NAF1 family."}
+{"protein": "MATSAPVTSRTETLAKYLKLDQKGQIMAEYVWVDAAGETRSKSRTLPEKDYKAEDLPVWNFDGSSTNQAPGDNSDVYLRPCAVYPDPFRGSPNIIVLAECWNAGGTPNKFNFRHDCVKVMDTYAEDEPWFGLEQEYTLLGPDNRPYGWPTGGFPAPQGEYYCGVGTGKVVQRDIVEAHYKACLYAGIQISGTNAEVMPAQWEYQVGPCLGIEMGDQLWVSRFFLARITEEFGAKVSLHPKPIAGDWNGAGLHSNFSTKAMREEGGMKVIEEALKKLEPHHAECIAEYGEDNELRLTGRHETGSIDSFSWGVANRGTSIRAPRETAAKGYGYFEDRRPASNADPYRVTKALLQFSLA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family."}
+{"protein": "MPPPVLALVSGQALPAFLLCSTLLVIKMYVVAVITGQVRLRKKAFANPEDALRHGGLQYCRSDQDVDRCLRAHRNDMETIYPFLFLGFVYSFLGPDPFIAQMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTVAQLPCASMALQIVWEAACHL", "text": "FUNCTION: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15- hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4- dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Cytoplasm, perinuclear region Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. SIMILARITY: Belongs to the MAPEG family."}
+{"protein": "MTDIVLNDLPFVDGPPAEGQSRISWIKNGEEILGADTQYGSEGSMNRPTVSVLRNVEVLDKNIGILKTSLETANSDIKTIQGILDVSGDIEALAQIGINKKDISDLKTLTSEHTEILNGTNNTVDSILADIGPFNAEANSVYRTIRNDLLWIKRELGQYTGQDINGLPVVGNPSSGMKHRIINNTDVITSQGIRLSELETKFIESDVGSLTIEVGNLREELGPKPPSFSQNVYSRLNEIDTKQTTVESDISAIKTSIGYPGNNSIITSVNTNTDNIASINLELNQSGGIKQRLTVIETSIGSDDIPSSIKGQIKDNTTSIESLNGIVGENTSSGLRANVSWLNQIVGTDSSGGQPSPPGSLLNRVSTIETSVSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVFLSTFLSPA", "text": "FUNCTION: Chaperone involved in tail fiber assembly and retraction. Acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. During phage assembly, twelve fibritin molecules attach to the phage neck via gp13: six molecules forming the collar and six molecules forming the whiskers. SUBCELLULAR LOCATION: Virion Note=Localizes to the neck."}
+{"protein": "MELLIHRLSAIFLTLAINALYLTSSQNITEEFYQSTCSAVSRGYFSALRTGWYTSVITIELSNIKETKCNGTDTKVKLIKQELDKYKNAVTELQLLMQNTPAANNRARREAPQYMNYTINTTKNLNVSISKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKNALLSTNKAVVSLSNGVSVLTSKVLDLKNYINNQLLPIVNQQSCRISNIETVIEFQQKNSRLLEINREFSVNAGVTTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSIIKEEVLAYVVQLPIYGVIDTPCWKLHTSPLCTTNIKEGSNICLTRTDRGWYCDNAGSVSFFPQADTCKVQSNRVFCDTMNSLTLPSEVSLCNTDIFNSKYDCKIMTSKTDISSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKLEGKNLYVKGEPIINYYDPLVFPSDEFDASISQVNEKINQSLAFIRRSDELLHNVNTGKSTTNIMITTIIIVIIVVLLSLIAIGLLLYCKAKNTPVTLSKDQLSGINNIAFSK", "text": "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 to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. 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. F protein may trigger p53-dependent apoptosis. 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 to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. 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. F protein seems to trigger p53-dependent apoptosis. 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": "MMNLLNKSLEENGSVLTAFYIFVAFVALYLLGRALQAFVQAADACCLFWYTWVVVPGAKGTTFVYKHTYGKKLNKPELETVIVNEFPKNGWKQ", "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": "MLSGYIAGAIMKQEVILVLDCGATNVRAIAVNRQGKIVARASTPNASDIAMENNTWHQWSLDAILQRFADCCRQINSELTECHIRGIAVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISAQRLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHDTQFALFGAGAEQNEPVLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQAGLYNPGMQWLASGVLEWVRKLFWTAETPWQMLIEEARLIAPGADGVKMQCDLLSCQNAGWQGVTLNTTRGHFYRAALEGLTAQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPLKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHYQFRYFYPQTEPEFIEEV", "text": "FUNCTION: Catalyzes the phosphorylation of L-fuculose. SIMILARITY: Belongs to the FGGY kinase family."}
+{"protein": "MSTEQTFIAVKPDAVQRGLIGYIISKFELKGYKLRALKFLVPSRDLVEEHYAEHKGKPFYEKLVGFMASGPVCAMIWEGKQAVKTGRLMLGASNPLDSAPGTIRGDYGIDLGRNVCHGSDSIESANREIKLWFQPSEIQVYDRTIEPWIYE", "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": "MKALILVGGFGTRLRPLTLTLPKPLVEFGNRPMILHQVESLAAAGVTDIVLAVNYRPDVMVSALKKYEEQYNVKIEFSVETEPLGTAGPLKLAESILAKDDSPFFVLNSDVICDYPFQQLAEFHKRHGDEGTIVVTKVDEPSKYGVVVHKPNHPSRIDRFVEKPVEFVGNRINAGMYILNPSVLKRIELRPTSIEQETFPAIVRDGQLHSFDLEGFWMDVGQPKDFLTGTCLYLTSLTKRNSKLLAPNSEPYVYGGNVMVDPTAKIGKNCRIGPNVVIGPNVVIGDGVRLQRCVLMENSKVKDHAWIKSTIVGWNSSVGRWARLENVTVLGDDVTIADEVYVNGGSILPHKSIKQNIDVPAIIM", "text": "FUNCTION: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
+{"protein": "LKVPDLPLPESYXXALNLAXD", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scolopendra toxin 8 family."}
+{"protein": "MFSVESLERAELCESLLTWIQTFNVDAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQREMEEKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSSRRSYPGHVQPATAR", "text": "FUNCTION: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Predominantly recruits 2 dyneins, which increases both the force and speed of the microtubule motor (PubMed:25035494, PubMed:33734450). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell (PubMed:32073997). FUNCTION: (Microbial infection) May serve as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Golgi apparatus Note=Enriched at the cis-face of the Golgi complex. Localizes to microtubule asters in prophase (PubMed:11238449). Localizes to the manchette in elongating spermatids (By similarity). SIMILARITY: Belongs to the hook family."}
+{"protein": "MSLINKEILPFTAQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNPGEVCPAKWEEGAKTLQPGLDLVGKI", "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. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. 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": "MNRLRVARLTPLELLLSLMSLLLGTRPHGSPGPLQCYSVGPLGILNCSWEPLGDLETPPVLYHQSQKYHPNRVWEVKVPSKQSWVTIPREQFTMADKLLIWGTQKGRPLWSSVSVNLETQMKPDTPQIFSQVDISEEATLEATVQWAPPVWPPQKVLICQFRYKECQAETWTRLEPQLKTDGLTPVEMQNLEPGTCYQVSGRCQVENGYPWGEWSSPLSFQTPFLDPEDVWVSGTVCETSGKRAALLVWKDPRPCVQVTYTVWFGAGDITTTQEEVPCCKSPVPAWMEWAVVSPGNSTSWVPPTNLSLVCLAPESAPCDVGVSSADGSPGIKVTWKQGTRKPLEYVVDWAQDGDSLDKLNWTRLPPGNLSTLLPGEFKGGVPYRITVTAVYSGGLAAAPSVWGFREELVPLAGPAVWRLPDDPPGTPVVAWGEVPRHQLRGQATHYTFCIQSRGLSTVCRNVSSQTQTATLPNLHLGSFKLWVTVSTVAGQGPPGPNLSLHLPDNRIRWKALPWFLSLWGLLLMGCGLSLASTRCLQARCLHWRHKLLPQWIWERVPDPANSNSGQPYIKEVSLPQPPKDGPILEVEEVELQPVVESPKASAPIYSGYEKHFLPTPEELGLLV", "text": "FUNCTION: Receptor for IL27. Requires IL6ST/GP130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1-type immune responses. Also appears to be involved in innate defense mechanisms. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 subfamily."}
+{"protein": "MPTNFAAIVPGKNQSLVVQEAPYPTAGENRIVVRVHALAVNAVDYATQMMGETLFPWVTYPLVLGEDIAGEVVAIGPGVTRFKPGDRVVGHAVGTNSNNSAEGAFQQYVVLLENMASPLPHALEYQQAAVVPLAFSTAIVGLFQKDYLGLQIPSLTPTRTGKTLLIWGGATSVGCNAIQLAVAAGYEVITTCSPHNFDLVKSLGATAVFDYKKPSIRDDLREAFRGKTCAGALAIAGVVPQTRNEAAEACLNLVAESEGDKFVALSMPAPPNVPDGVSCKFIFASTVKDNEVSHQLYGYLGEALAHGSFIAAPEAEVVGTGLEAVQGALNALKQGVSAKKLVVTLP", "text": "FUNCTION: Dehydrogenase; part 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). In the first step, the non-reducing polyketide synthase azaA forms the hexaketide precursor from successive condensations of five malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (PubMed:22921072). The reactive polyketide chain then undergoes a PT- mediated C2-C7 cyclization to afford the aromatic ring and is eventually released as an aldehyde through the R-domain (PubMed:22921072). The putative ketoreductase azaE is proposed to catalyze the reduction of the terminal ketone resulting in the early culture product FK17-P2a (PubMed:22921072). The monooxygenase azaH was demonstrated to be the only enzyme required to convert FK17-P2a to azanigerone E (PubMed:22921072). AzaH first hydroxylates the benzaldehyde intermediate FK17-P2a at C4, which triggers the formation of the pyran-ring to afford azanigerone E (PubMed:22921072). In parallel, the 2,4-dimethylhexanoyl chain is synthesized by the HR-PKS azaB and is proposed to be transferred to the C4-hydroxyl of azanigerone E by the acyltransferase azaD directly from the ACP domain of azaB (PubMed:22921072). Alternatively, the 2,4-dimethyl-hexanoyl chain may be offloaded from the HR-PKS as a carboxylic acid and converted to an acyl-CoA by azaF (PubMed:22921072). The resulting acyl- CoA molecule could then be taken up as a substrate by AzaD to form azanigerone B (PubMed:22921072). To yield the carboxylic acid substituent in azanigerone A, the hydroxypropyl side chain of azanigerone B would need to undergo a C-C oxidative cleavage catalyzed by cytochrome P450 AzaI (PubMed:22921072). AzaI is proposed to act on a vicinal diol that leads to a C-C bond scission either through an alkoxyradical intermediate or a peroxy complex (PubMed:22921072). In the biosynthesis of azanigerone A, azanigerone B first undergoes hydroxylation at C10, possibly catalyzed by one of the two FAD- dependent monooxygenases encoded in the cluster, azaG or azaL, resulting in the vicinal diol azanigerone C (PubMed:22921072). Oxidative cleavage of azanigerone C by azaI would yield the corresponding aldehyde derivative of azanigerone A (PubMed:22921072). Finally, the dehydrogenase azaJ is proposed to convert the aldehyde functional group into the carboxylic acid, completing the conversion from azanigerone B to azanigerone A (PubMed:22921072). Alternatively, the oxidation of aldehyde to carboxylic acid may be catalyzed by the same P450 enzyme azaI via consecutive oxidation or by endogenous alcohol dehydrogenase (PubMed:22921072). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MSVILLAIPTLFIGFISYYLWIWTYWRRRGIPGPLGYPLVGSFPKTLKSEYPQYLQIRDWTKLYGPIYGYTEGTIKTLIVSDIDIVRQIFVEQYDNFYGRKLNPIQGDPEKDERTNLFSAQGFRWKRLRAISSPTFSNNSLRKINVTVEDSAMELLRHIEEQTSEGQQIDMLQFYQEFTMDTIGRIAMGQTDSQMFKNPLLKFVRAIFGDNRKHIPLIGGVFPTLAQVFRFFMLKFPLLGAANFIHVNKTVVTAVQNRIDQRENDRKNGIEIGEPQDFIDLFLEARADDVEHFQENNGDFSKTSSYGNRQLTTQEIVGQCLVFLIAGFDTTALSLSYTTFLLATHPEVQKKLQEEIERECIEPSISFDHLSKLKYMDCIIKETLRLYPLGTMANSRRCMRATKLGNVEVEVGTMVQVDTWSLHTDTKIWGDDAKEFKPERWLDPNCDQVFQKGGYISFGLGPRQCVGMRLAYMEEKMLLAHILRKYTFEVGTKTEIPLKLVGRATTQPETVWMHLKQRI", "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: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MKSLLLLTTLLIPLHLGMAWSAKYAVDCPEHCDNTECRSSLRCKRTVLDDCGCCQVCAAGPGETCYRTVSGMDGVKCGPGLKCHFYSEEDDFGDEFGVCKDCPYGTFGMDCKETCNCQSGICDRVTGRCLDFPFFQYAAAKSPSRTSASQTERDAASGDGNAVREEIGDRNAARPSVMKWLNPR", "text": "FUNCTION: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions (By similarity). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MHKIVQQGSKSLIESRIKRKSLLSKVVTDVSQLIPYFQNGHYVSMGGFAGTGYPKVVPIALADHVEKNGLQGKLKMNLFVGASVGPETEDRWAMLDMIDKRYPHQNGHHIRNGINSGRIRFADQHLSTFASDLLAGYYTLDKPHGSKRTMDIAIVEATEITEDGCIVPGASVGITPEILQMADKIIIEINTSLPSFKGLHDMVKIALPPFSKPYQITRVDDRIGLEAFPVDPEKIIAIVESQLPDNTSVGAPEDETSSAIANNIVQFFIHEIEQGRFPKNLLPLQSGIGSIANAVIGGLSKGPFDNLSVWTEVIQDTFLDFFDNGKLKFASATSLRFSPPGFNRLFNNWENYKSKIILRNQAISNAAELISRVGCIALNTPCEVDIYGHVNSTNTMGSKMLNGLGGSGEFLRNSRISIVHTPSTRPTKTDPHGISCIVPFASHIDHTEHDIDIIVTEQGLADIRGLAPYERAKVIIQNCAHPIYKPILMEYLETSRQICLKNHMGHEPHQLDKAFKFYTNLSEKGTMKIDKW", "text": "FUNCTION: Presumably involved in regulating the intracellular acetyl- CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family."}
+{"protein": "MHPDSQLETAVKNGFDPKSLYSTELTKVNEPARTILEQYSKIPAEKVLQHVKDLKDRAFEVFPYACIGQASFLELSIASSPCYPEMLDRVKKGDRLLDLGCAFGQELRQLIYDGAPSQNLYGTDLRPEFLELGLDLFLDRSFIKSHFIDADVLDDKSALVTQLTGELNIVYISLFLHVFDFETQIKVAKRVLDLLAPKAGSLIVCRVVACRDQAIGNATNARLPYYYHDLASWNRLWERVQEETGLKLKVDNWEQDDALAKKHPLEGIYMLGSSIRRE", "text": "FUNCTION: Methyltransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (PubMed:28529508). The first step of the pathway is the synthesis of 3,5- dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (By similarity). DMAO is then converted to farnesyl- DMAO by the prenyltransferase adrG (By similarity). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (By similarity). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (By similarity). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily."}
+{"protein": "MTEVLSQDEIDQLLTAISSGDASIEDARPISDTRKITLYDFRRPDKFSKEQMRTLSLMHETFARLTTTSLSAQLRSMVHVHVASVDQLTYEEFIRSIPTPSTLAVITMDPLKGNAVLEVDPSITFSIIDRLFGGTGQAAKVQRDLTDIENSVMEGVIVRILANVRESWTQVIDLRPRLGQIETNPQFAQIVPPSEMVVLVTLETKVGEEEGMMNFCIPYITIEPIISKLSSQFWFSSVRRSSTTQYMGVLRDKLSTVDMDVVAEVGSLRLSVRDILGLRVGDIIRLHDTHVGDPFVLSIGNRKKFLCQPGVVGKKIAAQILERIESTSQEDFEELSADEEELYE", "text": "FUNCTION: FliM 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 Bacterial flagellum basal body. SIMILARITY: Belongs to the FliM family."}
+{"protein": "MTYFIDVPTMSDLVHDIGVAPFIGELAAALRDDFKRWQAFDKSARVASHSEVGVIELMPVADKSRYAFKYVNGHPANTARNLHTVMAFGVLADVDSGYPVLLSELTIATALRTAATSLMAAQALARPNARKMALIGNGAQSEFQALAFHKHLGIEEIVAYDTDPLATAKLIANLKEYSGLTIRRASSVAEAVKGVDIITTVTADKAYATIITPDMLEPGMHLNAVGGDCPGKTELHADVLRNARVFVEYEPQTRIEGEIQQLPADFPVVDLWRVLRGETEGRQSDSQVTVFDSVGFALEDYTVLRYVLQQAEKRGMGTKIDLVPWVEDDPKDLFSHTRGRAGKRRIRRVA", "text": "FUNCTION: Catalyzes the conversion of L-ornithine into L-proline with release of ammonia. Is likely involved in the L-ornithine degradation pathway that allows P.putida to utilize this compound as sole carbon and nitrogen source. SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin family."}
+{"protein": "MNNRPIRLLTSGRAGLGAGALITAVVLLIALGAVWTPVAFADGCPDAEVTFARGTGEPPGIGRVGQAFVDSLRQQTGMEIGVYPVNYAASRLQLHGGDGANDAISHIKSMASSCPNTKLVLGGYSQGATVIDIVAGVPLGSISFGSPLPAAYADNVAAVAVFGNPSNRAGGSLSSLSPLFGSKAIDLCNPTDPICHVGPGNEFSGHIDGYIPTYTTQAASFVVQRLRAGSVPHLPGSVPQLPGSVLQMPGTAAPAPESLHGR", "text": "FUNCTION: Shows weak esterase activity with the p-nitrophenol-linked aliphatic ester pNP-butyrate. Does not exhibit cutinase activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family."}
+{"protein": "MKWWKLSGQILLLFCFAWTGEWIAKQAHLPVPGSIIGIFLLLISLKFNLVKKEWIQDGADFLLKELILFFIPSAVAVIRYKDTLSQYGIDLILIIMISTLCVTLVTGLLTELLLKRKGSVQ", "text": "FUNCTION: Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CidA/LrgA family. CidA subfamily."}
+{"protein": "MSTQSTHPPKPEAPRLPPAISSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVLGVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKDRLMQESLTMHRPGGHIAHLHVLAVHCAFRQQGRGPILLWRYLHHLGSQPAVHRAALMCEDALVPFYERFGFHAMGPCAITVGSLSFTELHCSLQGHPFLRRNSGC", "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": "MLSCTTSTMPGMICKNSDLEFDSLKPCFYPEDDDIYFGGRNSTPPGEDIWKKFELLPTPRLSPGRALAEDSLEPANWATEMLLPEADLWSNPAEEEDIFGLKGLSGSSSNPVVLQDCMWSGFSSREKPETVVSEKLPGGCGSLAVGAGTLVPGAAAATSAGHARSGTAGVGRRKAAWLTELSHLDSECVDSAVIFPANKRESMPVATIPASAGAAISLGDHQGLSSSLEDFLSNSGYVEEGGEEIYVVMLGETQFSKTVTKLPTAAHSENAALTPECAQSGELILKRSDLIQEQHNYAAPPLPYAEDARPLKKPRSQDPLGPLKCVLRPKAPRLRSRSNSDLEDIERRRNHNRMERQRRDIMRSSFLNLRDLVPELVHNEKAAKVVILKKATEYIHTLQTDESKLLVEREKLYERKQQLLEKIKQSAVC", "text": "FUNCTION: Has apoptosis-inducing activity. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSFLKSFPPPGSADGLRLQQPDTEAVLNGKGLGTGTLYIAESRLSWLDGSGLGFSLEYPTISLHAVSRDPNAYPQEHLYVMVNARFGEESKEPFSDEDEDDNDDVEPISEFRFVPSDKSALEAMFTAMCECQALHPDPEDEDSDDYDGEEYDVEAHEQGQGDIPTFYTYEEGLSHLTAEGQATLERLEGMLSQSVSSQYNMAGVRTEDSVRTYEDGMEVETTPTVAGQFEDADVDH", "text": "FUNCTION: Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins (By similarity). Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre- mRNAs (By similarity). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (By similarity). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (By similarity). Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Cytoplasm, cytoskeleton Note=A small fraction is also associated with the cytoskeleton. SIMILARITY: Belongs to the pICln (TC 1.A.47) family."}
+{"protein": "MAVVLKPWTVLVALVLCLLVCLGTFVDAYPPKPENPGEDASPEEQAKYYTALRHYINLITRQRYGKRSSPEGVMSELLFGDNSEHNQRSRYDDSYMW", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
+{"protein": "MSERVFAELATIHYQKSLPCRHSFDPPRTTPILHLYIIHLLLPPLIAIVCLCYIAIVPFEEEEERMRMQVVETAAVEEEEAAAAMMSVYERVARMASGNAVVVFSASGCCMCHVVKRLLLGLGVGPAVYELDQLAAAADIQAALSQLLPPGQPPVPVVFVGGRLLGGVEKVMACHINGTLVPLLKQAGALWL", "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 Nucleus. SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily."}
+{"protein": "MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDPGPTFDYSHPHDVYSNLSHLPAAPGAAGAPPAQALPYCPERSPFLVGPVSVSFSPVPSLAEIVERNPRVESGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYRLLARELGPLYTNITADIGTDPRGPRSPSGPRYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPRGSH", "text": "FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein Note=Trans cisternae of Golgi stack. SIMILARITY: Belongs to the glycosyltransferase 7 family."}
+{"protein": "MTRYAGLGRTRPKKLTPKAPIPIYREHQIDDLEEEIQNGLQQVETGVEKAEESEYHLQVAINAVASGRVVNEAHIPTPETVLSNLQYDELYPPVFSQPATYIRFSSTVEDCCGCPYNMTDEDDVFLKIMNEKRDPADRCTEDQFEEVMNFFEETVRLKQPYAAVGSAPVLSFAEMQESMDATVEDYVRRLAKDVYDHWKTRRLNNGNQSLLPSLKFETGAETDDTDPYVCFRRREVRQVRKTRGRDAQSADKLRRLRKELEDARQLVALVRQRELARKEMLATERILFLQRAEVKDMKRKLNIKDDDEDLINQKPKKKPIEAPPMQRPAAAQLRMPPKPGAQAAEDLQLLEDVQAEKENEIIRDIKANIAKHMKWNEGYVDFTRAPLSPSPERTVDISFRPAITTQLPTPPSSDSSENTPDLALDMSGTVSYRDKLDEHALIMSEDANKMPSFRRRIGRGGRLLIDRRNFASRCRVELDPWKADRFKYDQEDSDEDLDYEMDQYDISLMQNRAIMLAKARDQAHAQAQAAQVRRLQAEQAALNNLNSGQTSGQTMGSNPGPGAIAPTPET", "text": "FUNCTION: 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. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the enhancer of polycomb family."}
+{"protein": "MVDMQSLDEEDFSVSKSSDADAEFDIVIGNIEDIIMEDEFQHLQQSFMEKYYLEFDDSEENKLSYTPIFNEYIEILEKHLEQQLVERIPGFNMDAFTHSLKQHKDEVSGDILDMLLTFTDFMAFKEMFTDYRAEKEGRGLDLSTGLVVKSLNSSSASPLTPSMASQSI", "text": "FUNCTION: Plays a role as an effector of the ADP-ribosylation factor- like protein 2, ARL2. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion intermembrane space Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, cilium basal body Note=Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). SIMILARITY: Belongs to the ARL2BP family."}
+{"protein": "MKRGFSDSPSSSAPPPSSRFKSNPEGDSQFLEDETTKNFARKVADHYSRRTNQTLEEREASPIIHLKKLNNWIKSVLIQLYARPDDAVLDLACGKGGDLIKWDKARIGYYVGIDIAEGSIEDCRTRYNGDADHHQRRKKFSFPSRLLCGDCFEVELDKILEEDAPFDICSCQFAMHYSWTTEARARRALANVSALLRPGGVFIGTMPDANVIIKKLREAEGLEIGNSVYWIRFGEEYSQKKFKSSSPFGIEYVFHLEDAVDCPEWIVPFNVFKSLAEEYDLELVFVKNSHEFVHEYMKKPEFVELMRRLGALGDGSNDQSTLSADEWEAAYLYLSFVLRKRGESDGARRSGRRKNGKMNLSKDDVLYIDS", "text": "FUNCTION: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family."}
+{"protein": "MTDIRDTDALFALADRVTGFMPADEGRTLYETAVRYLGDGVGVEIGTYCGKSTVLLGAAARQTGGVVFTVDHHHGSEEHQPGWEYHDPSLVDPVTGLFDTLPRLRHTLDEADLYDHVVAVVGKSAVVARGWRTPLRFLFIDGGHTEEAAQRDFDGWARWVEVGGALVIHDVFPDPKDGGQAPFHIYQRALNTGDFREVNAYGSMRVLERTSGIAGQPL", "text": "FUNCTION: Involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria (PubMed:30606802). Specifically methylates the 1-OH position of 3,3'-di-O-methyl-4alpha-mannobiose, a probable early precursor of MMP, yielding the reducing end dimannoside of MMP (PubMed:30606802). SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "MQQAIEQTATGGALRFNGICKVFPGVKALSDISFEARPGSVHALMGENGAGKSTLLKILGGSYQPNSGTLQIGEHSYQFKSTAESIAAGVAVIHQELHLVPEMTVAENLLLGHMPNRFGLINRGAMYRRAGELLKGLADEIDPRTRLGDLSLGQRQLVEIAKAMSRNAHVIAFDEPTSSLSAREIDRLMAIIVRLRDEGRVILYVSHRMEEIFRVCDAVTVFKDGRFVKTFEQMADLDHDRLVTCMVGRDIQDIYNYRPRQHQGPSLRVTGLLGLGLQEPVSFAVQKGEVLGFFGLVGAGRTELFRILSGLTRSTAGSLQLDGQPLTLKSPRDAIAAGVLLCPEDRKKEGIVPLSSVAENINIGARPRHVNLGCLIQGGWERDNARAQIKSMNVKTPSPEQQIMFLSGGNQQKAILGRWLSMPMKVLLLDEPTRGIDVGAKSEIYEIIHTLAADGIAVIVVSSDLMEVMGISDRILVMSEGAITGELNRDEADESRLLQLALPRTRG", "text": "FUNCTION: Part of the ABC transporter complex AraFGH involved in arabinose import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Arabinose importer (TC 3.A.1.2.2) family."}
+{"protein": "MGKQNSKLRPEMLQDLRENTEFSELELQEWYKGFLKDCPTGILNVDEFKKIYANFFPYGDASKFAEHVFRTFDTNSDGTIDFREFIIALSVTSRGRLEQKLMWAFSMYDLDGNGYISREEMLEIVQAIYKMVSSVMKMPEDESTPEKRTEKIFRQMDTNNDGKLSLEEFIRGAKSDPSIVRLLQCDPSSASQF", "text": "FUNCTION: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels. May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases. FUNCTION: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels (PubMed:28398555). May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases (By similarity). FUNCTION: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels (By similarity). May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases (PubMed:15336960). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Note=Association with membranes is calcium-dependent (PubMed:8360179, PubMed:1543495). Enriched in the perinuclear region, probably at the trans Golgi network in response to calcium (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Note=Association with membranes is calcium-dependent (By similarity). Enriched in the perinuclear region, probably at the trans Golgi network in response to calcium (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Note=Association with membranes is calcium-dependent (By similarity). Enriched in the perinuclear region, probably at the trans Golgi network in response to calcium (PubMed:28398555). SIMILARITY: Belongs to the recoverin family."}
+{"protein": "MGNKQGKSPNNSKGGKKYKIDNDVVKQLQESTNFDKVEAKKLYEVFYDLSNGGKEPLNRDRFKEGLTKLESCGLKNLDNSPFGDRLFDLLDTNKDNTVDLQEFISGLSILCKGTAEEKLELSFKAYDIDGNGYITKSELSQMFQQAWISGFKALSYQTNEEVNKDDLNNFSEEMAQIFADGAFSSLDVNGDGKLSFNEFKQFAMSHPKITATLNGSKRDVPITFD", "text": "SIMILARITY: Belongs to the recoverin family."}
+{"protein": "EAEVAEVQAWWNSERFRLTKRPYTARDVVSLRGNLRQTYASNEMAKKLWCLLKNHQANGTASRTFGALDPVQVTQMAKHLDTIYVSGWQCSATHTTSNEPGPDLADYPYDTVPNKVEHLFFAQQYHDRKQREERMRMSREERARTPYVDYLRPIIADGDTGFGGTTATVKLCKLFVERGAAGIHIEDQSSVTKKCGHMAGKVLVAISEHINRLVAARLQFDVMGVETVLVARTDAEAANLIQSNIDTRDHQFILGVTNPNLKGKSLATLMQQGMAAGKSGAELQALEDEWLSKAQLKTLSEAVVEAIERQNIGEEEKRRKLNEWMHHSSYERCLSNEEGREIAEKLGVRNLFWDWDLPRTREGFYRFKGSVIASVVRGWAFSPHADVIWMETASPNVIECTQFSEGVRSKHPQMMLGYNLSPSFNWDASGMSDEQMRDFIPKIAKLGYVWQFITVGGLHSNALITSTFARDFANRGMLAYVERIQREERNNGVDTLAHQKWAGANYYDRYLKTVQGGVASTAAMGKGVTEEQFKESWTRPGAVEIDRGSIVVAKARM", "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": "MFRLGVFLLTFLLLVSMATSEYSRGRIMARASECVNECVESGHNTFHCERHCSNT", "text": "FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MKIIGGPASQLLASRTARALGTEPVLCEFNRFPDGELYLRIADEIENEKVTIIQSTPTDSDFVALLQLIDACEGAAEINVVIPYMGYARQDKKFKPGESISARAIARCINASRIFTINIHERSILDHFPCPAVNLDAASLVGEYIAGSGLENPMLVAPDEGAQGLVKNVAAGHGFDHDHLQKTRLSGDTVVIKTKNLDVTGRHVVLVDDMIATGGTMAESVRMLKAQGAIDVHLACVHPVLTRNAALRLFNAGVKDIIATDTLEKAESLLSVAPLIAEALKRL", "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 III (archaeal) subfamily."}
+{"protein": "MEIIRPMRVAIVAESFLPNVNGVTNSVLRVLEHLKANGHDALVIAPGARDFEEEIGHYLGFEIVRVPTVRVPLIDSLPIGVPLPSVTSVLREYNPDIIHLASPFVLGGAAAFAARQLRIPAIAIYQTDVAGFSQRYHLAPLATASWEWIKTVHNMCQRTLAPSSMSIDELRDHGINDIFHWARGVDSKRFHPGKRSVALRKSWDPSGAKKIVGFVGRLASEKGVECLAGLSGRSDIQLVIVGDGPEAKYLQEMMPDAIFTGALGGEELATTYASLDLFVHPGEFETFCQAIQEAQASGVPTIGPRAGGPIDLINEGVNGLLLDVVDFKETLPAAAEWILDDSRHSEMCAAAWEGVKDKTWEALCTQLLQHYADVIALSQRIPLTFFGPSAEVAKLPLWVARALGVRTRISIEA", "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). SIMILARITY: Belongs to the glycosyltransferase group 1 family."}
+{"protein": "MLRLFYFSAIIASVILNFVGIIMNLFITVVNCKTWVKSHRISSSDRILFSLGITRFLMLGLFLVNTIYFVSSNXERSVYLSAFFVLCFMFLDSSSLWFVTLLNILYCVKITNFQHSVFLLLKRNISPKIPRLLLACVLISAFTTCLYITLSQASPFPELVTTRNNTSFNINEGILSLVVSLVLSSSLQFIINVTSASLLIHSLRRHIQKMQKNATGFWNPQTEAHVGAMKLMVYFLILYIPYSVATLVQYLPFYAGMDMGTKSICLIFATLYSPGHSVLIIITHPKLKTTAKKILCFKK", "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). In airway epithelial cells, binding of denatonium increases the intracellular calcium ion concentration and stimulates ciliary beat frequency (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell projection, cilium membrane. Note=In airway epithelial cells, localizes to motile cilia. SIMILARITY: Belongs to the G-protein coupled receptor T2R family."}
+{"protein": "MITIYTAPSCTSCKKAKTWLSYHHIPFNERNLIADPLSTTEISQILQKCDDGVEGLISSRNRFVKTLGVDFEDISLSQAIKIISENPQIMRRPIIMDEKRLHVGYNEEEIRAFLPRTVRVLENGGARLRSAI", "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": "MEVRTFAFLQIVVFVALGIQLFAAVTDAADADDEFFTVDYCGMNCTLQQDGSWTPCTQKNAECKCYHESGSSVGLCLSTAYTDFNQFGDPNNSDLDAATPRHPDASSR", "text": "FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1 and CXCL8. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQPLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS", "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). 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 T1A family."}
+{"protein": "MGFKLNPFSKKPKDEEPLPLEQYEASEQKILGLVTKKEAKLLAIAGTGFLLDSYDLFIINLVSPILAYLYWGGLTGHQDYPSGIRGVVNAATNIGNIMGQLLFGFLGDFFGRKFVYGKEMMVVIIATILIICLPDRIPTPTAKMMWLFAFRVMLGIGIGGDYPMSASITSEQSLINRRGALLAWIFSNQGWGTLAGCVATLIILACFEKPLNDRGEYTKLNGVWRIQFGIALFPAVIVLIPRLRMQESEQFKNSKNMKSPGEGDLDSASQIELHDFKKKESLTAEFTTSSPSTASLSDKKNPGSVHIRPNNEVAPSSAPSRAPSTTSVESNTEGKESDIQTGSSFVSYFKEWRHAKLLIGSALSWFLLDIAFYGINLNQSVILQEMGFNKGVNEYHILQKNAIGNLIIAVAGYIPGYWVSVVLIEVMGRKWIQIQGFLICCLLFGVLAGTWETISTGGRFACVALAQFFFNFGPNTTCFVIPAEVFPSRVRAFSHGICAACGKAGAILSALLFNKLTEVIGFGNVLWIFFGCMVAGAVVTLILPETANRDADLIDRLEIAAMQQGRTSIIDRSEKWAWWKHGI", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum Golgi apparatus Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
+{"protein": "MLLLKHGRIEILDQNTMYGWYELPKQEFLNGEQPEPITHYIKQFPLMKDVNSLENKKDACPMKWFLLSAPITNHWFN", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf15 family."}
+{"protein": "MKRVVIAGTSSMVGKTTISTGIMKALSKKNNVQPYKIGPDYIDPTYHTEATKNKSRNLDSFFMDEMQVRSIFKRHSKNKDINVIEGVRGLYEGISPYNDVGSTASVSKTLNAPVILLMDARSLTRSAAAIIKGFKSFDTELNIKGVIFNKIRGEGHLNKLKEAVKYYDNDIEIIGAIPRDDGLSVSQRHLGLVPTPENKQKLLERIDLWGNTVEECLDIEKIVELSDESFDFEVDEKNKEETLWKVEKNNSKIAVAFDESFNFYYWDNFDALEENGAKIKFFSPLNDVEVPDCDTIYLGGGYPELFSEKLSNNKSMIDSIRNFDGKIYGECGGLMYLTNSIDGKEMLKLIDADAVMTPNVQGLSYVKGTFEKDCIIGEKSKEFKAHEFHYSKLININENDFSYRINRGKGIINSMDGITSKDGDIVGGYAHQHCIGNPYFAANLSKT", "text": "FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. 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 ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. SIMILARITY: Belongs to the CobB/CbiA family."}
+{"protein": "MAEITASLVKELRDRTGAGMMECKKALVEANGDIELAIDNMRKSGQAKAAKKAGRVAAEGVILARVENGFGVLVEMNCETDFVAKDAGFLGLANEVTDFAAANKGTTIEALQAQFEEKRAALVAKIGENMNIRRVAYLDGQVIAQYLHGAKIGVLVAGEGSADELKKVAMHVAASKPEFVNPEDVSAEVVEHERQIQIDIAINSGKPKEIAEKMVEGRMKKFTGEVSLTGQAFVMDPSVSVGDFLKSVNTSVSNFIRLEVGEGIEKKEEDFAAEVAKITGGNA", "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). 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EF-Ts family. SIMILARITY: Belongs to the EF-Ts family."}
+{"protein": "MGKNNSGSRNEVLVRGAEQALDQMKYEIAQEFGVQLGADTTARSNGSVGGEITKRLVAMAEQQLGGRANR", "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. 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 (By similarity). SIMILARITY: Belongs to the alpha/beta-type SASP family."}
+{"protein": "METLTFEFPAGAPARGRALAGCVGSGDLEVLLEPAAGGALSIQVVTSVNGSGPRWQQLFARVFAAPTAPAASIRIHDFGATPGVVRLRLEQALEEAGHD", "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": "MRTPLLPLARSVLLLLVLGSGHYAAALELNDPSSGKGESLSGDHSAGGLELSVGREVSTISEMPSGSELSTGDYDYSEEYDNEPQISGYIIDDSVRVEQVIKPKKNKTEGEKSTEKPKRKKKGGKNGKGRRNKKKKNPCTAKFQNFCIHGECRYIENLEVVTCNCHQDYFGERCGEKSMKTHSEDDKDLSKIAVVAVTIFVSAIILAAIGIGIVITVHLWKRYFREYEGETEERRRLRQENGTVHAIA", "text": "FUNCTION: Ligand of the EGF receptor/EGFR. Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the amphiregulin family."}
+{"protein": "MASRVVEPLVVARVIGEVVDSFNPSVKLNVIYNGSKQVFNGHELMPAVIAAKPRVEIGGEDMRSAYTLIMTDPDVPGPSDPYLREHLHWIVTDIPGSTDSSFGREIVSYESPKPVIGIHRYVLLLYKQSGRQTVKPAATRDHFNTRRYTAENGLGSPVAAVYFNAQRETAARRR", "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": "MLAAAPLLLASGNGFATTGPAAKPAVKPVTESRGEILSLSCAGCHGTDGNSSSVIPSIYGKSPEYIETALIDFKNGSRTSTVMGRHAKGYTGEEIHLIAEYFGNLSKKNH", "text": "FUNCTION: Monoheme cytochrome that function as the electron transport subunit of sulfide dehydrogenase. SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MTSILNTVSTIHSSRVTSVDRVGVLSLRNSDSVEFTRRRSGFSTLIYESPGRRFVVRAAETDTDKVKSQTPDKAPAGGSSINQLLGIKGASQETNKWKIRLQLTKPVTWPPLVWGVVCGAAASGNFHWTPEDVAKSILCMMMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAISEPEVITQVWVLLLGGLGIAGILDVWAGHTTPTVFYLALGGSLLSYIYSAPPLKLKQNGWVGNFALGASYISLPWWAGQALFGTLTPDVVVLTLLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGTETAKWICVGAIDITQLSVAGYLLASGKPYYALALVALIIPQIVFQFKYFLKDPVKYDVKYQASAQPFLVLGIFVTALASQH", "text": "FUNCTION: Involved in one of the last steps of the biosynthesis of chlorophyll a. Catalyzes the esterification of chlorophillide a or b with a preference for geranylgeranyldiphosphate (GGPP) rather than for phytyldiphosphate (PhyPP). SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. Chlorophyll synthase subfamily."}
+{"protein": "IVRRGCCSDPRCAWRCG", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks neuronal alpha-3-beta-2/CHRNA3-CHRNB2 (human and rat), alpha-7/CHRNA7 (human and rat), and alpha-3-beta-4/CHRNA3-CHRNB4 (human) nAChRs (PubMed:8206995, PubMed:15609996, PubMed:19131337). Acts voltage-independently (PubMed:15609996). Competes with alpha- bungarotoxin for binding to the receptor (PubMed:12384509, PubMed:15609996). Binds to a different site than alpha-conotoxin ImII (PubMed:15609996). Is highly active against the neuromuscular receptor in frog (PubMed:8206995). Also exhibits inhibition of D.melanogaster alpha-7 nAChRs (PubMed:25466886). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
+{"protein": "MAVNVNTNVAAMTAQRYLTGATNAQQTSMERLSSGFKINSAKDDAAGLQISNRLNVQSRGLDVAVRNANDGISIAQTAEGAMNETTNILQRMRDLSLQSANGSNSKSERVAIQEEITALNDELNRIAETTSFGGNKLLNGTFSTKSFQIGADNGEAVMLTLKDMRSDNRMMGGTSYVAAEGKDKDWKVQAGANDITFTLKDIDGNDQTITVNAKEGDDIEEVATYINGQTDMVKASVNEKGQLQIFAGNNKVTGDVAFSGGLAGALNMQAGTAETVDTIDVTSVGGAQQSVAVIDSALKYVDSHRAELGAFQNRFNHAISNLDNINENVNASKSRIKDTDFAKETTALTKSQILSQASSSVLAQAKQAPNAALSLLG", "text": "FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaD is not essential for flagellar synthesis and motility. FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaD is not essential for flagellar synthesis and motility (By similarity). SUBCELLULAR LOCATION: Secreted Bacterial flagellum. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the bacterial flagellin family."}
+{"protein": "MVFPIEAIVGLVTFTFLFFFLWTKKSQKPSKPLPPKIPGGWPVIGHLFHFNDDGDDRPLARKLGDLADKYGPVFTFRLGLPLVLVVSSYEAVKDCFSTNDAIFSNRPAFLYGDYLGYNNAMLFLANYGPYWRKNRKLVIQEVLSASRLEKFKHVRFARIQASIKNLYTRIDGNSSTINLTDWLEELNFGLIVKMIAGKNYESGKGDEQVERFKKAFKDFMILSMEFVLWDAFPIPLFKWVDFQGHVKAMKRTFKDIDSVFQNWLEEHINKREKMEVNAEGNEQDFIDVVLSKMSNEYLGEGYSRDTVIKATVFSLVLDAADTVALHINWGMALLINNQKALTKAQEEIDTKVGKDRWVEESDIKDLVYLQAIVKEVLRLYPPGPLLVPHENVEDCVVSGYHIPKGTRLFANVMKLQRDPKLWSDPDTFDPERFIATDIDFRGQYYKYIPFGSGRRSCPGMTYALQVEHLTMAHLIQGFNYRTPNDEPLDMKEGAGITIRKVNPVELIIAPRLAPELY", "text": "FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'- nitrosonornicotine (NNN) (Ref.3, PubMed:17102129, PubMed:16192354). Catalyzes the demethylation of nicotine to form nornicotine (Ref.3, PubMed:17102129, PubMed:16192354). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family. CYP82E2 subfamily."}
+{"protein": "MENRFQNDTLFSEWFGQSLSDVRFPDNVTVYSQADSAVSFENVRQPIKLVRAAMGSGKTTALIHFLKQVPKELSVLLISCRKTFAAEILHRFTLNGLEDFELYCDITERQINNRKVIVQIESLHRLTENYDVLILDEIMSIIKQFYSKTMTKTKEVDCKFLSLIKNSSHVIAMDATLTRHVVEFFAAFKPDTQIALIRNTFVSAMFSNRVAYFCDTFFGKEFSFFARLEDKLRWDKKLCLFCSTVLAAEYMHDLIRSRFSLKKVLLLTSKQGKCSSIESWIRYDVVIYTSVVTVGLSFEPVYFSSLFVYIQLAKGGPDMVSIFQSIGRVRRVIDEDIYIYMNPVLIKSYDPLAPIAMPPCSDWSVAEQSIISESCIDFRGKCSGAHKYNFCSVLKCLFRYRHYIEKTTITSLSDSLFLLCSLLCENSIKVDIVGNGFPMRKEVFLSFLQILVEECHFIEKKITLPGDNMTFQEIISSRETIMNGDFYENGNQLLHKDYITDMGKFRATFLSPGVDIFIASDIVSDLKNESKRYVFVNVWLQKCVSAGVESTRIERVFNERIKSYVLPKSFLCDEYFVLGDISGVYEWGMLIDLAFLAEMIRKDLKLKSCTDTTTDISEDDLLLCAARRSSDILQIMQLVFTVHVQFFQRYSLQTLQLFNKLRGMRIVTGVFSIEKFSISILRLFFKCAFNMTLSASKPRYIPGKAYRNLTKNDLENMLDNWEISRTNLKTCKELRKALTEASRARRKQTIYKLQGSDISLSVSEVGVFGQHASPGVCVSS", "text": "FUNCTION: Probably involved in DNA replication. Binds the origin of replication (ori) (By similarity). SIMILARITY: Belongs to the herpesviridae OriBP family."}
+{"protein": "MLDMGQDRPIDGSGAPGADDTRVEVQPPAQWVLDLIEASPIASVVSDPRLADNPLIAINQAFTDLTGYSEEECVGRNCRFLAGSGTEPWLTDKIRQGVREHKPVLVEILNYKKDGTPFRNAVLVAPIYDDDDELLYFLGSQVEVDDDQPNMGMARRERAAEMLKTLSPRQLEVTTLVASGLRNKEVAARLGLSEKTVKMHRGLVMEKLNLKTSADLVRIAVEAGI", "text": "FUNCTION: Has reversible, light-dependent DNA-binding activity. Upon illumination an internal FMN-protein adduct is formed which changes the protein conformation so that the previously sequestered DNA-binding domain is free to bind DNA. Binds to sequences within in its own promoter when illuminated but not when it has been incubated in the dark."}
+{"protein": "MGIFQRLMKNKELIPLAFFISAAATGASSFALYALKKTDVVIDRKRNPEPWETVDPTQPQKLLTINQEWKPVEELQRVRRATR", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the complex I NDUFA4 subunit family."}
+{"protein": "MLNIIVVLLLLFFSNNVIDSRYISYSKPNYYKTNDKIPVYMNNVRSGLSIFDYYKYPFPKPSTIEYKQSFMSKLAGDLNSTSLYDEVSLHTSVDCIALGKPINYTLDDVNQLKYLIDKHFRINFFIDDLPIGELFKNNRLVEYNNSNSKSSEITSPPSSPSSSSSSSSSPSSSIEEEDDDDTENDHIYLGHPIGFKYNSKYYLYNHLIIIINSTSTKSDKGFYTIKSVNVEPYSCVDCKIDSGIGGVEISPELFDDDKIKQLTIQYTYSIRNHETTTTNSGKSFQSWSIYYVNQFKLSNIDIIMSFIIVLAVSACLAIILLKIFRKTNSKTYTQLSPDDGGWKSIYADVFRSPNNFMTFSIIIGFGVQIVASLFILMVFSVAGLTSIATPGGMAIASILIFSFTGIFNGYSSMRTYIMLGGTRKLYNSVITTTLIPFTILLLMFIGYFQVWSNKFTYGASIGTVFFILAMWLLVCVPCSLLSSYFVRTWPPAEYPVRINPIPRFIPTAKWYQNQYLHMILGGIIPFVIIFTDLSFFLSSWVLGEHYSYSLSFALTFILMIISIVETNMIIEYYQLSLENYNWWWRSLLGPMVTGLYTFIYFIYFGITRIETEGVGFYYFMFSLVFSILVSLFCSSIGFLGNLWFTKKIYSTLHFD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family."}
+{"protein": "MAAAAGDVRGAALGARPGLGAAAAAAAAAEARFISSAKGKGLFATRSIRKGEAVFVEKPVVSSQFLWNALYNYRACDHCLRALETAEENAQRLLGRSSLVLPHPEQCSIRKDLHQQCPRCQVTYCSAECRQAALEQYHQVLCLGPSRDDPTHPLNKLQEAWRNMHYPPETSSIMLMARMVATVKQAKDKDWWIKAFSQFCSKTANEEEEIAHKLLGDKFKGQLELLRLLFTEALYDEQLSRWFTPEGFRSLFALVGTNGQGIGTSSLSQWVHACDALDLPMLQREELDAFIDQLYKDIEKESGEFLNCEGSGLYMLQSCCNHSCIPNAETSFPDNNFLLYLTALEDIEAGEEICISYLDCCQRERSRHSRNKILRENYLFTCSCPKCLAQADDPDVTSDEEEEAEGETDDAELEDEMTDV", "text": "FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 to form trimethylated histone H4 lysine 20 (H4K20me3) which represents a specific tag for epigenetic transcriptional repression. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
+{"protein": "NGLCCSQYGFCGTTSQYCSRANGCQSN", "text": "FUNCTION: Chitin-binding protein which functions in defense against chitin-containing fungal pathogens."}
+{"protein": "MSNNNYERLITKKDVYRVANERLYYLFSLAFQTGDERYIDLMERIGRRMDITLPQDIKRMYCKKCKKPYKNVRVRLKKNVITVTCLECGDIRRFQINR", "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": "MRTLWIVAVCLIGVEGNLYQFGNMIFKMTKKSALLSYSNYGCYCGWGGKGKPQDATDRCCFVHDCCYGRVNGCDPKLSIYSYSFENGDIVCGGDDPCLRAVCECDRVAAICFGENLNTYDKKYKNYPSSHCTETEQC", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that has enzymatic activity but is non-toxic. Displays low binding affinity and enzymatic activity on phosphatidylserine-containing vesicles and HEK-293 plasma membranes, in contrast to ammodytoxins that have high activity on these phospholipids. 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": "MALVSQARSLGKYFLLFDNLLVVLGFFVVFPLISIRFVDQLGWAALVVGLALGLRQLVQQGLGIFGGAIADRFGAKPMIVTGMLMRAAGFALMAMADEPWILWLACALSGLGGTLFDPPRTALVIKLTRPHERGRFYSLLMMQDSAGAVIGALIGSWLLQYDFHFVCWTGAAIFVLAAGWNAWLLPAYRISTVRAPMKEGLMRVLRDRRFVTYVLTLTGYYMLAVQVMLMLPIVVNELAGSPAAVKWMYAIEAALSLTLLYPLARWSEKRFSLEQRLMAGLLIMTLSLFPIGMITHLQTLFMFICFFYMGSILAEPARETLGASLADSRARGSYMGFSRLGLALGGALGYTGGGWMYDTGKTLDMPELPWFLLGIIGLITLAGLYWQFNRRRIESAMLSSS", "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": "MAAACGPGAAGYCLLLGLHLFLLTAGPALGWNDPDRMLLRDVKALTLHYDRYTTSRRLDPIPQLKCVGGTAGCDSYTPKVIQCQNKGWDGYDVQWECKTDLDIAYKFGKTVVSCEGYESSEDQYVLRGSCGLEYNLDYTELGLQKLKESGKQHGFASFSDYYYKWSSADSCNMSGLITIVVLLGIAFVVYKLFLSDGQYSPPPYSEYPPFSHRYQRFTNSAGPPPPGFKSEFTGPQNTGHGATSGFGSAFTGQQGYENSGPGFWTGLGTGGILGYLFGSNRAATPFSDSWYYPSYPPSYPGTWNRAYSPLHGGSGSYSVCSNSDTKTRTASGYGGTRRR", "text": "FUNCTION: Negative regulator of store-operated Ca(2+) entry (SOCE) involved in protecting cells from Ca(2+) overfilling. In response to cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+) refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)- dependent SOCE activity: possibly act by facilitating the deoligomerization of STIM to efficiently turn off ORAI when the endoplasmic reticulum lumen is filled with the appropriate Ca(2+) levels, and thus preventing the overload of the cell with excessive Ca(2+) ions. SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=Translocates to the endoplasmic reticulum-plasma membrane (ER-PM) region in a STIM1-dependent manner following cytosolic Ca(2+) elevation. SIMILARITY: Belongs to the SARAF family."}
+{"protein": "MAVPGSLAECGYIRTVLGQQILGHLDSSSLALPSEARLRLAGSSGRGDPAARSQRIQEQVQQTLARRGRSSAVSGNLHRTSSVPEYVYKLHVVENDFVGRQSPVTRDYDMLKAGMTATYGSRWGRAAAQYSSQKSVEERSWRQPLRRLEISPDSSPERAHYGHSEYQYAWRSHVVPGGRLTLPRYARSEILGLRQAGTARRPPGCGSFSDAVFDNGPLKPTMPTHPPGTSHSAGSLLEETTVRVSQARLQSTQSRTARSSWPRSSVRSSLREPGRMLTTAGQAAVGSGDAHGDRSVFADAQLGNADIEMTLERAVNMLDADHVPVSKISAAATFIQHESFQKSEARKRVNQLRGIPKLLQLLKLQNEDVQRAACGALRNLVFEDNDNKLEVAELNGVPRLLQVLKQTRDLETKKQITGLLWNLSSSDKLKHLMITEALLTLTESVIIPFSGWPEGDYPKANGLLDFDIFYNVTGCLRNMSSAGPDGRKMMRRCDGLIDSLVHYVRGTIADYQPDDKATENCVCILHNLSYQLEAELPEKYSQSIYMQNRNIQTNSNKSIGCFGSRSRKLKEQYQDLQMPEERSNPHGIEWLWHSIVIRMYLSLIAKSTRNYTQEASLGALQNLTAGGGPIPTLVARMVVQKENGLQHTRKMLHVGDPSVKKTAVSLLRNLSRNLSLQNEIAKETLPDLVSIIPDTVPSTDLLIETTASACYTLNNLMQNSYQNARDLLNTGGLQKIMTISIGEGYAPNKASKAASVLLYSLWAHTELHHAYKKAQFKKTDFVNSRTAKAYHSLKD", "text": "FUNCTION: Regulates focal adhesion turnover resulting in changes in focal adhesion size, cell adhesion and cell spreading, potentially via transcriptional modulation of beta-integrins (By similarity). Required to maintain gingival epithelial barrier function (By similarity). Required for cardiac sodium current propagation and electrical synchrony in cardiac myocytes (By similarity). Required for the formation of desmosome cell junctions in cardiomyocytes, thereby required for the correct formation of the heart, specifically trabeculation and formation of the atria walls (PubMed:15479741). Loss of desmosome cell junctions leads to mis-localization of DSP and DSG2 resulting in disruption of cell-cell adhesion and disordered intermediate filaments (PubMed:15479741). Modulates profibrotic gene expression in cardiomyocytes via regulation of DSP expression and subsequent activation of downstream TGFB1 and MAPK14/p38 MAPK signaling (By similarity). May play a role in junctional plaques (By similarity). SUBCELLULAR LOCATION: Nucleus Cell junction, desmosome Cell junction Cytoplasm Note=Colocalizes with CTNNA3 and SCN5A/Nav1.5 at intercalated disks in the heart. SIMILARITY: Belongs to the beta-catenin family."}
+{"protein": "MDRDTKLAFRLRGSHSRRTDDIDDDVIVFKTPNAVYREENSPIQSPVQPILSSPKLANSFEFPITTNNVNAQDRHEHGYQPLDAEDYPMIDSENKSLISESPQNVRNDEDLTTRYNFDDIPIRQLSSSITSVTTIDVLSSLFINLFENDLIPQALKDFNKSDDDQFRKLLYKLDLRLFQTISDQMTRDLKDILDINVSNNELCYQLKQVLARKEDLNQQIISVRNEIQELKAGKDWHDLQNEQAKLNDKVKLNKRLNDLTSTLLGKYEGDRKIMSQDSEDDSIRDDSNILDIAHFVDLMDPYNGLLKKINKINENLSNELQPSL", "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 COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere- associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the CENP-U/AME1 family."}
+{"protein": "MSFCDDREGQRALRILQARLIRSPDACSFALTAVSSLLRKYSIDPRRIGRLEVGTESLVDKSKSIKSFVMQLFEESGNFDIEGVDTVNACYGGTNALFNAVNWVESSAWDGRDAIVVASDISLYGKGNARPTGGAGCVAMLVGPDAPIAFEPGRRGSYMAHTYDFYKPDFTTEYPYINGKHSIECYIQAVEACYRAYTKRERRATERLEEERPDHQAGYETPLDRFDYLCFHSPTNKLVSKSYARLLYVDYLENPANPIFAEVPDSIREVEYRASLTDKSIEKTFMGLAQERFARCVQPSTEIPNMCGNMYSASVYGSLCSLLCNVNSETLLGKRITIFSYGSGLASSMFSLKVRGSTKQMAEKLDVHRRLVDRVVVSPEDVRERAYLKKCFKPKGGAGPIPADVYSLAEVDELFRRVYTVKS", "text": "FUNCTION: Hydroxymethylglutaryl-CoA synthase-like protein; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype (PubMed:24611558). AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA) (PubMed:22846083). On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment (PubMed:22846083). The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8- hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety (PubMed:10432635, PubMed:10975654, PubMed:22846083). Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes (PubMed:20348386). The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated (PubMed:10432635, PubMed:10975654, PubMed:22846083). The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK- toxin, probably via the catalysis of a side reaction of EDA or its precursor (PubMed:24611558). SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase family."}
+{"protein": "MEAAQQKNESVMDYAPDWTQISVLFFVVMGGGVLASLSALALAGTVVLMLILTPVFLLLSPVILPVGAVIALAAAAFMAAVTIGIAGAAALIWVYRYARGQPTVGSEKIDRARVRLFEAAEKLKAQLQYKLFNENSKANFD", "text": "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": "MARTKQTARKSTGVKAPRKQLATKAARKSAPVSGGVKKPHKFRPGTVALREIRKYQKTTDLLIRKLPFQRLVRDIAMEMKNDIRFQSQAILALQEAAEAYLVGLFEDTNLCAIHARRVTIMTKDMQLARRIRGERF", "text": "FUNCTION: Macronuclear replacement variant which replaces conventional H3 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. Functions redundantly to H3.4. H3.3 deposition into chromatin is mainly transcription-associated and DNA replication- independent, but it can also enter a replication-coupled pathway. Although not essential for vegetative growth, minor H3 variants are required for producing viable conjugation progeny by affecting late developmental stages of conjugation (By similarity). SUBCELLULAR LOCATION: Nucleus. Chromosome Note=Localizes mainly to the large, transcriptionally active, somatic macronucleus (MAC) and only faintly to the small, transcriptionally inert, germ line micronucleus (MIC). SIMILARITY: Belongs to the histone H3 family."}
+{"protein": "MRSEAVPQPGGLERFASPGKGRGLRALRRYAVGELLFSCPAYTAVLTVSERGSHCDGCFARKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECAAMCAFGQNWNPSETVRLTARILAKQKIHPERTQSEKLLAVKEFESHLDKLDNEKRELIQNDIAALHHFYSKHMEYPDNAALVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVKEIEPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCDCRECTMKEKDKEKLKIRKLNDPPSAEAVRDMIKYARNVIEEFRRAKHYKPPSELLEICELSLDKMGAVFEDSNVYMLHMMYQAMGVCLYVQDWEGALRYGQKIIRPYSKHYPSYSLNVASMWLKLGRLYMALENRPAGDKALKKAIAIMEVAHGKDHPYISEIKKELEDH", "text": "FUNCTION: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
+{"protein": "MAILTLGWVSLLVVFTWSIAMVVWGRNGL", "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": "MNIRNARPEDLMNMQHCNLLCLPENYQMKYYFYHGLSWPQLSYIAEDENGKIVGYVLAKMEEDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRAALHLYSNTLNFQISEVEPKYYADGEDAYAMKRDLTQMADELRRHLELKEKGRHVVLGAIENKVESKGNSPPSSGEACREEKGLAAEDSGGDSKDLSEVSETTESTDVKDSSEASDSAS", "text": "FUNCTION: Catalytic subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase activity (PubMed:15496142, PubMed:19826488, PubMed:19420222, PubMed:20145209, PubMed:27708256, PubMed:25489052, PubMed:29754825, PubMed:20154145, PubMed:32042062). Acetylates amino termini that are devoid of initiator methionine (PubMed:19420222). The alpha (N-terminal) acetyltransferase activity may be important for vascular, hematopoietic and neuronal growth and development. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation (PubMed:12464182). Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration (PubMed:19826488). Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development (PubMed:20145209). Acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to preferential binding to co-chaperone HOPX (PubMed:27708256). Acetylates HIST1H4A (PubMed:29754825). Acts as a negative regulator of sister chromatid cohesion during mitosis (PubMed:27422821). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Also present in the free cytosolic and cytoskeleton-bound polysomes. SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily."}
+{"protein": "MNKLLESPYDIVLEEVREGKVNPFDVDLDHLIALFRKKAKELKGSEYMLEAGKFLEASSKLLLLKLEYFFPKSQKERKKVSLKEVQEVLIEEGEEDLSRFDTSFLWEYSPEVGRPKSSKGEKPKILEWREFWKLSKERVPLHREPNWQEEAKRVYEEIKRGVFRIRNLRDFIAFLFAYMEYEEVQKEELLRRLL", "text": "SIMILARITY: To A.aeolicus AQ_423."}
+{"protein": "MSGTTESQLNQLVGAMHLRHRFLGVFDKTFPGFLDPNRPASAIVNTGSRATGGMHWIAFAFDPIARKCYMFDPFGWSDRELWNLYKVKYDAFLRRTGLRQPDKCFELVRSVEAVQCPCSAACGLFSALFIASFDRYHTRPMDGNPIIDTVVGVKHSDMYKPEFQSILHRNQERMYFWFMKNNSFFRAHESELKRETAINSVPENH", "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": "MGIKQWLLSLVVVAISATATQARVDDPAGKAAQYHKEYALFRSANMPSPDKLASGVGFHSFRIPAVVRTNTGRILAFAEGRRHNNRDYGDINLVYKRTKSPTNNGENPTDWESLREVVGTGPHTWGNPTPVVDGNTIYLFLSMNDGAYSQNGGNTLPDGTKTKTIDSTWVGRRHLYLTTSTDDGDTWTKPVDMTKTLTPDGQAWDAVGPGNGIKLSTGELVIPAQGRNIIGHGPSGNRTWSMQVLKGAGSEGTICQTPDGKLMRNDRPGPMGHRSVARGTLAGFGPFATDNGLPDPACQGSILSYNSDEPARTIFMNSASTDRRTAMRVRISYDKDAAKFNFGRELKDAPLGNVGNEGGYSSMTKTSDYKIGALVESDWYEDKGGEKSHRCIIWRRFNLSWIINGPNN", "text": "FUNCTION: Sialidase is able to release sialic acid from a wide variety of natural substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 33 family."}
+{"protein": "MMELRCWGSDWGLPSVHPECLVVLAYARFAGAPLKVTPVDYTWASPKGTVPFLTSAGEDTHQPANILNFFRKQKYNADYVLSAKEGSDTLAYIALLEEKLLPAVLHTFWVDTENYCNVTRPWYASHTPFPLNYYLPGKMSRDALDRILVTRGQPPLYSLSEVEAQIYKDAKECLNLFSNRLGTAQYFFGSTPTSLDAFVFGFLAPLYKAHLHKVNLQQHLKQLSNLCHFCDHILSAYFVSDDAGTSAAGQEAIDANLQKLTQLVNKESNLIEKMDDNLRRSPQNRPQKLSTLKPVGGAENSHSSDLLSH", "text": "FUNCTION: Could function in transport of proteins into the mitochondrion. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion outer membrane. SIMILARITY: Belongs to the metaxin family."}
+{"protein": "MAALLMPRRNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALKRLSTEEATRWAESFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVTKAHRIFEEFVDVQAPREVNIDFQTREATRKNMQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLDLLSQSQRRLS", "text": "FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2. 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 DRD2 and CHRM2 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": "MKVSKYVAIFFFVFIQLISVGKVFANADEWMTTFRENIAQTWQQPEHYDLYIPAITWHARFAYDKEKTDRYNERPWGGGFGQSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRPLADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPATFQMTYIPGTYNNGNVYFAWMRFQF", "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": "MVGASLGPPGRGSLSRLIRLVICVLTLCALSVQGRSESTEGHSKDLLYKYKLYGDIDEYAYYFLDIDIGTPEQRISLILDTGSSSLSFPCAGCKNCGVHMENPFNLNNSKTSSILYCENEECPFKLNCVKGKCEYMQSYCEGSQISGFYFSDVVSVVSYNNERVTFRKLMGCHMHEESLFLYQQATGVLGMSLSKPQGIPTFVNLLFDNAPQLKQVFTICISENGGELIAGGYDPAYIVRRGGSKSVSGQGSGPVSESLSESGEDPQVALREAEKVVWENVTRKYYYYIKVRGLDMFGTNMMSSSKGLEMLVDSGSTFTHIPEDLYNKLNYFFDILCIQDMNNAYDVNKRLKMTNESFNNPLVQFDDFRKSLKSIIAKENMCVKIVDGVQCWKYLEGLPDLFVTLSNNYKMKWQPHSYLYKKESFWCKGIEKQVNNKPILGLTFFKNRQVIFDIQKNRIGFVDANCPSHPTHTRPRTYNEYKRKDNIFLKIPFFYLYSLFVVFALSVLLSLVFYVRRLYHMEYSPLPSEGKAPADA", "text": "FUNCTION: During the asexual blood stage, plays an essential role in the export of several proteins into the host erythrocytes by cleaving the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence (PubMed:24983235). Specifically, cleaves after the leucine residue in the RxLxE/Q/D (or RxLxxE) motif of exported proteins including EMP1 (By similarity). Also, by regulating protein export, plays an essential role in gametocyte development and thus parasite transmission to the mosquito vector (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MASLIQVRDLLALRGRMEAAQISQTLNTPQPMINAMLQQLESMGKAVRIQEEPDGCLSGSCKSCPEGKACLREWWALR", "text": "FUNCTION: May function as a transcriptional regulator that controls feoABC expression. FUNCTION: May function as a transcriptional regulator that controls feoABC expression. SIMILARITY: Belongs to the FeoC family. SIMILARITY: Belongs to the FeoC family."}
+{"protein": "MINKGKSWRLATVAAALMMAGSAWATEYSASFKNADIEEFINTVGKNLSKTIIIEPSVRGKINVRSYDLLNEEQYYQFFLSVLDVYGFAVVPMDNGVLKVVRSKDAKTSAIPVVDETNPGIGDEMVTRVVPVRNVSVRELAPLLRQLNDNAGGGNVVHYDPSNVLLITGRAAVVNRLVEVVRRVDKAGDQEVDIIKLRYASAGEMVRLVTNLNKDGNTQGGNTSLLLAPKVVADERTNSVVVSGEPKARARIIQMVRQLDRDLQSQGNTRVFYLKYGKAKDMVEVLKGVSTSIEADKKGGGTTAGGGNASIGGGKLAISADETTNALVITAQPDVMAELEQVVAKLDIRRAQVLVEAIIVEIADGDGLNLGVQWANTNGGGTQFTDTNLPIGSVAIAAKDYNENGTTTGLADLAKGFNGMAAGFYHGNWAALVTALSTSTKSDILSTPSIVTMDNKEASFNVGQEVPVQSGSQSSTTSDQVFNTIERKTVGTKLTVTPQINEGDSVLLNIEQEVSSVAQKQATGTADLGPTFDTRTIKNAVLVKSGETVVLGGLMDEQTQEKVSKVPLLGDIPVLGYLFRSTNNTTSKRNLMVFIRPTILRDAHVYSGISSNKYTMFRAEQLDAAAQESYLTSPKRQVLPEYGQDVAQSPEVQKQIELMKARQQATADGAQPFVQGNK", "text": "FUNCTION: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). 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": "MEKFKLLKLGKPATLLLEDGTVFRGKSFSNPQTVTGEIVFNTGMTGYQEIFTDPSYNEQLVVLTYPEIGNTGTNLDDYESLKIQAKGIILKNLSNAYSNFRAMRSLLSFLKRHKVVEIHDIDTRALVLHIRNNKTMLAVISNETYNLTFKEAKATIKYGKHTLNSNLASRVSTSLDYYQWMQPLNRKLKFGYSIIRSFNSAINKKLHTSKKLRIIVLDLGVKFNILRYLKSFECEVIIVNYKSTYQQVMKFHPDGIVISNGPGDPAKINRVVVRVNKFINKKIPILGICLGHQILARCFEAKTFKLKFGHRGLNHPVGINKRMEITSQNHGFAVNFEFLKSNKFYANHLNLNDGTLAGISSQNFPLISVQYHPEGSPGPHDSNYLFKYWVYIIYKSKSS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the CarA family."}
+{"protein": "MGLCHGKSAAVLEPTVEEEEEGATRVAEAAAAPAKPASPAPSAAAAAAAPAKPGTPKQHKFPFYLPSPLPASSYKGSPANSSVASTPARGGFKRPFPPPSPAKHIRALLARRHGSVKPNEASIPESGEPGVALDKGFGFSRHFAAKYELGREVGRGHFGYTCAATCKKGELKGDDVAVKVIPKAKMTTAIAIEDVRREVRILSSLAGHSNLVQFYDAYEDEENVYIVMELCKGGELLDRILARGGKYSEEDAKVVMRQILSVASFCHLQGVVHRDLKPENFLFSSKDENSAMKVIDFGLSDFVKPDERLNDIVGSAYYVAPEVLHRSYGTEADMWSIGVIVYILLCGSRPFWARTESGIFRAVLKADPSFEEAPWPTLSAEAKDFVRRLLNKDYRKRMTAAQALCHPWIRGTEEVKLPLDMIIYRLMRAYISSSSLRRAALRALAKTLTTDQIYYLREQFELIGPNKSDLITLQNLKTALMKNSTNAMKDSRVVDFVNTISNIQYRKLDFEEFSAAAISVYQMEGLETWEQHARQAYEFFDKEGNRPIVIDELASELGLGPSVPLHVVLQDWIRHPDGKLSFLGFMKLLHGVSSRTIPKT", "text": "FUNCTION: Possesses kinase activity in vitro. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MLLKSLALIASSSLAATFNIGDDLFADPQFTVQFHNRPLRQADVQNGLLPHRDPVYGHPLGYEMMQFNGTNHICGIPEVTTTKSSKSREEGELSPTEARDRALELMLPLLGDCLFYEQGFFSYRFCYGSGVVQYRRHGDNYFPRIYPPPQADDSPTFVLGSFEKDDTTNTVTSAGGIPFLAHRLRSGTHCPLTGANREIEVQFVCDKNVQHDHILWIKEKRTCNYVMQVGTPRLCKDMRFQPPPDESLPIMCYSVESEAPEFETIDGMFDGVAHVKEEQEAVSARAHQFVGSNVNKDKIDEIEVAWRFTKARALNYIGVWLGDCVNRQTLFKELGIATPSHDAPFIIQTRSMFVPAPINRHFEVRLMITRQQLLLSINDDDVTLEEKYAWWQEQGDMSNLEIQGLTMLDDAGIEDVLARATDEVMKQLNKEAKQSKKLAKKKEAASTKREEAKKQVEASVEEKAVDSAEDDGTDTVTSTQTFFRTQTLSTAEAESKQMPDKAEEDEDEDLIVTMYFEDGEFKIEGFEVADFEGVKSAMKDLADKEDDDDDYEDYGLSD", "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": "MPKRKVTFQGVGDEEDEDEIIVPKKKLVDPVAGSGGPGSRFKGKHSLDSDEEEDDDDGGSSKYDILASEDVEGQEAATLPSEGGVRITPFNLQEEMEEGHFDADGNYFLNRDAQIRDSWLDNIDWVKIRERPPGQRQASDSEEEDSLGQTSMSAQALLEGLLELLLPRETVAGALRRLGARGGGKGRKGPGQPSSPQRLDRLSGLADQMVARGNLGVYQETRERLAMRLKGLGCQTLGPHNPTPPPSLDMFAEELAEEELETPTPTQRGEAESRGDGLVDVMWEYKWENTGDAELYGPFTSAQMQTWVSEGYFPDGVYCRKLDPPGGQFYNSKRIDFDLYT", "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": "MRTGKQYLESLNDGRVVWVGNEKIDNVATHPLTRDYAERVAQFYDLHHRPDLQDVLTFVDADGVRRSRQWQDPKDAAGLRVKRKYHETILREIAAGSYGRLPDAHNYTFTTYADDPEVWEKQSIGAEGRNLTQNIHNFLKLLREKDLNCPLNFVDPQTDRSSDAAQARSPNLRIVEKTDDGIIVNGVKAVGTGIAFGDYMHIGCLYRPGIPGEQVIFAAIPTNTPGVTVFCRESTVKNDPAEHPLASQGDELDSTTVFDNVFIPWEQVFHIGNPEHAKLYPQRIFDWVHYHILIRQVLRAELIVGLAILITEHIGTSKLPTVSARVAKLVAFHLAMQAHLIASEETGFHTKGGRYKPNPLIYDFGRAHFLQNQMSVMYELLDLAGRSSLMIPSEGQWDDSQSGQWFVKLNNGPKGNPRERVQIGRVIRDLYLTDWGGRQFMFENFNGTPLFAVFAATMTRDDMSAAGTYGKFASQVCGIEFGGAEPTAYAATADYAKALDKGLAPEPAAAESATS", "text": "FUNCTION: Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 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 FADH(2)-utilizing monooxygenase family."}
+{"protein": "MIVDGRVSKIVLASIKNNIYKVFITVNSPIKFIAGQFVMVTINGKKCPFSIANCPTKNHEIELHIGSSNKDCSLDIIEYFVDALVEEVAIELDAPHGNAWLRSESNNPLLLIAGGTGLSYINSILTNCLNRNIPQDIYLYWGVKNSSLLYEDEELLELSLNNKNLHYIPVIEDKSEEWIGKKGTVLDAVMEDFTDLAHFDIYVCGPFMMAKTAKEKLIEEKKAKSEQMFADAFAYV", "text": "FUNCTION: Probable flavin reductase in the luminescent systems of different marine bacteria. SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein oxidoreductase family."}
+{"protein": "MVEAILRSTLGARTTVMAALSYLSVLCFVPLLVDRDDEFVYFHAKQGLVIWMWGVLALFALHVPVLGKWIFGFSSMGVLVFSLLGLVSVVFQRAWKLPVVSWVADRI", "text": "FUNCTION: Plays a role in regulating magnetite crystal size; partially redundant function with MamF. SUBCELLULAR LOCATION: Magnetosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the magnetosome MamF/MmsF protein family."}
+{"protein": "MAAASEERMAEEGGGGHGDGGSPSAIASTQRLPPPPPPQPPQPGSQAPPAPALAPDQLPQNNTLVALPIVAIENILSFMSYDEISQLRLVCKRMDLVCQRMLNQGFLKVERYHNLCQKQVKAQLPRRESERRNHSLARHADILAAVETRLSLLNMTFMKYVDSNLCCFIPGKVIDEIYRVLRYVNSTRAPQRAHEVLQELRDISSMAMEYFDEKIVPILKRKLPGSDVSGRLMGSPPVPGPSAALTTMQLFSKQNPSRQEVTKLQQQVKTNGAGVTVLRREISELRTKVQEQQKQLQDQDQKLLEQTQIIGEQNARLAELERKLREVMESAVGNSSGSGQSEESPRKRKKAAEAIDSLRKSKRLRNRK", "text": "FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore."}
+{"protein": "AAKYCKLPVRYGPCKKKIPSFYYKWKAKQCLPFDYSGCGGNANRFKTIEECRRTCVG", "text": "FUNCTION: Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family."}
+{"protein": "MVACCHRAPVVHRRSSESEEVGPAVVLGFSIALIVFSLLLMLLVLMHKGKGGGLSDMFGGGMQSSVGGSSVAERNLDRITVVVGLAWFACIMVLGLLMKANN", "text": "FUNCTION: Involved in protein export. Participates in an early event of protein translocation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecG family."}
+{"protein": "MEEVDRILIHSLRSCGTEVPEDVQSIRQFNTELIVEAVVRCLRVINPSLGATLSHVLPPGMSARFRIGTSLAQACQDLGYPGEVGYQTFLYSSEPDIRALLIFLAEKLPRDSPEDAHQPAGKSALLQREIAATIKRQLSLPWLPSSCRICALRRSQNSCRLHRFHAQPLSLATDPTLKSIPDERKEYWQCYLPSVTSQLPHLPSVAASLLERNTSELSAKQEWDAEWKSQGLASRLSPEDYRSRKRQRLQKRIQEQLRQCAQLLAENHLPSSSSQDLTDMLKAFNLDGGSDQKKGSRFTRTQRFTYQQDPHTLKEQMQRAAEILPKKDAQDTDAEQQELSSLQEQIDSIEQEIRGLSESNKRLQLTVSQVEGEVNEMRQSCEEKEKIVRVKKRAVELLPDADNNLVKLQALVDASSHRMANLVGQWESHQVRLSEEYRELKRVQQEQEDESSRWMKDAKDLYEKIRGAADEAKRKEELYKQLLSEYESLPKEVSRAAYTQRILEIVSNIKKQKEEITKILSDTKELQKEINNLTGKVDRTFVVTDELVFKDAKKDEPVRKAYKYLAALHENCSQLIQTIEDTGTILREIRDLEEQIETETTKKTLSNLQKILEDYRAIKQENAQLLARIREA", "text": "FUNCTION: May be involved in regulation of NF-kappa-B signaling. May be involved in copper-dependent atp7a trafficking between the trans-Golgi network and vesicles in the cell periphery (By similarity). SUBCELLULAR LOCATION: Endosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the CCDC22 family."}
+{"protein": "MFYKACPSTLTCSKWIHSIIKTKKFLYCRHYSSKSFIDNAPLRINPVGVQYLSPALQNQVFPQQNTQISQLHLDLAKFHLAKHQLLNKETIKLPSFNFRLPPLQGKTISEHFYNIGLEFAEPHLSKAIKFSKIDTPVQPKTWKRQPGWTKYAKDGSISCVPYPDSDCMVFDVEVLYKVSPFAVVATAVSEDAWYCWLSPWLLGKSENDRQLIPSNPKGALFVGHNVSFDRQRIREEYNIKSSRNVFLDTMSLHVATHGMCSRQKPTWFKARKAYIRSQSTETSEDDDSSSFDDDYQNYLKQEPWLAHSSVNSLKDVAKFHCNITLDKSKRDDFASLEKEPILQKLNELITYCAHDTYSTHQVFKKVFPQFLEVCPHPATFSAMLSLGSVFLPVNHSWTRYINGVEEQYQQMIQLVDQKLSQYAEKAKDLINTKDTVLKDPWLRQLDWTPCNLYRKLKKATQEVPVVPKWYKKAYCKTEKRAVITAKSRLAPILLRLKWKKHPLAWSDTYGWVFSVERTSKDEIEMLLDQGLVPCSREEDTKLDYNNYIFFKVPHKDGPEARCGSPLSKSYQRYFEEGILQSDYEVAKKALEMSASCSYWSSARDRIRSQMVVWDKDAELGVPSSVDGFGIILPCIIPMGTVTRRAVENTWLTASNSKKNRLGSELKAMIRAPDGYTFVGADVDSEELWIVALMGDSQFRLHGATALGMMTLEGKKSEGTDLHSKTAAILGVSRDSAKVFNYGRLYGAGLKHTTLLLMQMNPTLKTAEAKELAKKLYASTKGVKSKMSKRLQEMGLPKLTFWSQGTESFVFNKLEAMAQLPSPRTPVLDAGITQALSSKNLSKNSFMTSRVNWAIQSSAVDYLHLLLVSMNHLIKKYYLEARLSLTVHDEVRYLSSDKDKYRVAFALQVANLWTRAFFCQRLGINELPQSVAFFSSVDIDHVLRKDVKMDCVTPSNKVPIPPGEELTIESVLEKLEQSGQSLEPLEQIQCFVDVKATTSAEITEEDKKNIAYLKAQAFY", "text": "FUNCTION: Involved in the replication of mitochondrial DNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the DNA polymerase type-A family."}
+{"protein": "MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIGTQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAIIAILTPKKHTVKKRIGSRCINCCLIT", "text": "FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
+{"protein": "MTKNKNLEFIQNAIKKNKVVLFMKGTKEMPACGFSGTVVAILNKLGVEFSDINVLFDTALREDLKKFSDWPTFPQLYINGVLVGGCDIAKELYQNGELEKMLKDVVV", "text": "SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily."}
+{"protein": "MIFKRFVNLLVFLFLLGAGLLTFFLILSGGRESGTLKNFYWLQADTNGFNSAPSTTRWYNYNWCGYEDGQLANCSSRAPAKPFSPRDNFGNSVNLPSSFRNNRDTYYYLSRVGWAMLLISLFFIVLALVPGFLATFLPFKAVPVLYCVLSWLAFFFIILAACLYTGCYVKARKTFRNSGRSARLGPKNFAFIWTSVFLMLVNAIWSTIFSATHKAHSTYSDHDMYAQYESPSVDTGAQMEKSTYNSGATDGAGPITAAPVVGQPQPTTTTTPAGNGKFFQKLKTRKQVPSAELEPAGDGGLAGPVTVRD", "text": "FUNCTION: Involved in sporulation and affects the sphingolipid composition of the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Concentrates within cortical patches at the membrane. SIMILARITY: Belongs to the SUR7 family."}
+{"protein": "MNAGSDPVVIVSAARTAIGSFNGALSTVPVHEMGTTVIKEVLQRAKVAPEEVSEVIFGHVLTAGCGQNPTRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAAQSIAMGDSTIVVAGGMENMSKAPHLTHLRTGVRMGEVPLADSILCDGLTDAFHNYHMGITAENVAKKWQVSREAQDKVAVLSQNRAEHAQKAGHFDKEIVPVLVSSRKGLTEVKIDEFPRHGSNLEAMGKLKPYFLTDGTGTVTPANASGMNDGAAAVVLMKKTEAERRMLKPLARIVSWSQAGVEPSVMGVGPIPAIKQAVAKAGWSLEDVDLFEINEAFAAVSAAIAKELGLNPEKVNIDGGAIALGHPLGASGCRILVTLLHTLERVGGTRGVAALCIGGGMGVAMCVQRG", "text": "FUNCTION: Involved in the biosynthetic pathway of cholesterol. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
+{"protein": "MRVLFIIAVLALISVGCYASEMKDRSSRNEVLSAIFAIEEPQERDCLGLFWICNYMDDKCCPGYKCERSSPWCKIDIWG", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 35 (Jztx-27) subfamily."}
+{"protein": "MSVSAIFGTGIVTVAASPVLRQFQVPKLGNGGGLGMVIECSSRPQKKSTAHHRKTRPKKTQPWDIKRKPTVYAPLPPLPAEWSPFTLASDDGGAATAAGDLVSGAA", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cL38 family."}
+{"protein": "MSYGPLDMYRNPGPSGPQPRDFNSIIQTCSGNIQRISQATAQIKNLMSQLGTKQDSSKLQENLQQLQHSTNQLAKETNELLKELGSLPLPLSASEQRQQKLQKERLMNDFSSALNNFQVVQRKVSEKEKESIARARAGSRLSAEDRQREEQLVSFDSHEEWNQMQSQEEEAAITEQDLELIKERETAIRQLEADILDVNQIFKDLAMMIHDQGDLIDSIEANVESSEVHVERATDQLQRAAYYQKKSRKKMCILVLVLSVIVTVLVVVIWVASK", "text": "FUNCTION: SNARE promoting fusion of transport vesicles with target membranes. Together with SNARE STX6, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway. Through complex formation with GRIP1, GRIA2 and NSG1 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting. SUBCELLULAR LOCATION: Endosome membrane; Single-pass type IV membrane protein Golgi apparatus membrane; Single-pass type IV membrane protein Endomembrane system; Single-pass type IV membrane protein; Cytoplasmic side Early endosome membrane; Single-pass type IV membrane protein Recycling endosome membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the syntaxin family."}
+{"protein": "MPTTQKTLMFLSGFLTSLGSVVVICSILATQAWITSRIFFTDAISNGTIVITYGLFRGTSAQELNEGLQDLDKNFEVLGILDNSSQKSLHLVVILLLILSLAASVLSSVFTFYNSISNPYQTFLGPMGVYTWNGLSASFVFLAMVLFVGNAESNHLSDKLSQKLYPDTTNKRTTHTYGYSFWLTLHVIFLNIVTAVIIIFYQKARYRQKQEQRKPVEYAPRDGILF", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the clarin family."}
+{"protein": "MLFLHDVWVNWFEGEENGYNVCHFHEWRKEDTVELLDQVPLLRVPSVLFHYIENDLSELPKGLLEDVHQKSYIRKNHERTKLEYCFVVTDGIGILAVDTIGYTIPVRKSRLIPRQEQLVYEMVKDVEPETYEFEPKKLESSKEYHILSLAPEHVRGLTRKERQIKQLMFMALDQLKGLKNRAEIGYWYTEWNPHMYEQIKRMSFEEIWDMLYNETIEGWSDKHLAFCENLIKGQPFFEKLWEMENESKVN", "text": "SIMILARITY: Belongs to the UPF0736 family."}
+{"protein": "MVFPAKRLCVVPSMEGVRWAFSCGTWLPSRAEWLLAMRSIQPEEKERIGKFVFARDAKAALAGRLMIRKLVAEKLNIPWDHIRLQRTSKGKPVLAKDSLNPYPNFNFNISHQGDYAVLAAEPEVQVGIDIMKTSFPGRGSIPEFFHIMKRKFTKKEWETIRSFNDEWTQLDMFYRHWALKESFIKAIGVGLGFEMQRLEFDVSPLNMDIGQVYKETCLILDGEEEKEWAFEESKIDEHHFVAVAVRKPDGSRHQNVSYQDDSKLSQRKFTILNFNDLVASAIPMTPEDPSFWDCFCFTEEILIRNGTKS", "text": "FUNCTION: Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A, regardless of whether the CoA is presented in the free thiol form or as an acetyl thioester, to a serine residue of a broad range of acceptors including the acyl carrier domain of FASN. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family."}
+{"protein": "MAEFEIYREYVDKSYEPQKDDIVAVFRITPAEGFTIEDAAGAVAAESSTGTWTSLHPWYDEERVKGLSAKAYDFVDLGDGSSIVRIAYPSELFEPHNMPGLLASIAGNVFGMKRVKGLRLEDLQLPKSFLKDFKGPSKGKEGVKKIFGVADRPIVGTVPKPKVGYSAEEVEKLAYELLSGGMDYIKDDENLTSPAYCRFEERAERIMKVIEKVEAETGEKKSWFANITADVREMERRLKLVAELGNPHVMVDVVITGWGALEYIRDLAEDYDLAIHGHRAMHAAFTRNAKHGISMFVLAKLYRIIGIDQLHIGTAGAGKLEGQKWDTVQNARIFSEVEYTPDEGDAFHLSQNFHHIKPAMPVSSGGLHPGNLEPVIDALGKEIVIQVGGGVLGHPMGAKAGAKAVRQALDAIISAIPLEEHAKQHPELQAALEKWGRVTPI", "text": "FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3- phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase. SIMILARITY: Belongs to the RuBisCO large chain family. Type III subfamily."}
+{"protein": "MKKNQFLKESDVTAESVFFMKRRQVLKALGISATALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPYVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYAAQVASLYRGLDLRENF", "text": "FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons (PubMed:26641313). Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine (PubMed:26641313). 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 (PubMed:26641313). The catalytic subunit MsrP is non- stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide (PubMed:26641313). Can catalyze the reduction of a variety of substrates in vitro, including dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide (PubMed:15355966). Cannot reduce cyclic N-oxides (PubMed:15355966). Shows no activity as sulfite oxidase (PubMed:15355966). SUBCELLULAR LOCATION: Periplasm Note=Is attached to the inner membrane when interacting with the MsrQ subunit. SIMILARITY: Belongs to the MsrP family."}
+{"protein": "LVTLVFV", "text": "FUNCTION: cCF10 is involved in the conjugative transfer of the hemolysin plasmid pCF10."}
+{"protein": "MDKVTDNSPDVESTESTEGSFPTVGVDTGDTITATLATGTENVGGGGGAFGGASESSAAIHATAKWSTAQLKKHQAEQAARAAAAEAALAKAKSQRDALTQRLKDIVNDALRANAARSPSVTDLAHANNMAMQAEAERLRLAKAEQKAREEAEAAEKALREAERQRDEIARQQAETAHLLAMAEAAEAEKNRQDSLDEEHRAVEVAEKKLAEAKAELAKAESDVQSKQAIVSRVAGELENAQKSVDVKVTGFPGWRDVQKKLERQLQDKKNEYSSVTNALNSAVSIRDAKKTEVQNAEIKLKEAKDALEKSQVKDSVDTMVGFYQYITEQYGEKYSRIAQDLAEKAKGSKFNSVDEALAAFEKYKNVLDKKFSKVDRDDIFNALESITYDEWAKHLEKISRALKVTGYLSFGYDVWDGTLKGLKTGDWKPLFVTLEKSAVDFGVAKIVALMFSFIVGAPLGFWGIAIITGIVSSYIGDDELNKLNELLGI", "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: Host membrane. SIMILARITY: Belongs to the channel forming colicin family."}
+{"protein": "MTSVNLSRAPAAITRRRLQLQPEFHAECSWLKSSSKHAPLTLSCQIRPKQLSQIAELRVTSLDASQASEKDISLVQTPHKVEVNEKIEESIEYVQNLLMTSGDGRISVSPYDTAVIALIKDLKGRDAPQFPSCLEWIAHHQLADGSWGDEFFCIYDRILNTLACVVALKSWNLHSDIIEKGVTYIKENVHKLKGANVEHRTAGFELVVPTFMQMATDLGIQDLPYDHPLIKEIADTKQQRLKEIPKDLVYQMPTNLLYSLEGLGDLEWERLLKLQSGNGSFLTSPSSTAAVLMHTKDEKCLKYIENALKNCDGGAPHTYPVDIFSRLWAIDRLQRLGISRFFQHEIKYFLDHIESVWEETGVFSGRYTKFSDIDDTSMGVRLLKMHGYDVDPNVLKHFKQQDGKFSCYIGQSVESASPMYNLYRAAQLRFPGEEVLEEATKFAFNFLQEMLVKDRLQERWVISDHLFDEIKLGLKMPWYATLPRVEAAYYLDHYAGSGDVWIGKSFYRMPEISNDTYKELAILDFNRCQTQHQLEWIHMQEWYDRCSLSEFGISKRELLRSYFLAAATIFEPERTQERLLWAKTRILSKMITSFVNISGTTLSLDYNFNGLDEIISSANEDQGLAGTLLATFHQLLDGFDIYTLHQLKHVWSQWFMKVQQGEGSGGEDAVLLANTLNICAGLNEDVLSNNEYTALSTLTNKICNRLAQIQDNKILQVVDGSIKDKELEQDMQALVKLVLQENGGAVDRNIRHTFLSVSKTFYYDAYHDDETTDLHIFKVLFRPVV", "text": "FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including sclareol, a diterpene-diol that is used as fragrance and flavoring, and has anticancer effects (able to kill leukemic and colon cancer cells by apoptosis) (Probable). Sclareol can also be used as synthesis precursor of ambergris substitution fragance products such as ambrox (Probable). Terpene synthase that produces 8-hydroxycopalyl diphosphate from geranylgeranyl diphosphate (GGPP) (PubMed:23113661, PubMed:22959531). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MADAEDIEPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVSPDEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDCLMKILTERGYSFTTSAEREIVRDMKEKLAYVALDYEQELETAKSSSAVEKSYELPDGQVITIGAERFRCPEVLFQPSLVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWITKGEYDESGPSIVHRKCF", "text": "FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. 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": "MSSIARPPDPCLVAIILIVRSRAGPRLVFHYPPNPLSENGLRPARKERRTSRSKNGQDYKSNESSSSEESGSSSDDDEDEHQRQLQSQSQSQSHLSGSVVSGRRSSNFGLDDHVAMSVSPGGDSQRAGSMGSGSGRTSFRKRGGNSDVEEDSGAASDRQEDGSGGAGGPYRPPWESLLGLPADVWEKLLSPSPAWHKRRFEVGINDLAFIGWPVFVREDGTWRKQRRKKKKKRRADWEGGELGHNENAEDAPDDEDGDAGGNASGGGGLMAASTETLSPKQVTLSEAKRGSGSSGKAARSLVDCLDGDDKDSMTMFNVVFVLDPPLLEYSMRTKEVYDNIIKKFAKALKWEQARTDYVWREAQHISHLKEKAKERRTSLNTLYTELITQSSLARAIYTVHTSISASKIASVPLSPDVSISLQIPPLTSTPYLPGPTDKAYPGLWLTTADSVTPVEDPTADEYTAPHQVLAKHFALLLLDNEAAILRDVEASGGALAPALAHYLRCSKPTKSFAQISASSGIPLSTIQMLASHLVYWRRARAIPPIHQRDTYIVSPNCDLSKLEVATAAYQAAFPTLPSLPKMLSALSGTPRPYGSFIPSKDHKETYFAILAWLLRGGWVTQLRSFARVKVTPEIKMAVEVALRREEVDKYLRKGRSLEAQKSTDGENGNEEDENDDASSSSSSSLASQGSGEETPMPGRYQQESNPRLSHSMLDRNTSLRTSSLILFPHRASPLESRWLEQIVSRFPEHPRSAGRHRRGEGSNAGGGEIDPEYAALSTPMKDLWPTYIKYFNGLDALEKIPVREGLKRKFVWQVLTRLGLVTSQQSSIELDPREQVLVSVRHW", "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": "GKPFYPPPIYPEDM", "text": "FUNCTION: Stimulates insulin release. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Tryptophillin subfamily."}
+{"protein": "MDEVKEFTSKQFFYTLLTLPSTLKLIFQLEKRYAIYLIVLNAITAFVPLASLFIYQDLINSVLGSGRHLINIIIIYFIVQVITTVLGQLESYVSGKFDMRLSYSINMRLMRTTSSLELSDYEQADMYNIIEKVTQDSTYKPFQLFNAIIVELSSFISLLSSLFFIGTWNIGVAILLLIVPVLSLVLFLRVGQLEFLIQWQRASSERETWYIVYLLTHDFSFKEIKLNNISNYFIHKFGKLKKGFINQDLAIARKKTYFNIFLDFILNLINILTIFAMILSVRAGKLLIGNLVSLIQAISKINTYSQTMIQNIYIIYNTSLFMEQLFEFLKRESVVHKKIEDTEICNQHIGTVKVINLSYVYPNSNAFALKNINLSFEKGELTAIVGKNGSGKSTLVKIISGLYQPTMGIIQYDKMRSSLMPEEFYQKNISVLFQDFVKYELTIRENIGLSDLSSQWEDEKIIKVLDNLGLDFLKTNNQYVLDTQLGNWFQEGHQLSGGQWQKIALARTFFKKASIYILDEPSAALDPVAEKEIFDYFVALSENNISIFISHSLNAARKANKIVVMKDGQVEDVGSHDVLLRRCQYYQELYYSEQYEDNDE", "text": "FUNCTION: Probably implicated in the export process of the lantibiotic nisin. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Nisin exporter (TC 3.A.1.111.3) family."}
+{"protein": "APGNKAECEREKGYCGFLKCSFPFVVSGKCSRFFFCCKNIW", "text": "FUNCTION: Has antibacterial activity against the Gram-positive bacterium S.aureus 1056 MRSA (MIC=1.25 ug/ml) and the Gram-negative bacterium E.coli O157:H7 (MIC=0.96 ug/ml). Has antifungal activity against the yeast C.albicans 3153A (MIC=6.20 ug/ml). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "MPHHEFECSKVIPERKKHAVIKGKGETLADALPQGYLNTIPGSISERGCAYCVAKHVIGTPMKDVIHISHGPVGCTYDTWQTKRYISDNDNFQLKYTYATDVKEKHIVFGAEKLLKQNIIEAFKRFPQIKRMTIYQTPCTALIGDDINAIAEEVMEEMPEVDIFVCNSPGFAGPSQSGGHHKINIAWINQKVGTVEPEITGDHVINYVGEYNIQGDQEVMVDYFKRMGIQVLSTFTGNLSYDGLRAMHRAHLNVLECARSAEYICNELRVRYGIPRLDIDGFGFKPLADSLRKYGMFFGIEDRRKAIIDEEVARWKPELDWYKERLMGKKVSVWPGGSKLWHWAHVIEEEMGLKVVSVYTKFGHQGDMEKGMPRCGEGTLAIDDPNELEGLEALEMLKPDIILTGKRPGEVAKKVRVPYLNAHAYHNGPYKGFEGWVRFARDIYNAIYSPIHQLSGIDITKDNAPEWGNGFRTRQMLSDGNLSDAVRNSETLAQYTGGYDSVSNVREREYPAFERKVG", "text": "FUNCTION: This iron-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Other nitrogenase complexes utilize a molybdenum-iron protein or a vanadium- iron protein."}
+{"protein": "MTAEDAAAAMSSDSAAGGAASAKAPEGVAGAPNEAALLALLARTGYRMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVTYCHKGEAKRAVRELNNHEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFASREDAVLAMNSLNGTELEGSCLEVTLAKPVDKEQYSRYQKAAKGGGAAEAAAPQPGYVYSCDPYTLAYYGYPYNALIGPNRDYFVKAGSIRGRGRGAAGSRAPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEISAVNPVAIKPGTVAIPAIGAQYSMFQAAPAPKMIEDGKIHTMEHMISPIAVQPDPASAAAAAAAAAAAVIPAVSTPPPFQGRPITPVYTVAPNVQRIPAAGLYGAGYVPFAAPATATLATLQKNAAAAAVYGGYAGYIPQAFPAATIQVPIHDVYPTY", "text": "FUNCTION: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing. Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules. Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10. Also involved in the alternative splicing of several genes including TJP1. Binds the pre- mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs (By similarity). Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RRM RBM47 family."}
+{"protein": "MASLKKSLFLVLFLGLLSLSICEEQKRENEEDAEDENHEEESEEKRGLLDFAKHVIGIASKLGKRSEEKRFWPFMGKRSEEKRFWPFMGKRSEEKRFFRVLAKLGKLAK", "text": "FUNCTION: Fallaxidin-2.1 shows no antibacterial activity against Gram- positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. FUNCTION: Fallaxidin-3.2 shows antibacterial activity against the Gram- positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=500 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram- negative bacteria E.cloacae and E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
+{"protein": "MISFGPAQESSLKMEVQSVSSEVNGHQIMDEPMEEESYTHCDEGAYKEIPITHHVKEGCEKADPSQFELLKVLGQGSFGKVFLVRKLMGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVMFTEEDVKFYLAELALALDHLHNLGIVYRDLKPENILLDEAGHIKLTDFGLSKESVDQDKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSLGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSLEAQGLLRMLFKRNPSNRLGAGPDGVEEIKRHTFFSTIDWNKLYRRELQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGIPPSANAHQLFKGFSFVAPVSLEESKSAPLVNILPIVQVHGSSAQFSDVYELKEDIGVGSYSICKRCIHRVTAMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDEGRFVYLVTELMKGGELLDKILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSGNPDSIRICDFGFAKQLRGDNGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSGGNWDSVSDSSKDLLSHMLHVDPHHRYTAEQVLKHSWIACRDQNPHFQLTRHEAPHLVKGAMAATYSALNHKTCKPVLEPVAASSLAQRRNMKKLTSTDMS", "text": "FUNCTION: Serine/threonine kinase that may play a role in mediating the growth-factor and stress induced activation of the transcription factor CREB. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily."}
+{"protein": "MSFKPIDPKRDEIRRYLERGSVLDSLTKLFIRVIKERPENPMDYIRNHIGVVRHQHDKYERLQQDLQLANEEIQRLRAIINGINPDVLQGHQPVASSEVVVATEAPQTVAESTEAAEQQQQQQQQENGETELEKPNESSADVAEITAAVEACQIEGNSVVTTDEAAQPSPTVQAEASGSSE", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AMY1 family."}
+{"protein": "MNFIKRAFWNMKAKKGKTLLQLFVFTVICVFVLSGLAIQSAAQKSSELARQELGGSVTLQVDRQKQMEKQQDSGEKRSFESTPIKVSDANKLAALDHVKSYNYTTSASANAGNFDAIESSSSSDSSSSSSSSNAKNSQGGGQGGPQMVQADLSIEGVISTALVDDFSDGDSKITDGRAITKSDVGKKVTVINETLAEENDLSVGDSITIESATDEDTTVKLKIVGIYKTTSSGDDQAQNFSFLNPYNKLYTPYTATAALKGDDYKNTIDSAVYYMDDAKNMDTFVKAAKKTSIDFDTYTLNTNDQLYQQMVGPIENVASFSKNVVYLVSVAGAVILGLIVMMSIRERKYEMGVLMAIGEKRWKLIGQFLTEILIVAVIAIGLASVTGNLVANQLGNQLLSQQISSSTDSTQTASGQMPGGGGGMGGKMFGHSSSNVDVIDSLNVAVSMNDMLILGGIGILIAIIATLLPSISVLRLHPKTILTKQE", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-4 integral membrane protein family."}
+{"protein": "MGCCFTKRRKSEKAEGEEEQPKLYSWDQREKVDPKDYMFSGLKDETVGRLPGKVAGQQFVIQDCENCNIYIFDHSATITIDDCTNCVIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSTNIKFGCFQWYYPELAAQFKDAGLSIFNNIWSHVHDFTPVSGELNWSLLPENAVVQDYVPIPMTEEFKAVRISTEANRSIVPVSRGQRQKYSDESCLVVLFADDYTTANARKLIDEMVGKGFSLVQTKEMSMKTEDAQRVFQEKASDFLLLLNKGPVIALEFNGDDAVQECHLIVNGMFNGTKMFVSEKKETASGDVDSFYNFAEIQMGI", "text": "FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cell projection, cilium Note=Detected predominantly at the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus. SIMILARITY: Belongs to the TBCC family."}
+{"protein": "MAGSSSSKEIVDAVEKWMAFPTSGGGGATAGLEIVAEDAPSGSSGAHQQQAWRPVAPATAGRDSGGTGSGKSSVDGGVGRASHDSLPRVSQELKDALSSLQQTFVVSDATRPDCPIIYASEGFFTMTGYSPREVVGRNCRFLQGPDTDAAEVAKIRDAVKHGRSFCGRLLNYRKDGAPFWNLLTVTPIRDDNGKVIKFIGMQVEVSKYTEGLSDKRMRPNELPVSLIRYDERQKDKAMSSMTEVVQTVKQPRGARAPADAALLTPPKMSDADKMAAMSPVVAPGTPSGGGGGAGSFKSPLWDLKKEESRLSRLASGRKSGRSSLMGFKIGKRSSVGSREAPAVVEEPAPAPPPAPEVVERTDSWERAEREKDIRQGIDLATTLERIEKNFVITDPRIPDNPIIFASDSFLELTEYTREEILGRNCRFLQGPETDQGTVDKIREAIREQKEITVQLINYTKSGKKFWNLFHLQPMRDQKGELQYFIGVQLDGSDHVEPLRNRLSENTEIQSAKLVKATAENVDDAVRELPDANLRPEDLWAIHSMRVSPKPHKRNNPSWIAIEKATNLGEKIGLKHFKPVKPLGCGDTGSVHLVELQGSGELFAMKAMDKSVMLNRNKVHRACIEREIYALLDHPFLPTLYTSFQTPTHVCLITDFCPGGELFAVLDRQPMKIFREECARFYAAEVVIGLEYLHCLGIIYRDLKPENILLQADGHIVLTDFDLSFLTTSKPHVIKNSTSLKRRRSQEFLPPTFVSEPSTPSNSFVGTEEYIAPEVITGAGHTSAIDWWALGILLYEMLYGRTPFRGKNRKKTFYNILHKDLTFPSSIPVSLAAKQLIHGLLQRDPSNRIGSNAGANDIKQHSFFQDINWPLIRCMSPPELDVPLKLIGKETQPKAKPDEDVPLNLDTF", "text": "FUNCTION: Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for phototropic responses. Regulates a wide range of physiological activities in plants that maximize the efficiency of photosynthesis, such as chloroplast relocations, stomata opening, and leaf expansion (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MKKQQFIDMQEQGTSTIPNLLLTHYKQLGLNETELILLLKIKMHLEKGSYFPTPNQLQEGMSISVEECTNRLRMFIQKGFLFIEECEDQNGIKFEKYSLQPLWGKLYEYIQLAQNQTQERKAEGEQKSLYTIFEEEFARPLSPLECETLAIWQDQDQHDAQLIKHALKEAVLSGKLSFRYIDRILFEWKKNGLKTVEQAKIHSQKFRRVQAKQNEPQKEYKRQVPFYNWLEQ", "text": "FUNCTION: Probable component of primosome involved in the initiation of DNA replication."}
+{"protein": "METQSTGTEDGFTPVTHRGGRRAKKRQAEQSSAAGQDGEAGRMDTEEARPAKRPVFPPLSGDQLLTGKEETRKIPVPGNRYTPLKENWMKIFTPIVEHLGLQIRFNLKSRNVEIRTCKDTKDVSALTKAADFVKAFVLGFQVEDALALIRLDDLFLESFEITDVKPLKGDHLSRAIGRIAGKGGKTKFTIENVTRTRIVLADVHVHILGSFQNIKMARTAICNLILGNPPSKVYGNIRAVASRSADRF", "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. 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": "MIELKHVTFGYNKKQMVLQDINITIPDGENVGILGESGCGKSTLASLVLGLFKPAKGEIYLSDNAVLPIFQHPLTSFNPDWTIETSLKEALYYYRGLTDNTAQDQLLLQHLSTFELNAQLLTKLPSEVSGGQLQRFNVMRSLLAQPRVLICDEITSNLDVIAEQNVINILKAQTITNLNHFIVISHDLSVLQRLVNRIIVLKDGMIVDDFAIEELFNVDRHPYTKELVQAFSY", "text": "FUNCTION: Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MAQENAAFSPGSEEPPRRRGRQRYVEKDGRCNVQQGNVRETYRYLTDLFTTLVDLQWRLSLLFFVLAYALTWLFFGAIWWLIAYGRGDLEHLEDTAWTPCVNNLNGFVAAFLFSIETETTIGYGHRVITDQCPEGIVLLLLQAILGSMVNAFMVGCMFVKISQPNKRAATLVFSSHAVVSLRDGRLCLMFRVGDLRSSHIVEASIRAKLIRSRQTLEGEFIPLHQTDLSVGFDTGDDRLFLVSPLVISHEIDAASPFWEASRRALERDDFEIVVILEGMVEATGMTCQARSSYLVDEVLWGHRFTSVLTLEDGFYEVDYASFHETFEVPTPSCSARELAEAAARLDAHLYWSIPSRLDEKVEEEGAGEGAGAGDGADKEQNGCLPPPESESKV", "text": "FUNCTION: This receptor 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 (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ9 subfamily."}
+{"protein": "MLAYPTTSSPWPPRHHGAAAAPAARRHMAAAAARGKRRGAGAAAAEGADEAAEAADLVRFFLRRTSGGKERLVAVLDRHVKVVRTEHCFLLFEELGRRDGWLQCLEVFRWMQKQRWYVADNGIYSKLISVMGRKGQIRMAMWLFSQMRNSGCRPDTSVYNSLIGTHLHSRDKSKALAKALGYFEKMKTIDRCQPNIVTYNILLRAFAQAGDTKQLDILFKDLDESPVSPDIYTYNGVMDAYGKNGMITEMESVLVRMKSNQCRPDVITFNILIDSYGRKQAFDKMEQVFKSLLRSKEKPTHPTFNSMITNYGKARLREKAECVLDKMTEMGFKPNYVTQECLIMMYAYCDCVSRARQIFDELVSSQNNVHLSSVNAMLDAYCMNGLPMEADQLLDSVIKKGAVPSASTYKLLYKAYTKANDKKLIQKLLKRMNSQGIVPNKKFFLDALEAFGNTDKKPRTVPSKNSASKPDVESANNSGTDTSSKPNLSVWQVAA", "text": "FUNCTION: Involved in the biogenesis of the plastid translation machinery by promoting the splicing of group II introns in chloroplasts. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. P subfamily."}
+{"protein": "MTWPLPDRLSINSLSGTPAVDLSSFTDFLRRQAPELLPASISGGAPLAGGDAQLPHGTTIVALKYPGGVVMAGDRRSTQGNMISGRDVRKVYITDDYTATGIAGTAAVAVEFARLYAVELEHYEKLEGVPLTFAGKINRLAIMVRGNLAAAMQGLLALPLLAGYDIHASDPQSAGRIVSFDAAGGWNIEEEGYQAVGSGSLFAKSSMKKLYSQVTDGDSGLRVAVEALYDAADDDSATGGPDLVRGIFPTAVIIDADGAVDVPESRIAELARAIIESRSGADTFGSDGGEK", "text": "FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues (PubMed:16468985). In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins (PubMed:17082771). One function of the proteasome is to contribute to M.tuberculosis ability to resist killing by host macrophages, since the core proteasome is essential for persistence of the pathogen during the chronic phase of infection in mice (PubMed:18059281). Likely functions to recycle amino acids under nutrient starvation, thereby enabling the cell to maintain basal metabolic activities (PubMed:20711362) (By similarity). The mechanism of protection against bactericidal chemistries of the host's immune response probably involves the degradation of proteins that are irreversibly oxidized, nitrated, or nitrosated. A proteolysis- independent activity of the proteasome core is required for optimal growth of M.tuberculosis in mouse lungs and for RNI resistance; in contrast, long-term survival of M.tuberculosis in stationary phase and during starvation in vitro and in the chronic phase of mouse infection required a proteolytically active proteasome (PubMed:20711362). 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": "MASEWPETSRASSVEENPKLNIPEIVESVSDSKPSLKNQFSTTVIDSSDLNVFNDGAETTVKEQEFTSSELRRLQKLRLKMDLRIIPCLWILYFLSCCLRFTVSLSFTMNTAQGHSLIQTLSGYSAHYLALGLALFYVGYIIFEVPSNLMMAFIEPRIWVSRIQLTIGVVGACHAVLGTKHGNAQSYVALRFFLGVAESGLWPGLAYYMSRWYRGKHLGKRIGWYYTAAQIAAAAVSLVSAGFQKMDGARGLYGYQWMFLIWGVVAIAQALSIPWWLPAVASKEHRKSLSSFIPLPKWMKTLSPQRIGFLTPADKSLHSRYIAEMNVGKRWQWSDLLKSCLDLRVWPFILMYFGIVGVGNGIFNYCTLIIEEINPSFSGIDISLLNAPIWLADALGIVTVMPLYDRFHKKFSFFTGSCLIIIAGLAVANYAPRAWSRYGGLLMIGFGLGPTVPICMAWCSASMAKTYGDVGVASSLALVTGLGNLGSVVTTYALYSGWPGDPTFRKSNDVCIALIGVSIIACGIEFLLDKTGFGQFNASFNNHDHEVEDEQEMTDIKPALPSSQQADA", "text": "FUNCTION: Involved in uptake of biotin and desthiobiotin with the concomitant entry of protons. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Allantoate permease family."}
+{"protein": "MRLIGMPKEKYDPPDPRRIYTIMSAEEVANGKKSHWAELEISGRVRSLSTSLWSLTHLTALHLNDNYLSRIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNNNLLRVLPYELGRLFQLQTLGLKGNPLSQDILNLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKERDQILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAKIMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAADKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVADNHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENNITGCPHPHIPSDHFSLLTQLELHPPLLPLVNGVHLPNRR", "text": "FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Catalytic 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. May be involved in the deadenylation-dependent degradation of mRNAs through the 3'-UTR AU-rich element-mediated mechanism. Involved in deadenylation-dependent degradation of CDKN1B mRNA. Its mRNA deadenylase activity can be inhibited by TOB1. Mediates cell proliferation and cell survival and prevents cellular senescence. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. SIMILARITY: Belongs to the CCR4/nocturin family."}
+{"protein": "MLTPFNNFFQQRQNYHSSVIDHFENPRNVGSYDKSANDVGTGLVGAPACGDVMKLQIKVENDIIKDAKFRTFGCGSAIASSSLATEWIKGKSISDSLKITNKDIAKKLSLPPVKLHCSMLAEDAIKAAISDYQKKNGL", "text": "FUNCTION: Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitosomes, which is required for maturation of both [2Fe-2S] and [4Fe-4S] proteins (PubMed:18311129). First, a [2Fe- 2S] cluster is transiently assembled on the scaffold protein ISU1. In a second step, the cluster is released from ISU1, transferred to a glutaredoxin, followed by the formation of [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=It is unknown how the different localizations of several ISC components to mitosomes and cytoplasm can be reconciled with the usually tightly coordinated function of these components. SIMILARITY: Belongs to the NifU family."}
+{"protein": "MAAPGGVLNCEDFSLFQEVLKVMRTIDDRIVHSLNTTVPTASFSGKVDATQTCKELYESLMEAHLSRDKAIKSCIKETSAVVSQLREERAKDSDNLSVIKQLRKEQTKLKLMQSELNVEEVVNDRSLKVFNERCRIHYTPPKIK", "text": "SIMILARITY: Belongs to the MIX23 family."}
+{"protein": "MAAHRIRATTNNNTSLPRCKSEGTLIDLSEGVSEASLTDVKVPSPSALRLDATASFGAAREVVAIKDCCPSSFTTLKFSKGDRLYVLDSSGAEWWYAHNNTEMGYIPAAYVEPINYRDSSFSDSGMIDTVGDCNEEAAKEMDLLGEWAGVILKPTTFQNGNPFAATNSSTNPFLNGGPQSPLDQNSNEKSVDLLLFDTLAPSVPNSTSITADINGFGSGVLNMNPLSPTVGVGQTLRRDNPFFRSKRSYSLSELSILQAQSDAPQASTGFFGGLKAPAPEQFQSREDFRTAWLTHRKLARSCHDLDSLGQNPGWGQTQPVETNIVCRLDSSGGAVQLPDANISIHIPEGHVAPGDTQQISIKALLDPPLELNNDRCTTVSPVVEIKLSNMEIRTTVTLEMKVSVVVKIESRQTTEILCVRSDCKEGPYTPIPQAYIYGDMVQVCLDNLEPCMYVCVVAQSKSIAPDSTVWEHVVKKITLGVYGPKHIHPSFKTVVAMFGHDCAPKTLLVSEVGKQAQAVPPVALQLWGKHQFVLSRPQDLRVGVYSNMANYEVKASEQARVVRGFQVKLGKVSRLVYVIASRNADDVSDFTLRIQIKDDQDCILAQFCVQTPTPPPKAGPKTSVQRRFLKKKEVGKIVLSPLAITTKYPVFQDRRINNLKFGKLIKTVIRQTKNQYLLEYKKGDFVALLSEEKIRLKGQLWTKEWYIGYYQGRLGFVHAKNVLVVGKVKPIYFSGPDLTTSLFLEQILKPCKFLTYIYASVRTILMENIGNWRAFADSLGYINLPLTHFCRAELDSEPERVASVLEKLKEDCNNTESKERKSFQKELLTALLKMDCQGLVARLVMDFVLLTTAVELAGRWRELAEKLAKVSRQQMDAYEAPHRDKSGVVDSEAMWKPAYDFLVTWAAQIGDSYRDVIQELHMGLDKMKNPITKRWKHLTGTLILVNCMDALRSSAFSPAAQDDCAI", "text": "FUNCTION: Possible role in regulating endocytosis of the transferrin receptor at the plasma membrane. Alternatively, may function as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy (By similarity). SUBCELLULAR LOCATION: Membrane, clathrin-coated pit Cytoplasmic vesicle, clathrin-coated vesicle Nucleus Note=Specifically associated with transferrin receptor- containing clathrin-coated pits and clathrin-coated vesicles. May also localize to the nucleus (By similarity)."}
+{"protein": "MIKTIKTTPYQDQKPGTSGLRKKVPVFAQENYAENFIQSIFDALEGFEGQTLVIGGDGRYYNREVIQKAIKMAAAAGFGKVLVGQGGILSTPAASNVIRKYKAFGGIVLSASHNPGGPTEDFGIKYNIGNGGPAPEKITDAIYARSKVIDSYKISDAADIDLDKIGSFKVDELTVDVIDPVADYAALMEELFDFGAIRSLIAGGFKVVVDSMSAVTGPYAVEILEKRLGAPKGSVRNATPLPDFGGHHPDPNLVHAKELYDDVMSPEGPDFGAASDGDGDRNMVVGKGMFVTPSDSLAIIAANAKLAPGYAAGISGIARSMPTSAAADRVAEKLGLGMYETPTGWKFFGNLMDAGKVTICGEESFGTGSNHVREKDGLWAVLYWLNIVAARKESVKDIVTKHWAEYGRNYYSRHDYEEVDSDAANTLVAILREKLATLPGTSYGNLKVAAADDFAYHDPVDQSVSKNQGIRILFEGGSRIVLRLSGTGTAGATLRLYVERYEPDAARHGIETQSALADLISVADTIAGIKAHTADSEPTVIT", "text": "FUNCTION: This enzyme participates in both the breakdown and synthesis of glucose. Required for the synthesis of capsular polysaccharide and normal lipopolysaccharide. SIMILARITY: Belongs to the phosphohexose mutase family."}
+{"protein": "MRISIFGLGYVGAVCAGCLTARGHEVIGVDVSSTKIDLINQGKSPIVEPGLEALLQQGIANGRLRGTTDFAEAIRASDVSMICVGTPSKKNGDLGLEYIESVCREIGYVLRDTTRRHTIVVRSTVLPGTVKNVVIPILEDCSGKKAGVDFGVAVNPEFLRESTAIKDYDQPPMTVIGELDSASGDILQALYEELDAPIIRKPIEVAEMIKYTCNVWHATKVTFANEIGNIAKAVGVDGREVMDVVCQDKVLNLSQYYMRPGFAFGGSCLPKDVRALTYRAASLDVRAPLLDSLMRSNESQVQNAFELIEAHDKRKVALLGLSFKAGTDDLRESPLVELAERLIGKGYQLDIYDENVQYARVHGANKDYIESKIPHVSSLLNANLQQVIDNADIIVLGNRDEQFRALALQAPAGKQVIDLVGFMNKPTSTTARTEGICW", "text": "FUNCTION: Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (By similarity). SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase family."}
+{"protein": "MSAQSVEEDSILIIPTPDEEEKILRVKLEEDPDGEEGSSIPWNHLPDPEIFRQRFRQFGYQDSPGPREAVSQLRELCRLWLRPETHTKEQILELVVLEQFVAILPKELQTWVRDHHPENGEEAVTVLEDLESELDDPGQPVSLRRRKREVLVEDMVSQEEAQGLPSSELDAVENQLKWASWELHSLRHCDDDGRTENGALAPKQELPSALESHEVPGTLNMGVPQIFKYGETCFPKGRFERKRNPSRKKQHICDECGKHFSQGSALILHQRIHSGEKPYGCVECGKAFSRSSILVQHQRVHTGEKPYKCLECGKAFSQNSGLINHQRIHTGEKPYECVQCGKSYSQSSNLFRHQRRHNAEKLLNVVKV", "text": "FUNCTION: Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence (By similarity). Has transcription repressor activity in vitro. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MGNEAGPIFEESNAEVGTPPADAVHDDFFFDYKNATGYADDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETDDCDITGDCNETDDCNITGDCNETEVSDAADGTDGMFLKSSSSLKLVALCDGCPTEDSPKSSNAKGKGSSVSAGLLLLAGSTFLVLAVGLSAVLFLGRERQNAVVICDNEVMMEEVPGCLSDASFAVPVTQSSDEARP", "text": "FUNCTION: Supposed to function as cell surface receptor. Possibly involved in receptor-mediated endocytosis. SUBCELLULAR LOCATION: Flagellar pocket. Cell membrane; Single-pass membrane protein Note=Concentrated in the flagellar pocket."}
+{"protein": "MTSVPIFESVSRFLPPANEDEQYWWKITGQHMARMMHEAGYPEDRQVECLLFHRFKVIPCLGPRPRSDTPWYKSRVGGGAADGCPINYSWRFGTADRKPHIRNFIEPLGALTNTPADPLNEVATKALLQDYSMTLPNVDLEAFWTFAPHYRPRIIEKADIEKLAGASLLVGAEMSPDSYTIDIKAYMYPRVPSQTSQLLTTILPQAMRDAYGENVCLDSLNFVHEFMTKDPQGSQLVLTGTTGIDCCKLQDTRVKIYVITRNTSFDHIAAIMTLGGRRPISEELLGQLKALWYELKGAPAELPSSEQLPVQTKPDGSKNPIVVPFYFDIQPRLALPDVKAYIDVSTSPVSDLAAANAVVRHLEQHGSGQNPKAYLNVLKDITPVEELETQKGVLAFYSVAVKKNELDITSYFNPQVYKRYFAHEVHLNGQRRSVFE", "text": "FUNCTION: Prenyltransferase; 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, PubMed:23368997). 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 (PubMed:23758576). Neosartoricin C is a spirocyclic compound that is cyclized through the attack of C3 hydroxyl on C14, followed by dehydration (PubMed:23758576). 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 (PubMed:23758576). Both of these compounds are novel and possibly represent related metabolites of the gene cluster (PubMed:23758576). SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family."}
+{"protein": "MWPLLHVLWLALVCGSVHTTLSKSDAKKAASKTLLEKTQFSDKPVQDRGLVVTDIKAEDVVLEHRSYCSARARERNFAGEVLGYVTPWNSHGYDVAKVFGSKFTQISPVWLQLKRRGREMFEITGLHDVDQGWMRAVKKHAKGVRIVPRLLFEDWTYDDFRSVLDSEDEIEELSKTVVQVAKNQHFDGFVVEVWSQLLSQKHVGLIHMLTHLAEALHQARLLVILVIPPAVTPGTDQLGMFTHKEFEQLAPILDGFSLMTYDYSTSQQPGPNAPLSWIRACVQVLDPKSQWRSKILLGLNFYGMDYAASKDAREPVIGARYIQTLKDHRPRVVWDSQAAEHFFEYKKNRGGRHVVFYPTLKSLQVRLELARELGVGVSIWELGQGLDYFYDLL", "text": "FUNCTION: Saccharide- and LPS-binding protein with possible roles in pathogen sensing and endotoxin neutralization. Ligand-binding specificity relates to the length of the oligosaccharides, with preference for chitotetraose (in vitro) (By similarity). SUBCELLULAR LOCATION: Secreted. Lysosome. SIMILARITY: Belongs to the glycosyl hydrolase 18 family."}
+{"protein": "MRVLLSTCGSRGDVEPLVALAVRLRARGAEVRMCAPPDCADRLAEVGVPHLPLGRSARPAAAGEAKPLTAEDMLRFTTETIAMQFDRIPAAAEGCDAVVTTGLLAAALGVRSVAEKLGIPYFYAFHCPSYVPSPYYAPPPPLGEPPAPEGTDIRALWERNNQSAFRRYGAPLKSQRAAIGLPPVEDIFEHGYTDHPWMAADQVLAPLQPTDLDAVQTGAWILPDERPLSPEMEAFLDAGTPPVYLGFGSLRAPADAAKVAIEAIRAHGRRVILSRGWADLVLPDDRDDCFATGEVNQQVLFRRVAAVIHHGGAGTTHVATRAGAPQILVPQIADQPYYAGRVAELGIGVAHDGPTPTFESLSAALTTALAPETRVRAEAVAGTVLTDGAAAAADLLFAAVGEEKPAVPA", "text": "FUNCTION: D-glucosyltransferase that acts on the aglycone core, transferring D-glucose to the phenolic hydroxyl of OH-Phegly(4) to form a devancoaminyl-vancomycin (DVV) intermediate in the biosynthesis of glycopeptide antibiotic vancomycin. Also able to glycosylate A47934, an antibiotic with a teicoplanin-like heptapeptide, but lacking sugar residues. SIMILARITY: Belongs to the glycosyltransferase 28 family."}
+{"protein": "MSDTEKPIKSEEPVDEGVDRVDEEENVEEPAEDVGEAAEEASEAPEEAPAEAATTTEAAPADDDEDDSDLSDLDEDEIKNAAIEDDDDDYNKLSAHRRKVQSSGKKTLKKRATKDSRAADDDEDEIDHSHIDLDPSMARRREIEARIDAAMKPASQRRKKLGEDDIEMMQDERISNLREKMRNAAIADAESNREGQPATHKLQLLPEVKDVLQKHHLADSILDNNLLEAVRIWLEPLPDASLPSYSIQEELFDALVRLPIKSIHLRESGLGKVVTFYRKSKQPQLRIKRIADKLVADWTRPIMGRSDNYREKVVSTRSFDPSTQEIALAVAAKRAQTLKDGTLAEKQAERRRRAHIPSAQPANYRVAPKSEIIPQNRGGSTNDMTFKRLKGKLGVTKTGKKKSGVSIEGRGLNG", "text": "FUNCTION: Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post- recruitment and recruitment steps of transcription (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IWS1 family."}
+{"protein": "MNVTLLIPARYGSSRFPGKPLAHINGKPMIQHVYERASLAKGLKDIYVATDDVRIKNAVESFGGKVVMTGENAASGTDRIDEAISILGLADDDLVINLQGDQPLIDPIVIEQLVSVCERHAGEFDMATLGVEIKDEAQLNDPNHVKVVFDNNHNALYFSRARIPFGRDTSDYPVYKHIGIYAYTRKFIQTFAKLPLGRLEELEKLEQLRALEYGYKIKVAISAFDFPEVDTPEDIRICEARLTVD", "text": "FUNCTION: Activates KDO8N (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in the Shewanella genus. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsB family."}
+{"protein": "ELLQNSGNPCCDPVTCKPREGEHCISGPCCRNCKFKRAGTVCLDAKGDWMNNYCTGISSDCPRN", "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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIe sub-subfamily."}
+{"protein": "MKIFRCCFKYTLQQKLFILLLTLWLFSLLKLLNVGRLLFPQRDIYLVEYSLSTSPFVRNRFPESGDAARDNVNCSGVYEHEPLEIGKSLEIRRRSIIDLEDGDVVAMTSDCDVYQTLRQYHEKLVSREEEDFPIAYSLVVHKDAIMVERLIRAIYNQHNLYCIHYDLKSPDTFKAAMNNLAKCFPNIFIASKLETVEYAHISRLQADWNCLSDLLKSSVQWKYVINLCGQDFPLKSNFELVTELKSLQGRNMLETVRPPSAKTERFTYHHELRQVPYDYMKLPVKTNVSKGAPPHNIQVFVGSAYFVLSRAFVKYIFNSSLVEDFFAWSKDTYSPDEHFWATLIRIPGIPGGISSSSQDVSDLQSKTRLVKWFYYEGFLYPNCTGSHLRSVCIYGAAELRWLLNEGHWFANKFDSKVDPILMKCLAEKLEEQQRKLIALSSEKFMTEGTRQSHTL", "text": "FUNCTION: Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O- glycan or I-branching enzyme activity. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 14 family."}
+{"protein": "MENLLSVKDLSKQQILDLLALAKAVKANPAEYSQALAGKSIVTIYEKPSLRTRVTFDIGIHKLGGHAVYLDAQNGAIGERETVKDFAANISRWADAIVARVVSHKTLEGLVEHGSVPVVNSLCDLYHPCQALADFLTISEHYEDVSKVKLAYVGEGNNVTHSLMLTGAILGAEVTAVCPRGSSPDAQIVKQAMALAEISGGKINVTDNLDDIVDYDVIYGDTWVSMGDDTPLAQVKEKYMPYQINKALLMRTGIKHVLHCQPAHRELEITSEVMDGEHSLIFDQAENRMHAQNAVLLTLLK", "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": "MGNGGRSGLQQGKGNVDGVAATPTAASASCQYRCIECNQEAKELYRDYNHGVLKITICKSCQKPVDKYIEYDPVIILINAILCKAQAYRHILFNTQINIHGKLCIFCLLCEAYLRWWQLQDSNQNTAPDDLIRYAKEWDFYRMFAIAALEQTAYFIGIFTFLWVERPMTAKKKPNFILLLKALLLSSYGKLLLIPAVIWEHDYTSVCLKLIKVFVLTSNFQAIRVTLNINRKLSFLAVLSGLLLESIMVYFFQSMEWDVGSDYAIFKSQDF", "text": "FUNCTION: Plays a role as a mediator in the endoplasmic reticulum (ER) cholesterol and bile acid homeostasis (PubMed:11063737, PubMed:12145310, PubMed:20663892). Participates in sterol transport out of the ER and distribution into plasma membranes (PubMed:20663892). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ARV1 family."}
+{"protein": "MAGAIIENMSTKKLCMVGVALLLLQVLAFLVGGLIAPKPTSYVNPVAMKCVDVRKNHRSSKWLMPWGTEPCKSIQSFDEAANRMIEANDIVFAAHIPNSQFEMSPWFQFMLVVLQLDIAFKLNNYIEENSMVTLDVSVAYRDDLKEEWKELASSVEQRKLNCILPVEKTLANEGRHYDCDVIPLMELGSVSHKYYLFNIRLPVNERKKANIGIGEIRDLHVVSIFQNGGFTMVWFAMKTFLTPSIIIIMIWYWRRITMMTRSPVLLEKVIFALGFSMTFINIPVEWFSIGYDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQTERNRISVYWKQVGPIAFGSCCLFIFDMCERGVQLKNPFYSIWTTDVGAEIAMAFIIVAGICACLYFLFLCFMVYQVFRNISGKQSNLPAMTKARRLHYEGLIFRFKFLMIITLACAALTIVFFITTQITEGNWKLGDLSIELNSAFFTGVYGMWNLYVFALMFLYAPSHKHYGDGQSNDGAGMSSGEELQLTTTITHIDGPTEVYRLAGKEAQE", "text": "FUNCTION: Required for a subset of Wnt-dependent developmental processes, in particular, eye and pronephros development. Regulates the secretion of wnt4, which is required for eye development (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the wntless family."}
+{"protein": "MSHLRMLVMIEEHGQVSAAAAAMNMTQPAASRMLSEMEAIVKSPLCQRASRGVVLTKFGEALALARRARTILLELREASRELNQMKSGSGGSVYIGAVTAPAISLVVPAIRRAMDTYPGIEINVQVESSNVLARELLAARHDFIIGRIPDDFDPGLFSIHEIGIERACLVVREGHPLMRGEPVTLQDLSGYDWVFQPPGALLRRTMEDVFLTHGVAMPRNVINTPSVVLTLALVCNTNAIAPIAQDMAEFVAGQQADMAEPAFCQRISNSWSSLTASLPPKAGSCRPAPACFMIWCWMKAVS", "text": "FUNCTION: Activator of the expression of chvE when bound to its inducer and represses its expression in the absence of inducer (L-arabinose, D- fucose or D-galactose). Negatively regulates its own expression. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MPVSRMRMRPWLEMQINSNQIPGLIWINKDKMIFQIPWKHAAKHGWDMEKDACLFRSWAIHTGRYKVGEKDPDPKTWKANFRCAMNSLPDIEEVKDKSINKGSSAVRVYRMLPPLTKDQKKERKSKSSREARNKSKRKLYEDMRMEESAERLTSTPLPDDHSSYTAHDYTGQEVEVENTSITLDLSSCEVSGSLTDWRMPMEIAMADSTNDIYQLQVSPLGSSSEDEDEMKSNIIKLLEPTQDWHTTSVEGKGFFTNEPGTQTMCSTFGYKEQDGEIDTSSAELEFRMMDQKSSLDFSWLDTVRPMQAISCSL", "text": "FUNCTION: Transcriptional regulator that specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and activates those genes (By similarity). Acts as a tumor suppressor (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the IRF family."}
+{"protein": "MSDKRIAEESRFAGLALTEEELVARVAWCYYHDGLTQNDIGERLGLPRLKISRLLEKGRQSGVIRVQINSRYEGCLALETELQQRFGLKLVRVLPALNTVPMNVRLGIGAAQSLMGVLEPGQLLAVGFGETTMSCIQHLSGFISSQQVRLVTLSGGVGPYMTGIGQLDAACSVSMIPAPLRVSSAEVAGILKREASVRDVILAATAADAAVVGIGSVNQRRDATILRAGYISEGEQLMYARKGAVGDILGYFLNAAGERVSDLEIHHELLGVTLDELAQLPTIVGVAGGEEKADAIYAALKGRLINGLVTEETTARAVLALAG", "text": "FUNCTION: Regulates transcription of many different genes. In the absence of autoinducer 2 (AI-2), represses transcription of the lsrACDBFG operon and its own transcription. In the presence of AI-2, LsrR is inactivated by binding phospho-AI-2, leading to the transcription of the lsr genes (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SorC transcriptional regulatory family."}
+{"protein": "MAQSKFLREYKLVVVGGGGVGKSCLTIQLIQSHFVDEYDPTIEDSYRKQCVIDDEVALLDVLDTAGQEEYSAMREQYMRTGEGFLLVYSITSRQSFEEITTFQQQILRVKDKDYFPMVVVGNKCDLEGEREVTRQEGEALARSFNCKFIETSAKSRINVDKAFYDIVREIRRYNREMQGYSTGSGGSNAGGPSNKMEVNDSDAEAGCCSKCVLM", "text": "FUNCTION: Modulates the activity of the adenylate cyclase catalytic subunit and therefore affects the biosynthesis of cyclic-AMP (By similarity). Plays a role in both surface attachment and surface recognition of appressoria, a highly specialized infection structure for plant penetration. Regulates appressorium formation by coordinated regulation of cAMP signaling and Pmk1 MAPK pathways (PubMed:24835254). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MNLPPNPVIARGRGRGRKPNNVEANRGFAPSLGQKSDPSHSEGNQASGGNGGGGDAQVGPSIEKSSLSAVQMHKSEGDPRGSVRGRRLITDLVYSRPPGMTSKKGVVGTHITVQANYFKVLKRPNWTIYQYRVDFTPDVEATRLRRSFLYEHKGILGGYIFDGTNMFCINQFKAVQDSPYVLELVTKSRAGENIEIKIKAVGSVQSTDAEQFQVLNLILRRAMEGLDLKLVSRYYYDPQAKINLENFRMQLWPGYQTSIRQHENDILLCSEICHKVMRTETLYNILSDAIRDSDDYQSTFKRAVMGMVILTDYNNKTYRIDDVDFQSTPLCKFKTNDGEISYVDYYKKRYNIIIRDLKQPLVMSRPTDKNIRGGNDQAIMIIPELARATGMTDAMRADFRTLRAMSEHTRLNPDRRIERLRMFNKRLKSCKQSVETLKSWNIELDSALVEIPARVLPPEKILFGNQKIFVCDARADWTNEFRTCSMFKNVHINRWYVITPSRNLRETQEFVQMCIRTASSMKMNICNPIYEEIPDDRNGTYSQAIDNAAANDPQIVMVVMRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIAPRQQKPTGLMSIATKVVIQMNAKLMGAPWQVVIPLHGLMTVGFDVCHSPKNKNKSYGAFVATMDQKESFRYFSTVNEHIKGQELSEQMSVNMACALRSYQEQHRSLPERILFFRDGVGDGQLYQVVNSEVNTLKDRLDEIYKSAGKQEGCRMTFIIVSKRINSRYFTGHRNPVPGTVVDDVITLPERYDFFLVSQAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAESINRAPSAGLQNQLYFL", "text": "FUNCTION: Acts via the piwi-interacting RNA (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. 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. In ovary, associates predominantly with antisense piRNAs that contain uridine at their 5' end. In testis, associates with Su(Ste) antisense piRNAs (most abundant class of piRNAs found in complex with aub in testes) and negatively regulates Ste expression, most likely by cleaving its transcripts. Also in testis, may repress translation of vas when associated with a piRNA derived from chromosome X, termed AT-chX-1, whose sequence shows strong complementarity to vas mRNA. Aub-piRNA complexes from ovary and testis possess RNA cleavage activity. Involved in telomere regulation by repressing specialized telomeric retroelements HeT-A and TART; Drosophila telomeres being maintained by transposition of specialized telomeric retroelements. Also involved in telomeric trans-silencing, a repression mechanism by which a transposon or a transgene inserted in subtelomeric heterochromatin has the capacity to repress in trans, in the female germline, a homologous transposon, or transgene located in euchromatin. Involved in the suppression of meiotic drive of sex chromosomes and autosomes. Involved in transposon silencing in the adult brain. Required for dorsal-ventral as well as anterior-posterior patterning of the egg. Required during oogenesis for primordial germ cell formation and activation of RNA interference. During early oogenesis, required for osk mRNA silencing and polarization of the microtubule cytoskeleton. During mid-oogenesis, required for osk mRNA localization to the posterior pole and efficient translation of osk and grk. During embryogenesis, required for posterior localization of nos mRNA, independently of osk, and pole cell formation. Essential for the formation and/or structural integrity of perinuclear nuage particles. Required for the localization of Mael to the meiotic nuage. Forms a complex with smg, twin, AGO3 and specific piRNAs that targets nos mRNA (and probably other maternal mRNAS) for deadenylation promoting its decay during early embryogenesis. 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. In the oocyte and later in the embryo, concentrates at the posterior pole as a component of polar granules. In the cytoplasm of syncytial embryos, accumulates in discrete foci. SIMILARITY: Belongs to the argonaute family. Piwi subfamily."}
+{"protein": "MSDNKFIIGSEEWCAFPALGVPAIKARVDSGARTSSIHAVNIRPFKREGEPWVSFELHPIQNSRKIILRCESKVVDRRNIKSSNGESEKRYVIASVIQLGGNAWEVELTLTNRDSMGYRMLLGREAMSNKTLVDPSESFCLGEKGDLEVEQLYGVKTAKKSGLKIGLLASNPDLYSNRRIIEAGEQRGHEMVFLNISQCYLKLDASSPEVHYRGGRVLNNVDAVIPRIRPSMTFYGCALTRHFESLNIEALNTSDAITRSRDKLFSLQLLQKNNLDIPTSGFANSPVDTKDLIDMVGGAPLIVKLLEGTQGKGVVLAETTKAAESVINAFKSLRVNLLVQEFIKEAQGKDLRCFVIDGKIVASIERTAAPGEFRANIHMGGSASIVSVSAAEKQLAIKAAKTMGLRVAGVDIIRSSRGPLLLEINSSPGLEGIESATGIDIAGAMIESIEKKLGWKAD", "text": "SIMILARITY: In the C-terminal section; belongs to the RimK family."}
+{"protein": "LCPLDVLQLSSELLDIDGNEVEASRILSDITAFGGIRCPLTVVQSRGIGTIISSPYRFIAEGHPLSLKDMDGWFRVSDDEFNNYK", "text": "FUNCTION: Inhibition of trypsin (By similarity). Has anticarcinogenic activity, prevents transformation of DMBA-treated JB6 cells. Has antipromoter activity, prevents promotion by tetradecanoyl phorbal acetate (TPA) in JB6 cells. Prevents tertiary butyl hydroperoxide- induced mutagenesis. Protects AT base pairs and shows antimutagenesis activity in TA102 and TA104 S.typhimurium mutagenesis tests. Inhibits paw edema formation induced by phospholipase A2 in Swiss Wistar mice. Prevents the release of arachidonate, the parent compound for the synthesis of prostaglandins and prostacyclins. Has antimalarial activity, kills P.falciparum. Has antivenom activity, nullifies the lethal effects of N.naja venom and inhibits phospholipase A2 present in N.naja venom. Has antifungal activity, inhibits cilia formation by A.niger. Is not toxic or allergenic. SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz- type inhibitor) family."}
+{"protein": "MARTFFVGGNFKLNGTKKSIKEIVDRLNTASLPENVEVVICPPATYLDYTVSLVSKKQVTVGGQNTYTKASGAYTGENSVDQLKDVGAKWVILGHSERRTYFHEDDKIVAEKTKFALDQGLGVILCIGETLEEKKAGVTLKVVERQLDAVIAEVKDWTNVVIAYEPVWAIGTGLAATAEDAQDIHHSIRSYLAEKLGKDTAEKTRILYGGSANGANAGTFKDKADVDGFLVGGASLKPEFVDIINSRN", "text": "SIMILARITY: Belongs to the triosephosphate isomerase family."}
+{"protein": "MPDYVNWLRHASPYINSHRDRTFVVMLPGEGVEHPNFGNIVHDLVLLHSLGARLVLVHGSRPQIEARLAARGLAPRYHRDLRVTDAPTLECVIDAVGSLRIAIEARLSMDMAASPMQGARLRVAGGNLVTARPIGVVEGVDYHHTGEVRRIDRKGIGRLLDERSIVLLSPLGYSPTGEIFNLACEDVAMRAAIDLEAEKLILYGAEQGLLDASGKLVRELRPQQVPAHLQRLGNSYQAELLDAAAQACRAGVKRSHIVSYTEDGALLSELFTRTGNGTLVAQEQFEQLREAGIEDVGGLIELIRPLEEQGILVRRSREVLEREIEQFSIVEREGLIIACAALYPIADSEAGELACLAVNPEYRHGGRGDELLERIEERARGLGLKTLFVLTTRTAHWFRERGFQPSSVERLPAARASLYNFQRNSQVFEKSL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily. SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily."}
+{"protein": "MHTGGETSACKPSSVRLAPSFSFHAAGLQMAGQMSHSHQQYSDRRQQNLNDQQASALPYNDQIQQPLPNQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRAEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMSKIVEVLGIPPAHILDQAPKARKFFEKMPEGTWNLKKTKDGKKEYKPPGTRKLHNLLGVETGGPGGRRGGESGHTVADYLKFKDLILRMLDYDAKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFTAAVQAMDCETHSPQVRQQFPPGWTVPEAPTQVTIETHPVQETTFHVPSSQQNVPHHHGNGSHHHHHHHHHHHGQHVLSNRTRTRIYNSPSTSSSTQDSMDVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGTMDVNLTAFSNPRQETGITGHPDYQYSANTGPGHYVTEGHLTMRQGMDREDSPMTGVCVQQSPVASS", "text": "FUNCTION: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Plays an important role in double-strand breaks (DSBs) repair following DNA damage. Mechanistically, phosphorylates RNF169 and increases its ability to block accumulation of TP53BP1 at the DSB sites thereby promoting homologous recombination repair (HRR). Also acts as a positive regulator of transcription by acting as a CTD kinase that mediates phosphorylation of the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A (By similarity). Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily."}
+{"protein": "MKNIEELILKAVELQSNGLVTGQIANELNVSRETVTWLLTRSKKDVVAPAPKDISVTWNSVGQSSYRLRCISQALCDMVIEKLERTQQDADLVIGIGLSGIPIATMMAEELEIDFAIFHDYDDQKGKTNQRGIFSRNFADVEGKKCIIVDDVVSSGATVTDVAEQLREVGATPIAVAVIVDKMNADMIANVPMSSLVRITRVD", "text": "SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
+{"protein": "MYGVGVGGGGGGNYDGGGGNASSLFGGGGFMPSQATNAAEGTSGGGGGFPKSRNAQALLPLTVKQIMDASQTNDDKSNFAVNGMEVSTVRLVGRMLNKLDRVTDVSFTLDDGTGRVPVNRWENDSTDTKEMADIQNGDYVIVNGGLKGFQGKRQVVAYSVRRITNFNDVTHHFLHCVHVHLELTRPKSQVNANTATGTPNQTMPRDSMAYNQSPLTNQASTFSAPQNTGTGTNMIDLVLNVFHDPAVMNDDHGVGVDYVSRRLNLPEETVGKIIIDQVDLGHLYATIDDHHYKSTMNG", "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 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the replication factor A protein 2 family."}
+{"protein": "MPEAIEVRKVPLHSVSDASELAKLIDDGVLEADRVIAVIGKTEGNGGVNDYTRIIADRAFREVLSAKGNRSPEEVAEVPIVWSGGTDGVISPHATIFATVPADKVTKTDEPRLTVGVAMSEQLLPEDIGRTAMITKVAAAVKDAMADAGITDPADVHYVQTKTPLLTIHTIRDAKSRGKTVWTEQTHESMDLSNGGTALGIAVALGEIDMPTDEDVMHSRELFSSVASCSSGVELDRAQIVVVGNARGVGGRYRIGHSVMKDPLDQDGIWAAIRDAGLELPERPHSNDLDGQLVNVFLKCEASQDGTVRGRRNAMLDDSDVHWHRQIKSCVGGVTAAVTGDPAVFVSVSAAHQGPEGGGPVAAIVDLGQ", "text": "FUNCTION: Responsible for the hydrolysis of barbituric acid (2,4,6- trihydroxy-1,3-pyrimidine), an intermediate in the oxidative catabolism of pyrimidines. Catalyzes the hydrolytic opening of the pyrimidine ring of barbituric acid to yield ureidomalonic acid. SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family."}
+{"protein": "MERDFLGAIWRKEEAAGKPEEHSDYRGGGGGASAAMQWQFPATKVGAASSAFMSFRSSAAAAREEDPKEAAVFDRFSLSGFRPPPRPSPGDAFDGAAAMKQRQFGFNGRQQYAAAAQHGHREQGVDSYGVAAPHHFPSPSPSPRHPVPFGHANPMLRVHSLPNVAGGSPYRNQSFSVGNSVAGSTVGVYGGPRDLQNPKVTQMTIFYDGLVNVFDNIPVEKAQELMLLASRASIPSPPSAARKSDSPISAAAKLTVPEALPARQIVVQKPEASVPLVSGVSNPITIVSQAVTLPKSFSSSNDSAGPKSGGLPLAVTPLSQASPSQPIPVATTNASAIMPRAVPQARKASLARFLEKRKERVSSVAPYPSSKSPLESSDTIGSPSTPSKSSCTDITPSTNNCEDSLCLGQPRNISFSSQEPPSTKLQI", "text": "FUNCTION: Repressor of jasmonate responses. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TIFY/JAZ family."}
+{"protein": "MKLARKIKNRLFRSKKKTQKENTAVIVHPADNRVFSLFDKTKRIEENQQVPVRKISEFSWNGSILKIAGYMYIKGLPLQKEDQVRKRLLLVNNGVLFTAVSLRDIPVDQLSIDTSNVPGAYKWAGFSQQINFSKLMNDKPLPQGEYKLFLEIEAVDDQNVKHQEVHTVGNVSNFLSNDVYATKMEFHSAKKLMKFNLIVNYDEGEKTINLSCNKLQEIDPSLLELDTGKEANRFIRKLNTSLFHFAYDVFRLLPIKSNKIVFASDSRLDVTGNFEFVYEELLKREENFDFKFFLKSSIRDRKSLSELMSMAYHFATSKIIFIDDFYPIIYPLKIRKNADLVQLWHAVGAFKTFGYSRIGLPGGPSPHSKNHRNYTKVIVSSENIRKHYAEGFGVDIENVIATGVPRTDFFFDEAKKAFVKERLYTEYPFLKDKKVILFAPTFRGNGQQSAHYPFEVLDFDRLYRELKDEYIFLFKIHPFVRNDANIPYQYSDFFYDFSSFREINELLLVTDVLITDYSSVCFEYALLNKPMIFFSYDVDDYIRKRDFYYDYFDFIPGPLAKTSDQMISIIKEEKYNFEQIDSFVHYFFDDLDGKASERVVDQIVFPQEEEPVDDKVLKR", "text": "FUNCTION: Responsible for the polymerization of the main chain of the major teichoic acid by sequential transfer of ribitol phosphate units from CDP-ribitol to the glycerol phosphate attached to the disaccharide linkage unit. Synthesizes polymers of up to 40 ribitol phosphate units in length. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase family."}
+{"protein": "MGGCFSVSLPCDQVVSQFSQLLCVRGSYIHNLSKNLASLQKAMRMLKARQYDVIRRLETEEFTGRQQRLSQVQVWLTSVLIIQNQFNDLLRSNEVELQRLCLCGFCSKDLKLSYRYGKRVIMMLKEVESLSSQGFFDVVSEATPFADVDEIPFQPTIVGQEIMLEKAWNRLMEDGSGILGLYGMGGVGKTTLLTKINNKFSKIDDRFDVVIWVVVSRSSTVRKIQRDIAEKVGLGGMEWSEKNDNQIAVDIHNVLRRRKFVLLLDDIWEKVNLKAVGVPYPSKDNGCKVAFTTRSRDVCGRMGVDDPMEVSCLQPEESWDLFQMKVGKNTLGSHPDIPGLARKVARKCRGLPLALNVIGEAMACKRTVHEWCHAIDVLTSSAIDFSGMEDEILHVLKYSYDNLNGELMKSCFLYCSLFPEDYLIDKEGLVDYWISEGFINEKEGRERNINQGYEIIGTLVRACLLLEEERNKSNVKMHDVVREMALWISSDLGKQKEKCIVRAGVGLREVPKVKDWNTVRKISLMNNEIEEIFDSHECAALTTLFLQKNDVVKISAEFFRCMPHLVVLDLSENQSLNELPEEISELASLRYFNLSYTCIHQLPVGLWTLKKLIHLNLEHMSSLGSILGISNLWNLRTLGLRDSRLLLDMSLVKELQLLEHLEVITLDISSSLVAEPLLCSQRLVECIKEVDFKYLKEESVRVLTLPTMGNLRKLGIKRCGMREIKIERTTSSSSRNKSPTTPCFSNLSRVFIAKCHGLKDLTWLLFAPNLTFLEVGFSKEVEDIISEEKAEEHSATIVPFRKLETLHLFELRGLKRIYAKALHFPCLKVIHVEKCEKLRKLPLDSKSGIAGEELVIYYGEREWIERVEWEDQATQLRFLPSSRWRWRET", "text": "FUNCTION: Disease resistance (R) protein that specifically recognizes the avrPphB type III effector avirulence protein from Pseudomonas syringae. Also confers resistance against Hyaloperonospora parasitica (downy mildew). Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Requires PBS1 to trigger the defense reaction against avrPphB. In case of infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism via the cleavage of PBS1, suggesting that the cleavage of PBS1 could trigger an exchange of ADP for ATP, thereby activating RPS5. May function as a fine-tuned sensor of alterations in the structure of the effector target PBS1. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the disease resistance NB-LRR family."}
+{"protein": "MGSVDGDFEGLQAADRRAEVIEWLNALLPEYCLPLDSSDDELRELLSDGTVLCHIVNALIPGVLEESWGAYASSDQHAGHVKKFLAVVADMGLPGFSVKDLEEGSMSGVVDCLLVLRESVSSGLRDGTSKAPLRKKWRVPETGEPLVPGVAQGKTSPGEDKRNGLPDPKSQQKTPIFNGRKLREIFQLKRGSYADLPAAKISEMMHSNSLDNAPTQSLLSVVNGILDESIERKKGEIPHRVVYLLRKVVQEIERRLCIQAEHIRSQNVIIKTREDKYHSKIKALEILVNGTNEENQMAINRLQIIKEEKSKIEEKRKLGEQDVARLMKEKEISENTIASLKKEMEVMTSMHEQQLQKIELTAKQMEEHLTTKIKEVESLLVQSNKKIEEVEAASLLKSQLWNKKEGIFQKYMNSQQLYVKGLRISSWSIKNEMHALEMELRDEMSNFGSGLKCLVDAAENYHKVLAENQKLFNEVQELKGNIRVYCRVRPFLPGQDKKSTTVDYIGENGELLISNPFKQGKDGHRMFKFNKVFSPFSSQAEVFSDIQPLIRSVLDGFNVCIFAYGQTGSGKTYTMSGPSTSKQDWGVNYRALNDLFDISLSRRNAFSYEVGVQMVEIYNEQVRDLLSNDIAQKRLGIWSTSQPNGLVVPDASLHPVKSTSDVLDLMEIGQANRAVGSTALNERSSRSHSILTVHVRGLDVKNGSTSRGCLHLIDLAGSERVERSEATGDRLKEAQHINKSLSALGDVIFALAQKNAHVPYRNSKLTQVLQSSLGGQAKTLMFVQINPDVESYSETISTLKFAERVSGVELGAARSNKEGKDIKELLEQVASLKDTIVRKDTEIEQLQLMKDKVKSPSFAVDINGASMPKNSNSDLRSVLSITTNQQSQLSDPQSYAEVNRDGGPTSYTDITPTCLDEADFEDNASEDGFSGGTDYSVGCAAGASVFPNSCSDRTADTSIRRISSRIARFSLTKNGQPATSRPKPKDTAPKTPNQTRVQSSQLIGGSSLRASKRWQK", "text": "SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-14 subfamily."}
+{"protein": "MASSSCLWLLALAFLLGSCASLALGHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEKKIPGIHVLSLEIGKTLREDVENSFFLNVNSQVTTVCQILAKDPKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMVNLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYNKAIQERLVQAEYWHDPIREDIYRNHSIFLADINQERGVNESYKKNLMALKKFVMVKFLNDTIVDPVDSEWFGFYRSGQAKETIPLQESTLYTQDRLGLKAMDKAGQLVFLALEGDHLQLSEEWFYAHIIPFLE", "text": "FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons. SUBCELLULAR LOCATION: Lysosome Secreted. SIMILARITY: Belongs to the palmitoyl-protein thioesterase family."}
+{"protein": "MVLGGYPVSYLLLCGQAALLLGNLLLLHCVSRSHSHNATAEPELTSAGAAHPEGSPGAASWEYGDPHSPVILCSYLPDEFIECEDPVDHVGNTTAFQELGYGCLKFGGQAYRDVEHTRVQCRALDGIECASPRTFLRENKPCIKYTGHYFITTLLYSFFLGCFGVDRFCLGHTGTAVGKLLTLGGLGIWWFVDLILLITGGLMPSDGSNWCTIY", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TM2 family."}
+{"protein": "MDYPTLLLALLHVYRALCEEVLWHTSVPFAENMSLECVYPSVGILTQVEWFKIGTEKDSIAIFSPTHGMVIRKPYAERVYFLNSTMASNNMTLFFRNASEDDVGYYSCSLYTYPQGTWQKVIQVVQSDGFEAAVPPNSHIVSEPGKNITLTCQPQMTWPVQEVRWEKIQPHQIDLLTYCDLVHGRNFTSKFPRQIVSNCSHGSWSFIVVPDVTASDSGLYRCHLQASAGENETFVMRLTVAEGQTDNQYTRFVTGGTVLLLLFVISITTIIVIFLNRRRRRERSDLYTESWDTQKAPKNYRSPISASQPTNQSMDDTREDIYVNYPTFSRRPKTRV", "text": "FUNCTION: Involved in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T- lymphocyte (CTL) and NK cell. Cell surface receptor for NECTIN2. Upon ligand binding, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Competes with PVRIG for NECTIN2-binding. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MSKLFYAFAVLAVHVLTSSPTTAASNLPVNLVTGPAFTTPAGAAHRRFLRSIHEGEDSLKPSAFSEERTALRAMAYLLKPKQKKLAAALKKSTSKHKLSVAPEKMKSIQVLGDPKNPEREWFKRLYNSKRGDPQTLRKLGQFKTEAQLSRYIKFYDDMLAKAKNVRVQTK", "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 cytoplasm Host nucleus. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MSDIVYANVSHYNKIEASKYDNPSTLAISKVISSKILQFEDNSETSLRHDLPKYDQDRLLLTSDDDLTNVNNFWKKSGMSILDFACGTGLISQHLFPYCKQIVGIDVSQDMVDVYNEKFRKMNIPKERACAYVLSLDDLDGNGDEPFSTEFDAVVCSMAYHHIKDLQEVTNKLSKLLKPNGRLFVADLIKGGDTFHGNLHPDEIAKLGVAHHGGFTPQSILNLFKNASLSNAEVIGKAQANVWVDEAKYQRSTQSKDAKTLDLANGEKLYEVKLQLMVISGIKT", "text": "FUNCTION: Probable methyltransferase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the methyltransferase superfamily."}
+{"protein": "MRVSVSLVLGVGLGCSSPALWAETESPAELEVLTVTAEAERAEGPVQGYRANRTASATRTDTRIEDIPQAISVVPRQVLDDLDSARIERALDFAGGVSRQNNFGGLTMFEYNVRGFTTSEFYRDGFSANRGYMNAPDSATIERVEILKGPASSLYGRGDPGGTVNLVTKKPQAERFARLHASAGSWDRYRSTLDLNTPLDEEGDLLYRMNLAVEDSKGFRDYADGQRLLVAPSISWQLDPDTSLLVEAEVVRNRQVFDRGTVAPHNHLGSLPRSRFFGEPDDGKIDNNNETLQATLRHHFNEQWSLRLASHYKHGHLDGYASENSSLAADGYSLRREYRYRDFEWHDSITQLDLLGDLHTGSIRHQLLMGLEYERYHNDELILRSIPSRNPYAIDIRRPVYGQPKPPFGRDDRNHEEVDAMALNLQDQIEFSEKWRGLLGVRFDRYRQDMNATRLNNGRFRETSSQQTQRAATPRIGVLYQATPEVGLFANASKSFKPNGGTDMAGKAFDPEEGRGYEAGVKLDLLDGRLGMTLAAFHLKKKNVLTADPSNPGYQQTAGEARSQGFDLQFSGQLTEQLRLIGAYAYIDAEVTKDENIARGSRLLNVPKHSGSLMGVYEFREGWLHGADAGAAVNYVGERAGDSSDSGFELPAYTTVDLLARYPLASNATLGVNVNNLFDRRYYERSYNNVWVAPGEPRNLTMSLTLNY", "text": "FUNCTION: Transports the metallophore pseudopaline, which is involved in the acquisition of nickel and zinc, and thus enables bacterial growth inside the host, where metal access is limited. Is probably involved in the import of pseudopaline-metal complexes. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family."}
+{"protein": "MIVLRDSSDYSDSEVDLPSIEVNGERGNVPTSVLCNVEGSLLNSNPALRQPNLKCIKHNQDVENTTFQLDLRGCRVPSSQPQVITELENNIDIPKNIDAMQNWIFPQTQQYRNYQKEFCEQALFHNLLLALPTGLGKTFIAAVVMLNYFRWFPESKIIFLAPTKPLLLQQRVACSNVAGMSPGATAELNGEVSPDRRLFEYNTKRVFFMTPQTLQNDLKEHLLDAKSIICLIFDEAHRATGNHSYAQVMRAVLRSNSHFRVLGLTATPGSSTASVQKVVDCLHISKLIVRNEESIDIRSYVFHKKIQLIKVTISSEMNILKSDFANLYRPYFNFLRQKKLIPINCECLNIKAYTLFVSLRKYSFSSKNVQSKEKSKIMSCFTLLISCAHITYLLDCHGIIQFYQKLVETKNKAEGKGSGQSFWLFTSKPFAFYLEHLHNKIQGLSLNHPKMNHLLELLKEHFKDTSEGYQNQRVMIFTEFRNTAEYITTTLLAIRPMVRASLFIGQANSAYSTGMNQMQQKETIDQFRAGVINTLVATSIGEEGLDIGDTDMIICYDASSSPIRTIQRMGRTGRKKSGKVFVLLTEDCEDSKWERSQVSYRRVQKVIESGKKIALKKDVPRLIPSNIQPIFKFQALQNNADATLILNSYNNNSSSLSPVNTLANQAHSRSKRYLPFIVDDVFEDMESNLRVPTEDAKIKRFKSDYRSCIYNARRNVFSKPTYMGDKLTKFAKVPHSLLTLSIYRRGRLLQQCSPSSVTKYLKYEEKFKRKRMKKTSNALFQST", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily."}
+{"protein": "MAQVAPTGAPTDAPPAYPPPPQQAPPPQQPGYGQPQLGYGQPPPQLGYGQPPPQLGYGYPPPPQNNNMMMNNTVVVTAPAPAPANNVVIINQKKDNCCRQAIPAHHIAAAILCLIFNIFFPGIGTIIAGFAVFCCGNPGADGGSKVGTMCINFWIGLLQIGTVWFFFLGWIWSIMWGAAFIGMSADYHSGGDTTIVATGGGGTTVINN", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Cell projection, cilium Note=In cilia and Golgi complexes. SIMILARITY: Belongs to the SPEC3 family."}
+{"protein": "MTRDTNSNVGRRSVLKAASALGAFLGLGGVASATPGREPGPKKDEIIVGVSERVSSTEATVESKIPTNAEIVHTNETLGYVAVKFPSNAAEQARENFKRNVLQEDDIEYAEDNATYETLEVPNDPMYGQQYAPQQVNCEGAWAETYGDDDVVISVVDQGIQYDHENLAENMDGSVSDYGYDFVDDDGDPYPVSAGENHGTHVGGIAAGGTNNDTGHAGISNCSMLSARALGDGGGGSLSDIADAIQWSADQGADIINMSLGGGGFSETLDNACQYAYDEGTLLVAAAGNDHGGSVSYPAAYDSVMAVSSLDEGETLSSFSNVGPEIELAAPGGNVLSAVNWDDYDSLSGTSMASPVAAGVAGLALSAHPGLSNDELRDHLHDTAVDIGLSDDEQGYGRVDAELAVTTDPDNGDDDDDDDDDEDDPGDGECGDETNTATADGELSGGWGGNPSDTYSYELSTDNPCHATVTLDGPSSGATFDLFLTLDGRTPTTSDYDRRSYNWGADEEIEVDLDGDEELGILVDRYDGSGSYTLTIEELGS", "text": "FUNCTION: Serine protease that hydrolyzes large proteins such as casein and gelatin. Cleaves preferentially at the carboxyl terminus of Phe, Tyr or Leu (PubMed:10879563). Is also able to catalyze peptide synthesis under different salt concentrations in the presence of dimethyl sulfoxide (DMSO) (PubMed:21039670). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
+{"protein": "MMVTARTPWGWFLGCLILEVTGASASSVSSRIIQGQDCSPHSQPWQAALFSEDGFFCSGVLVHPQWVLSAAHCLQESYIVGLGLHNLKGSQEPGSRMLEAHLSIQHPNFNDPSFANDLMLIKLNESVIESNTIRSIPVATQCPTPGDTCLVSGWGQLKNGKLPSLLQCVNLSVASEETCRLLYDPVYHLSMFCAGGGQDQKDSCNGDSGGPIVCNRSLQGLVSMGQGKCGQPGIPSVYTNLCKFTNWIQTIIQTN", "text": "FUNCTION: Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily."}
+{"protein": "MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQDKFEVLNYTSIPIFLPEVTIGAHQTDRVLHQFRELPGRKYSPGYNTEVGDKWIWLK", "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 matrix. SIMILARITY: Belongs to the complex I NDUFA10 subunit family."}
+{"protein": "GFLSGSTGIEXIPGPQL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen."}
+{"protein": "MDPTISSHDTESTPLNETGHPNCTPILTLSFLVLITTLVGLAGNTIVLWLLGFRMRRKAISVYILNLALADSFFLCCHFIDSLLRIIDFYGLYAHKLSKDILGNAAIIPYISGLSILSAISTERCLCVLWPIWYHCHRPRNMSAIICALIWVLSFLMGILDWFSGFLGETHHHLWKNVDFIITAFLIFLFMLLSGSSLALLLRILCGPRRKPLSRLYVTIALTVMVYLICGLPLGLYLFLLYWFGVHLHYPFCHIYQVTAVLSCVNSSANPIIYFLVGSFRQHRKHRSLKRVLKRALEDTPEEDEYTDSHLHKTTEISESRY", "text": "FUNCTION: Orphan receptor activated by neuropeptides terminating in Arg-Phe or Arg-Phe-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": "MATKSVSTFAIFFILVLAIFETPEIEAYDRKCLKEYGGDVGFSYCAPRIFPTFCDQNCRKNKGAKGGVCRWEENNAIGVKCLCNFCSEEPSDQTLSRI", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family. Protease inhibitor I18 (RTI/MTI-2) subfamily."}
+{"protein": "MRLNGEISSGEEEEEEKQTGTTTFSSQKVVVGYALTSKKKKSFLQPSFTGLARNRGINFVAIDLNKPLPEQGPFDIILHKLSGEVWREIIEDYREKHPEVTVLDPPDAIQHLHNRQSMLQDVLDLNLSDCHGKVGVPRQLVITKEKDPSSIPYEVTKAGMKLPLVAKPLVVDGTAKSHELFLAYDEFSLSAVEPPLVLQEFVNHGGLLFKIYIVGETIKVVRRFSLPNISKRELSKVAGVFRFPRVSCAAASADDADLDPNIAEHPPRPLLERLARELRHRLGLHLFNIDMIREYGTKDVFYVIDINYFPGYGKMPGYEHVFTDFLLSLVESKCSNKKLAA", "text": "FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). SIMILARITY: Belongs to the ITPK1 family."}
+{"protein": "MGSLSSEEDDEVSSERCGSYSPSADISESESSSSFSCHRFDGEGASSSIPSSPRVVAGRGFYFPAPVMLPVIGGKDVVWDDKQPDNDLSEIEMMKERFAKLLLGEDMSGGGKGVCTALAISNAITNLSATVFGELWRLEPLAPQKKAMWRRELEWLLCVSDSIVELIPSIQQFPGGGTYEIMETRPRSDLYANLPALKKLDAMLIDMLDAFSDTEFWYTDRGIVLGDCDKDSYNSPASVRQEDKWWLPCPKVPPNGLSEEARKKLQQCRDFANQILKAALAINSGVLAEMEIPDPYLETLPKSGKECLGEIIYQYLTANKFSPECLLDCLDLSSEHQTLEIANRIEAAVHVWRQKNGRRHKKQAKLKLSSWGGKVKGLVNDNERNDFLVQRAETLLQSLRIRFPGLPQTTLDMNKIQYNKDVGQSILESYSRVMESMAFNITARIDDVLYVDDAMRRSISVTESLSLFSINGLNPQKAFSVQSSPHGSPFATPALSVASRSPRRAPPLYSVKRNGTREKGIVGETEKAWSYAGNLSSRRVTGVTPERD", "text": "FUNCTION: Guanine-nucleotide exchange factor (GEF) that acts as an activator of Rop (Rho of plants) GTPases by promoting the exchange of GDP for GTP. Acts downstream of PRK2 in the control of polarized pollen tube growth by activating ARAC11/ROP1. In association with ROPGEF4, acts as specific regulator of ARAC10/ROP11 function in ABA-mediated stomatal closure. May play a role in the Rac/Rop-signaling pathway that controls ROS-mediated root hair development. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane Note=Localizes to the apical region of the pollen tube plasma membrane to activate ARAC11/ROP1 and interacts with ARAC10/ROP11 on plasma membrane in guard cells."}
+{"protein": "MKIILTGATGFVGCSLVPLLHQQGHELTLLVRSVSKAQRLFAPGSFPQLKAIAYEATKSGDWQKVVDGQDAVINLAGEPISERWTEAYKAEIFDSRKLGTEKLVEAIAKADRKPQVMISGSAIGYYGTSETATFTESSKPGDDFLAEVCQAWENAAHQVEQLGVRLVVFRIGIVLGADGGALAKMLPPFKLFAGGPLGSGEQWFSWIDRRDLIALIDKALTDSTLRGTYNATAPNPVKMKEFCHTLGKVLARPSWLPVPDIALELLLGEGAKLVLEGQEVLPGAISKTDFQFQAPDLETSLRQILGS", "text": "SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. SDR39U1 subfamily."}
+{"protein": "MSHYKSNVRDQVFNLFEVFGVDKVLGADKFSDLDADTAREMLTEIARLAEGPIAESFVEGDRNPPVFDPETHTVTLPEGFKKSMRALFDGGWDKVGLAEHLGGIPMPRALQWALIEHILGANPAAYMYAMGPGMSEIFYNNGTDEQKKWATIAAERGWGATMVLTEPDAGSDVGAGRTKAVQQPDGTWHIEGVKRFITSADSDDLFENIMHLVLARPEGAGPGTKGLSLFFVPKFHFDHETGEIGERNGVFVTNVEHKMGLKVSATCELSLGQHGIPAVGWLVGEVHNGIAQMFDVIEQARMMVGTKAIATLSTGYLNALEYAKERVQGADMTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRAIYLYTATFQDAEVAQAVHGVDGDLAARVNDLLLPIVKGFGSETAYAKLTESLQTLGGSGFLQDYPIEQYIRDSKIDSLYEGTTAIQAQDFFFRKIIRDKGQALAYVAGEIEQFIKNENGNGRLKTERELLATALADVQGMAASLTGYLMAAQEDAASIYKVGLGSVRFLMAVGDLLSGWLLARQAAVAIEKLDAGATGADKSFYEGKIAAASFFAKNMLPLLTSTRQIIENLDNDVMELDEAAF", "text": "FUNCTION: Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
+{"protein": "MSGFTNKDGRQNLAPCFNFRSSPFRLTVGERELKLEEDKNQLSKGLDPWTSNPTASASTLHYLLQEKERAQQAHEQLQIYQQQQGFGSFLQHRIRQPASRGPGGGGGGGDGGGSSGESTPVDALATAFGAGRIVRSAAGRKDRHSKVCTARGLRDRRVRLAAHTAIRFYDVQDRLGYDRPSKAVDWLMRNAKAAIDELPDRAEAPPPPAAASTEQPEGTEQANSTSYGFGNTTGGTMTSAASAAAGSFLPHSLGADRVSDSVKSLFPSSSTASGAASAGHDEYRGSPPDLLSRTTSNQQPQELCLTLQSNQHQIFSHVSSNHHGMISSAGVPGWPDHSQRMQAWHAPENSTGDGRGGGNGDGYMFAMPSRQGLDQSQLFSHGEPLQSSGRGWASARAWLDPLAVAAIHHQPSTMAAGQVGFGHLVGGAGGGGGFMGFLAPAAQRLEGEEEHGSEVIR", "text": "FUNCTION: Transcription activator. Binds the promoter core sequence 5'- GGNCC-3'. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLFHGITGGHIQGIMEEMERRSKSADNRLAKTIQVNGRETRMPPLSPEKPTLCAGCGGKISDRYYLLAVDKQWHLRCLKCCECKLALESELTCFAKDGSIYCKEDYYRRFSVQRCARCHLGISASEIVMRARESVYHLSCFTCTTCNKTLSTGDHFGMKENLVYRRAHFELLVQGDFHSQLNYTELSAKGGGLSALPYFTNGTGAVQKGRPRKRKSPALGVDIINYTSGCNENDTDLDRDQSYPPSQKTKRMRTSFKHHQLRTTKSYFAINHNPDAKDLKQLAQKTGLTKRVLQVWFQNARAKFRRNLLRQENGGGDKVEGPSLSAPASTDSAALTPTGAASTLSDLTSPSLNVGASVTPNMDSHESGSPSQTTLTNLF", "text": "FUNCTION: May be involved in gonadal development. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MGDFQSRYEILAAIMGPPNTASFKEEEHSGSQTKNYPVVVKCIQEHDPVDTTNVLVADDLDSNFEPFSITDDYGKYENTLVSHSSTILNEPYNESPSSSSSDSSSRSTSPFSQLSSQSLRLNAEEIAPSSLINKAVQSTLRLSEPLVSPIKCPLSEQFINFINQQDSDKVVLIRGFLLPHLASLTTKNVSEPELDKLRHSLYNWWVSILRRLQSNISTSERITYTKAILAIAKHHCWNKVEHSALLYLEHQLILYDTLTFVVHLLSQKSLPYSLTTFCASILVLSFFQLPLFADHFLSALDVKKKYIDALGSSFDEKIMIISHKYLAPFFTDQFSSTMHPYYPKRTSTPFTIGYNRQPIEFTRAWMRRFKSSTGGFFFEFLSCYHSFLALQFSFELPDNVIYFAPGYICLHAYLLELTISVIHISDKKPLMLPTGHEQFPCKTLPEVNPSMEEYNPKMPVTATTLSTLQQFVGHIKDAFKKIGDCRQEQMRLLAVLEQVLINVAKNTPAFNLQSCFLLCSLVEQCFGVFNDFSHRFDFSFWISVAKRLISTSHNMSIVRSITFIYAVWPYLDIKSKELVTLQWLLEENTFQELFLHWSPLVRAYFQRLVCWRFLKLDDMEEFQFKGTVTLRVKNLLKHYFTAQALYHEECLVNGRASPITKPSEPVPMRRLTIVCNHYQNYGNSESTEFELSNYKQDDGTIQALVTDVVSISNSFSSGLKKAFGSLFKNVSGLPAETEIAYHHTLSASNSYVFTDLVDNPDSMLKSTLKYRFVFKFSPSQPLSSLGKNKEKYDALLERSSHGVLPVQSKMLLYNSNHISCPLSSIKGVSVNGKRLVYTSRALVEWALVVNEFDHALSLRKGNETEDMEAPTLTVRIPKSYASNIYN", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0592 family."}
+{"protein": "MSAIENFDAHTPMMQQYLRLKAQHPEILLFYRMGDFYELFYDDAKRASQLLDISLTKRGASAGEPIPMAGIPYHAVENYLAKLVNQGESVAICEQIGDPATSKGPVERKVVRIVTPGTISDEALLQERQDNLLAAIWQDSKGFGYATLDISSGRFRLSEPADRETMAAELQRTNPAELLYAEDFAEMSLIEGRRGLRRRPLWEFEIDTARQQLNLQFGTRDLVGFGVENAPRGLCAAGCLLQYAKDTQRTTLPHIRSITMEREQDSIIMDAATRRNLEITQNLAGGAENTLASVLDCTVTPMGSRMLKRWLHMPVRDTRVLLERQQTIGALQDFTAGLQPVLRQVGDLERILARLALRTARPRDLARMRHAFQQLPELRAQLETVDSAPVQALREKMGEFAELRDLLERAIIDTPPVLVRDGGVIASGYNEELDEWRALADGATDYLERLEVRERERTGLDTLKVGFNAVHGYYIQISRGQSHLAPINYMRRQTLKNAERYIIPELKEYEDKVLTSKGKALALEKQLYEELFDLLLPHLEALQQSASALAELDVLVNLAERAYTLNYTCPTFIDKPGIRITEGRHPVVEQVLNEPFIANPLNLSPQRRMLIITGPNMGGKSTYMRQTALIALMAYIGSYVPAQKVEIGPIDRIFTRVGAADDLASGRSTFMVEMTETANILHNATEYSLVLMDEIGRGTSTYDGLSLAWACAENLANKIKALTLFATHYFELTQLPEKMEGVANVHLDALEHGDTIAFMHSVQDGAASKSYGLAVAALAGVPKEVIKRARQKLRELESISPNAAATQVDGTQMSLLSVPEETSPAVEALENLDPDSLTPRQALEWIYRLKSLV", "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. 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. SIMILARITY: Belongs to the DNA mismatch repair MutS family."}
+{"protein": "MSVLEECCYLPVVSAQQLPEPSDEGYLEDQLEIFGILALNKKLTRAECCLTQLDTLMAPELTFYTCRAARRLLLGLVHVPCVSVGYMPPGMCLHKGSSFSGAGLVFNGYQYYTTNQLTTDTFIPGIRSMEETDPVLDKNFTWRIIYFPKLLTTRVSWTLMFQIISRYVNMYELDECVSLFCNSLNPHLKQVCTYNYSLLTYHLKNPSLQRWPHSSKTVGKTSEEFLLINFLLHWPSSTCLAQLRAKVLKGVKQFPGILQYLSALPVSKAVTVQGLEILKYIECIGLLFPQWAPVLLKRTPKKFTCVITVVNNHTNSSIWLQFPESGAMLRTALCMAVAKHICREKELISPGKQQLSLARALVANFEKMQYAPKDFPIILYPTEIYRPMPVDDQPASDIKNSFNALTHISINSFKVNVFNTNMVINTNITCLQAPCCYSQIVNVPKLVNNFVIKKYSVKEPAFTVSIFYSEDFNLKAAINVNISGDIINFLLAMNTLKCFLPVTDIFPASMANWNSTFDLHGLENQHLVRSGRRDVFWTTNFPSVVSSNEGYNVSWFKAATATVSKIHGSDLTKQVQGEIRRLIGHRHARISFCKNKLFATLESRNCAQIQAAHKRFLECLYECCSWFRANTNALTQLVQCGAFDFSKRIIAHSKSRHECALCGYKVCNSIPKVIINHKKTRLDDCGRNANFLSYLHRGAPHMINTKAKLFKHICRRASLRSYHFAGCAKAKEWSKALRLAHQMPS", "text": "SIMILARITY: Belongs to the herpesviridae UL87 family."}
+{"protein": "MKEANQWSSKLGFILAAAGSAIGLGAIWKFPYVAGTSGGGAFLLIFILFTVLIGLPLLLGEFIIGRRTQKDAVQSYKTLAPGTKWHWIGYLGMVTCFILLSFYSVVGGWILIYIIKGFTGGLSQTSGFDTIFASTISNPYLAVGGQLLFMVVTILVVAKGVSSGIEKASQVLMPALFLLFIILMVRSVTLDGAMEGIKFFLMPDLTAIDANTILYAMGQSFFLLSVGVSVMVTYSAYLEKQENLVQSAVSVTVMNMLVAVMAGIAIFPAVFSFGLKPDQGPVLLFNVLPTVFNQMPFGIIFLLAFLLLFLFAALTSAFSMLEILVAVLSKGDINKRKRFAWLGGIAIFIVGVPSALSYGVLSDVTIFHLSIFDAADYLVSNILMPLGALLISIFVPLKIPKQDLFDELKSGSNLKRKWFAVWLLLIRYLSPVAIIIVFLHVIGIF", "text": "FUNCTION: Putative sodium-dependent transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family."}
+{"protein": "MSIPLLEYAPSSQNQRVEGYEVPNEDTPTIYRLAAAIDDADVDAIIWAGYRQIFSEHLIIKSNRQSFLESQLRNRAINVRDFIRGLGKSEVYRTQVADLNSNYRLVDITLKRFLGRAAYNQDEEIAWSIVIGSQGLHGFIDALLDSDEYRENFGDDIVPYQRRRYKDRPFNLVNPRYNAYWRDRQTLNALGGRSFYSARTSGTLTKDDIRRAIPANFMALAGKILTPERNYQRTIASVTSQIKDIKIPDTSREVTTPEVTVKPVAVALPYRYIPGNKTT", "text": "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. FUNCTION: Rod-core linker protein required for attachment of phycocyanin to allophycocyanin in cores of phycobilisomes. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=Part of a phycobilisome rod. SIMILARITY: Belongs to the phycobilisome linker protein family."}
+{"protein": "MSSSSYNTSVIPSSSSSAQPFFITSSGTGDNDFNRKDTFMSMIQQPNSSAPPPKKRRNQPGNPNPDAEVVALSPKTLMATNRFICDVCNKGFQREQNLQLHRRGHNLPWKLKQKSTKEVKRKVYLCPEPTCVHHDPSRALGDLTGIKKHYYRKHGEKKWKCEKCSKRYAVQSDWKAHSKTCGTKEYRCDCGTIFSRRDSYITHRAFCDALIQETARNPTVSFTSMTAASSGVGSGGIYGRLGGGSALSHHHLSDHPNFGFNPLVGYNLNIASSDNRRDFIPQSSNPNFLIQSASSQGMLNTTPNNNNQSFMNQHGLIQFDPVDNINLKSSGTNNSFFNLGFFQENTKNSETSLPSLYSTDVLVHHREENLNAGSNVSATALLQKATQMGSVTSNDPSALFRGLASSSNSSSVIANHFGGGRIMENDNNGNLQGLMNSLAAVNGGGGSGGSIFDVQFGDNGNMSGSDKLTLDFLGVGGMVRNVNRGGGGGGRGSARGGVSLDGEAKFPEQNYPFGRG", "text": "FUNCTION: Transcription factor that may act a transcriptional activator of nuclear-encoded photosynthetic gene expression (Probable). Binds DNA via its zinc fingers (PubMed:24821766). Recognizes and binds to SCL3 promoter sequence 5'-AGACAA-3' to promotes its expression when in complex with RGA (PubMed:24821766). SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus."}
+{"protein": "MIESKRLRIAMQKSGRLSQESQALLKQCGVKINLQEQRLIAYAENMPIDILRVRDDDIPGLVFDGVVDLGIIGENVLEEEELTRQAAGETVNYKKLRRLDFGGCRLSIAIPQDEAYNGISDLKNARIATSYPNLLKRYMQQQGVDFKTCSLTGSVEVAPRAGLADAICDLVSSGATLEANGLKEVEIIYRSKSCLIQRAAELSPEKQALVDKLLTRIQGVQQAAESKYIMLHAPKEKLEEITALLPGVENPTILPLAHDNSKVAMHVVSQENLFWETMEQLKDAGASSILVLPIEKMMG", "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. Long subfamily."}
+{"protein": "MSEQQTMSELKQQALVDINEANDERALQEVKVKYLGKKGSVSGLMKLMKDLPNEEKPAFGQKVNELRQTIQNELDERQQMLVKEKLNKQLAEETIDVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYITDEILLRTHTSPVQARTMESRHGQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGADREIRLRPSYFPFTEPSVEVDVSCFKCKGKGCNVCKHTGWIEILGAGMVHPNVLEMAGFDSSEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFLDQFKAVEDRGDM", "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."}
+{"protein": "MDANMNKILKWSIQNSTNASSDQNAAADATSRGLTPEMMATLFGGPSDADLMKASMEALRSDEVDLENKLVAFDNFEQLIESIDNANNLEPLGLWTPLVELLRHEEADMRRMAAWCVGTAVQNNEKAQDKLVVLNALPTLVAMSTSDPNPAARKKAVYALSSAVRNYQPAMDEVAKHLPEGYPRGEKIDAADMDAVDGIMDKLRAHPVESSA", "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": "MVLSLQTLAKKVLAGQRPTKCHPHFLKCYGLWWHNGPMIFDQNQKKIWSPIFTDGVHINAALVKAAAENNYDLIKLFTEWGANIDYSLLSVNTERTRDLCRELGAKEQLKQEEVLYYFNTIKRNLTSSNIILCHEVFSHNPILETINRTKLRGIIYEQLEALMENTDILSELLTKYWYGIAIEFNLTKAIHYFYQRYVHLHQWRLMYALFYNNVCDLHELYAKEKIRMDMDEMLKWACRKNYNYLTIYYCCIVLGADINQAMFHSIQFYNIGNMFFCIDLGANAIEEGKTLALQKDKSFIASLLSINCYSMNDSLSLKETDPEVIKRMLKDYHSKNMSIAHKYYIKHGFNDI", "text": "FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. In addition, inhibits IFN- beta-induced IFN-stimulated genes (ISGs) transcription. Mechanistically, degrades host STAT1 and STAT2 through apoptosis and ubiquitin-proteasome pathways respectively. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the asfivirus MGF 360 family."}
+{"protein": "MNCEVKHALHCAVLVAWIVCFAYFCGVFTEPVEGSVPESPVASYGLIWTVCLYLLRFTALLVLPQCLCNLGGLMMFNAFREKVQLKAAPLLSPFVCFRVVTKGNFPLLVKENIDTNMKTCFEAGMENFIFEVVTDKAINLPPNPRVREVVVPTVYKTKSGAKFKARALQYCLEDDVNILQPTDWIVHLDEETLLTTNAICGILNFCEDGKHQFGQGVITYANGDIVNWLTTLSDSFRVADDMGKLRFQFKLFHKPLFGWKGSYVVTQVEAERDVSYDHGMEGSIAEDCFFSMVAMKHGYSFDFIEGEMHEKSPFTMWDFLQQRKRWLQGILLTVHSSKIAVVHKALLALSLYAWATMPLTSLQVFLCPLFPLPRCLPFDFLLSFVGALNLYMYIFGVVKSFSHKYRNSLLRLAMYLAGALMTIPFNILIENAAVLVGMFGRKDQFYIVNKDIQTV", "text": "FUNCTION: Glycosyltransferase with a proposed role in glycosphingolipid biosynthesis (PubMed:12944392, PubMed:10924467). Involved in susceptibility to pore-forming crystal toxins in conjunction with bre- 1, bre-2, bre-4 and bre-5 (PubMed:12944392, PubMed:10924467). Involved in resistance to the nematotoxic C.cinerea galectin Cgl2 (PubMed:20062796). Has a role in determining brood size (PubMed:12944392, PubMed:10924467). SUBCELLULAR LOCATION: Cytoplasm Note=In punctate structures throughout the cell. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
+{"protein": "MISGSATASHGRVLLPSQRERRPVSTGSNILRFRETVPRQFSLMMVTKATAKYMGTKMREEKLSEMIEEKVKEATEVCEAEEMSEECRVAWDEVEEVSQARADLRIKLKLLNQDPLESFCQENPETDECRIYED", "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": "MHSAILATFFLLSWTPCWSLPLPYGDDDDDDLSEEDLVFAEHYLKSYYHPATLAGILKKSTVTSTVDRLREMQSFFGLEVTGKLDDPTLDIMRKPRCGVPDVGEYNVFPRTLKWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQFLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEAELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDILEGYPRKISDLGFPKEVKRLSAAVHFENTGKTLFFSENHVWSYDDVNQTMDKDYPRLIEEEFPGIGNKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSILWC", "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. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the peptidase M10A family."}
+{"protein": "MGRRVPALRQLLVLAVLLLKPSQLQSRELSGSRCPEPCDCAPDGALRCPGPRAGLARLSLTYLPVKVIPSQAFRGLNEVVKIEISQSDSLERIEANAFDNLLNLSELLIQNTKNLLYIEPGAFTNLPRLKYLSICNTGIRTLPDVTKISSSEFNFILEICDNLHITTIPGNAFQGMNNESVTLKLYGNGFEEVQSHAFNGTTLISLELKENIYLEKMHSGAFQGATGPSILDISSTKLQALPSHGLESIQTLIALSSYSLKTLPSKEKFTSLLVATLTYPSHCCAFRNLPKKEQNFSFSIFENFSKQCESTVRKADNETLYSAIFEENELSGWDYDYGFCSPKTLQCAPEPDAFNPCEDIMGYAFLRVLIWLINILAIFGNLTVLFVLLTSRYKLTVPRFLMCNLSFADFCMGLYLLLIASVDSQTKGQYYNHAIDWQTGSGCGAAGFFTVFASELSVYTLTVITLERWHTITYAVQLDQKLRLRHAIPIMLGGWLFSTLIATMPLVGISNYMKVSICLPMDVESTLSQVYILSILILNVVAFVVICACYIRIYFAVQNPELTAPNKDTKIAKKMAILIFTDFTCMAPISFFAISAAFKVPLITVTNSKILLVLFYPVNSCANPFLYAIFTKAFQRDFLLLLSRFGCCKRRAELYRRKEFSAYTSNCKNGFPGASKPSQATLKLSTVHCQQPIPPRALTH", "text": "FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Secreted. Note=Some isoforms may be secreted. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily."}
+{"protein": "MGFHSKNNSEYNGDFIILSSIYYWMILLYCIKFFLSKYLIYCMSLTYIDLFSGAGGFSLGFDRAGFHQLLSVEIEPHYCDTYRANFPDHQVLQQDLTTLSDDNLLRHINHRKVDVVIGGPPCQGFSMAGKIGRTFADDPRNHLFKEFVRVVKLTQPKFFVMENVARLFTHNSGKTRAEITEQFERLGYKVKCKVLNAADFGVPQLRSRIVFIGRKDGGEITFPEPSHTEYNTVGDAIGHFPKLNAGENSLILNHEAMNHSTQMLEKMSFVKNGGDRNDIPESLRPISGDVRKYIRYHSDKPSVCVTGDMRKVFHYEQNRALTVRELAALQSFPDDFVFLGKKIAQQQQVGNAVPPLLAQAIAEAVLKMNTNE", "text": "FUNCTION: A methylase that recognizes the double-stranded sequence 5'- GGTGA-3' and protects the DNA from cleavage by the HphI endonuclease (PubMed:8759008). Probably methylates C-2 on the bottom strand (Probable) (PubMed:12654995). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family."}
+{"protein": "MLSPTFILWDVGYPFYTYGSIIIIALIIWQVKKNHRGLKLGPNRNCCRRHQKVKQRAKEKTPRARRHSRKEADKPLELLSIMRSQGWLPQEGSVRRLLCADPCCQICNSVALEIQQLISGETTLTTPTSSGPSQGSSCLEVLSMSSLSFDQSQESLPFKQLSLPSATRTVSQLTNQKSVTQSAAKSATKPATKSVSAISIRQYWAGHQQLRQECRGPELPLDAGALSSSSVEEPRIPVNQHVKKKSNSEGILKKQEAVEADLGNKLKHFTQWINPDMKGQGRKECILRCKDEKVAKTKTKKAEKSPPSTKRPMKGAKLEKEEGFFDALQCLDSEFQRQSMESVRSSQSCFLPLSSGSSKRSPLLTCATQPENPSHVSVSTSAEGTCLPQESTQSRKKELRGSQTSASS", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SPATA31 family."}
+{"protein": "MKTLLLLLLVLLELGEAQGSLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAPAVP", "text": "FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain. SUBCELLULAR LOCATION: Endosome Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MRQRTIVCPLIQNDGCYLLCKMVDNRGVFPGQWALSGGGVEPGERIEEALRREIREELGEQLILSDITPWTFRDDIRVKTYADGRQEEIYMIYLIFDCVSANRDICINDEFQDYAWVKPEELALYDLNVATRHTLALKGLL", "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": "MAAELAMGAELPSSPLAIEYVNDFDLMKFEVKKEPPEAERFCHRLPPGSLSSTPLSTPCSSVPSSPSFCAPSPGTGSSAGGGGSAAQAGGAPGPPSGGPGTVGGASGKAVLEDLYWMSGYQHHLNPEALNLTPEDAVEALIGSGHHSAHHGAHHPAAAAAYEAFRGQSFAGGGGGGADDMGAGHHHGAHHTAHHHHSAHHHHHHHHHHGGSGHHGGGAGHGGGGAGHHVRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHILESEKCQLQSQVEQLKLEVGRLAKERDLYKEKYEKLAGRGGPGGAGGAGFPREPSPAQAGPGAAKGAPDFFL", "text": "FUNCTION: Transcription factor that activates insulin gene expression (PubMed:15665000). Acts synergistically with NEUROD1/BETA2 and PDX1 (By similarity). Binds the insulin enhancer C1/RIPE3b element (PubMed:15665000). Binds to consensus TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequence (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
+{"protein": "MQKLINSVQNYAWGSKTALTELYGIANPQQQPMAELWMGAHPKSSSRITTANGETVSLRDAIEKNKTAMLGEAVANRFGELPFLFKVLCAAQPLSIQVHPNKRNSEIGFAKENAAGIPMDAAERNYKDPNHKPELVFALTPFLAMNAFREFSDIVSLLQPVAGAHSAIAHFLQVPNAERLSQLFASLLNMQGEEKSRALAVLKAALNSQQGEPWQTIRVISEYYPDDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEPKPAGELLTAPVKSGAELDFPIPVDDFAFSLHDLALQETSIGQHSAAILFCVEGEAVLRKDEQRLVLKPGESAFIGADESPVNASGTGRLARVYNKL", "text": "FUNCTION: Involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family."}
+{"protein": "MGCVTSQEDKAAVERSKQIDKSLRMDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEKGYSQEECLQYNPVVYSNAIQSMIAIIKAMGQLKIQFGHPDRAEEARQFFALAGHADEGEMSQELSGIMKRLWKDVGVQECFSRSREYQLNDSAEYYLNALDRISAPGYIPTEQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFIVAMSEYDLTLAEDQEMNRMMESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKKSPLTICFPEYTGANTYEEAAAYIQLQFENLNKKKDTKEIYSHFTCATDTNNVQFVFDAVTDVIIKNNLKDCGLF", "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. G(i/o/t/z) subfamily."}
+{"protein": "MVNEEEKDLTAEGDSNNTGVSPDSIKNKTLDFYPKEKTTERKTRSRERISRKEVNLRFKAYLKSRLFRDYAYIIFAAFLGMASYDYFIAATTSNGITPSGIGGVARGIAVGIWPNQDQLQMQTSMYWVFYFVFNIPLFIFGVIKIGIRFSFRTIVYIGLQNGFHFAFAYIPVINPQELFFIVNYNSLNIFSNYGGMYQIWLFVFAAVAGILNGIAYGLVYKGGASTAGTDFVFAYYSAKKKISIANYNRIVNYIIIVVMLAIHTTLLSRSELTSIYFGKYWAANIEQIQRLGFKIDDGGLYDSDFTSHKIKYFFGPALFASYLFVVVQAITIDIIFPKFKYRSLMVITSKADAVVSGLQYVHYPNDIIRLPARD", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.genitalium MG432 and MG443."}
+{"protein": "AEDSRGTQLHRALRKATKLSESTRCKRKGSSCRRTSYDCCTGSCRNGKCG", "text": "FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin selectively and potently inhibits depolarization-activated rat Cav2.2/CACNA1B currents (IC(50)=89 nM), when coexpressed with alpha-2/delta-1 (CACNA2D1) and beta-3 (CACNB3) subunits. In vivo, is lethal to fish and displays potent analgesic activity in mice pain models of hot plate and acetic acid writhing but has fewer side effects on mouse motor function and lower toxicity in goldfish. Shows higher or similar analgesic activity in the pain models mentioned above compared to MVIIA, and lower side effects. In addition, it blocks Cav2.2/CACNA1B more rapidly than MVIIA and also dissociates more rapidly. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
+{"protein": "MIVSTSVEQSAQFSVKSLTPFGALLEATEDHSDIQQLSIEQLCQLTWEHRLIVLRGFSLLEREELSTYCQRWGELLVWNFGTVLDLIVHQNPENYLFTNGNVPFHWDGAFAEAVPRFLFFQCLKAPEAGSGGESLFCDTVRILQNVSPQQREIWQKTEISYKTQKVAHYGGEITKSLVIKHPITGLSTLRFAEPLNDASVHLNPLYVEVCNLPAEEQNPFINELIENLYLPQNCFAHEWQEGDFLIADNHALLHGRNPFLSNSQRHLQRVHIL", "text": "FUNCTION: Involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids (PubMed:24180436). Responsible for the synthesis of Z-3-(2-isocyanoethen)-indole, a biosynthetic precursor to all ambiguines (PubMed:24180436, PubMed:28212039). SIMILARITY: Belongs to the TfdA dioxygenase family."}
+{"protein": "KIKWFKTMKSLAKFLAKEQMKKHLGE", "text": "FUNCTION: Forms pore that permeabilize the cell membrane. Promotes efflux of calcium from synaptosomes, causes hemolysis, and dissipates voltage gradients across muscle membrane. Potently inhibits the growth of bacteria and yeast. May function both in the prey capture strategy as well as protection from infectious organisms arising from prey ingestion (By similarity). SUBCELLULAR LOCATION: Secreted. Target cell membrane Note=Forms a membrane channel in the prey. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 05 subfamily."}
+{"protein": "MVFYFTSSSVNSSTYTIYMGKDKYENEDLIKYGWPEDIWFHVDKLSSAHVYLRLQKGEKIEDIPKEVLMDCAHLVKANSIQGCKMNNVNVVYTPWSNLKKTADMDVGQIGFHRQKDVKIVTVEKKVNEILNRLEKTKLEKFPDLAAEKEGRDREERNEKKAQIQEMKRKEKEEMKKKREMDELRSYSSLMKVENMSSNQDGNDSDEFM", "text": "FUNCTION: Transmembrane receptor that senses neutrophil extracellular traps (NETs) and triggers the ILK-PARVB pathway to enhance cell motility. NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Formation of NETs is also associated with cancer metastasis, NET-DNA acting as a chemotactic factor to attract cancer cells (By similarity). Specifically binds NETs on its extracellular region, in particular the 8-OHdG-enriched DNA present in NETs, and recruits ILK, initiating the ILK-PARVB cascade to induce cytoskeleton rearrangement and directional migration of cells (By similarity). In the context of cancer, promotes cancer metastasis by sensing NETs and promoting migration of tumor cells (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Endomembrane system Note=Localizes to cytoplasmic membrane in tumor cells. SIMILARITY: Belongs to the CCDC25 family."}
+{"protein": "MPGQKIETGHEDIVHDVQMDYYGKRIATASSDCTIKITGVSNNGGSQQLATLTGHRGPVWEVAWAHPKYGSILASCSYDGQVILWKEGNQNQWTQDHVFTDHKSSVNSIAWAPHDIGLSLACGSSDGNISVFTARADGGWDTSRIDQAHPVGVTSVSWAPATAPGALVSSGLLDPVYKLASGGCDNTVKVWKLANGSWKMDCFPALQKHTDWVRDVAWAPNLGLPKSTIASGSQDGKVIIWTVGKEGEQWEGKVLKDFMTPVWRVSWSLTGNLLAVSDGNNNVTVWKEAVDGEWEQVTAVEP", "text": "FUNCTION: Required for protein transport from the endoplasmic reticulum to the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus Endoplasmic reticulum Nucleus envelope Nucleus, nuclear pore complex. SIMILARITY: Belongs to the WD repeat SEC13 family."}
+{"protein": "MGNHLSDAMKILESGKLETEQGQEGRKMSWKEIPGPLQGDGQDVVSILQLVQNLMHGDDEEQGHRMQFVGEQGHMALLGHSLAAYISVLERERLRKLTTRILSDTTLWLCRLFRYENGSAYFHEDDREGLLKVCRLVMNTHYEDFTTEGFTALSSKHPVIYQSAACRPGLGQHLCSQLGLPLSCLCVVPCNTMFGSLHQMDVALLDKLVKDDRDSGKLPLLLIANAGTPGAGHTDKLSRLKELCVQYNMWLHVEGVNLATLVLGQVSSTVTAATKCDSMTLTPGPWLGLPAVPAVTLYRHEDPALSLAAGLTSSQPVEKLRALPLWLSLQYLGHDGIVERIKHASQLSQQLLEHLKTLASIKTSVEDELNSPVVVFRFSHENSAPSSGGSVEGSYAGERDILDAFNRWLGDQLAEQVPLSGVDVVELEDEGTCVRFSPLMTAAALGTQENDVAALVEKLAEMIPLLCCTLRLRQDFRDEVLQQASLSYIEDLNWPGLGVVRFEPRTTDLDEDKRQDRVEKINSDLLKKLMELDTDLNFSGGPEFSEEKNCIFIGIATEDLDVAELVETIMSLGRDIEESGKLFENMTEVVRKGIQEAELQLQKANEEKLMEEGVLRQIPLVSSVLNWFSPVQASVKGRTFNLAEGCLDSTEPVYSIKAQMRKEDSPDSPKANTRRFPGQKLFRRPGAGSDSISETSSVSQLEESFRETLHSQAADEAEVPQERPAHILEETAIADQRVPEGQEAESVETIR", "text": "SIMILARITY: Belongs to the group II decarboxylase family."}
+{"protein": "MQKLLIILILFCILKFNVDVEGRTAFPCNQSKCQERCKKEIKKGKCILQFISVSASQSCRCY", "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": "MMPASNPKKNSSERRIVFHVDMDSFFASVEVRERPELKNLPVIVGSDPKGGSGRGVVSTCSYEARKYGIHSAMPISQAYRFCPDAVFLPVNMKLYAGVSAGVMEILRGFAEKFQQVSVDEAYLIPGSGVRNFEEAALYALRIKDEVQRQQKITCSVGVGPNKLVSKIASGFQKPDGLTVVRPEDVRDFLFPLPVSRIPGVGEKTEETLKKMGINRVEELANCDVQMLSEKLGKMGFRLKQLANGLDFEELVEKESVKSISRHGTFAEDTDDPVKVSGSLDLLIESVHGSLMKHSFLFKTITLTVRFEDFSTYTRSRTLSIWTSDVFVIKRTAMQLLSEFTGRRKFRLVGVGVTKLRERDERQTLITDFP", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DNA polymerase type-Y family."}
+{"protein": "MRSKFMSSPTLSDLGKREATAAAALDERGTQQKRAGANATWNSIQNGVISVFQKKGLADHELYSLNEGVRQLLKTELGSFFTEYLQNQLLTKGMVILRDKIRFYEGQKLLDSLAETWDFFFSDILPMLQAIFYPVQGKEPSIRQLALLHFRNIITLNLKLDDALSRPRARVPPSIIQMLLILQGVHESKGVTEEYMNLESLIQKVVSPYLGTYGLYSNEAPFCHSSCILEKRMFRRCPKSGEILTKNPVVRSKSYNNPLLTPVAEYEMENLVANGSGIRRHSVSEMTSVLELPMGYSNLTTDSTSKLSMAGTKPPGEGERPPISNGQFPPLHNLSDSQQGLYNSQRDSPLLPAPSSSPETIVDQILESIDSDSEGIFIDFGRGCSKSPEFSMEIGRQSLV", "text": "FUNCTION: Subunit of TORC2, which regulates cell growth and survival in response to hormonal signals. SIMILARITY: Belongs to the PROTOR family."}
+{"protein": "MAWRQLRKRALDAVIILGGGGLLFTSYLTATGDDHFYAEYLMPGLQRLLDPESAHRLAVRVTSLGLLPRATFQDSDMLEVKVLGHKFRNPVGIAAGFDKNGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAQLTADGLPLGINLGKNKTSEDAAADYAEGVRTLGPLADYLVVNVSSPNTAGLRSLQGKTELRHLLSKVLQERDALKGTRKPAVLVKIAPDLTAQDKEDIASVARELGIDGLIVTNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRIPIIGVGGVSSGQDALEKIQAGASLVQLYTALIFLGPPVVVRVKRELEALLKERGFTTVTDAIGADHRR", "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": "MIEQINKDGEKKNSTDTRTIVITSGKGGVGKTTTTANLGMSIARLGYKVALIDADVGLRNLDLLLGLENRVIYTAMEVFEGECCLDQALIRDKRWSNLALLAISKTRQRYHLTRRNMEMLVDSIRLRNYNFILIDCPAGIDVGFVNAVAPAEEAVVVTTPEITSIRDADRVAGLLEASGIYEVKLLVNRVRPDMIQKNDMLSVRDVQEMLGIPLLGAIPEDTNVIVSTNRGQPLVLNKKLTLSGISFENAARRLVGRKEYLVNLETGNKGLLKRVQQFLTGSEENV", "text": "FUNCTION: ATPase required for the correct placement of the division site. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ParA family. MinD subfamily."}
+{"protein": "DTATCGKVFYSASAVSAASNAACNYVRAGSTAGGSTYPHVYNNYEGFRFKGLSKPFYEFPILSSGKTYTGGSPGADRVVINGQCSIAGIITHTGASGNAFVACGGT", "text": "SIMILARITY: Belongs to the ribonuclease N1/T1 family."}
+{"protein": "MSSDLKKINKVKKNSRRISNTQEPKLVERLIKISRVSKVTKGGKKLSFRAIVVVGDENGKVGVGVAKADDVVNAFKKAKTDGRKNLIELPITKALSIPHNVAGNFGACKVIMRPSIEGSGVIAGGAVRIVLEVAGVKNVIAKQLGSNNLLNNARASVCALQNLTTKAQVAKKRNLD", "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": "MSCSRPCVCSHGTSVEESTWYGFDFYPNLFYNDWLGTTTLPYNPERIPIRYINRPWPSLCWKVTVAVASLFLLLGVAALTTGYAVPPKLELVNESKFSSMEDPVADYNQALMTCRVVGATLCGVAGIMLAVCLFLIASGWMFQDIKAEPLVTETDSPVEVFRDEPEKLSPAFHETSSQSPFLTPPSPFGQQSVQTSQPQRDL", "text": "FUNCTION: May play a role in maintenance and/or transport of vesicles. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the VMP family."}
+{"protein": "MATFTDAEIDELFETSGTVIDSIITAQGKPVETVGRSAIPRGKTKALSSAWEKHGSVQSPASQDTPDRQDRSDKQLSTPEQVTPHDSPPATSTDQPPTQAADEAGDTQLKTGASNSLLSMLDKLSNKSSNAKKGPMVKPPGRASSTSDSTAGESTKPRKQSRETAEPGQGRPWKPGHRREHSISWTMGGVTTISWCNPSCSPIRAEPRQYSCTCGSCPATCRLCASDDVYDGGDITEGK", "text": "FUNCTION: Protects the virus against cell antiviral state by blocking host interferon signaling. Mechanistically, targets host phosphorylated STAT1 (phospho-STAT1) for degradation, thereby inhibiting the interferon alpha signaling pathway. Plays a role in the inhibition of host apoptosis. Interacts with and down-regulates the expression of host TXNL1. In turn, inhibits TXNL1-induced apoptosis through the BCL2- BAX-caspase 3 pathway. Inhibits host apoptosis also by negatively regulating host CacyBP/SIP. Promotes viral replication by activating the extracellular signal-regulated kinase (ERK) pathway. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus."}
+{"protein": "MASYTVSFIPLTLSNPRIFVSRQNGSPSSSSRIPLTSSLLGKKLLATQPSHRCFVPKLRCLTSASTVLNVPIAQPENGSSDKIPKWSARAIKSLAMGELEARKLKYPSTGTEAILMGILVEGTSTVAKFLRGNGVTLFKVRDETLSLLGKSDMYFFSPEHPPLTEPAQKAIAWAIDEKNKSDVDGELTTAYLLLGVWSQKDSAGRQILEKLGFNEDKAKEVEKSMNEDVDLSFKKQGQ", "text": "FUNCTION: Accessory protein regulating the assembly of the plastidial Clp protease system (PubMed:21266658, PubMed:25921872). CLPT1 first binds to the heptameric P-ring containing the CLP3-6 subunits followed by CLPT2, and only then does the P-ring combine with the R-ring composed of the clpP1 and CLPR1-4 subunits (PubMed:21266658). Once the core complex is fully assembled, it then associates to the CLPC chaperone partner to form the functional protease (PubMed:21266658). CLPT1 and CLPT2 are partially redundant (PubMed:25921872). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ClpA/ClpB family."}
+{"protein": "MASSASLETMVPPACPRAGASPATSKTLAFSIERIMAKTSEPRAPFEPRPGALEADGSQGKKLLNLCSPLPCMIPLQPLGYEVPSKTLLSYSELWKSSLRAGGGGGGGGGGGGGGGGAPVCGASGLCKTNCGVCCKAELGLAPSALPAGRVIKPQVINQAVGLPASGSLYYFNYLDSTAYPPSELLSGHLFPSGLLNAQAPAALAAHPKLFLLENAKLAGLAADKFPHPAPYPHKERLPAPLEQVLKENSALTAERGGVKGHSKLPGGSADGKPKNFTCEVCGKVFNAHYNLTRHMPVHTGARPFVCKVCGKGFRQASTLCRHKIIHTQEKPHKCNQCGKAFNRSSTLNTHIRIHAGYKPFVCEFCGKGFHQKGNYKNHKLTHSGEKQYKCTICNKAFHQVYNLTFHMHTHNDKKPFTCATCGKGFCRNFDLKKHVRKLHDSVGPAAPSAKDLTRTVQS", "text": "FUNCTION: Transcription repressor. Required for the specification of corticospinal motor neurons and other subcerebral projection neurons. May play a role in layer and neuronal subtype-specific patterning of subcortical projections and axonal fasciculation. Controls the development of dendritic arborization and spines of large layer V pyramidal neurons. May be involved in innate immunity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MKRFFKMALFLGVSALYGQQGGMWIPSLLEGMNAKEMKTLGMKMTVADIYSVNKSSLKDAAPHFNGGCSSEVISDKGLLLTNHHCGYGQIQAHSTLQNDYLANGFWAKSLAEELPNKNLKVTFMVRIDDVTKQVLKGTESITDETEKAKLIEKNIAEVIKTAPKEAWQENSVKAFYDGNQYILFVTETFKDVRLVGAPPSSIGKFGSDTDNWVWPRHTGDFSLFRIYADKNNRPAEYSKDNVPYKPKHFFPISLKGVKEGDFVLVFGYPGTTQEYLPSAAVAQIENVINPARIGIRDIVLKVQDSYMRKDQGIKIKYAAKYARVANYWKKWMGETKGLKKSGAVALKQQQEAKFQQAIQKANKQAQYGNLLSDFNRLYKEIEPYTLAANLNSEFIFRNIDLLSNGSRLLQLEKALEDKGEQSFNDRKKNLLNTFKEIFKDNDKQVDKDVFEKVVVFYAANMPKNLLINSLKNFDAKKLADNLYNNSFLTSLSGVESVLNLSAAEFKERMKNDVGIQFVRELKEMNDTQVFPVYDRLNTQIHALQRTYMKAILEFSKPSDRIFPDANGTLRVTYGKVAGFSPADAVTYSAHTTLDGVMEKYVPGDYEFDVPQHLRDLQAKKDFGRYGDKNGKMPLCFLSTCHTTGGNSGSPAIDANGNLIGLNFDRVWEGTMSDIHYDPKLCRNIMVDIRYVLFVIDKYAGAGHLVNEMKLIK", "text": "FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has probably a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA. SIMILARITY: Belongs to the peptidase S46 family."}
+{"protein": "MSNEYDYLFKLLLIGDSSVGKSCLLLRFADDAYIDSYISTIGVDFKIRTIEQDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIIVYDCTEMESFNNVKQWLSEIDRYANESVCKLLIGNKNDMVESKVVSTETGRALADELGIPFLETSAKDSINVEQAFLTIAGEIKKKMGSQTNANKTSGPGTVQMKGQPIQQNNGGCCGQ", "text": "FUNCTION: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane Golgi apparatus membrane; Lipid-anchor. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MAISPWKQFKLSVLNANQWFRKTPERALNMAYDAANKIRSIEEEHFEGRKISNVSISYSNSTKSYFNSQLNRYLKIIQVRLAEFNTSISVVGTLDQNKVDKQKDKFDQNYQQEFPGRSSIILDKLEFIDQVSSRYYKSSNHEAQELNTDLEIPHSSSSIAIVSSNVNVNNYPNNVRAGSSQNQNNLAELKSNIPNTNFLPRSLLKTFKKIKQELDPEAETEVIRKFRKSQIKTLTSVRFILLVILVPLLIHQLSKITFVGYLVDNFMSLPHQQAELFLNSNMEEEALVKLHQYEEKLHFKMYLGQAPELFPELYESGKEITEIPKSEREELIEHKVEKKAQEIALEYKAKGNNGIKNIFCDFISLITFVIIISTRKRELEVLKSFMDDVVYGLSDSAKAFIIILLTDMFVGFHSPHGWEVILENITRHFGLPESRDFNFLFIATFPVILDAVFKYWIFRYLNRSSPSAVATYKNMNE", "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": "MLRPKALTQVLSQANTGGVQSTLLLNNEGSLLAYSGYGDTDARVTAAIASNIWAAYDKNGHQAFNEDNLKLILMDCMEGRVAITRVSNLLLCMYAKETVGFGMLKAKAQALVYYLEEPLNQVSSA", "text": "FUNCTION: Regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, may activate the TOR signaling cascade in response to amino acids. Adapter protein that may regulate the MAP kinase cascade (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GAMAD family."}
+{"protein": "MGTARFLSAVLLLSVLLMVTFPALLSAEYHDGRVDICSLPYDSGDCLRFFEMWYFDGTTCTKFVYGGYGGNDNRFPTEKACMKRCAKA", "text": "FUNCTION: Serine protease inhibitor that inhibits chymotrypsin and blocks voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family. 03 (sub-Kunitz) subfamily."}
+{"protein": "MDIEERIKLVLKKPTEEVLTVENLRHLFEIGAPLQHYIGFEISGYIHLGTGLMAGAKIADFQKAGIKTRVFLADWHSWINDKLGGDLETIQEVALKYFKVGMEKSIEVMGGKPEKVEFVLASEILEKGDYWQTVIDISKNVTLSRVLRSITIMGRKMGEAIDFAKLIYPMMQVADIFYQGVTIAHAGMDQRKAHVIAIEVAEKLRYHPIIHNGEKLKPVAVHHHLLLGLQEPPKWPIESEEEFKEIKAEMKMSKSKPYSAVFIHDSPEEIREKLRKAFCPAREVKYNPVLDWVEYLVFREEPTEFTIHRPAKYGGDVTYTTFEELKRDFAEGKLHPLDLKNAVAEYLIDLLEPIRKYFERHPEPLELMKSVQITR", "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": "MKVSQILPLAGAISVASGFWIPDFSNKQNSNSYPGQYKGKGGYQDDCGDDYKKGYKSKTYSKVKPITSTDCTTPIQPTGTTTGYTKDVVESTSYTTDTAYTTTVITVTKCDGGSCSHTAVTTGVTIITVTTNDVITEYTTYCPLTSTPATESTPATESTPATESTPATESTPATESTPATESTPCTTSTETTPATESTPATESTPATESTPATESTPATESTPATESTPATESTPATESTPCTTSTETTPATESTASTETASSTPVESTVIVPSTTVITVSSCYEDKCSVSSVTTGVVTISSEETIYTTYCPITSSITIPVPNTSTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPGTEATPVTTQPVSVLSTSQVVTASGEFSTVTAHSTSIVASCPEGGCVPEGQQTETSPSVPTNGPEVEASSSVLSIPVSSVTTSTIASSSETSVPPAQVSTFEGSGSALKKPYYGLAVAALVYFM", "text": "FUNCTION: Cell wall protein which mediates cell-cell and cell-substrate adhesion. Required for biofilm formation and plays a role in virulence. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the PGA18 family."}
+{"protein": "MSCMKDPLSLERLGAGNNKLCSSSPSSSSSSSSCHHQQPALAMATALAPGQARSSLEAAKHRLEVHTISDTSSPEAAEKEKSQQGKSEDAGPEDPSKKKRQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGPQFNGLMQPYDDMYPGYSYNNWAAKGLTSASLSTKSFPFFNSMNVNPLSSQSMFSPPNSISSMSMSSSMVPSAVTGVPGSGLNSLNNLNNLSNPSLNSAVPTPACPYAPPTPPYVYRDTCNSSLASLRLKAKQHSSFGYASVQNPASNLSACQYPVDRPV", "text": "FUNCTION: May play an important role in development and maintenance of anterior structures. May play a role in determining left-right asymmetry and in vasculogenesis during avian embryogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily."}
+{"protein": "MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFIALGAPLAPRDAGSQRPRKKEDNILVESHEKSLGEADKADVDVLTKAKSQ", "text": "FUNCTION: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D- glucose (2DG) transport and glycogen synthesis in osteoblastic cells (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the parathyroid hormone family."}
+{"protein": "MTTRLLQGKKGLITGIANNMSISWAIAQLAKKHGAELWFTYQSEALEKRVKPLAEEIGCNFISELDVTDQKSISNLFNDIKEKWNSFDFLLHGMAFANKNELKGRYVDTSLENFYNSLHISCYSLLELSRSAETLMHDGGSILTLTYYGAEKVIPNYNIMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAISDFSTMLKFHASTAPLKRNITQEDVGGAAVYLFSELSKGVTGEIHYVDCGYNIIGSSKLL", "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": "MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE", "text": "FUNCTION: Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate. SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
+{"protein": "MPVMKGLLAPQNTFLDTIATRFDGTHSNFLLANAQGTRGFPIVYCSDGFCELTGYGRTEVMQKTCSCRFLYGPETSEPALQRLHKALEGHQEHRAEICFYRKDGSAFWCLLDMMPIKNEMGEVVLFLFSFKDITQSGSPGLGPQGGRGDSNHENSLGRRGATWKFRSARRRSRTVLHRLTGHFGRRGQGGMKANNNVFEPKPSVPEYKVASVGGSRCLLLHYSVSKAIWDGLILLATFYVAVTVPYNVCFSGDDDTPITSRHTLVSDIAVEMLFILDIILNFRTTYVSQSGQVISAPRSIGLHYLATWFFIDLIAALPFDLLYIFNITVTSLVHLLKTVRLLRLLRLLQKLERYSQCSAVVLTLLMSVFALLAHWMACIWYVIGRREMEANDPLLWDIGWLHELGKRLEVPYVNGSVGGPSRRSAYIAALYFTLSSLTSVGFGNVCANTDAEKIFSICTMLIGALMHAVVFGNVTAIIQRMYSRRSLYHSRMKDLKDFIRVHRLPRPLKQRMLEYFQTTWAVNSGIDANELLRDFPDELRADIAMHLNREILQLPLFGAASRGCLRALSLHIKTSFCAPGEYLLRRGDALQAHYYVCSGSLEVLRDNMVLAILGKGDLIGADIPEPGQEPGLGADPNFVLKTSADVKALTYCGLQQLSSRGLAEVLRLYPEYGAAFRAGLPRDLTFNLRQGSDTSGLSRFSRSPRLSQPRSESLGSSSDKTLPSITEAESGAEPGGGPRPRRPLLLPNLSPARPRGSLVSLLGEELPPFSALVSSPSLSPSLSPALAGQGHSASPHGPPRCSAAWKPPQLLIPPLGTFGPPDLSPRIVDGIEDSGSTAEAPSFRFSRRPELPRPRSQAPPTGTRPSPELASEAEEVKEKVCRLNQEISRLNQEVSQLSRELRHIMGLLQARLGPPGHPAGSAWTPDPPCPQLRPPCLSPCASRPPPSLQDTTLAEVHCPASVGTMETGTALLDLRPSILPPYPSEPDPLGPSPVPEASPPTPSLLRHSFQSRSDTFH", "text": "FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits an outward current, but shows no inactivation. Channel properties may be modulated by cAMP and subunit assembly. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC 1.A.1.20) subfamily. Kv12.3/KCNH4 sub-subfamily."}
+{"protein": "MPPKGHKKTADGDFRPVNSAGNTIQAKQKYSIDDLLYPKSTIKNLAKETLPDDAIISKDALTAIQRAATLFVSYMASHGNASAEAGGRKKITPQDVFVALKDVDLAQFVPSVTQSVNEFEQEVAQRKKDKVVRAQDDQDHISSSESETEATEEEGNKRIRTDE", "text": "FUNCTION: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MEGQVVGRVFRLFQRRLLQLRAGPPQDNSGEALKEPERAQEHSLPNFAGGQHFFEYLLVVSLKKKRSEDDYEPIITYQFPKRENLLRGQQEEEERLLKAIPLFCFPDGNEWASLTEYPRETFSFVLTNVDGSRKIGYCRRLLPAGPGPRLPKVYCIISCIGCFGLFSKILDEVEKRHQISMAVIYPFMQGLREAAFPAPGKTVTLKSFIPDSGTEFISLTRPLDSHLEHVDFSSLLHCLSFEQILQIFASAVLERKIIFLAEGLSTLSQCIHAAAALLYPFSWAHTYIPVVPESLLATVCCPTPFMVGVQMRFQQEVMDSPMEEVLLVNLCEGTFLMSVGDEKDILPPKLQDDILDSLGQGINELKTAEQINEHVSGPFVQFFVKIVGHYASYIKREANGQGHFQERSFCKALTSKTNRRFVKKFVKTQLFSLFIQEAEKSKNPPAGYFQQKILEYEEQKKQKKPREKTVK", "text": "FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MMPAKLQLDVLRTLQSSARHGTQTLKNSNFLERFHKDRIVFCLPFFPALFLVPVQKVLQHLCLRFTQVAPYFIIQLFDLPSRHAENLAPLLASCRIQYTNCFSSSSNGQVPSIISLYLRVDLSPFYAKIFQISYRVPMIWLDVFQVFFVFLVISQHSLHS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0479 family."}
+{"protein": "MIENRPWLTIFSHTMLILGIAVILFPLYVAFVAATLDKQAVYAAPMTLIPGTHLLENIHNIWVNGVGTNSAPFWRMLLNSFVMAFSITLGKITVSMLSAFAIVWFRFPLRNLFFWMIFITLMLPVEVRIFPTVEVIANLKMLDSYAGLTLPLMASATATFLFRQFFMTLPDELVEAARIDGASPMRFFCDIVFPLSKTNLAALFVITFIYGWNQYLWPLLIITDVDLGTTVAGIKGMIATGEGTTEWNSVMAAMLLTLIPPVVIVLVMQRAFVRGLVDSEK", "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": "MAKIIVVTSGKGGVGKTTTSASIATGLALRGYKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIQGEATLNQALIKDKNCENLFILPASQTRDKDALTREGVEKVMQELSGKKMGFEYIICDSPAGIEQGALMALYFADEAIVTTNPEVSSVRDSDRILGILQSKSHKAEQGGSVKEHLLITRYSPERVAKGEMLSVQDICDILHIPLLGVIPESQNVLQASNSGEPVIHQDSVAASEAYKDVIARLLGENREMRFLEAEKKSFFKRLFGG", "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 inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ParA family. MinD subfamily."}
+{"protein": "MAVSTVFSTSSLMLALSRHSLLSPLLSVTSFRRFYRGDSPTDSQKDMIEIPLPPWQERTDESIETKRARLLYESRKRGMLENCILLSLFAKEHLQHMTEKQLNLYDRLINEPSNDWDIYYWATEAKPAPEIFENEVMALLRDFAKNKNKEQRLRAPDLEYLFEKPR", "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 SDHA of the SDH catalytic dimer. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the SDHAF2 family."}
+{"protein": "MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYHQKQVVILSQDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGLSKRQTNGYLNGYTPSRKRQASESSSRPH", "text": "FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. SIMILARITY: Belongs to the uridine kinase family. SIMILARITY: Belongs to the uridine kinase family."}
+{"protein": "MDYVSLLNQVWQKQVNSSQEGTLAPVRPTYAYRPVQGNLQCPIKWRCIYTFAGYTGTATEPTKVLAKQEAARKVCLRLQEYGRLDGFGLRLRYSTAFEHNRYDASKSYFYTQTSSSSHE", "text": "FUNCTION: Induces host cell G0/G1 arrest and apoptosis. SUBCELLULAR LOCATION: Host nucleus, host nucleolus Host mitochondrion."}
+{"protein": "MKYDTILVDGYQRVGIITLNRPQALNALNSQMMNEITNAAKELDIDPDVGAILITGSPKVFAAGADIKEMASLTFTDAFDADFFSAWGKLAAVRTPMIAAVAGYALGGGCELAMMCDLLIAADTAKFGQPEIKLGVLPGMGGSQRLTRAIGKAKAMDLILTGRTIDAAEAERSGLVSRVVLADDLLPEAKAVATTISQMSRSATRMAKEAVNRSFESTLAEGLLHERRLFHSTFVTDDQSEGMAAFIEKRAPQFTHR", "text": "FUNCTION: Could possibly oxidize fatty acids using specific components. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
+{"protein": "MDITIHNPLIRRPLFSWLTPSRIFDQIFGEHLQESELLPTSPSLSPFLMRSPFFRMPSWLETGLSEMRLEKDKFSVNLDVKHFSPEELKVKVLGDMIEIHGKHEERQDEHGFIAREFSRKYRIPADVDPLTITSSLSLDGVLTVSAPRKQSDVPERSIPITREEKPAIAGSQRK", "text": "FUNCTION: May contribute to the transparency and refractive index of the lens. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MLGKGVVGGGGGTKAPKPSFVSYVRPEEIHTNEKEVTEKEVTLHLLPGEQLLCEASTVLKYVQEDSCQHGVYGRLVCTDFKIAFLGDDESALDNDETQFKNKVIGENDITLHCVDQIYGVFDEKKKTLFGQLKKYPEKLIIHCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQAPKLLKRLFLFSYATAAQNNTVTDPKNHTVMFDTLKDWCWELERTKGNMKYKAVSVNEGYKVCERLPAYFVVPTPLPEENVQRFQGHGIPIWCWSCHNGSALLKMSALPKEQDDGILQIQKSFLDGIYKTIHRPPYEIVKTEDLSSNFLSLQEIQTAYSKFKQLFLIDNSTEFWDTDIKWFSLLESSSWLDIIRRCLKKAIEITECMEAQNMNVLLLEENASDLCCLISSLVQLMMDPHCRTRIGFQSLIQKEWVMGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQLVHQHPPAFEFTETYLTVLSDSLYIPIFSTFFFNSPHQKDTNMGREGQDTQSKPLNLLTVWDWSVQFEPKAQTLLKNPLYVEKPKLDKGQRKGMRFKHQRQLSLPLTQSKSSPKRGFFREETDHLIKNLLGKRISKLINSSDELQDNFREFYDSWHSKSTDYHGLLLPHIEGPEIKVWAQRYLRWIPEAQILGGGQVATLSKLLEMMEEVQSLQEKIDERHHSQQAPQAEAPCLLRNSARLSSLFPFALLQRHSSKPVLPTSGWKALGDEDDLAKREDEFVDLGDV", "text": "FUNCTION: Acts as an adapter for the myotubularin-related phosphatases (PubMed:11504939, PubMed:12847286, PubMed:23818870). Regulates phosphatase MTM1 protein stability and possibly its intracellular location (PubMed:23818870). By stabilizing MTM1 protein levels, required for skeletal muscle maintenance but not for myogenesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Sarcoplasmic reticulum Cytoplasm, myofibril, sarcomere Note=Localizes to punctate vesicles when associated with MTM1 (PubMed:12847286). Localizes to triads, a structure formed by a T tubule and two sarcoplasmic reticulum terminal cisterna (By similarity). In skeletal muscles, co-localizes with MTM1 in the sarcomere (By similarity). Partially localizes to the sarcoplasmic reticulum in skeletal muscles (By similarity). SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily."}
+{"protein": "MVTLIVATTADPASINPAAALLAMPGWTAGPILPPDIKSFSNKQTRVIQHDRSIVKEDDLDLRWEEATGEVVDEVIFLSRHTAVSNRPALTVHPIGVLHLKDGESPPQGGKPGWAALPSTRIGPWFRLLKKMAEAHGLVPEFEITLEATHHGPITNKPTMFLEIGSTEEYWKRQDAAQVMALLMWEGLGLGGSEEVGKWKSETGKRKVLLGIGGGHYAPRHMDIALKDDIWVGHLLSGYSLPMEDPTQTKTTPGENYIGGNWRQSIKAAFEATKASFPGGEILAHLDHKSFKGWQKKAITEFLAEESINVGKPNDFT", "text": "FUNCTION: Hydrolyzes D-aminoacyl-tRNA into D-amino acid and free tRNA. Broad specificity toward the amino acid, but strict specificity toward the D-isomer. Seems to be required for ethanol tolerance. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the DtdA deacylase family."}
+{"protein": "MSAYWIAVASAQHVRRGRNDGFMQVNHGKAAPLRRVKPGDGIVYYSPTTILGEKDGLQAFTAIGTVRYGKESPYQGEMGGGFTPFRRDVEWAVAEEAPIKPLLDRLDFTAGKSNWGYHLRFGLFEITDHDFRLIAEAMGAPKTLAEATA", "text": "SIMILARITY: Belongs to the UPF0310 family."}
+{"protein": "MGFTTKIIFLYNLVLVYAGFDDPRKAIELVQKRYGRPCDCSGGQVSEPPSDRVSQVTCSGKTAYLMPDQRWKCKSIPKDTSPSGPLQECPCNSYQSSVHSSCYTSYQQCRSGNKTYYTATLLKTQTGGTSDVQVLGSTNKLIQSPCNGIKGQSICWSTTAPIHVSDGGGPLDTTRIKSVQRKLEEIHKALYPELQYHPLAIPKVRDNLMVDAQTLNILNATYNLLLMSNTSLVDDCWLCLKLGPPTPLAIPNFLLSYVTRSSDNISCLIIPPLLVQPMQFSNSSCLFSPSYNSTEEIDLGHVAFSNCTSITNVTGPICAVNGSVFLCGNNMAYTYLPTNWTGLCVLATLLPDIDIIPGDEPVPIPAIDHFIYRPKRAIQFIPLLAGLGITAAFTTGATGLGVSVTQYTKLSNQLISDVQILSSTIQDLQDQVDSLAEVVLQNRRGLDLLTAEQGGICLALQEKCCFYVNKSGIVRDKIKTLQEELERRRKDLASNPLWTGLQGLLPYLLPFLGPLLTLLLLLTIGPCIFNRLTAFINDKLNIIHAMVLTQQYQVLRTDEEAQD", "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 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). SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane; Peripheral membrane protein. Note=The R-peptide is membrane-associated through its palmitate. 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). 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."}
+{"protein": "MAASTDVAGLEESFRKFAIHGDPKASGHEMNGKNWAKLCKDCKVADGKAVTGTDVDIVFSKVKAKSARVINYEEFKKALEELAPKRFKGKSKEEAFDAICQLVAGKEPANVGVTKAKTGGAVERLTDTSKYTGSHKERFDESGKGKGIAGRQDILDDSGYVSAYKNAGTYDAKVKK", "text": "FUNCTION: Regulator of microtubule dynamic that has microtubule bundling activity (By similarity). Required for embryo implantation; possibly by regulating beta-catenin (By similarity). Also required for decidualization via regulation of beta-catenin (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TPPP family."}
+{"protein": "MYKFEIYQDKAGEYRFRFKASNGETMFSSEGYKAKASAIHAIESIKRNSAGADTVDLTTMTA", "text": "SIMILARITY: Belongs to the UPF0339 family."}
+{"protein": "MAASFLTMDNSRTRQNMNGSANWSQQSGRTSTSSLEDLEIPKFRSFAPSSISISPSLVSPSTCFSPSLFLDSPAFVSSSANVLASPTTGALITNVTNQKGINEGDKSNNNNFNLFDFSFHTQSSGVSAPTTTTTTTTTTTTTNSSIFQSQEQQKKNQSEQWSQTETRPNNQAVSYNGREQRKGEDGYNWRKYGQKQVKGSENPRSYYKCTFPNCPTKKKVERSLEGQITEIVYKGSHNHPKPQSTRRSSSSSSTFHSAVYNASLDHNRQASSDQPNSNNSFHQSDSFGMQQEDNTTSDSVGDDEFEQGSSIVSRDEEDCGSEPEAKRWKGDNETNGGNGGGSKTVREPRIVVQTTSDIDILDDGYRWRKYGQKVVKGNPNPRSYYKCTTIGCPVRKHVERASHDMRAVITTYEGKHNHDVPAARGSGYATNRAPQDSSSVPIRPAAIAGHSNYTTSSQAPYTLQMLHNNNTNTGPFGYAMNNNNNNSNLQTQQNFVGGGFSRAKEEPNEETSFFDSFMP", "text": "FUNCTION: Transcription factor. Interacts specifically with the W box (5'-TTGAC[CT]-3'), a frequently occurring elicitor-responsive cis- acting element. Involved in defense responses. Required for resistance to the necrotrophic fungal pathogen B.cinerea (PubMed:17059405, PubMed:21990940). Regulates the antagonistic relationship between defense pathways mediating responses to the bacterial pathogen P. syringae and the necrotrophic pathogen B.cinerea (PubMed:17059405). Required for the phytoalexin camalexin synthesis following infection with B.cinerea. Acts as positive regulator of the camalexin biosynthetic genes PAD3 (CYP71B15) and CYP71A13 by binding to their promoters (PubMed:21498677, PubMed:22392279). Acts downstream of MPK3 and MPK6 in reprogramming the expression of camalexin biosynthetic genes, which drives the metabolic flow to camalexin production (PubMed:21498677). Functions with WRKY25 as positive regulator of salt stress response and abscisic acid (ABA) signaling (PubMed:18839316). Functions with WRKY25 and WRKY26 as positive regulator of plant thermotolerance by partially participating in ethylene-response signal transduction pathway (PubMed:21336597). The DNA-binding activity of WRKY33 is increased by SIB1 and SIB2 (PubMed:21990940). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRKY group I family."}
+{"protein": "ELVSEFCLKKERVCEDSSLTISCPEGEGIVIYDAIYGRKRGEVCPGLFGAFTKNRKCRSSNSQQVVENSCEGKSSCTVLASNSVFGDPCPGTAKYLAVTYICSFL", "text": "FUNCTION: This protein binds D-galactoside. May have an important role in the activation of eggs (triggered by fertilization), or in their subsequent differentiation. The dimeric form is essential for hemagglutination activity. SUBCELLULAR LOCATION: Cytoplasm. Note=Cytoplasmic in unfertilized eggs, and shifted to the peripheral regions after fertilization."}
+{"protein": "MSNQWWDEWAEKCHSKAHRQLLFWRYLVKQTLLLVEDDKNLADGLLVSLEQAGYDCLHAETIADVKQHWDKADLVILDRQLPDGDSVQHLMDWKKIKDIPVILLTALVTVKDKVTGLDAGANDYLTKPFAEAELFARIRAQLRSPDSGQDDSKVVTSNLTIDKATREVFFNGESITLTRTEFDLLLFLASNLGRVFTRDELLDHVWGYNHFPTTRTVDTHVLQLRQKLPGLEIETLRGVGYKMKA", "text": "FUNCTION: Member of the two-component regulatory system VxrB/VxrA involved in the regulation of diverses processes, including virulence, the type VI secretion system (T6SS) and biofilm formation (PubMed:26000450, PubMed:28607158). VxrB positively regulates the expression of the T6SS, a virulence nanomachine that directly translocates effectors into bacterial or host cells, thereby facilitating colonization by competing with sister cells and intestinal microbiota (PubMed:26000450). In addition, it activates vpsL expression and biofilm formation, and represses motility (PubMed:28607158). May regulate biofilm formation via its regulation of key biofilm regulators and cyclic di-GMP levels (PubMed:28607158). Significantly contributes to both attack and defense via T6SS, while also influencing competition via regulation of biofilm matrix production (PubMed:35880882). Is critical for colonization in the infant mouse model (PubMed:26000450). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MAELISKEGNKVEFKVSVPAAEVNRAYDQVWAGLARDVRVPGFRPGKAPRKVIENRVGKGYVESQVRDRLLETHYSQGLRELGLNLVDATVDPQDVQSGQAFEFTVKGETYPEVKLGDWQGLKVSAQAPEITDEVLEQTLSDLRERNASFEKAERPIEAADQVTIQELGEGDSEEGGSYPIYLDMAEEHVRNALLGKSAGDVVDITVPAHQHGDHEHAEHTVRVKVVEVSSKKLQDLNDEFATSLNYESMDKLRTDLREELERRAQQEGDNLRREELVGHLVEGMTVEIPQALIDRRREGMMSEIQDDLRRQGVQWKEYEAFMQEQGKLDEFEADLTKNAETRVRRDLALEQLATDLNAQVNEAEFNQTLMNLAQANGMNVQQLVQQLGQDGVQSYYISLLRERGLQRALAQLSGEGQSTEAASPKATGTEAAGTEQSEPAQTETAQNDAGQTETAQSEGEQQSE", "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). Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24), exposing a hydrophobic crevice that is probably important for its chaperone activity (PubMed:16091460, PubMed:16271892). 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": "MSLSRRQFIQASGIALCAGAVPLKASAAGQQQPLPVPPLLESRRGQPLFMTVQRAHWSFTPGTRASVWGINGRYLGPTIRVWKGDDVKLIYSNRLTENVSMTVAGLQVPGPLMGGPARMMSPNADWAPVLPIRQNAATLWYHANTPNRTAQQVYNGLAGMWLVEDEVSKSLPIPNHYGVDDFPVIIQDKRLDNFGTPEYNEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQMNDGRPLHVISGDQGFLPAPVSVKQLSLAPGERREILVDMSNGDEVSITCGEAASIVDRIRGFFEPSSILVSTLVLTLRPTGLLPLVTDSLPMRLLPTEIMAGSPIRSRDISLGDDPGINGQLWDVNRIDVTAQQGTWERWTVRADEPQAFHIEGVMFQIRNVNGAMPFPEDRGWKDTVWVDGQVELLVYFGQPSWAHFPFYFNSQTLEMADRGSIGQLLVNPVP", "text": "FUNCTION: Cell division protein that is required for growth during stress conditions. May be involved in protecting or stabilizing the divisomal assembly under conditions of stress. SUBCELLULAR LOCATION: Periplasm Note=Localizes to the division septum. Localization requires FtsZ, FtsQ, FtsL and FtsN. SIMILARITY: Belongs to the FtsP family."}
+{"protein": "MSEIQDYNSSVSDPSSRKFETFSYLPELGVEKIRKQVEYIVSKGWNPAVEHTEPENAFDHYWYMWKLPMFGETDVDAILAEAEACHKAHPSHHVRLIGYDNYAQSQGTAMVIFRGPISAKC", "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. SIMILARITY: Belongs to the RuBisCO small chain family."}
+{"protein": "MPSQSPYHALSRYFSFPNRDHQAWWTGKGPLLGNMLADAGYPEQQQYQYLTLFNLHLIPALGPSESHGAGIDGAEWKSLLSGSGKLEFSMTYRKSAVSLRIAFEPTSLLAGTKKDVFNKRRTQQLLGDLERLDIDIDTVLYHPLFDTLVVSDEEEAALQNAGTVIPDSSRTQQLLALNLIEGNVRADLYVYPYVKALATGTASSTLLWAAVKKIDRYNRFRDALSILKGYFETYPSSTTNPMFLSSDLAAPRNAFCRLFFSETNFSWERVQHLWTLGGTLSDKPTLKGLELAKILWDILGISTAPASPDSFPLLFTFELRPEQPYLRQKLGIPVSGLTESAIANACVAFFERLGWDDHAASYRTNLSAY", "text": "FUNCTION: Prenyltransferase; 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 tryptophan dimethylallyltransferase family."}
+{"protein": "MGLVDGYDTSSDSDLNFDEGKSVHEKKNGNLHEDTSYEPSSNNIHKRKSHFTKSELKRRRKTRKGDGPWGSWSSSDDETSQASETQKEDQDIFVHALAEDNLDSEQIEVEEVSHFYGKSEKDYQGRGYLYPPNDVDVDLREERISFRCYLPKKVIRNYPGHPEGTTALKFLPKTGHLILSGGNDHTIKIWDFYHDYECLRDFQGHNKPIKALRFTEDCQSFLSSSFDRSVKIWDTETGKVKTRLHLNSTPADVESRPTNPHEFIVGLSNSKILHYDDRVSENQGLVQTYDHHLSSILALKYFPDGSKFISSSEDKTVRIWENQINVPIKQISDTAQHSMPFLNVHPSQNYFCAQSMDNRIYSFSLKPKYKRHPKKIFKGHSSAGYGISLAFSGDGRYICSGDSKSRLFTWDWNTSRLLNNIKIPGNKPITQVDWHPQETSKVICSGAAGKIYVCD", "text": "FUNCTION: May function in the second step of pre-mRNA splicing. Regulatory protein involved in replication and mitotic spindle formation and/or maintenance. Required for initiation and completion of S-phase and for initiation and completion of DNA replication. Might be required for the maintenance of microtubules. Essential only at elevated temperatures. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLKEEDKIFTNLHGQQSHDLKSSKKRGDWENTKALLDKGRDFIVEEVKKSGLRGRGGAGFSTGMKWSFMPKNSEKPCYLVVNADESEPGTCKDRDILRFEPHKLIEGCLLASFAIGANNCYIYIRGEFYNEASNIQRALDEAYKEGLIGKNACDSGFDCNIYLHRGAGAYICGEETALLESLEGKKGMPRLKPPFPAGFGLYGCPTTINNVESIAVVPTILRRGASWFAGIGKPNNTGTKIFCISGHVNKPCNVEEAMGISLKELIEKYAGGVRGGWDNLKAIIPGGSSVPLLPKLLCEVEMDFDSLRTAGSGLGTGGIIVMDKSTDIIYAIARLSKFYMHESCGQCTPCREGTGWMWRVMMRLVKGNAKKSEIDELLNVTKEIEGHTICALGDAAAWPIQGLIRHFRSEIEARIKSYSVV", "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": "MRSKKLWISLLFALTLIFTMAFSNMSAQAAGKSSTEKKYIVGFKQTMSAMSSAKKKDVISEKGGKVQKQFKYVNAAAATLDEKAVKELKKDPSVAYVEEDHIAHEYAQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVAPSASLYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPTGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSTSTVGYPAKYPSTIAVGAVNSSNQRASFSSVGSELDVMAPGVSIQSTLPGGTYGAYNGTSMATPHVAGAAALILSKHPTWTNAQVRDRLESTATYLGNSFYYGKGLINVQAAAQ", "text": "FUNCTION: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Subtilisin NAT also has fibrinolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
+{"protein": "MKINISYPATGCQKLIEVDDERKLRPFYEKRMSHQMTAESLGDEWKGYLVRISGGNDKQGFPMKQGVLTNGRVRLLLGKGHSCYRPRRTGERKRKSVRGCIVDSNLSVLNLVILKKGEQDIPGLTDTTIPRRLGPKRAGRIRKLFNLNKEDDVRQYVVRRPLPQKEGKKQKFKTPKIQRLITPQRLQRKRHMRAVKRRRYAKQREEEATYAKLLAKRKKEEREAHAKRRSSARESSLRESKSKA", "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": "MAMRELVEGECGGANPLMKLATHFTQDKALRQEGLRPGPWPPGASAAETVSKPLGVGTEDELVSEFLQDQNATLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVAQDYNETDWSQEFIAEVTDPLSVSPARWAEEYLEQSEEKLWLGDQEGSSTADRWYDEYHPEEDLQHTASDFVSKVDDPKLANSEFLKFVRQIGEGQVSLESAAGSGGAQAEQWAAEFIQQQGTSEAWVDQFTRPGNKIAALQVEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSASYDKGYQFEEENPLRDHPQPFEEGLHRLEEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNRTALMALAVSFTNESLQRQACETLRDWLRYSPAYAHLVAPGEEGATGAGPSKRILGSLLSDSLFLEVKDLFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPNDYLMWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLALSMLGQSDAYGAADARDLSALLAMFGLPQ", "text": "FUNCTION: [Isoform 1]: In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7. Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal. PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX5. FUNCTION: [Isoform 2]: Does not mediate translocation of peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal. FUNCTION: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle. SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome matrix Note=Cycles between the cytosol and the peroxisome matrix (By similarity). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (By similarity). Cys-11 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix. The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting PEX5 for a subsequent import cycle (By similarity). SIMILARITY: Belongs to the peroxisomal targeting signal receptor family."}
+{"protein": "MATAASNPYLPGNSLLAAGSIVHSDAAGAGGGGGGGGGGGGGGAGGGGGGMQPGSAAVTSGAYRGDPSSVKMVQSDFMQGAMAASNGGHMLSHAHQWVTALPHAAAAAAAAAAAAVEASSPWSGSAVGMAGSPQQPPQPPPPPPQGPDVKGGAGRDDLHAGTALHHRGPPHLGPPPPPPHQGHPGGWGAAAAAAAAAAAAAAAAHLPSMAGGQQPPPQSLLYSQPGGFTVNGMLSAPPGPGGGGGGAGGGAQSLVHPGLVRGDTPELAEHHHHHHHHAHPHPPHPHHAQGPPHHGGGGGGAGPGLNSHDPHSDEDTPTSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSSTGSPTSIDKIAAQGRKRKKRTSIEVSVKGALESHFLKCPKPSAQEITNLADSLQLEKEVVRVWFCNRRQKEKRMTPPGIQQQTPDDVYSQVGTVSADTPPPHHGLQTSVQ", "text": "FUNCTION: Transcription factor that acts synergistically with SOX11 and SOX4. Plays a role in neuronal development (PubMed:31303265). Is implicated in an enhancer activity at the embryonic met-mesencephalic junction; the enhancer element contains the octamer motif (5'-ATTTGCAT- 3') (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the POU transcription factor family. Class-3 subfamily."}
+{"protein": "MTSNPLDESMESLTVVPPAASPASRILVVEDEAVIRDMVALVLQQEGFTVDVAADGRTALNYFRSDSPEAGSVTENPDLVVLDLMLPAVNGLDFCRLLRRQGVTVPILMLSAKDTETDRVVGLEIGADDYLTKPFGTRELVARCRALLRRSQNQPAETPAVLRYEGLKLFPEECRVLLDDRELTLSPKEFRLLELFMRHPRRVWSRDQLLEKIWGIDFMGDSKTIDVHIRWLREKIEANPSNPSYLLTVRGFGYRLG", "text": "FUNCTION: Member of the two-component regulatory system SphR/SphS. Response regulator. Involved in inducible production of alkaline phosphatase in response to phosphate limitation as it is directly involved in the regulation of phoA transcription in response to phosphate limitation. Binds to two distinct sites upstream from the phoA promoter."}
+{"protein": "MRSIRKRWTICTISLLLIFYKTKEIARTEEHQETQLIGDGELCLSRSLVNSSDKIIRKAGSTIFQHSVQGWKINSSLVLEIRKNILRFLDAERDVSVVKSSFKPGDVIHYVLDRRRTLNISHNLHSLLPEVSPMKNRRFKTCAVVGNSGILLDSGCGKEIDSHNFVIRCNLAPVVEFAADVGTKSDFITMNPSVVQRAFGGFRNESDREKFVHRLSMLNDSVLWIPAFMVKGGEKHVEWVNALILKNKLQVRTAYPSLRLIHAVRGYWLTNKVPIKRPSTGLLMYTLATRFCDEIHLYGFWPFPKDLNGKAVKYHYYDDLKYRYFSNASPHRMPLEFKTLNVLHNRGALKLTTGKCMKQ", "text": "FUNCTION: Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
+{"protein": "METIRPLKFGTLSLPDRESRLVCRSILLDMLGEATIAPDEGDLTGVTGLFWKYVSLSLATVYFPRTMLRVNASGMGDSGVVILRAMDSPLVIRHRRIKVEAARADVIFLPSDASSEITLPEGGRFDCAHLPAYALASKRDLLKPIMMQPLAAECLPLQLLTNYAGYLLRQEYQSEEHAGMMVAHFYDLLPVLAQDIGNVSPRETPHNRMASIKMRVEQNLANGSFSITDVAEAERITPRAIQKFFSREGTTFSRYVLGRRLSLAKSLILAEGEATSISQIAYNVGFNDLSYFNRTFRSRYGVRPSDLRRLAAAA", "text": "FUNCTION: Transcriptional activator of the rhizobactin regulon."}
+{"protein": "MSHHSPPPPKHKGEHKGHGLPRGSERGSSSRGKDRSASVSNSVPMPAGGKASRTNCPPPAPQKTANRLINEKSPYLLQHAHNPVDWYPWGQEAFDKAKKENKPIFLSVGYSTCHWCHMMEEESFQNEEIGHLLNENFVSVMVDREERPDVDKVYMTFVQATSSGGGWPMNVWLTPSLQPFVGGTYFPPEDGLTRVGFRTVLMRICDQWKQNKNTLLENSQRVTTALLARSEISVGDRQLPPSAATMNSRCFQQLDEGYDEEYGGFAEAPKFPTPVILNFLFSYWLSHRVTQDGSRAQQMALHTLKMMANGGIRDHVGQGFHRYSTDRQWHIPHFEKMLYDQAQLSVVYCQAFQISGDEFFSDVAKGILQYVTRNLSHRSGGFYSAEDADSPPERGVKPQEGALYLWTVKEVQQLLPEPVGGASEPLTSGQLLMKHYGLSEAGNINPTQDVNGEMHGQNVLTVRDSLELTGARYGLEVEAVRALLNTGLEKLFQARKHRPKAHLDNKMLAAWNGLMVSGFAVAGSVLGMEKLVTQATNGAKFLKRHMFDVSSGRLKRTCYAGAGGTVEQSNPPCWGFLEDYAFVVRGLLDLYEASQESSWLEWALRLQDIQDKLFWDSHGGGYFCSEAELGTDLPLRLKDDQDGAEPSANSVSAHNLLRLHGLTGHKDWMDKCVCLLTAFSERMRRVPVALPEMVRALSAQQQTLKQIVICGDPQAKDTKALLQCVHSIYIPNKVLILADGDPSSFLSRQLPFLSNLRRVEDRATVYIFENQACSMPITDPCELRKLLHQ", "text": "FUNCTION: May play a role in fertility regulation. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MVNEQKRFALFLATSDSTFVKKAYGGYFNVFVSTFGEDGEQWDLFRVIDGEFPDDKDLDKYDGFVISGSLNDAFGDDDWIVKLCSLCQKLDDMKKKVLGICFGHQILSRIKGGKVGRASRGLDMGLRSITMVTDAVKPGGYFGSQIPKSLAIIKCHQDEVLELPESATLLAYSDKYNVEMCSYGNHLLGIQGHPEYNKEILFEIIDRVVNLKLMEQDFADKAKATMENAEPDRKQWQTLCKNFLKGRSEQV", "text": "FUNCTION: Involved in glucosinolate biosynthesis. Hydrolyzes the gamma- glutamyl peptide bond of several glutathione (GSH) conjugates to produce Cys-Gly conjugates related to glucosinolates. The gamma-Glu- Cys-Gly-GSH conjugates are the sulfur-donating molecule in glucosinolate biosynthesis. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the peptidase C26 family."}
+{"protein": "SCNCVCGVCCSCSP", "text": "FUNCTION: Has bacteriocidal activity against Gram-positive bacteria including multi-drug resistant strains such as S.aureus MS9610 and methicillin-resistant S.aureus, but is not active against most Gram- negative bacteria and fungi. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the thiocillin family."}
+{"protein": "MITINTYALQKRRTFAIISHPDAGKTTLTEKFLLNGKIIRTSGTIKARRSKKYAKSDWMEIEKKKGISITTSVIQIPYNRYLINILDTPGHQDFSEDTYRVLTAVDFCVMIVDAAKGVEERTRKLIHVARTHRTPIITFINKLDRNSLDPIEILDQLEIELKIKCSPIIWPISCGKAFKGIYHIYNNLVYFYSYKTSEGINDTNNFLLKTCCLNDVFLDKIIGLELAQEFREEVELVNSIYKAFNKRIFLESDLTPIFFGSALKNFGVNFLMQGILDWAPSPVFKKSNIRKVQPYEKNFSGFVFKIQANMDLRHRDRMAFIRIVSGKYRKRMKLYHVRIKKYIIQTEVFSFVAGDRFIIETAYPGDIIGFHSYNSIKIGDTFTEGEKLKFFGIPNFAPELFRLVSLVDPFHKKKLLKGLTQLSEEGAIQVFKPYENNELILGAIGSLQFDIVIERLKIEYNIFILVHKVNIFSIRWISSNSLDTLSTFKNQNKSCLALDINNHLVYLASSEINLRLVQSRYPDIIFNVTCEN", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily."}
+{"protein": "MSSHQQKQPCTVPPQLHQQQVKQPCQPPPQEPCAPKTKDPCHPVPEPCNPKGPEPCHPKAPEPCHPKAPEPCNPKVPEPCQPKVPEPCQPKVPEPCNPKVPEPCQPKAPEPCHPKAPEPCHPVVPEPCPSTVTPSPYQQKTKQK", "text": "FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. May participate widely in the construction of cell envelopes in cornifying epithelia characterized by either increased thickness or a requirement for extreme flexibility. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cornifin (SPRR) family."}
+{"protein": "MADQLTLEIISAINKLVKAENGERTSVALGEITTDTELTSLGIDSLGLADVLWDLEQLYGIKIEMNTADAWSNLNNIGDVVEAVRGLLTKEV", "text": "FUNCTION: Proposed to synthesize nod factor fatty acyl chain. Involved in trans-2,trans-4,trans-6,cis-11-octadecatetraenoic acid biosynthesis."}
+{"protein": "MDHEADAYRTDLMTITRYVLNEQSRNPEARGDLTILLSHIVLGCKFVASAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNEVFVKALVSSGRTCVLVSEEDEEATFVDPALRGKYCVCFDPLDGSSNIDCGVSIGTIFGIYMIKDKENVTLEDVLQPGKNMVAAGYCMYGSSCTLVLSTGNGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDEPTAKFVEKCKFPKDGSSPKSLRYIGSMVADVHRTLLYGGVFLYPADKKSPNGKLRVLYEVFPMSFLMEQAGGQSFTGKERALDLVPTKIHERSPIFLGSFEDVEEIKGLYAAQAK", "text": "FUNCTION: Catalyzes the first irreversible reaction from fructose-1,6- bisphosphate to fructose-6-phosphate and inorganic phosphate and plays an important regulatory role in sucrose biosynthesis and metabolism. Required for sucrose supply and tiller bud outgrowth. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family."}
+{"protein": "MEGPPGDLKHLFIEWLQEAAINATKKGTKAAILYNKALGSVRNYPLPINDPKTLKSVQFVGDKTCIHLSKKLEEYCKLNNFELPVAFGGLINGGVGEKRKHEVSDTSNLPDAKPKKQRKQKQYIPRKRSGGYAILLALYFGDKKKTGLTKEEIIQRATPYSDKSFKSNPSANEFYSAWSSIKSLQTHDLVDSSGRSSKSYFLTEEGYELAKQLKDAEGFESSPITNHIADLSFDNQVRVTPDSSYSKISQQLDSSPLMKTKNNKDRYGLGPSRLSSTRERILDLSSSPRLISSPLKPKDFVLRESLSSHNSTRPLQDRESISKAEDGINTKTKARLVHDASKRIYDGTNYDIWVPGEFEIILIIDNREIRSQRDRDFFQTRLTSLKVECDVRPLSVGDVVWTAKHKKTGREVILNYICERKRLDDLVSSIKDGRFQEQKNRLKKSGMKQFYYLVEDVVTSDMNKFGDMSDAIQTAMSMTMTISNFYLKRFKSIEDTIAFLASLTQVIKDQFAKNKTNLLVLKARSIKNQAEYSSLIAKFKEKFENRSTSYECAHLFSTFQDSMGKTGMMTVKETFILMLMGIRGVSLERAVAIQNRFKTPKNLIEFFFVENNHLSELDKKQLMMDVFKNEIGNKKIGKVLSEKIYDVWGCV", "text": "FUNCTION: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single- end invasion (SEI) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XPF family."}
+{"protein": "MSKLFRRVVTVLALTSMASSFASGKIEAAAAESLATRFIASAENSDDNISQRKAKKVRFGRNKYQKQEQKNNGPYCDKEFYPCQDGSCQSSVDTKQEPCYGKMYCVRVSDDSNVEISQAVPEYATVGSPYPIEILAVGKRDCVNVVITQQLPCEVEFISSDPATTPTSDSKLIWTIDRLGQGERCKITVWVKPLKEGCCFTAATVCACPELRSYTKCGQPAICIKQEGPECACLRCPVCYKIEVTNTGSAIARGVVVDNPVPDGYSHPSGQRVLSFNLGDMRPGDTKCFTVEFCPQKRGKITNVATVSYCGGHKCSANVTTVINEPCVQVNISGNDWSYVCKPVEYTIVVSNPGDLKLYDVVIEDLIPSGITILEAPGAEICCNKAVWCIKEMCPGETLQFKVVAKAQTPGKFTNQVSVKTNSDCGSCTSCAEVTTHWKGLAATHMCVIDTNDPICVGENTVYRICVTNRGSAEDTNVSLILKFSKELQPVSSSGPTKGTITGNTVVFDALPKLGSKESVEFSVTLKGVAPGDARGEAILSSDTLTVPVADTENTHVY", "text": "FUNCTION: In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the major outer membrane porin. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan. It is present but the disulfide bonds are reduced in reticulate bodies (RBs) (By similarity). SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MRLSVAAAISHGRVFRRMGLGPESRIHLLRNLLTGLVRHERIEAPWARVDEMRGYAEKLIDYGKLGDTNERAMRMADFWLTEKDLIPKLFQVLAPRYKDQTGGYTRMLQIPNRSLDRAKMAVIEYKGNCLPPLPLPRRDSHLTLLNQLLQGLRQDLRQSQEASNHSSHTAQTPGI", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
+{"protein": "MNFKYIVAVSFLIASAYARSEENEIQSLSQRDVLEEESLREIRGIGTKILGGVKTALKGALKELASTYVNGKRTAEEHEVMKRLETVMRDLDSLDYPEEASERETRGFNQEEIANLFTKKEKRILGPVLGLVSNALGGLLKNIG", "text": "FUNCTION: Maximin-H8 shows antimicrobial activity against bacteria and against the fungus C.albicans. Shows strong hemolytic activity (By similarity). FUNCTION: Maximin-2 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans, but not against A.flavus nor P.uticale. It has little hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
+{"protein": "MTRDEALPDSHSAQNFYENYEPKEILGRGVSSVVRRCIHKPTCQEYAVKIIDITGGGSFSSEEVQELREATLKEVDILQKVSGHPNIIQLKDTYETNTFFFLVFDLMKRGELFDYLTEKVTLTEKETRKIMRALLEVVCTLHKLNIVHRDLKPENILLDDNMNIKLTDFGFSCQLQPGEKLREVCGTPSYLAPEIIQCSMDEGHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMDGKYQFGSPEWDDYSDTVKDLVSRFLVVQPQDRCSAEEALAHPFFQEYVVEEVRHFSPRGKFKVICLTVLASVRIYYQYRRVKPVTREIVIRDPYALRPLRRLIDAYAFRIYGHWVKKGQQQNRAALFENTPKAVLLSLAEEEDF", "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": "MLSFVLLLCVALVNAYSDPGACSGTCWAHDPNVIRRVSDGTYFRFSTGGGVHISSASAITGPWTDLGYALPNGSIVTVGNASNLWAPDVHYVDGTYYMYYASSTLGSRDSTIGVATSTTLEADSWTDHGEIGVTSSSSTPYNAIDPNWITIGSTPYLQFGSYWQGLYQVEMTDSLSASSSTPTNLAYNASGNHAIEASYLYEYGGYYYLTFSSGKAQGYTTSLPAQGDEYRIVVCRSKTGTGNFVDKDGVSCLNSGGTTVLASHDYVYGPGGQGIINTTSHGIVVYYHYANKNIGLAVDDYQFGWNTLTWTDGWPVVA", "text": "FUNCTION: Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 43 family."}
+{"protein": "MTTAPFLFPSLSRLHSARASSFPKPPVGSGAGVAFPARPYGSSLRLRSSVMAATGVGGNGSPMAPEESTVSSRLGEVKRVTKETNVHVKINLDGTGVANSSTGIPFLDHMLDQLASHGLFDVYVKATGDTHIDDHHSNEDIALAIGTALLQALGDRKGINRFGHFTAPLDEAAVEVILDLSGRPHLSCGLSIPTERVGTYDTQLVEHFFQSLVNTSGMTLHIRQLAGNNSHHIIEATFKAFARALRQATEYDLRRQGTIPSSKGVLSRS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
+{"protein": "MMQDVSSSPVSPADDSLSNSEEEPDRQQPQSGKRGGRKRRSSRRSAGGGAGPGGAAGGGVGGGDEPGSPAQGKRGKKSAGCGGGGGSAGGGGGSSSGGGSPQSYEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDELDSKMASCSYVAHERLSYAFSVWRMEGAWSMSASH", "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": "MDTRSSLCPKTQAVVAVFWGPGCHLSTCIEMFNITTQALGSAHNGTFSEVNCPDTEWWSWLNAIQAPFLWVLFLLAALENIFVLSVFCLHKTNCTVAEIYLGNLAAADLILACGLPFWAITIANNFDWLFGEVLCRVVNTMIYMNLYSSICFLMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLVIWSCTLLLSSPMLVFRTMKDYREEGHNVTACVIVYPSRSWEVFTNMLLNLVGFLLPLSIITFCTVRIMQVLRNNEMKKFKEVQTEKKATVLVLAVLGLFVLCWFPFQISTFLDTLLRLGVLSGCWNERAVDIVTQISSYVAYSNSCLNPLVYVIVGKRFRKKSREVYQAICRKGGCMGESVQMENSMGTLRTSISVDRQIHKLQDWAGNKQ", "text": "FUNCTION: Receptor for bradykinin. It is 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. Bradykinin receptor subfamily. BDKRB2 sub-subfamily."}
+{"protein": "MALPSCLKTGALMSPATGFNFSGSLMKSDSGFAVPTKLQSTRKGDRERLRVQAIFSFPPAFLTRNGRAEKQKQLKQELLEAIEPLERGATASPDDQLRIDQLARKVEAVNPTKEPLKSDLVNGKWELIYTTSASILQAKKPRFLRSITNYQSINVDTLKVQNMETWPFYNSVTGDIKPLNSKKVAVKLQVFKILGFIPIKAPDSARGELEITYVDEELRLSRGDKGNLFILKMFDPTYRIPL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid Note=Located in thylakoid as a peripheral protein at the stromal side. SIMILARITY: Belongs to the PAP/fibrillin family."}
+{"protein": "MSEPGEEPVAAPAGPAPDPVLNELYGSERPAVELLPGVPLSPIVNSCWLPADAKAMLAESWIPVPPEDAGEEAGPPPPAFEAAAPEYNELVRRLAKTAPFRKWNELTIQAKQLEQEVAGLKGPDAEAKQAELENVKVQIADAEAAVAEVKQSFSDDPLSLTGWMQALTDLADGGMTTFEVSGQGWPYCSLRQLFGEMPSAAPPAGFFDGVERVLGTFKRRYEKERGPGSVQLMLKLAPNVFSDAWSTGGAPAAVAAVEAYVERARANVFGPDGGVTPEGVPEPLDLVQLVWWDFAAADPLPVLKALQRMATDQLQVDEDSGEVSVSEPKKIRGIGLVDFPADRLKAAIQAGVPITCVQVEHSVLVRSAQPVLDLCAKYGIKVLARGGTLGGLLSAKYLGAPPPDPVRGDADLDSVPGCLDAVNNVGGWARLQAALAVIKGIADKHGVKPETVALRWQIDAGCFPLVTTRWSSRVWRQFGYEGWSSFEVSGGRPGVDGPLFQVESFLDVEDVRALAGLAAVHLGPKAG", "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. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme Note=Radial spoke. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MKTEISTADSLRDPPSNGLKADSELVIREDIDQFLPSEVSSLGSDHQNDGEDSDTDSDNFLQDPEDDVDEESTGRGTVTTTSTSTESRGRPSSCIFVASLAAALSDDELCLSVTENFKKYGDLARVKVLRDNANRPYAFVQYNNDHDAKHALIRAQGTLLNGRRLRCEPAKVNRTLYLKNQQSIDFNEISQICEKFGGLEQIVPDRTDNQYTRRYTYPISSANSWFVQFVYRDDAIRAYANLRTDPNWIIEWAQNINVPKNYNLLHKSKFKSSKYHQNNGIINNDGSNNNDNNNSNNNNREDSRRNGDVIEEECGHVHGSDSEEKLTSDGIYDDEDKDSEITIDKRSIFVGQLDKETTREELNRRFSTHGKIQDINLIFKPTNIFAFIKYETEEAAAAALESENHAIFLNKTMHVQYKEVGGRHNRKFSGKNGGSNFNHHQFFSTRSGKTFTGPELNLAPPPINMYRKMSGGSQQESETMMPYMPMGPMPMGPPPPNAASLSDFDMFPPSYSTFMKGMMPLRRKSMPNSWSSPSSKSVNSENESVNGGDENSELPSEIPESSGRYNAANSFTTYNNSSAGNSNNNNNNNNSNSNKSQYKKRYARRSSYGYNEVPPKPYYFQPYYYHPMQYHMGPMGPLHPSQGSAGNHHPYMMVYPMSPPPPSGLDGSMIPPPINVSQSHAANHGSTHVHANEFISNDTGDINEDNKAYSLDY", "text": "FUNCTION: Positive regulator of sporulation-specific genes and of sporulation. Required for premeiotic DNA synthesis and meiotic chromosomal segregation. May act in a nutritional signaling pathway."}
+{"protein": "MGNLFGRKRRSRVTEQDKAVLQLKQQRDKLRQYQKRISLGLERERELARQLLKEGKKEKAMLLLKKKRYQEQLLDKTDNQISNLERMVQDIEFTQIEMKVIEGLKIGNECLNKMHQVMSIEEVERIIGETQDAVEYQRQIDEILAGSLTEEDEDAILEELNAITQEQLELPDVPSEPLPEEPPEATPVKNRPKPELVAAS", "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. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes (By similarity). SUBCELLULAR LOCATION: Endomembrane system; Lipid-anchor Late endosome membrane. SIMILARITY: Belongs to the SNF7 family."}
+{"protein": "MEAEEGHQRDRLCDYCDSSVALVYCKADSAKLCLACDKQVHVANQLFAKHFRSLLCDSCNESPSSLFCETERSVLCQNCDWQHHTASSSLHSRRPFEGFTGCPSVPELLAIVGLDDLTLDSGLLWESPEIVSLNDLIVSGGSGTHNFRATDVPPLPKNRHATCGKYKDEMIRQLRGLSRSEPGCLKFETPDAEIDAGFQFLAPDLFSTCELESGLKWFDQQDHEDFPYCSLLKNLSESDEKPENVDRESSVMVPVSGCLNRCEEETVMVPVITSTRSMTHEINSLERNSALSRYKEKKKSRRYEKHIRYESRKVRAESRTRIRGRFAKAADP", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CONSTANS family."}
+{"protein": "MAAAKDTHEDHDTSTENADESNHDPQFEPIVSLPEQEIKTLEEDEEELFKMRAKLFRFASENDLPEWKERGTGDVKLLKHKEKGTIRLLMRRDKTLKICANHYITPMMELKPNAGSDRAWVWNTHADFADECPKQELLAIRFLNAENAQKFKTKFEECRKEIEEKEKKGSGKNDSTEKVVEKLEALSVQEGEQPQDAAPAAVEEEQ", "text": "FUNCTION: Plays a role in RAN-dependent nucleocytoplasmic transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and mediates the dissociation of RAN from proteins involved in transport into the nucleus (By similarity). Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (By similarity). Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis via its effect on RAN. Does not increase the RAN GTPase activity by itself, but increases GTP hydrolysis mediated by RANGAP1. Inhibits RCC1-dependent exchange of RAN-bound GDP by GTP (By similarity). SIMILARITY: Belongs to the RANBP1 family."}
+{"protein": "MDIFFVISGFLITGIIITEIQQNSFSLKQFYTRRIKRIYPAFITVMALVSFIASAIFIYNDFNKLRKTIELAIAFLSNFYLGLTQGYFDLSANENPVLHIWSLAVEGQYYLIFPLILILAYKKFREVKVLFIITLILFFILLATSFVSANFYKEVLHQPNIYYLSNLRFPELLVGSLLAIYHNLSNKVQLSKQVNNILAILSTLLLFSCLFLMNNNIAFIPGITLILPCIFTALIIHTTSQNNIR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acyltransferase 3 family."}
+{"protein": "MDEGIPHLQERQLLEHRDFIGLDYSSLYMCKPKRSLKRDDTKDTYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALTALTEQQHQKIIALQNGERSLKSPVQADLDAFHSGFQTCAKEVLQYLARFESWTPREPRCAQLVSHLHAVATQLLTPQVTPGRGPGRAPCSAGAAAASGSERVARCVPVIQRTQPGTEPEHDTDTDSGYGGEAEQGRAAVKQEPPGDPSAAPKRLKLEARGALLGPEPALLGSLVALGGGAPFAQPAAAPFCLPFYLLSPSAAAYVQPWLDKSGLDKYLYPAAAAPFPLLYPGIPAAAAAAAAAAFPCLSSVLSPPPEKAGSAAGAPFLAHEVAPPGSLRPQHAHSRTHLPHAVNPESSQEDATQPAKDAP", "text": "FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA/B/G, NR1H3/LXRA, NR1H4 and VDR transactivation activity (By similarity). Inhibits HNF1A-mediated transactivation of CYP1A2, CYP2E1 and CYP3A11 (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MATFEEVSVLGFEEFDKAVKEHEGKTIFAYFSGSKDTEGKSWCPDCVEAEPVIREGLKHVTEDCVFIYCQVGDKPYWKDPNNDFRQKLKITAVPTLLKYGTPQKLVESECCQSSLVEMIFSED", "text": "FUNCTION: Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioredoxin family."}
+{"protein": "MPLLDSFAVDHTRMQAPAVRVAKTMNTPHGDAITVFDLRFCIPNKEVMPEKGIHTLEHLFAGFMRDHLNGNGVEIIDISPMGCRTGFYMSLIGTPDEQRVADAWKAAMADVLKVQDQNQIPELNVYQCGTYQMHSLSEAQDIARHILERDVRVNSNKELALPKEKLQELHI", "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) (By similarity). 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": "MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGADLLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVVSFVPPPLDQEEMES", "text": "FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 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. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF- kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc- N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression (By similarity). Phosphorylates S100A9 at 'Thr-113' (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
+{"protein": "MIGLRSISKNKQTINSISKSFYCTSSPSSSSVKLSVTRLIDGYRAHGHLAANIDPLARMERIRSQLLDLDRYNLVKGQSIPSTIDLINQDLTNLDQVVSFLENAYCNDVTAQFDHIESIEEKAWLYEKFEQLQHQNPSKSEKINILKNLIKSEIFDQFMQKKFPTFKRYGLEGNESMMVSCDSIFRESAKNQLKNVVIGMPHRGRLNLLVQMCNYPAKDFFWKVKGNSEFSEGILGVGDVTSHIAVSTDLQFNNNKESVHVSLIHNPSHLEAVDPVAAGKTRAKQFYEKNEGGSESLCLMLHGDAAVAGQGVVTETLQLSQLSGFNIGGCVHVIVNNQIGFTTVPTNGRSNRYSSDIGKFIGAPIIVVNSQSPEQVEKVSRLAVEYRQKFKKDIIIDLIGWRKFGHNEVDEPSFTQPTMYQNIRKRQSIPQKYATQIISQGIFSEQELLEFTQKEQAILEEQFQLSTPENFKYSPMDHLQGKWSGLIQSKHIADDSKLDTGYSVEELSEIANDSVKVPSDFQVHQRLLRSFSNARLEKLKQNQADWATAESMAVGSLMKQGYNVRISGQDVGRGTFSQRHFNLTEQNSDRIYQPLNNMGAKGELDVVNSNLSEFAVLCYEYGYSLESPDTLPIWEAQFGDFINGAQIAIDQFVTSGESKWLRQSGIVILLPHGFDGAGPEHSSCRIERFLQLSDTEAVNVKDDTLINQETNFYFINPSTPANYFHALRRQMIRNYRKPLIVAGPKVLLRHPNCFSTLNEMAPGTHFQTVLSDPDTINNASTIKRVIFCSGKVFYDLQEERKAKNFNDVAIIRLEQIAPFPYQRIQEEINRYSNATKFAWVQEEQQNGGCWSFVEPRFKQRYPQTSQIKYIGRPPLAASAIGISSIHKKEVSQLLIDAFNF", "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) (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family."}
+{"protein": "MPYGTRYPTLAFHTGGVGESDDGMPPQPFETFCYDSALLQAKIENFNIVPYTSVLPKELFGNILPVDQCTKFFKHGAVLEVIMAGRGATVTDGTQAIATGVGICWGKDKNGELIGGWAAEYVEFFPTWIDDEIAESHAKMWLKKSLQHELDLRSVSKHSEFQYFHNYINIRKKFGFCLTALGFLNFENAAPAVIQ", "text": "FUNCTION: Part of the AaxABC system, catalyzes the decarboxylation of L-arginine. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the pyruvoyl-dependent arginine decarboxylase family."}
+{"protein": "MSAPAATGVFILSLTAIPATYTFNFFFAFNSSWPVAAGGAGILLVIAILARLLVIQKPPKDPLFYVYAVFAFTSVIGLIIGLEQDGIIDGFMTHYLKESEPYLNTAYGHMICYWDGTAHYLMYLLMVVAIAWDQNYRTIGLYWVGSILMSTIVFIPGNIVGKYGTRVCSALLLNLPYLCLPLWAGFKIYKQPSVTPNYSSKEIQNIQHKSIYRRPSDLLLALYLILATLFCIFRGMIALDCPADPCRFYIQLQEPYIKDPSAYPRLQMLVLMFYCVPYNLILLYGLLVPECTWMPDLSLISAGGIAQAQFSHIGASLHARTPYIYRVPDEARIFFFTANILYGLGSQLLAHRCVNKPEFFLKAKSGAKDK", "text": "FUNCTION: May function as sterol isomerase. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TM6SF family."}
+{"protein": "MKKILQLIKQRSITRKLLVSFLSILIIPVVILAIFAYQSASSSLDRQMMGSALENVQQLNEIINTSIGEKENSADYFSEWLTKEKYNAKSNASIAEKFSQYISINKDVESIYTSDTKGHFTRYPDLPMPSGYNPVERDWYKKAVANKGKVVITDPYKTASTNTMVVTIAQQTKDGSGVIAINMTIENLLKTTKKVNIGTQGYAFIMTKDKKVVAHPNEQSGTELKGDWLDKMLSADKGDFQYTMDGDKKKMAFDTNKLTGWKIGGTMYLDEIHEAAQPVLHLALIVLAAAIIIGIIVMTLIIRSITTPLKQLVGSSKRISEGDLTETIDIRSKDELGELGKSFNNMASSLRSLIHAIQDSVDNVAASSEELTASAAQTSKATEHITLAIEQFSNGNEKQNENIETAAEHIYQMNDGLTNMAQASEVITDSSVQSTEIASEGGKLVHQTVGQMNVIDKSVKEAEQVVRGLETKSKDITNILRVINGIADQTNLLALNAAIEAARAGEYGRGFSVVAEEVRKLAVQSADSAKEIEGLIIEIVKEINTSLGMFQSVNQEVQTGLDITDKTEMSFKRISEMTNQIAGELQNMSATVQQLSASSEEVSGASEHIASISKESSAHIQDIAASAEEQLASMEEISSSAETLSSMAEELRDMTKRFKIE", "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. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyltransferase and removed by a methylesterase. McpA is required for taxis towards glucose and alpha-methylglucoside. 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. SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein family."}
+{"protein": "MTSKSLNVAFIHPDLGIGGAERLVVDAAVGIQKKGHQVIFYTSHHDPNHCFEETRDGTLKVQVRGDWLPRTIFGRFYILCAILRQFVLVASLILWERHSYDIFFVDQLSACVPLLKWFTTAKILFYCHFPDKLLTQRNSTIKKLYRAPVDKMEELTTGMSDLIAVNSGFTAGMFKKSFPSVHQTPQILYPPINFDAYDRPVDRNDPTVKILETDKRVLLSINRFERKKNVELALRAFAALKIKNMVPKDVFANYRLVLAGGYDKRVRENVEYLEELDQLATEEFGLQTFTIHPSSAAADVPADAQVVFLCSFNDAQRTFLLDQAKLLLYTPSNEHFGITPVEGMYASVPVIAVNTGGPVETVKNKETGLLLPSDPDVWAEGIRDFIIEKYNGKQMGQHGRQHVQSKFSLPAFADRLEAMMIELETSTPDQSSSGAVYLLGAIGVLFACIIYCIKQ", "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: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
+{"protein": "MNFLWEVENPTVTTMPLNVSFANRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSSSSDSLLSSESSPRATPEPLVLHEETPPTTSSDSEEEQDDEEEIDVVSVEKRQPPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQADEHKLISEKDLLRKRREQLKHKLEQLRNSGA", "text": "FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes (PubMed:17304222). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (By similarity). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus."}
+{"protein": "CISARYPCSNSKDCCSGNCGTFWTCFIRKDPCSKECLAP", "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": "MLAGQLEARDPKEGTHPEDPCPGAGAVTEKTAVAAEVLTEDCNAGEMPPLQQQVIRLHQELGRQKSLWADVHGKLRSHIDALREQNMELREKLRALQLQRWKARKKSAASPHAGQESHTLALEPAFGKMSPLSADEETIPKYIGRKNQSATLLGQFSSSKGDPLCLSSPMSLKIERISSWKTPPQEKRDKSLSRRRQDRRATPTGRPTPCAERRGGV", "text": "FUNCTION: May be involved in transcriptional regulation. Has in vitro transcription inhibition activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TCP10 family."}
+{"protein": "MLLIALNTDLRTTGKKFLPNDINGGKVEKVNGPCVLQIQKIRNISAPKDNEESQAAPRMLRLQLTDGHTSCTAIELNYLSKISLNTPPGTKIKLLGTIEVKNGYLLLDDTNTVVLGGEVEHLIEKWELQRSLSKHSRSNIGIEGGPPPFVPFGQRCASVASVDSKELDSRKTLQASSVTKPVGENDEFEKQRTAAIAEVAKSKETKTFGGGGNAGSNLNPGAGGSRNKEVFQKEKIIRAEGKSEGVYRELVDEKALRHITEMGFSKDAARQALMDHSNNVEAALNSLLTGNKSKPVQGPPARGKGKGRGRTRAEEDDELTSARPSAPSTLFDFLESKMGSFSIEDHKLQSQSQSQVHQKPLNLEQNGIKDYNHKDYNQPRQFTRNDTRAPRNEKPPRFQKEIQASRQYEGNGPPKSRGSEKQSSSVAEQWMEERNKCERGYPRNDRLKDFSHLPSSHQNEGSYKKSYTNPMQGRGMKGGNHTEVKEEFHHQNSNTEGSHQKRGKKDDQRYNSEFYTDRRARTGNTETFTNIPNEKCFSANNELSNFQTILIKDGANDLSNGEVDQKARRFGPIKPIGTNLNSSHEDKSKMFSYNNAKKRSGPIKQERPLEAVYSGFSWRPGDECLALYWEDNKYYRAEVEALHSSGTTAVVKFSDYGNYEEVLLENIRPIQAEAWEEEGDFGDFRRGGDGQPRRSTRPTQQFYQPPRARN", "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": "MNKPKKVAILTAGGLAPCLNSAIGSLIERYTEIDPSIEIICYRGGYKGLLLGDSYPVTAEVRKKAGVLQRFGGSVIGNSRVKLTNVKDCVKRGLVKEGEDPQKVAADQLVKDGVDILHTIGGDDTNTAAADLAAFLARNNYGLTVIGLPKTVDNDVFPIKQSLGAWTAAEQGARYFMNVVAENNANPRMLIVHEVMGRNCGWLTAATAQEYRKLLDRAEWLPELGLTRESYEVHAVFVPEMAIDLEAEAKRLREVMDKVDCVNIFVSEGAGVEAIVAEMQAKGQEVPRDAFGHIKLDAVNPGKWFGEQFAQMIGAEKTLVQKSGYFARASASNVDDMRLIKSCADLAVECAFRRESGVIGHDEDNGNVLRAIEFPRIKGGKPFNIDTDWFNSMLSEIGQPKGGKVEVSH", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'P' sub-subfamily."}
+{"protein": "MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASRESKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPVAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDMDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDIDLHNQASVPLEPRPLRRESEI", "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. Can be blocked by extracellular barium and cesium. 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": "MALVPPLGREFPPEPVNCPLAAPRELDVVGGTICPAPEEETSRPEQVQASLGLPEHCMGELKSTESATSPSRLPLASSHEHQDGGKPCEHSDSGLEVLEAEQDSLHLCLLRLNFRLQDLERGLGSWTLAHNRIVQMQALQAELRGAAERVDALLAFGEGLAERSEPRAWASLEQVLRALGTHRDTIFQRLWQLQAQLISYSLVLEKANLLDQDLEVEGDSDGPAAGGVWGPWAPSTFPTPAELEWDPAGDVGGLGPSGQKISRIPGAPCELCGYRGPQSSGQGLEDLLSLGLGHRKHLAAHHRRRLRKPQDRKRQVSPSLPDAMLEVDRGVPAPASKRPLTLFFLLLFLLLVGATLLLPLSGVSCCSHARLARTPYLVLSYVNGLPPI", "text": "FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology, by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus. SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass type IV membrane protein Note=Localization at the nucleus outer membrane location requires the presence of SUN1. SIMILARITY: Belongs to the nesprin family."}
+{"protein": "MVKANYIRAGRLVRILRGPRQNRVGVIVDIVDANRVLVENPCEQKMWRHVQNLKNVEPLKFCVSISRNCSTKALKEALESKKVLEKYAATKVRRPHRAKKAFAESTDFERYQLRVAKRSRAYWARKIFDENDKKNPVSWHKVALKKLLKNAKKVDSTPAAKKRVEKARAARKARLAAGKSKTKVAASKK", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL14 family."}
+{"protein": "MALPNKFLLWFYCFAWLCFPVSLGSQASGGDAQIAASAELESGATPWSLLQPIDERDRAGLLPPLFKVLSVGRGGAPRLQPDSRALHYMKNLYKTYATKEGIPKSNRSHLYNTVRLFTPCTQHKQVPGDQVTGILPSVDLLFNLDRITTVEHLLKSVLLYTINNSVSFSSAVKCVCNLMIKEPKFSSKTLHRALYSFTFNSQFEFGKKHKWIEIDVTSLLQPLVASNKRSIHMSINFTCMKDQLEHPSAQNGLFNMTLLVPPSLILYLNDTSAQAYHRWYSLYYKRRPSQGPDQERSLSAYPVGEDAAEDGRSSHHRHRRGQETVSSELKKPLVPASFNLSEYFKQFLFPQNECELHDFRLSFSQLKWDNWIVAPHRYNPRYCKGDCPRAVGHRYGSPVHTMVQNIIYEKLDSSVPRPSCVPAKYSPLSVLTIEPDGSIAYKEYEDMIATKCTCR", "text": "FUNCTION: Required for ovarian folliculogenesis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
+{"protein": "QVRFRQCYFNPISCF", "text": "FUNCTION: Strongly inhibits juvenile hormone biosynthesis in vitro by the corpora allata from fifth-stadium larvae and adult females. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the allatostatin family."}
+{"protein": "MMNMKIVLFSLLLFVIRWNIISCNKNDKNQGVDMNVLNNYENLFKFVKCEYCNEHTYVKGKKAPSDPQCADIKEECKELLKEKQYTDSVTYLMDGFKSANNSANNGKKNNAEEMKNLVNFLQSHKKLIKALKKNIESIQNKKHLIYKNKSYNPLLLSCVKKMNMLKENVDYIQKNQNLFKELMNQKATYSFVNTKKKIISLKSQGHKKETSQNQNENNDNQKYQEVNDEDDVNDEEDTNDDEDTNDEEDTNDDEDTNDDEDTNDEEDTNDEEDHENNNATAYELGIVPVNDVLNVNMKNMITGNNFMDVVKNTLAQSGGLGSNDLINFLNQGKEIGENLLNITKMNLGDKNNLESFPLDELNMLKDNLINYEFILDNLKTSVLNKLKDLLLRLLYKAYVSYKKRKAQEKGLPEPTVTNEEYVEELKKGILDMGIKLLFSKVKSLLKKLKNKIFPKKKEDNQAVDTKSMEEPKVKAQPALRGVEPTEDSNIMNSINNVMDEIDFFEKELIENNNTPNVVPPTQSKKKNKNETVSGMDENFDNHPENYFKEEYYYDENDDMEVKVKKIGVTLKKFEPLKNGNVSETIKLIHLGNKDKKHIEAINNDIQIIKQELQAIYNELMNYTNGNKNIQQIFQQNILENDVLNQETEEEMEKQVEAITKQIEAEVDALAPKNKEEEEKEKEKEEKEKEEKEKEKEEKEKEEKEKEEKEKEEKEEEKKEKEEEQEEEEEEEIVPENLTTEESK", "text": "FUNCTION: During the asexual blood stage, involved in the sialic acid- independent (SAID) merozoite invasion of host erythrocytes by binding to host SLC4A1/Band 3 protein on the surface of the host erythrocyte. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side Parasitophorous vacuole lumen Secreted Note=Localizes to the merozoite surface at the time of schizont rupture. SIMILARITY: Belongs to the plasmodium ABRA family."}
+{"protein": "MASRAAPVRQTCCCFNIRVATIALAIYHIVMSVLLFIEHVVEVARGKVSCRFFKMPYLRMADLLSSFLLIGVLFIISISLLFGVVKNREKYLIPFLSLQIMDFLLCLLTLLGSYIELPAYLKLARPRPGPSKVPLMTLQLLDFCLSILTLCSSYMEVPTYLNFKSMNHMNYLPSQEGVPHSQFINMMLIFSVAFITVLILKVYMFKCVYTCYKFLKHMNSAMEDSSSKMFLKVALPSYEEALSLPPKTPEGDPAPPPYSEV", "text": "FUNCTION: May have a special functional role during embryogenesis and in adult hematopoietic cells. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LAPTM4/LAPTM5 transporter family."}
+{"protein": "MFKYVGEMLDRGLLLAIAFFVVYRAVLFCCARQRQQRQQLPSTADLQLDAM", "text": "FUNCTION: Minor virion component that plays an essential role in virus infectivity. SUBCELLULAR LOCATION: Virion Host cell membrane. SIMILARITY: Belongs to the arteriviridae ORF5a protein family."}
+{"protein": "MSAFEIEHLASCITAHAWNADRSRVALCPNNNEVHIYAKQGTSWVVEHVLAEHDQLVTSIDWAPKTNRILTSSQDRNAYVWTFKDGQWKPVLVLLRINRAATHVKWSPQENKFAVATGAKLVCICFFEEEHDWWASNHIKKHKSTVLKVDWHPNNLLLATSSSDYKVRVFDAYIKKADGRSVTRPYGEVAFGEPVFEFDQCASWVHALKWSPSGSTLAYSSHDGVFAVANFSTNPPTIEKLRVRNLPLRDLLYITENSIAGVGYDCAPLLITNQNGWKYSGEMDKASEGGAAAGSETSARKLFQNKVDLGESKSADKKLTTVHQNCITSIVPFKSVGGVVSDFSTSGLDGNIVVWHVKALEAKNKFKVI", "text": "FUNCTION: Functions 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. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium. SIMILARITY: Belongs to the WD repeat ARPC1 family."}
+{"protein": "MAVEEIASRKDISLRDMQISAILKMLFLNKDLNNNDNITTITDDIFNQQEIIWKVLILDIKSTATISSVLRVNDLLKAGITVHSLIKQDRSPLPDVPAIYFVSPTKENIDIIVNDLKSDKYSEFYINFTSSLPRNLLEDLAQQVSITGKSDKIKQVYDQYLDFIVTEPELFSLEISNAYLTLNDPKTTEEEITGLCANIADGLFNTVLTINSIPIIRAAKGGPAEIIAEKLGTKLRDFVINTNSSSTSTLQGNDSLERGVLIILDRNIDFASMFSHSWIYQCMVFDIFKLSRNTVTIPLESKENGTDNTTAKPLATKKYDIEPNDFFWMENSHLPFPEAAENVEAALNTYKEEAAEITRKTGVTNISDLDPNSNNDTVQIQEVVKKLPELTAKKNTIDTHMNIFAALLSQLESKSLDTFFEVEQDPGSTKTRSRFLDILKDGKTNNLEDKLRSFIVLYLTSTTGLPKDFVQNVENYFKENDYDINALKYVYKLREFMQLSNMSLQNKSLEDGSDSAFKPSNLTLSGIYGLTEGKLQGGVGSLISGIKKLLPEKKTIPITNVVDAIMDPLNSSQKNLETTDSYLYIDPKITRGSHTRKPKRQSYNKSLVFVVGGGNYLEYQNLQEWAHSQLHNPKKVMYGSTAITTPAEFLNEISRLGASNSSNNDA", "text": "FUNCTION: Able to suppress the functional loss of YPT1. SLY1 is essential for cell viability. May interact indirectly, or directly with YPT1. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family."}
+{"protein": "MFDPKYLESGEFYQRRYRNFPTLIIVPIFLLVVFIVLFSLFAKREIVVKASGEIIPAKVLSDIQSTSNNAIDSNQLAENKMVKKGDTLVTFTSGNEKISSQLLTQQINNLNNRIQSLDTYKHSIIDGRSEFGGTDQFGYDNLFNGYMAQVDTLTSEFNQQNSDKQTADQQANHQIDVLKQGQSKNNQQLANYQAILTSINSNTKPTNNPYQSIYDNYAAQLKSAQTTDDKEQVKQTALSSVQQQIDQLQTTSSSYDSQIAGITKSGPLSQSSTLDKIADLKQQQLASAQKEINDQQQSLDELKAKQSSANEDYQDTVIKAPESGILHLTSDKATIKYFPKGTTVTQIYPMLNKRTKLSVEYYVPTSNSVGLKRGQNIRFVANQNVTKPLILTGTIKTISSAPIIIKEESFYKCIASINVNVREHEQIKYGLAGKVTTTKGTKTWFNYYKDILLGNTN", "text": "FUNCTION: Involved in the secretion of mesentericin Y105. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family."}
+{"protein": "MAATKEAKQPKEPKKRTTRRKKDPNAPKRGLSAYMFFANENRDIVRSENPDVTFGQVGRILGERWKALTAEEKQPYESKAQADKKRYESEKELYNATRA", "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. Also augments the fidelity of transcription by RNA polymerase III independently of any role in the FACT complex. Required for transcriptional initiation fidelity of some but not all tRNA genes. Seems to be functionally redundant with NHP6A. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the NHP6 family."}
+{"protein": "MNQESSFRAPPKRRVRGPNPNISTPHQLFDDTSGGPVPHGGEYPNHSSPALGIPAQAFLSEPMSNFAMAYGSSLASQGKEMMDKNIDRIIPVSKIKYYFAVDTVYVGKKIGLLMFPYMHQDWEVRYQQDTPVAPRFDINAPDLYIPVMAFITYILVAGLALGTQSRFSPEILGMQASSALAWLIVEVLAILLSLYLVTVNTDLTTVDLVAFSGYKYVGMISGVISGLLFGKTGYYVVLSWCGISVVFFMIRTLRLKILSEAAAEGVLVRGARNQLRMYLTMAIAAVQPIFMYWLTYHLVR", "text": "FUNCTION: Functions in endoplasmic reticulum to Golgi vesicle-mediated transport and regulates the proper organization of the endoplasmic reticulum and the Golgi (By similarity). Plays a key role in targeting to neuronal dendrites receptors such as HTR1A (By similarity). Plays also a role in primary cilium and sperm flagellum assembly probably through protein transport to these compartments (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Note=Shuttles between the endoplasmic reticulum, the intermediate compartment and the Golgi apparatus. SIMILARITY: Belongs to the YIF1 family."}
+{"protein": "MSKDTHDDELPSYEDVIKEEERLQSQPPRPPRPAANLAQGHQSRPHQRPSTMPATSSSQTYAHSHSYTPTSSQPRPPPRPQQNPSLPWTYPPRFYCSKCGNTGYKLKNGRSCKSCWRRFAPQNNVVSAPTYYTNYTMPVYTNAWQGNRPLYVQPGDPRLGGVLCGECRGSGRTRFLLDEDICPLCHGVGRIITQPQRY", "text": "FUNCTION: May be involved in assembly and disassembly of the actin cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HUA1 family."}
+{"protein": "MAPTKKKTSRKPKNRCVKNEKLASFIKDFDSQVKIITEELKASVVNILKEVDSQYNIEIIKLPMAIREMCWLDYIAKGGSQKALEAAATVKVDMEEITSTVTKTPFKLDKKVKKGKCKSDETLEPNPLQSVIRTKTKAKVAAKKPSTARKTRASTANLTNTSKRTSKRGRATPSASKQIETSLLGYTPAATPRIDTSIFKTPALRTPCLQEPVYTFSANGSPLAGMDELFINVPAGDGKNIRLLASEVDSLDINRLDNQAFENIKLLSSQLQRFCKKLK", "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. Contributes to CPC function by facilitating loading of the CPC onto chromosomes (By similarity). SUBCELLULAR LOCATION: 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 borealin family."}
+{"protein": "MTLDHQILNQSFKRSHPPTPSSELLVQHGHPSPESDTGLTGNPLTRLLTLGKEDDNTEWHVSGSILDVYSGEQEISPVNMGLTSASCPSSLPMKREITETDTRALAKERQKKDNHNLIERRRRYNINYRIKELGTLIPKSNDPDMRWNKGTILKASVEYIKWLQKEQQRAQELEHRQKKLEQANRRLLLRIQELEIQARAHGLPTLASLVTVDLGAHITKQTHLEQNSGDYCQQLVLSQGTSPELCDQAMAFSDPLSHFTDLSFSAALKEEQRLDNMLLDDTVSPFGTDPLLSAISPAVSKESSRRSSFSSEDGDEL", "text": "FUNCTION: Transcriptional regulator that acts as a repressor or an activator. Acts as a transcriptional repressor on minimal promoter containing element F (that includes an E-box sequence). Binds to element F in an E-box sequence-specific manner. Acts as a transcriptional transactivator on the proximal promoter region of the tartrate-resistant acid phosphatase (TRAP) E-box containing promoter. Collaborates with MITF in target gene activation. Acts as a transcriptional repressor on minimal promoter containing mu E3 enhancer sequence. Binds to mu E3 DNA sequence of the immunoglobulin heavy-chain gene enhancer. Binds DNA in a homo- or heterodimeric form (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MiT/TFE family."}
+{"protein": "MASSSIASFAPFESYSPPLNTSETSLISVQLTQDGLDYHGALAFLCGALLFGFVYSVFYNLYLSPIARVPGPLIAQVSPLWLMRAVCRKQLNCDIKKLHEKYGKKPERSPVVRLSPTEVSFATVEAQNAIHRPGASAKQGLFFTKEGTLEAMMGEIIWPATNLLTATVPEEHQRLKKALQPAFTEKALQLQEPIQQQHTDRLIRSVQEASRQNRVVDLTPHMSQAIWDIISDLSFGEPLLKDQLAKFERLKTTFCMVSPLLEALQVLLAVPGAQTLAKACVGLVPLLFWLPTNVLPSAQLRKRFERQDSNEDFLTAIMRCREMGIQMTDMELQSNASLLVMVGYDTTATSLSATMNLLLRHPLCLQALQDELHSHFSSTSDMTSKPLSQLPILNGCIQESLRLFPPANGKGTNRTSPGTMIDGVYIPRGVNVSADMYTIQRSPTYWSRPNEFCPDRWFDNGPGTEFAQDVRSSHNPFLLGPRMCIGRAVALQSMRMLIAKLVYTFDLEAVEDYSWDLHVANSYLWTGYRCNARV", "text": "FUNCTION: Cytochrome P4590 monooxygenase part of the gene cluster that mediates the biosynthesis of betaestacins (Ref.3). The bifunctional terpene synthase btcA converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene betaestacin I (Ref.3). The C-terminal prenyltransferase (PT) domain of btcA catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into betaestacin I (Ref.3). The cytochrome P450 monooxygenase btcB oxidizes the C25 methyl group of betaestacin I to yield the carboxylic acid betaestacin IV via the alcohol betaestacin III (Ref.3). The cytochrome P450 monooxygenase btcC further catalyzes the multistep oxidation of betaestacin IV to produce several compounds, including betaestacins Va, Vb, Vc and VI (Ref.3). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "YADAIFTNSYRKILGQLSARKLLQDIMNRQQGERNQEQGAKVRL", "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": "MAMVPRVLVVDDDPVIRELLQAYLGEEGYDVLCAGNAEQAEACLAECAHLGQPVELVLLDIRLPGKDGLTLTRELRVRSEVGIILITGRNDEIDRIVGLECGADDYVIKPLNPRELVSRAKNLIRRVRHAQASAGPARQALRQFGDWLLDADRRRLIDHAGNETLLTHGEFQLLGAFLRNSGHTLSRDQLMDQIRNREWLPSDRSIDVLVGRLRRKLRDDPAEPQLIITIHGAGYLFTAAASDA", "text": "FUNCTION: Member of the two-component regulatory system AruS/AruR, which is involved in the regulation of the arginine transaminase (ATA) pathway in response to exogeneous L-arginine. Regulates transcription of aruH and aruI. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MAKNVGILAMDIYFPPTCVQQEALEAHDGASKGKYTIGLGQDCLAFCTELEDVISMSFNAVTSLFEKYKIDPNQIGRLEVGSETVIDKSKSIKTFLMQLFEKCGNTDVEGVDSTNACYGGTAALLNCVNWVESNSWDGRYGLVICTDSAVYAEGPARPTGGAAAIAMLIGPDAPIVFESKLRASHMAHVYDFYKPNLASEYPVVDGKLSQTCYLMALDSCYKHLCNKFEKIEGKEFSINDADYIVFHSPYNKLVQKSFARLLYNDFLRNASSIDEAAKEKFTPYSSLTLDESYQSRDLEKVSQQIAKPFYDAKVQPTTLIPKEVGNMYTASLYAAFASLIHKKHNDLAGKRVVMFSYGSGSTATMFSLRLNDNKPPFSISNIASVMDVGGKLKARHEYAPEKFVETMKLMEHRYGAKDFVTTKEGIIDLLAPGTYYLKEVDSLYRRFYGKKGEDGSVANGH", "text": "FUNCTION: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase. Devoided of acetoacetyl-CoA thiolase (AACT) activity. Required for the development of both tapetosomes and elaioplasts in tapetal cells and for pollen viability during pollen tube elongation. SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase family."}
+{"protein": "MALSKAFGQKPVKFQLEDGGDFYMIGSEVGNYLRMFRGSLYKRYPSLWRKLASVEERKKIVESSHDHGYTQLATSVTLLKASEVEEILDGNDEKYKAVSISTEPPAYLREQKAKRNSQWVPTLPNSSHHLDAVPCSTTINRSRLGRDKKRTFPLCFDDHDPAVIHENASQSEVLVPIRLDMEIEGQKLRDAFTWNMNEKLMTPEMFAEILCDDLDLNPLAFVPAIPSAIRQQIESYPTDAILEEQTDQRVIIKLNIHVGNISLVDQFEWDMSEKENSPEKFALKLCSELGQGGEFVTTIAYSIRGQLSWHQKAYAFSENPLPTVEIAIRNTGAADQWCPLLETLTDAEMEKKIRDQDRNTRRIRRLANTAPGW", "text": "FUNCTION: Involved in chromatin-remodeling. Core component of the BAF (SWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex) and may play a role in neural development (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNF5 family."}
+{"protein": "GLVDVLGKVGGLIKKLLP", "text": "FUNCTION: Has activity against Gram-positive bacteria and S.cerevisiae. Has non-hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ponericin-G family."}
+{"protein": "MQTNKQPKQQFSEKQFIAFVFNYIAGFGFISVVMTMFDVGPFSYLVLGLTSFAILGVVLSFSRLSVLCGNSAYGGSYLIAKKAVGTNSKTKRFFVFLSGWNVSLTGSFNGVVIPAVLIFSFADIPVVKANNNIIIGLLVGGFLLFGLLTFISLFGLKINKKAIFYFAVIKWIVVIGGFILGIYLIGTTNGKGFVENNLIGTRENIDFFKIIFISLALTIAFAGTEDLASITPDVKSNNLRKCFLIAFGCVVLLYLVGFVIISGLDGIRGYGLALGNKDPKAINNYGSIYRLVGGVPLLVIYGLGLLVNSLASRLSMTITTARKYVALAQDGFLPSFLAKTNKHNEYHHAVLISNLMTLLVMLIMVIIPFLPDHNNNNNSLFNAIEQLVTVTIEMAAAISLIQYFITFIFFFMIFAKKENQKLIPLWEKVSYVISFALVSVLLFVPLFPFNQWTVFNTFKIVVLICFYLLGVGFFGYAEWKNKNKYQLMNNNS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.genitalium MG225."}
+{"protein": "MVMAAVIHKKGGPDNFVWEEVKVGSPGPGQVRLRNTAIGVNFLDTYHRAGIPHPLVVGEPPIVVGFEAAAVVEEVGPGVTDFTVGERVCTCLPPLGAYSQERLYPAEKLIKVPKDLDLDDVHLAGLMLKGMTAQYLLHQTHKVKPGDYVLIHAAAGGMGHIMVPWARHLGATVIGTVSTEEKAETARKLGCHHTINYSTQDFAEVVREITGGKGVDVVYDSIGKDTLQKSLDCLRPRGMCAAYGHASGVADPIRVVEDLGVRGSLFITRPALWHYMSNRSEIDEGSKCLFDAVKAGVLHSSVAKTFPLREAAAAHKYMGGRQTIGSIVLLPQA", "text": "FUNCTION: Involved in the degradation of unsaturated organohalogen compounds. Catalyzes the NADPH-dependent reduction of the carbon-carbon double bond of 2-chloroacrylate to produce (S)-2-chloropropionate, which is probably further metabolized to (R)-lactate by (S)-2-haloacid dehalogenase. Can also use 2-bromoacrylate as substrate. Does not act on acrylate, methacrylate, 1,4-benzoquinone and 1,4-naphthoquinone. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "MWIQVRTMDGKETHTVNSLSRLTKVQELRKKIEEVFHVEPQLQRLFYRGKQMEDGHTLFDYDVRLNDTIQLLVRQSLALPLSTKERDSELSDSDSGYGVGHSESDKSSTHGEGAAEADDKTVWEDTDLGLYKVNEYVDVRDNIFGAWFEAQVVQVQKRALSEDEPCSSSAVKTSEDDIMYHVKYDDYPEHGVDIVKAKNVRARARTVIPWENLEVGQVVMANYNVDYPRKRGFWYDVEICRKRQTRTARELYGNIRLLNDSQLNNCRIMFVDEVLMIELPKERRPLIASPSQPPPALRNTGKSGPSCRFCKDDENKPCRKCACHVCGGREAPEKQLLCDECDMAFHLYCLKPPLTSVPPEPEWYCPSCRTDSSEVVQAGEKLKESKKKAKMASATSSSRRDWGKGMACVGRTTECTIVPANHFGPIPGVPVGTMWRFRVQVSESGVHRPHVAGIHGRSNDGAYSLVLAGGYEDDVDNGNYFTYTGSGGRDLSGNKRTAGQSSDQKLTNNNRALALNCHSPINEKGAEAEDWRQGKPVRVVRNMKGGKHSKYAPAEGNRYDGIYKVVKYWPERGKSGFLVWRYLLRRDDTEPEPWTREGKDRTRQLGLTMQYPEGYLEALANKEKSRKRPAKALEQGPSSSKTGKSKQKSTGPTLSSPRASKKSKLEPYTLSEQQANLIKEDKGNAKLWDDVLTSLQDGPYQIFLSKVKEAFQCICCQELVFRPVTTVCQHNVCKDCLDRSFRAQVFSCPACRFELDHSSPTRVNQPLQTILNQLFPGYGSGR", "text": "FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. Plays a role in DNA repair by cooperating with UHRF1 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation (). SUBCELLULAR LOCATION: Nucleus Note=Associated, through the YDG domain (also called SRA domain), with replicating DNA from early to late S phase, including at replicating pericentric heterochromatin (PubMed:36056023). Also localizes to euchromatic regions. In non-S- phase cells, homogenously distributed through the nucleus (PubMed:36056023)."}
+{"protein": "METTVGTLGENTTNTFTDFFSARDGSGAETSPLPFTFSYGDYDMPSDEEEDVTNSRTFFAAKIVIGMALVGIMLVCGIGNFIFITALARYKKLRNLTNLLIANLAISDFLVAIVCCPFEMDYYVVRQLSWEHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLRPRMKCQTAAGLIFLVWSVSILIAIPAAYFTTETVLVIVESQEKIFCGQIWPVDQQFYYRSYFLLVFGLEFVGPVIAMTLCYARVSRELWFKAVPGFQTEQIRRRLRCRRRTVLGLVCVLSAYVLCWAPFYGFTIVRDFFPSVFVKEKHYLTAFYVVECIAMSNSMINTLCFVTVRNNTSKYLKRILRLQWRASPSGSKASADLDLRTTGIPATEEVDCIRLK", "text": "FUNCTION: Receptor for prokineticin 1. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase. May play a role during early pregnancy (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MEPVLNLNNEVVKLRKDVKKVKVLIIRKLTRHIAKLKSKKGTEELILKNQRRAQRLLEEIHSVKELKPDDVTKTALRKEISFEKVCKKPNSTAEERALARLATHPLLKQKITAIKEAIKAFKDARKTAAEGEREREKDEPEQVTKIKETKKPVQAKLNKNTEEIKSAKEHVKEEKCKNLLEDSDKGTEKALELPYVQENLPEQTAENKEQPKAQDVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPVVESPAVERPPVESPPKKKACLEQELGCELSDIEDSDKEKEYFDDSTEERFYKHSSSFEDSDSGSDNDFFIGKIRRTKKKKSDKDGSKQKEEKVPPTKEKAQTSEVQKEIPTAKSMKLKSVFCKSLSQTKPKPSFTKRETNFRQERNKRPVMPQASPLAKKPLQSKATSVRQPGRKLEAQPLHPSWEASRKRKEQQAQITKFQGKKIVFDD", "text": "FUNCTION: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region."}
+{"protein": "MNHLRAEGPASVLAIGTANPENILIQDEFPDYYFRVTKSEHMTQLKEKFRKICDKSMIRKRNIFLNEEHLKQNPKLVEHDVQTLDARQDMLVVEVPKLGKDACAKAIKEWGQPKSKITHLIFTSASTTDMPGADYHCAKLLGLSPSVKRVMMYQLGCYGGGTVLRIAKDIAENNKGARVLAVCCDIMACLFRGPSDSDLELLVGQAIFGDGAAAVIVGAEPDESVGERPIFELVSTGQTILPNSEGTIGGHIREAGLIFDLHKDVPMLISNNIEKCLIEAFTPIGISDWNSIFWITHPGGKAILDKVEEKLHLKSDKFVDSRHVLSEHGNMSSSTVLFVMDELRKRSLEEGKSTTGDGFEWGVLFGFGPGLTVERVVVRSVPIKY", "text": "FUNCTION: Polyketide synthase responsible for the biosynthesis of secondary metabolites. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family."}
+{"protein": "MESILFIAIAFLINSFISYKITNMQPKIKSRIFKRVKMHYLNLIEGKKAEFDKKAMPILFGFMIIALISFNILLYVVYNCPVSITSIIAEILIIISMIIIWKAFNKEISVYLCDDGIYYSNKFISWKNIENVKKDDGFIVLFGKKKKILGRKLYLLQRIYLKYDEEIENIIKNQIEKFRDKA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.jannaschii MJ0803."}
+{"protein": "MKTLALMSLFVLTSLNALAAPKTVTLEVPTMNCVTCPFTVEKALQKVDGVSKAEVTFKTKLAVVTFDDEKSTVKALTEATTNAGYPSTLKE", "text": "FUNCTION: Involved in mercury resistance. Acts as a mercury scavenger that specifically binds to a mercuric ion in the periplasm and probably passes it to the cytoplasmic mercuric reductase MerA via the mercuric transport protein MerT. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the MerP family."}
+{"protein": "MMITKQSYQRFALMRVFVFSLSAFIFNTTEFVPVALLSDIAKSFEMESATVGLMITAYAWVVSLGSLPLMLLSAKIERKRLLLFLFALFIFSHILSALAWNFWVLLLSRMGIAFAHSIFWSITASLVIRVAPRNKKQQALGLLALGSSLAMILGLPLGRIIGQILDWRSTFGVIGGVATLIMLLMWKLLPHLPSRNAGTLASVPILMKRPLLVGIYLLVIMVISGHFTTYSYIEPFIIQISQFSPDITTLMLFVFGLAGVVGSFLFGRLYAKNSRKFIAFAMVLVICPQLLLFVFKNLEWVIFLQIFLWGIGITSLTIALQMRVLQLAPDATDVASAIFSGSYNVGIGSGALFGSIVIHQLGLEYIGFVGGALGLLALFWLRFITIKFKKT", "text": "FUNCTION: Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. SotB (TC 2.A.1.2) family."}
+{"protein": "MERILEKVRAKSEIPVYDKSIENVLSAILTTNDFWKIVDLSEEPLPLVADIIRILEEEGLVKISNGIEFTEKGNEFIKSYGIGAKDNSVCECCEGRGVSLKNYQDLLERFKEIVKNRPMPKHEYDQGFVTPECTISRIALMNSRGDLFNKDVLVLGDDDLTSIALMLSNLPKKIVVVDIDDRLINFIKEVAEQLNYKNIEVITLDLRKPLPEKYSRAFDTFITDPPETVYAVKTFIGRGISALKGERRAGYFGITRRESSLDKWREIQRTLINDFNVVITDIIRNFNHYVNWGYEEETRAWKLAPVKKKPEDIWYKSYMFRIETLKDSRGFEEEVDVGDELYNDAESSTT", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the branched-chain polyamine synthase family."}
+{"protein": "MLISGSSAALCALALPFAAAKSLWSDSPGNYSSFITTAFPLGNGRLGAMPIGSYDKEIVNLNVDSLWRGGPFESPTYSGGNPNVSKAGALPGIREWIFQNGTGNVSALLGEYPYYGSYQVLANLTIDMGELSDIDGYRRNLDLDSAVYSDHFSTGETYIEREAFCSYPDNVCVYRLSSNSSLPEITFGLENQLTSPAPNVSCHGNSISLYGQTYPVIGMIYNARVTVVVPGSSNTTDLCSSSTVKVPEGEKEVFLVFAADTNYEASNGNSKASFSFKGENPYMKVLQTATNAAKKSYSALKSSHVKDYQGVFNKFTLTLPDPNGSADRPTTELLSSYSQPGDPYVENLLFDYGRYLFISSSRPGSLPPNLQGLWTESYSPAWSGDYHANINLQMNHWAVDQTGLGELTEPLWTYMAETWMPRGAETAELLYGTSEGWVTHDEMNTFGHTAMKDVAQWADYPATNAWMSHHVWDHFDYSQDSAWYRETGYPILKGAAQFWLSQLVKDEYFKDGTLVVNPCNSPEHGPTLTPQTFGCTHYQQLIWELFDHVLQGWTASGDDDTSFKNAITSKFSTLDPGIHIGSWGQIQEWKLDIDVKNDTHRHLSNLYGWYPGYIISSVHGSNKTITDAVETTLYSRGTGVEDSNTGWAKVWRSACWALLNVTDEAYSELSLAIQDNFAENGFDMYSGSPPFQIDANFGLVGAMVQMLIRDSDRSSADASAGKTQDVLLGPAIPAAWGGGSVGGLRLRGGGVVSFSWNDSGVVDSCKADLSARGSDVSQVKFYVAGGRAIDCSS", "text": "FUNCTION: Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 95 family."}
+{"protein": "MAELWTSIGAAPAEKQEQPPKPRDVILVKSPALLSSTSSSDLHPLKKIRTDDKCLKPKRVNGEGGGGNSKGGPGHSSSVTWSFPQGASSSSSSLCLGNPGKTEKPTKPREKRDKEKKRRREGGGEENGEVKTAGIPCLPAASPVTAVRNEIKIKDKEKQKEKKKHKLMNEIKKENGEVKLLQKGTNEKPRPNAEDLQIKKVKKKKKKKHKEGEKRKHPKMHSKSIQTICSGLVSDAENNQFKEAKVEKDVYFMGLLGKTEVKKVKVEKEIPFVSLKEPRVEHKLKCLDSLEFKHLIHIEHQPNGGASLIHAYSSELSQLSPVEMERFSEEFVTLVFSENENCAAFYVMGIVHGAATYLPDFLDYFSFNFPNSPVKMEILGKKDIETTTISNFHAQVKRTYSHGTYRAGAMRQISLVGAVDEEVGDYFPEFLDMLETSPFLKRTLPWGTCSSLQLKSRKESDDGPIMWVRPGEQMIPVADMPKSPFKRKRTTNEIKNLQYLPRASEPREMLFEDRTRAHADHIGQGFERETTAAVGVLKAVHCVEWNENPRITKDVICFHAEDFLEVVQRLQLDLHEPPLSQCVQWVDDAKLNQLRREGIRYARIQLYDDDIYFIPRNVVHQFKTVSAVCSLAWHIRLKMYHPESAATQNSDNLEETESGKETKADIERRDKTLYSSSTYTCNVQFKDPKQKPPQIKHEQTYPLQTSEECGNINLPTISPAPTECHTFETKTDYTTDTPVKNEMESTLELINQDFADRHVTPKDTRQHILTNSVIRTEEENMC", "text": "FUNCTION: Lysine-specific demethylase that specifically demethylates methylated lysine residues of proteins. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the round spermatid basic protein 1 family."}
+{"protein": "MRTLLVFLLLTILVAVLIGNNQVEACTNNADCHGLGHCYRGTCFPVMG", "text": "FUNCTION: Leech salivary gland peptide with unknown function. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the annelide toxin family."}
+{"protein": "MFQSILFLAFYGRPVFGSAAARDYACVNTAESRDCWKDGFNIETDYYGKEEAPEGKLVEYELTLSQQIISPDGYEMLGMVVNGQYPGPTIEADWGDTLRITVKNNFTENYNGTAVHWHGIRQKETNWLDGVPGVTQCPITPGDSQVYEFRVTQYGTSWYHSHYSLQYSNGAYGPIVIHGPSSANWDVDLGPWLLSDWYHDDAFALDHVGITTNRAAIPKSSLINGKGYYECDPTNDAKCTGTRDYYEVVLKQGTKYKFGIINTSTILTYTFWIDGHNFTIIAIDFVPIEPLTVDTLNVGIGQRYEIIIETNPDFDDDSSFWMHAQYCFINQTDIVDDKVGIVRYESAGSSDPPYINKSDYHLNFGCADPKPESLVPILKQQVGAQANPLAAEDYFRVGLGNFTWPDATNSTGSVFLWFLQKLPLYVNWSEPSVKKLTIDETADFPPNSRPIELDYETGQWVYFVIESDWDPAGAVDQYGQEIRVEPSVHPFHLHGHDFLILAQGLGKFTSDIQPNLDNPPRRDTVDVEPLGYVWIAFQIDNPGAWLFHCHIAFHSSDGIAIQFLEQPSKLKPIMEEAGVLGDFADRCNKWDDWYQAVNIPHNATQADSGV", "text": "FUNCTION: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702). The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA (PubMed:24302702). As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta- lactamase domain (PubMed:24302702). The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702). Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC (PubMed:24302702). Spontaneous decarboxylation of endocrocin occurs to generate emodin (PubMed:24302702). An O-methyltransferase (ptaH or ptaI) could methylate emodin to form physcion (PubMed:24302702). PtaJ could then catalyze the oxidative cleavage of physcion, and rotation of the intermediate could then afford desmethylisosulochrin (PubMed:24302702). PtaF, a putative NADH-dependent oxidoreductase, might also participate in the oxidative cleavage step (PubMed:24302702). Desmethylisosulochrin is then transformed by another O-methyltransferase (ptaH or ptaI) to form isosulochrin (PubMed:24302702). Chlorination of isosulochrin by ptaM in the cyclohexadienone B ring then produces chloroisosulochrin (PubMed:24302702). PtaE is responsible for the oxidative coupling reactions of both benzophenones isosulouchrin and chloroisosulochrin to RES-1214-1 and pestheic acid respectively, regardless of chlorination. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "MSRILVEDDNATPFHSMEIISSSLTLGQLLKNVSDVRKVEVGDETPVHEFFDRDGSSLDGDNDHLMRPVPFVLSFNNLTYNVSVRRKLDFHDLVPWRRTSFSKTKTLLDNISGETRDGEILAVLGASGSGKSTLIDALANRIAKGSLKGTVTLNGEALQSRMLKVISAYVMQDDLLFPMLTVEETLMFAAEFRLPRSLPKSKKKLRVQALIDQLGIRNAAKTIIGDEGHRGISGGERRRVSIGIDIIHDPIVLFLDEPTSGLDSTSAFMVVKVLKRIAESGSIIIMSIHQPSHRVLSLLDRLIFLSRGHTVFSGSPASLPSFFAGFGNPIPENENQTEFALDLIRELEGSAGGTRGLVEFNKKWQEMKKQSNPQTLTPPASPNPNLTLKEAISASISRGKLVSGGGGGSSVINHGGGTLAVPAFANPFWIEIKTLTRRSILNSRRQPELLGMRLATVIVTGFILATVFWRLDNSPKGVQERLGFFAFAMSTMFYTCADALPVFLQERYIFMRETAYNAYRRSSYVLSHAIVTFPSLIFLSLAFAVTTFWAVGLEGGLMGFLFYCLIILASFWSGSSFVTFLSGVVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPQYWIWFHYLSLVKYPYEAVLQNEFSDPTECFVRGVQLFDNSPLGELTYGMKLRLLDSVSRSIGMRISSSTCLTTGADVLKQQGVTQLSKWNCLLITVGFGFLFRILFYLCLLLGSKNKRR", "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": "MITLAPSLDTPKTDQNQVSDPQTSHVFKSKLPDIPISNHLPLHSYCFQNLSQFAHRPCLIVGPASKTFTYADTHLISSKIAAGLSNLGILKGDVVMILLQNSADFVFSFLAISMIGAVATTANPFYTAPEIFKQFTVSKAKLIITQAMYVDKLRNHDGAKLGEDFKVVTVDDPPENCLHFSVLSEANESDVPEVEIHPDDAVAMPFSSGTTGLPKGVILTHKSLTTSVAQQVDGENPNLYLTTEDVLLCVLPLFHIFSLNSVLLCALRAGSAVLLMQKFEIGTLLELIQRHRVSVAMVVPPLVLALAKNPMVADFDLSSIRLVLSGAAPLGKELEEALRNRMPQAVLGQGYGMTEAGPVLSMCLGFAKQPFQTKSGSCGTVVRNAELKVVDPETGRSLGYNQPGEICIRGQQIMKGYLNDEAATASTIDSEGWLHTGDVGYVDDDDEIFIVDRVKELIKYKGFQVPPAELEGLLVSHPSIADAAVVPQKDVAAGEVPVAFVVRSNGFDLTEEAVKEFIAKQVVFYKRLHKVYFVHAIPKSPSGKILRKDLRAKLETAATQTP", "text": "FUNCTION: Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MSDLEPSESLNHESDSHLEQLKPSTTPSIPARPQSRPQKQTTTTTTKVPTDQDSNDKTPLEKPQDELDQLAHEIEKVLTDPVIPPRPQHGSSAKPNETQTEHKEQDFGSAHPVIPSRPTNKKETIETEMVDQNNGLESKSDSTANKESLENQVPIDEDSTHVKPSIPNVPSRPQNRDLDSSEVDNTKASTTPSIPARPQRQTAPTQNEHKPQVSNTPVIPTRPQTKTEKLHLNEELDKLDGESSSKNQENKRHTDDNNTSKPIYEAESIVPPEEKEGETANKQALPTTSTDPPAEPTASTRGFRLPLHMQQSSGPISTSTPVTGSEAELNSLDNSNTFGDGEITPGNSDTKATFKSDEDVENNNRTDSSSFDDDMETISQDQEDREEDRRHRQETTTGENVQESEDPQFETTIIESGEIEERDGDDTDSGELYSEQQQNKEKEDVVPATSTPKIPQRPPKKQSLSRATTDDSLTSLDNTSKPPKPVVPKRPTSEESSSNLEPTIPTRPSIKKAPSIGESDPEPIVPNRPGNKELESIPRDTQTSIKSKPPPPKPKKLSSKIAAFQQQLFNPMNASSEEDVGSTGSKQPEPGIRKRSTENSILSRFGGKAIPLPGMFNPNQMPKPSISHGEETSDDKEEKEEKEENVTANVPVRRTRGPRGKKLPKAVADAEIKTESRFTIESGKLWSLEFKREIKEEKEIGHSDLEKSKILVDDVEADGDGEEKAAENEVIESQENTIGDKLEHNDVVNIASAAADIDNDGDVDDDDDDDVPPEVNERFIKDEEISNVGIERTIASETTTEKHSTDEEVEEEEEELEVDSVDIPIRRVTVNTVDTIEDQKDVDDEPL", "text": "FUNCTION: Involved in mitochondrial migration along actin filaments. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch Note=Cortical actin patches. SIMILARITY: Belongs to the AIM21 family."}
+{"protein": "MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGGLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIYTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL", "text": "FUNCTION: Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
+{"protein": "MGTHDMSPNASHSYIYRVLSDILEFPDNEQRMWWHSVAPMFAEMLRACGYDIHEQYKILGIWKKAVIPFLGCYPTNDGPRWLSILTRYGTPFELSLNCSHRLVRYTFEPINAATGTDKDPFNTQAIWESLSQLRRLNGDVDTELFNHFKANLTVDNAESAHLVESNLAGSKIRTQNKLALDLQNGSFVVKAYFYPTLKSAATGRSITDLMLSSVRQQVQKWSPTLAQPLSVLEEYIEARGPDSTASPRLLSCDLINPERARTKIYLLERQVSIEAMEDLWTLGGRRKSDSALAALDIIREIWSLIQLPPCLASYPSGYLPLGTVPDEQLPLMVNYTLRPDDPMPEPQVYFTTFGQNDLHVTNALTAFFERQGWTELAESYKENLRAYYPHADQETANYIHAYVSFSYRKGVSYMSVYLQTLETGDWPITYSPKRQYLCNEHPIHLKELAKACA", "text": "FUNCTION: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of communesins, a prominent class of indole alkaloids with great potential as pharmaceuticals (PubMed:25571861). Communesins are biosynthesized by the coupling of tryptamine and aurantioclavine, two building blocks derived from L- tryptophan (PubMed:25571861). The L-tryptophan decarboxylase cnsB converts L-tryptophan to tryptamine, whereas the tryptophan dimethylallyltransferase cnsF converts L-tryptophan to 4-dimethylallyl tryptophan which is further transformed to aurantioclavine by the aurantioclavine synthase cnsA, probably aided by the catalase cnsD (PubMed:25571861). The cytochrome P450 monooxygenase cnsC catalyzes the heterodimeric coupling between the two different indole moieties, tryptamine and aurantioclavine, to construct vicinal quaternary stereocenters and yield the heptacyclic communesin scaffold (PubMed:26963294). The O-methyltransferase cnsE then methylates the communesin scaffold to produce communesin K, the simplest characterized communesin that contains the heptacyclic core (PubMed:25571861). The dioxygenase cnsJ converts communesin K into communesin I (PubMed:25571861). Acylation to introduce the hexadienyl group at position N16 of communesin I by the acyltransferase cnsK leads to the production of communesin B. The hexadienyl group is produced by the highly reducing polyketide synthase cnsI, before being hydrolytically removed from cnsI by the serine hydrolase cnsH, converted into hexadienyl-CoA by the CoA ligase cnsG, and then transferred to communesin I by cnsK (PubMed:25571861). Surprisingly, cnsK may also be a promiscuous acyltransferase that can tolerate a range of acyl groups, including acetyl-, propionyl-, and butyryl-CoA, which lead to communesins A, G and H respectively (PubMed:25571861). The roles of the alpha-ketoglutarate-dependent dioxygenases cnsM and cnsP have still to be determined (PubMed:25571861). SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family."}
+{"protein": "MNALIDNPEALASGYLAMAQVFSYPDAGAWSRLTERGLVDPALTHETLEAEYLAAFEMGGGKATVSLYEGQNRPDLGRDGILQELLRFYEFFDAQLSEDDREYPDHLVTELEFLAWLCLQEHAAVRDGRDAEPFRRAARDFLDRHLAAWLPEFRRRLEATDSAYAQYGPALGELVEAHRSRLGEQAPQLGELQ", "text": "FUNCTION: May function as a system-specific chaperone protein essential for the assembly of an active selenate reductase SerABC. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type II DMSO reductase enzyme chaperone family."}
+{"protein": "MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTSMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYEKESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG", "text": "FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). 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": "MRLQPLFVSLALAAPCALLPTASLSAAPAAAARQADTAPVLVTAAQWQQMASEGRRYPWFAKEQARTEATLKKMMKAGIDVPVPRDKGGGRTHEQHKRNYQALLAAGTLYRLTGDRAYVDYARDMLLQYAQLYPTLGPHPEGRGQIPGRVFWQVLNDSVWLVNAIQGYDAIRDALSAEDRNTIESKVFRPMAEFLVSEPKNYDQIHNHATWAVAATGMTGYVLRDQELVEKSLRGSQKDDKFGFLRQIDLLFSPDGYYEEGPYYQRYALAPFLLFANAIERNEPQRKIFARRDGVLLKAVDVLVQSSYGGLFFPINDAILDKGIDTEELVAGIGIAYARTGDDRLLSVAEQQKRLLLSPEGLQVAQALAANKAKPFDYHPMLLRDGPDGDRGGLAILRMNGERGQALVQKDTMQGMGHGHFDKLNWLFYDNGNPVVTDYGAARFLNVEAKRGGIYLAENRSWAKQTVAHNTLVVDEQSHFNGNWKRGEAHAPQVRFFQADADTQIASATMRDAYPGVAFTRTQALLRHPDLGLPVVLDLLQVHGDKAARYDLPLHFNGHIVTTGFEAEHFPSQRPVLGKDNGYQHLWLDARSKPGSEPRSLAWLLDGRFYTYRFGSSAPAQALLVESGANDPEFNLRREPALLQRVDGQKDVTFFSVLEPHGEYNGTAEYVHGADSRIREIVRTRGSDAEVIELRLASGARIALGVADNSATTSEHSVTVDGHVYRWNGSHARLDRSKGDGK", "text": "FUNCTION: Polysaccharide lyase that catalyzes the depolymerization of alginate via a beta-elimination mechanism, cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues. Acts specifically on alginate and each of its block structures, with highest activity toward poly-beta-D-mannuronate (poly-ManA). Shows an exolytic mode of action, producing unsaturated monomers. Displays a very low activity against poly-beta-D-glucuronate (poly-GlcA), and is not active on poly- alpha-D-galacturonate, hyaluronan, heparin, heparan sulfate and chondroitin sulfate. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the polysaccharide lyase 17 family."}
+{"protein": "MEDNFASVVESLSGTSASALPLLTVSPADTSLKAPETKVQETKTEEKKPPKKRKSWGQELPIPKTNLPPRKRAKTEDEKEQRRIERVLRNRAAAQTSRERKRLEMEKLENEKIQMEQQNQFLLQRLSQMEAENNRLSQQLAQLTAEVRNSRNSTPKPGSPATASPTLTPTLFKQEGDELPLERIPFPTPSITDYSPTLKPSSLAESSDVTQHPAVSVGGLEGPGSALPLFDLGSGVEHDAANDIAAPLSDDDFHRLFNGDSSTEPDSSVIEDGFSFDILDSGDLSAFPFDSMVNFDSEPVALEGIEPAHGLPNETPYQTSGLQPSLGASTSRCDGQGIAAGC", "text": "FUNCTION: Master transcriptional regulator of the unfolded protein response (UPR) that recognizes and binds to the UPR element (UPRE) in the promoter of UPR-regulated genes (PubMed:19132084, PubMed:22028661, PubMed:21217201). In the canonical UPR pathway, the ireA RNase splices the cytoplasmic mRNA hacA, which alters the reading frame to allow translation of the bZIP transcription factor hacA (PubMed:19132084, PubMed:33087521). Induces the expression of pmrA, scrA and spfA in response to UPR (PubMed:32487759, PubMed:34663092). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
+{"protein": "MGASVLPLGLGAGDCQSSSGRRMSACLPRTALSFLLSLLLATPGARAAGYETCPMVQPGMLNVHLVAHTHDDVGWLKTVDQYYWGIHNDLQQAGVQYILDSVISALLAEPTRRFVYVEMAFFSRWWHQQTNETQEVVRRLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGSDGRPRVAWHIDPFGHSREQASLFAQMGFDGVFFGRIDYQDKLVRKKRREMELVWRASASLKAPAADLFTGVLPNNYGPPEGLCWDVLCADPPVVDDPRSPEYNAKKLVSYFLQLATAQGRYYRTNHTVMTMGSDFQYENANTWFKNLDKLIQLVNMQQANGSRVHVLYSTPACYLWELNKANLTWPVKEDDFFPYADGPHMFWTGYFSSRPALKRYERLSYNFLQVCNQLEAQVGPAANVGPYGHGDSSPLNQAMAVLQHHDAVSGTSKQHVADDYARQLAAGWGPCEVLLSNALAKLSGSKETFLFCRDLNISICPFSQTSERFQVLVYNPLGRKVDRMVRLPVRKGLFLIKDPGNNTVPSTVVELTSSGNPELLFPALVPALGFSVYSVTRVSDQNPQTRSQHSRPQKYSSPVLSIKNEYLRASFHPDTGLLSMIEVLDRKLTLPVNQAFFWYNASVGDKRSSQASGAYIFRPSQQWPFPVSHLARTRLVKTALVQEVHQNFTAWCSQVVRLYSGQRHLELEWTVGPIPVGDKWGKEIISRFDTPLETGGVFFTDSNGREVLERRRDYRPSWKLNQTEPVAGNYYPVNSRIYITDGKMQLTVLTDRSQGGSSMSDGSLELMVHRRLLKDDGRGVGEALQEPGSGGWVRGRHLLLLDTAREAAAEHRLLAEKELLAPQLVLAPGQGPSYHHDHHEAVPRKQFSGLRRQLPPSVRLLTLARWGPDTLLLRLEHQFALGEDSSRNLSLPVTLDLQDLFSTFTITRLQETTLAANQLRASASRLKWTTEIDPISRPAVPRLDPSSITLQPMEIRTFVASVQWEENS", "text": "FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the glycosyl hydrolase 38 family."}
+{"protein": "MLNDAKQTRANPGTSRPHSNGGGSSHGNELPRRTEQRAQGPRQPARLPKQGKTNGKSDGNITAGETQRGGIPRGKGPRGGKTNTRRTPPKAGAQPQPSNNRK", "text": "FUNCTION: Not known. Encoded on a subgenomic RNA (RNA3) synthesized during replication and which is co-terminal with RNA1."}
+{"protein": "MTWQSDYSRDYEVKNHMECQNRSDKYIWSPHDAYFYKGLSELIVDIDRLIYLSLEKIRKDFVFINLNTDSLSEFINRDNEWLSAVKGKQVVLIAARKSEALANYWYYNSNIRGVVYAGLSRDIRKELAYVINGRFLRKDIKKDKITDREMEIIRMTAQGMQPKSIARIENCSVKTVYTHRRNAEAKLYSKIYKLVQ", "text": "FUNCTION: Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP plays a dual role in early-stage biofilm development and host cell recognition. Positively regulates the expression of the ecp operon (By similarity). 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. Positively regulates the expression of the ecp operon (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EcpR/MatA family."}
+{"protein": "MKTEVTENIFEQAWDGFKGTNWRDKASVTRFVQENYKPYDGDESFLAGPTERTLKVKKIIEDTKNHYEEVGFPFDTDRVTSIDKIPAGYIDANDKELELIYGMQNSELFRLNFMPRGGLRVAEKILTEHGLSVDPGLHDVLSQTMTSVNDGIFRAYTSAIRKARHAHTVTGLPDAYSRGRIIGVYARLALYGADYLMKEKAKEWDAITEINDDNIRLKEEINMQYQALQEVVNFGALYGLDVSRPAMNVKEAIQWVNIAYMAVCRVINGAATSLGRVPIVLDIFAERDLARGTFTEQEIQEFVDDFILKLRTMKFARAAAYDELYSGDPTFITTSMAGMGNDGRHRVTKMDYRFLNTLDTIGNAPEPNLTVLWDSKLPYSFKRYSMSMSHKHSSIQYEGVETMAKDGYGEMSCISCCVSPLDPENEEGRHNLQYFGARVNVLKAMLTGLNGGYDDVHKDYKVFDIEPVRDEILDYDTVMENFDKSLNWLTDTYVDAMNIIHYMTDKYNYEAVQMAFLPTKVRANMGFGICGFANTVDSLSAIKYAKVKTLRDENGYIYDYEVEGDFPRYGEDDDRADDIAKLVMKMYHEKLASHKLYKNAEATVSLLTITSNVAYSKQTGNSPVHKGVFLNEDGTVNKSKLEFFSPGANPSNKAKGGWLQNLRSLAKLEFKDANDGISLTTQVSPRALGKTRDEQVDNLVQILDGYFTPGALINGTEFAGQHVNLNVMDLKDVYDKIMRGEDVIVRISGYCVNTKYLTPEQKQELTERVFHEVLSNDDEEVMHTSNI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily."}
+{"protein": "MALVAGIGQLDAVVQGGHSATPRPATGPAGPAAHSGRHQYDPDAWWARATGDSREAGGLGRTLAAASVAGQQQRHGALLESAVTVVRPALLWNDTRRPGAAADLIQELGGADKWAEAVGIVPVASLTLTNSGWLARHEPANAAKVAAICLPHDWLTWKLSGS", "text": "FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5- phosphate. SIMILARITY: Belongs to the FGGY kinase family."}
+{"protein": "MHRVPRLTTPWANRDLQRAWEKTYQDHRKKVQNAQPLVDTHPPQIYSHLCLKFKKLKMEEERLSIIDRNNYLLLQRVASAMKTRGQTDGRNNFTQRRS", "text": "SIMILARITY: Belongs to the CFAP97 family."}
+{"protein": "GIGSAILSAGKSALKGLAKGLAEHFAN", "text": "FUNCTION: Has antimicrobial activity, but no hemolytic activity. Preference on killing Gram-negative non-enteric bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
+{"protein": "MSYTPMSDLGQQGLFDITRTLLQQPDLASLSEALSQLVKRSALADSAGIVLWQAQSQRAQYYATRENGRPVEYEDETVLAHGPVRRILSRPDALHCNFHEFTETWPQLAASGLYPEFGHYCLLPLAAEGRIFGGCEFIRQEDRPWSEKEYDRLHTFTQIVGVVAEQIQNRVNNNVDYDLLCRERDNFRILVAITNAVLSRLDIDELVSEVAKEIHHYFNIDAISIVLRSHRKNKLNIYSTHYLDEHHPAHEQSEVDEAGTLTERVFKSKEMLLINLNERDPLAPYERMLFDTWGNQIQTLCLLPLMSGKTMLGVLKLAQCEEKVFTTANLKLLRQIAERVAIAVDNALAYQEIHRLKERLVDENLALTEQLNNVDSEFGEIIGRSEAMYNVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRSGRRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKLIQTDVRLIAATNRDLKKMVADREFRNDLYYRLNVFPIQLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSSMEWPGNVRELENVVERAVLLTRGNVLQLSLPDITAVTPDTSPVATESAKEGEDEYQLIIRVLKETNGVVAGPKGAAQRLGLKRTTLLSRMKRLGIDKDALA", "text": "FUNCTION: Required for induction of expression of the formate dehydrogenase H and hydrogenase-3 structural genes."}
+{"protein": "MTSRLARLWQPGNPQRRVFLPDFWMAVVESPSVGRNRLPRNCVKFEVDPRMSRHDIREYLTKIYDLPVRDVRTEVQMGDITWNSKLDHQYKKAMWKDEDKKIAYVFMSKGFEFSYPQMFEALEEDLELVKAMKQQEELKDKLNERYANRNRRVGQFLGA", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL23 family."}
+{"protein": "MDWQPDEQGLQQVLQLLKDSQSPNTATQRIVQDKLKQLNQFPDFNNYLIFVLTRLKSEDEPTRSLSGLILKNNVKAHYQSFPPPVADFIKQECLNNIGDASSLIRATIGILITTIASKGELQMWPELLPQLCNLLNSEDYNTCEGAFGALQKICEDSSELLDSDALNRPLNIMIPKFLQFFKHCSPKIRSHAIACVNQFIMDRAQALMDNIDTFIEHLFALAVDDDPEVRKNVCRALVMLLEVRIDRLIPHMHSIIQYMLQRTQDHDENVALEACEFWLTLAEQPICKEVLASHLVQLIPILVNGMKYSEIDIILLKGDVEEDEAVPDSEQDIKPRFHKSRTVTLPHEAERPDGSEDAEDDDDDDALSDWNLRKCSAAALDVLANVFREELLPHLLPLLKGLLFHPEWVVKESGILVLGAIAEGCMQGMVPYLPELIPHLIQCLSDKKALVRSIACWTLSRYAHWVVSQPPDMHLKPLMTELLKRILDGNKRVQEAACSAFATLEEEACTELVPYLSYILDTLVFAFGKYQHKNLLILYDAIGTLADSVGHHLNQPEYIQKLMPPLIQKWNELKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVTLVQKTLAQAMMYTQHPEQYEAPDKDFMIVALDLLSGLAEGLGGHVEQLVARSNIMTLLFQCMQDSMPEVRQSSFALLGDLTKACFIHVKPCIAEFMPILGTNLNPEFISVCNNATWAIGEICMQMGAEMQPYVQMVLNNLVEIINRPNTPKTLLENTGRLTSPSAIPAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICMMIGVNPGGVVQDFIFFCDAVASWVSPKDDLRDMFYKILHGFKDQVGEDNWQQFSEQFPPLLKERLAAFYGV", "text": "FUNCTION: Probably functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the importin beta family. Importin beta-2 subfamily."}
+{"protein": "MSGKPVLHYANTRGRMESVRWLLAAAGVEFEEKFLEKKEDLQKLKSDGSLLFQQVPMVEIDGMKMVQTRAILNYIAGKYNLYGKDLKERALIDMYVEGLADLYELIMMNVVQPADKKEEHLANALDKAANRYFPVFEKVLKDHGHDFLVGNKLSRADVHLLETILAVEESKPDALAKFPLLQSFKARTSNIPNIKKFLQPGSQRKPRLEEKDIPRLMAIFH", "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. SIMILARITY: Belongs to the GST superfamily. Alpha family."}
+{"protein": "MAPLALVGVTLLLAAPPCSGAATPTPSLPPPPANDSDTSTGGCQGSYRCQPGVLLPVWEPDDPSLGDKAARAVVYFVAMVYMFLGVSIIADRFMAAIEVITSKEKEITITKANGETSVGTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFQAGELGPGTIVGSAAFNMFVVIAVCIYVIPAGESRKIKHLRVFFVTASWSIFAYVWLYLILAVFSPGVVQVWEALLTLVFFPVCVVFAWMADKRLLFYKYVYKRYRTDPRSGIIIGAEGDPPKSIELDGTFVGAEAPGELGGLGPGPAEARELDASRREVIQILKDLKQKHPDKDLEQLVGIANYYALLHQQKSRAFYRIQATRLMTGAGNVLRRHAADASRRAAPAEGAGEDEDDGASRIFFEPSLYHCLENCGSVLLSVTCQGGEGNSTFYVDYRTEDGSAKAGSDYEYSEGTLVFKPGETQKELRIGIIDDDIFEEDEHFFVRLLNLRVGDAQGMFEPDGGGRPKGRLVAPLLATVTILDDDHAGIFSFQDRLLHVSECMGTVDVRVVRSSGARGTVRLPYRTVDGTARGGGVHYEDACGELEFGDDETMKTLQVKIVDDEEYEKKDNFFIELGQPQWLKRGISALLLNQGDGDRKLTAEEEEARRIAEMGKPVLGENCRLEVIIEESYDFKNTVDKLIKKTNLALVIGTHSWREQFLEAITVSAGDEEEEEDGSREERLPSCFDYVMHFLTVFWKVLFACVPPTEYCHGWACFGVSILVIGLLTALIGDLASHFGCTVGLKDSVNAVVFVALGTSIPDTFASKVAALQDQCADASIGNVTGSNAVNVFLGLGVAWSVAAVYWAVQGRPFEVRTGTLAFSVTLFTVFAFVGIAVLLYRRRPHIGGELGGPRGPKLATTALFLGLWLLYILFASLEAYCHIRGF", "text": "FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells. Contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory. Plays a role in regulating urinary Ca(2+) and Na(+) excretion. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Perikaryon Cell projection, dendrite Cell projection, dendritic spine. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC8 subfamily."}
+{"protein": "MNALLNHMNTEQSEAVKTTEGPLLIMAGAGSGKTRVLTHRIAYLLDEKDVSPYNVLAITFTNKAAREMKERVQKLVGDQAEVIWMSTFHSMCVRILRRDADRIGIERNFTIIDPTDQKSVIKDVLKNENIDSKKFEPRMFIGAISNLKNELKTPADAQKEATDYHSQMVATVYSGYQRQLSRNEALDFDDLIMTTINLFERVPEVLEYYQNKFQYIHVDEYQDTNKAQYTLVKLLASKFKNLCVVGDSDQSIYGWRGADIQNILSFEKDYPEANTIFLEQNYRSTKTILNAANEVIKNNSERKPKGLWTANTNGEKIHYYEAMTERDEAEFVIREIMKHQRNGKKYQDMAILYRTNAQSRVLEETFMKSNMPYTMVGGQKFYDRKEIKDLLSYLRIIANSNDDISLQRIINVPKRGVGPSSVEKVQNYALQNNISMFDALGEADFIGLSKKVTQECLNFYELIQSLIKEQEFLEIHEIVDEVLQKSGYREMLERENTLESRSRLENIDEFMSVPKDYEENTPLEEQSLINFLTDLSLVADIDEADTENGVTLMTMHSAKGLEFPIVFIMGMEESLFPHIRAIKSEGDHEMQEERRICYVAITRAEEVLYITHATSRMLFGRPQSNMPSRFLKEIPESLLENHSSGKRQTIQPKAKPFAKRGFSQRTTSTKKQVSSSDWNVGDKVMHKAWGEGMVSNVNEKNGSIELDIIFKSQGPKRLLAQFAPIEKKED", "text": "FUNCTION: Essential helicase. SIMILARITY: Belongs to the helicase family. UvrD subfamily."}
+{"protein": "MQKYALHAYPVMALMVATLTGCAWIPAKPLVQGATTAQPIPGPVPVANGSIFQSAQPINYGYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTSFGFDTVPRYLQGLFGNSRADMEASGGNSFNGKGGANASNTFSGTLTVTVDQVLANGNLHVVGEKQIAINQGTEFIRFSGVVNPRTISGSNSVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM", "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. 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": "MKLLLLALPILVLLPQVIPAYGGEKKCWNRSGHCRKQCKDGEAVKETCKNHRACCVPSNEDHRRVPTTSPTPLSDSTPGIIDNILTIRFTTDYFEISSKKDMVEESEAGQGTQTSPPNVHHTS", "text": "FUNCTION: Host defense peptide that exhibits antimicrobial activity against both Gram-negative bacteria, such as E.coli and S.typhimurium, and Gram-positive bacteria, such as S.aureus and B.subtilis (By similarity). Inhibits cell adhesion of E.coli on intestinal epithelial enterocytes (By similarity). Causes rapid permeabilization of both the outer and inner membrane of E.coli, leading to morphological alterations on the bacterial surface (By similarity). Binds to bacterial lipopolysaccharides (LPS) with high affinity, and may thereby be involved in immunoregulation through LPS neutralization (By similarity). May contribute to epididymal innate immunity and protect the sperm against attack by microorganisms (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "MYRLPADQKLKCTEFMSITEATEAKAIQYLKDASWRTDAAVDNFYSNPSNFANKFDKKAIETIFNKYKDSGEEQISEKLPEFVKDININDEMMELAVLWKFKTKQMGVITKNEFMETMERLRCDNISSLEKQMETVRQQLSSKDLNNNSAFKEFYMFVFDLGKAENQKNVSLQMCIELWTIVLKSKFDNLQIWFDFLNKHHKLAISKDTWNLFLDFVKIANDSITKYDSEGAWPVLIDEFVEYYKENCK", "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": "MSTTNKIYFIAGGNRGIGLSLVKELSNREGTVVFASARKPEAATELQEWSKSHSNVHIIKLDISSLESANEAAQEVAKAVGKVDVLWVNSGIFHSFNTVLNTPDDVWNSHYKTNVLGPIHVYQAFYPLVKKGESKIIVFTSSLVGSMGAFFPFNQSGYGQSKAALNFTMKEISFELQDEGFIVISIHPGMVRTDSAQEAVNQHAEAKPEILDIFAKQALAPDQSASDMLKVVDNLKPENNGFFFNYDGTTIPY", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MSTGAQTKAAAASQHADGPRLLADVGGTNARFALETGPGEITQIRVYPGAEYPTLTDAIRKYLKDAKIGRVNHAAIAIANPVDGDQVRMTNHNWSFSIEATRRALGFDTLLVVNDFTALAMALPGLTDAQRVQIGGGARRQNSVIGLMGPGTGLGVSGLIPADDRWIALGSEGGHATFAPMDEREDLVLQYARRKYPHVSFERVCAGPGMEIIYRALAARDKKRIAANVDTADIVERAHAGDALALEAVECFCAILGTFAGNLAVTLGALGGIYIGGGVVPKLGELFMRSPFRARFEAKGRFEAYLANIPTYLITAEYPAFLGVSAILAEQLSNRTGGASSAVFERIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPMSHSQVHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSSNTPLAKRATVALETDHIEMRESQLSMISRILHLVMIDILAVGVAIRRAAPNAELAEAMARAKARAGASAGDEAADVLDWLSHGAAPAAKD", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the bacterial glucokinase family."}
+{"protein": "MVQDRKVLDALDTAKTQWYHFTAVVIAGMGFFTDAYDLFSISLVTKLLGRIYYFNPASKSPGSLPPNVSAAVNGVAFCGTLAGQLFFGWLGDKMGRKKVYGMTLMLMVICCLASGLSFGSSAKGVMATLCFFRFWLGFGIGGDYPLSATIMSEYANKRTRGAFIAAVFAMQGFGNLTGGIVAIIVSAAFKLRFDAPAYRDDRAGSTVPQADYAWRIVLMFGAIPALLTYYWRMKMPETARYTALVAKNDKKAAADMARVLNVELVDEQEKAAAATAAAAEEEAARREQYGLFSREFARRHGHHLLGTTVCWFVLDIAYYSQNLFQKDIYTAVQWLPKADTMSALEEMFKISRAQTLVALCGTIPGYWFTVLFIDIVGRFAIQLGGFFLMTAFMLGLAVPYHHWTTPGNHVGFVVMYAFTFFFANFGPNSTTFIVPAEIFPARLRSTCHGISSAAGKMGAIVGSFGFLYAAQSTDPSKTDAGYPRGIGVRNSLFLLAGCNVVGFLFTFLVPESKGKSLEELSGENEMEAEPAAATNSYRQTVPDSGQSE", "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": "MWASFPRPEAIPPGYVGETQHQHRSIMLLNGKSRSWIFLYERLPAPSHDRVKCIAEDVIEFADSFADWSIWNNTKLEDVVDHSTAGMSNLEEGIVKNFSHGRIVLVGDACHKFTSNAGLGLNNGIQDIVAGCNSIRKVVTESGFDLPDVKALEATFKTYYEMRLGPFNDDFIHSKMMTRMQAWANTWYFLFTRYLFFIFSEWILFRFTMLRRVCTGLVLTMHLAKSRLVALLNGFIRSGYHSFIWISAIRPCNDQLLNQLLAGAIQIEILCSLNTWRISSCRAPLLLVFDQARG", "text": "FUNCTION: FAD-dependent monooxygenase; part of the satratoxin SC1 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 paxM FAD-dependent monooxygenase family."}
+{"protein": "MAYNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMSLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPVLPDWCFEDEDEEDEDEDGKKDSEPGSSASFSKRRKERLKLGAIFLEGITVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDKVNGQAVPRYLIYDIIKFNAQPVGDCDFNIRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRPKQFFDINISRKLLEGNFAKEVSHEMDGLIFQPIGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRIDKSFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCAAAAQGQKRKYPLDPDTELMPPPPPKRLHRPT", "text": "FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'- triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase family. SIMILARITY: In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family."}
+{"protein": "MLRTEKEKMAAGELYNSEDQQLLLERKHARQLIRQYNETPEDDAVRTKLLKELLGSVGDQVTILPTFRCDYGYHIHIGDHTFVNFDCVILDVCEVRIGCHCLIAPGVHIYTAGHPLDPIERKSGKEFGKPVTIGDQVWIGGRAVINPGVTIGDNAVIASGSVVTKDVPANTVVGGNPARILKQL", "text": "FUNCTION: Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars. Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
+{"protein": "MAIPILDALTSSSGKKNSAEFSIHSTSNPTNPEEPNITSEADNAEDLAALGYKQEFQRGLSLFSVFSVSFSLLGLLPSVATTLPYSIGYTGTPGLLWGWLIAMVFIICIALSMAELCSAMPTSGGLYYAAAVLAPEGWGPLAAWFTGWSNYIAQLVGGPSINYSTAAMLLGAVNIGNPNYEVQNYQLFLVSIAIQFIHFILASMPTKYIAKLNSVGTYLNTLFLFISMIVILAMSSKNHGFNETSKVWSHIENYTDWPDGFAILMSFCGVIWTMSGYDAPFHMSEETANASVNAPRGIILTAAIGGIMGWVMQIVIAYTVVDQTAVVTGSDSMWATYLSQCLPKRAALGILSLTIVSSFLMGQSNLIASSRIAYSYARDGVLPYSEWVATVNPITKTPIRAVFVNFVIGVLILFLAFAGAITIGAVFSVTAIAAFTAFVAPVAMRVFFVKDADFRTGPFNLGKFSKPIGFCSVSFVALMIPILCFPSVKNPTPAEMNWTCLVFGAPMLAVLIWYAISGRKWFKGPRINLASEGDNSTLEGVELYTGSEELPQKKEKE", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily."}
+{"protein": "MFRAQQNAFDDAVAKATDENLTSENWEYILDVCDKVAAEESGAKDAVAAMIKRLAHRNANVQLYTLELANALAQNCGPKIHRELASRSFTDALLRLANDRMFANNPDFGIMEQAYMKLKTQNPNLQPPSKPGKREITEADRQKEEEELQMALALSIREKPSAAPEPKAEPSTSVSEPASQTQTATSQAVPPGTSAATVSRVRALFDFQPSEPGELQFRKGDIIAVLESVYKDWWKGSLRGQTGIFPLNYVEKLPDPTVEELQREAQMEAEVFGQIKNVEKLLTLLSTRSSELNVQDNEEITSLYHSTLSIRPKLIELIGKYSQKKDEFTQLNEKFIKARRDYESLLEASMAHPAQPQYGRPGQAPYGYPGPAAPLGYPQGPPQSDPQRYFSPRPQDQTHMYPPTSHSPDPRGRTPPAGPSFPQHQQPPPDSYQPVHHRPESTYDNPQELGTSVYDSPVEHPSSSQRLPYPPSGAQVPPGVHQQFQHQQQEYPPSGYPPEDASKPPAAGFALQPPQQTLQQPPYPTAPGAHQPTPSHQPPPVPSTASKPTPYPSLTPGTPSGGEYQAYNPSQAGAANSNPNSYYR", "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": "MSCIQIISSSQTSIAGHRKLCNKLFTLRTQEGFETDILRALNIILTVKKGNSNADRVLRFLVTFVNYLQQKDPEIDIVQPILKHILRGLDAKDKTVRYRCCQIIARVVNCVKEIDDDLYNTLKEKLLSRVLDRESIVRLEAVVALSRLQEDTGDEENDVRNILLFLLQNDPSSEVRRSVLLNIEVSNSTLPFILERARDVDAANRKCVYARVLPKIGDFRYLSIKKRVRILKWGLNDRDESVEKAAADMLAYQWIENADNNLLELLERLDVSNNSDVAVLAIKKFFDVRVDSLSQLEFPEQFWLELTAESSLLARTFNEICIEKNYTDLLDKMPEVVQLTYYIERQYVSLRDKSSYDESCFIIEQLLYIGLSQDMVDEIGRRKLLKSLTNSLSTMALPDSLISLHIELLRKLCSSENDFCSLLVEIITEVFEQGHSQNQTEEQGNSNAPELNKNDYEGEEITVSQKSPSPSLPPNELNEPEPDDMDGYKEAFNELRCLSYVQCLFENITSSLNENLYMVDMLKTLIIPAVRSHDLPIREKGLECLSLVCLLNADLAFENVPLYLHCYEKGSVVLKCTAIRTLTDMLIQHGKAKFTEYEDAISSILFEALGEFENAELQTLGAEAIAKLLVILHYRDELFLKPLIIQYFEPNTVDNHALRQVLGYFFPVYAFGAHENQWRIATIFCDALLSLLEIYRDLDEDDVQLSIGHIAQQMLDWTDNEKLYERKTQTGDDYIALNHNVHLHLANMIFESLPNASEGKERKFMISLLGKLKIPTDLPSSDYQRTKRKLETYESHGFTMDSTSLSILAKFERMLLQNEEARSKFEETEEERLMENAEENEHAGAEAISGEIIPDTVEANMEDEEEVYVKQEEDL", "text": "FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. SIMILARITY: Belongs to the CND3 (condensin subunit 3) family."}
+{"protein": "MVRPEDFNSLELDNSLTDGETVHEMMAHKAGLTYNDFNILPGFINFGVHDVSLETNITKDLKIKAPLVSSPMDTVTESGMAIVMALYGGIGIIHGNFPKPEDQAAEVLKVKRFKQGYVMQPHCLSRDSTAFDMIQIKKKYGYTGAPVTEDGRVGSKLIGMVTSRDFDFITMDVAGQKGTPISDTNDVTPTTPITRIMVSVDQLHLGHINDAPELSQKKLKEHRLGKLPIVNDNGELCALLCRSDLLKARDYPMASYDSKGQLLCGAAVNTRGESQYTVDRVVEAGVDVLIIDSSNGSSTYQISMLRYIKEKHPHVQVIAGNVVTRAQAKLLIDQGADGLRIGMGSGSICITQDVMAVGRAQGTAVYDVARYANQRGIPIVADGGIRDVGYITKAISLGASAVMMGGLLAATTEAPGEYFWGPGGVRVKKYRGMGSLDAMEAHASSQDRYFTAESDQIKVAQGVSATMKDRGSCHKFIPYLIRGVQHGMQDIGVRSLRDFREKVDNGIVKFERRSTNAQLEGGVHSLHSFEKRLY", "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": "MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPITGTNGATCGHSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVPLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVNTRLKHCTPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE", "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. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF- beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1. Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation. SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation. Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell membrane Membrane raft Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts."}
+{"protein": "MDLSLAPTTTTSSDQEQDRDQELTSNIGASSSSGPSGNNNNLPMMMIPPPEKEHMFDKVVTPSDVGKLNRLVIPKQHAERYFPLDSSNNQNGTLLNFQDRNGKMWRFRYSYWNSSQSYVMTKGWSRFVKEKKLDAGDIVSFQRGIGDESERSKLYIDWRHRPDMSLVQAHQFGNFGFNFNFPTTSQYSNRFHPLPEYNSVPIHRGLNIGNHQRSYYNTQRQEFVGYGYGNLAGRCYYTGSPLDHRNIVGSEPLVIDSVPVVPGRLTPVMLPPLPPPPSTAGKRLRLFGVNMECGNDYNQQEESWLVPRGEIGASSSSSSALRLNLSTDHDDDNDDGDDGDDDQFAKKGKSSLSLNFNP", "text": "FUNCTION: Regulates lateral organ growth. Functionally redundant with NGA1, NGA2 and NGA4. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MDPSKVKIPPMKDLTVDNITENVIRINSLCQDERLKYVLERLVTHLHDFARETRLSTDEWMTGLRFLTEVGKICSDVRQEYILLSDILGLSILVDSIDHPKPPNSTEGTVLGPFHTHDAEPLTPGASISHDPAGEPLLVVCTVKDTHGNPVSDVKIDIWETDSTGHYDVQYAGRDGPDGRCIMTSDKEGVFWFKAITPVPYPIPHDGPVGKLLKLLGRHPYRPSHMHFMFEKGGFDHLITALYLRNDPYETSDAVFGVKDSLVVDIGKAGPEYAAKYGVSEDHALLTYDFVLVSDEETSELRARNSKEALDKLGRKVKIVNGLPVPDLD", "text": "FUNCTION: Intradiol ring-cleavage dioxygenase involved in an alternative pathway to the protocatechuic acid pathway since it is active on hydroxyquinol and catechol but not on protocatechuic acid. SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family."}
+{"protein": "MAAQLNVEQLEVSLDGLTLSPDSEERPGAEGAPLQTPPSSPPRDGLGSGTAGQQREPGEAAAEGAAEEARRMEQHWGFGLEELYGLALRFYKIKDGKAFHPTYEEKLKFVALHKQVLLGPYNPDTSPEVGFFDVLGNDRRREWAALGNMSKEDAMVEFVKLLNKCCPLLSAYVASHRIEKEEEEKRRKAEEERRQREEEERERLQKEEEKRKREEEDRLRREEEERRRIEEERLRLEQQKQQIMAALNSQTAVQFQQYAAQQYPGNYEQQQILIRQLQEQHYQQYMQQLYQVQLAQQQAALQKQQEVVVAGASLPASTKVNTAGASDPLPVNGQAKTHTENPEKVLEPEAAEEALENGPKDSLPVIAAPSMWTRPQIKDFKEKIRQDADSVITVRRGEVVTVRVPTHEEGSYLFWEFATDSYDIGFGVYFEWTDSPNAAVSVHVSESSDDEEEEEEENVTCEEKAKKNVNKPLLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKSVYYRVYYTR", "text": "FUNCTION: Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells. Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme activity of PI4KB activity via its membrane recruitment thereby increasing the local concentration of the substrate in the vicinity of the kinase. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion Note=Also mitochondrial (via its interaction with PBR)."}
+{"protein": "GLLGAPAVATYAAAPAVAYSAAPAVSTAYINQAAPVLAHAGPVAVAHAAPYAVHAPAVGASHQAIVRSLGGNQAVSHYSKAVDSAFSSVRKFDTRITNDALLHAPVAVAHAAPVVSTYAAHAPVVSSYAHAPLVSSYAAHAPLVSSYAAHAPLVSSYAAHAPVLSTAYAAHAPVVSSYAAPVVARTAAVGYSPAAVVSHTSFTGLGASYAW", "text": "FUNCTION: Component of the cuticle of the pupa of Tenebrio molitor."}
+{"protein": "MAEQTEKAFLKQPKVFLASKKTGKGKRPGKGGNRFWKSIGLGFKTPREAIDGTYIDKKCPFTGTVSIRGRILAGTCHSAKMNRTIIVRRNYLHFIKKYQRYEKRHSNIPAHVSPCFRVKEGDHVIIGQCRPLSKTVRFNVLKVIPAGSSGGVKKAFTAI", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS17 family."}
+{"protein": "MGVRFSWGTEVRKLDVEGDKVRGVVTNWERLAADAVVVALGSYSPLLLKRHGIKLPVYPVKGYSLTIPITDASRAPESTIMDETYKIAITRLGDRIRVGGMAEISGYTNDLGPARRRTLEHSVMDLFPGGDAKEASYWSGLRPMTPDGTPVIGPTKIAGLFLNTGHGTLGWTMSSGSARVIADLVSGRKPEIDATDLAVSRYA", "text": "FUNCTION: Either a functional dehydrogenase or a non-functional fragment. SIMILARITY: Belongs to the DadA oxidoreductase family."}
+{"protein": "MSYMNNTFQSNYDYSKDKNFMSTDIGPSMREMKAQKRRSRPMDNPDADNPYIPKFISTAPWYAQDDDAVERLAHQRIGKKETPSGGRSSIEGSWYVRGKKLGPAATKYRKGACENCGAMSHKVKDCMERPRKRGARWTGEDIQADEVIQDINVSWDAKRDRWNGYDATDYKKVIERYEKLDELQNKGEENRDASENSAVKASRNSTVSGSEDSASITTPSLRMREDVVAYLRADNKNLQYEPKSRSMRDETGYHMVDDSSGGAGFVKASGGEKEDFEKLQMFAWEAERSGTRVHVVANPTAGELEFRKNKASRMTTQKHIDQSILDRYGDGTSKVKDKKAKNNEKEVPDLAILDKSEKSKGESNTDEESENLVIVEGDL", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLU7 family."}
+{"protein": "MAFAVSTACRPSLLLPPRQRSSPPRPRPLLCTPSTAAFRRGALSATTTPTPARAALPSTTGRNRIVCGKVSKGSAAPNFTLRDQDGRAVSLSKFKGRPVVVYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDAASHKEFKKKYKLPFTLLSDEGNKVRKEWGVPADLFGTLPGRQTYVLDKNGVVQYIYNNQFQPEKHIGETLKILQSL", "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 thylakoid lumen. SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily."}
+{"protein": "MSKIFVNPSAIRAGLADLEMAEETVDLVNKNVEESQAHLQAEPIEVDALPEDMKRLQISEPKPCQLPDGTCMKEEGGDEDFYMAESGDPYIPLQSYLDTMGIQIVRKMKTGERFFKIWSQSVEEIISYVAVNFPVPPGKSLADKSTQTSVEKSKPASQPTQPKKEDQLSKVNIDSQESSGPPALDWAATNDDDDASVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVREAKGIPGVTRRAGDGVRLPLRCILGWVASTHSRRFQLLVNSDKLNKVMQDDINRYLAY", "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: [Isoform P4]: Host nucleus. SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm. SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus. SIMILARITY: Belongs to the lyssavirus protein P family."}
+{"protein": "MASPVEASPGCASGLGPHRRKRTTFSVGQLVELERVFAARPYPDISTREHLAQVTHLPEAKIQVWFQNRRAKRIKDRKPGALNSRLELPPNSCSLPDTPQLPWDPGTSSHPLHPTSSAQYTSACPPQTSCLGPILGPGQSWSGAKVAAPWGTSGASGIHSSLEQIVPQTSLGNLSDLIYTSAIVTNVDHF", "text": "FUNCTION: Probable transcription factor involved in the control of specification of mesoderm and endoderm. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family."}
+{"protein": "RGICLEPKVVGPCKARIRRFYYDSETGKCTPFIYGGCGGNGNNFETLHACRGICRA", "text": "FUNCTION: Serine protease inhibitor that inhibits trypsin (Ki=50 nM) and probably also chymotrypsin (Kd=1.6 nM). Has an anti-inflammatory effect in LPS-activated macrophages in vitro, specifically reducing release of TNF and IL6 but not nitric oxide and reducing expression of IL1B precursor. FUNCTION: Dual-function toxin that inhibits both serine proteases and voltage-gated potassium channels (PubMed:26404319, PubMed:33158163). Has potent activity on both trypsin (Ki=50 nM) and chymotrypsin (Kd=1.6 nM) (PubMed:26404319). Shows inhibitory activity against 5 of the 7 potassium channels tested (rKv1.1/KCNA1; IC(50)=12.6, hKv1.2/KCNA2; IC(50)=181.7, hKv1.3/KCNA3; IC(50)=29.7, rKv1.6/KCNA6; IC(50)=43.9, drosophila Shaker; IC(50)=114.9) (PubMed:33158163). Has an anti- inflammatory effect in LPS-activated macrophages in vitro, specifically reducing release of TNF and IL6 but not nitric oxide and reducing expression of IL1B precursor (PubMed:26404319). In contrast to some paralogs, this protein decreases reactive oxygen species (ROS) level in the oxidative stress agent 6-hydroxydopamine (6-OHDA)-induced neurotoxicity model, but does not show cytoprotective activity on neuroblastoma cells (PubMed:33802055). This protein also shows a weak free-radical scavenging activity (PubMed:33802055). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily."}
+{"protein": "MSLQGIHLSDLSYKHAILKESQYTIKRDVGTTTAVTPSSLQQEITLLCGEILYAKHADYKYAAEIGIQYISTALGSERVQQILRNSGSEVQVVLTRTYSLGKVKNNKGEDLQMLDIHGVEKSWVEEIDKEARKTMATLLKESSGNIPQNQRPSAPDTPIILLCVGALIFTKLASTIEVGLETTVRRANRVLSDALKRYPRMDIPKIARSFYDLFEQKVYYRSLFIEYGKALGSSSTGSKAESLFVNIFMQAYGAGQTMLRWGVIARSSNNIMLGHVSVQAELKQVTEVYDLVREMGPESGLLHLRQSPKAGLLSLANCPNFASVVLGNASGLGIIGMYRGRVPNTELFSAAESYAKSLKESNKINFSSLGLTDEEKEAAEHFLNVSDDSQNDYE", "text": "FUNCTION: Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases. RNA replication depends on the availability of soluble nucleoprotein. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Localizes in cytoplasmic inclusion bodies. SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family."}
+{"protein": "MGNECFLTFTTTHLSEAEQKLALYRLQLVEPPKLPLEKKTNPDKDGPDIKPNLWMWVNPNMVYPPGKLEVAVKEEDQSALSAFQPALKEEEDSCSEASEVQQPLPPCRQKRKQRRSTVPLPLAPGRRAPLENPWRLPQAISPEGRLWSRPPLHYFHLIALALRNSPPCGLSVQQIYSFTREHFPFFRTAPEAWKNTVRHNLSFRDSFEKVPASRQGGASTGPRSCLWKLTEEGHRRFSKEARTLASTQLQSIQQCMSQPGVKPFLFDL", "text": "FUNCTION: Transcription factor which acts as both an activator and a repressor (By similarity). Activates transcription of a number of genes including the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 which are involved in protection against oxidative stress (By similarity). Required for normal brain development (PubMed:34723967). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, perinuclear region Note=Localizes to the nucleus and cytoplasm with higher levels in the nucleus where it is expressed in a diffuse manner (PubMed:34723967). Located in the cytoplasm of spermatocytes and strongly accumulates at the perinuclear region in elongated spermatids (PubMed:25609838)."}
+{"protein": "MAALCEAFTLCGLGPAGGVGLGSGLLALEPGADPDHVLLTDRGRTTTLFKVSDQKPLGCWSVKHGQIITCPVVCNFETHEYIAVHDNKVLRIWKDEDVNLDKVFKATLSAEVYRIHSLPHAEPLVLFKGGGVRTLDVLLEAPQQEIENVISDEVIKWSEAFLESRQPVLIFVTEKDGDFFVYVQKPKMRSLHKYKLEQQELCNPLSFTAYIKKQIITLLCLYSSDSVYKVLIPLQQSSEEEEQTSSKSLLLNLSISGSVLKGTSFVVLDKDHVAVLGSLAASGEESKECLTIWNTKFQTLQASKELPLGTSGQLWCYGEKFFFTHGKVLTVVIYKCETSSLAAAVGKLKDSQTSDLSSFVNWNTLGDEELLVSLQSQQSVALKSESKMTLRSKKSAVANIQPDTSTVGQFLLSIKDASTAAVEDQLRQLLSKAQMPDFQATIGCIISALINRCKTDPKFYPRNFLVQMIQKGELSYSLCPDLMAVALEKKDVHLLQICLQRFPDIPEEITYACLKVFLSISDDYLERTDVNLESVISYIDIEPNNKEVKTEVVENGFNTELEEDGCDVTGMKETHMMDSVEFCPVGPQKAALLNAVLHSAYSETFLLPHLKDLPAQQAVLFLRYLHYLYVKCSEKINTTLPGILSPTISQIMDWMCLLLDAHFTVMVMLPEAKGLLSSMHRFVRAQVRLYSELNKIEGSLQELQRIKCQKHSQAYSIEVLELI", "text": "FUNCTION: Ribosome biogenesis factor. May be required for both optimal rDNA transcription and pre-rRNA processing (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus."}
+{"protein": "MSTRNPAQSHWGVPKGQRTELYVYNTLTHSKVPFVSNGSNLTWYCCGPTVYDASHMGHARNYVTTDILRRILQSYFGYNITFVQNVTDIDDKIILRARQQYLFEEYKKQQGTNKSHSEAREKVTEAWFAYAKKNLPEPPSSMSEWPQWLASHDIPTLAINNPKLPMHVDALKSALDALQVSEASEIISLDGFWPKVQDVLVPLLDAELGSTVTDPAIFRKLAAYWEDDFNKDMANLNVLPPTAVTRVSEYVPEIVDFVQRIIDRGYAYPVTDGSVYFDTEAFEKGGHFYAKLEPWNKGNRELIAEGEGSLAALTGKKRPGDFALWKASKPGEPSWDSPWSKGRPGWHIECSVMASALLGSNIDIHSGGIDLAFPHHDNELAQSEAYFDCPQWVNYFFHAGHLHIEGQKMSKSLKNFITIKEILKKFTPRQLRLAFLLQQWNTQLDFKETLLAYVLNIEQALENFFRTVRALMNETEGVSANGGHVPEKFDKLEIELLEKFQQTQQNTHLALCDSFNTPLVMQHIDNLVTQANIYIREVGQQPCSRLLGQIASWITSMLQIFGLDENGHPNAVGWSSSKGSSSENTDAMPYIRAVSSFRDRVRELCIAKASSQEILKACDIFRDYDMAALGVSFNDRPQGSALVKLVDAEELIAAREQKLEEERAKQAKKAQAKAEQEKKQVERVMKGKTSPSEMFKMFKEYLSFDEAGLPTKMRGEDGSEIDVPKSRKKKLQKEYAQQEKLHKEYLSYIESNKS", "text": "SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
+{"protein": "MDGEDIPDFSSLKEETAYWKELSLKYKQTFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVMNSNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPLSAPGMLPLSV", "text": "FUNCTION: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also 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 ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Chromosome, centromere, kinetochore Cytoplasm, cytoskeleton, spindle Note=Localizes to the interphase centrosome and the mitotic spindle. Localizes to the cell body of the motor neurons and colocalizes with assembled neurofilaments within axonal processes. Localizes to the microtubules of the manchette in elongated spermatids. Colocalizes with DISC1 in the perinuclear region, including the centrosome. Localizes to the kinetochore in a CENPF- dependent manner (By similarity). SIMILARITY: Belongs to the nudE family."}
+{"protein": "MPRSSATARKSHSNRHENGSANTGKKVAKQKSNGHLNGNLNGGSASSSLSSSQVDLPSSRSSSDPVVPTTTAASTKLNGTPDSSKGDCNAPDHLNGYAKGNADMSYVQNDGVASQTGGDVAGPASRRTEKSATGSKRSPSNASVNPLQLASTILKSCPMYDTIAILIFLLQLPPMVLTLVQFLFASLTFLPPSGASAGSLTSNFDIFQGPAGTPSLGTMIAMDGFCLLIWGLFMWTWAQNFALDLAHVQVAITLGGGGFGKNGGVNTLCVGIVLIMHLVRSKGIQDFVIGHLLSSNIISPDMLSQYSHLLPTEFRRTEPQTSPSWLRSLLAVHILAQAGTAMARRSMAKNRTPNPPRTGKRIDTEASAGSQTQIDSAFESGASVSSYIGADGQIVTSAAHKDGRDRLLSAKKRRRQANQVRSRQPFWAALASTKITVMREYEHSRALSKTARSLPMTEDDLQGLSLDDGLVWITEIDSSTIKFAAGDFSSADDSSGSGACEAGCLGSEDMEPFYVCVNGALWATATICKVHDAPKGSSMVHWRGEISGLAPNCAYTCSFVRSDTDEEICVISVKTPANNDAEQVSSVSTPPHPSYRPSSPTTTLKNSIVNAEAKLNEKRSRLRKAKNDHKLIISKIRKELDNYNHRLHSGTDENRQKQRSLQLERNIRQTEEATALLEDQLDNLENVPEEELRKWSDQKAKYEHELGLLNSAKEELASARSAIAREVSSLETELSSAIQRRERLQSRRTRINEQYERIVSANAQGLNERERRAAEQFAREQDQAKLEATFNEQFATIGQSVQEYQLRAQQIWQQCDAIEQAIQQQHQQMLLDPGPLTPEGNLPGTNPFSESALPLGALTSTAPSSRSLLGLSFPPLKSSPLQTASSPVGASSSHPTSPVQQPSYLNFPTSPLVNASSHLDSDFVYRHRSFSNRSARSSLYGSDFMDSSRRQPFQLDLSELLADKRSPGSDSNTALNSGLRPVSSPFQRAGSRGSGSGSNGSGGSGSGSGSPSSVYGKTN", "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 (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acrB family."}
+{"protein": "MDVCARLALWLLWGLLLHQGQSLSHSHSEKNTGASSGATSEESTEAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVIQWLITYVELPQYEETFRKLQLTGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAERQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQLGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMGRAADEALNAMPSNGSHRLIEGVHPGSLVEKLPDSPALAKKTFMALNHGLDKAHSLMELNPSVPPGGSPLLDSSHSLSPSSPDPDTPSPVGDNRALQGSRNTRIPHLAGKKAMAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK", "text": "FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release- activated Ca(2+) (CRAC) channel subunit ORAI1. Involved in enamel formation. Activated following interaction with STIMATE, leading to promote STIM1 conformational switch. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single- pass type I membrane protein Sarcoplasmic reticulum Cytoplasm, cytoskeleton Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular Ca(2+) and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane. Associated with the microtubule network at the growing distal tip of microtubules. Colocalizes with ORAI1 at the cell membrane. Colocalizes preferentially with CASQ1 at endoplasmic reticulum in response to a depletion of intracellular calcium (By similarity)."}
+{"protein": "MSILIYKVSKSLGNLKILDRVSLYVPKFSLIALLGPSGSGKSSLLRIIAGLDNCDYGNIWLHGIDVTNISTQYRRMSFVFQHYALFKHMTVYENISFGLRLRGFSAQKITNKVNDLLNCLRIADISFEYPAQLSGGQKQRVALARSLAIQPDFLLLDEPFGALDGELRRHLSKWLKRYLQDNKITTIMVTHDQKEAISMADEIVILKEGRLLQQGKPKNLYDQPINFFVGIFLGLLIEIPKLNESITLKNIPSKTPQNLKKFAFDPIWVKIFANRSINKYRFFLRPYEFCIKSEMDLEATPVQIKTIIYKRTFVQLDLFVTSFLWNLTIPIGYQSFRNLHIESFMQTLYIKPRLQVFLRAYPILTNIKKN", "text": "FUNCTION: Part of the ABC transporter complex involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ABC transporter superfamily. Sulfate/tungstate importer (TC 3.A.1.6) family."}
+{"protein": "MGRSSKDKRDAYYRLAKEQGWRARSAFKLLQLNEQFNLFEGAKRVVDLCAAPGSWSQVLSRELLKNIDTSIAADEKPMIVAVDLQPMAPIDGVCTLQLDITHPNTLSIILSHFGNEPADLVVSDGAPDVTGLHDLDEYIQAQILLAAFNLAVCVLKPGGKFVAKIFRGRDVSLLYSQLRLMFRKVSCAKPRSSRASSIESFVVCEDFNPPSNFQPDLTKPLCVIDPTNAHEIAPFIACGDLDGYDADATYPVEINMKKATLDVIQPPTAPPYKRAIELKHSKMMS", "text": "FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily."}
+{"protein": "MSRIYQDSALRNKAVRSARLPGAWDPAAHQRGDGVLLEGELLDVSRHSILDAHGRKERYYVLYIRPSRIHRRKFDPKGNEIEPNFSATRKVNTGFLMSSYKVEAKGDSDRLTPEALKGLVNKPELLALTESLTPAETVAFWMPESEMEAMELELGAGVRLKTRGDGPFLDSLAKLEAGTVTKCNFAGDGKTGASWTDNIMAQKSSEGAASETREQGDGAADEEWDD", "text": "FUNCTION: Regulates actin polymerization by inhibiting the actin- nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence (By similarity). SUBCELLULAR LOCATION: Cell projection, lamellipodium Note=Colocalized with the WAVE complex at lamelliupodium tip. SIMILARITY: Belongs to the Arpin family."}
+{"protein": "MGASIDDYCLIHKKILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSSALVPADEGLFLSMLLKLMNAKRTIEIGVYTGYSLLTTALALPEDGKITAIDVNKSFFEIGLPFIQKAGVEHKINFIESEALPVLDQMLQETKEEDLYDYAFVDADKSNYANYHERLVKLVRIGGAILYDNTLWYGSVAYPEYPGLHPEEEVARLSFRNLNTFLAADPRVEISQVSIGDGVTICRRLY", "text": "FUNCTION: 4'-O-methyltransferase converting norbelladine to 4'-O- methylnorbelladine (By similarity). 4'-O-methylnorbelladine is a precursor to all Amaryllidaceae alkaloids such as galanthamine, lycorine and haemanthamine, and including haemanthamine- and crinamine- type alkaloids, promising anticancer agents (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family."}
+{"protein": "MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQALTSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL", "text": "FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5- phosphate, a key step in isoprenoid and cholesterol biosynthesis (PubMed:9325256, PubMed:18302342, PubMed:9392419, PubMed:11278915). SUBCELLULAR LOCATION: Cytoplasm Peroxisome. SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase subfamily."}
+{"protein": "MVAFDANEILTPFCEGHREGAILFDCQRMRQVEYGLFVPAWWGERAHPVSEGGRGSAWFVEASFGNAVLRQYRRGGMIAMLNRDRYFWCGGHRTRSVLEFRLMRELISRGLPVPTPLAACYVRYGVQYRAAILIERLEGVSSLAMCIRGNSKETHWEQIGRMISRFHREGLDHADLNAHNILLDPAGQCWLIDFDRGALRIPATKWRERNLARLLRSLLKIRGERSVDAVYRDFERLRRAYDLAWSRGC", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D- manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP family."}
+{"protein": "MAAQCESIGGDMNQSDPGSNSERSADSPVPGSEDDSPHDPEWREERFRVDRKKLETMLQAAAEGKGKSGEDFFQKIMEETNTQIAWPSKLKIGAKSKKDPHIKVSGKKENVKEAKERIMSVLDTKSNRVTLKMDVLHTEHSHVIGKGGNNIKKVMEETGCHIHFPDSNRNNQAEKSNQVSIAGQPAGVESARVRIRELLPLVLMFELPIAGILQPIPDPNSPTIQQISQTYNLTVSFKQRSRVYGATVIVRGSQNNTSAVKEGTAMLLEHLAGSLATAIPVSTQLDIAAQHHLFMMGRNGCNIKHIMQRTGAQIHFPDPNNPLKKSTVYLQGTIDSVCLARQYLMGCLPLVLMFDMKEEIEIEPQCITQLMEQLDVFISIKPKPKQPSKSVIVKSVERNALNMYEARKCLLGLDSSGVTVTNQSTLSCPVPMNCHGLDILAAGLGLSGLGLLGPNTLSVNSTTAQNSLLNALNSSLSPLHSPSSAAPSPTLWAASLANNATGFSAIPHLMIPSAAQATLTNFLLSGVPNYGQNTPSPPPGLTPVDVHMNGIHSECKKVTSALNGHVKPTNMKYGTISSSSLGDKVLNTNLAEASRQSNNHSSAEEVNSKTDPEGCNDAFVEVGMPRSPSHSANTKDLKQMLNSTKAPCPTRQTVKLLHGTKNSHLHGERLLSDSEMSPMEGPVTDKKAPGSERAAERAAAQQNSERARLTSQSEYGTMQAYDYEQKKLLATKAMLKKPVVTEVRTPTNTWSGLGFSKSTPAETIKELRRANHVPYKPTMTTTYENSSLSRSNSREQLGNGSDSENWRERNGIDSSQNDYSSSIGSPKRKQNKSAEHYLSSSNYMDCISSLTGSNGCNLNSSFKGSDLPELFSKLGLGKYTDIFQQQEIDLQTFLTLTDQDLKELGISTFGARRKMLLAISELNKNRRKLFEPTNIRASFLEGGASGRLPRQYHTDIASVSGRW", "text": "FUNCTION: Putative RNA-binding protein. May be involved in regulating gene expression during embryonic development. Seems to be involved in endoderm formation. Ectopic expression results in endoderm formation in the absence of mesoderm induction. SIMILARITY: Belongs to the BicC family."}
+{"protein": "MFNRIKVVTSLLLVLVLFGALQLISGGLFFSSLKSDKENFTVLQTIRQQQLLLSESRVDLLQARNSLNRAGIRYMMDTNKIGSGATIDELLAKAKEELARAERNYTAYEKIPQDPRQDPQATEKLKQQYGILYGALSELIQLLGEGKINAFFDQPTQKYQDDFEQTYNAYLQQNGKLYQIAVDASNSSYSSAIWTLIVVIIVVLAAIVGVWMGIHHILVRPLNRMIEHIKRIASGDLTQPIPVTSRNEIGVLAASLKHMQNELIETVSGVRQGADAIYSGASEIAAGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASQLALSASETAQKGGKVVANVVETMHDIASSSQKIADITGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAKEIKALIEDSVNRVDMGSVLVESAGDTMGDIVNAVTRVTDIMGEIASASDEQSRGIDQVGQAVAEMDRVTQQNASLVEESASAAAALEEQASLLTQSVAVFRLKSEGQEEYKAPVSNKTAPAAIATHKKTSASDYQDNWETF", "text": "FUNCTION: Receptor for the attractant L-serine and related amino acids. 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. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein family."}
+{"protein": "MQMQTYKLVVVGGGGVGKSAITIQFIQSYFVTDYDPTIEDSYTKQCNIDDVPAKLDILDTAGQEEFSAMREQYMRSGEGFLLVFALNDHSSFDEIPKFQRQILRVKDRDEFPMLMVGNKCDLKHQQQVSLEEAQNTSRNLMIPYIECSAKLRVNVDQAFHELVRIVRKFQIAERPFIEQDYKKKGKRKCCLM", "text": "FUNCTION: May be involved in endocytic processes and/or other transport pathways mediated by vesicle trafficking. May interact functionally with ROP protein. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MKTLQTSPKKDGYRMPGEFEAHKDVYLLWPERPDNWREGAKPAQATFAKVAETIAQFESVTVGVSDRQYTNARHMLADNIQVVEMSNNDSWIRDCGPTFVVNDKGDSRGVDWTFNAWGGLVDGLYFPWDKDDRVAQKVCEIEGRDRYRLDDLVLEGGSTHVDGEGTLLVTEECLLSDGRNPQLSKEQIESILKEYLNVEKIIWLKKGIYLDETNGHVDNIANFVKPGQVVLAWTDDQSDPQYAISKENYDMLINETDAKGRKLQVEKLYLPKPILITEAESQGVDTVDGTLPRLAGDRLAASYVNYYTANGGIVFPLFNDPMDEKAQEILQKLYPDRKIVGVPAREILLGGGNIHCITQQIPAGR", "text": "SIMILARITY: Belongs to the agmatine deiminase family."}
+{"protein": "MSLAYSQATSLLLSSTTRGGVPSLMHIPATNSPARINTGATPFWKLPFPARPLRQYKSITRARNQVILTAEKSVDVDTEKNTHHQKATAETTRELVERIRWMLQNMDDGELSVSPYDTAWVALVEDIGGSGRPQFPTSLEWISNNQYPDGSWGDRKFLFYDRILNTLACVVALKTWNMHPDKCEKGLKFIKENIHSLENENEEYMPVGFEVAFPSLIETAKKLGIEIPDDSPGMKDIYAKRHLKLKKIPMDLLHKMPTSLLFSLEGMKGLDWQKLLNLRFEGSFLSSPSSTAYALQHTKDELSLQYLLKAIKKFNGGVPNAYPVDMFEHLWSVDRLQRLGISRYFEPEIEECMKYAYRYWTDKGICWARNTNVQDVDDSSMGFRLLRLHSFPVTIDAFKQFEKGGEFCSIPGQSTHAITGMYNIFRASQVLFPGDHILADARKYSAKFLHQKRVNEAIVDKWIITKDLPGEVGYALDVPFYASLPRLEARFFLEHYGGDDDVWIGKTLYRMLYVNCDTYLELAKLDYNVCQAVHQHEWTNIRRWYKDCSVGEFRLAERSLLRAYYIAASTVFEPERSGERLAWAKTAILLETILSQKLHSEEKHTVVDEFKHGSISISGNGRRHQTRISLAETLIYTVNQLSSDIKQAHGRDIHQQLHHAWQKWLTTWEGRGNLGEAEAELLVRTLHLSSGLDESWFSHPKYQQLLEVTSKVCHQLRLFQNRKMHDPKGCTIDLVTGTTFQIEAGMQELVKLVFTKSSEDLDAHTKQSFFAIARSFYYTAYCDPEAIESHVDKVLFDKVV", "text": "FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase that produces kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP) (PubMed:29315936). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MPGISSQILTNAQGQVIGTLPWVVNSASVAAPAPAQSLQVQAVTPQLLLNAQGQVIATLASSPLPPPVAVRKPSTPESPAKSEVQPIQPTPTVPQPAVVIASPAPAAKPSASAPIPITCSETPTVSQLVSKPHTPSLDEDGINLEEIREFAKNFKIRRLSLGLTQTQVGQALTATEGPAYSQSAICRFEKLDITPKSAQKLKPVLEKWLNEAELRNQEGQQNLMEFVGGEPSKKRKRRTSFTPQAIEALNAYFEKNPLPTGQEITEIAKELNYDREVVRVWFCNRRQTLKNTSKLNVFQIP", "text": "FUNCTION: Transcription factor that binds preferentially to a variant of the octamer motif (5'-ATGATAAT-3'). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the POU transcription factor family. Class-6 subfamily."}
+{"protein": "MNEQPLIAALSLQRAGAPRVGGDRIRLLEAIARHGTIAGAAREVGLSYKTAWDAVGTLNNLFEQPLVEAAPGGRTGGNARVTEAGQALIAGFGLLEGALTKALGVLEGGVSAPEKALNTLWSLTMRTSNRNTLRCTVTRVTLGAVNAEVELALTDGHSLTAVITERSATEMGLAPGVEVFALIKASFVMLAAGGDPGRISACNRLTGIVAARTDGPVNTEIILDLGNCKSITAVITHTSADALGLAPGVPATALFKASHVILAMP", "text": "SIMILARITY: Belongs to the ModE family."}
+{"protein": "MHANPLSSFNRAQHGNLTNVEASQVKSAGTSSTTNIDSKNIEEHVADRLSDLGRPDGGWFFEKSLGTLKNLNLEQLAGIHDVLKLTDGVKNIVSFGAREGGFELAMQFRHDLYRSQHPDENSPHDAATHYLDAISLQSNKFTKLEKLQHVDVFKMQNPFWDVGYKNGIAHAKKMAFFITPEWLGSDFCKQEFQWLSETKNKDIKSAFVIFKDVDLKSKNMTSIFNFADFHKSRVMMASTPPESGLNNVKIENSVDLNFKRLLTDRESWELNNFLGD", "text": "FUNCTION: NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR) (PubMed:34657283, PubMed:36048923). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself (PubMed:34657283). Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+) (PubMed:36048923). SUBCELLULAR LOCATION: Host cytoplasm Host cytoplasm, host cytosol Note=Delivered into plants by a type III secretion system (T3SS)."}
+{"protein": "MMCLKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLKYASDLHDYSKKPLFLSISGLSVEENVAMVRRLAPVAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLPFGVKMPPYFDIAHFDTAAAVLNEFPLVKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRCPDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVKTIE", "text": "FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily."}
+{"protein": "MSSVTIGKCYIQNRENGGRAFYNLGRKDLGIFTGKMYDDQIWSFQKSDTPGYYTIGRESKFLQYNGEQVIMSDIEQDTTLWSLEEVPEDKGFYRLLNKVHKAYLDYNGGDLVANKHQTESEKWILFKAY", "text": "FUNCTION: Galbeta1-3GalNAcbeta1-4Galbeta1-4Glc oligosaccharide-binding lectin. Binds strongly to the oligosaccharides of ganglioside GM1b and to a lesser extent its precursor asialo-GM1 (PubMed:31769916, PubMed:33328520). Binds weakly to asialo-GM2 oligosaccharide and to the glycan moiety of globo-series stage-specific embryonal antigen 4 (SSEA- 4) hexaose (PubMed:31769916). Binds galactose, N-acetylgalactose and lactose. Does not bind GM1 (PubMed:33328520). Does not bind to Gal- beta1,3-GalNAc (Thomsen-Friedenreich antigen), the oligosaccharide of GM1a ganglioside or SSEA-4 tetraose. Does not bind to N-glycans, O- glycans or glycosaminoglycans of glycoproteins. Does not bind Lewis glycans, derivatives of lactose or N-acetyllactosamine or blood group (ABH-type) oligosaccharides (PubMed:31769916). Does not bind glucose (PubMed:33328520). Has hemagglutination activity towards rabbit erythrocytes (PubMed:31769916, PubMed:33328520). Displays cytotoxic effects against various cultured cell lines including human breast (MCF-7), cervical (HeLa) and colon cancer (Caco2) cell lines, as well as dog kidney (MDCK) cell line that express asialo-GM1 oligosaccharide at their cell surface. Shows dose- and time-dependent activation of MKK3/6, ERK1/2 and p38 MAPK, as well as caspase-3/9 in HeLa cervical cancer cells. No cytotoxic effect on BT474 human breast cancer cell line. May be involved in recognition of glycans found on parasitic or symbiotic microorganisms (PubMed:31769916)."}
+{"protein": "MGLIIDTSIIIALERGKVSTKQWSHYGQAYISPIVLTELLIGVDRVNNENKRIKCLAFIEYVKSLFTILPFGIEEVYTYARIINDLYKQRITIGTHDMLIAATAITHGYSLLTLNVKDFKRIQGLEVLTVSSKD", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has ssRNase activity. Upon expression in E.coli inhibits growth in liquid culture; this toxic effect is neutralized by coexpression with cognate antitoxin VapB1. Its RNase activity is partially inhibited in vitro by VapB1 (PubMed:22046301). SIMILARITY: Belongs to the PINc/VapC protein family."}
+{"protein": "MPMVTRRLRDPDVNPCLSESDASTRCMAENNYDKESCSSHFLKYKNCRKFWNSVMIQRRQNGVKPPMPTAAERDEILGGLGKMPY", "text": "SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: Belongs to the CHCHD7 family."}
+{"protein": "MAASLVGKKIVFVTGNAKKLEEVIQILGDNFPCTLEAQKIDLPEYQGEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPYIKWFLQKLKPEGLHQLLAGFEDKSAYALCTFALSTGDPSQPVLLFRGQTSGQIVMPRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEYFSVAAGAGDH", "text": "FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and 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": "MSIDRTQPLLPVTPVQPRETSDIAQQTRKPSAQSKTPVSGTEVKLSDAQAKLMQPGSQDINVERVETLKQAIRSGQLTMDTGKIADALLKNVADDLKNS", "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 (By similarity). SIMILARITY: Belongs to the FlgM family."}
+{"protein": "MSTGLRYKSKLATPEDKQDVDKQYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKERKLLSAEERISQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNSECWKPITDYVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKALHEKVNIVPLIAKADCLVPGEIRKLKERIREEIDKFGIHVYQFPECDSDEDEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMESPIPILPLPTPDAETEKLIRMKDEELRRMQEMLQKMKQQMQDQ", "text": "FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
+{"protein": "MRTVVIDYGMGNLRSVSKALEAVGFPEVVVSNDYRVASEADVLVLPGVGAFGDAMKNLEELNLVSVIRRHIEKGKPFLGICLGLQLLFEKSYEHGEHRGLGILKGEVILLPLGVKIPHIGWNQLWFKKESEILEGLKEGDFVYFVHSYRVVPEDESVVLTKTDYGEYFVSSIELDNVVAFQFHPEKSQKKGLKLLENFKRKAEKLTT", "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": "MAGGFRPYDQDSCPNLTNSEAPEFSMSVVCKTEPHYFHPQTAILPSVQYSHPYHHYLSQFAPNFVPYYYRLLSRPIMKQEEMDIENYINYEVAAQQTMMRQRTLKPLGQLQIQMPPPIIVNQPVKPVPVKAVPVRRSSPPKRRVINAQLVAVATASGGIKNIEPRVEPLPRLEESFKQQVAKIQKSQHHYEQLFGRLTSMLKTLNQRYDNDAEDVPAPPSKRPRHMSTSSSESHIPDTASEKDEKDTLVQYPHRVQKEDGSAVYVLGPNGTQITAHQYGEVFWTNAPVATRCLLCVVFSSDELATHTLTGKPSPAFYGRERPPKLQLDQRKVDDIVVCVRNRTGGKERVIRATITTKCADTAKKYKRRAKKAQKVAIKEEY", "text": "FUNCTION: The heterotrimeric Elba complex is required for chromatin domain boundary function during early embryogenesis. It binds to a 8-bp sequence 5'-CCAATAAG-3' in the Fab-7 insulator or boundary element in the bithorax complex and contributes to its insulator or boundary activity (PubMed:23240086). Elba2 can act as a transcriptional repressor and binds the palindromic sequence 5'-CCAATTGG-3' to mediate transcriptional repression (PubMed:25561495). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MDAARDGRPERRPRRSGTYRTHPFQRPSARRSLLDALRAADAEAAERPRVRRPRPDFQRPPDEDTSEDENVYDYIDGDSSDSADDYDSDYFTANRGPNHGAGDAMDTDAPPERAPEGGAPQDYLTAHLRAIEALPESAPHRSLLERTARTVYAHEFPPRDLSAGSRAPAQRARRSLRGFPRGGGGGQEPGPDDEGDDAADLREDLVPDEAYAHLERDERLSEGPPLLNMEAAAAAAGERSVVEELFTYAPAQPQVEVPLPRILEGRVRPSAFFAQMPLDALCRTPPNDQRVVRERRAWDMAGTPHGLLITTWSTVDPEFSIGGMYVGAPEGTRPRLVWRRAMKQAMALQYRLGVGGLCRAVDGARMPPTEALLFLAARAAARSAQLPFFVAAGARGRRRAAPARGGGWAAGSHAVHATGRVPHATLFRGSMGSLIYWHELRVMLTAVPALCARYAGAGLQSAELYLLALRHSEAPGYTANERYALSAYLTLFVALAERAVRWLYLAGAHLLGPHPTAAAFREVRAKIPYERLPLGSATLHDAEVETVDSATFQEALAFSALAHVYGEAYVAVRTATTLLMAEYAAHAERRDVREMTAAFLGVGLIAQRLMGSLEPAAELRSRRSGVRGPACPTVREGTLARYSLLADAALPLVRPVSLVEFWEARDGVMRELRLRPVASPPLAGKRRVMELYLSLDSIEALVGREPLGSRPVLGPLVDIAEALADHPHLVTGDGRGPRLGGR", "text": "FUNCTION: Tegument protein that can bind to various RNA transcripts. Plays a role in the attenuation of selective viral and cellular mRNA degradation by modulating the activity of host shutoff RNase UL41/VHS. Also plays a role in the primary envelopement of virions in the perinuclear space, probably by interacting with two nuclear egress proteins UL31 and UL34. SUBCELLULAR LOCATION: Virion tegument Host nucleus Host cytoplasm Note=Major tegument protein of the virion. Undergoes nucleocytoplasmic shuttling during infection. Localizes to the major sites of transcription in the infected cell nucleus. SIMILARITY: Belongs to the alphaherpesvirinae HHV-1 UL47 family."}
+{"protein": "MSSVKRSLNQEIISQFHYSAAEGDIAKLTAILSHSPSLLNETSENGWSALICDRSIVNKSRQTALDIAKFWGYKHIANLLANAKGGKKPWFLTNEVEECENYFSKTLLDRKSEKRNNSDWLLAKESHPATVYILFSDLNPLVTLGGNKESFQQPEVRLCQLNYTDIKDYLAQPEKITLIFLGVELEMKKEFFNYAGEISKEEEDGLVAWFALGIDTVAAEEFKQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKRVCLKEDCPSLHGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPGETIEDAVRREVEEESGVKVGHVQYVSCQPWPMPSSLMIGCLAVAVSTEIKVDKNEIEDARWFTREQVVDVLTKGKQQAFFVPPSRAIAHQLIKHWIGMNPNL", "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 RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Preferentially acts on NAD-capped transcripts in response to nutrient stress (By similarity). Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-ADP. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (By similarity). Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By similarity). SUBCELLULAR LOCATION: Cytoplasm Peroxisome Cytoplasmic granule Note=Localizes to cytoplasmic granules in the presence of BLMH. SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily."}
+{"protein": "MLVCNYTQKRVDMMWDAIAYNDSRKYAFMTVNARWIHADRYFDTSAQLYSYIVQNKVSDVHVKPLDDGGGREWVVDADYKNYVDEHDLMLKIYIGATAFLLFYTEENVSRVMYTGNRGFHLWLKFTDKFKITSAQNVRVHRYKAFEKPAKLDSDYIQPGSFAHCVREAVRLYVPHMQDSNLDALTLQYWPDVDRDIFCNVNKQIRAPYSYNYKGTKFSRCITKELLDKLKQCYPGYGTGGCGPVTTTTTPSPPKIGSMQTTTKSTT", "text": "FUNCTION: Plays an essential role in viral DNA replication. May 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. SIMILARITY: Belongs to the baculoviridae LEF-1 family."}
+{"protein": "MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGGPHHHHQTRGAYSSHDPQGSRGSRRRRRQRTEKKKLHHRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEEDHGDGCSYTDLLPQDDGGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLIMALSAGGHSRLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCGKEEKCQGKGDESETDKNNCSNAKAVETDV", "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:8020965). 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 (By similarity). 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:8020965). Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity). 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": "MAQNLLFCTIAFVFVAVAMAGPGGRGGPHGPGGHGPRGGPGLPPFLVNVTAAGRKEFEAVFKNETLTIAEANTQIAALAEKYGVTATYNEFVANRTALLAEVKKNQTAVIGNLTAVSAQLATIYQNKDQTRKAQEEAVDALRKEHPVEVNAIKFIRAQLGGEKVHGGSHGGLRGGPGGPRDGPRGGPRGGPRGGR", "text": "SIMILARITY: Belongs to the SXP/RAL-2 family."}
+{"protein": "MQSLWIYPEDTEVLGAACKSLLKALKPRYQKIALFSPISGGCEGFGECESLSSLEVHSAIDKQKALELVSTAQEELLFETILKRYDELQSTHDFVINLGYAPKFFLNALLDLNTILAKHLNAPVVAVAQTSLDHLKAMHSHILKKEAPFAIGLFVGETLEKPHFLSASLCKQQCELEASAIENLLQTKSEIITPLAFQRSLEKKAKKQIKKVVLPESEDERILKAAHRLNLMGAVGLILLGDKEAINSQAKNLNLNLENVEIINPNTSHYREEFAKSLYELRKSKGLSEQEAERLALDKTYFATMLVHLGYAHAMVSGVNHTTAETIRPALQIIKTKPGVSLVSSVFLMCLDTQVFVFGDCAIIPNPSPKELAEIATTSAQTAKQFNIAPKVALLSYATGNSAQGEMIDKINEALTIVQKLDPQLEIDGPLQFDASIDKGVAKKKMPNSQVAGQASVFIFPDLNAGNIAYKAVQRSAKAVAIGPILQGLNKPINDLSRGALVEDIVNTVLISAIQAQDY", "text": "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": "MVQLPAMKRVKGRAPLSVVVAIIGGLALAGIIFTEDLRGLTEVKEKVTDKEKKRTSLRTVMRTSALLSADQPPPPAVLSVEPATATPPPAPKMAFNATRCSVTDGYWAYDRSKKLPYTDQTCPYVDRQDSCQRNGRPDSDYLYWDWHLDDCLLPRFDPVSMLEKLRGKRIMFVGDSLQLGQWLSFVCLVNSAVPDTPGAKSMERSRTLSVYTVKEYNASIEFYWAPFLVESNSDRNIALGAGGRVLHVDAIEEHGKHWRRADILVFDSYVWWMTGYRIKSVWGSFGDDGYEELDAWVAYRLGLKTWANWVDSNVDPATTRVFFMSISTTHMRSEDWGREGGIRCYNETWPITQRGYRGSGSDRRMMEVMSDVLGRMRTPVTLLNITQLTEHRVDAHVSVYTETGGLLVTDEEKTDPQRYTDCIHWCIPGVPDTWNRLLYAHL", "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": "MASEKVETIVAGNYVEMEREGAATAGEGVGGAAAASGRRRGKLAVSSLFWHGGSVYDAWFSCASNQVAQVLLTLPYSFSQLGMASGVAFQVFYGLMGSWTAYLISVLYVEYRTRRERDKVDFRNHVIQWFEVLDGLLGRHWRNAGLLFNCTFLLFGSVIQLIACASNIYYINDRLDKRTWTYIFGACCATTVFVPSFHNYRVWSFLGLLMTSYTAWYLTVAAVVHGKVDGAAPRAGPSKTMVLYFTGATNILYTFGGHAVTVEIMHAMWRPRRFKMIYLAATAYVLTLTLPSAAAMYWAFGDALLDHSNAFALLPRTPWRDAAVVLMLIHQFITFGFACTPLYFVWEKAIGVHGGAGVLRRAAARLPVVLPIWFLAVIFPFFGPINSTVGSFLVSFTVYIIPAMAHMATFAPAAARENAVEPPPRALGGWPGTFAANCFVVAWVLVVGFGFGGWASTVNFVRQVDTFGLFTKCYQCPPRH", "text": "FUNCTION: Carrier protein involved in proton-driven auxin influx. May mediate the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips (By similarity). 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.18.1) subfamily."}
+{"protein": "MLNNSHLLIIWLFGLISGFNLMITGNTLNYWLAKEDIALQTIGILSFITLPYSINFLLAPIFDAVQIKYLNKIFGHRLSWICLTSTALIFLIYIFSFLDPRTNLVLFTFTALIISFFSAAQDTILSALRTEIVPKESLGFTSGIYIFGYRIGMLLAGSGAIYLSIYFTFNEIYKIFAGLVFIYLILLIVAARYTNSFGLVEERICHSPSFLCHSRGSGNPNNEFFIKRYYSNFLKIFLDSRFRGNDIKSGNDISLAYFIILILIFLVLYRLPDNLINVMINPFLLHLEYDAFEIASVGKFWGVVGAIIGGLVGGFIMKHKNILNSIFLFGIIHALGHILFIFLEINGKNSLLLFITIGIESITGGMTMTAYIAFISSLCQGKFRATQYSFLSSMMGISRSIFPIISGYMVVNFGWQNFFLFTTIITIPSLLILLKIKTKLQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MISMLRCISLFLSVILITGYFVTPVMSCNCKAPETALCARRCQQHG", "text": "FUNCTION: Neurotoxin that blocks voltage-independent calcium-activated potassium channels (KCNN1=SK1, KCNN2=SK2, KCNN3=SK3). SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MPSKESWSGRKTNRATVHKSKQEGRQQDLLIAALGMKLGSQKSSVTIWQPLKLFAYSQLTSLVRRATLKENEQIPKYEKVHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKPDLKHVKKVYSCDLTTLVKAHITKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFDRDGEKADISVNMYEDINIITGALKLYFRDLPIPLITYDAYPKFIESAKIVDPDEQLETLHEALRSLPPAHCETLRYLMAHLKRVTLHEKENLMSAENLGIVFGPTLMRSPELDPMAALNDIRYQRLVVELLIKNEDILF", "text": "FUNCTION: GTPase-activating protein for p21-rac and a phorbol ester receptor. Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance."}
+{"protein": "MYGKIIFVLLLSEIVSISASSTTGVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ", "text": "FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Appears to be colocalized with SLC4A1. SIMILARITY: Belongs to the glycophorin A family."}
+{"protein": "MRKHLLDHLKTRKILGARIAKGEKTEQDLINLNMAPQVFMFKNLFSGQVLYSQVPAFHQDQIDEQFTRPNWENRKPSRRNDLWRIMCVANFENYEYAIAAYKGLVQLRQVRDVVQKKEAKALRKKNDEGNVWFSGQYRPTYSQEAVADLSHVIDEFELEGTSVMWESLWRKGEDTHWRSDLVEHDTLPPFNPRDQTILLDELRAKAVEEFANLRQQAQQSEQQSQSELESQTA", "text": "FUNCTION: Transcription factor involved in regulation of RNA polymerase II-dependent transcription. Also involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells (By similarity). SUBCELLULAR LOCATION: Nucleus Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL67 family."}
+{"protein": "MKLPRSSLVWCVLIVCLTLLIFTYLTRKSLCEIRYRDGHREVAAFMAYESGK", "text": "FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system. Part of the plasmid-stabilizing activity of plasmid R1; when R1 is lost cells die rapidly. When overexpressed kills cells within 5 minutes; causes collapse of the transmembrane potential and arrest of respiration (PubMed:3019679). Its toxic effect is partially neutralized by antisense RNA Sok. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Hok/Gef family."}
+{"protein": "MASVALLRSFRRREVQMASVSAFKSVSANGKNSMFGKLGYLARPFCSRPVGNDVIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQKEMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGLDVQRIINEPTAAALSYGMNNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSLGIETLGAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGITTVSAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAEIASEIETAVSDLRTAMAGEDVEDIKAKVEAANKAVSKIGEHMSKGSGSSGSDGSSGEGTSGTEQTPEAEFEEASGSRK", "text": "FUNCTION: Chaperone involved in the maturation of iron-sulfur [Fe-S] cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HSCB and ISU1 (PubMed:19865480). In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable). SUBCELLULAR LOCATION: Mitochondrion Cytoplasm, cytosol. SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family. DnaK subfamily."}
+{"protein": "MNKKVVLSVLSTTLVASVAASAFAAPKDGIYIGGNIKKYYSTDVLFEMTPQAKATYASELNAMASDFNNVVFVDYKGKGASIEELFTKGSKVALGEPLKKEDFADLYKVVNKDGSSTATEDARAKVDPTPTGDLNVESVSANNLKEVVVTFDKAVDADTAGDKAYYTFTANKLAVDKVTVSGKTVVLTLAAKAENQASYELNVDGIKGLVKTTKEVKFFDNTTPTVAAVAAIGPKQVKVTFSEPLSAKPSFSVNNGAIAVVADNFVEGTKEVILTLGAQPTASTNTVTVEGGADYASYKVEKVTKDFTVVADTTPPTVSVKKASAKQVVLEFSEDVQNVQDKNVVFYHTTKGHEGYKGTILGVDGKEVTISFVNPLPEGQFKIFVDYVVDNGTQISDLWGNKLPEQVITGTFAADTTPPTVTKVEAKTNTEIHVTFSETVNGADNKANFTLKGVTGNVIPLTKAEVVDAAKNIYKVVTTEPLNGGSYYLTVKGIEDASKNKLVEYTATVAVADTVPPNVKDLDPATPGTDAQLISPTKVKIAFTEPMDKASIENKNNYMFNGFNLDSKVTLTATDSNTAVVVDFTNVVGFNGFKNGDAISVGRVLDTAGNPKTEMQTKVNLPNSVSAPLFDKAEVTGKNTVKLYFKELIINAKADDFAVDNGEGYKAVNSISNDVVENKSVITLTTGNDLPTTAAGVKVKTVGEVDAKNQYGVAVALTDVPADDKIGPNWLKAETVDTNNNGKIDQFKLTFSEALYVASVQDSDFRIEGYTIAGVETKGEVVTIKVTELDIDDSDATPTVAVIGSVEDLKRNASGPFEPQKAIDGVSAPDKEAPVVTGVEAGKTYNTAVTPDSADKDIKTVVLKKDGKELAGYALKTPISENGSYELVVTDNAGNTTTVKFKVDIPAEDKKAPEIKTVTDDKVAVADAPKWEAPKATATDDVDGDISDKIAVTYSSEDAGSKVTDLASAQTHLGTAGNTVKVTYNVTDKAGNPATAVSATFTAI", "text": "FUNCTION: The outer wall protein binds to the middle cell wall protein. SUBCELLULAR LOCATION: Secreted, cell wall, S-layer. Note=This bacterium is covered by a S-layer with hexagonal symmetry."}
+{"protein": "MSSRENYVYNRNPVFTAPKNNKRRPSFICYAMKKASEIDVARCELNYVIQPKNIKTGLPLKRFRRLNEHRACALRAMVSAMLYHFNISSELVQASVEQLSDECGLSTLSKVGNKSITRASRLITNFMEPMGFVTCKKIWDRVLGNYMPKMITLTPLFFMLLDISEKQLINAKKQQLGWINKNLITKGLKPITVIEAKRRAKDIQMRNLFKYRISKHNFYKKRKNAQRLIALDEKEARQKILRALVAKYSISELTTLGPSGLKKQVNISYYYLKKIATNRYPDN", "text": "FUNCTION: This protein is essential for plasmid replication; it is involved in copy control functions. SIMILARITY: Belongs to the IncFII RepA family."}
+{"protein": "MGTGNQTWVREFVLLGLSSDWDTEVSLFVLFLITYMVTVLGNFLIILLIRLDSRLHTPMYFFLTNLSLVDVSYATSIIPQMLAHLLAAHKAIPFVSCAAQLFFSLGLGGIEFVLLAVMAYDRYVAVCDPLRYSVIMHGGLCTRLAITSWVSGSMNSLMQTVITFQLPMCTNKYIDHISCELLAVVRLACVDTSSNEIAIMVSSIVLLMTPFCLVLLSYIQIISTILKIQSTEGRKKAFHTCASHLTVVVLCYGMAIFTYIQPRSSPSVLQEKLISLFYSVLTPMLNPMIYSVRNKEVKGAWQKLLGQLTGITSKLAT", "text": "FUNCTION: Putative odorant or sperm cell receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MGFSLTHTPHTTASPNLQLRFHSLLPPSFTSQPFLSLHSTFPPKRTVPKLRAQSENGAVLQASEEKLDASNYGRQYFPLAAVIGQDAIKTALLLGATDPRIGGIAISGRRGTAKTIMARGMHAILPPIEVVQGSIANADPSCPEEWEDGLYKRVEYDSDGNVKTHIIKSPFVQIPLGVTEDRLIGSVDVEESVKTGTTVFQPGLLAEAHRGVLYVDEINLLDEGISNLLLNVLTEGVNIVEREGISFRHPCRPLLIATYNPDEGSVREHLLDRIAINLSADLPMSFENRVEAVGIATEFQDNCGQVFKMVDEDTDNAKTQIILAREYLKDVTISKEQLKYLVIEALRGGVQGHRAELYAARVAKCLAALEGREKVYVDDLKKAVELVILPRSIITDTPPEQQNQPPPPPPPPQNQESNEEQNEEEEQEEEEEDDNDEENEQQQDQLPEEFIFDAEGGLVDEKLLFFAQQAQRRRGKAGRAKNVIFSEDRGRYIKPMLPKGPVKRLAVDATLRAAAPYQKLRREKDTENRRKVYVEKTDMRAKRMARKAGALVIFVVDASGSMALNRMQNAKGAALKLLAESYTSRDQVSIIPFRGDSAEVLLPPSRSIAMARKRLERLPCGGGSPLAHGLTTAVRVGLNAEKSGDVGRIMIVAITDGRANISLKRSNDPEAAAASDAPKPTSQELKDEIIEVAAKIYKTGMSLLVIDTENKFVSTGFAKEIARVAQGKYYYLPNASDAVVSLATREALAALKSS", "text": "FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and CHLH. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Mg-chelatase subunits D/I family."}
+{"protein": "MIHSGAVMSMSILAFCLLACIHSGINAYPAKPASPRDGAPPEELAKYYSALRHYINLITRQRYGKRDTPDTVFSDVLMRESTESIPGSNYVRYDGLPLW", "text": "FUNCTION: Gastrointestinal hormone and neuropeptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
+{"protein": "MNMANFLRGFEEKGIKNDRPEDQLSKEKKKILFSFCEVCNIQLNSAAQAQVHSNGKSHRKRVKQLSDGQPPPPAQASPSSNSSTGSTCHTTTLPALVRTPTLMMQPSLDIKPFMSFPVDSSSAVGLFPNFNTMDPVQKAVINHTFGVSIPPKKKQVISCNVCQLRFNSDSQAEAHYKGSKHAKKVKALDATKNKPKMVPSKDSAKANPSCSITPITGNNSDKSEDKGKLKASSSSQPSSSESGSFLLKSGTTPLPPGAATSPSKSTNGAPGTVVESEEEKAKKLLYCSLCKVAVNSLSQLEAHNTGSKHKTMVEARNGAGPIKSYPRPGSRLKMQNGSKGSGLQNKTFHCEICDVHVNSEIQLKQHISSRRHKDRVAGKPLKPKYSPYNKLQRSPSILAAKLAFQKDMMKPLAPAFLSSPLAAAAAVSSALSLPPRPSASLFQAPAIPPALLRPGHGPIRATPASILFAPY", "text": "FUNCTION: May play a role in p53/TP53-mediated apoptosis. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MGGSASSQLDEGKCAYIRGKTEAAIKNFSPYYSRQYSVAFCNHVRTEVEQQRDLTSQFLKTKPPLAPGTILYEAELSQFSEDIKKWKERYVVVKNDYAVESYENKEAYQRGAAPKCRILPAGGKVLTSEDEYNLLSDRHFPDPLASSEKENTQPFVVLPKEFPVYLWQPFFRHGYFCFHEAADQKRFSALLSDCVRHLNHDYMKQMTFEAQAFLEAVQFFRQEKGHYGSWEMITGDEIQILSNLVMEELLPTLQTDLLPKMKGKKNDRKRTWLGLLEEAYTLVQHQVSEGLSALKEECRALTKGLEGTIRSDMDQIVNSKNYLIGKIKAMVAQPAEKSCLESVQPFLASILEELMGPVSSGFSEVRVLFEKEVNEVSQNFQTTKDSVQLKEHLDRLMNLPLHSVKMEPCYTKVNLLHERLQDLKSRFRFPHIDLVVQRTQNYMQELMENAVFTFEQLLSPHLQGEASKTAVAIEKVKLRVLKQYDYDSSTIRKKIFQEALVQITLPTVQKALASTCKPELQKYEQFIFADHTNMIHVENVYEEILHQILLDETLKVIKEAAILKKHNLFEDNMALPSESVSSLTDLKPPTGSNQASPARRASAILPGVLGSETLSNEVFQESEEEKQPEVPSSLAKGESLSLPGPSPPPDGTEQVIISRVDDPVVNPVATEDTAGLPGTCSSELEFGGTLEDEEPAQEEPEPITASGSLKALRKLLTASVEVPVDSAPVMEEDTNGESHVPQENEEEEEKEPSQAAAIHPDNCEESEVSEREAQPPCPEAHGEELGGFPEVGSPASPPASGGLTEEPLGPMEGELPGEACTLTAHEGRGGKCTEEGDASQQEGCTLGSDPICLSESQVSEEQEEMGGQSSAAQATASVNAEEIKVARIHECQWVVEDAPNPDVLLSHKDDVKEGEGGQESFPELPSEE", "text": "FUNCTION: Regulates phosphorylation of a number of proteins involved in translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be involved in the endoplasmic reticulum stress response (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Lipid-anchor. SIMILARITY: Belongs to the Niban family."}
+{"protein": "MEGEELIYHNIINEILVGYIKYYMNDISEHELSPYQQQIKKILTYYDDCLNKQVTITFSLTSAQEIKTQFTEVVTELFKDLINWGRICGFIVFSARMAKYCKDANNHLESTVITTAYNFMKHNLLPWMISHGGQEEFLAFSLHSDIYSVIFNIKYFLSKFCNHMFLKSCVHLLRNCNLI", "text": "FUNCTION: Suppresses apoptosis in host cell to promote the viral replication (By similarity). Has the ability to potentially bind to all the members of the proapoptotic Bcl-2 family (By similarity). Inhibits autophagy by interacting with host Beclin 1 (BECN1) (By similarity). SUBCELLULAR LOCATION: Host mitochondrion Host endoplasmic reticulum. SIMILARITY: Belongs to the Bcl-2 family."}
+{"protein": "MQIVNLTRRGFLKAACVVTGGALISIRMTGKAVAAAKQLKDYMMDRINGVYGADAKFPVRASQDNVQVQKLYADFLEKPMSHKAEQLLHTHWVDRSKAIERMKAQGAYPNPRAKEFEGNTYPYE", "text": "FUNCTION: May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme. SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MEPLTIVSLAVASFLLFAFWALSPKTSKNLPPGPPKLPIIGNIHQLKSPTPHRVLRNLAKKYGPIMHLQLGQVSTVVVSTPRLAREIMKTNDISFADRPTTTTSQIFFYKAQDIGWAPYGEYWRQMKKICTLELLSAKKVRSFSSIREEELRRISKVLESKAGTPVNFTEMTVEMVNNVICKATLGDSCKDQATLIEVLYDVLKTLSAFNLASYYPGLQFLNVILGKKAKWLKMQKQLDDILEDVLKEHRSKGRNKSDQEDLVDVLLRVKDTGGLDFTVTDEHVKAVVLDMLTAGTDTSSATLEWAMTELMRNPHMMKRAQEEVRSVVKGDTITETDLQSLHYLKLIVKETLRLHAPTPLLVPRECRQACNVDGYDIPAKTKILVNAWACGTDPDSWKDAESFIPERFENCPINYMGADFEFIPFGAGRRICPGLTFGLSMVEYPLANFLYHFDWKLPNGLKPHELDITEITGISTSLKHQLKIVPILKS", "text": "FUNCTION: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones (PubMed:30468448). Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti- cancer drugs highly active against colon cancer cells (PubMed:30468448). Hydroxylates germacrene A acid to 6-alpha-hydroxy- germacrne A acid, a precursor of sesquiterpene lactones that spontaneously undergoes a lactonization which yields costunolide (PubMed:21515683). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MADLHQKQIIDKLQHIIFKDGTFLNKVISDIIIKGNNIGFSIDISGKNKLEAEELKAKAIDKLNEISEINKITIVFTESKPMEKKAQKPKHFVENVKKIILVASGKGGVGKSTISALIAQQLSLENYRVGIVDADIYGPSIPHIFGINEVPKTKDGRIIPITVKSIQVISIGFFVKDHSAIIWRGPMASKTIYQLLSVTKWDNLDYLIIDMPPGTGDIHLSMLENYHLDGVIIVTTPQKISEIDVIRSIDLYQKLNLPILGIIENMSYMFESNSGGHLSQKYNIPLIAQIPIMPQIADACDKSLPLTDLLTLPLKEYL", "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": "MGFKLVLFIAVLTLVGSSNAEISAKMDSRDSPMIQERRCLPAGKTCVRGPMRVPCCGSCSQNKCT", "text": "FUNCTION: Possesses strong antiplasmodial activity against the intra- erythrocyte stage of P.falciparum in vitro. IC(50) for inhibiting P.falciparum growth is 1.15 uM. Specifically interacts with infected erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. Has neither antibacterial nor antifungal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 36 family. 02 subfamily."}
+{"protein": "MSATDRYSHQLLYATVRQRLLDDIAQGVYQAGQQIPTENELCTQYNVSRITIRKAISDLVADGVLIRWQGKGTFVQSQKVENALLTVSGFTDFGVSQGKSTKEKVIEQERVSAAPFCEKLNIPGNSEVFHLCRVMYLDKEPLFIDSSWIPLSRYPDFDEIYVEGSSTYQLFQERFDTRVVSDKKTIDIFAATRPQAKWLKCELGEPLFRISKIAFDQNDKPVHVSELFCRANRITLTIDNKRH", "text": "FUNCTION: May regulate the transcription of the frlABCDR operon, involved in the utilization of fructoselysine and psicoselysine."}
+{"protein": "MDPDAVKSTLSNLAFGNVMAAAARNYQKEVLANEKAQGSNPVNEEVDLDELMDDPELERLHADRIAALKREVEKRESFKRQGHGEYREVSEGDFLGEVTRSEKVICHFYHKEFYRCKIMDKHLKTLAPRHVDTKFIKVDAENAPFFVTKLAIKTLPCVVLFSKGVAMDRLVGFQDLGTKDDFTTNKLENVLLKKGMLSKKKKEEDDEDAEYQESIRRSVRSSENLDSDSD", "text": "FUNCTION: Tubulin-binding protein involved in microtubule formation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the phosducin family."}
+{"protein": "MGGLEKKKYERGSATNYITRNKARKKLQLSLPDFRRLCILKGIYPHEPKHKKKVNKGSTAARTFYLIKDIKFLLHEPIVNKFREYKVFVRKLRKAYGKSEWNAVERLKDNKPCYKLDHIVKERYPTFIDALRDLDDALSMCFLFSTFPRTGKCHVQTIQLCRRLTVEFLHYVITARALRKVFLSIKGIYYQAEVLGQPIVWIAPYAFSHDHPTDVDYRVMATFTEFYTTLLGFVNFRLYQSLNLHYPPKLEGQAQAETKISEDTYALDSESSMEKLAALSASLARVVVPAIEEAEADEFPTDGEVTAQEEDRKKELEAQEKHKKLFEGLKFFLNREVPREALAFIIRSFGGDVSWDKSLCIGATYDVTDSCITHQIVDRPGQQTPIIGRYYVQPQWVFDCVNARLLLPVAEYFPGMQLPPHLSPFVSEKEGDYIPPEKLKLLALQRGEDPGHLEEEEEEDEDDDNEGDVAAENEEEDVEVESEEEEEEEVHLSALEQHRLEEKKPQVMAGTVKLEDKQRLAQEEESEAKRLAIMMMKKREKYLYQKIMFGKRRKIREANKLAEKRKAHDDAVRSEKKAKRTRPV", "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. Chromosome. Note=Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli. SIMILARITY: Belongs to the pescadillo family."}
+{"protein": "MEVKIFAFLQIAVLIAFSLHLASAGSKELSGPESSENSIEAAFCDTNCTEGTDGVWSGCSAGCFCVHVGNSTVGRCMTFNGVD", "text": "FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL10, CXCL11 and CXCL13. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MEIPVSVQPSWLRRASAPLPGLSAPGRLFDQRFGEGLLEAELAALCPAALAPYYLRAPSVALPTAQVSTDPGHFSVLLDVKHFSPEEIAVKVVGDHVEVHARHEERPDEHGYIAREFHRRYRLPPGVDPAAVTSALSPEGVLSIQAAPAPAQAPLQSPPGAAAK", "text": "FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus Secreted Note=Translocates to nuclear foci during heat shock. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MTAEDSTAAMSSDSAAGSSAKVPEGVAGAPNEAALLALMERTGYSMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPVDKEQYSRYQKAARGGGAAEAAQQPSYVYSCDPYTLAYYGYPYNALIGPNRDYFVKAGSIRGRGRGAAGNRAPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEIPTVNPVAIKPGTVAIPAIGAQYSMFPAAPAPKMIEDGKIHTVEHMISPIAVQPDPASAAAAAAAAAAAAAAVIPTVSTPPPFQGRPITPVYTVAPNVQRIPTAGIYGASYVPFAAPATATIATLQKNAAAAAAMYGGYAGYIPQAFPAAAIQVPIPDVYQTY", "text": "FUNCTION: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing (PubMed:24038582, PubMed:24916387, PubMed:27050523, PubMed:30844405, PubMed:31358901, PubMed:34160127). Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules (PubMed:24038582, PubMed:24916387, PubMed:30844405). Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10 (PubMed:34160127). Also involved in the alternative splicing of several genes including TJP1. Binds the pre- mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs (PubMed:31358901, PubMed:27050523). Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RRM RBM47 family."}
+{"protein": "MKRVLTALAATLPFAANAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFSEAMAVHPKGVDIMKPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPEYKDAAGHLIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFKKGATEREELRVSKITVLILGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMMGGWLGLITAVVLMILGPTIWVQILGHEKAIFPYEYPALFSITVAFLGIWFFSATDNSAEGARERELFRAQFIRSQTGFGVEQGRAH", "text": "FUNCTION: Transports acetate. Also able to transport glycolate. FUNCTION: Transports acetate. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family."}
+{"protein": "MNQPIYTELPPANFPGEFPVYRRNSSFSRLIPCLTETWGDLPLKVDDSEDMVIYTLLKDALNVGWSPFNFSAGEVKSEQREEEIVVSPAETTAAPAAELPRGRHYRGVRRRPWGKFAAEIRDPAKNGARVWLGTYETDEEAAIAYDKAAYRMRGSKAHLNFPHRIGLNEPEPVRVTAKRRASPEPASSSENSSPKRRRKAVATEKSEAVEVESKSNVLQTGCQVELLTRRHQLLVS", "text": "FUNCTION: Probably acts as a transcriptional activator and may be involved in disease resistance pathways (By similarity). Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways mediated by ethylene, that seems to depend on a protein kinase cascade and to be influenced by methyl- jasmonate. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ethylene-response factor family. Class 1 subfamily."}
+{"protein": "MSIIFQLALIALVLFSFVMVIGVPVAYASPQNWNQSKPLLYLGSAIWAILVVIVAILNFFVI", "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": "MGVLVVLLGVLSFLGRTLGGSPALHWDSTSCHLARPIPGRPLRSLSFLGKDAQGLALFHAHWDGHGRLQVCSRQDEPELTAAYGALCAGEITRGSFIHTPGPELQRALATLQSQWEACRGPAESPAGTREKRAAGQNGVPGIGRQWVKRGWTVPGTLWCGVGDSAGNSSELGVFQGPDLCCREHDRCPHNVSPFQYNYGIRNYRFHTISHCNCDARFQQCLQDQRDSVSDIMGVAFFNVLAIPCFVLEEQEACVEWYWWGGCRRYGSVPFARLQPRTFYNASWSSPATSLTPSPQNPALSRPQPMQHPQQWPSEWKESKSPSKTNATALQAPVASPGSDRASTVQLEVTHPGFQGTTGGRKPPGAHRACRSFRHLDQCEHQIGPQETKFQLFNSAHEPLFHCNCTRRLARFLRLHGPPVGASMLWELPGMTCFKLAPPLDCAEGKGCPRDPRAFKVSARHLLRLQQRRLQLQGTGTDNGQVWPSEDQGAPISFYNRCLQLT", "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 (By similarity). 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 (By similarity). May act in an autocrine and paracrine manner. 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 (By similarity). 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 (By similarity). Coupled to cyclooxygenase pathway provides arachidonate to generate prostaglandin E2 (PGE2), a potent immunomodulatory lipid in inflammation and tumorigenesis (By similarity). 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 (By similarity). Releases C16:0 and C18:0 lysophosphatidylcholine subclasses from neuron plasma membranes and promotes neurite outgrowth and neuron survival (By similarity). 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": "MDENPEFAAIEQARDLVIDSIAETMDLYGITRSVGILYGTMYMRDEMTLDEMREELQMSKPSMSTGVKKLQDLNVVKKTFHRGIRKHTFVAEKDFFKFFTNFFPPKWEREVQVNVTAIEEAQADLQKVLCKEDLDEDIKNEALQLYDQLESSKAYYDWLKRLAESVQTGEIFKFIPVETK", "text": "FUNCTION: Negatively regulates the expression of the gbsAB and opuB operons. Required to control expression of these genes in response to choline availability. Also required to down-regulate glycine betaine production once cellular adjustment to high osmolarity has been achieved. SIMILARITY: Belongs to the GbsR family."}
+{"protein": "MPAINAKRVYRIMRQNALLLERKPAVPPSKRAHTGRVAVKESNQRWCSDGFEFCCDNGERLRVTFALDCCDREALHWAVTTGGFNSETVQDVMLGAVERRFGNDLPSSPVEWLTDNGSCYRANETRQFARMLGLEPKNTAVRSPESNGIAESFVKTIKRDYISIMPKPDGLTAAKNLAEAFEHYNEWHPHSALGYRSPREYLRQRACNGLSDNRCLEI", "text": "FUNCTION: Involved in the transposition of the insertion sequence IS2."}
+{"protein": "MQFSKITLAIVLYALGTAALPTASRCAGAPGRDVAATRGAKLQAREEDKPTPQYRCDKCEKEFVKGNDFFNHGGRGHCKMSGY", "text": "FUNCTION: Probable secreted effector that translocates into the nuclei of host cells to reprogram the expression of targeted genes by binding on effector binding elements in rice. SUBCELLULAR LOCATION: Secreted Host nucleus."}
+{"protein": "MFVSRLAASGLLLLSLLALSLDGKPLPQRQPHHIQPMEQKWLAPDAPPLEQKWLAPDAPPLEQKWLAPAAPPLEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAAPLEQKWLAPDAPPMEQKWLAPDAPPMEQKWQPQIPSLMEQRQLSSGGTTALRQELSPRAEAASGPAVVGGGGGGGGGSKAALALPKPPKAKGAAAATSRLMRDLRPDGKQASQKWGRLVDHDHDHHHHHHPGSSVGGGGGGGGGGARRLKGLAKKGVAKGCFGLKLDRIGSMSGLGC", "text": "FUNCTION: pEKW and poly-His-poly-Gly 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 prey. FUNCTION: [C-type natriuretic peptide]: Exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3). SUBCELLULAR LOCATION: Secreted. SIMILARITY: In the C-terminal section; belongs to the natriuretic peptide family. SIMILARITY: In the central section; belongs to the pHpG family."}
+{"protein": "MNAITIFFIILSTVAVCIIIFQLYSIYLNYDNIKEFNSAHSAFEFSKSVNTLSLDRTIKDPNDDIYDPKQKWRCVKLDNDYVSVSMFGFKSNGSEIRKFKNLESCIDYTFSQSTHSDIKNPCILQNGIKSKECIFLKSMF", "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": "MNNAPHLYFAWQQLVEKSQLMLRLATEEQWDELIASEMAYVNAVQEIAHLTEEVAPSTTMQEQLRPMLHLILDNESKVKQLLQIRMDELAKLVGQSSVQKSVLSAYGDQGGFVLAPQDNLF", "text": "FUNCTION: Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the FliT family."}
+{"protein": "MNLRPVIVGGGSAGMAAAIELARRGVPCVLFDEASRPGGVVYRGPLRAGVDPAYLGARYTRMLEKLRRDFSACAGHIDLRLNSRVVGGDGQRLMVLDEAERLHEVEYSHLLLATGCHERSVPFPGWTLPGVMLLGGLQLQIKSGVVKPLGDTLIAGSGPLLPLVACQLHAAGVRVAGVYEACAFGRMARESLALLNKPQLFLDGLSMLGYLKLNGIPLHYGWGVVEASGDGELTEVTVAPYDEEWRPDLENARPVKASTLAVGYGFIPRTQLSQQLGLEHGFSDDGYLRAECNVWQQSSQPHIHLAGDMAGIRGGEAAMIGGRIAALSILLQREAIAPAEAIERRESHLARLEAIKRFRAGVERYTQRGARQVELARADTVICRCEQVTRGDIERALEQGVQDIAGLKMRTRAGMGDCQGRMCIGYCSDRLRRATGRHDVGWLRPRFPIDPIPFSAFQNLGTEA", "text": "FUNCTION: A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain. SUBCELLULAR LOCATION: Cell membrane."}
+{"protein": "MADDYRRSVELERRIFELDNKCATLRTEKPDDDYLQNASSILDKLKTYYRHGGESSSLPKLLQDYTQVVLDITFYEENKLVDQEFPEDSSPFKIQQLLQDLTEPEVLAGRLVPAQEVQSVLGLELLECLYWRRGALLYMYCHTLHQRKQWIKKNKATFLKCLQEGVRYLMRMLQVRNSVKLNDGVVFHDSATANFLAEGIFSDTHLLTMMYIGEMCFWAVKYEDCSMDTTERKEDRLHFRDIGTQILHKYVLACEGPLQGQGWNTENAKEILSILQ", "text": "FUNCTION: Plays an important role in the removal of damaged mitochondria via mitophagy by controlling the stability and localization of RAB7A (By similarity). Required for the recruitment of RAB7A and ATG9A vesicles to damaged mitochondria and promotes the stability of RAB7A by inhibiting its proteasomal degradation during mitophagy (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the RIMOC1 family."}
+{"protein": "APEESPKRAPSGFLGVR", "text": "FUNCTION: Myoactive peptide. Increases the amplitude and frequency of spontaneous contractions and tonus of hindgut muscle. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MDNKSNGKLIALAIGGAVLMGTLFFLVSFLTGYSPAPNHSAILTPLRSFMGWFLLIFCASLIIMGLGKMSGAISDKWFLSFPLSIFVIVMVMFFSLRFYWEKGRTTTVDGKYIRSVEQLNDFLNKPAATSDLPPVPADFDFAAAEKLTDAKCNKCHTLGSVADLFRTKYKKTGQVKLIVKRMQGFPGANISDDEVIEIGTWLQEKF", "text": "FUNCTION: Monoheme cytochrome which is the immediate electron donor to P840 of the photosynthetic reaction center complex. FUNCTION: Monoheme cytochrome which is the immediate electron donor to P840 of the photosynthetic reaction center complex. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MTIKDESESCGSRAVVASPSQENPRHYRMKLDVYSEVLQRLQESNYEEATLPDFEDQLWLHFNRLPARYALDVKVERAEDVLTHQRLLKLAADPATRPVFEVRSVQVSPRISADSDPAVEEDAQSSHQPSGPGVLAPPTFGSSPNFEAITQGSKIVEDVDSVVNATLSTRPMHEITFSTIDKPKLLSQLTSLLGELGLNIQEAHAFSTVDGFSLDVFVVDGWSQEETDGLRDALSKEILKLKDQPGSKQKSISFFEHDKSSNELIPACIEIPTDGTDEWEIDVTQLKIEKKVASGSYGDLHRGTYCSQEVAIKFLKPDRVNNEMLREFSQEVFIMRKVRHKNVVQFLGACTRSPTLCIVTEFMARGSIYDFLHKQKCAFKLQTLLKVALDVAKGMSYLHQNNIIHRDLKTANLLMDEHGLVKVADFGVARVQIESGVMTAETGTYRWMAPEVIEHKPYNHKADVFSYAIVLWELLTGDIPYAFLTPLQAAVGVVQKGLRPKIPKKTHPKVKGLLERCWHQDPEQRPLFEEIIEMLQQIMKEVNVVV", "text": "FUNCTION: Serine/threonine protein kinase that specifically phosphorylates chloroplast precursor proteins in the cytosol within the cleavable presequences (transit peptides). May be part of a cytosolic regulatory network involved in chloroplast protein import. Does not phosphorylate mitochondrion precursor proteins. Specific for ATP and does not utilize other NTPs (PubMed:17090544, PubMed:16429265). Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins (PubMed:21799034). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MNNYFIGKVLSGHHINNNGNGNTLSRTALTPTNNNVNRGDLVTNGLTPIDNNFIGSNGFIPRNVTRKDPFRKRTTQEFIREWTEWKEKSASLFTAPIVGVITSTLLEALKKLVAGRVLMSLTNLLFPNNSTSTMEEILRATEQYIQEQLDTVTWNRVSQELEGLKNDLRTFNDQIDDFLQNRVGISPLAIIDSINTMQQLFVNRLPQFQVSDDQVLLLPLFAQAVTLHLTFVRDIIINADEWNIPEAQLNTYKRYLKQYVAQYSNYALSTYEEAFRARFYPRNTVENMLEFKTFMTLNVLDLVSMWSLLKYVNLYVSTSANLYNIGDNKVNEGEYSISYWPFFNTYIQTKSNYVLSGVSGYAMRWSYTNPFFGEYIQDHLYNITASYIGGVNGPQIGQQLSTTELDQLVQQQARADIPVDFTQIPINCTLRNPLEVPYYATRFNELTSLGTAGVGGFVRSDVFISNDSVCGLGTNYSSGQTFYPDYYITNISATVQVNGTNTDISPLYFGENRAITSTNGVNKVIAIYNRKTNYDDFTNIRGTIVHEAPTDSTGFTISPLHLDTVNINSYLYIQENYGNNGDSLRVINRAIIKYRLSAARSVIYRLVLRVSGTASSIVAIYENYPVGSANQINTGTDNEGVIDNDSKFIDLIFNTPFSVSGTARELQLQVSGATTSSPLDIMNIILIPINDVPLY", "text": "FUNCTION: Binds to the brush border membrane vesicles of scarab larvae and damages the gut wall somehow to allow the vegetative cells of P.popilliae to enter the hemolymph. SIMILARITY: Belongs to the delta endotoxin family."}
+{"protein": "MASFSEEAMDSYMYPAYNPYSYRYMTPKNKGMSWRQKNYLASYGDTGDYYDNYQRAQLKAILSQVNPNLTPRLRKANTRDVGVQVNPRQDASVQCSLGPRTLLRRRPGALRKPQQSPPEQGSPASPTKTVRFPRTIAVYSPVAAGRLAPFQDKGENLSEKTEALRSEGSRGEGGRPEGKQEDGEIKEQTKMDKADQEEVAPDQTRPKFQFLEQKYGYYHCKDCNIRWESAYVWCVQGTNKVYFKQFCRTCQKSYNPYRVEDIMCQSCKQTRCMCPVKLRHVDPKRPHRQDLCGRCKGKRLSCDSTFSFKYII", "text": "FUNCTION: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation (By similarity). Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similarity). Binds to the 3'-UTR of maternal mRNAs in immature oocytes, inhibiting their translation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule. SIMILARITY: Belongs to the ZAR1 family."}
+{"protein": "MNSRIMFIGGVPGVGKTSISGYIARNTDIDIVLSSDYLREFLRPFAPQESHLETSVYDAWKFYGDMSDDNIIRGYLDQARPIMGGINRVIARALANGEDLIIESLYFVPDMMDEMVLKNAFLAYVYIDDPDLHRSRLEDRINYTHRNSPGSRLAAHLKEYRTIMDYSMDMARGRGIGLYSTDDYALARQRLLDDFRKFVDRR", "text": "FUNCTION: Phosphorylates mevalonate 3-phosphate to form mevalonate 3,5- bisphosphate. 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."}
+{"protein": "MGKAASAKKVLERVPISKPPFEYNDLKKAVPPHCFSRPLSRSLYFLFHDIIVTCILFYVASNYIHMLPRFLSCIVWPVYWISQGVFLGRLWMIGHECGHHSFSNYRWVDDTVGFLIHTATLTPYFSFKYSHRNHHAHTNSMEYDEVHIPKRKSEALYFEFLGNNPIGLMITMLCKLTFGYAAYIMFNYTGKKHKSGGLASHFYPQSPLFNDSERNHVLFSDIGICIVLYACYRIVTVTGAMPAFYVYGIPWVIMSAILFAATYLQHTHPSIPHYDTTEWNWLRGALSTIDRDLGFFNMNKTHYHVIHHLFPVIPEYHAQEATEAIKPILGQYYKYDGTPFLKALWREMKECIYVESDEGQKKQGIYWFKNKT", "text": "FUNCTION: Fatty acid conjugase converting 18:2(9Z, 12Z) to calendic acid 18:3(8E, 10E, 12Z) (PubMed:11067856). Converts alpha-linolenic acid (18:3(9Z, 12Z, 15Z)) into 18:4(8E, 10E, 12Z, 15Z) (PubMed:11067856). Also has weak activity on the mono-unsaturates 16:1(9Z) and 18:1(9Z) producing two conjugated double bonds at delta(8) and delta(10) position (By similarity). SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
+{"protein": "MATEPPSPLRVEAPGPPEMRTSPAIESTPEGTPQPAGGRLRFLNGCVPLSHQVAGHMYGKDKVGILQHPDGTVLKQLQPPPRGPRELEFYNMVYAADCFDGVLLELRKYLPKYYGIWSPPTAPNDLYLKLEDVTHKFNKPCIMDVKIGQKSYDPFASSEKIQQQVSKYPLMEEIGFLVLGMRVYHVHSDSYETENQHYGRSLTKETIKDGVSRFFHNGYCLRKDAVAASIQKIEKILQWFENQKQLNFYASSLLFVYEGSSQPTTTKLNDRTLAEKFLSKGQLSDTEVLEYNNNFHVLSSTANGKIESSVGKSLSKMYARHRKIYTKKHHSQTSLKVENLEQDNGWKSMSQEHLNGNVLSQLEKVFYHLPTGCQEIAEVEVRMIDFAHVFPSNTIDEGYVYGLKHLISVLRSILDN", "text": "FUNCTION: Inositol phosphate kinase with a broad substrate specificity (PubMed:12027805, PubMed:12223481, PubMed:28882892, PubMed:30420721, PubMed:30624931). Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) first to inositol 1,3,4,5-tetrakisphosphate and then to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) (PubMed:12027805, PubMed:12223481, PubMed:28882892, PubMed:30624931). Phosphorylates inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) (PubMed:12223481). Phosphorylates glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate to glycero-3-phospho-1D-myo-inositol 3,4,5- trisphosphate (PubMed:30420721, PubMed:28882892). Plays an important role in MLKL-mediated necroptosis via its role in the biosynthesis of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Binding of these highly phosphorylated inositol phosphates to MLKL mediates the release of an N-terminal auto-inhibitory region, leading to activation of the kinase. Essential for activated phospho- MLKL to oligomerize and localize to the cell membrane during necroptosis (PubMed:29883610). Required for normal embryonic development, probably via its role in the biosynthesis of inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) and inositol hexakisphosphate (InsP6) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family."}
+{"protein": "MLEFFRPPRARSPRELVQLLPEAWTTSRSSTGSANPSASRKPARYPRIHAPELQSGEARWPLWSRIRPLEDPLKQRLTNLEKKITNVTTKFEQIEKCCKRNDEVLFRLENHAETLRAAMISLAKKIDVQTGRRPYE", "text": "FUNCTION: This protein appears to play an important role in virus penetration at the level of cell fusion. The N-terminal proximal region is essential for fusion ability. Essential in fusing the outermost of the two Golgi-derived membranes enveloping the virus with the plasma membrane, and in its subsequent release extracellularly. SUBCELLULAR LOCATION: Virion membrane. Note=Envelope fraction of virions. SIMILARITY: Belongs to the poxviruses fusion protein family."}
+{"protein": "MKSNSKVNINNNGDNHNQTKNNGTNGFLPNSLKFISTCIRTASSGVRSASASVAASLSSDSHELKDQVLWSSFDRLHTSESSFKNVLLLGYTNGFQVLDIDDSNDVTEFVSRRDDPVTFLQMQPLPAKCDGVEGFRSSHPILLAVADEAKGSGPIVTSRDGSVRNGYEDPLALSPTVVRFYSLRSHNYVHVLRFRSTVYMVRCSPRIVAVGLGSQIYCFDALTLENKFSVLSYPVPQLGNQGISGVNVGYGPMAVGARWLAYASNSPLSSSIGRLSPQNVTPPGVSPSTSPNNGNLVARYAMESSKHLAAGLLNLGDKGYKTISKYCQDLKHDGPGPSLSSSPGRKVGRVGSHSAESDVVGTVIVKDFESRAIIAQFRAHTSPISALCFDPSGTLLVTASIHGNNINVFRIMPTPTKNGPGAQSYDWSSSHVPLYKLHRGMTSAVIQDICFSSYSQWIAIVSSKSTCHIYVLSPFGGENVLEIRNSQFDGPTLAPTLSLPWWSSPSFMTTHFSYPPPASVTLSVVSRIKCNNFFHAASSVVGKPTFPSGCLAAVFHQSVPQESQSSSPALDYLLVYTPSGHVVQYKLIPSLGGDQAESNTRNGATSGLTSEEELRVKVEPVQCWDVCRRADWPEREENICGLTYGGRKNAELTVDTSDSEDQTKPLEKHHVYLANAEVLINSGRKPIWQNSEISFYPMYPPDSDGKNLNSHQGGGETEIGKVSANEVDIRRKDLLPVYDNFHSVYTSMRNRGFSGERDSDSSSSSDPGQVKEMHPFNGMVYPEDEERRGSAHFALTPNQNPHTGIVTFKQPVVSISSAVKDTDYIDDDAHVLPKNASLPAETKIENSSGISGDSNVSSNRSDMSMNAADEGEGPIDGSPNFEQFFEEVVSNETVTETEHKDAPSDGKLDDDEDDDMLGGVFAFSEEG", "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": "MAVQLKWPILGVIIPCIIIFSLSYGSHYFILRHHLTMKQQLIYEFYVTMIWISYLLAIYTNPGRVPKNYKPSLASSTRIEQTEDDSDGLGLESREDETLIREEPISGDRCEWIRYCKKCNNYKPPRSHHCKICQQCVLQMDHHCPWTLNCVGNNNLPHFMRFLGWIIWGTGYLMIQLIKLIINYYENSNMPHYLFNKTELVAIIAITPLNFFVFASILVLFIRCLINICKGMTQIEIWEWERLELQWSSKRLWRLIRFNYGRLHKGKPFPELNTWTNTTNNVNYNDNDDDGDEDVELINLATNNNEDSTIVPQNFTIDDLIFPYNLGIWKNLVNALGYPYMWLIPFGKPKSNGYQPQISQDYKQDDQLNLPWPPDGIRQKEIEINVLQQQGYQRDREEEDEEELRSIRNYQELRRRLDPRLNVQRSDFINDMGEGLTDFGVDEDSD", "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": "MQAAVAVSVPFLLLCVLGTCPPARCGQAGDASLMELEKRKENRFVERQSIVPLRLIYRSGGEDESRHDALDTRVRGDLGGPQLTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVKGGEHCYYQGHIRGNPDSFVALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVYKSRLFEFSLDDLPSEFQQVNITPSKFILKPRPKRSKRQLRRYPRNVEEETKYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRDFIKEKSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECVLEGAECCKKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIHKMDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPVASFNFSTCLSSKEGTICSGNGVCSNELKCVCNRHWIGSDCNTYFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQGDYVKKPGDGDSFYSDIPPGVSTNSASSSKKRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNLGGNKKKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEDKKVNRQSARLWETSI", "text": "FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein (PubMed:19692335). Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation. Neuronal receptor for LGI1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon."}
+{"protein": "MKAGCSIVEKPEGGGGYQFPDWAYKTESSPGSRQIQLWHFILELLQKEEFRHVIAWQQGEYGEFVIKDPDEVARLWGRRKCKPQMNYDKLSRALRYYYNKRILHKTKGKRFTYKFNFNKLVMPNYPFINIRSSGVVPQSAPPVPTASSRFHFPPLDTHSPTNDVQPGRFSASSLTASGQESSNGTDRKTELSELEDGSAADWRRGVDPVSSRNAIGGGGIGHQKRKPDIMLPLFARPGMYPDPHSPFAVSPIPGRGGVLNVPISPALSLTPTIFSYSPSPGLSPFTSSSCFSFNPEEMKHYLHSQACSVFNYHLSPRTFPRYPGLMVPPLQCQMHPEESTQFSIKLQPPPVGRKNRERVESSEESAPVTTPTMASIPPRIKVEPASEKDPESLRQSAREKEEHTQEEGTVPSRTIEEEKGTIFARPAAPPIWPSVPISTPSGEPLEVTEDSEDRPGKEPSAPEKKEDALMPPKLRLKRRWNDDPEARELSKSGKFLWNGSGPQGLATAAADA", "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": "MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM", "text": "FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:10759893, PubMed:11897662, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:16151251, PubMed:21454524). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198). Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51 (PubMed:29478807). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol (PubMed:21454524, PubMed:29408485). Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit (PubMed:15621527). FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. May also cooperate with HIRA to promote replication-independent chromatin assembly. SUBCELLULAR LOCATION: Nucleus Chromosome. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ASF1 family."}
+{"protein": "GFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSSGIYHVTNDCPNSSIVYETADTILHSPGCVPCVREGNASKCWVPVAPTVATRDGNLPATQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQDCNCSIYPGHITGHRMAWDMMMNWSPTAALVMAQLLRIPQAILDMIAGAHWGVLAGIAYFSMVGNWAKVLVVLLLFAGVDATTYTTGGNAARTTQALTSFFSPGAKQDIQLINTNGSWHINRTALNCNASLDTGW", "text": "FUNCTION: [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). FUNCTION: [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Virion membrane; Single-pass type I membrane protein Host endoplasmic reticulum membrane; Single-pass type I membrane protein Host lipid droplet Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). SUBCELLULAR LOCATION: [Mature core protein]: Virion Host cytoplasm Host nucleus Host lipid droplet Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). SUBCELLULAR LOCATION: [Envelope glycoprotein E1]: Virion membrane; Single-pass type I membrane protein Host endoplasmic reticulum membrane; Single-pass type I membrane protein Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane; Single-pass membrane protein Host mitochondrion membrane; Single-pass type I membrane protein Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. SIMILARITY: Belongs to the hepacivirus polyprotein family."}
+{"protein": "MTALGITVALLVWLVTLLLISIWKHIHSSWKLPPGPFPLPIVGNIFQLDLKNIPKSFTMLAERYGPVFTVYLGSRRIVVLHGYKAVKEVLLHYKNEFSGRGEIPTFQVHKDKGVIFNNGPTWRDTRRFSLTTLRDFGMGKQGNEQRIQREAHFLLEALRKTHGQPFDPTFLIGCAPCNVISDILFRQHFDYNDKTCLRLMSMFNENFYLLSTGWIQLYNNFSGYLRYLPGSHRKLMKNISEIKDYALERVKDHRDSLEPSCPRDFTDTLLMEMEKEKYSAEPIYTLDNIAVTVADMFFAGTETTSTTLRYGLLILMKYPEVEEKLHEEIDRVIGPNRIPAIKDRLVMPYLDAVVHEIQRFIDLIPSNLPHEATRDTDFRDYIIPKGTVVIPTLDSVLYDSQEFPEPEKFKPEHFLNENGKFKYSDHFKAFSAGKRVCVGEGLARMELFLFMAAILQHFNLKSLVDPKDIDLSPIAIGFAKIPPHYKLCVIPRSQV", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. 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. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein Mitochondrion inner membrane; Peripheral membrane protein Note=Post-translationally targeted to mitochondria. TOMM70 is required for the translocation across the mitochondrial outer membrane. After translocation into the matrix, associates with the inner membrane as a membrane extrinsic protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MWSLALATLFVLGTVIRADQCPPVPADTKDKLEKILELIGHVNRPLTPETPEPAGYDETKLKGLGILPQHEIFSLFDERTWPEATKAAEFLMEATDFEHFIQRADVLRHRINEDMFMYALNVAVLHRKDTRGVQVPRIHKIYPDKFLKQDILVEVREKVNHGEEKPVVDATELHQNQLDPNYRLSYFLEDIGMNSHHYHWHVVHPAVWLPKHGPRKDRKGELFYYMHHQMVARYDSERLSNNLPRTEPFENWDDPLEEGYAPHLTIHKTGYNYMFRPEGLIVRDLPELNKNKMRQWKSRILHGIHLNVLYAENGTKISLDNEHGIDLLGDAIESSLLSVNRAFYGNIHCYAHVMAARIADPDGRYGEDNGVMHDVATSARDPLFYRWHKFIDNIFLEYKDNLDPYTQYELTWPDVVLNDVTVKPHKGDYDDEVHTYWEVDNYELGKGFDYTRKTTATVKVRHLQHEDYHYEIDIDNNAGKAKKAVFRIFLAPKYNEKGELFPVNEQRQLLVELDKFVATLEPGHNVIERQSKESSVTMSKDHVFGEIRNLADDHQCSCGWPDYLLLPKGKYEGMTYQLFVVATDYEEDHVEDAGEECQCRDSMSYCGSVEHKLPDNKPLGYPFDRRIDGTGFEEFKTQNMYYGDVVIQFTGETVTH", "text": "FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily."}
+{"protein": "MSWNHNRRWKDFQALVNAEDYFAFFELPYDPRVVNVNRLHILRKFAQYLAPLEHFQGSEEEWLEQARQALEKAYQTFLTSTPQQEKLFRVFQDYGCPDPVGGCAGCSSSGERGECSPGIPA", "text": "FUNCTION: May protect the nitrogenase Fe-Mo protein from oxidative damage. SIMILARITY: Belongs to the NifW family."}
+{"protein": "MNIYKEIDNASNWISDNHILFIKYISNIILSLIILIVGYSASKVTQKIIKNFMIKKNIDIIISEFFCSIIKYSILIFTIVTSLGCIGIQTTSIIAVIGAAGIAIGLALQGSLSNFAAGVLLVTLRYFRTGDYVNLCGVKGKIKTVQIFCTKIKTKDGKIIIIPNNKIISSNIINYSEELHRLMEVIISTEYTSDIKNVKEIIIDVLKKETRIVKEKKITVRLKNLGESSLDFLVRGWVYKKELKQTTSDILEKIKIELDKNKINIPYKQIDVNLKYSKEK", "text": "FUNCTION: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscS (TC 1.A.23) family."}
+{"protein": "MAEIIGIDLGTTNSCVAVMEGGKVRVIENAEGSRTTPSIVAYTKDGEVLVGASAKRQAVTNADRTLYAIKRLIGRRFDDNVVQKDIKMVPYKIIKADNGDAWVEVKDKEGKSQKLAPPQISAQVLIKMKKTAEDYLGHEVKDAVITVPAYFNDSQRQATKDAGKIAGLNVKRIINEPTAAALAYGMDKKKGDRKIAVYDLGGGTFDISIIEIAEVDGEHQFEVLATNGDTFLGGEDFDLRLIDYLAGEFKKDEGVDLHNDPLALQRLKEAAEKAKIELSSSQQTDVNLPYITADASGPKHLNIRLTRAKLESLVEDLVERTIEPCKVAIKDAGLKVSEIDDVILVGGQTRMPKVQEAVKNFFGKEARKDVNPDEAVAIGAAIQGAVLSGEVKDVLLLDVTPLSLGIETLGGVMTKLIEKNTTIPTKANQVFSTADDNQTAVTVHVLQGEREMASANKSLGRFDLSDIPPAPRGVPQIEVTFDIDANGILHVSAKDKATGKEQSIVIKASSGLSDEEVEKMVKDAEAHRDSDRKFHELVDARNQADAMIHAAEKSVKDLGSEVSADEKSAIEKAVNELKEAMKGNDKDAIEAKTKALTEHSSKLAERVYAKKGGAAGAPPGGEAEGEPQAQAGGKKEDVVDAEFEEVKDEKKKDEDK", "text": "FUNCTION: Acts as a chaperone (By similarity). Might have a role in the infectious process. FUNCTION: Acts as a chaperone. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the heat shock protein 70 family. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MASVENRTPNVSVFLCFFVLFATLLLSGGRVSSQTSAVFACDVAKNPALANYGFCNKKLSVDARVKDLVRRLTLQEKVGNLVNSAVDVSRLGIPKYEWWSEALHGVSNIGPGTHFSNVIPGATSFPMPILIAASFNASLFQTIGKVVSTEARAMHNVGLAGLTYWSPNINIFRDPRWGRGQETPGEDPLLASKYAAGYVKGLQQTDDGDSNKLKVAACCKHYTAYDVDDWKGVQRYTFNAVVTQQDLDDTYQPPFKSCVIDGNVASVMCSYNQVNGKPTCADPDLLKGVIRGKWKLNGYIVSDCDSVDVLFKNQHYTKTPEEAAAKSILAGLDLNCGSFLGRYTEGAVKQGLIGEASINNAVYNNFATLMRLGFFDGDPSKQPYGNLGPKDVCTSANQELAREAARQGIVLLKNCAGSLPLNAKAIKSLAVIGPNANATRAMIGNYEGIPCKYTSPLQGLTALVPTSFAAGCPDVQCTNAALDDAKKIAASADATVIVVGANLAIEAESHDRINILLPGQQQQLVTEVANVAKGPVILAIMSGGGMDVSFAKTNKKITSILWVGYPGEAGGAAIADVIFGYHNPSGRLPMTWYPQSYVDKVPMTNMNMRPDPATGYPGRTYRFYKGETVFSFGDGISYSTFEHKLVKAPQLVSVPLAEDHVCRSSKCKSLDVVGEHCQNLAFDIHLRIKNKGKMSSSQTVFLFSTPPAVHNAPQKHLLAFEKVLLTGKSEALVSFKVDVCKDLGLVDELGNRKVALGKHMLHVGDLKHPLSVMI", "text": "FUNCTION: A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo- enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the glycoside hydrolase 3 family."}
+{"protein": "MGKNILFFSFVGVMVLVLVACGGSSSSSSDADETSVIGDDIEGATELIFWTFAGQHVDLFEDAVVSWNEEFPDRPIKLVAETYPFDQMHNNLLLALQSGSGAPDLADIEVSRFPNFLQGVPQLLPMNDHVEPVIDKFVEARFNLYAKDGEYYGIPTHVGASVMYYNKEIMDEAGVDIESIETWDDYVEAGKQVVERTGKVMTTVPTDDYLPMFQMVSQRGSDFFDENGNLTLDTQENIEVLQFLYDLIYVHEIAELTPGGQPHAEEYYQYMNDGNVASMAMPIWYMGRFLDNMPDLAGKMLIQPLPAWEEGGFRSAGMGGTGTVVTNQTDHEELAKDFLAYAKISEKANEKLWTILGFDPPRWDVWDNPVFQEDNDFYQFFGENIFEVLLDVRDEINSINISQYTPSVANEFSTNIFNDVLRQQTHTPEEALKKAQETIEANMQQ", "text": "FUNCTION: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides (By similarity). AraN captures the substrate and delivers it to the two transmembrane components (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
+{"protein": "MSYQPTPEDKFTFGLWTVGWQGRDPFGDATRGALDPAESVRRLAELGAHGVTFHDDDLIPFGATDSERAEHIKRFRQGLDETGMKVPMATTNLFTHPVFKDGGFTANDRDVRRYAVRKTIRNIDLAVELGAQTYVAWGGREGAESGAAKDVRVALDRMKEAFDLLGEYVTSQGYDTPFAIEPKPNEPRGDILLPTIGHALAFIDGLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQSGIKYDQDLRFGPGDLAAAFWLVDLLESAGYEGPRHFDFKPPRTEDFDGVWASAAGCMRNYLILKERAAAFRADPEVQEALRAARLDELAQPTAGDGLQALLPDRSAFEDFDPDAAAARGMAFERLDQLAMDHLLGARG", "text": "FUNCTION: Involved in D-xylose catabolism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the xylose isomerase family."}
+{"protein": "MTNALLSIAVLLFSMLSLAQAETHTFNWTTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIKDDSFPYDYDEELSLSLSEWYHDLVTDLTKSFMSVYNPTGAEPIPQNLIVNNTMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKFDDTMLDVIPSDLQLNATSYMVYNKTAALPTQNYVDSIDNFLDDFYLQPYEKEAIYGEPDHVITVDVVMDNLKNGVNYAFFNNITYTAPKVPTLMTVLSSGDQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRTYDDALGEVPHSFDPDNHPAFPEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWHLLQGLGLVLVEDPFGIQDAHSQQLSENHLEVCQSCSVATEGNAAANTLDLTDLTGENVQHAFIPTGFTKKGIIAMTFSCFAGILGIITIAIYGMMDMEDATEKVIRDLHVDPEVLLNEVDENEERQVNEDRHSTEKHQFLTKAKRFF", "text": "FUNCTION: Iron transport multicopper ferroxidase required for Fe(2+) ion high affinity uptake. Required to oxidize Fe(2+) to Fe(3+), which is then transported into the cell via the ferric iron permease FTR1. Essential component of copper-dependent iron transport. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein; Extracellular side. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "MKYLNLVFVLQLLISIKYASFGRAFSLFEDDTTFANLDKQLKLPQNTQQTLKLDRLNHDDPLFTTFISSVDTDYSLRLRTVDPSKLGIDTVKQWSGYMDYKDSKHFFYWFFESRNDPANDPIILWLNGGPGCSSFTGLLFELGPSSIGADMKPIHNPYSWNNNASMIFLEQPLGVGFSYGDEKVSSTKLAGKDAYIFLELFFEAFPHLRSNDFHIAGESYAGHYIPQIAHEIVVKNPERTFNLTSVMIGNGITDPLIQADYYEPMACGKGGYHPVLSSEECEKMSKAAGRCRRLNKLCYASKSSLPCIVATAYCDSALLEPYINTGLNVYDIRGPCEDNSTDGMCYTGLRYVDQYMNFPEVQETLGSDVHNYSGCDNDVFTGFLFTGDGSKPFQQYIAELLNHNIPVLIYAGDKDYICNWLGNHAWSNELEWINKRRYQRRMLRPWVSKETGEELGQVKNYGPFTFLRIYDAGHMVPYDQPEASLEMVNSWISGNRAFSDLSTLENAS", "text": "FUNCTION: Vacuolar serine-type carboxypeptidase involved in vacuolar zymogen activation, breakdown of the autophagic body, and autophagosome-dependent protein synthesis (PubMed:29514932). Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates (PubMed:19897216). SUBCELLULAR LOCATION: Vacuole lumen Note=The vacuolar sorting receptor VPS10 is required for the delivery of ATG42 to the vacuole lumen. SIMILARITY: Belongs to the peptidase S10 family."}
+{"protein": "MIKLIWCEDLNHGIAKNNQIPWKIDEELNHFHQTTTNHPIIMGYNTYLAMNKILANQANIVISKKHQRELKNKNELFLYSDLKKALIDFSIVDLFIIGGKKTIEQAIKYADQLVISKLNADYGCDLFVNLNYDDFSLVQTKEYDQFVVEYWERKPNTKKPEDLIEELNINLNDDFLNLSFKHFSGPFDLLLHLIKDKKMDIMALDLFELTNQYFAYINKHMINLDLVSDYLYMACELLRIKSDLSIPNFEDETKIDLNNDDERDRIVKRIIEYKRYSELLPSLQKMQLERFSLFAKEEDDWDVFKLTSNDLLEAPLPDYVNPKKLKKAMERVFEKLKIKTITEHKIVIEELSIEDVKNEILSIIKKLLNNQYDRFIDLEKIFEQIDPKKLNLRYFVTSFVCLLILVREQKIDLNQKNDDESISACLVDPTKIVNSQESIQEVIQRQQEDEKALKESIKQIQEERKQSFFKQREEYLKKKYGEYYVSREQYQKLTPEEKINIRINQRKIDEQEKLNKAKAQNLVDENNQIIDLKTKKPSAKQILYEADLIIKQLDDLINDQQEDYDSQAELEALHTDLIKLDDEQEQDLIKEE", "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 (By similarity). 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": "MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQCSQTYGRVHKVSELPSDFQQRVSLHMEKHGCSLPSALCHPAYADSVPTCVIAKVLEKPDPGSLSSRMSDASARDLGYRDGVEKSGPRPPYKGDIYCSDPALYCPDEREHARRPSVDTPVTDVGFLRAQNSTDSAAEEEEEAEAAAFPEAYRREAYQGYAASLPTSSSYSSFSATSEEKEHAQAGTLTASQQAIYLSSRDEFFNRKPSATYGSGPRFAKAASTLGSPLEAQVAPGFARTVSPYPAEPYRYPASPGPQQALMPPNLWSLRAKPSGNRLAGEDIRGQWRPVSVEDVGAYSYQAGAAAGRAASPCNYSERYYGGGGGGGAAGGGSPGDKAEGRASPLYATYKADSFSEGDDLSQGHLAEPCFLRAGGDLSLSPSRSADALAGYAASDGDGDRLRVQLCGAGSSPEPEHGSRESLEPSSMEASPEMHPPTRLSPQQAFPRTGGSGLSRKDSLTKAQLYGTLLN", "text": "FUNCTION: May sustain the structure of the postsynaptic density (PSD). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein."}
+{"protein": "MASDGEDISVTPAESVTSATDTEEEDIDSPLMQSELHSDEEQPDVEEVPLTTEESEMDELIKQLEDYSPTIPDALTMHILKTAGFCTVDPKIVRLVSVSAQKFISDIANDALQHCKTRTTNIQHSSGHSSSKDKKNPKDRKYTLAMEDLVPALADHGITMRKPQYFV", "text": "FUNCTION: TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TAF10 family."}
+{"protein": "MKWLVLLGLVAFSECIVKIPLRRLKTMRNVVSGKNMLNNFLKEHAYSLSQISFRGSNLTTHPLRNIKDLVYMGNITIGTPPQEFQVVFDTASSDLWVPSDFCTSPACSTHVRFRHLQSSTFRLTNKTFRITYGSGRMKGVVVHDTVRIGNLVSTDQPFGLSIEEYGFEGRIYDGVLGLNYPNISFSGAIPIFDKLKNQRAISEPVFAFYLSKDEREGSVVMFGGVDHRYYEGELNWVPLIQAGDWSVHMDRISIERKIIACSDGCKALVDTGTSDIVGPRRLVNNIHRLIGAIPRGSEHYVPCSEVNTLPSIVFTINGINYPVPGRAYILKDDRGRCYTTFQENRVSSSTETWYLGDVFLRLYFSVFDRGNDRIGLARAV", "text": "FUNCTION: Appears to be proteolytically inactive. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MSTCPFNDVFNSTDSSMINTFLKNVQVLLEAASYIESAERKDGKCEHGYASTFPSIQHSSYQRQRKFRNKKCNNNHYRSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQRHLRRRLDLLRDGGGSLEAERIRTDSMGSTPCSERSDRSDSDQEEMEVDVESTEFSHGELDSVSTASTSDLDDHSSLQSTASDEGYSSCSIKLAFSS", "text": "FUNCTION: Transcriptional repressor. MXI1 binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MXI1 thus antagonizes MYC transcriptional activity by competing for MAX. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSIGLLCCAALSLLWAGPVNAGVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQDPGMGLRLIHYSVGAGITDQGEVPNGYNVSRSTTEDFPLRLLSAAPSQTSVYFCASSY", "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": "MKLTEVIEGKARLVIPDPSEFSREGKFDPAWSPVFYNPRMVFNRDVSVLAVSVISPPSVLDAMSATGVRGIRYVKESGVKGEVLFNDKNPVSVELISKNLELNGITGKVLRSDANSLMHQVKVGYTDLDPFGSPAPYLFSAISSLRRKGVLGVTATDLSALEGKSRTSSKRKYGVQGSRLSYSKEAGLRVLLGKIVKEASVQEKGIRPLMGFYHDYYYRLFVKMEDGAKRADRSLESLGTLYECDRCGYSFMSSDECERKCPVCGGELKYYGPAWIGEFNDLEFLKEMKNRLTEFSYLSNSVKISELLEYLERENRFGPYYRVDVLASRLKVNMPPMNSLLGCLGDAVRTHFDPRGFKSFREFSEILECVKGSSATYETSGR", "text": "FUNCTION: Dimethylates a single guanine residue at position 26 of a number of 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": "MAVEEEGLRVFQSVKIKIGEAKNLPTYPGPNKMRDCYCTVNLDQEEVFRTKVVEKSLCPFYGEDFYCEIPRSFRHLSFYIFDRDVFRRDSIIGKVAIKKEDLQKYHNRDTWFQLQHVDADSEVQGKVHLELRLSEVITDSGVVCHKLATRILECQGLPIVNGQCDPYATVTLAGPCRSEAKKTKVKKKTNNPQFDEVFYFEVTRPCSYSRKSHFDFEDEDVDKLEIRVDLWNASNLKFGDEFLGELRVPLKVLRQSSPHEAWYFLQPRDNGSKSLKPGDLGSLRLNVVYTEDHVFSSDYYSPLRDLLLKSADVEPVSASAAHILGEVCREKQEAAIPLVRLFLHYGRVVPFISAIASAEVRRTQDPNTIFRGNSLTSKCIDETMKLAGMQYLHVTLKPTIEEICQSHKSCEIDPVRLKDGESLESNMENLRQFVDRVFSVITKSGVSCPTVMCDIFFSLREAAAKRFQDDLDVRYTAVSSFIFLRFFAPAILSPNLFQLTPHHTDPQTSRTLTLVSKTIQTLGSLSKSKSASFKESYMAAFYEFFNEQKYADAVKNFLDLISSSGRRDPKSVQQPILLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYQKSKGDPPLYSIPIENILAVEPLEEESFKMKNMFQVIQPERALYIQANNCVEAKAWIDILTKVSQCNQKRLAVYHPSAYLNGHWLCCRASSDTAAGCSPCTGGLPANIQLDIDGDRETERIYSLSSSYMSKLETMQEACGSRSVYDGPEQEEYSTFIIDDPQETYKTLKQVVAGVGALEQEHAQYKRDKFRRTKYGSQEHPIGDKSFQSYIRQQSETPAHSM", "text": "FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4)."}
+{"protein": "MASTPWISFTTDYGLADGFVAACHGVLARLAPTARVIDVTHLVPPGDVRRGAAVLAQTVPYLPAAVHVAVVDPGVGTARRAIALTAGNGLLVGPDNGLLLDAATALGGVDAAVELTNPDWLGARMSATFHGRDVFAPVAARLALGAPLADAGPAVEPGALVRLPTPLVQPETDGFTAEVLTVDHFGNVQLAATGALLESLPRSLRVAHRPAVHARTFDDAPPGGLLVHVDSAGLVAVAVNGGRAADLLAVTPGDQLRVTAG", "text": "FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-methionine (SAM) into adenosine and L-methionine (PubMed:18720493, PubMed:19739191). Is likely stereoselective, specifically hydrolyzing (R)-S-adenosyl-L- methionine ((R)-SAM), the inactive form of the ubiquitous cofactor SAM, and not the active form of SAM, (S)-S-adenosyl-L-methionine (By similarity). Probaly plays a role in preventing accumulation of (R)-S- adenosyl-L-methionine in cells; maintenance of (S)-S-denosyl-L- methionine homochirality is important for cellular health given that the (R)-form is largely inactive as a methyl donor and can function as an inhibitor of methyltransferases (By similarity). Shows very slow iodinase activity in vitro (PubMed:18720493). SIMILARITY: Belongs to the SAM hydrolase / SAM-dependent halogenase family."}
+{"protein": "MRLFPKSDKLEHVCYDIRGPVHKEALRLEEEGNKILKLNIGNPAPFGFEAPDEILVDVLRNLPSAQGYCDSKGLYSARKAIVQYYQSKGILGATVNDVYIGNGVSELITMAMQALLNDGDEVLVPMPDYPLWTAAVTLSGGKAVHYLCDEDANWFPTIDDIKAKVNAKTKAIVIINPNNPTGAVYSKELLQEIVEIARQNNLIIFADEIYDKILYDGAVHHHIAALAPDLLTVTLNGLSKAYRVAGFRQGWMILNGPKHNAKGYIEGLDMLASMRLCANVPMQHAIQTALGGYQSINEFILPGGRLLEQRNKAYDLITQIPGITCVKPMGAMYMFPKIDVKKFNIHSDEKMVLDLLRQEKVLLVHGKGFNWHSPDHFRIVTLPYVNQLEEAITKLARFLSDYRQ", "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. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MLLFLVFILVVSQVVLLLLSPQFRDKFIFRWYYDEVYKPMILDNSRYRIKFYVVPVFYLSVYSYMVYIFYSRTFAIISPMLTSIETYVVIPLMLILPLFFGSMSMIIKPDSSNAHQIGSEKRYPYDNLLYFPQHECRTCKQVKPARSKHCTVCNSCIYLADHHCVWINNCVGMGNYMYFYSFLCSNLLLLSYSFIRLIFIQFNKSAYNTTPTGEKSLLILSILCGSFTVILAVYCYFVFELVNSGMTTNEKDKWQMVHDYINTGDLVRDPEGKYFIKYQNGGNNYEFYSTDSYDGTQYTIVDYFTVKSPAEITNIYDKGNFINNLREFIG", "text": "FUNCTION: Palmitoyltransferase that targets several endosomal SNAREs. Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic end of their transmembrane domain. May have a role in the cellular quality control of transmembrane domain-containing proteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. SWF1 subfamily."}
+{"protein": "MFVSRLAASGLLLLALLAVSLDGKPLQQWSQRWPHLEIPPLVVQNWKSPTQLQARESPAGGTTALREELSLGPEAALDTPPAGPDGGPRGSKAAAAAPQRLSKSKGASATSAASRDLRTDGKQARQNWGRLVSPDHHSAAGGGCGGGGGARRLKGLAKKRAGNGCFGLKLDRIGSMSGLGC", "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). 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. Synthetic Cdt1a, Cdt1b and the short hexapeptide Cdt3 are able to potentiate the hypotensive effect mediated by Bk on the blood pressure of anesthetized 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": "MSMMLSNWALSPRYVGQRNLIHCTTLFHTLTRWAKDADDKYHDINSMYENMFTPSNDNVSILQDEGKSDYDTTKTSSMQEDISAFNKDLYNFYNIGYAKQIMSASQLENIVKAKGRFVIQSLSTSPYYNLALENYVFKNTPRAKRGPDNCRLLFYINDRCAVIGKNQNLWQEVDLAKLKSKNFELLRRFSGGGTVLHDLGNVNYSYLTSREKFETKFFNKMIIKWLNSLNPELRLDLNERGDIIQDGFKISGSAYKIAGGKAYHHATMLLNADLEQFSGLLEPSLPNNMEWESSGVHSVKSKIKNVGIITPNQFIAVVSERFQKTFKVDGEIPIYYCDEFKSINDEIKDAMNTLQSEQWKYFSGPKFSVKIKDKGLTIKVEKGMIYDCDRNDLIGLEFKGFLENIDSYT", "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. SIMILARITY: Belongs to the LplA family."}
+{"protein": "MDNHSSVPWASAASVTCLSLDAKCHSSSSSSSSKSAASSISAIPQEETQTMRHIAHTQRCLSRLTSLVALLLIVLPMVFSPAHSCGPGRGLGRHRARNLYPLVLKQTIPNLSEYTNSASGPLEGVIRRDSPKFKDLVPNYNRDILFRDEEGTGADRLMSKRCKEKLNVLAYSVMNEWPGIRLLVTESWDEDYHHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLESGVRKPLGELSIGDRVLSMTANGQAVYSEVILFMDRNLEQMQNFVQLHTDGGAVLTVTPAHLVSVWQPESQKLTFVFADRIEEKNQVLVRDVETGELRPQRVVKVGSVRSKGVVAPLTREGTIVVNSVAASCYAVINSQSLAHWGLAPMRLLSTLEAWLPAKEQLHSSPKVVSSAQQQNGIHWYANALYKVKDYVLPQSWRHD", "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 (PubMed:25639794, PubMed:27195754, PubMed:8166882, PubMed:1394430, PubMed:1340474, PubMed:11319862). 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 (PubMed:25639794). 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 (PubMed:27195754, PubMed:25639794, PubMed:8166882, PubMed:1394430, PubMed:1340474, PubMed:11319862). 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) (PubMed:7885476). 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 (PubMed:12586063). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm (PubMed:1280560). Also secreted in either cleaved or uncleaved form to mediate signaling to other cells (PubMed:1280560). SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane; Lipid-anchor Note=The N-terminal peptide remains associated with the cell surface (PubMed:12586063). 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 (PubMed:15875013). SIMILARITY: Belongs to the hedgehog family."}
+{"protein": "MSARESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEAMMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS", "text": "FUNCTION: Synthesizes selenophosphate from selenide and ATP. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Nucleus membrane; Peripheral membrane protein. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class II subfamily."}
+{"protein": "MDKYKSINEKLDIKIEEDEENDIGFKEERYNSQQEDEQLKKDLTICERFGVDSCLISRIIIFVVIFSWIIFIFYISLFE", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein."}
+{"protein": "MSVPLILTILAGAATFIGAFLGVLGQKPSNRLLAFSLGFAAGIMLLISLMEMLPAALAAEGMSPVLGYGMFIFGLLGYFGLDRMLPHAHPQDLMQKSVQPLPKSLKRTAILLTLGISLHNFPEGIATFVTASSNLELGFGIALAVALHNIPEGLAVAGPVYAATGSKRTAILWAGISGLAEILGGVLAWLILGSMISPVVMAAIMAAVAGIMVALSVDELMPLAKEIDPNNNPSYGVLCGMSVMGFSLVLLQTAGIG", "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": "MASNGESKHSEVGHKSLLQSDALYQYILETSVYPREPEAMKELREVTAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALALPDDGKILAMDINRENYEIGLPIIEKAGVGHKIDFREGPALPVLDHMLEDGKYHGTFDFVFVDADKDNYINYHKRLIDLVKIGGLIGYDNTLWNGSVAQPADAPMRKYVRYYRDFVIELNKALAADPRIEICMLPVGDGVTLCRRIS", "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": "MSAQTLAISNLKPNTTRHLASFHPNIWGDRFLSCAAESTDIEDDMEQQVERLKEEVKKMIASADEPSQILNLIDLLQRLGVSYHFEKEIEEALQQVLNMNSDSDKDDDLHSVALRFRLLREQGLNVSCDVFNKFRDRNGHFIQTLKTDLQGMLSLYEAAHFRVHGEGILDDALAFTTTYLESIVPNLSPPLAAQISRTLRQPLRKSLARVEARHFISIYQEDTSHNEVLLTFAKLDFNLLQKLHQKELKYISLWWKDLDFVNKLPFTRDRVVEGYFWILGVYFEPQYHRARKFVTKVINVVSVIDDIYDAYGTLEELVVFTDAINRWDIDCIDQLPEYMKVCYKALLNVYEEIERALSEQGRSYRLHYAKEAMKKLVQAYLVEANWMNKNYVPTMDEYMSIALVSCAYPLLTVTSFVGMGDIATKEVFDWASNDPKIVRVASIICRLMDDIVSHEFEQKRGHIASSVECYMKQNGVSEEATRDEFNKQIVDAWKDINEEHLQPNYVPMPFRTRVVNSARIMDYLYKDDDEYTHVGELMKGSVAALLIDPA", "text": "FUNCTION: Probable sesquiterpene synthase. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MEYQSSVENLDEDGYTQLDFSSRNITRRSVVSEKGLCAASSHWRLIAVTLGILCSVMLVITVVLSTSGIWRSSSGNNLLKSDSFPSRNKDNQSQPTQSSLEDSVIPTKALTTTGVFSSSCPPNWITHEDSCYLFSTLLDSWDGSKRQCFQLGSHLLKIDSSKELEFISRQVSSQPDHSFWIGLSRRQTEEPWLWEDGSTLLSNLFQIRSTVTEKDSSHNCAWIHVSDIYDQLCSVHSYSICEKKLSV", "text": "FUNCTION: Lectin that functions as pattern recognizing receptor (PRR) specific for beta-1,3-linked and beta-1,6-linked glucans, which constitute cell wall constituents from pathogenic bacteria and fungi. Necessary for the TLR2-mediated inflammatory response and activation of NF-kappa-B: upon beta-glucan binding, recruits SYK via its ITAM motif and promotes a signaling cascade that activates some CARD domain-BCL10- MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation. Induces phosphorylation of SCIMP after binding beta-glucans. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
+{"protein": "MSHDTNTIDSRTHEGELNKLGFWIFITAEFALFGTLFATLLTLQHGGDYAGKMTTELFELPLVLIMTFALLFSSYTCGIAIYYMRQEKQKLMMFWMIITLLLGLVFVGFEIYEFAHYASEGVNPTIGSYWSSFFILLGTHGCHVSLGIVWAICLLIQIQRRGLDKYNAPKLFIVSLYWHFLDVVWVFIFTAVYMIGMVYSG", "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": "KPNFIRF", "text": "FUNCTION: Myoactive; induces a rapid concentration-dependent muscle tension increase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
+{"protein": "MDAIADTVFQGTKSKTQEIEDTPSLLTVVVDTSIHSWVQLTKQQSGSGSEGSSGEKQLIEALKSIVVFLNAHLAFNSGNQVCLIAAHSEGMKYLYPSADSKPSMSMVSSDMYRGFRNVDEIVVEQWYRLFKEELEGQESKVSMKSSLSGAMSSALTYVNRILKENENTSLRSRLLVITCGTSQGKDEIFQYIPIMNCIFSATKMKCSIDVVKIGGGIESTFLQQATDATSGVYLHVENTRGLIQYLSTAMFIDPSLRNVIIKPNQGSVDFRTSCFLTGKVVAVGFVCSVCLCVLSVIPPGQKCPACDSPFDSKIIARLRRKPVLSNGVPKKKNVSNK", "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 TFB4 family."}
+{"protein": "MLRLLFTLVLLALYGPSVDASRDYVHVRLLSYRGDPLVFKHTFSGVRRPFTELGWAACRDWDSMHCTPFWSTDLEQMTDSVRRYSTVSPGKEVTLQLHGNQTVQPSFLSFTCRLQLEPVVENVGLYVAYVVNDGERPQQFFTPQVDVVRFALYLETLSRIVEPLESGRLTVEFDTPDLALAPDLVSSLFVAGHGETDFYMNWTLRRSQTHYLEEMALQVEILKPRGVRHRAIIHHPKLQPGVGLWIDFCVYRYNARLTRGYVRYTLSPKARLPAKAEGWLVSLDRFIVQYLNTLLITMMAAIWARVLITYLVSRRR", "text": "FUNCTION: Chaperone protein that plays an important role in HCMV tropism. Cooperates with UL116 to regulate the abundance of gH-gL complexes in virion. Favors the incorporation of gL into virions once UL116 has regulated the early folding steps of virion assembly. Interacts with the host ERAD machinery and slows gO decay which would otherwise be constitutively degraded. Reorganizes the host endoplasmic reticulum and activates the unfolded protein response. Additionally, plays a role in the evasion of antiviral immune response by down- regulating cell surface expression of host CD58. Mechanistically, interacts with host CD58 and retains its immature form intracellularly. The capacity to cause endoplasmic reticulum reorganization and the intracellular retention of host CD58 are functionally independent properties. SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass type I membrane protein."}
+{"protein": "GIKDYLKKLLQKAINKIKSLRKKQDA", "text": "FUNCTION: May have cytolytic and antimicrobial activity. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSLPLPSHMKSVFLGMKVEISTSVPVTRIGFWRKSVDCKESRIGKQPITVPANVAIAMEGQDLKVKGPLGELSITYPREVLVEKQESGFLRVRKAVETRRANQMHGLFRTLTDNMVVGVSKGFEKKLQLVGVGYRATVEGKDLILSLGFSHPVRMAIPDELQVKVEENTKVTVSGRDKSVVGQFAATIRSWRPPEPYKGKGVRYVDEVVRRKEGKAGKKK", "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 uL6 family."}
+{"protein": "MLARTCLRSTRTFASAKNGAFKFAKRSASTQSSGAAAESPLRLNIAAAAATAVAAGSIAWYYHLYGFASAMTPAEEGLHATKYPWVHEQWLKTFDHQALRRGFQVYREVCASCHSLSRVPYRALVGTILTVDEAKALAEENEYDTEPNDQGEIEKRPGKLSDYLPDPYKNDEAARFANNGALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGASVGAGLNFNPYFPGTGIAMARVLYDGLVDYEDGTPASTSQMAKDVVEFLNWAAEPEMDDRKRMGMKVLVVTSVLFALSVYVKRYKWAWLKSRKIVYDPPKSPPPATNLALPQQRAKS", "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 (PubMed:3015618) (Probable). 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 (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c family."}
+{"protein": "MKFACRAITRGRAEGEALVTKEYISFLGGIDKETGIVKEDCEIKGESVAGRILVFPGGKGSTVGSYVLLNLRKNGVAPKAIINKKTETIIAVGAAMAEIPLVEVRDEKFFEAVKTGDRVVVNADEGYVELIE", "text": "SIMILARITY: Belongs to the UPF0107 family."}
+{"protein": "MKKTKFFLLGLAALAMTACNKDNEAEPVVETNATVSFIIKSGESRAVGDDLTDAKITKLTAMVYAGQVQEGIKTVEEDGGVLKVEGIPCKSGANRVLVVVANHNYELTGKSLNEVEALTTSLTAENQNAKNLIMTGKSAAFTIKPGSNHYGYPGGTASDNLVSAGTPLAVTRVHAGISFAGVEVNMATQYQNYYSFKPADAKIAALVAKKDSKIFGNSLVSNTNAYLYGVQTPAGLYTPDAAGETYELEASLNTNYAVGAGFYVLESKYDASNELRPTILCIYGKLLDKDGNPLTEPALTDAINAGFCDGDGTTYYPVLVNYDGNGYIYSGAITQGQNKIVRNNHYKISLNITGPGTNTPENPQPVQANLNVTCQVTPWVVVNQAATW", "text": "FUNCTION: Structural subunit of the major fimbriae (PubMed:27062925). These long, 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. They play an important role in the invasion of periodontal tissues. Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence-based classification correlates with pathogenicity. SUBCELLULAR LOCATION: Fimbrium Cell outer membrane Note=Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein. SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily. FimA/Mfa1 family."}
+{"protein": "MAGPRVEVDGSIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMIRDLCDGRLEGAEIGSTEITFTPEKIKGGIHTADTKTAGSVCLLMQVSMPCVLFAASPSELHLKGGTNAEMAPQIDYTVMVFKPIVEKFGFRFNCDIKTRGYYPKGGGEVIVRMSPVKQLNPINLTDRGCVTKIYGRAFVAGVLPFKVAKDMAAAAVRCIRKEIRDLYVNIQPVQEPKDQAFGNGNGIIIIAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLIVFMALANGVSRIKTGPVTLHTQTAIHFAEQIAKAKFIVKKSEDEEDASKDTYIIECQGIGMTNPNL", "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": "MNQASSRIRIALSGRIETALENIYRKHNLTPINDETRQRLSSIPENLGFELVRKVFSLQAGLIYNLDSFIVSKVNQAVSFTGYPQPANSLSPSGRHVSRVLQEEMSVDSDAPSPKSLKSEDKGGSLHIPQLVALGELEFKKVFLLLSYIPGQHVGQVITADEIRLWKDLPMVEYEAAVWDRLGRHYCPQKDRRMLQWDSGKTHYYQCNVAPNGSYTFKVLSALQGPLLEHTGTHLHKVLGDDNVLTVKFADVQKSSSTYSIDHYFTYKGIAKNGIMIGLRRYQFFVFKDGGKEEKKKDLSTKKVKCYFIRTDSTAFYDMQNPYILTGKSIYEARMHFMHVHRAPTLANYMARFSLILSKTKTLEVDMTGITFDQIDDIHCHDQDGKDVLDKNKKPCIHSDGTGYISEDLARMCPLNIFKGKCLRSESIQEACYQDPPLLIQFRMFYDGYAVKGTFLLNKKLCPRTVQVRPSMIKVSKDPSLSNFSTFNALEVVTTSNPPKRTKLSKNLVALLSYGGIPNEFFLDILLNTLEESKSIFYNKRAALNAALNYGEMDDQNAAQMILVGIPLDEPHLKNYLSILLKTEKNDLKAGKLPVTESYYLMGTVDPTGALKEDEVCVILESGQISGEVLVYRNPGLHFGDIHILKATYVKALEEYVGNSKFAVFFPQKGPRSLGDEIAGGDFDGDMYFISRNPELLENFKPSEPWVSLTPPSKSNSGRAPSQLSPEELEEELFEMFLTAGFHASNVIGIAADSWLTIMDRFLILGDDRAEEKAEMKKKMLELIDIYYDALDAPKKGDKVYLPNKLKPDIFPHYMERDKKFQSTSILGLIFDFVKSQTTEEPSPSSEISKLPCFEDEPVSEFHMQKCRLWYDNYRTEMTQAMKTDKDESANEVIQRYKQEFYGAAGFEDSKKSLEELYPQALALYKIVYDYAIHAGVSKCRFVWKVAGPVLCRFYLNKKMQEKCLVCAPSVLKELWG", "text": "FUNCTION: Probably involved in the RNA silencing pathway and required for the generation of small interfering RNAs (siRNAs). SIMILARITY: Belongs to the RdRP family."}
+{"protein": "DCLPGWSSHEGHCYKVFNQEMYWADAEKFC", "text": "FUNCTION: Calcium-dependent prothrombin activator. This protein may activate prothrombin via recognition by the regulatory subunit of the calcium ion bound conformation of its gamma-carboxyglutamic acid (GLA) domain, and the subsequent conversion of prothrombin to active thrombin is catalyzed by the catalytic subunit. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
+{"protein": "MSVVSQVILQADDQLRYPTSGELKGIQAFLTTGAQRIRIAETLAENEKKIVDQAQKQLFKKHPEYRAPGGNAYGQRQYNQCLRDYGWYLRLVTYGVLAGNKEPIETTGLIGVKEMYNSLNVPVPGMVDAVTVLKDAALGLLSAEDANETAPYFDYIIQFMS", "text": "FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 654 nanometers (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=Forms the core of the phycobilisome. SIMILARITY: Belongs to the phycobiliprotein family."}
+{"protein": "MVTRMATKVSLEGKRVVLVPYMAEHVPKYHQWMQDSALLEATGSEPLSLEQEYEMQLSWTQDPNKRTFIVLDKDFVKGDLAHGQPHVEAMTGDVNIYMNDVDDPKVAEVEIMIAEPRSRGKGLGKESVLIMMAYGVKNLEIHKFTAKIGESNTASLSLFRKLGFEESSYSGIFKEVTLEYPVTNLRREELLKLLDEVIRHTHSSNNPSDSLLSGEATA", "text": "FUNCTION: Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily."}
+{"protein": "MYQEERLVAILDFLKQHNRITTEQICTLLQVSRDTARRDLVKLEEQNAIIRTRGGAILPTVHQKIQSYSGRLKTVSEEKNKIGRLAASLIHDGDRVILDASTTVQACAKHLNAVDCTVITNSINLADVLSDKEGIEIYLLGGKLEKEHRFLYGSSVIEKLSSYHVDKALIGVVGISEHGITIAHEEDGMVKRKMIQQAKQVIALADHSKLGSTSFYQYAELNEIDLLITDRLPNQAFCDLLDRNGVELLVTEQDEGKD", "text": "FUNCTION: Plays a role in carbon catabolite repression (CCR). Specifically required for transcriptional repression of the levanase operon by glucose but not by other sugars."}
+{"protein": "MAELAKSAVLVSSCTDDLLGDAKQVVVGPNQEDLHSAEAVLNRYSTVGFQASNLARAFSICEMMLTPQSPSPSLMPTEGDQASESPVMVQPTLFVGVTANLFGTGCREAIRFLCTECVPLPNGVEPATPLDDMAGISCDGTGALKPSPCDSRALIHVLVVSGGAMEHDIRRACESYKLSRDGAEEEGEQFHHPVERDRSRSKGTDCHFGNVRYNSSGVASRNLFSCVMRCLVKRLAEAQRKEKANREAAPIPEAYYDVCSWAITPSTLWYMAGLWMADIFTEALQETGEVTDEKVASEEGLKRAKSTVLYWAARNGVPIFSPSLTDGDIMEFILTAGDTGVPLLQLDLVADIHRLNRLAMRSRRTGMMILGGGVVKHHVCNANLMRNGADYAVFLNNAQEFDGSDAGARPGEAVSWGKLRLDSTAVKVYSEVTIVFPLIVVHVFVAWVRMMRSKGKENIRS", "text": "FUNCTION: In association with the non-catalytic regulatory subunit DHSp, 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 eIF5A precursor protein to form the intermediate deoxyhypusine residue. Regulates protein levels of its regulatory subunit DHSp. Required for cell growth and survival. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the deoxyhypusine synthase family."}
+{"protein": "MPCVADWLNNPFSIVQGIFAQNTPNSDWEKKVTDYFKEKLKENNATNWVPSLNDVPVHYLKPNSLVKFRCMVQDMFDPEFYMGVYETVDPNTNARVLHFGKYRDVAECGPQQEIDMNSSQTVTLERQTFYCVPVPGESAWVKEYLFSLQARVSPSTSYTPSRHKRSYEEDEDMEQHPSKQKEQHMGSGGDSHGCGEPKRLETEASAGHHLISPNCSPPLDLNFPLPGEKGPACLVKVYESWDTFKVNDVLEVYGILSVDPVLSIVNSEERDSSMLDPMECMDTAEEQRVHSPPSSLVPRIHVILAHKLQHLNPLLPACLNEEESKTFVSNFMSELSPVRAELLGFLTHALLGDSLAAEYLILHLISTVYARRDVLPLGKFTVNLSGCPRNSIFTEHIYRIIQQLVPASYRLQMTIENMNHSRFIPRKDYTANRLVSGILQLASNTSLVIDETQLEQGQLDTKGVHNVKALGNLITWQKVDYDFSYHQMEFPCNINVLITSEGRSLLPSDCQVQLQPQIIPPNMEEYMNSLLTAVLPSVLNKFRIYLSLLRLLDYSISDEVTKAVEEDFVEMRKNDPESITADDLHRTLLVARFLSLSAGQTTLSRERWLRAKQLEALRKARLQQQKCVNGNEL", "text": "FUNCTION: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Associates with chromatin. SIMILARITY: Belongs to the MCMBP family."}
+{"protein": "LKFVVLICLVIMASTSAQQCGDETCGAGTCCAVFSQNHCRRLSQMYDLCSDHADASPSGNYLFFCPCEPGLHCDRNTWTCTEGSSRSE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MIT-like AcTx family."}
+{"protein": "MMQVLLVTISLAVFPYQGSSIILESGNVNDYEVVYPQKVTALPKGAVQQPEQKYEDTMQYEFEVNGEPVVLHLEKNKILFSEDYSETHYYPDGREITTNPPVEDHCYYHGRIQNDAHSSASISACNGLKGHFKLRGEMYFIEPLKLSNSEAHAVYKYENIEKEDEIPKMCGVTQTNWESDKPIKKASQLVSTSAQFNKIFIELVIIVDHSMAKKCNSTATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDLMTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVEIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKCIFNPPLRKDIVSPPVCGNEIWEEGEECDCGSPANCQNPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRDQLQQNGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQENLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLNNSPRNKNPCNMHYSCMDQHKGMVDPGTKCEDGKVCNNKRQCVDVNTAYQSTTGFSQI", "text": "FUNCTION: Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIId sub-subfamily."}
+{"protein": "MDRRLSKKEEERIVNELNKLQMIEMVDTSVNLTNKCFQSCITNFRIRKLDDEEQLCVYKCVEKNMFFTSALNNHFMKLSNEGMF", "text": "FUNCTION: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the small Tim family."}
+{"protein": "MMVEDLGVEAKEAAVREVAKLLPLPELLQSISSIKADYIARQQANDAQLSTMVAEQVEQAQAGLESLSSSEKTIYELRDNFISIDKLCQECQTLIDNHDQIKLLSNARNNLNKTLKDVEGMMSISVEAAAARDSLSDDKEIVNTYERLTALDGKRRFALAAAGEEVGRLREYFEDVDRTWETFEKTLWGHVSNYYKLSKESPQTLVRALRVVEMQEILDQQLAEEAAEAEGEGAMASVANPRRPGKKSTTTSASSKGLAQQKLKVQGKGYKDKCYEQIRKAVEDRFNRLLTLVFEDLKAALEEARMIGEELGDIYDYVAPCFPPRYEIFQLMVNLYTERFIQMLRLLSDRANDLTNIEILKVTGWVVEYQENLIALGVDDSLAQVCSESGSMDPLMNAYVERMQATTKKWYMNILEADKVQPPKKTEEGKLYTPAAVDLFRILGEQVQIVRDNSTDVMLYRIALAIIQVMIDFQAAEKKRVDEPASDIGLEPLCAMINNNLRCYDLAMELSNSTLEALPQNYAEQVNFEDTCKGFLEVAKEAVHQTVRVIFEDPGVQELLVKLYQKEWCEGQVTEYLVATFGDYFTDVKMYVEERSFRRFVEACLEETVVVYVDHLLTQKNYIKEETIERMRLDEEVLMDFFREYISASKVESRIRIMSDLRELASAESLDAFTLVYSNILEHQPDCPAEVVEKLVSLREGIPRKDTKEVVQECKEIYENTLVDGNPPKTGFVFPRVKCLTASKGSMWRKLT", "text": "FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane Cytoplasm, cytoskeleton, phragmoplast Secreted, cell wall Secreted, extracellular exosome Note=During cytokinesis, localizes to the nascent cell plate and later to the cell plate insertion site and along the post-cytokinetic wall (PubMed:20870962). Shuttles from the cytoplasm to the exocyst-positive organelle (EXPO) in the presence of EXO70E2 (PubMed:24307681). SIMILARITY: Belongs to the SEC6 family."}
+{"protein": "MSFRSILLTALLSLSFTNTMQAAHHHYHRYDDKLRRQYHKKDLPTQENVRKEFCNPYSHSSDPIPLSQQRGVLSPICDLVSECSFLNGISVRSLKQTLKNSAGTQVALDWSILPQWFNPRSSWAPKLSIRDLGYGKPQSLIEADSPCCQTCFNPSAAITIYDSSCGKGVVQVSYTLVRYWRETAALAGQTMMLAGSINDYPARQNIFSQLTFSQTFPNERVNLTVGQYSLYSIDGTLYNNDQQLGFISYALSQNPTATYSSGSLGAYLQVAPTESTCLQVGFQDAYNISGSSIKWNNLTKNKYNFHGYASWAPHCCLGPGQYSVLLYVTRKVPEQMMQTMGWSVNASQYISSKLYVFGRYSGVTGQLSPINRTYSFGLVSPNLLNRNPQDLFGVACAFNNIHASAFQNAQRKYETVIEGFATIGCGPYISFAPDFQLYLYPALRPNKQSARVYSVRANLAI", "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": "MEAISIFSDYQLQFFKRIGMKPKPIETLDDVSDVMKACSNVFSFENLDIVSNSCEPLNKDVLIKQVICNNQGGLCYKINTLLYHFLLEFGFKIHIIRGSVENQETHSDWNIPTGHMINIINFENRLYVVDVAFGCNLSLRPIPITDDGSEVVESCTGLYRVRKVENCVSGKYNYTHILEHRKLDSFLIESGKTWVTGYAFDPLLIVDNNNNNEKTTHQTLVQQLVIDDPTKEFSTKPLATKIVNDGSSFSIATLTANSFTLTDCKTGQKTKTNFDNDKSSFEQFNQHLISIFNLPPLKTIPPIFLN", "text": "SIMILARITY: Belongs to the arylamine N-acetyltransferase family."}
+{"protein": "MVVSEKSKILIIGGTGYIGKYLVETSAKSGHPTFVLIRESTLVNPEKSKLIDTFKSYGVTLLFGDISNQESLLKAIKQVDVVISTVGGQQFADQVNIIKAIKEAGNIKRFLPSEFGFDVDHAHAIEPAASLFALKVKIRRMIEAEGIPYTYVICNWFADFFLPNLGQLEAKTPPRDKVVIFGDGNPKAIYVKEEDIATYTMKAVDDPRTLNKTLHMRPPANILSFNEIVSLWEEKIGKTLEKLYLSEEDILHIVQEGPMPLRVNLAICHSVFVNGDSANFEIQPSTGVEATELYPKVKYTTVDEYYNKFV", "text": "FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'- nitrosonornicotine (NNN) (PubMed:19002761). Reductase that may be involved in a late step of tobacco alkaloid biosynthesis (PubMed:19002761). Maybe involved in either the formation of a nicotinic acid-derived precursor or the final condensation reaction of tobacco alkaloids (PubMed:19002761). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily."}
+{"protein": "MSKPTIAFLGATGGCINACLAHTLQTGYHAVALARTPSKLTALLRTQNIDQETLDSRLRIVTGDATDPEAVKSTLLLQPGFPTDPTTSASSPTPTLVSHIISGIGATGNFRGWCFEFDQPHICEEATRALLTALRNIYATYPEFMLPANVKSRPLLTVLSGMGVDPSQKQMDVPFLLRRVYHGLLHVPHADKWVMEEMLAKREAREFFRGVITVRPGSLLTGDHMLGSGYGYEKVRVGTEREEPSVGWTIPRADVGEWVFREVVVMGGGRWVDEKVTLTCW", "text": "FUNCTION: Oxidase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds (PubMed:24106156, PubMed:26414728). 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 avfA family."}
+{"protein": "MAKIIISLILLLSLFSFSYGAYNCNKLNCSSKNTKCRTFSCTSVVGCYYTDKCTSPDLCHNSACNASTGNCTLTTISCNDNNPCTDDFCHPGYGCYSVPNSCDPGVICQQNCNDNDPCTYDFCDALNICRHSETYCNDGDACTLNTCGVNGCNFTKISCDDNDPCTADYCSTLYGCYHEPIECSIKVPCNIDSDCNRNNGCETFTCNLSTNTCDYYAKNCGGWPCINNQCTTGSISN", "text": "FUNCTION: PDI acts by binding stoichiometrically to cyclic nucleotide phosphodiesterase, changing the KM of the enzyme for cAMP from 10 uM to 2 mM."}
+{"protein": "MTPSEGARAGTGRELEMLDSLLALGGLVLLRDSVEWEGRSLLKALVKKSALCGEQVHILGCEVSEEEFREGFDSDINNRLVYHDFFRDPLNWSKTEEAFPGGPLGALRAMCKRTDPVPVTIALDSLSWLLLRLPCTTLCQVLHAVSHQDSCPGDSSSVGKVSVLGLLHEELHGPGPVGALSSLAQTEVTLGGTMGQASAHILCRRPRQRPTDQTQWFSILPDFSLDLQEGPSVESQPYSDPHIPPVDPTTHLTFNLHLSKKEREARDSLILPFQFSSEKQQALLRPRPGQATSHIFYEPDAYDDLDQEDPDDDLDI", "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) (PubMed:29332244). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). Involved in cell migration (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the ELP5 family."}
+{"protein": "MQLEHCLSPSIMLSKKFLNVSSSYPHSGGSELVLHDHPIISTTDNLERSSPLKKITRGMTNQSDTDNFPDSKDSPGDVQRSKLSPVLDGVSELRHSFDGSAADRYLLSQSSQPQSAATAPSAMFPYPSQHGPAHPAFSIGSPSRYMAHHPVITNGAYNSLLSNSSPQGYPTAGYPYPQQYGHSYQGAPFYQFSSTQPGLVPGKAQVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNISGLDPTAHYNIFVDVILADPNHWRFQGGKWVPCGKADTNVQGNRVYMHPDSPNTGAHWMRQEISFGKLKLTNNKGASNNNGQMVVLQSLHKYQPRLHVVEVNEDGTEDTSQPGRVQTFTFPETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDTIYTGCDMDRLTPSPNDSPRSQIVPGARYAMAGSFLQDQFVSNYAKARFHPGAGAGPGPGTDRSVPHTNGLLSPQQAEDPGAPSPQRWFVTPANNRLDFAASAYDTATDFAGNAATLLSYAAAGVKALPLQAAGCTGRPLGYYADPSGWGARSPPQYCGAKSGSVLPCWPNSAAAAARMAGANPYLGEEAEGLAAERSPLAPAAEDAKPKDLSDSSWIETPSSIKSIDSSDSGIYEQAKRRRISPADTPVSESSSPLKSEVLAQRDCEKNCAKDIGGYYGFYSHS", "text": "FUNCTION: Transcriptional repressor involved in multiple aspects of cortical development, including neuronal migration, laminar and areal identity, and axonal projection (PubMed:9883721, PubMed:11239428, PubMed:21285371). As transcriptional repressor of FEZF2, it blocks the formation of the corticospinal (CS) tract from layer 6 projection neurons, thereby restricting the origin of CS axons specifically to layer 5 neurons (PubMed:21285371). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSTTTTASIEGYKLGKVIIEGKTKQVYDLPEQPGLCLLLSKDRITAGDGVKAHDLAGKAEISNTTNGQVFRLLNEAGIRTAYVKQCGAKAFIARKCQMIPIEWVTRRLATGSFLKRNVGVPEGYRFSPPKQETFFKDDANHDPQWSEEQIVSAKFELNGLVIGQDEVDIMRRTTLLVFEILERAWQTKNCALIDMKVEFGICDDGNIVLADIIDSDSWRLWPAGDKRLMVDKQVYRNLASVTASDLDTVKRNFIWVAEQLADIVPKKDHLVVILMGSASDISHSEKIATSCRSLGLNVELRVSSAHKGPEETLRIVREYESVMSNLIFVAVAGRSNGLGPVVSGSTNYPVINCPPVKSDNMQVDVWSSLNLPSGLGCATVLYPEAAALHAATILGLGNFMVWSKLRVKALNNFITLKKADKELRGVRNA", "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": "MHINGGPLASWICCVIGSIHLAHASTRPENGGTSGMQRKKENSVLGMEDTVPLRLIFSNEEDNQTTQGLLSTRVRAGSPQHQDQLTHVAQASFQIDAFGSSFILDVELNHDLLSSDYRERHVTQDGKTVEVKGGEHCYYQGQIRGKAKSFVALSTCNGLHGMFCDGNHTYLIEPGEKYNPNEDYQFHSVYKSKVLEFPLDELPSEFWALNDTSVRLSQQTRSQRKKRQTRRYPRNVEDETKYVELMIVNDHLMYKKHRLSVGHTNSYAKSVVNMADLIYKEQLNTRIVLVAMETWATDNKFSISENPLLTLKEFMKYRRDFIKDKSDAVHLFSGSQLRVAAVVLRILVEWCSLLKGGGVNEFGKPDVMAVTLAQSLAHNLGIFSDKKKLLSGECKCEDTWSGCIMGDIGYYLPSKFSVCNIEEYHEFLNNGGGACLFNKPLKLLDPPECGNGFVETGEECDCGTIAECAMEGEECCKKCTLTQDSECSDGLCCSNCKFNPKEMLCREAVNDCDIPETCTGNTSQCPANIHKLDGYSCESMQGLCFGGRCKTRDRQCKYIWGEKVSAADRYCYEKLNIEGTEKGNCGRNKETWIQCNKQDVLCGYLLCTNISNVPRLGELDGDVTSSSIVNQGKLYNCSGGHVKLDEDTDLGYVEDGTPCGTGMMCLEHRCLPIDSFNFSTCLGSTNKICSGHGVCSNEVRCICDRFWTGEDCSSYLHYDHIKPEGDNRDEGVISTNIIIGAIAGTILVLALVLGITAWGYKNYRRERQIPQGDYVKKPGDADSFYSDLPPGVSSNSASSSKKRSAILSHFQISACSIPHYSISQNISLFCRRSNGLSHSWSERIPDTKHVSDVCENGRPRSNSWQGNVTSSRKKLRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRRYPYPMPPLPDEERKASKQSARLWETSI", "text": "FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MSTSNAQSGRAAAIARRNAQVKGKGYTASAAPAAPRKPAAPVAEPVVAAAPAPSQPSRSRRKVSVAPTATPAASAAGREAAKLKRQQQKNGKSSAGAANAMPHPKAKAKQKPEEPIVEPRQAKAEKPTKRSERRTGVKPQVASQQPSGRLQSKAYRKAQAKGKAGQEAFKSNGSSQSGAKAKLANPDASTREIAQQVRAERCAQGKTCSTGGSRPMRKRRNAKEAPQKVGESQTLHGQSVSGTQVGQGEKKMTGSESGACQLVSGTEYLGAEEFSKNCDVQPTPQPAKVTQTQTTRGQVVSGSTKVGRSDKMTGNETGTCSAITGTEYLPADQSKMYCGETPAKSKATGFSVMSQATQKSEQKVTGGDSRKSQSTTFKPKNPASAPHKVMPSQTAKGNTTTGSQVGRLESVTGGERGSCHAVTGTGYQGAEEAKACDMPMTETADKVTASGTAGGQKVTGDRSGAYYGMTGAEAGDCKTITGTSYTGTEQFQFCSVDEQNEMKVRQRKGANPSISGVQPGPQGLTGAQKGACELVTGSHYQGGDQTAMVCDSTNAAAPGESDFPAMIGQAQPAFSTNEVEPMVDEGSKITGDGWDRGSKVTGTDGPWAAQRNASIRGVAGQSPMGASQYRPVNNEVPMSPITGSSGNTDTGAKVTLSGGARA", "text": "FUNCTION: Required for alpha-carboxysome (Cb) assembly, mediates interaction between RuBisCO and the Cb shell. The protein is probably intrinsically disordered. The C-terminal repeats act as the encapsulation signal to target proteins to the Cb; they are necessary and sufficient to target both CsoS2 and foreign proteins to the Cb. The N-terminal repeats of this protein bind simultaneously to both subunits of RuBisCO. Probably also interacts with the major shell proteins (CsoS1); that interaction would increase the local concentration of CsoS2 so that it can condense RuBisCO and full carboxysomes can be formed. SUBCELLULAR LOCATION: Carboxysome Note=This bacterium makes alpha-type carboxysomes. SIMILARITY: Belongs to the CsoS2 family."}
+{"protein": "MPRAPALLTNDARHQFTCCLCLHVRTGTIIFGITQIIIQLVFISFLFLMTFNPRLIPEDNHGNTDPSEDKIRFYVFSTLFRLVPAVSDIHESLTLPSPGTRNVNGNKLYLGHNVESETNFNYDIPPGYKDDVLVDVNNMSPSLVSYTQKNERGSHEVKIKHFSPYIAVCVTTFSLAFCCFMVHGAITKQPTHLLPFFFIQVFDLIICLIHILGFMSSTSDLRLMIHTKTGPIYIKSTGFTFIILSISCMMLAFKAYCLGMVWDCYKYLMLNRRGNLLDDWYSDQWGHLSTFWSLLRAGRNRGNNSIGNSGSPNEPNTRPRPEPITYDPANDLPKYEDILKIPANAYAPPPYYCSNINGNVNTTEASAVTTNTSNSATAANTTTTTTNTGTTTSVISTLTTTNKDDTQINSAPSNAHSSC", "text": "FUNCTION: Cell surface receptor that binds to human complement C2a protein. This results in inhibition of the classical and lectin pathways of complement activation, probably due to interference with binding of C2a to C4b and interference with cleavage by C1 or MASP2 such that C3 convertase cannot be formed. This infers resistance to complement-mediated cell lysis, allowing parasite survival and infection (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Located on the surface tegumental plasma membrane, and tegumental surface pits of adult schistosomes so in contact with host blood plasma."}
+{"protein": "MVTAAMLLQRCPVLIRSPTGLLGKMIKTHQFLFGIGRCPILATQGPSFSQIHLKATKAGGDSPSWAKSHCPFMLLELQDGKSKIVQKAAPEVQEDVKTFKTDLPTSLASTSLKKTFSSPQEPEKNSEKVTHLIQNNMAGDHVFGYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAEHFFEASVASKDVSVWCSNDYLGMSRHPRVLQATQEILQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLKKSNPETPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGDAMLNTRICDLLLSKYGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLEAWTEVGLPLQDISIAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA", "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": "MVTEPLTKPALVAVDMRPARRGERLFKLAASAAGSTIVIAILLIAIFLLVRAVPSLRANHANFFTSTQFDTSDDEQLAFGVRDLFMVTALSSITALVLAVPVAVGIAVFLTHYAPRRLSRPFGAMVDLLAAVPSIIFGLWGIFVLAPKLEPIARFLNRNLGWLFLFKQGNVSLAGGGTIFTAGIVLSVMILPIVTSISREVFRQTPLIQIEAALALGATKWEVVRMTVLPYGRSGVVAASMLGLGRALGETVAVLVILRSAARPGTWSLFDGGYTFASKIASAASEFSEPLPTGAYISAGFALFVLTFLVNAAARAIAGGKVNG", "text": "FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import; probably responsible for the translocation of the substrate across the membrane. FUNCTION: Part of the binding-protein-dependent transport system for phosphate; 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. CysTW subfamily."}
+{"protein": "MTEPQFRSKGPELLVELSQHVADTVKTVTELDPQTAELVGNARFAKHMMTVWGGQNVYFPMGISWRASQRDLQIYEEFDGRNHSALAKKYNVSLQWIYKIVRTMRKEELLAKQHTQA", "text": "FUNCTION: Regulates pectin lyase production in response to DNA damage. SIMILARITY: Belongs to the c/mor transcriptional regulatory family."}
+{"protein": "MKENNNAEILELKKQFTALQQKCGAKTDTIVRLGQDLEKSENEKKGLAARVETLERNLERSERELQLVCACQNDMKIKFGTERQDLIEDIEKYKRENQQLRTDRQELLDQKADLKKDCKTFRQTIAQFEVEKMGGPVRNSFSTENDEVSKLEAHEKLQAKCKGLESDLRSMLGIKEELLMERDEMQRKVARLSNELSYLLNGDPRRVAEDLDSLVAENRFLKAKLNTAEEESESIKMTLAKYKQMAEAVNVQTMVNRSPKAGEGDDKPSVAVINMKQIRELLASHAIELVESDYRAITTILLDLCNDKQMALAHSRRANKVLGMRLHEVESKLAVLDIKSRSSSPRHELPRDEDIELVVPKAVASTSSK", "text": "SUBCELLULAR LOCATION: Cell projection, cilium Note=Localizes to the base of the cilium. SIMILARITY: Belongs to the CCDC149 family."}
+{"protein": "MNKKYFKKYSWVLILSTSILAPMTLASCNHNVAKKEDKTQNDSSNLSNKTNKSDPNDHLKDKDKNVSQDNKDSTNKAVSNENSQTQSQKTNESSQNTKDDSSKTSNLITNQNSSSNTKSKIQENKQSQKDQNTSAVNVSALEKQTKNDENISLVNSKDTNVILKNDEKVALAKDDSKEKSKNSSNLNLKTPVENRQNKNEVKDDKKALQWWQKLNESASILESFSYDQTSLSLTFKEGMPLGLEVVLKLENLDSHEEKEISFKTTNGKVQNVLLTSSNLTSGKWKIKSFSFDKTYSHSPTIETTFDFKTNEKLKQERIEKIQKAIDKYQIKIKQNYKDKPLISKYALSNFDLNLNFKDLEIVNNSLKFDGSNLNQDLKSEKQMKITFEKVSENQANKTRKAHFKITTLDNLVFEKTLEWSYKTNKEYLDEFKNGSALWDDLQASLTSVFEKSLWHPYQLPKAKSKINTINLINDVSASFQGYDYLDDFNGSAKLKFKLQRGQEQRDITFTINGFLKVSLIDPLYKGNLRNSEFDVKASSNGYWLGQYYTAAEVFKHYSNGKSYWYATANDGNPWLEFS", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the M.pulmonis LipAB lipoprotein family."}
+{"protein": "MARKHTFPSLKRAEILECIDGLGIPFTAKELDQPTSKAVIPLYEEFLDLFMGLTRQNLEEKVNSLQDSVENFEIIHESLRFTVFYQILSQFMQNICFHDFTIQDLLKPDRNRLQLILSAVINFAKLREERLQQFDDDIQKRESLLETYTLLDAQRKDLEEKVLLSQDRKLESEAIIKQNEERNEEMFQSLIEDKRLCSQVRTEYDRIRMEASELKIRYHNVDSLMASTLEEIEKLQSSIVHSPEKLKGKIADTSLRIQNDRSQQVELDKKSKILHTKLNSLQLIEGDLNACLKVLEECLVELDKLEHATVLLSTNQELCDQIEINKKKLEFRKEQLLKQLSNAQEKLEHEQHSRNQKLEAAKQRMDNIREEYKVITQERNKKIQETEKKNAMIEMTEQKIAGMREELESQISSITMEFEKLKSHVELYIAELLRNLRSSNS", "text": "FUNCTION: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. 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. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Associated with kinetochores. SIMILARITY: Belongs to the NUF2 family."}
+{"protein": "MLSRRGHRLSRFRKNKRRLRERLRQRIFFRDKVVPEAMEKPRVLVLTGAGISAESGIRTFRAADGLWEEHRVEDVATPEGFDRDPELVQAFYNARRRQLQQPEIQPNAAHLALAKLQDALGDRFLLVTQNIDNLHERAGNTNVIHMHGELLKVRCSQSGQVLDWTGDVTPEDKCHCCQFPAPLRPHVVWFGEMPLGMDEIYMALSMADIFIAIGTSGHVYPAAGFVHEAKLHGAHTVELNLEPSQVGNEFAEKYYGPASQVVPEFVEKLLKGL", "text": "FUNCTION: NAD-dependent lysine deacetylase that specifically removes acetyl groups on target proteins. Also acts as a protein-lysine deacylase by mediating protein desuccinylation and de-2- hydroxyisobutyrylation. 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": "MDNIDEDLTPEQIAVLQKAFNSFDHQKTGSIPTEMVADILRLMGQPFDRQILDELIDEVDEDKSGRLEFEEFVQLAAKFIVEEDDEAMQKELREAFRLYDKQGNGYIPTSCLKEILKELDDQLTEQELDIMIEEIDSDGSGTVDFDEFMEMMTGE", "text": "SIMILARITY: Belongs to the troponin C family."}
+{"protein": "MMVFVVFVMCRYKILEELGDGTCGSVYKAVNLETYEVVAVKKMKRKFYYWEECVNLREVKALRKLNHPHIIKLKEIVREHNELFFIFECMDHNLYHIMKERERPFSEGEIRSFMSQMLQGLAHMHKNGYFHRDLKPENLLVTNNILKIADFGLAREVASMPPYTEYVSTRWYRAPEVLLQSSLYTPAVDMWAVGAILAELYALTPLFPGESEIDQLYKICCVLGKPDWTTFPEAKSISRIMSISHTEFPQTRIADLLPNAAPEAIDLINRLCSWDPLKRPTADEALNHPFFSMATQASYPIHDLELRLDNMAALPNLELNLWDFNREPEECFLGLTLAVKPSAPKLEMLRNVSQDMSENFLFCPGVNNDREPSVFWSLLSPDENGLHAPVESSPLSLSFSPMQQHTVGPPQSSGFTMTSSMQPNMLDRPWMAVSAPFQQSHYL", "text": "FUNCTION: May play a role in the regulation of plant growth and development. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "MLETLRERLLSVQQDFTSGLKTLGDKSREAKKSRQRTAQCSPEFSAGLELLSRYEDAWAALHKGAKDCAKAGELVDSEVVMLSAHWEKKRNSLVELQDQLQQIPGFLADLECLTASLARLEANFEEMETHLLCLEDLCEQCELERYKCVQTLQLENYKKTKRKELENFKAELDAEHAQKVLDMEHTQQMKLKERQKFFEEAFQQDMEQYLSTGYLQIAERREPIGSMSSMEVNVDMLEQMDLMDMSDQEALDVFLNSGGEDNNMLSPMLGPDSSTYVNEISLQVPSQSELRHKLSSLSSTCTDSASQEASEGESPVVQSDEEEVQVDTALAAVAERKGASDVSDESDSQTI", "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 Note=Detected at axon terminals and in dendrites. Detected at synapses, at postsynaptic density, at presynaptic vesicle membranes and microtubules. Detected at tubulovesicular elements in the vicinity of the Golgi apparatus and of melanosomes. Detected in neuron cell bodies, axons and dendrites (By similarity). SIMILARITY: Belongs to the dysbindin family."}
+{"protein": "MRRLVYCKVVLATSLMWVLVDVFLLLYFSECNKCDDKKERSLLPALRAVISRNQEGPGEMGKAVLIPKDDQEKMKELFKINQFNLMASDLIALNRSLPDVRLEGCKTKVYPDELPNTSVVIVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKTLEVPVKIIRMEERSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFRKATPYTFPGGTGHVINKNNRRLAEVWMDEFKDFFYIISPGVVKVDYGDVSVRKTLRENLKCKPFSWYLENIYPDSQIPRRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLSGPVIMLKCHHMRGNQLWEYDAERLTLRHANSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRNMTLGT", "text": "FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine (GalNAc) residue from UDP-GalNAc to a serine or threonine residue on the protein receptor (By similarity). Generates GalNAc-O-Ser/Thr structure also known as Tn antigen, which itself is immunogenic but also serves as a precursor for the synthesis of different mucin-type O-glycan core structures (By similarity). Contributes to the synthesis of O-linked glycans on mucins and proteoglycans of the central nervous system (By similarity). Can glycosylate both unmodified peptides and glycopeptides that already contain an O-linked GalNAc sugar. Transfers GalNAc to Thr-/Ser-rich tandem repeats GTTPSPVPTTSTTSAP of MUC5AC. Transfers GalNAc to three consecutive serine/threonine residues on SDC3 forming a triplet-Tn epitope expressed in Purkinje cells of the developing brain (By similarity). May promote neurogenesis through glycosylation and stabilization of PDPN (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily."}
+{"protein": "MSSAAPAKKPYRKAPPEHRELRLEIPVSRLEQEESLTDAERMKLLQQENEELRKRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHALASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDARNTINKLEELNERYRLDCNLAVQLLKCNKSHFRNHKLADLPCELQDMVRKHLRSGQEVASPSPSPSSSLSPGAVVPTSVIARVLEKPESLLLNSAQSGSAGRPLAEDVFVHVDMSGGDPASPPAPGSPNGECCSVSTAGGSPEEELPLPAFDKLSPYPTPSPPHPLYPGRKVIEFSEDKIRIPRNSPLPNCTYATRQAISLSLVEDGSERAHRSSVPSSPASAQGSPHHQPSPAPSALSAPASSASSEEDLLASWQRAFVDRTPPPAAVVQRTAFGRDSLPELQLHFSPGHSTAPPPSPHRERGLVLPAEPDSGFPQDEEEEMLNLPVSPEEERQSLLPDKEGTEEASGPSHVDGRAWPLPSPSRPQRSPKRMGVHHLHRKDSLTQAQEQGTVLS", "text": "FUNCTION: Plays a role in regulating the structure of the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network Cell junction, tight junction Cell membrane; Peripheral membrane protein Note=Recruited to tight junctions (TJ) during late stages of maturation of the TJ complexes. Excluded from adherens junctions and desmosomes."}
+{"protein": "MDDIDSSDGAAAARAGEIGSIGVSTPWKPIQLVFKRYLPQNGSASKVHVAVKKPVVVRLTRDLVETYKICDPQFKYRGELNPKRYLTTPSVGVNNDGFDNVNYDLILAVNDDFCSSDSRQRYIVKDLLGHGTFGQVAKCWVPETNSFVAVKVIKNQLAYYQQALVEVSILTTLNKKYDPEDKNHIVRIYDYFLHQSHLCICFELLDMNLYELIKINQFRGLSLSIVKLFSKQILLGLALLKDAGIIHCDLKPENILLCASVKPTEIKIIDFGSACMEDKTVYSYIQSRYYRSPEVLLGYQYTTAIDMWSFGCIVAELFLGLPLFPGGSEFDILRRMIEILGKQPPDYVLKEAKNTNKFFKCVGSVHNLGNGGTYGGLKSAYMALTGEEFEAREKKKPEIGKEYFNHKNLEEIVKSYPYKINLPEDDVVKETQIRLALIDFLKGLMEFDPAKRWSPFQAAKHPFITGEPFTCPYNPPPETPRVHVTQNIKVDHHPGEGHWFAAGLSPHVSGRTRIPMHNSPHFQMMPYSHANSYGSIGSYGSYNDGTIQDNSYGSYGGTGNMFAYYSPVNHPGLYMQNQGGVSMLGTSPDARRRVMQYPHGNGPNGLGTSPSAGNFAPLPLGTSPSQFTPNTNNQFLAGSPGHHGPTSPVRNSCHGSPLGKMAAFSQINRRMSAGYSGGSQSQDSSLSQAQGHGMDNFYQNEGYSGQFSGSPSRRQLDSGVKNRKQTQGGTTLSTGYSTHNNANSSLRSNMYNPSSTAHHLENPDTALSVPDPGDWDPNYSDDLLLEEDSADESSLANAFSRGMQLGSTDASSYSRRFNSNASTSSSNPTTQRRYAPNQAFSQVETGSPPSNDPHARFGQHIPGSQYIPHVSQNSPSRLGQQPPQRYNHGRPNAGRTMDRNHMNAQLPPSNTNSGGQQRSPRSSSYTNGVPWGRRTNNHVPNVPSTSHGRVDYGSIA", "text": "FUNCTION: Dual specificity protein kinase that phosphorylates ANN1, ANN2 and CP29B at serine and threonine residues, and ANN1, ANN2 and ANN4 at tyrosine residues. May regulate the phosphorylation status of annexin proteins (PubMed:26452715). Acts as positive regulator in abscisic acid (ABA)-mediated regulation of postgermination growth and drought response. May regulate the expression of ABA-responsive genes such as RD22, RD29A, LTI65/RD29B and RAB18 (PubMed:27264339). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "QQGEGGPYGGLSPLRFS", "text": "SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MEFSRETRRLALQKMQERDLDLLIIGGGITGAGVALQAAASGLDTGLIEMQDFAQGTSSRSTKLVHGGLRYLKQFDVEVVSDTVSERAVVQQIAPHIPKPDPMLLPVYDEPGSTFSMFRLKVAMDLYDLLAGVSNTPAANKVLTKEEVLKREPDLKQEGLLGGGVYLDFRNNDARLVIENIKRANRDGALIASHVKAEDFLLDDDGKIIGVKARDLLSDQEIIIKAKLVINTTGPWSDEIRQFSHKGQPIHQMRPTKGVHLVVDRQKLPVSQPVYVDTGLNDGRMVFVLPREEKTYFGTTDTDYTGDLEHPQVTQEDVDYLLGVVNNRFPNANVTIDDIESSWAGLRPLLSGNSASDYNGGNSGKVSDDSFDHLVDTVKAYINHEDSREAVEKAIKQVETSTSEKELDPSAVSRGSSFDRDENGLFTLAGGKITDYRKMAEGALTGIIQILKEEFGKSFKLINSKTYPVSGGEINPANVDLEIEAYAQLGTLSGLSMDDARYLANLYGSNAPKVFALTRQLTAAEGLSLAETLSLHYAMDYEMALKPTDYFLRRTNHLLFMRDSLDALIDPVINEMAKHFEWSDQERVAQEDDLRRVIADNDLSALKGHQEG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family."}
+{"protein": "MSTKDKLNLPPKRTINTRLSTPVHIPPPINSESTRITPQHGSPPRFGDHRISAAQGLFQRRRNARKIDHPLGWFLKNRHAAAHIPQRTTKTSQKLVLLPENHAVNSFNEEESNYEDLLTPSDAYNLIKLENLPRDKREELGFPRATAYCVCEAFQLPKVKHFLKHYHKVRAKKYDEVLYAVYHLPLVYGRSESCRVSSGPAPDDMPSSASNHNQKHLDSDKPDNENFDSHIISQLYRISEIFVFSYGVVVFWNFSLSQEKDILADLTFGGDNSLMVKPLAEEECEIEDLHFHYAPNTKRPRIYNDMIHIPSADNKMKLAMSHALAQSVKLSRFELRTDVTMNSALFYPKKLALYGHLGLSRVEVVRMSGHLFQLRVDVNLISNILDTPDFLWDSEPLLLPLYTAFREYLEIGPRTNVLNRRCKVIFDMLDIFGKSSADRKMNSITWIIIILISLFVIIFTLEVILRLRWAHR", "text": "SUBCELLULAR LOCATION: Nucleus membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RMD1/sif2 family."}
+{"protein": "MLHRINPVRFSMQSCQRYFSKLVSPLEQHKSNTFTNRVRIPIEAGQPLHETRPFLIKSGELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQFASGAVFYPFQQENDLFYLSGWNEPNSVMILEKPTDSLSDTIFHMLVPPKDAFAEKWEGFRSGVYGVQEIFNADESASINDLSKYLPKIINRNDFIYFDMLSTSNPSSSNFKHIKSLLDGSGNSNRSLNSIANKTIKPISKRIAEFRKIKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSFLHYKFISGGCDKDAYIPVVATGSNSLCIHYTRNDDVMFDDEMVLVDAAGSLGGYCADISRTWPNSGKFTDAQRDLYEAVLNVQRDCIKLCKASNNYSLHDIHEKSITLMKQELKNLGIDKVSGWNVEKLYPHYIGHNLGLDVHDVPKVSRYEPLKVGQVITIEPGLYIPNEESFPSYFRNVGIRIEDDIAIGEDTYTNLTVEAVKEIDDLENVMQNGLSTKFEEDQVAPL", "text": "FUNCTION: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome. SUBCELLULAR LOCATION: Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=Has the same dual localization (mitochondrion and nucleus) as one of its substrate, NFS1. SIMILARITY: Belongs to the peptidase M24B family."}
+{"protein": "MVRAKNWTLKKHFHGHPTDSDFELKTVELPPLNNGEVLLEALFLSVDPYMRLGSKRLKEGDTMMGQQVARVVESKNPAWPVGTLVLAHSGWASHSISDGQQLEKLLTEWPDTLPLSLALGTVGMPGITAYFGLLEICGAKSGDTVLVNAAAGAVGAVVGQIAKIKGCRVVGAAGSEEKVDYLKKIGFDFAFNYKTVKSLEETLKKAAPDGYDCYFDNVGGEFSNTVIRQMKKFGRVAICGAISMYNSTGQLPPGPSPESVLYQEIRMEGFIFNRWKGEVGQKALKELLTWVLEGKIQYREFVIEGFENMPAAFMRMLKGENVGKARSESLKSGTCKPGDHPHDLIFPIT", "text": "FUNCTION: NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX). Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2- alpha (By similarity). Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites (By similarity). Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil recruitment at the inflammatory site (By similarity). Plays a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta- unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen- 2-one (By similarity). May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family."}
+{"protein": "MKPQSSFNKLMFIPLVLFLLLVVAFLIQLTRNANGEDPTMLESALIGKPVPAFKLESLEQPGKTFDQAVLRDGKPILLNVWATWCPTCRAEHEYLNKLAAQGIRVVGLNYKDDRSKAVQWLNSLGNPYFLSLYDGDGMLGLDLGVYGAPETFLIDGQGVIRYRHAGDLNDRVWQQEILPLYKKYQGGA", "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": "MAAPRASLRLVAPVWNRGTSGIRGLSKAVDPEGSQKKGRTLLQFLTDHFYDVEAVREYLLRKQVLKVQKKNRSFTYIKERYGPYVAGAYFVLKQGGAVKFRDREWMRANEQGLSSLEFRKLQEVPVEAVDASGCAINYQGLDNLLALKELQSLSLRRCPHVDDWCLGRLYQLADSLQELSLAGCPRISERGLACLHHLQNLRRLDISDLPAVSNPGLTQILVEEMLPHCEVLGADWAQGLKVGPEEQSRDAASSPIPAWPSAPPHQARSLPGCAERPTAHPSGSVGLTQLGGSGWGEGRRA", "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": "MGSLRRSTSNRSRKKGTAVKMNRMPSSLSPPTPPCSAIVGGTGKSKKRRGGVCLWTRFDRTGFMEVAGCDKSTIIERSSVSAKDLRTAFSHSSKILAREKAIVLNLEVIKAVITSEQVMLLDSLRPEVLTLTDRLKHHFPRKDGPENILQASSHGHQEGGEEGLKSKLPFEFRVLEIAFEVFCSFVDSNVVDLETQAWSILDELTKKVSNENLKDLRSLKTSLTHLLARVQKVRDEIEHFLDDKEDMEDLYLTRKWIQNQQTEAASNSIVSQPNLQRHTSNRISTSMVTEEDDIDDMEMLLEAYFMQLEGMRNKILLMKEHIDSTEAYVKILQNSRRNGLIHLMMLVNIGNYAITAGTVVVNLFGMNIPIGLYSTPDIFGYVVWAVVALCIVLFIVTVGYAKWKKLLD", "text": "FUNCTION: Magnesium transporter that mediates the influx/efflux of magnesium in a concentration-dependent manner. Plays a crucial role in male gametophyte development and male fertility. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35.5) family."}
+{"protein": "MILLLAGTSDARALAVQVKKAGYDVTATVVTDNAAIELQRAEVKVKIGRLTKEDMTDFINEHGVKAIVDASHPFAEEASKNAIGAAAETAIPYIRYERASQAFTYDNMTMVSTYEEAAEVAAEKKGVIMLTTGSKTLQVFTEKLLPLSDVRLVARMLPRLDNMEKCQQLGLPQKNIIAIQGPFTKEFDRALYKQYGVTVMVTKESGKVGSVDKKVEAAKELGLDIIMIGRPKIEYGTVYSTFEEVVHALVNQTRS", "text": "FUNCTION: Catalyzes the reduction of the macrocycle of cobalt- precorrin-6A to cobalt-precorrin-6B. SIMILARITY: Belongs to the precorrin-6x reductase family."}
+{"protein": "MGRGRIEIKKIENINSRQVTFSKRRNGLIKKAKELSILCDAEVALIIFSSTGKIYDFSSVCMEQILSRYGYTTASTEHKQQREHQLLICASHGNEAVLRNDDSMKGELERLQLAIERLKGKELEGMSFPDLISLENQLNESLHSVKDQKTQILLNQIERSRIQEKKALEENQILRKQVEMLGRGSGPKVLNERPQDSSPEADPESSSSEEDENDNEEHHSDTSLQLGLSSTGYCTKRKKPKIELVCDNSGSQVASD", "text": "FUNCTION: Probable transcription factor involved in the negative regulation of flowering, probably through the photoperiodic pathway. Prevents premature flowering. Downstream regulator of a subset of the MIKC* MADS-controlled genes required during pollen maturation. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSQPVQRAAARSFLQKYINKETLKYIFTTHFWGPVSNFGIPIAAIYDLKKDPTLISGPMTFALVTYSGVFMKYALSVSPKNYLLFGCHLINETAQLAQGYRFLKYTYFTTDEEKKALDKEWKEKEKTGKQ", "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": "MIRLFTFAIITVFLIVISRLALQRAYKYIKLNKKINNTESKTRLSIRLVSTVPYYLPLFEGLQNFGQYVLPDYPVAAIPLYKKIILPMLIFYMNHAILGLVTFFALYYVLVRNKSPIPVHQLVRFNSMQSILLFLVGSLFGAVFRAFPIEFRISFLGLMVCNMMFWFVLSTITYSIVKAVQGKYSNIPVISEAVRIQISGYST", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tic20 family."}
+{"protein": "MAGEGDQQDAAHNMGNHLPLLPAESEEEDEMEVEDQDSKEAKKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL", "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 (PubMed:33009960). Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 (PubMed:20223979, PubMed:24328678, PubMed:25043012, PubMed:25108355). 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 (PubMed:18414909, PubMed:29530986). Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (PubMed:18414909). 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 (PubMed:31620128). SUBCELLULAR LOCATION: Cytoplasm Nucleus Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CRBN family."}
+{"protein": "MVGSGAAGGGGGGGGGGDHARSKEAAGMMALHEALRNVCLNSDWTYSVFWTIRPRPRCRGGNGCKVGDDNGSLMLMWEDGFCRPRVAECLEDIDGEDPVRKAFSKMSIQLYNYGEGLMGKVASDKCHKWVFKEPSECEPNIANYWQSSFDALPPEWTDQFASGIQTIAVIQAGHGLLQLGSCKIIPEDLHFVLRMRHMFESLGYQSGFFLSQLFSSSRGTSPSPSSFPLKQQQPPPPQLFNWPGHAPPQLPPGASPLFPPGPAAFHPSSRPMPPFPGGGKDESHLFHLPPAAAAKQPQHMDEHHHHQQQPMAAPQQHGGEAPEGDLKWPNGLSFFTALTGRTEDAKFLFGGGGGGGADDGSKTAAAAQDAGHGGAENVEEYLSLESHSNKARRMESAQSTKFKRSFTLPARMSSSTTSTSPSVSASTAPAPPQQQQGMEYRGPHEGGVYSDLMETFLE", "text": "FUNCTION: Involved in the repression of jasmonate (JA)-induced genes. Forms a ternary complex with TIFY11A/JAZ9 and BHLH094 to negatively regulate JA-responsive genes. Involved in transcriptional regulation in the root tip. Plays a regulatory role in root cell elongation. Regulates root cell elongation during salt stress. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MRELGRRLAKLLRAGDLVMLSGELGAGKTTLTRGLGEGLGVRGAVTSPTFVIARVHPSLGDGPPLVHVDAYRLSGGLDEMEDLDLDVSLSDSVIVVEWGEGKVEELTEDRLRLRIDRAVGDTADEVRHVTVTGLGERWATADVSVLAG", "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": "MARSRCVHRVVHQAACIGVIGLSTSALTTCDFTGIFVAIQSEVPIKTPSIPGAIYGLVKAGSKLYATNGQLWKKNVAEEGKDWERESCFDSVIGDSRITSLAADNGENGVLVACILGKGAYKWSQGSADQTSGNPSALSGTEKALSVVGTGTSCVYLNHTDDKVGETSSSESGGMTASGETNEFCLHAGNGFLVTTKKVCVGSDGSPVAKSDGEEPVPPILAATDDGSGHVYILTKDKVYCKKVNQSEGKIQDCPQSAAAAPEPTGAHSVAHKVADAHSIAFFKNGSDEFLLIGGRQGYGEIKLERGSGSNGNGAQCVHLKEENVHDQTGWHEKGSTPKGSAEQYRSTIGRWAVSGIYVIKKSTSGGRGKRSTSTDCERPDLYVAVGDTNDTYTGLWRFDSAAQKWNRE", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the TP013X lipoprotein family."}
+{"protein": "MVQGKGLTGFILAIILLQGSLAQSFEENRKLNVYNQEDGSVLLTCHVKNTNITWFKEGKMIDILTAHKNKWNLGSNTKDPRGVYQCKGSKDKSKTLQVYYRMCQNCIELNAATILGFVFAEIISIFFLAVGVYFIAGQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLRMN", "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 to this role of signal transduction in T-cell activation, CD3G plays an essential role in the dynamic regulation of TCR expression at the cell surface. Indeed, constitutive TCR cycling is dependent on the di-leucine-based (diL) receptor-sorting motif present in CD3G. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MDSTDKKVQVASRLPVPPKRKYVSNDENQEQMQRKRLRSSLESELPAVRVAASIATSKPRAAPVAALPKPQVIGRQSLAVMRPKNSGPGITSTSFSGKTKVSSSVTQPAAIGAEKKKRAAWDLKGQVNDMRDTVSNYKGKMQNLTGENARLLNSKEKLQREVEVLASENSKLSQERCTLESQLREVRQQVSTFEREVARLTELCQRQEKELSSHTNTIEELQGANAILTKQLLDKEVKLDCVSGENTSLKHTVNEQTDEIAALKVCLAEKDTEVHSLDTERRRLHNLVQELKGNIRVFCRVRPTLTPERELPAGHISFPSNDGKAIVLSKMEESHIGREKKDAVKYDFNFDCVFPPPCSQESVFEEISLLVQSALDGYPVCIFAYGQTGSGKTYTMEGPEDVTDDSMGMIPRAIHQIFSSAEELKAKGWQYTFTASFLEIYNETIRDLLINRPDKKLEYEIRKVNSANMLLYVTNLRYVKVSCVEEVHELLKIAKANRSVAKTAINDRSSRSHSVFQLKIEGENKQRDLKTSSMISLIDLAGSERLDRSLSTGDRLKETQCINTSLSTLGMVITSLCNKDSHIPYRNSKLTYLLQNSLGGNAKVLMFVNISPLEENFAESLNSLRFASKVNECVIGTARANRK", "text": "FUNCTION: Promotes mitotic spindle assembly. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. NCD subfamily."}
+{"protein": "MKMTRLYPLALGGLLLPAIANAQTSQQDESTLVVTASKQSSRSASANNVSSTVVSAPELSDAGVTASDKLPRVLPGLNIENSGNMLFSTISLRGVSSAQDFYNPAVTLYVDGVPQLSTNTIQALTDVQSVELLRGPQGTLYGKSAQGGIINIVTQQPDSTPRGYIEGGVSSRDSYRSKFNLSGPIQDGLLYGSVTLLRQVDDGDMINPATGSDDLGGTRASIGNVKLRLAPDDQPWEMGFAASRECTRATQDAYVGWNDIKGRKLSISDGSPDPYMRRCTDSQTLSGKYTTDDWVFNLISAWQQQHYSRTFPSGSLIVNMPQRWNQDVQELRAATLGDARTVDMVFGLYRQNTREKLNSAYDMPTMPYLSSTGYTTAETLAAYSDLTWHLTDRFDIGGGVRFSHDKSSTQYHGSMLGNPFGDQGKSNDDQVLGQLSAGYMLTDDWRVYTRVAQGYKPSGYNIVPTAGLDAKPFVAEKSINYELGTRYETADVTLQAATFYTHTKDMQLYSGPVRMQTLSNAGKADATGVELEAKWRFAPGWSWDINGNVIRSEFTNDSELYHGNRVPFVPRYGAGSSVNGVIDTRYGALMPRLAVNLVGPHYFDGDNQLRQGTYATLDSSLGWQATERMNISVYVDNLFDRRYRTYGYMNGSSAVAQVNMGRTVGINTRIDFF", "text": "FUNCTION: Receptor for the bacteriocin pesticin and for the siderophore yersiniabactin. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family."}
+{"protein": "MAFGSKILNIGSKSDEYNDDAVPLDQVEEGAQERRYYLGLTKREFKLMMLAGVGFFLDSYDLFIINLVTPIFEYLYWGGIEKGPTGKGHYPSGIRGLVNASANIGNIFGQLLFGFMGDFFGRKFVYGKEMVIVIIATVLVIAMPKSIHSPLSKMMWVFCWRWLLGVGIGGDYPMSAAITSERSKIKRRGTLISLIFAFQGFGTLAGAIVTIILLGCFEHPLNREGHYHKLEGVWRLQFGLALVPAIGVLIPRLIMKESKSYENSKALNSAEGKDPKAFFNTDDEDNMKKSSSHGDSEVVEASDRYANQADAADAEVDNIEKQFAAVTTPENSSGFITYFRQWRHFKHLLGTSVCWFLLDIAFYGVNLNQSVILKNIGFSTGTNEYRTLMKNAIGNLIIAVAGYVPGYWFNVFLVEILGRKWIQLQGFVITGLMFAILAGRWNEISTGGRFACFVIAQLFSNFGPNSTTFIYPAEVFPARVRGTAHGVSAALGKCGAILASLLFNFLTGVIGYGNVMWIFCGCMWGGILFTLLLPETKGRDADEIDRLELFYGKDGKVQCDSKWKSWYFNGIF", "text": "FUNCTION: High-affinity transporter for external inorganic phosphate. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
+{"protein": "MDDDLMLALRLQEEWNLQEAERDHAQESLSLVDASWELVDPTPDLQALFVQFNDQFFWGQLEAVEVKWSVRMTLCAGICSYEGKGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINSLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHRPPYYGYVKRATNREPSAHDYWWAEHQKTCGGTYIKIKEPENYSKKGKGKAKLGKEPVLAAENKDKPNRGEAQLVIPFSGKGYVLGETSNLPSPGKLITSHAINKTQDLLNQNHSANAVRPNSKIKVKFEQNGSSKNSHLVSPAVSNSHQNVLSNYFPRVSFANQKAFRGVNGSPRISVTVGNIPKNSVSSSSQRRVSSSKISLRNSSKVTESASVMPSQDVSGSEDTFPNKRPRLEDKTVFDNFFIKKEQIKSSGNDPKYSTTTAQNSSSSSSQSKMVNCPVCQNEVLESQINEHLDWCLEGDSIKVKSEESL", "text": "FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:27852435, PubMed:27871366, PubMed:27871365, PubMed:32649882, PubMed:30893605). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (PubMed:27852435, PubMed:27871366, PubMed:27871365, PubMed:32649882). Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis (PubMed:27852435, PubMed:27871366, PubMed:27871365, PubMed:32649882). Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (PubMed:27871366). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs (By similarity). SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage (PubMed:22902628, PubMed:23042605, PubMed:23042607, PubMed:32152270). Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation (PubMed:31316063). Does not activate CHEK1 in response to DNA damage (PubMed:31316063). May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA (PubMed:22681887, PubMed:22894931, PubMed:22902628, PubMed:22987070). Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (PubMed:22681887). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to sites of UV damage via the PIP-box (PubMed:22894931, PubMed:23042605). Recruited to stalled replication forks at sites of replication stress following deubiquitination (PubMed:22894931, PubMed:23042605, PubMed:22987070, PubMed:27871365, PubMed:32649882). CHEK1 stimulates recruitment to chromatin (PubMed:31316063). SIMILARITY: Belongs to the Spartan family."}
+{"protein": "MAASTASHRPIKGILKNKSSTTSSVVSTAEQPGKSVDEELSKKSQKWDEMSILATYHPADKDYGLMKIDEPSTPYHSMVADDEDALSDSETTEALTPDILARKLTAAAAESLEPKYRVREQESSGDEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLNDEEEDEEMSETAAGESMNMEESSQGSATSDQLQNKSQSS", "text": "FUNCTION: Inhibitor of protein-phosphatase 1. SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family."}
+{"protein": "MPPSGLRLLPLLLPLLWLLMLTPGRPVAGLSTCKTIDMELVKRKGIEAIRGQILSKLRLASPPSQGDVPPGPLPEAILALYNSTRDRVAGESAETEPEPEADYYAKEVTRVLMVEYGNKIYDKMKSSSHSIYMFFNTSELREAVPEPVLLSRADVRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLTHREEIEGFRLSAHCSCDSKDNTLQVDINGFSSGRRGDLATIHGMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS", "text": "FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1. Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia. Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs). Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency- associated peptide chain and subsequent release of the active TGF-beta- 1. FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. FUNCTION: [Transforming growth factor beta-1]: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency- associated peptide (LAP) and Transforming growth factor beta-1 (TGF- beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix. At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus. TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin- binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1. Once activated following release of LAP, TGF- beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency- associated peptide chain (LAP) and 'milieu molecules'. Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner. At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development. At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus. Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (By similarity). SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix. SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
+{"protein": "MLSPFDWRRGISSSGTGGTMAAQPLSSTAATTAAATGATAATAATAATTSATLSTAAASTSTTAAPSAGATWINHHLAVEADSSQPANGSDAQAGVEGPTMPAGYLPLYEDVETAAEDAGYALIDDISEWLLGSVGSEAAVGGPENSTNLAVTGANGTLAWLEALNSTQPAQSNSSAEDGERGRYSLRSFVEQQLAGGGAAGAGDGGDAGIALIDSGEEAALDNVADAETDYGMLGGFGDAELLQRTATVARETLGNRTAPSTTSYDGGGSGDVGVAGGLAGTAGGGVGGAGGSGGSTFMLLLENFNDYFPNYNGSTVSGTSTIAPGVAITGSRGSGLLLEQNLTGLYLDGYRLNCTNETLNLTDSCGELRVVDHNYWALILILFPILTLFGNILVILSVCRERSLQTVTNYFIVSLAIADLLVAVVVMPFAVYFLVNGAWALPDVVCDFYIAMDVICSTSSIFNLVAISIDRYIAVTQPIKYAKHKNSRRVCLTILLVWAISAAIGSPIVLGLNNTPNREPDVCAFYNADFILYSSLSSFYIPCIIMVFLYWNIFKALRSRARKQRAARKPHLSELTGGSVIENIAQTRRLAETALDSSRHASRILPDEAATNTASGSNEEEDENAISPDIDDCHVIVNDKSTEFMLATVVEETGNSVVAQITTQPQLVVADPNGNHDSGYAASNVDDVLAGVAPASASAATSAAPRSSGSPPDSPLPSGATLQRSSVSSQRRPTGDDSPKRGEPALRSVGVDNSSVAMKPLSFVRYGVQEAMTLARNDSTLSTTSKTSSRKDKKNSQASRFTIYKVHKASKKKREKSSAKKERKATKTLAIVLGVFLFCWLPFFSCNIMDAMCAKFKKDCRPGLTAYMMTTWLGYINSFVNPVIYTIFNPEFRKAFKKIMHMG", "text": "FUNCTION: Receptor for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MTTGKPNILIIMVDQLNGKLFPDGPADFLHAPNLKALAKRSARFHNNYTSSPLCAPARASFMAGQLPSRTRVYDNAAEYQSSIPTYAHHLRRAGYYTALSGKMHFVGPDQLHGFEERLTTDIYPADFGWTPDYRKPGERIDWWYHNLGSVTGAGVAEITNQMEYDDEVAFLANQKLYQLSRENDDESRRPWCLTVSFTHPHDPYVARRKFWDLYEDCEHLTPEVGAIPLDEQDPHSQRIMLSCDYQNFDVTEENVRRSRRAYFANISYLDEKVGELIDTLTRTRMLDDTLILFCSDHGDMLGERGLWFKMNFFEGSARVPLMIAGPGIAPGLHLTPTSNLDVTPTLADLAGISLEEVRPWTDGVSLVPMVNGVERTEPVLMEYAAEASYAPLVAIREGKWKYVYCALDPEQLFDLEADPLELTNLAENPRGPVDQATLTAFRDMRAAHWDMEAFDAAVRESQARRWVVYEALRNGAYYPWDHQPLQKASERYMRNHMNLDTLEESKRYPRGE", "text": "FUNCTION: Converts choline-O-sulfate into choline. SIMILARITY: Belongs to the sulfatase family."}
+{"protein": "MPFRDSLQPDTRYLTDGSLFHGYFYQYGDIWLAITFWCTVVTTISYLISGFVASFVLKKSKFSPFIPIFTAMYGMAIGICYGGISALILSAIYVSGSFLLSWYQGIICGVGLAIVHLLFAFTQGKLQV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM170 family."}
+{"protein": "MKGTFLICLILIAGFSFKSTQAGSICLEPKVVGPCTAYFPRFYFDSETGKCTPFIYGGCEGNGNNFETLHACRAICRA", "text": "FUNCTION: Serine protease inhibitor that specifically inhibits trypsin (Ki=73.8-78 nM) and chymotrypsin (Ki=993 nM) (PubMed:17886436, PubMed:17288251, PubMed:33802055). In vitro, it shows cytoprotective activity in the oxidative stress agent 6-hydroxydopamine (6-OHDA)- induced neurotoxicity model (PubMed:33802055). In this model, it decreases reactive oxygen species (ROS) level, and increases cell viability in a correlated manner (PubMed:33802055). It is possible that the observed effect is due to the ability of this peptides to act as free-radical scavenger (PubMed:33802055). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily."}
+{"protein": "MWRMTTLLHLTALLVLIPLCHCASMHRHDHYMDMDQTYPNGLGYCEPSGESSCKAGFSYNRDICQGPYHWHTISSCYKACGHKRRQSPINIWSHKAVFLPYLPRLKFKPHMKSLDTDVTNHQNRAPEFEPEDGDKLHVKLKNLVDGHYKFHNLHIHNGKSRRKGSEHSVNRHFTPMEAHLVFHHDDKKEIKPPRVKLGGVYAGRNKFVVVGVFLEVGDEGYGDEPDDDECKRILKGHCENNGDNGNNCDNGNNGNNDNNGNNGNNGNGNNGYNGNNGDNGNNGNGNGNNGYNGNNGYNGNNGNNGNGNNDNNGNDNNGNNGGNGNNGNNGNGNNGNNGNGNNGNNGGNGNNGNNGNSNNGNNGNGNNGNNGGNGNNGNNGNGNNENNGNGSNGNNGGNGNNGNNGDNGNGDNGYNGDNGNSDGRLRRWDLANVRRMHAERYHFSGGCIVKKAKRLSRILECAYRHKKVREFKRNGEEKGLDVDITPEMVLPPMKYRHYYTYEGSLTTPPCNETVLWVVEKCHVQVSRRVLDALRNVEGYEDGTTLSKYGTRRPTQRNKHPLRVYKNSI", "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). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
+{"protein": "MSTPQLMQGMQKDLTCQLCLELFRAPVTPECGHTFCQGCLTGVPKNQDQNGSTPCPTCQSPSRPETLQINRQLEHLVQSFKQVPQGHCLEHMDPLSVYCEQDKELICGVCASLGKHKGHNIITASEAFAKLKRQLPQQQVILQEARLKKEKTVAVLDRQVAEVQDTVSRFKGNVKHQLNAMRSYLNIMEASLGKEADKAESAATEALLVERKTMGHYLDQLRQMEGVLKDVEGQEQTEFLRKYCVVAARLNKILSESPPPGRLDIQLPIISDEFKFQVWRKMFRALMPALENMTFDPDTAQQYLVVSSEGKSVECADQKQSVSDEPNRFDKSNCLVSKQSFTEGEHYWEVIVEDKPRWALGIISETANRKGKLHATPSNGFWIIGCKEGKVYEAHTEQKEPRVLRVEGRPEKIGVYLSFSDGVVSFFDSSDEDNLKLLYTFNERFSGRLHPFFDVCWHDKGKNSQPLKIFYPPAEQL", "text": "FUNCTION: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)- dependent membrane resealing process (By similarity). SUBCELLULAR LOCATION: Cell membrane, sarcolemma Cytoplasmic vesicle membrane Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. SIMILARITY: Belongs to the TRIM/RBCC family."}
+{"protein": "MAAAGSCSSAGKSLLQFMKLVGQLKRVPRTGWIYRQVEKPESVSDHMYRMAVMAMLTEDRKLNKDRCIRLALVHDMAECIVGDIAPADNIAKEEKHRKEKAAMEHLTQLLPDNLKTEVYDLWEEYEHQFTAEAKFVKELDQCEMILQALEYEELEKRPGRLQDFYNSTAGKFKHPEIVQLVSAIYEERNSAIAENARTSQT", "text": "FUNCTION: Catalyzes the dephosphorylation of the nucleoside 5'- monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP). SIMILARITY: Belongs to the HDDC2 family."}
+{"protein": "MAECRASGGGSGGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHPGKDAEQDHEPPYEISVQEEITARLHFIKFENTYMEACLDFIRDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFMYQKDSDPEFRFQTNHPNIFPYLLVNIGSGVSIVKVETEDRFEWIGGSSIGGGTFWGLGALLTKTKKFDELLQLASRGRHANVDMLVQDIYGGAHQTLGLSGNLIASSFGKSATADREFSKEDMAKSLLHMISNDIGQLACLYAKLHGLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLKGAEQDNPNQYSWGENYAASSGLMSTAPELCPTQRARSGTFDLLEMDRLERPLVNLPLLLDPSSYVPDTVDLTDDALARQYWLTCFEEALDGVVKRAVASQPESVDAAERAEKFRQKYWGKLQTLRHQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQKENGLALKCFQSVTRSLDSLGWEERQLALVKGLLAGNVFDWGAKAVSDVLESDPQFGFEEAKRKLQERPWLVDSYTKWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLCRGIEVILACNSGPALNDVTYSESLIVAERIAAMDPIICTALREDRLLLVQTGSSPPCLDLSRLDKGLAVLVRERGADLVVIEGMGRAVHTNYHALLRCESLKLAVVKNAWLAERLGGQLFSVIFKYEVPAE", "text": "FUNCTION: Phosphatase which shows a preference for 4'- phosphopantetheine and its oxidatively damaged forms (sulfonate or S- sulfonate), providing strong indirect evidence that the phosphatase activity pre-empts damage in the coenzyme A (CoA) pathway. Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein. May play a role in the physiological regulation of CoA intracellular levels. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the type II pantothenate kinase family. SIMILARITY: In the C-terminal section; belongs to the damage-control phosphatase family. Phosphopantetheine phosphatase (II) subfamily."}
+{"protein": "MSSSNKNWPSMFKSKPCNNNHHHQHEIDTPSYMHYSNCNLSSSFSSDRIPDPKPRWNPKPEQIRILESIFNSGTINPPREEIQRIRIRLQEYGQIGDANVFYWFQNRKSRAKHKLRVHHKSPKMSKKDKTVIPSTDADHCFGFVNQETGLYPVQNNELVVTEPAGFLFPVHNDPSAAQSAFGFGDFVVPVVTEEGMAFSTVNNGVNLETNENFDKIPAINLYGGDGNGGGNCFPPLTVPLTINQSQEKRDVGLSGGEDVGDNVYPVRMTVFINEMPIEVVSGLFNVKAAFGNDAVLINSFGQPILTDEFGVTYQPLQNGAIYYLI", "text": "FUNCTION: Probable transcription factor, which may be involved in embryonic patterning (PubMed:14711878). May be required for basal embryo development after fertilization (PubMed:14711878). Acts partially redundantly with STIP in promoting embryonic cell division and proliferation (PubMed:17706632). Promotes cotyledon boundary formation by maintaining the symmetry in CUC genes expression domains (PubMed:22827849). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WUS homeobox family."}
+{"protein": "MDLAPRPLGRQHSKSQSAFAFDNTATSIAASTMKNELNHLASTVKDPLAKKAFQKEMDNFFSLFSRYLQEDARGSEINWDLVESPKPEQVVEYDTITEAGGLSRDYLNKLAVLKLNGGLGTTMGCVGPKSIIEVRDGNSFLDLSVRQIEHLNRKYNVNVPFVLMNSFNTDEATAKVIKKYEAHKIDILTFNQSRYPRVHKETLLPVPHTADSAIDEWYPPGHGDVFEALTNSGIIDTLIAQGKEYLFVSNIDNLGAVVDLNILNHMVETNAEYLMELTNKTKADVKGGTLIDYDGNVRLLEIAQVPPQHVEEFKSIKKFKYFNTNNLWFHLPSVKRVVNNHELSMEIIPNKKTIKHKGENINIIQLETAAGAAIRHFKNAHGVNVPRRRFLPVKTCSDLLLVKSDLYSINHGQVEMNPRRFGGTAPLVKLGAHFKKVADFSAHIPSIPKILELDHLTITGDVNIGRNVTLKGTVIIVASDANRIDIPNGSVLENCVITGNLNILEH", "text": "FUNCTION: Plays a central role as a glucosyl donor in cellular metabolic pathways. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the UDPGP type 1 family."}
+{"protein": "MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD", "text": "FUNCTION: [Isoform 2]: In tooth development, may play a role in the recruitment and the differentiation of cells that contribute to cementum formation. May also bind hydroxyapatite and regulate its crystal nucleation to form cementum. FUNCTION: [Isoform 1]: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum- bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD family."}
+{"protein": "MGAIGGDEVVQWDKMDGGEVVNGGGGGGVGKLERILVSVRLRPLSDKEIARGDPSEWECINDTTIISRSTFPDRPSAPTAYSFDRVFRSDCDTNEVYKQGAKEVALSVVSGINSSIFAYGQTSSGKTYTMTGITEYTVADIYDYIGKHEERAFVLKFSAIEIYNEVVRDLLSAENTPLRLWDDAEKGTYVENLTEVVLRDWNHLKELISVCEAQRKTGETYLNENSSRSHQILKLTIESSAREFLGKDKSTTLVASVNFVDLAGSERASQALSAGARLKEGCHINRSLLTLGTVIRKLSKVRNGHIPYRDSKLTRILQPSLGGNARTAIICTMSPARSHMEQSRNTLLFASCAKEVVTNAQVNVVMSDKALVKQLQKELARLESELRCPASYSSLESLVKEKDNQIRKMEKEIKELKLQRDLAQSRLQDLLQVVGDNHVHVSKQSSVSGRNFTFDVPQTCEDEQSTTESSEVVDSVQNFRFQGRRVAQREHKPQQAENNVQFTTPSRYSVSSPPFSGMLPTNRSDHLSQISNEDSDDICKEVRCIETNETGGNECLESSAVGSNSLQDPNAGSSMHINNDSNSSMNSRLRDESPVTLEQHLENVRKPFANIVKDLGSSTRNSSSSKVLGRSRSCRSLTGSSLFEDLEKDDCTPPNRSFIDFAGRPQNCQRRGSALNYDAESETLSRAGSMLSEITTTRDGLKANSSVAGDTEFTGIGEFVAELKEMAQVQYQKQLGHSGNGDLAEGTIRSVGLDPITDALQSPSRWPLEFEKKQQEIIDFWHACNVSLVHRTYFFLLFKGDPADSIYMEVELRRLSFLKDTYSNGAIASIPNTSLVSSAKKLQREREMLCRQMQRRLSIEERESMYTKWGVSLASKRRRLQVARCLWTETKDLEHVRESASLVARLIGLLEPGKALREMFGLSFAPQQFTRRSYNSWRYGRSSLN", "text": "FUNCTION: Binds ATP/ADP in vitro. Possesses low ATPase activity but high affinity for microtubules. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-7 subfamily."}
+{"protein": "MEKIKSAGPSSVPRHVAIIMDGNNRWARKRLLPGVAGHKAGVDAVRAVIEVCAEAKVEVLTLFAFSSENWQRPAEEVGALMELFFTALRRETKRLNENDISLRIIGDRSRFHPELQAAMREAEVRTSGNSRFVLQIAANYGGQWDIAQAAQRLAREVQAGHLQPEDITPQLLQTCLATGDLPLPDLCIRTGGEHRISNFLLWQLAYAELYFSDLFWPDFKHDAMRAALADFASRQRRFGKTSEQVEAGARA", "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": "MAKMRPSVSLDTWREYFRRGDSDIFGIIDHAIMVAAADWPKEFKSRSDRIAELLFSCKVSRCIGCDHLELSIAGDEAAVEIVGVGGGGDRGDSGVATGEGEEASVSVDEVMRIRDILSNKDDEKDSVLLESLRKLESMSMSVDILKDTEIGKAVNGLRRHSSDKISKLAKTLFAEWKRLVDQWMNTPEEMAGTEGTPESLNLSVIDEEEAFPSPPHDLDIYAPEPNGFELSQILDCLDCDGNPRHSVESKHERKSQSSAGRRPKGTNDANVVGRYCNDQQTRREEADVRPMKHSATDVVEPKRQTKQSREQMVSAIQRKPTAVTEQKRKLAGPQQDKLKALDPDSKFEFAKRKLQESYHQHENAKRQRTIQVLETIPKQNKVQKPQLKRPATRRYIYWYFWSSEFPGYELPSLILNLANPRDSSSQFSRHDELMIDIPVYFGLVLVQIDKAEMVDEMMIFKKMSVLLTEKDFVDAIVSVSLKDLTRSLFVRFEAKACPKFDLIHKTSVETVRCVGKTFMHMLSKVSREFPPRNRTHPGGLLYQRFDPTHLSLARQQVAICKETDSQYPHEIVIHWTSASA", "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 (By similarity). May play a role in transcription elongation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 26 family."}
+{"protein": "MNNVLNSGRTTICDAYNVVAHDPFSFEHKSLDTIQKEWMEWKRTDHSLYVAPVVGTVSSFLLKKVGSLIGKRILSELWGIIFPSGSTNLMQDILRETEQFLNQRLNTDTLARVNAELIGLQANIREFNQQVDNFLNPTQNPVPLSITSSVNTMQQLFLNRLPQFQIQGYQLLLLPLFAQAANMHLSFIRDVILNADEWGISAATLRTYRDYLRNYTRDYSNYCINTYQTAFRGLNTRLHDMLEFRTYMFLNVFEYVSIWSLFKYQSLMVSSGANLYASGSGPQQTQSFTAQNWPFLYSLFQVNSNYILSGISGTRLSITFPNIGGLPGSTTTHSLNSARVNYSGGVSSGLIGATNLNHNFNCSTVLPPLSTPFVRSWLDSGTDREGVATSTNWQTESFQTTLSLRCGAFSARGNSNYFPDYFIRNISGVPLVIRNEDLTRPLHYNQIRNIESPSGTPGGARAYLVSVHNRKNNIYAANENGTMIHLAPEDYTGFTISPIHATQVNNQTRTFISEKFGNQGDSLRFEQSNTTARYTLRGNGNSYNLYLRVSSIGNSTIRVTINGRVYTVSNVNTTTNNDGVNDNGARFSDINIGNIVASDNTNVTLDINVTLNSGTPFDLMNIMFVPTNLPPLY", "text": "FUNCTION: Promotes colloidosmotic lysis by binding to the midgut epithelial cells of both dipteran (Aedes aegypti) and lepidopteran (Manduca sexta) larvae. SIMILARITY: Belongs to the delta endotoxin family."}
+{"protein": "MSDKPTETVSVSESVATPAVAATEPAPSLPVVNPSSLPSGFEWWRQTMAYKTGFMSAEESVQYEQDRLIKERYAECLSCEKNKQWVMAYSPTVRFMKDQIEKIGGDISSNNVFCDHCDDFKAGGFHPKYGILVCQNHVKSRSHLEDTLAHEMVHYYDNTKFKVDWMNLKHHACSEIRASTLSGECRMMNELMKGKLARLTRGHQECAKRRAILSVMANPGCKDEAQATQVVNEVWDSCFNDTRPFDTIYR", "text": "FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Note=Associates loosely with the inner membrane. SIMILARITY: Belongs to the peptidase M76 family."}
+{"protein": "MASTEEQYDLKIVKVEEDPIWDQETHLRGNNFSGQEASRQLFRQFCYQETPGPREALSRLRELCHQWLRPEIHTKEQILELLVLEQFLTILPEELQAWVREHHPESGEEAVAVVEDLEQELSEPGNQAPDHEHGHSEVLLEDVEHLKVKQEPTDIQLQPMVTQLRYESFCLHQFQEQDGESIPENQELASKQEILKEMEHLGDSKLQRDVSLDSKYRETCKRDSKAEKQQAHSTGERRHRCNECGKSFTKSSVLIEHQRIHTGEKPYECEECGKAFSRRSSLNEHRRSHTGEKPYQCKECGKAFSASNGLTRHRRIHTGEKPYECKVCGKAFLLSSCLVQHQRIHTGEKRYQCRECGKAFIQNAGLFQHLRVHTGEKPYQCSQCSKLFSKRTLLKKHQKIHTGERP", "text": "FUNCTION: May function as a transcription factor. May be involved in the development of multiple embryonic organs. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MQNNEQTEYKTVRGLTRGLMLLNMLNKLDGGASVGLLAELSGLHRTTVRRLLETLQEEGYVRRSPSDDSFRLTIKVRQLSEGFRDEQWISALAAPLLGDLLREVVWPTDVSTLDVDAMVVRETTHRFSRLSFHRAMVGRRLPLLKTASGLTWLAFCPEQDRKELIEMLASRPGDDYQLAREPLKLEAILARARKEGYGQNYRGWDQEEKIASIAVPLRSEQRVIGCLNLVYMASAMTIEQAAEKHLPALQRVAKQIEEGVESQAILVAGRRSGMHLR", "text": "FUNCTION: Activator of the mhpABCDFE operon coding for components of the 3-hydroxyphenylpropionate degradation pathway."}
+{"protein": "MAGGIRKKTSLRDKSSRKSGLASKISEFKQQSTIENGQDEHFHENPLLKLSKISKKEKQQQKTDTFNQKLLHKVTFNTSSNISKSAVRRRKRKEKEQLKPKMDELLTSLPDDMFAPTAASTTTIRRATKTGEATSGYVKSTKANLNLPNANKATGHKQILKQENKNFTNVLKNPEFRQSPFSALKNAIKENLQG", "text": "FUNCTION: Involved in ribosome biogenesis. Required for normal pre-rRNA processing in internal transcribed spacer 1 (ITS1). May be involved in the movements of the replication forks (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the SLX9 family."}
+{"protein": "MARLVFSLNLPSSHGFNLSPRNLQSFFVTQTGAPRFRAVRCKPNPESSETKQEKLVIDNGETSSASKEVESSSSVADSSSSSSSGFPESPNKDINRRVAAVTVIAALSLFVSTRLDFGISLKDLTASALPYEEALSNGKPTVVEFYADWCEVCRELAPDVYKIEQQYKDKVNFVMLNVDNTKWEQELDEFGVEGIPHFAFLDREGNEEGNVVGRLPRQYLVENVNALAAGKQSIPYARAVGQYSSSESRKVHQVTDPLSHG", "text": "FUNCTION: Thiol-disulfide oxidoreductase that participates in various redox reactions in the chloroplast. Mediates the reduction of PSI-N in the thylakoid lumen. May interact and probably reduce other target proteins of the thylakoid membrane, such as FTSH2, FTSH8, LHCB5, atpA, atpB, atpE, petA and petC. Involved in the biogenesis of the plastid cytochrome b6f complex. Reducing equivalents are provided by stromal M- type thioredoxins and probably transduced through the thylakoid membrane by CCDA. Possesses low insulin disulfide bonds reducing activity. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the thioredoxin family."}
+{"protein": "MDKLTFPIFPAADLVNFFRQNILTGTEAKNFNKNDLYPNPKPEMVQKLYMRILQQVFSYGVEQFYMVPMDLDIQYPHLVEGFAPVANILKLMARLLPMCRVYDFHPSDVLNPKGKRTLHLLSGIFNFLQFRTTQREVYMEYCSGYKSALENVRQLQKTNHEAEIKIEKLTTVPPEQQAEFKALSSEIHDLQQIISQEYRAKDVMFQEKIAQRKAEFAEKNKRLNEQKLTIATMKEEQERMKSQIVESPEQRKSKTERMKETVHRLKQARQETSDKCDHYRDRVALAFMWQSDVQGYLKKLQNIDANLEIHRKIHEEIRHIEEQLMNLNLELKSLSNEDAQLKRIILVKKEKLAKVDIKNKKKQEDFNQQKQEILEVCSHIQEKRQVIHGRVAQVLQEIQQTISKKEQLLETTEAGKNKCQEVITDFRAALEKYHDSLQKASERSADRRREKIAELNRRLSRQ", "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. SIMILARITY: Belongs to the NUF2 family."}
+{"protein": "MAPGSWFSPLFIAVITLGLQWPKEAATFPAMPLSNLFANAVLRAQHLHLLAAETYKEFERTYIPEEQRHANKNSQSAFCYSETIPAPTGKDDAQQKSDMELLRFSLVLIQSWLTPVQYLSKVFTNNLVFGTSDRVYEKLKDLEEGIQALMRELEDRSSRGPPLLRSTYDKFDIHLRNEEALLKNYGLPSCFKKDLHKVETYLKVMKCRRFGESNCTI", "text": "FUNCTION: Growth hormone plays an important role in growth control. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
+{"protein": "MARWCPPANRSASAAATCSSVVANTACMRWCKKRSQCPARRTP", "text": "FUNCTION: May initiate with G7P 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 G7P (By similarity). SIMILARITY: Belongs to the inovirus G9P protein family."}
+{"protein": "MLKLEMMLVVLLILPLFYFDAGGQVVQRDWRSDGLARYLQRGDRDVRECNINTPGSSWGKCCLTRMCGPMCCARSGCTCVYHWRRGHGCSCPG", "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": "MHFSTLFGAAATAALAGSTNASPLARRQVPVGTPILQCTQPGLVALTYDDGPFTFTPQLLDILKQNDVRATFFVNGNNWANIEAGSNPDTIRRMRADGHLVGSHTYAHPDLNTLSSADRISQMRHVEEATRRIDGFAPKYMRAPYLSCDAGCQGDLGGLGYHIIDTNLDTKDYENNKPETTHLSAEKFNNELSADVGANSYIVLSHDVHEQTVVSLTQKLIDTLKSKGYRAVTVGECLGDAPENWYKA", "text": "FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate (PubMed:15555935, PubMed:7592838, PubMed:8987657, PubMed:9373940, PubMed:16232493, PubMed:16878976). May play a role in evasion of the host immune response; plant chitinases liberate chitin molecules from the fungal cell wall which act as elicitors of the plant immune response, deacetylation of the liberated chitin neutralizes elicitor activity (PubMed:8987657, PubMed:10913295). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide deacetylase family."}
+{"protein": "MIHEKYTEMRNEQEALLSRKNTKTSFYNGIYDRYEHPVLTREHIPLHWRYDLNKETNPFFQERLGINAVFNAGAIKLNDRYCLVARVEGNDRKSFFAVAESDKGTEGFRFRQYPVCLPALTDDETNVYDMRLTQHEDGWIYGVFCVEKSAGTADLSEAVASAGIARTKDLTNWERLPDLVTLRSPQQRNVTLLPEFVDGKYAFYTRPMDGFIETGSGGGIGFGLADDITHAVIDEERMTSIRRYHTITESKNGAGATPIKTERGWLNIAHGVRNTAAGLRYVIYCFVTDLSEPWKVIAEPGGYLIAPFKDERVGDVSNVVFTNGAIVDDNGDVYIYYASSDTRLHVAVSSIDKLLDYAFNTPADALRTAECVKQRCDLIKRNIELL", "text": "FUNCTION: Converts 4-O-beta-D-mannopyranosyl-D-glucopyranose (Man-Glc) to mannose 1-phosphate (Man1P) and glucose. Involved in a mannan catabolic pathway which feeds into glycolysis. SIMILARITY: Belongs to the glycosyl hydrolase 130 family."}
+{"protein": "MFNFNASRWTRAQAMKVNKFDLTTSMPEIGTDFPIMRDDLWLWDTWPLRDINGNPVSFKGWNVIFSLVADRNIPWNDRHSHARIGYFYSKDGKSWVYGGHLLQESANTRTAEWSGGTIMAPGSRNQVETFFTSTLFDKNGVREAVAAVTKGRIYADSEGVWFKGFDQSTDLFQADGLFYQNYAENNLWNFRDPHVFINPEDGETYALFEANVATVRGEDDIGEDEIGPVPANTVVPKDANLCSASIGIARCLSPDRTEWELLPPLLTAFGVNDQMERPHVIFQNGLTYLFTISHDSTYADGLTGSDGLYGFVSENGIFGPYEPLNGSGLVLGGPASQPTEAYAHYIMNNGLVESFINEIIDPKSGKVIAGGSLAPTVRVELQGHETFATEVFDYGYIPASYAWPVWPFPDRRK", "text": "SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 68 family."}
+{"protein": "MANAAQKKLAAQNKHILTFMLAADLIVNVLFWILRFFVRSGLSKFSKFVYAFASISSGFLHYQLHRAAAPKYDARGSLLYVGQDLLQEGVTSYMVDYMYFSWILIFLAALTSVKVFAFYLLVPIFVVYKAAPLLKMLLQQLKNFKNQALNQPPQQQQQQQQQQHQQHATPSEPVLSKRQQKLRKKAAKYSRP", "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 (By similarity). Has a role in meiosis (PubMed:16303567). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM208 family."}
+{"protein": "MKSNRQARHILGLDYRISNQRKVVTEGDTSSVVNNPTGRKRRADSQK", "text": "FUNCTION: Although this protein associates with the 30S subunit of the ribosome it is not considered to be a bona fide ribosomal protein. SIMILARITY: Belongs to the SRA family."}
+{"protein": "MARTKHTARKSFGGKAPRKSLATKAARKVFPVDGQVKKRYRPSSNALKEIRKYQKSTELLVRKLPFQRLVREVAQEIMPNVRFQSAAIQALHEAAEAYLIGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERG", "text": "FUNCTION: Putative variant histone H3 which may replace conventional H3 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 (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H3 family."}
+{"protein": "MIASGPPPRVYWTSLIFLLLACCLLPTGAQGQTYQVRVEPKDPVVPFGEPLVVNCTLDCPGPGLISLETALSKEPHSRGLGWAAFRLTNVTGDMEILCSGICNKSQVVGFSNITVFGFPKRVELAPLPLWQPVGEELNLSCLVSGGAPRAHLSVVLLRGEEELGRQPLGKEEPAKVTFMVQPRREDHGTNFSCRSELDLRSQGLELFQNTSAPRKLQTYAMPKTAPRLVFPRFWEMETSWPVNCSLNGLFPASEAHIQLALGNQMLNATVVSHADTLTATATAKTEQEGTQEIVCNVTLGVENRETRESLVAYRFQGPNLNLSESNATEGTPVTVTCAAGPQVQVMLDGVPAAVPGQPAQLQLKATEMDDRRTFFCNATLKVHGVTLHRNRSIQLRVLYGPTIDRAKCPQRLMWKEKTMHILQCQARGNPNPQLQCLREGSKFKVPVGIPFLVLLNYSGTYSCQAASSRGTDKMLVMMDVQGRNPVTINIVLGVLAILGLVTLAAASVYVFWVQRQHDIYHLTPRSTRWRLTSTQPVTVAEELS", "text": "FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM3 is also a ligand for integrin alpha-D/beta-2. In association with integrin alpha-L/beta-2, contributes to apoptotic neutrophil phagocytosis by macrophages. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family."}
+{"protein": "MSIREDRNQDATIYLGNLDEKVTDSILFELCLQAGPVVNIHIPRDRVRNSHNGFGFCEFLHEQDVEYACQILNQVKLFGKPIRVNRASQDRGVNTLIGANLFVGNLDPLVDERVLYDTFSALGQLVKAPQVARDENGRSKGYGFVSYDSFETADAAIEAMNNQFLMNKPITVSYAFKREGKGERHGDIAERKLAAAAKKNKVAVTPQSTLPPGFSPATPAPTSAANTPATIAATSIPPVPNVPLVGATTAVPPLSIPNVLPFTAAQHFPGMPAMPMMNVPMGPGGAPLVPPPPPGMVMASPSPAAATIPGAPVMPNIPFYQTINAQNGYSQQQRR", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SF3B4 family."}
+{"protein": "MNKDSTQTWGLKRDITPCFGARLVQEGHRLHFLADRAGFTGSFSEVQTLQLDEAFPHFVAHLELMLLSCELNPRYAHCVTLYRNGLTGEADTLGSHGYVYIAILNRHGFNRHLRVI", "text": "FUNCTION: Putative antitoxin component of a type IV toxin-antitoxin (TA) system; its cognate toxin is unknown. SIMILARITY: Belongs to the CbeA/YafW/YfjZ antitoxin family."}
+{"protein": "MGPLPAPSCTQRITWKGLLLTASLLNFWNPPTTAEVTIEAQPPKVSEGKDVLLLVHNLPQNLPGYFWYKGEMTDLYHYIISYIVDGKIIIYGPAYSGRETVYSNASLLIQNVTRKDAGTYTLHIIKRGDETREEIRHFTFTLYLETPKPYISSSNLNPREAMEAVRLICDPETLDASYLWWMNGQSLPVTHRLQLSKTNRTLYLFGVTKYIAGPYECEIRNPVSASRSDPVTLNLLPKLPIPYITINNLNPRENKDVLAFTCEPKSENYTYIWWLNGQSLPVSPGVKRPIENRILILPSVTRNETGPYQCEIRDRYGGLRSNPVILNVLYGPDLPRIYPSFTYYRSGENLDLSCFTESNPPAEYFWTINGKFQQSGQKLFIPQITRNHSGLYACSVHNSATGKEISKSMTVKVSGPCHGDLTESQS", "text": "FUNCTION: Binds to the small latent transforming growth factor-beta complex, consisting of the N-terminal TGFB1 latency-associated peptide (LAP) and the mature form of TGFB1, thereby leading to the activation of TGFB1 (PubMed:27389696). The activation of TGFB1 leads to stimulation of naive CD4(+) T-cells to increase FoxP3 expression and to an increase in the number of FoxP3(+) regulatory T-cells (PubMed:27389696). Induces the differentiation of a suppressive CD4(+)LAP(+)FoxP3(-) T-cell subset (PubMed:27389696). Induces the secretion of TGFB1 in macrophages, but not in activated CD4(+) T-cells (PubMed:27389696). May reduce the expression of several pro- inflammatory cytokines and chemokines by CD4(+) T-cells, including IL2 and IL6 (PubMed:27389696). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family."}
+{"protein": "MTREHQGGTRGLAAARKGFWSGLRFTSLRLRLVLVFGLVALTAAVSASGIAYWLNREAVLTRTQDAVLRDFEQEMQNRAGALPEHPTQDEVQHTAGQMANSSQRFSVLLVAENADGTAVYGSSGGLGGVALSDVPESLRTAVNKEQKLTSANKHPYHLYWQRITDDGTPYLVAGTKVIGGGPTGYMLKSLEPEAKDLNSLAWSLGIATALALLGSALLAQALATTVLKPVHRLGVAARRLGEGKLDTRLRVSGTDELADLSRTFNSAAENLEKRVADMAGREQASRRFVADMSHELRTPLTALTAVTEVLEEELEYAGEGEGEGGSFDPMVEPAVRLVVSETRRLNDLVENLMEVTRFDAGTARLVLDDVDVADQITACIDARAWLDAVDLDAERGVHARLDPRRLDVILANLIGNALKHGGSPVRVSVARADHEIVIRVRDNGPGIPEDVLPHVFDRFYKASASRPRSEGSGLGLSIALENAHIHGGEITAENAPEGGAVFTLRLPQDPSPPADEDGGPDEETEDRGKDAKGQV", "text": "FUNCTION: Forms part of a two-component regulatory system AfsQ1/AfsQ2 involved in secondary metabolism. May activate AfsQ1 by phosphorylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MAPGRAVAGLLLLAATSLGHPSEGPELAFSEDVLSVFGANRSLSAAQLGRLLERLGAASQQGALDLGQLHFNQCLSAEDIFSLHGFSNVTQITSSNFSAICPAILQQLNFHPCEDLRKHNAKPSLSEVWGYGFLSVTIINLASLLGLILTPLIKKSYFPKILTYFVGLAIGTLFSNAIFQLIPEAFGFNPKIDNYVEKAVAVFGGFYMLFFVERTLKMLLKTYGQNDHTHFRNDDFGSKEKTHQPKTLPLPAVNGVTCYANPAVTEPNGHIHFDTVSVVSLQDGKTEPSSCTCLKGPKLSEIGTIAWMITLCDALHNFIDGLAIGASCTLSLLQGLSTSIAILCEEFPHELGDFVILLNAGMSTRQALLFNFLSACSCYVGLAFGILVGNNFAPNIIFALAGGMFLYISLADMFPEMNDMLREKVTGRQTDFTFFMIQNAGMLTGFTAILLITLYAGDIELQ", "text": "FUNCTION: Electroneutral divalent metal cation:bicarbonate symporter of the plasma membrane mediating the cellular uptake of zinc and manganese, two divalent metal cations important for development, tissue homeostasis and immunity (PubMed:16638970, PubMed:18037372, PubMed:22563477, PubMed:29337306). Transports an electroneutral complex composed of a divalent metal cation and two bicarbonate anions or alternatively a bicarbonate and a selenite anion (PubMed:16638970, PubMed:18037372, PubMed:22563477, PubMed:27166256). Thereby, it also contributes to the cellular uptake of selenium, an essential trace metal and micronutrient (PubMed:27166256). Also imports cadmium a non- essential metal which is cytotoxic and carcinogenic (PubMed:15722412, PubMed:16638970, PubMed:17108009, PubMed:18037372, PubMed:24529376). May also transport iron and cobalt through membranes (PubMed:16638970, PubMed:22898811, PubMed:24529376). Through zinc import, indirectly regulates the metal-dependent transcription factor MTF1 and the expression of some metalloproteases involved in cartilage catabolism and also probably heart development (PubMed:24529376, PubMed:29337306). Also indirectly regulates the expression of proteins involved in cell morphology and cytoskeleton organization (PubMed:29927450). Indirectly controls innate immune function and inflammatory response by regulating zinc cellular uptake which in turn modulates the expression of genes specific of these processes (PubMed:23403290). Protects, for instance, cells from injury and death at the onset of inflammation (By similarity). By regulating zinc influx into monocytes also directly modulates their adhesion to endothelial cells and arteries (PubMed:30015240). Reclaims manganese from the bile at the apical membrane of hepatocytes, thereby regulating the activity of the manganese-dependent enzymes through the systemic levels of the nutrient (PubMed:28481222). Also participates in manganese reabsorption in the proximal tubule of the kidney (By similarity). By mediating the extracellular uptake of manganese by cells of the blood-brain barrier, may also play a role in the transport of the micronutrient to the brain. With manganese cellular uptake also participates in mitochondrial proper function (By similarity). Finally, also probably functions intracellularly, translocating zinc from lysosome to cytosol to indirectly enhance the expression of specific genes during TCR- mediated T cell activation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Note=Localizes to the lysosome of activated T-cells. A large fraction of the protein is found intracellularly in microvascular capillary endothelial cells that constitute the blood-brain barrier. Localized and functional at both apical and basolateral membranes of microvascular capillary endothelial cells that constitute the blood-brain barrier. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
+{"protein": "MVLPLLKVGSLLIKSLAKPLSKQIKIRASKSPIFHDRVVRGARLWHKLDLKLTKFNGDTTRKPVDLNVNAAIDLGTEIVSEAFLLSVAIGLLLYETSRSSEKDKKKEEALQNRFKNLEEKLEVQQETINNLTNVIEAIQSSNPNLNIYIDPNQSTKSSIAEYINTHNIKLNSLKNAQTENDYKSISSEGIPNKRISNVN", "text": "SIMILARITY: Belongs to the OPA3 family."}
+{"protein": "MRLKSIMCAALFVVAGQAAAQEKSITIATEGAYAPWNFSGPNGKLDGFEIDLAKVLCERMKVKCQIVAQNWDGIIPSLVAKKYDVIMAAMSVTPKRQEVISFSTPYGAHMNGFAVMKDSKLADMPGSGEVYSLNTQADAAKKRIDDVNAFLDGTTVGVQGSTTGSQFLENYFKNSVDIKEYKTVEEFNIDLMSGRVDAVFASATVLTAAFEQPDMKDAKVVGPLFSGDELGKVAVGLRKDDAALKAEFRLGAVGLRKEDAALKADFDSSIKAVADEGTIKTLSSKWFKVDVTPH", "text": "FUNCTION: Component of the octopine active transport system probably consisting of four subunits: Q, M, P and T. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 3 family."}
+{"protein": "MPAVRILILAACCCWLLLLPVRCCGPGRGPVGGRRRYMRRLVPLLYKQFVPNVPEKTLGASGKSEGKIRRGSERFIKLVPNYNPDIIFKDEENTGADRLMTERCKDRVNALAISVMNMWPGLKLRVTEGWDEDGHHAHDSLHYEGRALDITTSDRDRNKYGMLARLAVEAGFDWVYYESKAHIHVSVNTDNSLGVRSGGCFPGTAMVMMETGKKKPLSELKLGDTVFTTDETGLLIHSVVLLFLHRDPYKTATFVLIEAEGHPTKLLVTPNHLLFIKSSSSTGFQPTFAYRVQIGDLIQIYVNGTQVQSSKVVRVSVDEQTGVYAPMTEHGTLLVDGVLTSCYATVESHTLAHASLAPLRLFQGIASMLPDLHTSDGVHWYCHILYVLAKYVLWWDMP", "text": "FUNCTION: [Desert hedgehog protein B]: The C-terminal part of the desert hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts (DhhN and DhhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated DhhN (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). FUNCTION: [Desert hedgehog protein B N-product]: The dually lipidated desert hedgehog protein N-product (DhhNp) is essential for a variety of patterning events during development (By similarity). Involved in the early induction and patterning of anterodorsal ectoderm, nervous system and somites. Induces ectopic cement gland formation in embryos (PubMed:7671800). Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes (By similarity). SUBCELLULAR LOCATION: [Desert hedgehog protein B]: Endoplasmic reticulum membrane Golgi apparatus membrane Secreted Cell membrane Note=Co-localizes with HHAT in the ER and Golgi membrane. SUBCELLULAR LOCATION: [Desert hedgehog protein B N-product]: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the hedgehog family."}
+{"protein": "MGTIHLFRKPQRSFFGKLLREFRLVAADRRSWKILLFGVINLICTGFLLMWCSSTNSIALTAYTYLTIFDLFSLMTCLISYWVTLRKPSPVYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLEQPEIHTGRLLVGTFVALCFNLFTMLSIRNKPFAYVSEAASTSWLQEHVADLSRSLCGIIPGLSSIFLPRMNPFVLIDLAGAFALCITYMLIEINNYFAVDTASAIAIALMTFGTMYPMSVYSGKVLLQTTPPHVIGQLDKLIREVSTLDGVLEVRNEHFWTLGFGSLAGSVHVRIRRDANEQMVLAHVTNRLYTLVSTLTVQIFKDDWIRPALLSGPVAANVLNFSDHHVIPMPLLKGTDDLNPVTSTPAKPSSPPPEFSFNTPGKNVNPVILLNTQTRPYGFGLNHGHTPYSSMLNQGLGVPGIGATQGLRTGFTNIPSRYGTNNRIGQPRP", "text": "FUNCTION: Has probably no intrinsic transporter activity but together with SLC30A5 forms a functional zinc ion:proton antiporter heterodimer, mediating zinc entry into the lumen of organelles along the secretory pathway (PubMed:15994300, PubMed:19366695, PubMed:19759014). As part of that zinc ion:proton antiporter, contributes to zinc ion homeostasis within the early secretory pathway and regulates the activation and folding of enzymes like alkaline phosphatases and enzymes involved in phosphatidylinositol glycan anchor biosynthesis (PubMed:15994300, PubMed:19759014, PubMed:35525268). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily."}
+{"protein": "MAMVTGGWGGPGGDTNGVDKAGGYPRAAEDDSASPPGAASDAEPGDEERPGLQVDCVVCGDKSSGKHYGVFTCEGCKSFFKRSIRRNLSYTCRSNRDCQIDQHHRNQCQYCRLKKCFRVGMRKEAVQRGRIPHSLPGAVAASSGSPPGSALAAVASGGDLFPGQPVSELIAQLLRAEPYPAAAGRFGAGGGAAGAVLGIDNVCELAARLLFSTVEWARHAPFFPELPVADQVALLRLSWSELFVLNAAQAALPLHTAPLLAAAGLHAAPMAAERAVAFMDQVRAFQEQVDKLGRLQVDSAEYGCLKAIALFTPDACGLSDPAHVESLQEKAQVALTEYVRAQYPSQPQRFGRLLLRLPALRAVPASLISQLFFMRLVGKTPIETLIRDMLLSGSTFNWPYGSGQ", "text": "FUNCTION: Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal responses. Represses transcriptional activity of the lutropin- choriogonadotropic hormone receptor/LHCGR gene, the renin/REN gene and the oxytocin-neurophysin/OXT gene. Represses the triiodothyronine- dependent and -independent transcriptional activity of the thyroid hormone receptor gene in a cell type-specific manner. The corepressing function towards thyroid hormone receptor beta/THRB involves at least in part the inhibition of THRB binding to triiodothyronine response elements (TREs) by NR2F6. Inhibits NFATC transcription factor DNA binding and subsequently its transcriptional activity. Acts as transcriptional repressor of IL-17 expression in Th-17 differentiated CD4(+) T cells and may be involved in induction and/or maintenance of peripheral immunological tolerance and autoimmunity. Involved in development of forebrain circadian clock; is required early in the development of the locus coeruleus (LC). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 subfamily."}
+{"protein": "MEPSGSKKGRAEEPREEVECQMSSQPSTSSAKTKATGKKQRKSEKDDGCKPEEKSAQDPETPGHARRKVPVPPFPQHLPPVNLIHRDVLRAWCQEMKLSSKGQKLDAYKRLLARAFPDQMPELKNVPDSAKEARLKMPRKKMKTEPGEESQVTVPLEIVTVPEEQIPALVDPPVLYEEVSTTVVTTSASEAVLASWARIAANAKKLEAVPSNATSETYGSTGEMWCVVHGTSLPATSSGWVRLQFHAGQAWVPDKKGKAIALFLLPACTFPPPHLEDNMLCPKCVHKNKILTKSLEG", "text": "FUNCTION: May be involved in the maintenance of active epigenetic status of target genes. May inhibit differentiation of embryonic stem (ES) cells into a primitive ectoderm lineage (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Associated with transcriptionally active chromatin."}
+{"protein": "MLLSFLPLLPLATAALTYRGADISSLLIEEDAGIAYKNLNGQTQALESILADNGVNSIRQRLWVNPSDGSYDLDYNLKLAKRAKAAGMSVYLDLHYSDTWADPSHQTTPAGWSTDDIGTLAWQVYNYTKEVCDTFAANDIALEMVSIGNEIRNGLLWPLGATDSYPNIARLLHSGAWGVKDSALATTPQILLHLDNGWDWAAQKYFYDTVLAAGSELTSADFDLIGVSYYPFYNADATLSALKTSLGNLASAYGKKVLVVETNWPVACPNPEYQFPADLADIPFSVDGQSTFLRRLGEVVAGTDGGAGVYYWEPAWTKNAGLGSSCQDNLLVDYNTDQVRASISALGGI", "text": "FUNCTION: Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 53 family."}
+{"protein": "MASQQEKKQLDERAKKGETVVPGGTGGKSFEAQQHLAEGRSRGGNTRKEQLGSEGYQQMGRKGGSTPDKTDKEDAEDEPSTRT", "text": "FUNCTION: This protein may play a role in equipping the seed for survival, maintaining a minimal level of hydration in the dry organism and preventing the denaturation of cytoplasmic components, or may play a role during imbibition by controlling water uptake. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the small hydrophilic plant seed protein family."}
+{"protein": "MAASSAVTANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNGDLLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLKVVKTPNAVNPLVLGSFPLLTIDVWEHAYYLDFQNRRPDYIKTFMTNLVSWEAVSARLEAAKAASA", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Cell membrane Plastid, chloroplast membrane. Plastid, chloroplast stroma. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
+{"protein": "MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPLLRMKNGKYDKEGEFTPITWDQAFDVMEEKFKTALKEKGPESIGMFGSGQWTIWEGYAASKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGANMAEMHPILWSRITNRRLSNQNVTVAVLSTYQHRSFELADNGIIFTPQSDLVILNYIANYIIQNNAINQDFFSKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFEDYKAFVAEYTLEKTAEMTGVPKDQLEQLAQLYADPNKKVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFAHRLPADMVVTNEKHRDICEKKWNIPSGTIPAKIGLHAVAQDRALKDGKLNVYWTMCTNNMQAGPNINEERMPGWRDPRNFIIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVQAPGEAKSDLWQLVQFSRRFKTEEVWPEDLLAKKPELRGKTLYEVLYATPEVSKFPVSELAEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHKARGLRWPVVNGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAEAPDEEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKARDLRRGDKVKVVSRRGEVISIVETRGRNRPPQGLVYMPFFDAAQLVNKLTLDATDPLSKETDFKKCAVKLEKV", "text": "FUNCTION: Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. 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. 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": "MAPRGKRLSSTPLEILFFLNGWYYATYFLLELFIFLYKGLLLPYPTANLVLDVVMLFLYLGVEVIRLFFGTKGNLCQRKMPLGISVALTFPSTMMASYYLLLQTYVLRLEAIMNSILLFFCGSELLLEVLTLTAFSSMDRM", "text": "FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. SUBCELLULAR LOCATION: 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": "MESLSLKFIEPYWFKFVDYYGEEFLLTYGTFIAHQVFYFGCFIPFLIADFIPFFRKYKIQQTKENDWKSQTYCAIKVILTQVLIQLPMMYIFDPAIKAIGLSARAPLPSIPYLLLTLVSSFIIEDFYFYWAHRALHHGIWYKYIHKVHHDYASPFGITAEYAHPLETIILGVGTVIGPFLFSRDLFTLWVWLGVRLYQTVECHSGYDFPWSFTNLIPFWGGAPFHDYHHEVFIGNYASTFTYLDKIFGTSGKSYYSRIEKKSINKSE", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
+{"protein": "MSHGHSHDGAPCGGHHGDDGAGGSRPSVNDVQALVDQLRLAGVDVSNMPNIPTAPRDMDEARSKSFQFWSTQPVPQMDETVPADVNCAIEENIALDKVRAEPFSLPAGFRWSNVDLSDEEQLNELYNLLTRNYVEDDDSMFRFDYSADFLKWALQVPGFRPEWHCGVRADSNNRLLAFIGAVPQTVRVYDKTVNMVEINFLCVHKNLRSRRVAPVLIREITRRVNVTGIFQAAFTAGIVIPKPVSVCRYYHRSLNPRKLIDVRFSHLSAKMTMARTIKLYKLPEETATRNLREMKSTDVPQVFKLLTTSLKQYSLAPVYNSEEELAHALVPKKGVVYSYVAENQNGKITDFVSFYSLPSTVMGHTTHKTIYAAYLYYYVAGSVTPKQLINDSLILANREKFDVFNALDLMHNEKIFSDLKFGKGDGNLQYYLYNWKCADMKPSQIGLVLQ", "text": "FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NMT family."}
+{"protein": "MELAFRESLKKMRGTKSKEKFSQELEMSRSNYSRIESGKSDPTIKTLEQIVKLTNSTLVVDLIPNEPTEPEPETEQVTLELEMEEEKSNDFV", "text": "FUNCTION: Involved in copy control of plasmid pIP501."}
+{"protein": "MSVAFAAPRQRGKGEITPAAIQKMLDDNNHLIQCIMDSQNKGKTSECSQYQQMLHTNLVYLATIADSNQNMQSLLPAPPTQNMPMGPGGMNQSGPPPPPRSHNMPSDGMVGGGPPAPHMQNQMNGQMPGPNHMPMQGPGPNQLNMTNSSMNMPSSSHGSMGGYNHSVPSSQSMPVQNQMTMSQGQPMGNYGPRPNMSMQPNQGPMMHQQPPSQQYNMPQGGGQHYQGQQPPMGMMGQVNQGNHMMGQRQIPPYRPPQQGPPQQYSGQEDYYGDQYSHGGQGPPEGMNQQYYPDGHNDYGYQQPSYPEQGYDRPYEDSSQHYYEGGNSQYGQQQDAYQGPPPQQGYPPQQQQYPGQQGYPGQQQGYGPSQGGPGPQYPNYPQGQGQQYGGYRPTQPGPPQPPQQRPYGYDQGQYGNYQQ", "text": "FUNCTION: Appears to function synergistically with RBM14 as a transcriptional coactivator. Isoform 1 and isoform 2 function in nuclear receptor coactivation. Isoform 1 and isoform 2 function in general transcriptional coactivation. Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:29374058). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SS18 family."}
+{"protein": "SGSCTTKTCWTTLPKFREIGYILKEKYNAAVQVEVVRASRLRQPTFLKIKQIKSYQKPMETDLVYIEKSPNYCEEDASTGSVGTQGRLCNRTSPNADGCDMMCCGRGYNTHQYTKVWQCNCKF", "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). Required for normal fusion of the chorion and the allantois during placenta development (By similarity). Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MSQIKIELIKSINDLNSRGLLLSSKWSSEQLNGLSPTILATPLTNEEQLSIISQPSISSPPIGSNEYYKYILAKNYFDLKEYRRCSDVLIDCNKYQLPIFLRSYATYLAIEKRREEDIIEQQAQQQQQQQQAQQQAQQAQQESQQNDKNNDTNNNNKTDQQQQQQQQQKIEQCQEFKQLFQFYKKLYIENKKDMDGFLLYFYSMLLKKQRDFTMARKVLIESVHKYPCNWSAWSDLSSLCSDSADIIMQLSLPDHFMKDFFLAHFKLELQQNNESLVIYQQLSRTLFTQSTYILAQTAIGNYNLRAYDIGEELFERLIELEPNRLENIDIYSNILYVRDKKASLSMLAHKAMKIEKYCPETCCIIGNYYSLKLEHDKAILYFQRALKLNDRYLSAWTLIGHEFLEIKNVSAAINAYRKAVDINPRDYRAWYGLGQTYQLLKLPLYSLYYFKKATTLRPYDPRMWCAAGGCYEFIERIPEAIKCYERAEENYDRERVAINKLAKLYQEIQNNEKAAFYYKKNLYYCDQEKIDGQEIIDALLFLANFYKNQNQTQSEQYCLRLLDYAGPEKEEAKSILREIHSKSKLSSKSKPK", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the APC8/CDC23 family."}
+{"protein": "MYLHLTALCVVIPLCYGASMFKHDHYMDNGVRYPNGDGICKQLNETKCDAGFSYDRSICEGPHYWHTISKCFIACGIGQRQSPINIVSYDAKFRQRLPKLKFKPHMEKLKTEVTNHQNRAPEFEPEDGENLYVKLNNLVDGHYKFHNLHVHNGRTRRKGSEHSVNGRFTPMEAHLVFHHDDQTHFEPTRTKLGGAFPGHNDFVVVGVFLEVGDDGFGDEPDDEECKHILKGHHPDNNENGNGDNGNNGYNGDNGNNGDNGNNSYNGDNGNNGVNGNNGYNGDNGNNGDNGNNGYNGDNGNNGDNGNNGENGNNGENGNNGENGHKHGCRVKKAKHLSRILECAYRNDKVREFKKVGEEEGLDVHLTPEMALPPLKYRHYYTYEGSLTTPPCTESVLWVVQKCHVQVSRRVLHALRNVEGYKDGTTLRKYGTRRPTQKNKVTVYKSFK", "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. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
+{"protein": "MSRSICTLTCILPTFSMDYWNQECVELSQVENLFTELASRLELLEMNSKNVLYRLTIGTNPDRNWEAIAFIREFFDSAKHGYVIPKHEIRNRIRLLSEASLISCLRWLLHRIPGGVITWSTYKLFDEAETRANYPVRGFDIFMKHATKHSCHFNILKCFLKLLMSLSAKLAVSSNSSTVSSLELVSQIASIWAFDWPMMNLQETFIYWDRCTNACLRLLLCYIRYTNKSSETGFSCLPSALQSQLQSFNYPPSLKKLNDAKAHVFTFSMNYYMTRDPLEMIQIVTKMNIPDHLTATLPRSSDDIQNDCLFALRQVSKRSSYHSVFSAQESAWTDFIKNGFDHPILPTCTQETVYSLLTGNDTACVYPFPNKPYRLPDVDFEIFSHCSFESLTTVTTNTNIWWVWAESRCTEIPESKRTVFPNCTMLIDKTGRLIILQQTVPQKPVALTASSNKRKNRIFGKIRRSFKRILKPRKINKTVKIMSNSQRRSCQSVLSEGNRTILLHLADQMNACSLQTKSRESIKTLKLIEEKDEYWEPETAGYFNTIVGWADQRKSLYDEAVIKINHSNMLNTLPPTSQGATSTTVSSASSNFLSSSCTPIDDTNSVTGSTLSCSFDEMKLSDKIDDANSLKDDDFIQGSKKDFFEMNLNHSSYQNKDELKPFQLLVKHAFKPPSYRLIRPPLRDWQSSDTLSSEMSKSISSSRSSPFSLEQTISKIQNKL", "text": "FUNCTION: Has a role in meiosis and septation. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to the barrier septum."}
+{"protein": "MWEKMETKTIVYDLDTSGGLMEQIQALLAPPKTDEAEKRSRKPEKEPRRSGRATNHDSCDSCKEGGDLLCCDHCPAAFHLQCCNPPLSEEMLPPGEWMCHRCTVRRKKREQKKELGHVNGLVDKSGKRTTSPSSDTDLLDRSASKTELKAIAHARILERRASRPGTPTSSASTETPTSEQNDVDEDIIDVDEEPVAAEPDYVQPQLRRPFELLIAAAMERNPTQFQLPNELTCTTALPGSSKRRRKEETTGKNVKKTQHELDHNGLVPLPVKVCFTCNRSCRVAPLIQCDYCPLLFHMDCLEPPLTAMPLGRWMCPNHIEHVVLNQKNMTLSNRCQVFDRFQDTVSQHVVKVDFLNRIHKKHPPNRRVLQSVKRRSLKVPDAIKSQYQFPPPLIAPAAIRDGELICNGIPEESQMHLLNSEHLATQAEQQEWLCSVVALQCSILKHLSAKQMPSHWDSEQTEKADIKPVIVTDSSVTTSLQTADKTPTPSHYPLSCPSGISTQNSLSCSPPHQSPALEDIGCSSCAEKSKKTPCGTANGPVNTEVKANGPHLYSSPTDSTDPRRLPGANTPLPGLSHRQGWPRPLTPPAAGGLQNHTVGIIVKTENATGPSSCPQRSLVPVPSLPPSIPSSCASIENTSTLQRKTVQSQIGPPLTDSRPLGSPPNATRVLTPPQAAGDGILATTANQRFSSPAPSSDGKVSPGTLSIGSALTVPSFPANSTAMVDLTNSLRAFMDVNGEIEINMLDEKLIKFLALQRIHQLFPSRVQPSPGSVGTHQLASGGHHIEVQRKEVQARAVFYPLLGLGGAVNMCYRTLYIGTGADMDVCLTNYGHCNYVSGKHACIFYDENTKHYELLNYSEHGTTVDNVLYSCDFSEKTPPTPPSSIVAKVQSVIRRRRHQKQDEEPSEEAAMMSSQAQGPQRRPCNCKASSSSLIGGSGAGWEGTALLHHGSYIKLGCLQFVFSITEFATKQPKGDASLLQDGVLAEKLSLKPHQGPVLRSNSVP", "text": "FUNCTION: Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional TLE5 complexes to DNA. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKTIAAYLVLVFYASTALSESISENLAWNKEFSSESVHGVFVLCKSSSNSCTTNNAARASTAYIPASTFKIPNALIGLETGAIKDERQVFKWDGKPRAMKQWEKDLKLRGAIQVSAVPVFQQIAREVGEIRMQKYLNLFSYGNANIGGGIDKFWLEGQLRISAFNQVKFLESLYLNNLPASKANQLIVKEAIVTEATPEYIVHSKTGYSGVGTESSPGVAWWVGWVEKGTEVYFFAFNMDIDNESKLPSRKSISTKIMASEGIIIGG", "text": "FUNCTION: Hydrolyzes both oxacillin and methicillin. SIMILARITY: Belongs to the class-D beta-lactamase family."}
+{"protein": "MSADVSTTPAAENVNGAAEASPAPAAAAPSATTPEVTAVENSTPAPAANQPHSASLYVGELDPSVTEAMLYELFSSIGQVASIRVCRDAVTRRSLGYAYVNYNNTADGERALEDLNYTLIKGKPCRIMWSQRDPALRKTGQGNVFIKNLDSAIDNKALHDTFAAFGNILSCKVAQDEFGNSKGYGFVHYETAEAANNAIKHVNGMLLNDKKVFVGHHISKKDRQSKFEEMKANFTNVYIKNLDSEIDDDEFRKMFEKFGEITSATLSRDQEGKSRGFGFVNFSTHESAQAAVEEMNDKEIRSQKLYVGRAQKKHEREEELRKQYEAARLEKASKYQGVNLYVKNLTDDIDDEKLRELFGPYGTITSAKVMRDTNVERDQSPDSAGKEKEADKENDKEATPEAEKAEKAEEKPSESSEEKDKEAKKSDKKPFGKSKGFGFVCFSSPDEASKAVTEMNQRMVNGKPLYVALAQRKDVRRSQLEASIQARNTIRQQQAAAAAGMPQPYMQPAVFYGPGQQGFIPGGQRGMAFPPQPGMVMGIPGGRPGQYPGPFPGQQGGRGMGPNQQIPPNFAQGIPMGMQGPGGIPNGMGYPQMAQVQFGRGAGGRGQVPGMPMGQGMRGGPGYGQGRGAPVQQGQMRPGQGGRGQNAAAPAGPQEGAAGGVNAQTLGAAPPAQQKQMLGEALYPKIQAQQPELAGKITGMLLEMDNTELLSLTRKPCAPRSMRPLAFTMST", "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": "MISAEEALYQSCYCEENVYKLIEKIDDKNGIFAIIISNDCKMIPLWKQKAAKSINGHVLWDYHVIAIEKEKNGSKVYDLDSTLEWSCDFLEYWEKTMNLAEMAQRDTKFRRKFRVIPGENYISLLSSDRSHMLSKNGVYLKPPPEWPLINSHKPSNLMELIRMSEQIENTTVMDEPELFQLFSK", "text": "FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. SIMILARITY: Belongs to the NTAQ1 family."}
+{"protein": "MKGSYKSRWVIVIVVVIAAIAAFWFWQGRNDSQSAAPGATKQAQQSPAGGRRGMRSGPLAPVQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTLPESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTPEEKATSREYAKKGARS", "text": "FUNCTION: The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family."}
+{"protein": "MAPSQKKSRKSRNKSRSTLMISGLPILNSTDLEDRLLTSAIASQPLSQDWVRWIIDLWVSRVRSRNYLTQVARTLRAYPHWVTESMLSNHELTVWIRSRLISLDEHPLWRQMLEAYGQN", "text": "SIMILARITY: Belongs to the orthoreovirus sigma-1s protein family."}
+{"protein": "MKVLLVFDFDNTIIDDNSDTWIVQCAPDKKLPIELQDSYQKGLWTEFMGRVFKYLRDEGVKADELKRAVTSLPFTSGMIELLSFLRMNKDRFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDSSGRLTVKNYHAHSCTRCPKNLCKNTVLGEFIDKQLQKGVRYTRIVYIGDGGNDVCPVTFLKKNDVAMPREGYTLHRTLAKMSQNLEPMESSIVVWSSGVEIISHLQFLIKM", "text": "FUNCTION: Phosphatase that has high activity toward pyridoxal 5'- phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO family."}
+{"protein": "MKPAMETAAEENTEQSQERKGCFECCIKCLGGVPYASLVATILCFSGVALFCGCGHVALAGTVAILEQHFSTNASDHALLSEVIQLMQYVIYGIASFFFLYGIILLAEGFYTTSAVKELHGEFKTTACGRCISGMFVFLTYVLGVAWLGVFGFSAVPVFMFYNIWSTCEVIKSPQTNGTTGVEQICVDIRQYGIIPWNAFPGKICGSALENICNTNEFYMSYHLFIVACAGAGATVIALLIYMMATTYNYAVLKFKSREDCCTKF", "text": "FUNCTION: May be involved in neural development. Involved in regulation of osteoblast function and bone formation. Involved in matrix vesicle release by osteoblasts; this function seems to involve maintenance of the actin cytoskeleton. May be involved in cellular trafficking of SERT and thereby in regulation of serotonin uptake. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Colocalizes with SERT at the plasma membrane. SIMILARITY: Belongs to the myelin proteolipid protein family."}
+{"protein": "MDNIISGQAQKVEDVDGTRVQNEFSKFLKSFKGDKNELQYKTAMKELVQPEKNTIFVDMQHLYKFSNNLATTIELQYYRVYPFMCEALHLATLDGCDENERQQMFKKQLYVSLYNLDAKTKVRELSADKVGGLVRIAGQIVRTHPVHPELSRACFVCEDCGVSTRDVQQQFRYTQPTKCANPQCMNRTRFSLDVNSSTFVDFQKIRIQETQAELPRGSIPRTVDVIVRGEMVETVQPGDKCDIVGTLIVIPDIAQLSTPGLRAETSNQNRGRATDKSEGITGLKALGVRDLTYKMAFLACHIQQTESLVGGDASGAMEENDYLELWTKMSPEDRSVLKQMSDDKKIEKNIVDSLFPNIYGNHEVKLGVLLMLLGGVAKKSKDEGTSLRGDINVCLVGDPSTAKSQVLKAVEEFSPRAIYTSGKASSAAGLTAAVVKDEESFEFVIEAGALMLADNGVCCIDEFDKMDVKDQVAIHEAMEQQTISITKAGVKATLNARASILAAANPVGGRYDRSRPLKYNVQMSAPIMSRFDLFFVLVDECNEVTDYAIARRILDNHRSISEHTERNTVYKIDDIKKYIAFARCFKPKISDKAAEALVREYKKLRMSDSNNAATSSWRITVRQLESLVRLSEALARLHCGKEVLEQHVEKAAELLNKSIVRVEQPDIALDEDDFDNNIVIVEANKENQGGDDDMEHDGEKDETAKVDPAKLKISFKEYKQLSDVLVLHMRADEESQGEEEYDGVKQSALVEWYLTTIEGEMETEEDFNVQKTVCERVIHRLVHQDHILLEVEPGEDPTLCVHPNYVVSDE", "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. SIMILARITY: Belongs to the MCM family."}
+{"protein": "MGRVIRAQRKSGGIFQAHTRLRKGAAQLRTLDFAERHGYIRGVVQKIIHDPGRGAPLAKVAFRNPYHYRTDVETFVATEGMYTGQFVYCGKNAALTVGNVLPVGEMPEGTIISNVEEKAGDRGALGRSSGNYVIIVGHDVDTGKTRVKLPSGAKKVVPSSARGVVGIVAGGGRIDKPLLKAGRAFHKYRVKRNCWPRTRGVAMNPVDHPHGGGNHQHVGHSTTVPRQSAPGQKVGLIAARRTGLLRGAAAVEN", "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. 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. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
+{"protein": "MAQVVWTWRALADLTAIRDYIGQFSPLAAQRMALRLKTAADSLAEYPERGRLATATLRELVVVPPYVIRYYVADGLVHIVRIRHAARL", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Its toxic effect is neutralized by coexpression with cognate antitoxin RelB2 but no other ParD or RelB antitoxin. SIMILARITY: Belongs to the RelE toxin family."}
+{"protein": "MTYLFLICAILAEVVATSLLKSTQGFTRLWPTVICLLGYAVSFALLAVSISRGMQTDVAYALWSAIGTALIVLIAVLFLGSPISVTKVVGVGLIIAGVVTLNLTGAH", "text": "FUNCTION: Multidrug efflux pump. Confers resistance to tetraphenylphosphonium (TPP), erythromycin, ethidium bromide, acriflavine, safranin O and pyronin Y (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. Mmr subfamily."}
+{"protein": "MEKKTIVLGVIGSDCHAVGNKILDHSFTAAGFNVVNIGVLSPQEDFINAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKEDLNIK", "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": "MSYLDGLQQCVDSLQISIGTLSSSIDTLESGIHDFPRIKHILKVQRHFNLISEDELSARQAKFEEIVKPILSKAFQRLEDSISSLQRQEDSLKTKYELQEARLDMLKNRPATSAFSVTTESSEQLKAIIAKRQKLVYTLERYTLQLQQKRGH", "text": "FUNCTION: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. May be necessary for growth under high osmotic stress. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore Note=Associates with the mitotic spindle and the kinetochore. Kinetochore association occurs only during mitosis (By similarity). SIMILARITY: Belongs to the DASH complex SPC19 family."}
+{"protein": "MPDEAISILSQKSSDSGLHIQLHPLALLTISDHITRHAARSQQGPIVGGLLGQHNGREITVEHGFECVVEIGPNGEAQLPNEWFVDRVKQFKDVHKVPALDLIGWWSTAPPSGPTTAHLPIHRQILQNHNESAVFLTFHPSQVQGASQSQGKLPLTIYESVYEGESVTENGKAMQVDGEEQLLNIRFRELPYTIETGEAEMIGIDTVARTARNAAATETSTVAAPSSQIDSDKQEQQPANTDLLSPEEEELIASLNTRLNAIRTLESRISLIKSYLSSISPSSEEGQKDSATKPDHTILRDINSLLSNLSLLTPHEQSAFSAETLAQNNDVSLVALLGQLSQSVNGMREVGKRTAIVNSVRRNRKQLGAQSRYEDDILGRDGVALG", "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. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily."}
+{"protein": "MSELPADQGVPPAGAANDNGDVRQAEVGGRRREPAPAQPVAARDRPMAAAVEGSMASPVEGPVPEAREGPMAASREGLGAAAREARMAEVARLLAEPAEEEGPEGRPRSRPGNGPGLAALPYLRLRHPLGVLGINYQQFLRHYLEHYPIAPGRIQELEGRRRRFVEACRAREAAFDAEYQRNPQRMDFDILTFSITLTASEIINPLIEELGCDKFISRE", "text": "FUNCTION: Interacts with EP300 and acts as a repressor of MYOD- dependent transcription and muscle differentiation. Inhibits EP300 histone acetyltransferase activity. Acts as a repressor of TGFB/SMAD transcriptional responses. May act as a repressor of the TGFB/SMAD3- dependent signaling by selectively blocking formation of TGFB-induced SMAD3-SMAD4 complex (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MRQGAARGCRWFVVWALLGLTLGVLVASAAPSSPGTPGVAAATQAANGGPATPAPPAPGPAPTGDTKPKKNKKPKNPPPPRPAGDNATVAAGHATLREHLRDIKAENTDANFYVCPPPTGATVVQFEQPRRCPTRPEGQNYTEGIAVVFKENIAPYKFKATMYYKDVTVSQVWFGHRYSQFMGIFEDRAPVPFEEVIDKINAKGVCRSTAKYVRNNLETTAFHRDDHETDMELKPANAATRTSRGWHTTDLKYNPSRVEAFHRYGTTVNCIVEEVDARSVYPYDEFVLATGDFVYMSPFYGYREGSHTEHTSYAADRFKQVDGFYARDLTTKARATAPTTRNLLTTPKFTVAWDWVPKRPSVCTMTKWQEVDEMLRSEYGGSFRFSSDAISTTFTTNLTEYPLSRVDLGDCIGKDARDAMDRIFARRYNATHIKVGQPQYYLANGGFLIAYQPLLSNTLAELYVREHLREQSRKPPNPTPPPPGASANASVERIKTTSSIEFARLQFTYNHIQRHVNDMLGRVAIAWCELQNHELTLWNEARKLNPNAIASATVGRRVSARMLGDVMAVSTCVPVAADNVIVQNSMRISSRPGACYSRPLVSFRYEDQGPLVEGQLGENNELRLTRDAIEPCTVGHRRYFTFGGGYVYFEEYAYSHQLSRADITTVSTFIDLNITMLEDHEFVPLEVYTRHEIKDSGLLDYTEVQRRNQLHDLRFADIDTVIHADANAAMFAGLGAFFEGMGDLGRAVGKVVMGIVGGVVSAVSGVSSFMSNPFGALAVGLLVLAGLAAAFFAFRYVMRLQSNPMKALYPLTTKELKNPTNPDASGEGEEGGDFDEAKLAEAREMIRYMALVSAMERTEHKAKKKGTSALLSAKVTDMVMRKRRNTNYTQVPNKDGDADEDDL", "text": "FUNCTION: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress (By similarity). Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation). 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 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). SIMILARITY: Belongs to the herpesviridae glycoprotein B family."}
+{"protein": "MQLILLSSLLLLGLSLANGHETDPEGQILNSLVETVGRLEKKIDKVENAFLTVHRARSFGSGSERLYVTNKQVGNFEAVRNTCVQAGGHIPSPQLLNENKAFASVLERHNKAAYLVVQNSAKFTNWAAGEPNNADGNKLCVKADAQGAWHSASCDEDLLVVCEFSFI", "text": "FUNCTION: Does not show any inhibitory activity against various snake venom PLA2s. Does not inhibit the endogenous PLA2 activities in various tissue homogenates prepared from this snake. SUBCELLULAR LOCATION: Secreted Note=Secreted in plasma. SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor family."}
+{"protein": "MWWTSLVFSVLLFDLIFISNCDYIHLPGNSDIPDLKLQSGYLNANENGTQKMFYFLLEARDIPVGEASLIIWFNGGPGCSSLSAFFEEFGPLYVNFGGKSLFENVHSWYHKANILFLESPIGVGFSYDTEQSNFTKVNDDSIAEQNFNSVIDFFQRKHSSYVNHDFFIAAESYGGVYGPMLSALVVDSISKREFPNENFKGLIIGNGFMNVKLSTNTMILWSAYHDRTSPDEWDEIKEKCATSGAHDVDYYDFMQFMKTTNKMDYLADNSTECGRLIEPLLGQFSETFDGYDFFNYYHDCYTNFSIPNATDPIKETLAQIPRRRISALFNKHSTDGQASYRCWADDALHKYLNLKEVQNALGIDRAWKDRKKKWEVCNMPIYDQYVMTHQDMTPFFSKIFDKFTGPAFRVLIYSGDIDTACNYLADGYFVRDLASIHGFKKTLKHGPWYHSEHKVIAGNFMRYEGANHLGSKLSIDVVTVKGSGHFVPLDRPGPALQMVHNFLTGKPGKMTNYTSPV", "text": "SIMILARITY: Belongs to the peptidase S10 family."}
+{"protein": "MYKLLGSLKSYLKWQDIQTDNAVFRLHNSFTTVLLLTCSLIITATQYVGQPISCIVNGVPPHVVNTFCWIHSTFTMPDAFRRQVGREVAHPGVANDFGDEDAKKYYTYYQWVCFVLFFQAMACYTPKFLWNKFEGGLMRMIVMGLNITICTREEKEAKRDALLDYLIKHVKRHKLYAIRYWACEFLCCINIIVQMYLMNRFFDGEFLSYGTNIMKLSDVPQEQRVDPMVYVFPRVTKCTFHKYGPSGSLQKHDSLCILPLNIVNEKTYVFIWFWFWILLVLLIGLIVFRGCIIFMPKFRPRLLNASNRMIPMEICRSLSRKLDIGDWWLIYMLGRNLDPVIYKDVMSEFAKQVEPSKHDRAK", "text": "FUNCTION: Structural component of the gap junctions. Essential for generation and/or maintenance of postembryonic neuroblasts and normal development of optic lobe. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell junction, gap junction. Basolateral cell membrane. Note=Accumulates in the basolateral membrane of follicle cells in oocytes and epithelial cells in embryonic salivary gland and hindgut. SIMILARITY: Belongs to the pannexin family."}
+{"protein": "MNALTVKRRLPVLLFLFHISLSSISSNTILENDFHSSFVQRRLKGHERREIQKEILTILGLQHRPRPYLPEKKKSAPLFMMDLYNAVNIEEMHAEDVSYSNKPISLNEAFSLATDQENGFLAHADTVMSFANLVDNDNELHKNSYRQKFKFDLTDIPLGDELTAAEFRIYKDYVQNNETYQVTIYQVLKKQADKDPYLFQVDSRTIWGTEKGWLTFDITATGNHWVMNPHYNLGLQLSVESMDMQNVNPRLVGLVGKNGPQDKQPFMVAFFKTSDIHLRSVRSTSNKHWNQERAKTYKEQDNLPPANITDGIMPPGKRRFLKQACKKHELFVSFRDLGWQDWIIAPEGYAAYYCDGECAFPLNSFMNATNHAIVQTLVHFINPETVPKPCCAPTQLNGISVLYFDDSANVILKKYKNMVVQACGCH", "text": "FUNCTION: Growth factor of the TGF-beta superfamily that plays important role in various biological processes, including embryogenesis, hematopoiesis, neurogenesis and skeletal morphogenesis. Initiates the canonical BMP signaling cascade by associating with type I receptor ACVR1 and type II receptor ACVR2A. Once all three components are bound together in a complex at the cell surface, ACVR2A phosphorylates and activates ACVR1. In turn, ACVR1 propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
+{"protein": "MATEYALRMGDGKRIYLTKEKIIAEIEDGTANAADLGEIPALNANEMEKLAEILMMPGKTVSVEQGMEVPVTHDIGTIRLDGDQGNSGVGIPSSRLVGCMTHERAFGADTMELGHIDYSFKPVKPVVSNECQAMEVCQQNMIIPLFYGAMPNMGLYYTPDGPFENPGDLMKAFKIPEAWESMEHAAEHLTRDTVWVMQKLFASGADGVNFDTTGAAGDGDMYGTLHAIEALRKEFPDMYIEAGMAGECVLGMHGNLQYDGVTLAGLWPHQQAPLVAKAGANVFGPVCNTNTSKTSAWNLARAVTFMKAAVEASPIPCHVDMGMGVGGIPMLETPPIDAVTRASKAMVEIAGVDGIOIGVGDPMGMPIAHIMASGMTGMRAAGDLVARMEFSKNMRIGEAKEYVAKKLGVDQMDLVDEHVMRELREELDIGIITSVPGAAKGIAAKMNIEKLLDIKINSCNLFRKQIA", "text": "FUNCTION: Catalyzes the transfer of a methyl group from dimethylamine to the corrinoid cofactor of MtbC. SIMILARITY: Belongs to the dimethylamine methyltransferase family."}
+{"protein": "MDYLVGIFLLLCGVALPGRVAPQHTKENVPRLKLSYNEMLESSNLVTFTGLANSSGYDTFLMDGERGRLLVGAEDHVFSFDLVNINRDVKQIAWPATPSKRDECKWAGKDLRKDCSNFVRVLQSYNQTHIYICGTGAFHPICSFLEMGKRAEDNIFRLDANYFENGRGKSPYDPKMQSSSLLLDGELYSGTSADFMGRDFAIFRTLGSHHPIRTEQHDSRWLNEPRFLGIHLIPESDNPEDDKIFLFFKENAMDGEHTGKATISRIGQLCKNDMGGHRSLVNKWTTFLKAKLTCSVPGLNGIDTHFDELQDVFLMSAKDPKNPVIYAVFTTSSNIFRGSAICMYSMADIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARLHPAMYNPVQPMGGKPIVVRTNVEYQFTQLVVDRVEAEDGQYDVMFIGTDLGTVLKVVTIPRESWHDLEEVVLEEMTVFREPTPITAMELSTKQQQLYLGSDLGISQMPLHRCEVYGKACAECCLARDPYCAWDGTECSRYFPTAKRRTRRQDIRNGDPLSQCSDLHHNDDLEGYSSVEERSVYGVENSSMFLECSPKSQRALIYWQLQKPNDERKHEIVIDERLSLTGQGLLIRSLTQADSGVFLCHAVEHGFIQPLRRINLQVIPSQRVGELLLRAGTNDKDPAPKHKLWYRDFMSLLEHPDLNSVDEFCERIWKREKKPKGKKAPKVNPGTGVSIKNEKTPQTTAQSLQNPTQRAQNAPKVPNNPSVQIFPKSTGLQRSQSPGGTVSTESQSTKPDTQKASESQRAQPNQAKKGPQTPQRGPPHTAKWKQLQENKRGRNRRTHEQQRPPRSV", "text": "FUNCTION: May influence outgrowth by a variety of growth cones including those of the posterior lateral line ganglion. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the semaphorin family."}
+{"protein": "MVKLTPELINQSMQYINPCRERELDLRGYKIPQIENLGATLDQFDTIDLSDNDLRKLDNLPHLPRLKCLLLNNNRILRISEGLEEAVPNLGSIILTGNNLQELSDLEPLVGFTKLETICLLINPVSTKPNYREYMAYKFPQLRLLDFRKIKQKDRQAAQEFFRTKQGKDVLKEISRKSKMSAAAAIAAEAGNGKGRGSEGGRLANPQDMQRIREAIKRASSLAEVERLSQILQSGQLPDKFQHEMEAVAQNGAGHNGSGAVAMEY", "text": "FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (By similarity). Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA (By similarity). In the germ line, has a role in oogenesis, by regulating spermatogenesis and nurse cell nuclei chromatin decondensation and dispersal, probably by regulating the splicing of proteins necessary for germline differentiation such as the meiotic protein mei-P26 (PubMed:27035939, PubMed:24244416). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the U2 small nuclear ribonucleoprotein A family."}
+{"protein": "MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGKPKGHPHMNSIRIDGDITLGGLFPVHGRGSEGKPCGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSRDTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILRLFKIPQISYASTAPDLSDNSRYDFFSRVVPSDTYQAQAMVDIVRALKWNYVSTVASEGSYGESGVEAFIQKSREDGGVCIAQSVKIPREPKAGEFDKIIRRLLETSNARAVIIFANEDDIRRVLEAARRANQTGHFFWMGSDSWGSKIAPVLHLEEVAEGAVTILPKRMSVRGFDRYFSSRTLDNNRRNIWFAEFWEDNFHCKLSRHALKKGSHVKKCTNRERIGQDSAYEQEGKVQFVIDAVYAMGHALHAMHRDLCPGRVGLCPRMDPVDGTQLLKYIRNVNFSGIAGNPVTFNENGDAPGRYDIYQYQLRNDSAEYKVIGSWTDHLHLRIERMHWPGSGQQLPRSICSLPCQPGERKKTVKGMPCCWHCEPCTGYQYQVDRYTCKTCPYDMRPTENRTGCRPIPIIKLEWGSPWAVLPLFLAVVGIAATLFVVITFVRYNDTPIVKASGRELSYVLLAGIFLCYATTFLMIAEPDLGTCSLRRIFLGLGMSISYAALLTKTNRIYRIFEQGKRSVSAPRFISPASQLAITFSLISLQLLGICVWFVVDPSHSVVDFQDQRTLDPRFARGVLKCDISDLSLICLLGYSMLLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIVWLAFIPIFFGTSQSADKLYIQTTTLTVSVSLSASVSLGMLYMPKVYIILFHPEQNVPKRKRSLKAVVTAATMSNKFTQKGNFRPNGEAKSELCENLEAPALATKQTYVTYTNHAI", "text": "FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 3 family."}
+{"protein": "MGIASHSAFRERESSPTGASLDASPRPWDKGLSGREPPRHVQVRPRSAVLNMLRRLDRIRFRGHKREDLLDLAESPNASDTECGDEIPLKTPRPSPRDSEELRDPAGPGTLIMAAGVQDFNRTEFDRLNEIKGHLEIALLEKHFLQEELRKLREETNSEMLRQELDRERQRRIELEQKMQEVLKARSEEQPAQPQQPPKGQSQASNGTGTERRSQGLASRVQKWFYERFGEYIEDFRFQPEENTVETEEPLSARRLTENMRRLKRGAKPVTNFVKNLSALSDWYSIYTSAIAFTVYMNAVWHGWAIPMFLFLAILRLSLNYLIARGWRIQWSIVPEVSEAVEPAKEDLTVSEKFQLVLDVAQKAQNLFGKMADILEKIKNLFMWVQPETTQKLYVALWAAFLASCFFPYRLVGLAVGLYAGIKFFLIDFIFKRCPRLRAKYDTPYIIWRSLPTDPQLKERAGATVSRRLQTASSRSYVSSAPAGLSKDEDAGRFHSTKKGNFHEIFNLTENERPLAVCENGWRCCLINRDRKMPTDYIRNGVLYVTENYLCFESSKSGSSKRNKVIKLMDITDIQKYKVLSVLPGSGMGIAVSTPSTQKPLVFGAMVHRDEAFETIFSQYVKITSAAASGGDS", "text": "FUNCTION: Plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53 (By similarity). Inhibits TLR9 response to nucelic acids and regulates TLR9-mediated innate immune response (PubMed:25917084). SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Colocalizes with COX4I1."}
+{"protein": "MRLLLLLLVAASAMVRSEASANLGGVPSKRLKMQYATGPLLKFQICVSUGYRRVFEEYMRVISQRYPDIRIEGENYLPQPIYRHIASFLSVFKLVLIGLIIVGKDPFAFFGMQAPSIWQWGQENKVYACMMVFFLSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDNEMKLNVHMDSIPHHRS", "text": "FUNCTION: Selenoprotein with thioredoxin reductase-like oxidoreductase activity (By similarity). Protects dopaminergic neurons against oxidative stress and cell death (PubMed:26866473). Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion (By similarity). Plays a role in fibroblast anchorage and redox regulation (By similarity). In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation (By similarity). In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP- induced insulin secretion (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SelWTH family. Selenoprotein T subfamily."}
+{"protein": "MILMNPKTSKILWLLGFLSLLSSFSLEIAAQTTQNINVLFINEVDNEPAAKAVEVVLTYLKKNIRYGLSVQLDSIEANKSDAKVLLEAICNKYATSIEKKQTPHLILDTTKSGIASETVKSFTQALGLPTISASYGQQGDLRQWRDLDEAKQKYLLQVMPPADIIPEAIRSIVIHMNITNAAILYDDSFVMDHKYKSLLQNIQTRHVITAIAKDGKREREEQIEKLRNLDINNFFILGTLQSIRMVLESVKPAYFERNFAWHAITQNEGEISSQRDNATIMFMKPMAYTQYRDRLGLLRTTYNLNEEPQLSSAFYFDLALRSFLTIKEMLQSGAWPKDMEYLNCDDFQGGNTPQRNLDLRDYFTKITEPTSYGTFDLVTQSTQPFNGHSFMKFEMDINVLQIRGGSSVNSKSIGKWISGLNSELIVKDEEQMKNLTADTVYRIFTVVQAPFIMRDETAPKGYKGYCIDLINEIAAIVHFDYTIQEVEDGKFGNMDENGQWNGIVKKLMDKQADIGLGSMSVMAEREIVIDFTVPYYDLVGITIMMQRPSSPSSLFKFLTVLETNVWLCILAAYFFTSFLMWIFDRWSPYSYQNNREKYKDDEEKREFNLKECLWFCMTSLTPQGGGEAPKNLSGRLVAATWWLFGFIIIASYTANLAAFLTVSRLDTPVESLDDLAKQYKILYAPLNGSSAMTYFERMSNIEQMFYEIWKDLSLNDSLTAVERSKLAVWDYPVSDKYTKMWQAMQEAKLPATLDEAVARVRNSTAATGFAFLGDATDIRYLQLTNCDLQVVGEEFSRKPYAIAVQQGSHLKDQFNNAILTLLNKRQLEKLKEKWWKNDEALAKCDKPEDQSDGISIQNIGGVFIVIFVGIGMACITLVFEYWWYRYRKNPRIIDVAEANAERSNAADHPGKLVDGVILGHSGEKFEKSKAALRPRFNQYPATFKPRF", "text": "FUNCTION: Integral part of various neural sensory systems in the antenna that provide the neural basis for the response to environmental changes in temperature (thermosensation), humidity (hygrosensation) and odor detection (PubMed:21220098, PubMed:27161501, PubMed:27656904). Required for odor-evoked electrophysiological responses in multiple neuron classes in the antenna and is likely to function as part of an olfactory receptor complex with Ir76a and Ir76b (PubMed:21220098). Together with Ir21a and Ir93a, mediates the response of the larval dorsal organ cool cells, a trio of cool-responsive neurons, to cooling and is required for cool avoidance behavior (PubMed:27126188, PubMed:27161501, PubMed:27656904). Required in chordonotal organ neurons for behavioral synchronization to low-amplitude temperature cycles and mediates circadian clock resetting by temperature (PubMed:26580016). Together with Ir40a and Ir93a, mediates the response of the hydrosensory sacculus neurons to changes in relative humidity, and is required for dry detection and humidiy preference behavior (PubMed:27161501, PubMed:27656904). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, axon Cell projection, dendrite Perikaryon Cell projection, cilium Note=Low levels detected in the axon segment adjacent to the perikaryon in some sensory neurons of the antenna but not detected along axons as they enter the brain or at synapses within antennal lobe glomeruli. In coeloconic neurons, prominently expressed both in the perikaryon and in the distal tip of the dendrite which corresponds to the ciliated outer dendritic segment innervating the sensory hair. Relatively low levels detected in inner dendrites (PubMed:19135896). Detected in dendritic bulbs of the dorsal organ cool cells (PubMed:27126188). SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family."}
+{"protein": "MKKKNIYSIRKLGVGIASVTLGTLLISGGVTPAANAAQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPKADAQQNNFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPKADNNFNKEQQNAFYEILNMPNLNEEQRNGFIQSLKDDPSQSANLLSEAKKLNESQAPKADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKADNKFNKEQQNAFYEILHLPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKLNDAQAPKEEDNNKPGKEDNNKPGKEDNNKPGKEDNNKPGKEDNNKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDNKKPGKEDGNKPGKEDGNKPGKEDGNGVHVVKPGDTVNDIAKANGTTADKIAADNKLADKNMIKPGQELVVDKKQPANHADANKAQALPETGEENPFIGTTVFGGLSLALGAALLAGRRREL", "text": "FUNCTION: Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins (PubMed:2938951, PubMed:4163007, PubMed:10805799). In turn, Staphylococcus aureus is protected from phagocytic killing via inhibition of Ig Fc region. In addition, the host elicited B-cell response is prevented due to a decrease of antibody-secreting cell proliferation that enter the bone marrow, thereby decreasing long-term antibody production. Inhibits osteogenesis by preventing osteoblast proliferation and expression of alkaline phosphatase, type I collagen, osteopontin and osteocalcin. Acts directly as a pro-inflammatory factor in the lung through its ability to bind and activate tumor necrosis factor alpha receptor 1/TNFRSF1A (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor; Extracellular side Secreted Note=Cell wall anchoring is confered by the LPXTG motif and following sequences (PubMed:1638631). Anchored by sortase A (PubMed:10427003). SpA from strains A676 and V-I is secreted whereas SpA from Cowan 1 and 8325-4 is mostly attached to the cell wall (Probable). Newly synthesized protein is deposited at 2-4 foci/cell and eventually is distributed in a ring around the cell (PubMed:17416657). SIMILARITY: Belongs to the immunoglobulin-binding protein SpA family."}
+{"protein": "MNHSPATTFSPHSRYQELKVRNKKSTKKSHKEKYRLKCLRLRRVAKDMVFENAALCDEIARTEDKFIRAKEERRFLLKRLLQLQALSEEEPGTSHNSNVSAGYSVPDMAAMNEGNLDMCYSSVLDDGGSCKKVKKDKREKGKENKSEAMKKPSKKKRVTEGTTRKWVQPIALDPCGRPVFPIVLEGLTVYSLGEIISDRAGFHEKVAIYPVGFCSTRVYVGMKNPDQKCLYTCQIKDGGTGPQFEIVPDDDPQNSIVASSADECHSILLQKISTPLGKRFSTPDLAGAYFFGFTHPTIQNLIQSCPGARKCTGYQWVKFEVCRAGEEQVPRDICESSASVNFEAFQRQSFATINNSTALAGTLDLPEIHASHDYISTYQEIFLSHSQLASGMQHLKSPSNQYSPSRSSE", "text": "FUNCTION: May act as a growth inhibitor. May be involved in maintaining chromosomal stability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TBRG1 family."}
+{"protein": "MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED", "text": "FUNCTION: C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MDTMITTPLILILITCGANSQTVKPDTASESDQPTWSNPLFTYPEGCTLDKLSKVNASQLRCPRIFDDENRGLIAYPTSIRSLSVGNDLGEIHTQGNHIHKVLYRTICSTGFFGGQTIEKALVEMKLSTKEAGAYDTTTAAALYFPAPRCQWYTDNVQNDLIFYYTTQKSVLRDPYTRDFLDSDFIGGKCTKSPCQTHWSNVVWMGDAGIPACDSSQEIKAHLFVDKISNRVVKATSYGHHPWGLHRACMIEFCGKQWIRTDLGDLISVEYNSGAEILSFPKCEDKTMGMRGNLDDFAYLDDLVKASESREECLEAHAEIISTNSVTPYLLSKFRSPHPGINDVYAMHKGSIYHGMCMTVAVDEVSKDRTTYRAHRATSFTKWERPFGDEWEGFHGLHGNNTTIIPDLEKYVAQYKTSMMEPMSIKSVPHPSILAFYNETDLSGISIRKLDSFDLQSLHWSFWPTISALGGIPLVLLLAVAACCCWSGRPPTPSAPQSIPMYHLANRS", "text": "FUNCTION: Binds to specific receptor at cellular 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 viral nucleocapsid 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 G, releasing a fusion hydrophobic peptide (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the novirhabdovirus glycoprotein family."}
+{"protein": "MFNLLPAFSLGVLLIVMEGRGSAVNTPASRPVTRKSKSYGRSCVEAPSYFWQTPGHLTVLKVPTSRGAAKSQIITNKVDPEHIALLVKNEWKLSYVTPLHHFRHTQLKSYAKHLSAFIVAEKQQGVAVEVGLDAGFKVTFTAVLGLAETDEDAETVFIQIQSKPVFAAAADAPKVVWRGWLTCVNGDPEYLRSLPPDFVSLPLFCTSGPESLTNLVKSWFERAFDCNFGSLALNSSTLNWLAALWTGCHPACNIRYLKLSWSLPTEPPLDVLYTVNPQDAWELWNSIHPQENTDDRIDIKDVQAFMSGMETHFFRHFKIHLSAGTLLKVSTALGSAHHDGKIKIGNSDYITTLLALLTECALLKMPT", "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-L/IML3 family."}
+{"protein": "MSEARRDSTSSLQRKKPPWLKLDIPSAAPATAEEPSFLQPLRRQVFLRSVSMPAETAHISSPHYELRRPVLQRQTSITQTIRRGAADWFGVSKESDSTQKWQRKSIRHCSQRYGKLKPQVLRELDLPSQDNVSLTSTETPPPLYVGPCQLGMQKIIDPLARGRAFRVADDTAEGLSAPHTPVTPGAASLCSFSSSRSGFHRLPRRRKRESVAKMSFRAAAALMKGRSVRDGTLRRAQRRSFTPASFLEEDTTDFPDELDTSFFAREGILHEELSTYPDEVFESPSEAALKDWEKAPEQADLTGGALDRSELERSHLMLPLERGWRKQKEGAAAQQPKVRLRQEVVSTAGPRRGQRIAVPVRKLFAREKRPYGLGMVGRLTNRTYRKRIDSFVKRQIEDMDDHRPFFTYWLTFVHSLVTILAVCIYGIAPVGFSQHETVDSVLRNRGVYENVKYVQQENFWIGPSSEALIHLGAKFSPCMRQDPQVHSFIRAAREREKHSACCVRNDRSGCVQTSEEECSSTLAVWVKWPVHPSAPELAGHKRQFGSVCHQDPRVCDEPSSEDPHEWPEDITRWPICTKNSAGNHTNHPHMDCVITGRPCCIGTKGRCEITSREYCDFMRGYFHEEATLCSQVHCMDDVCGLLPFLNPEVPDQFYRLWLSLFLHAGILHCLVSICFQMTVLRDLEKLAGWHRIAIIYLLSGVTGNLASAIFLPYRAEVGPAGSQFGILACLFVELFQSWQILARPWRAFFKLLAVVLFLFTFGLLPWIDNFAHISGFISGLFLSFAFLPYISFGKFDLYRKRCQIIVFQVVFLGLLAGLVVLFYVYPVRCEWCEFLTCIPFTDKFCEKYELDAQLH", "text": "FUNCTION: Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Note=Predominantly localized in the endoplasmic reticulum membrane. SIMILARITY: Belongs to the peptidase S54 family."}
+{"protein": "MAKDDSTVRCFQGLLIFGHVIVGMCGIALTAECIFFVSDQHSLYPLLEATNNDDIFGAAWIGMFVGICLFCLSVLAIVGIMKSNRKILLAYFIMMFIVYGFEVASCITAATQRDFFTTNLFLKQMLMRYQNNSPPTNDDEWKNNGVTKTWDRLMLQDHCCGVNGPSDWQKYTSAFRVENNDADYPWPRQCCVMDKLKEPLNLDACKLGVPGYYHSQGCYELISGPMDRHAWGVAWFGFAILCWTFWVLLGTMFYWSRIEY", "text": "FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MSLIRGLISTIYYLPKIYKWFYRPYYFLSLLMTLAFVIVRCCPGLCEHLPSQREDGDSCAFDWREVEIFMFLGAIVMMKNRRAVTVEQHIGNIFLFSKVANVVLFFRVDLRFGLLYLTLCVVFLITCKPPAYMGPENIKYFRDSTIDEELQRDSRVTWIVEFYANWSPECQSFAPIFADLSLKYTCLGLKFGKVDIGHYGAVAERYKVNPSPLCKQLPSLLMLQAGRELMRRPLVDKKGRAVSWNFTEDNIIRDFNLNEIFQKYKKFSKGEKPEEPQPVLEEESESPLEEEEEDSESKKDK", "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. 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": "MAEAHQAVAFQFTVTPDGVDFRLSREALRHIYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVVMATVGSNYCKVDISMGLVDCIQRCLPERYGHFGTPQTEALLSMVIFSTGVWATGIFFFRQTLKLLLSYHGWMFEMHSKTSHATKIWAICVRLLSSRRPMLYSFQTSLPKLPVPSVPATIHRYLDSVRPLLDDEAYYRMETLAKEFQDKTAPRLQKYLVLKSWWATNYVSDWWEEYVYLRSRSPLMVNSNYYAMDFVLIKNTNVQAARLGNAVHAMIMYRRKLDREEIKPVMALGMVPMCSYQMERMFNTTRIPGKETDLLQHLSESRHVAVYHKGRFFKVWLYEGSRLLKPRDLEMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAEARQTFFSSGKNKMSLDAIERAAFFVTLDEDSHCYNPDDETSLSLYGKALLHGNCYNRWFDKSFTLISCKNGLLGLNTEHSWADAPIIGHLWEFVLGTDTFHLGYTETGHCVGEPNTTLPPPQRLPWDIPEQCREAIENSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDKGKFCLTYEASMTRMFREGRTETVRSCTNESAAFVQAMMKGSHKKQDLQDLFRKASEKHQNMYRLAMTGAGIDRHLFCLYIVSKYLGVSSPFLAEVLSEPWSLSTSQIPQFQICMFDPKQYPNHLGAGGGFGPVADDGYGVSYMIAGENTMFFHISSKYSSSETNAQRFGNHIRQALLDIAELFKISKTDS", "text": "SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the carnitine/choline acetyltransferase family."}
+{"protein": "MSHYHEQFLKQNPLAVLGVLRDLHKAAIPLRLSWNGGQLISKLLAITPDKLVLDFGSQAEDNIAVLKAQHITITAETQGAKVEFTVEQLQQSEYLQLPAFITVPPPTLWFVQRRRYFRISAPLHPPYFCQTKLADNSTLRFRLYDLSLGGMGALLETAKPAELQEGMRFAQIEVNMGQWGVFHFDAQLISISERKVIDGKNETITTPRLSFRFLNVSPTVERQLQRIIFSLEREAREKADKVRD", "text": "FUNCTION: Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. When bound to c-di-GMP it binds to elements of the flagellar motor (MotA (PubMed:20303158) and/or FliG and FliM (PubMed:20346719), binding to FliM also occurs in the absence of c-di-GMP), causing the motor to slow down. Thus, increasing levels of c-di-GMP lead to decreased motility. Probably binds 1 c-di-GMP dimer per subunit. SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the YcgR family."}
+{"protein": "MATFVSELEAAKKNLSEALGDNVKQYWANLKLWFKQKISKEEFDLEAHRLLTQDNVHSHNDFLLAILTRCQILVSTPEGAGSLPWTGGSAAKPGKPKGKKKLSSVRQKFDHRFQPQNPLSGAQQFVAKEPQGDDDLKLCSHTMMLPTRGQLEGRMIVTAYEHGLDNVTEEAVSAVVYAVENHLKDILTSVVSRRKAYRVRDGHFKYAFGSNVTPQPYLKNSVVAYNNLVEGPPAFSAPCANQSPASQPHPDDAEQQAAFLLACSGDTLPASLPPVNMYDLFEALQVHREVIPTHTVYALNIERIIMKLWHPNHEELQQDKVHRQRLAAKEGLLLC", "text": "FUNCTION: Probably involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TADA1 family."}
+{"protein": "MSTQEERQINTEYAVSLLEQLKLFYEQQLFTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAAALQMIIAYAYTGNLAVNDSTVEQLYETACFLQVEDVLQRCREYLIKKINAENCVRLLSFADLFSCEELKQSAKRMVEHKFTAVYRQEAFMQLSHDLLIDILSSDNLNVEKEETVREAAMLWLEYNTESRSQYLSSVLSQIRIDALSEVTQRAWFQGLPPNDKSVVVQGLYKSMPKFFKPRLGMTKEEMMIFIEASSENPCSLYSSVCYSPQAEKVYKLCSPPADLHKVGTVVTPDNDIYIAGGQVPLKNTKTNHSKTSKLQTAFRTVNCFYWFDAQQNTWFPKTPMLFVRVKPSLVCCEGYIYAIGGDSVGGELNRRTVERYDTEKDEWTMVSPLPCAWQWSAAVVVHDCIYVMTLNLMYCYFPRSDSWVEMAMRQTSRSFASAAAFGDKIFYIGGLHIATNSGIRLPSGTVDGSSVTVEIYDVNKNEWKMAANIPAKRYSDPCVRAVVISNSLCVFMRETHLNERAKYVTYQYDLELDRWSLRQHISERVLWDLGRDFRCTVGKLYPSCLEESPWKPPTYLFSPDGTEEFELDGEMVALPPV", "text": "FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of the insulin signaling pathway, modulating insulin sensitivity by limiting PIK3R1/p85alpha abundance in adipocytes. Targets PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase (PI3K), for 'Lys-48'-linked polyubiquitination and proteasome-mediated degradation."}
+{"protein": "MRAERTSFLLALGLLVAGIRSVHCLPENVVVKDQHRRVDGHTLASSNTDFAFSLYKQLALKNPNKNVILSPLSVSIALAFLSLGARGSTLTEILEGLKFNLTEIQEKEIHHSFQHLLQALNQPSNQLQLSVGNAMFVQEELKLLDKFIEDAQVLYSSEAFPTNFRDSEAARSLINDYVKNKTQGKIEELFKYLSPRTELVLVNYIYFKAQWKTPFDPKHTEQAEFHVSDNKTVEVPMMTLDLETPYFRDEELGCTLVELTYTSNDSALFILPDEGKMRDLEAKLTPETLTRWRNSLQPRRIHELYLPKFSIKSNYELNDILSQLGIRKIFANADLSGITGTADLVVSQVVHGAALDVDEEGTEGVAATGIGIERTFLRIIVRVNRPFLIAVVLKDTQSIIFLGKVTNPSEA", "text": "FUNCTION: Serine protease inhibitor. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule Secreted. SIMILARITY: Belongs to the serpin family."}
+{"protein": "MTHSLKALFALLFLYTAAVNAGVIGIFNALPPPNTKPINGESPLYQCDILDKQLVEIKEVNLDPNPPVRGENLTISANGEVFETIEEGAYIDVEVRLGYIRLLSQTFDLCETLEDNDIEGLSCPIEPGEYNIKKIVEIPGEVPPGKYVVVARAYTEKDDLITCLTGEVIFPPR", "text": "FUNCTION: Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the NPC2 family."}
+{"protein": "MKADYKKINSILTYTSTALKNPKIIKDKDLVVLLTIIQEEAKQNRIFYDYKRKFRPAVTRFTIDNNFEIPDCLVKLLSAVETPKAWSGFS", "text": "FUNCTION: Imparts immunity to sakacin-A to naturally sensitive host strains."}
+{"protein": "MPTVDDVLEQVGEFGWFQKQAFLLLCLISASLAPIYVGIVFLGFTPGHYCQNPGVAELSQRCGWSQAEELNYTVPGLGPSDEASFLSQCMRYEVDWNQSTLDCVDPLSSLVANRSQLPLGPCEHGWVYDTPGSSIVTEFNLVCGDAWKVDLFQSCVNLGFFLGSLVVGYIADRFGRKLCLLVTTLVTSVSGVLTAVAPDYTSMLLFRLLQGMVSKGSWVSGYTLITEFVGSGYRRTTAILYQMAFTVGLVGLAGVAYAIPDWRWLQLAVSLPTFLFLLYYWFVPESPRWLLSQKRTTRAVRIMEQIAQKNGKVPPADLKMLCLEEDASEKRSPSFADLFRTPNLRKHTVILMYLWFSCAVLYQGLIMHVGATGANLYLDFFYSSLVEFPAAFIILVTIDRIGRIYPIAASNLVTGAACLLMIFIPHELHWLNVTLACLGRMGATIVLQMVCLVNAELYPTFIRNLGMMVCSALCDLGGIFTPFMVFRLMEVWQALPLILFGVLGLTAGAMTLLLPETKGVALPETIEEAENLGRRKSKAKENTIYLQVQTGKSSST", "text": "FUNCTION: [Isoform 2]: Functional isoform capable of transporting TEA. FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:7990927, PubMed:8955087, PubMed:10570053, PubMed:10997918, PubMed:10864577, PubMed:11502595, PubMed:11408531, PubMed:12395288, PubMed:16142924, PubMed:15640376, PubMed:16272756, PubMed:15662044, PubMed:16581093, PubMed:17567940). Functions as a pH- and Na(+)-independent, bidirectional transporter (PubMed:8955087, PubMed:16142924). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (PubMed:8955087, PubMed:9405386, PubMed:16142924, PubMed:17567940). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors (By similarity). Primarily expressed in the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds from the blood by hepatic and renal clearance (PubMed:7990927, PubMed:9703985, PubMed:10997918). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal excretion and elimination of organic cations from the systemic circulation (By similarity). Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, neurotransmitters dopamine, serotonin, noradrenaline, adrenaline and histamine, and quaternary ammonium compound such as choline (PubMed:8955087, PubMed:9776363, PubMed:10570053, PubMed:11502595, PubMed:11408531, PubMed:11758759, PubMed:15662044, PubMed:16581093, PubMed:17567940). Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover (By similarity). Involved in the hepatic uptake of vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism (By similarity). Contributes to the influx and efflux of fatty acid carriers carnitines and acylcarnitines across the basolateral membrane of hepatocytes, from the liver to the systemic circulation and inversely and may be involved in regulating the systemic availability of hepatic acylcarnitines (By similarity). Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium (PubMed:15817714). Transports dopaminergic neuromodulators cyclo(his-pro) and salsolinol with lower efficency (By similarity). Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (By similarity). May contribute to the transport of cationic compounds in testis across the blood-testis-barrier (Probable). Also mediates the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N- methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)- quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n- pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N- methylpyridinium (ASP) (PubMed:8955087, PubMed:10864577, PubMed:11408531, PubMed:12395288). SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Lateral cell membrane; Multi-pass membrane protein Basal cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Localized to the sinusoidal/basolateral membrane of hepatocytes (PubMed:9703985). Mainly localized to the basolateral membrane of renal proximal tubular cells (PubMed:7990927, PubMed:9808712, PubMed:10997918, PubMed:11083459). Localized to the luminal/apical membrane of ciliated epithelial cells in the airway (PubMed:15817714). SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family."}
+{"protein": "MASNTDQASLEQEVRSLQAYANEYSQQFELLTQQLRFIESARGEALASTESLEAFSGLEGDVPTLLNLGGGISVHAIVTDTKKILVGIGAGITVEKPVEEAITFLHDRVTEMDASAKRLSESLGKLQEQMRAVEQRMQEIYSQTQHR", "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": "MILKPENEKKLIIDVLKKFGVPEEDAKITADVFVDADLKGFTSHGIGRFPQYITALKLGNINPKPDIKIVKESPATAVIDGDLGLGQVVGKKAMELAIKKAKNVGVGVVATRNANHFGIAGYYSELAMNQDMIGITITNTEPAMAPFGGKEKILGTNPIAIAFKGNKYKFSLDMATASIARGKILEALRKKIKIPEGCAVDKDGKPTTDPAKALEGCILPFGGPKGYGLALAIEMLSAIGGAEVGTKVKGTANPEERCTKGDLFIAINPEFFMGKEEFKRKVDELLDEIKNSEPAEGFEILIPGEIEERNKMKRKDGFEIDKNLYNQLKEICNELGLNIEDYIE", "text": "FUNCTION: Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate much more efficiently than the reverse reaction. Also catalyzes the reduction of oxaloacetate, alpha-ketoglutarate, and to a much lower extent, KHTCA, but not pyruvate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha- ketoglutarate). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family."}
+{"protein": "MEKEKKDDEKPDLENSVDFSEQFNQLELLKTHGHLIPTGTQSLWVGNSDEDEEQEEKNEEWYQLQEKKMEKDPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHIDVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLAAGNRDSRDTLELLLMNRYIKPELKNNSQETASDIARRTSIYHYLFEIAEGCTNSSPPS", "text": "FUNCTION: May have a role in spermatogenesis where it promotes autophagy in response to serum starvation, via the NF-kappaB pathway. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAFYRGVKAGRGGKGSIFVWASGNGGSRQDSCSADGYTTSVYTLSVSSATIDNRSPWYLEECPSTIATTYSSANMNQPAIITVDVPHGCTRSHTGTSASAPLAAGIIALALEANPNLTWRDMQHIVLRTANPVPLLNNPGWSVNGVGRRINNKFGYGLMDAGALVKLALIWKTVPEQHICTYDYKLEKPNPRPITGNFQMNFSLEVNGCESGTPVLYLEHVQVLATFRFGKRGDLKLTLFSPRGTSSVLLPPRPQDFNSNGIHKWPFLSVQTWGEDPRGKWTLMVESVSTNRNVGGTFHDWSLLLYGTAEPAQPNDPRHSSVVPSSVSAESPFDRITQHIASQEKKKKQRDSRDWQPKKVENKKSLLVSAQPELRV", "text": "FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily."}
+{"protein": "MSSGGAGEYNEDRHLLRSTDGDEVGIGGGEGDLDVESQSPAIRSGAGGVRDLFKHIDRRFSLSGRRLSFKRMENIRVDRERHNPSSSSAFSAAGEEDGGGISNLHSVDDRNDEYGFDEEVLGDSAPPEWALLLIGCLIGVAAGICVAGFNKGVHVIHEWAWAGTPNEGAAWLRLQRLADTWHRILLIPVTGGVIVGMMHGLLEILDQIRQSNSSQRQGLDFLAGIYPVIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMMENNRERRIALTAAGAASGIASGFNAAVAGCFFAIETVLRPLRAENSPPFTTAMIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSVVFSRLVTWFTKSFDFIKDKFGLPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHTGKSASAPGIWLLAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGGSAAEIINRAIPGNAAVAQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILLPLMGAVGLAIWVPSVANQGKESDSSEGRSTGRGYSSLSPSERKTEGVWRHTDNADSLELTVIENPDHNSFLDEETILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDENTCPVSSVCTKKISYRGQERGLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVIHKGKRRKLLGLLHYDSIWTFLRDEMSRRRSINDRRKDKEVGTNGH", "text": "FUNCTION: Voltage-gated chloride channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family."}
+{"protein": "MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQPCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKAPVEKCKKKKSQCTLL", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
+{"protein": "MSPRSTLRSPLPSRTARSSASSDTPSPGADRQDRMSKAKELFVLCDKEGKGFITKRDMQRLQQELPLSPEQLESVFESLDRDRNGYLTPLEFHTGLGELVGSGPEEKVRSAGEIVGEEREEPTEIRFTQILMELGADKLFKDQWELCGLWCELQRDKPELLGVLEEVLSYTVSHLQDALKEKDNLEHALRRREEDHDRVVRSMYEDMESQLKEERERRQALDSMRQGDKKEQLLHELRTREQELEFTLTKQRELESRINSLSSDQADARGENRRLQNVNQQLQDQLEQSREELQNSLSQLQQLQNTIKLQQRGKEREVLKVSRNMQKERESLVRQLELLRDMNKRLRDDKDAHQAQKMVSQKHSFTPPTYYPACRCVHNFSPWPRSIYPY", "text": "SIMILARITY: Belongs to the EFCAB4 family."}
+{"protein": "MKKVNVMIYMAFMITLEIVFTRFLSIQTPIIRIGFGFIPVAMSGMMFGPLLAGIVGATSDVLGMMIFPKGAYFPGFTLSAFVGAVIYGVFFYNKKVSVKRVLLAVGIITVLVNLTMNTIWLQILTGKAVKVLFVTRLVKEAIMFPIHAIVIYGAWKMVDRLEIMNKVAKFNK", "text": "FUNCTION: Folate-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 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MLSAISKVSTLKSCTRYLTKCNYHASAKLLAVKTFSMPAMSPTMEKGGIVSWKYKVGEPFSAGDVILEVETDKSQIDVEALDDGKLAKILKDEGSKDVDVGEPIAYIADVDDDLATIKLPQEANTANAKSIEIKKPSADSTEATQQHLKKATVTPIKTVDGSQANLEQTLLPSVSLLLAENNISKQKALKEIAPSGSNGRLLKGDVLAYLGKIPQDSVNKVTEFIKKNERLDLSNIKPIQLKPKIAEQAQTKAADKPKITPVEFEEQLVFHAPASIPFDKLSESLNSFMKEAYQFSHGTPLMDTNSKYFDPIFEDLVTLSPREPRFKFSYDLMQIPKANNMQDTYGQEDIFDLLTGSDATASSVRPVEKNLPEKNEYILALNVSVNNKKFNDAEAKAKRFLDYVRELESF", "text": "FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family."}
+{"protein": "MADFRTSTHRERWIFQTNDLMDRWGAANQRATETLVQYGTTRLKVDPVDGSLSYPEPAPDHVVGSSGVKPLSCEEERLMRVFYEQKIQEVCSAFKFPHKIQATAIIYFKRFYLQWSVMEHHPKHIMLTCIYSSCKVEENHVSAEELGKGIQQDHQIILNNEMIVLKSLDFDLIVYAPYRSIEGFVDDMEDFCRAGNGEHQRLQDLRQTAISQVDKMMLTDAPLLYTPGQLALAALHKSNDMHKILNFERYLESVFSRQHSDCPIEQFVGSINMINYLVEQLKIPTPKDMRHIDRKLKHCLDPSSQDEHKKKEKKSKHKSKRAANEAQLDS", "text": "FUNCTION: Involved in cell cycle regulation. May be a regulatory subunit of CDKD-1/CAK-R2. SIMILARITY: Belongs to the cyclin family. Cyclin F subfamily."}
+{"protein": "MATGEKKPETEAARAQPTPSSSATQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSNLLVSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRDGSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCIFANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDKTIKLWKSDC", "text": "FUNCTION: Contributes to histone modification (By similarity). May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (By similarity). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (By similarity). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). May regulate osteoblasts differentiation (By similarity). In association with RBBP5 and ASH2L, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat WDR5/wds family."}
+{"protein": "MADIDGVTGSAGLQPGPSEETDEELTARFERDAIPLLDQLYGGALRMTRNPADAEDLLQETMVKAYAGFRSFRHGTNLKAWLYRILTNTYINSYRKKQRQPAEYPTEQITDWQLASNAEHSSTGLRSAEVEALEALPDTEIKEALQALPEEFRMAVYYADVEGFPYKEIAEIMDTPIGTVMSRLHRGRRQLRGLLADVARDRGFARGEQAHEGVSS", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor (RshA) until released. This sigma factor is involved in heat shock and oxidative stress response; it is believed to control protein processing in the extracytoplasmic compartment (By similarity). FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor (RshA) until released. This sigma factor is involved in heat shock and oxidative stress responses; it positively regulates the expression of itself, sigE, sigB and a number of transcriptional regulators as well as other effectors of heat and oxidative stress, leading to direct and indirect control of up to 25% of the bacterial genome. Modulates expression of host genes for intercrine beta (chemokine CC) and apoptosis, altering the host immune response. FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor (RshA) until released. This sigma factor is involved in heat shock and oxidative stress responses; it positively regulates the expression of itself, sigE, sigB and a number of transcriptional regulators as well as other effectors of heat and oxidative stress, leading to direct and indirect control of up to 25% of the bacterial genome. Modulates expression of host genes for intercrine beta (chemokine CC) and apoptosis, altering the host immune response. SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily."}
+{"protein": "MTHLLIVDDEQDIVDICQTYFEYEGYKVTTTTSGKEAISLLSNDIDIMVLDIMMPEVNGYDIVKEMKRQKLDIPFIYLTAKTQEHDTIYALTLGADDYVKKPFSPRELVLRINNLLTRMKKYHHQPVEQLSFDELTLINLSKVVTVNGHEVPMRIKEFELLWYLASRENEVISKSELLEKVWGYDYYEDANTVNVHIHRIREKLEKESFTTYTITTVWGLGYKFERSR", "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 transcriptional regulator via a specific DNA-binding domain, recognizing motifs near the promoter sequences of target genes (By similarity). 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 transcriptional regulator via a specific DNA-binding domain, recognizing motifs near the promoter sequences of target genes. 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. 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 transcriptional regulator via a specific DNA-binding domain, recognizing motifs near the promoter sequences of target genes (By similarity). Modulates the expression of several genes. 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 transcriptional regulator via a specific DNA-binding domain, recognizing motifs near the promoter sequences of target genes. SaeR/SaeS activates the expression of exoproteins involved in adhesion and invasion of host cells, including hemolysins (Hla, Hlb), Coa, DNase, Spa and cell wall- associated proteins (Emp, Eap, FnbA). Acts probably downstream of the Agr system in the regulatory cascade of virulence factors. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MILKTAFSLPTPTTTLLSPSSPHQLNTLFFTRRRRRLISPSRLNSIFSQRRFSFSAAASGNNVFTSPETSKTFDFSSEEKIYKWWESQGYFKPNFDQGGSPFVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMNGRPTLWLPGTDHAGIATQLVVEKMLASEGIKRVDLGRDEFTKRVWEWKEKYGGTITNQIKRLGASCDWSRERFTLDEQLSRAVVEAFVKLHDKGLIYQGSYMVNWSPNLQTAVSDLEVEYSEEPGFLYHIKYRVAGSPDFLTIATTRPETLFGDVALAVHPEDDRYSKYVGQTAIVPMTYGRHVPIIADKYVDKDFGTGVLKISPGHDHNDYLLARKLGLPILNVMNKDATLNDVAGLFCGLDRFEVREKLWADLEEIGLAVKKEPHTLRVPRSQRGGEVIEPLVSKQWFVHMDPLAEKALLAVENKELTIIPERFEKIYNHWLTNIKDWCISRQLWWGHRIPVWYVVGKDCEEDYIVAKSAEEALEKALEKYGKDVEIYQDPDVLDTWFSSSLWPFSTLGWPDVAAKDFNNFYPTNMLETGHDILFFWVARMVMMGIEFTGTVPFSHVYLHGLIRDSQGRKMSKSLGNVIDPLDTIKDFGTDALRFTIALGTAGQDLNLSTERLTANKAFTNKLWNAGKFVLHSLPSLSDTSAWENLLDLKLDKEETLLSLPLPECWAVSKLHILIDSVTASYEKLFFGDVGRETYDFFWSDFADWYIEASKSRLYGSGGNSVSLASQAVLLYVFENILKLLHPFMPFVTEDLWQALPYRKEALIVSPWPQNSLPRNVESIKRFENLQALTRAIRNARAEYSVEPVKRISASVVGSAEVIEYISKEKEVLALLSRLDLNNVHFSNAPPGDANLSVHLVASEGLEAYLPLAAMVDISSEVQRISKRLSKMQTEYDALITRLSSPKFVEKAPEEVVRGVKEQVEELEEKIKLTKARLDFLKSTTSLVSQ", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast Mitochondrion. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
+{"protein": "MSGFVVWFTGLSGAGKSTLAAMLSAELRARSVHVEVLDGDEVRTNLSKGLGFSKEDRDTNIRRIGYVAKLIARSGACAMTAAISPYKAIRDEQRAQIPHFVEVFCSCEIPVLAERDAKGLYKKALAGEIKNFTGIDDPYEAPESPEVVVDTGKETKEESLAKILAKLEELGYVPRRGAAVAVSGAAAAGAAAGGARGLIAPHGGELVNRWVEGAAKASLAERAKGLPVIELDERTESDVEMIAIGAFSPLRGFMNSKDYLRVVREMRLESGLPWSMPITLAVSEQAAEGLRVGSEAALRARDGRIVAVIELSDKWRPNKELEAQEVFRTTETKHPGVAYLMSTGPVYLGGEIRVLERPVDSAFPAYDRSPATTRAYFAEKGWRRIVGFQTRNPIHRAHEFITKTALEICDGLMIHPLVGATKSDDIPADVRMRCYEELIAKYYVKDRVLLSIYPAAMRYAGPREAIFHALARKNYGCSHFIVGRDHAGVGSYYGTYDAQEIFNAFSPGELGITTLNFENAFYSTVVGAMATAKTAPGDASTQVNLSGTKVRELLQRGELPPPEFSRPEVARILIESMRSSS", "text": "SIMILARITY: In the N-terminal section; belongs to the APS kinase family. SIMILARITY: In the C-terminal section; belongs to the sulfate adenylyltransferase family."}
+{"protein": "MADFDDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFALYNMDQFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEVDGGLKSWRESCDSALRAYVKDHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSLTVSNEAQTAKEFIKIIENAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA", "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": "MAKSSKRRPAPEKPVKTRKCVFCAKKDQAIDYKDTALLRTYISERGKIRARRVTGNCVQHQRDIALAVKNAREVALLPFTSSVR", "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. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family."}
+{"protein": "MSVSLSKGGNVSLSKTAPSMKNVLVGLGWDARSTDGQDFDLDASAFLLAANGKVRGDADFIFYNNLKSADGSVTHTGDNRTGEGDGDDESLKIKLDAVPGDVDKIIFVVTIHDAQARRQSFGQVSGAFIRLVNDDNQTEVARYDLTEDASTETAMLFGELYRHNGAWKFRAVGLGYAGGLASVCAQYGINAS", "text": "FUNCTION: Not known; seems to contribute to the tellurium resistance (Ter) mechanism. SIMILARITY: Belongs to the CAPAB/TerDEXZ family."}
+{"protein": "MRRAVILVLDRAGPV", "text": "FUNCTION: Involved in control of the biosynthesis of leucine."}
+{"protein": "MGCTLSTDDKAAQERSKMIDRNLRDDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFADQARADDARQLFILAGSTEEGFMTGELAGVIQRLWKDGGVQACFSRSREYQLNDSAAYYLNDLDRISHASYVPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNGMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSLLTICFPEYAGSNTYEEAAAYVQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (By similarity). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cell cortex Membrane; Lipid-anchor. SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily."}
+{"protein": "MEILMYKRLPPLNSLKSFESAARYLSFTKAADELCVTQAAVSHQIKLLEXFLGIDLFKRKNRSLELTELGKAYFVDINKILRRLNEATERLLTLKTDPHLNISVPQTFGIQWLVPHLSEFNQLYPQIEVRLTGVDQDEGLLNKEIDLAIYYGLGNWQNLQVDRLCEENLLILASPELLAENPIIQPEDLKKHTLIHIHTCDNWQAMANHLQLDDLNIQQGPLFSHTFMALQAAIHGQGIVLANRLLALQEIENGSLQAVLPTNLPDPKSFYVVNHLDRLDDQKIQAFRQWIINSIKQEENE", "text": "FUNCTION: Not known, the gcv operon regulated by the E.coli homolog does not exist in H.influenzae, so it probably acts as a transcriptional regulator on some other operon. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MRKESPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGSLLLGASSLSGRCWAGSLWFFKDPSAAPNEGFCSAGVQTEAGVADLTWVGDKGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVTVLSSGTQAVSGSKDFCIKIWDLAQQMSLNSYRAHAGQVTCVAASPHRETVFLSCSEDSRILLWDTRCPKPASQMGCNASGYLPTSLAWHPQQSEIFVFGDENGSVSLVDTKNASCTLSSAVHSQCVTRLVFSPHSVPFLASLSEDCSLAVLDSSFSEVFRSRAHRDFVRDATWSPLNHSLLTTVGWDHQVIHHVVPLEPLPAPGPDSVVE", "text": "FUNCTION: Substrate-recognition component of the DCX(WDR77) complex, which mediates ubiquitination and degradation of Irgm in intestinal cells. FUNCTION: Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MSTTTQNIPWYRHLNRAQWRAFSAAWLGYLLDGFDFVLIALVLTEVQGEFGLTTVQAASLISAAFISRWFGGLMLGAMGDRYGRRLAMVTSIVLFSVGTLACGFAPGYITMFIARLVIGMGMAGEYGSSATYVIESWPKHLRNKASGFLISGFSVGAVVAAQVYSLVVPLWGWRALFFIGILPIIFALWLRKNIPEAEDWKEKHAGKAPVRTMVDILYRGEHRIANIVMTLAAATALWFCFAGNLQNAAIVAVLGLLCAAIFISFMVQSTGKRWPTGVMLMVVVLFAFLYSWPIQALLPTYLKTELAYNPHTVANVLFFSGFGAAVGCCVGGFLGDWLGTRKAYVCSLLASQLLIIPVFAIGGANVWVLGLLLFFQQMLGQGISGILPKLIGGYFDTDQRAAGLGFTYNVGALGGALAPILGALIAQRLDLGTALGSLSFSLTFVVILLIGLDMPSRVQRWLRPEALRTHDAIDGKPFSGAVPFGSAKNDLVKTKS", "text": "FUNCTION: Catalyzes the proton-dependent transport of sialic acid. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sialate:H(+) symporter (SHS) (TC 2.A.1.12) family."}
+{"protein": "MPFDHAHWQERFDALRTEHHVPGAALAVFVDGDLHELASGVLHRGTGVAVTTDSVFQSGSVAKVYTATLVMQLVDAGELRLDTRVADVLPGFAVADAEVARTVTIGRLLSHTSGIAGDFTLDTGRGDDCLARFVDACADVGQDCPPDTVISYCSTGYAILGRIVEVLTGQSWDDALRDRLFTPLGLHQSMTLPEEALRFRVAMSHLGELGTDPEPAPVWDMLPRSAGPYGRVLITAADVVRFARMHLDDGVAPDGTRVLSAASAALMRQQVAGCLDTWSFMATGWGHGWALYDWDGVPGYGHDGASGGQFSYLRVVPGSGVVAALLTNGGVATSFFTDLFRELLGELAGVRMPEVFAPPAEPRPIDVAPLAGTYEREGGAP", "text": "FUNCTION: Involved in cell wall biosynthesis and may also act as a sensor of external penicillins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the beta-lactamase family."}
+{"protein": "MTTLTHRARRTEVGKNSEKKVESEENVNQDRNQDNEDIGDSKDIRLTLMEEVLLLGLKDKEGYTSFWNDCISSGLRGGILIELAMRGRIYLEPPTMRKKRLLDRKVLLKSDSPTGDVLLDETLKHIKATEPTETVQTWIELLTGETWNPFKLQYQLRNVRERIAKNLVEKGILTTEKQNFLLFDMTTHPVTNTTEKQRLVKKLQDSVLERWVNDPQRMDKRTLALLVLAHSSDVLENVFSSLTDDKYDMAMNRAKDLVELDPEVEGTKHSATEMIWAVLAAFNKS", "text": "FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that may antagonize the action of GOLPH3 which is required for the process of vesicle budding at the Golgi and anterograde transport to the plasma membrane. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side Note=Phosphatidylinositol 4-phosphate (PtdIns4P)- binding mediates recruitment to Golgi membranes. SIMILARITY: Belongs to the GOLPH3/VPS74 family."}
+{"protein": "MSETNGGNAARENSEVKQTAVENPIDKLDGTPKRPREKDQDEQAEETSDKSEAPNKNDEEKKEEGKKDQEPSHKKIKVDDGKTVESGIVEDDKKEDKFVFGAASKFGTGFGVAKKDTKDGDATTSTESLPASDSKTKKPFAFGSGLSFGSGFNILKNKTENNSESEKKATDVDKDKVHSGSEQLANASEDTKDKPKPLKLQKQEVKSGEESEECIYQVNAKLYQLSNIKEGWKERGVGIIKINKSKDDVEKTRIVMRSRGILKVILNIQLVKGFTVQKGFTGSLQSEKFIRLLAVDDNGDPAQYAIKTGKKETTDELYNIIVKSVPK", "text": "FUNCTION: Important for the export of protein containing nuclear export signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MNGRADFREPNAQVSRPIPDIGGGYIPTEEEWRLFAECHEECFWFRSVPLAATSMLITQGLISKGILSSHPKYGSIPKLIFACIVGYFAGKLSYVKTCQEKFKKLENSPLGEALRSGELRRSLPPGHYTQKPKYDSNVSGQSSFGTSPAADNIEKETLPRYEPIPFSASMNESTPTGITDHIAQGPDPNLEDSPKRKSVTYEELRNKNRESYGVTLSHKTDPSVRPMQERGPQKEVKVNKYGDTWDE", "text": "FUNCTION: Maintains stem cell potency (By similarity). Increases STAT3 phosphorylation and controls ERK phosphorylation (By similarity). May act as a scaffold, increasing STAT3 recruitment onto endosomes (By similarity). SUBCELLULAR LOCATION: Endosome. SIMILARITY: Belongs to the OCIAD1 family."}
+{"protein": "MSEEAVALVVDNGSGMVKSGLAGDDAPKCVFPSIVGRPKMPNIMIGMEQKECYVGDEAQNKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVSPEEHPVLLTEAPLNPKTNREKMTQIMFETFDVPAMYVSIQAILSLYASGRTTGIVLDSGDGVSHTVPIYEGYVLPHAINRIDMAGRDLTYHMMKWFTERGHTFTTTAEREIVRDIKEKLCYIAMDYDEELKRSEEHSDEIEEIYELPDGNLITVGSERFRCPEALFNPTLIGRECPGLHITAYQSIMKCDIDIRKELYNNIVLSGGTTMYNNIGERLTKEMTNLAPSSMKIKVIAPPERKYSVWIGGSILSSLSTFQQMWITKEEYEDSGPSIVHRKCF", "text": "FUNCTION: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm. Polymerizes into longer and more stable actin filaments compared to ACT1/actin-1. 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 in male gametocyte development in the mosquito midgut, functioning in several processes including male gametocyte egress from host erythrocytes, formation of a beating flagellum and relocalization of ACT1/actin-1 to the cytoplasm. On the basal side of the mosquito midgut epithelium, required for the development of ookinetes into sporogonic oocysts. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Note=Prior to gametocyte activation in the mosquito midgut, localizes to the cytoplasm. Following gametocyte activation, localizes to a ring around the nucleus. SIMILARITY: Belongs to the actin family."}
+{"protein": "MSALTKASGALKSVDYEVFGRVQGVCFRMYTEEEARKLGVVGWVKNTRQGTVTGQVQGPEDKVNAMKSWLSKVGSPSSRIDRTNFSNEKEISKLDFSGFSTRY", "text": "FUNCTION: Its physiological role is not yet clear. SIMILARITY: Belongs to the acylphosphatase family."}
+{"protein": "MAKVSLEKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGTQLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDIPALCDALASKHLAGAAIDVFPTEPATNSDPFTSPLCEFDNVLLTPHIGGSTQEAQENIGLEVAGKLIKYSDNGSTLSAVNFPEVSLPLHGGRRLMHIHENRPGVLTALNKIFAEQGVNIAAQYLQTSAQMGYVVIDIEADEDVAEKALQAMKAIPGTIRARLLY", "text": "FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family."}
+{"protein": "MSPTYDVIVIGLGGMGSAAAHHLSARGARVLGLEKFGPVHNRGSSHGGSRITRQSYFEDPAYVPLLLRAYELYEELERATGRNVATLCGGVMAGPPDSRTVSGSLRSATEWDLAHEMLDAKEIRRRFPTLAPDDDEVALFEAKAGLLRPENMVAAHLQLATRQGAELRFEEPVLRWEPYRDGVRVHTGENTYTAGQLVICPGAWAPQLLADIGVPITVERQIMYWFQPKGGTGPFVPERHPVYIWEDADGVQVYGFPAIDGPEKGAKVAFFRKGQHTTPETIDRTVHAHEVRAMADHMSALIPDLPGTFLKAATCMYSNTPDEHFVIARHPAHPESVTVACGFSGHGFKFVPVVGEILADLALTGATAHPIGLFDPARLTAPAARGVQP", "text": "FUNCTION: Catalyzes the oxidative demethylation of sarcosine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MSOX/MTOX family. MSOX subfamily."}
+{"protein": "MDVGELLSYQPNRGTKRPRDDEEEELKTRRKQTGPRERGRYREEEATAAEDTADDKKRLLQIIDRDGEEEEEEEEPLDESSVKKMILTFEKRSYKNQELRIKFPDNPEKFMESELDLNDIIQEMHVVATMPDLYHLLVELSAVQSLLGLLGHDNTDVSIAVVDLLQELTDIDTLHESEEGAEVLIDALVDGQVAALLVQNLERLDESVREEADGVHNTLAIVENMAEFRPEMCTEAAQQGLLQWLLKRLKAKMPFDANKLYCSEVLAILLQDNDENRELLGELDGIDVLLQQLSVFKRHNPSTAEEQEMMENLFDALCSCLMLSSNRERFLKGEGLQLMNLMLREKKVSRSSALKVLDHAMIGPEGTDNCHKFVDILGLRTIFPLFMKSPRKIKKVGTTEKEHEEHVCSILASLLRNLRGQQRTRLLNKFTENDSEKVDRLMELHFKYLSAMQVADKKIEGEKHDIVRRGEIIDNDMEDEFYLRRLDAGLFILQHICYIMAEICNANVPQIRQRVHQILNMRGSSIKIVRHIIKEYAENIGDGRSPEFRETEQKRILALLENF", "text": "FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing (By similarity). Participates in AID/AICDA-mediated somatic hypermutation (SHM) and class-switch recombination (CSR), 2 processes resulting in the production of high-affinity, mutated isotype-switched antibodies (PubMed:20585033). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MMAYMNPGPHYSVNALALSGPSVDLMHQAVPYPSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGGQAKARPAKRKAGTSPRPSTDVCPDPLGISDSYSPPLPGPSGSPTTAVATVSIWSPASESPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYGSPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYGAYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL", "text": "FUNCTION: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family."}
+{"protein": "MSDRPTQGLTWGPRRDFYNESGSQKIIRKLKEEPLVPIGCILTIAAFTNAYRAMRRGDHHKVQRMFRARVAAQGFTVLAMVGGGMYYAEDRNKRKELGKLKQQQEAEEKRQKWIRELEARDEEEKALQEMMDKKRKRASERTMRAETGSEGIAAQARAAFKDKANKGEAAGAEKTEAPSQRADNEKKPAGSGFLGGWFGGSSKTPETPAKDTKGKNLDSESSS", "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": "MSKKTTPSSAPLDNTPYDVTEQVGHLLRKAYQRHTAIFQQQACDPQLTSIQFVTLCALRDHGPSSQAELIKATAVDQATIRGIVERLKARELVQLSPDPGDRRKVIVELTESGAALLDAMIPCARQISELSMGSLNAGERVAILYLLRKMIDSDENAG", "text": "FUNCTION: Transcriptional repressor for the nicCDEFTP and nicXR operons, encoding the lower aerobic nicotinate degradation pathway. Acts under non-induced conditions: repression of the nicCDEFTP and nicXR operons becomes alleviated in presence of 6-hydroxynicotinate (6HNA)."}
+{"protein": "MSAQISDSIEEKRGFFTRWFMSTNHKDIGVLYLFTAGLAGLISVTLTVYMRMELQHPGVQYMCLEGMRLVADAAAECTPNAHLWNVVVTYHGILMMFFVVIPALFGGFGNYFMPLHIGAPDMAFPRLNNLSYWLYVCGVSLAIASLLSPGGSDQPGAGVGWVLYPPLSTTEAGYAMDLAIFAVHVSGATSILGAINIITTFLNMRAPGMTLFKVPLFAWAVFITAWMILLSLPVLAGGITMLLMDRNFGTQFFDPAGGGDPVLYQHILWFFGHPEVYMLILPGFGIISHVISTFARKPIFGYLPMVLAMAAIAFLGFIVWAHHMYTAGMSLTQQTYFQMATMTIAVPTGIKVFSWIATMWGGSIEFKTPMLWALAFLFTVGGVTGVVIAQGSLDRVYHDTYYIVAHFHYVMSLGALFAIFAGTYYWIGKMSGRQYPEWAGQLHFWMMFIGSNLIFFPQHFLGRQGMPRRYIDYPVEFSYWNNISSIGAYISFASFLFFIGIVFYTLFAGKPVNVPNYWNEHADTLEWTLPSPPPEHTFETLPKPEDWDRAQAHR", "text": "FUNCTION: Subunit 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). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the heme-copper respiratory oxidase family."}
+{"protein": "MEARRARQKALKVKNLKDVRYMKLISMETSSSSDDSCDSFASDNFANTRLQLNREGCRTRSQCRHSGPLRVAMKFPARNTRRAASKKAAPPKPSESSANDSHSDSEEEEEEEEEEDGMNFLEKRALNIKQNKAMLAKLMSELESFPGLFSGRHSLPGHRAKDSKSPRRRTFPGVATRRNPERRTRPLTRSRSRILGSLGALPTEEEEEEEEEEEDKYMLVRQRKSMDSYMNDDDVPRSRRPGSMTLPHIIRPVEEVTEEEIRNICSNSREKIYNRSLGSTCHQCRQKTTDTKTNCRNPDCWGIRGQFCGPCLRNRYGEEVKDALLDPNWHCPPCRGICNCSFCRQRDGRCATGVLVYLAKYHGFGNVHAYLKSLKQEFEMQA", "text": "FUNCTION: Participates in MYC-mediated cell transformation and apoptosis; induces anchorage-independent growth and clonogenicity in lymphoblastoid cells. Insufficient to induce tumorigenicity when overexpressed but contributes to MYC-mediated tumorigenesis. May play a role as transcriptional regulator (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Predominantly nuclear with some expression also seen in the cytoplasm. Predominantly cytoplasmic when phosphorylated at Thr-170 (By similarity)."}
+{"protein": "MILPSEKSATDVAAQCFLNALIRETKDWQLAEYPPDELIIPLDEQKSLHFRVAYFSPTQHHRFAFPAHLVTASGSYPVDFTTLSRLIIDKLRHQLFLPVPLCETFHQRVLESYAHTQQTIDARHDWAILREKALNFGEAEQALLTGHAFHPAPKSHEPFNRQEAERYLPDMAPHFPLRWFSVDKTQIAGESLHLNLQQRLTRFAAENAPQLLNELSDNQWLFPLRPWQGEYLFQQVWCQALFAKGLIRDLGEAGTSWLPTTSSRSLYCATSRDMIKFSLSVRLTNSVRTLSVKEVERGMRLARLAQTDGWQMLQARFPTFRVMQEDDWTGLRDLNGNIMQESLFSPAWKTLLLEQPQSQTNVLVSLTQAGPHGGDSLLVSAVKRLSDRLGITVQQAAHAWVDAYCQQVLKPLFTAEADYGLVLLAHQQNILVQMLGDLPVGFIYRDCQGSAFMPHATEWLDTIDEAQAENIFTREQLLRYFPYYLLVNSTFAVTAALGAAGLDSEANLMARVRTLLAEVRDQVTHKTCLNYVLESPYWNVKGNFFCYLNDHNENTIVDPSVIYFDFANPLQAQEV", "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": "MFRLRDFEYYNRTVFLRVDLNSPMSNGKIISDARFRAVLPTIKYLIESGAKVVVGTHQGKPYSEEYSTTEEHARILSELLNMHVEYVEDIFGKYARERIKAMKPGEVIVLENLRFSAEEVKNATIEECEKTFFVRKLSQVIDLVVNDAFAAAHRSQPSLVGFARIKPMIMGFLMEKEVDALTKAYESEEKPRVYVLGGAKVDDSLKVAENVLRKEKADLILTGGLVGQLFTLAKGFDLGRENIKFLEKKGILKYVDWAEKILDEFYPYVRTPVDFAIDFKGERVEIDLLSDEKRLFDEYPILDIGSRTVEKYREILLKARIIVANGPMGVFEREEFAVGTIGVFKAIGESPAFSVIGGGHSIASIYKYNITGISHISTGGGAMLTFFAGEKLPVLEALKISYEKFSNLLS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
+{"protein": "MPRDGTNEQRFLELPSPMSFILNILRNVLEYFGVPVDQDLLICQNKNCGSARSIVRIIGRRLPLKPCRRPHFELIPHVNSTESDDYELRVPSFADVLCVANDEEASCLRFRHSLWQKKEERKIAPFYPSKLTWDPSSPGLRQNKTETDDLPVNEAAIKKIAALEDELTFLRSQIAAIVAMQDLRESRETGFIDLSDEQVPPSSATTGLSVEPDHAPSVVLPPPPPPPPPPQFSLQPPSSLPMQPGSANTHDIDSLATEMERQLSGVKKTDDSHHSKSQRLRDVPNMLDVLKDVNKVRLRPVERSPGGRPVQKRKRRSSEWDPVSLISNALKQKFAFQDDSFDRENSSWECSPFSSPETSRF", "text": "FUNCTION: May play a role in mitochondrial aerobic respiration essentially in the testis. Can also promote mitochondrial fission. SUBCELLULAR LOCATION: Mitochondrion Note=Associated with membranes. SIMILARITY: Belongs to the MTFR1 family."}
+{"protein": "MSVHHKKKLMPKSALLIRKYQKGIRSSFIGLIIVLSFLFFMSGSRSPEVPIAQGTSVSRVASKDYLMPFTDKSQGVIHPVDDGKKEKGVMVTLARNSDLWNLVKSIRHVEDRFNNRYHYDWVFLNDQPFSDEFKRVTSALVSGKAKYGTIPKDHWSIPSWIDTEKFDEKRLAMGKLDIPYGSSVPYRHMCRFQSGFIWRHPLLEEYEWFWRVDTDITLFCDIQYDIFKFLKVNNKKYGFILSVSEYERTIPTLWETTKKFIKKNPKFLHKNNLMKFISNDDGDTYNMCHFWTNFEIGSLDFFRSDAYREYFDYLDSSGGFFYERWGDAPVHSIAASLFLDKSEIHFFDGLGFHHPDFTSCPIEQKIRLQNKCICEPSKDVTWTPDYFCTRKYFSAGNYKLPPGI", "text": "FUNCTION: Possible glycosyltransferase that 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": "MQYKNLGRSGLRVSQLSYGAWVTFGNQLDVKEAKALLQACRDAGVNFFDNAEVYANGRAEEIMGQAMRDLGWRRSDVVVSTKLFWGGQGPNDKGLSRKHIVEGLRGSLKRLDMDYVDVVYCHRPDATTPVEETVRAMNWVIDHGMAFYWGTSEWSAQQITEAWSVANRLDLVGPIVEQPEYNLFSRHKVESEFLPLYSTYGLGLTTWSPLASGVLTGKYAKGNIPADSRFALENYKNLANRSLVDDTLRKVNGLKPIASELGVSLAQLAIAWCASNPNVSSVITGATKENQIVENMKALDVIPLLTPEVVDKIEAVVQSKPKRTESYR", "text": "FUNCTION: Probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. SIMILARITY: Belongs to the shaker potassium channel beta subunit family."}
+{"protein": "MADNTDNRRSLWGVPEKLQLHIAMLTLQFGYAGFHVVSRAALNMGISKLVFPVYRNIIALLLLLPFAYFLEKKERPAITLNFLIQFFFLALIGITANQGFYLLGLDNTSPTFASSMQNSVPAITFLMAALLRIEKVRINRRDGISKILGTALCVAGASVITLYKGPTIYTPASHLHAHLLTTNSAVLAPLGNAAPKNWTLGCIYLIGHCLSWSGWLVFQAPVLKSYPARLSVTSYTCFFGIIQFLIIAAFCERDSQAWVFHSGWELFTILYAGIVASGIAFAVQIWCIDRGGPVFVAVYQPVQTLVVAIMASIALGEEFYLGGIIGAVLIIAGLYFVLYGKSEERKFAALEKAAIQSSAEHGIERAPVSRNSIKSSITTPLLHQSTDNV", "text": "FUNCTION: Required for secondary wall formation in fibers, especially in short days conditions. Promotes indole metabolism and transport (e.g. tryptophan, neoglucobrassicin and auxin (indole-3-acetic acid)). May prevent salicylic-acid (SA) accumulation. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Also detected in transvacuolar strands. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Plant drug/metabolite exporter (P-DME) (TC 2.A.7.4) family."}
+{"protein": "MTATVENLTFQKDTLGNAVDKNTSRLELRSYSLAGRHGSTEPLVLAWSSQFRRLTWGCALDALHRSPCVAASQHGVTHLIRSSRTPHSTRCRKEDAQPGHHGNGAASVTAQARGQRSVLQVPLPVPRSCLFSESFVVSVSSQSRFLASVPGTGVQRSTAADMAASTAAGKQRIPKVAKVKNKAPAEVQITAEQLLREAKERELELLPPPPQQKITDEEELNDYKLRKRKTFEDNIRKNRTVISNWIKYAQWEESLKEIQRARSIYERALDVDYRNITLWLKYAEMEMKNRQVNHARNIWDRAITTLPRVNQFWYKYTYMEEMLGNVAGARQVFERWMEWQPEEQAWHSYINFELRYKEVDRARTIYERFVLVHPDVKNWIKYARFEEKHAYFAHARKVYERAVEFFGDEHMDEHLYVAFAKFEENQKEFERVRVIYKYALDRISKQDAQELFKNYTIFEKKFGDRRGIEDIIVSKRRFQYEEEVKANPHNYDAWFDYLRLVESDAEAEAVREVYERAIANVPPIQEKRHWKRYIYLWINYALYEELEAKDPERTRQVYQASLELIPHKKFTFAKMWILYAQFEIRQKNLSLARRALGTSIGKCPKNKLFKVYIELELQLREFDRCRKLYEKFLEFGPENCTSWIKFAELETILGDIDRARAIYELAISQPRLDMPEVLWKSYIDFEIEQEETERTRNLYRRLLQRTQHVKVWISFAQFELSSGKEGSLTKCRQIYEEANKTMRNCEEKEERLMLLESWRSFEEEFGTASDKERVDKLMPEKVKKRRKVQTDDGSDAGWEEYFDYIFPEDAANQPNLKLLAMAKLWKKQQQEKEDAEHHPDEDVDESES", "text": "FUNCTION: Involved in pre-mRNA splicing process (PubMed:11991638, PubMed:12084575, PubMed:28076346, PubMed:28502770). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Note=Colocalizes with core spliceosomal snRNP proteins (PubMed:12084575). SIMILARITY: Belongs to the crooked-neck family."}
+{"protein": "MGLAKETTMGGRGRVAKVEVQGKKPLSRVPNTKPPFTVGQLKKAIPPHCFQRSLLTSFSYVVYDLSFAFIFYIATTYFHLLPQPFSLIAWPIYWVLQGCLLTGVWVIAHECGHHAFSKYQWVDDVVGLTLHSTLLVPYFSWKISHRRHHSNTGSLDRDEVFVPKPKSKVAWFSKYLNNPLGRAVSLLVTLTIGWPMYLAFNVSGRPYDSFASHYHPYAPIYSNRERLLIYVSDVALFSVTYSLYRVATLKGLVWLLCVYGVPLLIVNGFLVTITYLQHTHFALPHYDSSEWDWLKGALATMDRDYGILNKVFHHITDTHVAHHLFSTMPHYHAMEATNAIKPILGEYYQFDDTPFYKALWREARECLYVEPDEGTSEKGVYWYRNKY", "text": "FUNCTION: ER (microsomal) omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes. It is thought to use cytochrome b5 as an electron donor and to act on fatty acids esterified to phosphatidylcholine and, possibly, other phospholipids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
+{"protein": "MSHTTHPYQKELEVATLAVKRASLLTKQLSDSIVQTARSGTLTKDDKSPVTIGDFASQAIINHAIKLNFPSDEIVGEEDSQELQENSSLADQVLSLIIKIQQETSVYNDVVGTLTDKNKVFQSIDYGNSQGGSKGRFWALDPIDGTKGFLRGDQFAVCLALIEDGKVVLGVIGCPNLSENIVSNEEHSGVVGGLYSAVKGVGSFYSELFKEGTEPLSQQKPIKMQNHTNPSQLKVVEGVEKGHSSHSTQAEIKAKLGFDPTTVAKQTVNLDSQVKYCVLASGQADIYLRLPVSDTYREKIWDHAAGNILIYESGGQVGDVTGAPLNFGNGRTLDSKGVIAANKEIFDKVIDAVTEIRKSSTPRV", "text": "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. Involved in salt tolerance (By similarity). SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
+{"protein": "FNTNTQMTAYDQDRMXXXXLPVENVRVALEENTLIMKNGVLKVAVPKVKQEERKDV", "text": "FUNCTION: May play a protective role against oxidative stress. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MLVGYARVSTEGQSLNRQIDMLVDYGLDKRNIYQEKISGTKLRRDQLDKMIEELQEGDTVIITDLTRISRSTKDLLNIIDRIKEKGASIKSLKDTWLDTSGDNPYNSFLLTVMSGLSQLERDLISQRTKEGLRSAKARGRNGGRPSKRNDKADTVGLLYREGYKIVDIVKQTELSRATVYRILKDLNLK", "text": "FUNCTION: A likely role for the res protein would be to stabilize pCP13 by reducing the number of plasmid multimers resulting from homologous recombination. SIMILARITY: Belongs to the site-specific recombinase resolvase family."}
+{"protein": "MNKIESRHQLILSLIMEKKIHTQQELQELLEVNGVSVTQSTLSRDIKMLNLVKVNEDDSSHYVINPIAPTRWEKRLRLYMEDALVMLKPIQHQVVLKTLPGLANSFGSILDAMEIPQIVATVCGDDVCLIICEDVEGAQACFEHLKQFTPPFFFSKL", "text": "FUNCTION: In the presence of arginine, coactivates the transcription of the arcABDC operon, with other regulatory proteins such as ArcR and CcpA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ArgR family."}
+{"protein": "MKKKNHKYRGKKLNRGESPNFSGQHLMHNKKLIEEIVDRANISIDDTVLELGAGKGALTTVLSQKAGKVLAVENDSKFVDILTRKTAQHSNTKIIHQDIMKIHLPKEKFVVVSNIPYAITTPIMKMLLNNPASGFQKGIIVMEKGAAKRFTSKFIKNSYVLAWRMWFDIGIVREISKEHFSPPPKVDSAMVRITRKKDAPLSHKHYIAFRGLAEYALKEPNIPLCVALRGIFTPRQMKHLRKSLKINNEKTVGTLTENQWAVIFNTMTQYVMHHKWPRANKRKPGEI", "text": "FUNCTION: Involved in erythromycin resistance. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family."}
+{"protein": "MFAISVLKELYDSGEPLLFSPRGLHKILCNIRHGCNGNTKNQLDNLLEETIYDYGEDQALKHIITNISVLLIKRCYNINEKFIKDSNTIYNTDVLEFYNVRQIPRIMNKWIRSRSNNKITDIGCHIYDNTKSIIAEAMFFTMKHESIFGSTRKDTITFYKYDGTSLPVEAIHADPYYYPYRYFDDIKCSVLQLWKLGYAFNMFIILPDDEKGLDNLVDNITGDVFSKIMTEQMDYKRLELRMPVFSISQETNFCMPIFNLGCHSMFIDGDFSGISEVSDFQLSGIIQKNIIEVQYDKVKTTKPLNVRCSSFYVNKPFIFIVTDVGNYDTIPILLGIYQGSSK", "text": "SIMILARITY: Belongs to the serpin family. Poxviruses subfamily."}
+{"protein": "MYVSYLLDKDVSMYPSSVRHSGGLNLAPQNFVSPPQYPDYGGYHVAAAAAAAANLDSAQSPGPSWPAAYGAPLREDWNGYAPGGAAAAANAVAHGLNGGSPAAAMGYSSPADYHPHHHPHHHPHHPAAAPSCASGLLQTLNPGPPGPAATAAAEQLSPGGQRRNLCEWMRKPAQQSLGSQVKTRTKDKYRVVYTDHQRLELEKEFHYSRYITIRRKAELAATLGLSERQVKIWFQNRRAKERKINKKKLQQQQQQQPPQPPPPPPQPPQPQPGPLRSVPEPLSPVSSLQASVPGSVPGVLGPTGGVLNPTVTQ", "text": "FUNCTION: Transcription factor which regulates the transcription of multiple genes expressed in the intestinal epithelium (By similarity). Binds to the promoter of the intestinal sucrase-isomaltase SI and activates SI transcription (By similarity). Binds to the DNA sequence 5'-ATAAAAACTTAT-3' in the promoter region of VDR and activates VDR transcription (By similarity). Binds to and activates transcription of LPH (By similarity). Activates transcription of CLDN2 and intestinal mucin MUC2 (By similarity). Binds to the 5'-AATTTTTTACAACACCT-3' DNA sequence in the promoter region of CA1 and activates CA1 transcription (By similarity). Important in broad range of functions from early differentiation to maintenance of the intestinal epithelial lining of both the small and large intestine. Binds preferentially to methylated DNA (PubMed:28473536). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Caudal homeobox family."}
+{"protein": "MDQDYERRLLRQIVIQNENTMPRVTEMRRTLTPASSPVSSPSKHGDRFIPSRAGANWSVNFHRINENEKSPSQNRKAKDATSDNGKDGLAYSALLKNELLGAGIEKVQDPQTEDRRLQPSTPEKKGLFTYSLSTKRSSPDDGNDVSPYSLSPVSNKSQKLLRSPRKPTRKISKIPFKVLDAPELQDDFYLNLVDWSSLNVLSVGLGTCVYLWSACTSQVTRLCDLSVEGDSVTSVGWSERGNLVAVGTHKGFVQIWDAAAGKKLSMLEGHTARVGALAWNAEQLSSGSRDRMILQRDIRTPPLQSERRLQGHRQEVCGLKWSTDHQLLASGGNDNKLLVWNHSSLSPVQQYTEHLAAVKAIAWSPHQHGLLASGGGTADRCIRFWNTLTGQPLQCIDTGSQVCNLAWSKHANELVSTHGYSQNQILVWKYPSLTQVAKLTGHSYRVLYLAMSPDGEAIVTGAGDETLRFWNVFSKTRSTKVKWESVSVLNLFTRIR", "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) (PubMed:25349192). SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family."}
+{"protein": "MAPSTVAVEMLSPKEKNRLRKPVVEKMRRDRINSSIEQLKLLLEQEFARHQPNSKLEKADILEMAVSYLKHSKAFAAAAGPKSLHQDYSEGYSWCLQEAVQFLTLHAASDTQMKLLYHFQRPPAPAAPAKEPPAPGAAPQPARSSAKAAAAAVSTSRQPACGLWRPW", "text": "FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. Plays an important role as neurogenesis negative regulator. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSEILCTICARGGSKGVKNKNIRKINDLEMIAYSIIQAKNSKLFKHIVISTDSEEIAKIALKYGGEVFFKREAHLASDTAAKIPVMRDALLRSEEYFKCQFDTLIDLDASAPLRSSADIIKAFETFCQNQNDNLITAVPARRNPYFNLIEVQDGKVVKSKSGNFTTRQSVPKCYDMNASIYIFKRDFLLQNDSVFGKNTGLFIMDESTAFDVDSELDFKIVEFLIKEKNLQAKDF", "text": "FUNCTION: Required for biosynthesis of LAH modification in the post- translational modification of Campylobacter coli flagellin. SIMILARITY: Belongs to the CMP-NeuNAc synthase family."}
+{"protein": "MGLASTVSLALLGLCSLARAQTSAADAYVSAESPIAQAGILANIGPSGSKSHGAASGVIIASPSTSNPDYLYTWTRDAALVSRALVDEFIEGESSLQSVIDSYVSSQQKLQRVDNPSGSYTSGGLGEPKFNIDLTAFTGAWGRPQRDGPALRAITLITYGNHLLSSGNTSYVTDTIWPVVKADLDYVVSYWNQTGFDLWEEVSSSSFFTTAEQHTALRLGATFATAVGASASTYLTQADNVLCFLQSYWNSNGGYATANTGGGRSGIDANTVLTSIHTFDIEAGCDSVTFQPCSDRALSNLKVYVDSFRGLYSINPTGATDPILTGRYKEDVYYNGNPWYLTTFAVAEQLYDALNTWDKLGSLDVTSTSLAFFKQFDSSITAGTYASSTSEYATLTSAIRNWADGFLEVLADFTPADGGLTEQIDKSSGNPTSAADLTWSYASAITAFKARGGAIPASWGAAGLTVPATCSTGGGGGSGGDTVAVTLNVQATTVYGENIYVTGSVNQLANWSPDNAIALNADNYPTWSVTVNLPANTQIEYKYIRKNNGQVTWESDPNRSITTSASGSFTQNDTWR", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 15 family."}
+{"protein": "MPASMFSIDNILAARPRCKDSVLPVAPSAAAPVVFPALHGDSLYGASGGASSDYGAFYPRPVAPGGAGLPAAVSGSRLGYNNYFYGQLHVQAAPVGPACCGAVPPLGAQQCSCVPAPSGYEGPGSVLVSPVPHQMLPYMNVGTLSRTELQLLNQLHCRRKRRHRTIFTDEQLEALENLFQETKYPDVGTREQLARKVHLREEKVEVWFKNRRAKWRRQKRSSSEESENAEKWNKTSSSKASPEKREEEGKSDLDSDS", "text": "FUNCTION: Regulates chordin (CHRD). May play a role in spatial programing within discrete embryonic fields or lineage compartments during organogenesis. In concert with NKX3-2, plays a role in defining the structural components of the middle ear; required for the development of the entire tympanic ring (By similarity). Probably involved in the regulatory networks that define neural crest cell fate specification and determine mesoderm cell lineages in mammals (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily."}
+{"protein": "MERFLTKMPIKSKANEVPKKEAVAKKETPKVARKATKKDTPKELKDKENAGDDNTPKQTKGRPGRPAAKRKNLDTPDVKDEKIAMEEENPPKRRSSRLTRSTRSMAEDGSPSPEKEKPEKLPFIKYKGAIKYFTESQDIAASADDVLQWVEKQKDDVVPMAFDMEWPFSFQTGPGKSSVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKNDFRKLARDFPEVTAEPLIEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELERREKVKIKNEEEFKEKNGDAAFKAMKTLGETFLTKINEVTL", "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": "MISFLVQKSEAKYWKDVVQNKNKFLKNIGIISGPKLVDTYSNQFEADFLKKCVLIPTSYNKEDLPKDILDCPRIYLIEEEVKSVQTDEKLQIKVLRYVSQILHTTVSEEQYPVPSRFVIYPPLALLSLNSFGTKEWHLFFQSYANVDVKAGLFDIFAREWNVSHIAINEPIPVGDVMRRPLSLKPLYGDFGVLIDGNPSEQDFQKAFWVSCRQNGIYQTWAPLYTMFSRGNSIEKARVLNFSYIKDEIIADLYAGIGYFTFSYVKAGASTVFCWEINPWSVEALRRAALKNGWSIYVVRNGENYEFKVGTHRIVVFLESNVYAAERFSKMNISARHINLGMLPSSEKSWSTATSILKRESHSFIHVHENVKDEDIETYSSEVNSCFSKMLAKNTVCVTNCVKSFSPRVSHIVYDIETV", "text": "FUNCTION: S-adenosyl-L-methionine-dependent transferase 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. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S- adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family."}
+{"protein": "MDPGQQPPPQPAPQGQGQPPSQPPQGQGPPSGPGQPAPAATQAAPQAPPAGHQIVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTPTGVVSGPAATPTAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPRKAMLSQMNVTAPTSPPVQQNMMNSASGPLPDGWEQAMTQDGEIYYINHKNKTTSWLDPRLDPRFAMNQRISQSAPVKQPPPLAPQSPQGGVMGGSNSNQQQQMRLQQLQMEKERLRLKQQELLRQAMRNINPSTANSPKCQELALRSQLPTLEQDGGTQNPVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDTINQSTLPSQQNRFPDYLEAIPGTNVDLGTLEGDGMNIEGEELMPSLQEALSSDILNDMESVLAATKLDKESFLTWL", "text": "FUNCTION: [Isoform 2]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). FUNCTION: Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). Plays a key role in controlling cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:18158288). The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage- independent growth, and epithelial mesenchymal transition (EMT) induction (PubMed:18579750). Suppresses ciliogenesis via acting as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, involved in the regulation of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). FUNCTION: [Isoform 3]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell junction Note=Both phosphorylation and cell density can regulate its subcellular localization (PubMed:18158288, PubMed:20048001). Phosphorylation sequesters it in the cytoplasm by inhibiting its translocation into the nucleus (PubMed:18158288, PubMed:20048001). At low density, predominantly nuclear and is translocated to the cytoplasm at high density (PubMed:18158288, PubMed:20048001, PubMed:25849865). PTPN14 induces translocation from the nucleus to the cytoplasm (PubMed:22525271). Localized mainly to the nucleus in the early stages of embryo development with expression becoming evident in the cytoplasm at the blastocyst and epiblast stages (By similarity). SIMILARITY: Belongs to the YAP1 family."}
+{"protein": "MKYLYLEITSRCNLRCEMCFKQHWEDEEGDMDYDLFLKILDDAEKFPELKMIYFGGIGEPTVHPRFMDMVREVKKRGFALGISTNGTLLTDEMLKELAELGVDLVYFSMDVLPTAQNVVTLGHILAGVTAEKIKKLVKYREEVGTHKPSIGVEVVVTKENYKQLPELARYLLNLGVDAMLVSNLLPLTPEQVNDIVYDGSIDMTPIVNELYKIAHNGLYIKLPYFELKTERVCDFDENKVAVIRWDGEVVPCYRFLHTYREYIFGREKKVNTYSFGNVREKSLADIWTSERYTWFRFITKNYLYPSCTDCSLRDACDFVKTTDIDCWGNEPSCADCLWSRRIVMCPIPQYNFGKFL", "text": "FUNCTION: Involved in the biosynthesis of a molybdopterin-based tungsten cofactor. SIMILARITY: Belongs to the radical SAM superfamily."}
+{"protein": "MACVDEPPEKHCWVCFATEKEDRAAEWVSPCRCKGCTKWIHQSCLQRWLDEKQKGNSGGAVSCPQCGTEYRIVFPKMGPVVYFLQQVDRALSRASPFAAAGVVVGTVYWSAVTYGAVTVMQVVGHKKGLDVMERADPLFLLMGLPTIPVMLVLGKMIRWEDYVVRLWQRHSAKLQIFSGLVPGMGRALPRVPVEGSYGGDHLSVSRTLCGALIFPSIANLVGRLLFRRVTSNLQRTILGGIAFVVMKGVLKVYFKQQQYLIQANRHILNYPEPEGQADGATEDEDSSNE", "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": "MVSSSLTKLVFFGCLLLLTFTDNLVAGKSGKVKLNLYYESLCPGCQEFIVDDLGKIFDYDLYTITDLKLFPFGNAELSDNLTVTCQHGEEECKLNALEACALRTWPDQKSQYSFIRCVESDTKGWESCVKNSGREKAINDCYNGDLSRKLILGYATKTKNLKPPHEYVPWVTLNGKPLDDSVQSTDDLVAQICNAYKGKTTLPKVCNSSASMSKSPERKWKLQVSYANKATNY", "text": "FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. SUBCELLULAR LOCATION: Secreted Lysosome. SIMILARITY: Belongs to the GILT family."}
+{"protein": "MSGGLDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYVYKRKSDGIYIINLKKTWEKLLLAARAIVAIENPADVCVISSRNTGQRACLKFASGTGATTFAGRFTPGTFTNQIQAAFREPRLLIVTDPRADHQPLTEASYVNIPTIALCNTDSPLRYVDIAIPCNNKGPHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVGKEEFQGEWSAPVADIAQLEVPDWSEGVQVPSVPIQQFPAGIEAATAAAAVVAAKPGPTTEGYSEDWSAQPATEDWSAAPTAQAGDWGGSTAEWS", "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": "MNKVLVSLLLTLGITGMAHAAGDAEAGQGKVAVCGACHGVDGNSPAPNFPKLAGQGERYLLKQLQDIKAGSTPGAPEGVGRKVLEMTGMLDPLSDQDLEDIAAYFSSQKGSVGYADPALAKQGEKLFRGGKLDQGMPACTGCHAPNGVGNDLAGFPKLGGQHAAYTAKQLTDFREGNRTNDGDTMIMRGVAAKLSNKDIEALSSYIQGLH", "text": "FUNCTION: Diheme, high potential cytochrome c believed to be an intermediate electron donor to terminal oxidation systems. SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "MKSLVNLWGIYPFIRNNSLHGFAKIPRIVSTIPRQLRFSSLRHPTRQMDLIHDTVVVENLNTFAVVGQDQWKRKEPQPVQIDVYMRNNVQLAGEKDELKSTIHYGIASKLLRKEIEGSFFTTPKDLVNKIASLCFEDVIDTSHVSIKLTLPKCVLRSKNGLHYYAERERNSTSNFVDRIEFSDLELATILGIHAFERQEKQRVCLNISFANTEVEALEIARAIAEYVEQSAFLTIEALVVNLSKYLCFTKNLDDISIKAEKPSAITFANASAVQIYRTRSYFLQESLHKYESTKNKIAYLSFGSNIGDKFEQIQTALSMLHKIEGIRVLDVSPLYETEPMYYKDQPSFLNGVCKIETRMSPINLLRACQSIEQEMGRIKTILKGPRCIDLDIVLYEDCVYESEVLTIPHLGLQEREFVLRPLLALSPDLVHPYTHQPLQEALDKLPSQGIRLYSSFDNKKIINGALTMGILNVTPDSFSDGGKVSQNNILEKAKSMVGDGASILDIGGQSTKPGADPVSVEEELRRVIPMISLLRSSGITVPISIDTYYSKVAKLAIEAGANIINDVTGGMGDEKMLPLAASLQVPICIMHMRGTPETMKALSIYEKDIVEEVAVELSSRVEAAVQSGVHRYNIILDPGFGFAKTPKQSAGLLGRLHELMKKPQFKDMHWLSGPSRKGFTGYFTGDASPKDRIWGTSACVTASVLQGVSIVRVHDTKEMSKVVGMANAIRYVP", "text": "FUNCTION: Catalyzes three sequential steps of tetrahydrofolate biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the DHNA family. SIMILARITY: In the central section; belongs to the HPPK family. SIMILARITY: In the C-terminal section; belongs to the DHPS family."}
+{"protein": "MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSMAAAKSGTKAKRAARPAKYSYVDENGETKTWTGQGRTPAVIKKAMEEQGKQLEDFLIKE", "text": "FUNCTION: Binds tightly to dsDNA (PubMed:10844682). Acts as a global transcriptional regulator through its ability to bind to AT-rich DNA sequences (PubMed:1423593, PubMed:16933988, PubMed:21673140). Binds in the minor groove of AT-rich DNA (PubMed:21673140). Was found to bind 746 genes, about half of which show no change in expression in disruption experiments suggesting these sites are important for nucleoid structure (PubMed:16933988). On a global level genes bound by H-NS are expressed at a lower than average level; H-NS is excluded from binding to highly transcribed genes and does not co-localize with RNA polymerase in DNA-binding studies during exponential growth in rich medium (PubMed:16933988). The best correlation for H-NS binding is AT- content rather than predicted DNA curvature (PubMed:16933988). Has a strong preference for DNA that has been recently acquired by horizontal gene transfer, binding strongly to Salmonella pathogenicity islands 1 and 2 (SPI1 and SPI2); this offers the selective advantage of silencing foreign DNA while keeping it in the genome in case of need (PubMed:16933988). DNA-binding influences plasmid DNA topology (PubMed:1423593). For the proU locus (the proV-proW-proX operon) inhibits transcription at low osmolarity by binding to AT-rich, curved, DNA downstream of the transcription start site of proV; repression is greater when more than 1 curved DNA sequence is present (PubMed:1423593). It plays a role in the thermal control of pili production (By similarity). It is subject to transcriptional auto- repression (By similarity). It binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150 (By similarity). 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. As many horizontally transferred genes are AT-rich, it plays a central role in silencing foreign genes. A subset of genes are repressed by H-NS in association with other proteins (By similarity). FUNCTION: A DNA-binding protein implicated in transcriptional repression (PubMed:19521501) and chromosome organization and compaction. Modifies gene expression, regardless of whether the gene is chromosomal or was acquired by horizontal gene transfer (PubMed:19521501). Binds nucleation sites in AT-rich DNA and bridges them, forming higher-order nucleoprotein complexes and condensing the chromosome. As many horizontally transferred genes are AT-rich, it plays a central role in silencing foreign genes. A subset of genes are repressed by H-NS in association with Hha and/or Cnu (ydgT) (By similarity). FUNCTION: A DNA-binding protein implicated in transcriptional repression and chromosome organization and compaction. Binds AT-rich DNA, repressing its transcription; about 754/4438 tested genes (15%) bind to H-NS, 70% of these are AT-rich and correspond to horizontally transferred geness (HTG), thus playing a central role in silencing foreign genes (PubMed:16763111). This offers the selective advantage of silencing foreign DNA (PubMed:16763111). Binds nucleation sites in AT- rich DNA and bridges them, forming higher-order nucleoprotein complexes and condensing the chromosome (By similarity). A subset of genes are repressed by H-NS in association with Hha and/or YdgT (By similarity). SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the histone-like protein H-NS family. SIMILARITY: Belongs to the histone-like protein H-NS family."}
+{"protein": "GCKARGDTCQKDCDCCGCFYKCHCPLDWFGGKWHPLGCSCVYGDKYICEKKKKECPNV", "text": "FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 09 (Tx3-6) family."}
+{"protein": "MPQITLVFISLSGNTLSFVKRLSLYLADNYDYHVKQINIKDLKHETFPVKEEFVAILPTYLEGGNGVDSGEAEILTTPLGEFIAAHGNAQRCLGIIGSGNKNFNHQYCLTAKQYAKRFGFPLLGDFELRGTPDDISRLAQVIMEASSRHSSNDTQTLPNS", "text": "SIMILARITY: Belongs to the NrdI family."}
+{"protein": "MAMAAAASLLPACAAPTLPGRAFRPRRNSTPTASLSCDGGSRGRGVGLGVILGGGRAQGVRRNAAAETYVPGSGKYIAPDYLVKKVTAKELEELVRGERKVPLIVDFYATWCGPCVLMAQDIEMLAVEYENNALFVKVDTDDEYELARDMQVRGLPTLYFFSPDQSKDALRTEGLIPIDMIRNIIDNEL", "text": "FUNCTION: Probable thiol-disulfide oxidoreductase that may play a role in proper chloroplast development. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the thioredoxin family. Plant CITRX-type subfamily."}
+{"protein": "MSTKVENILEELKSLNLLEAAELVKQIEETFDVDASAASGGVMMAAPSSAPAASDVEEKTEFDVVLEEVPAPKKIAVLKVVRSLTGLGLKEAKDLVESAPKTLKEGASKDDAEAMKKQLEDAGATVGVK", "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": "MVIILKKTLEKKGADDVIASRANLGPFQAQTMSQGAALFSCGLMETSRWHDSCSIRQRPVGTSLESLWDVLPEVHSGSAQWDWDVGSASSTLTSLLQDLSLTESSSHSTAPPSKKQCRSLSCSDELGGCRSTWRPQGSRVWTTVEKRRCHSGGSVQRSSGGNLQLGFPAMQRSFSFSLPARSNAVEPPSFTQRLPYAFTSLTHSSSMPLASDPPAQPLSLSNEQICFPEPHGPSPSSSPDSTPELERRSGQGGLARSRSQPCELNEKKIGVKRRRPDDTHKQRPSLDLAKMTQKLHSFHSLSCPGITGEETCESEATPPPRSVQQRDAVDSPAHEHNLKDFQPQEGDFNGNKSSDPITEEVDWNCDDGTPETSNGKDTEPLWVGLCSMKRDVYQLGGELDIEQIERN", "text": "FUNCTION: Acts as a regulator of Wnt signaling pathway by regulating beta-catenin (ctnnb1) nuclear localization. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FAM53 family."}
+{"protein": "MTSTLIPKETSTPGGRDLRDARADYFFKLLLTAAVAFVLIALVSAALSMLWGGRQALQLQGVSFFYSTEWNPVENKYGALTPIYGTIVTALIAMLIAMPVSLGIAFFLTEVAPRWLRTPIGTAIELLAGIPSIIYGMWGLFVLVPVMTDYITPFLNDHIGTLPLIGTLFQGPPLGIGTLTAGFVLAIMVIPFISSMMREVFLTVPTQLKESAYALGSTKWEVSWNIVLPYTRSAVIGGMFLGLGRALGETMAVAFVIGNSVRLSPSLLTPGTTIAALIANDFGEATETYRSALLLLGFVLFIVTFAVLVIARLMLLRLSRKEGN", "text": "FUNCTION: Part of a binding-protein-dependent transport system for phosphate; 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. CysTW subfamily."}
+{"protein": "MKGDKKIIAHLNKLLGNELVAINQYFLHARMFKNWGLMRLNDKEYHESIDEMKHADRYIERILFLEGIPNLQDLGKLNIGEDIEEMLRSDLALELAGAKNLREGIAYADSIHDYVSRDLMIDILADEEEHIDWLETELDLIARLGIQNYAQAQILERKE", "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": "MGALGDSAYGARGRLIKFSYIVTALISILFSISCICYGIWLLARRSQYAELVSPSLYVDVGRILVIISILSILNYLICFYAIFKEMRCFVTSCAVASIVIAVMLIIGGCIGLNFRDQLTHYTPLNLKMLTSLRELYGTHDMKGITESWDALQSNFKCCGVNGTDNAQIWKTSKWYMHQRAPKLLIPESCCIPSEIERCRSNPFDQDAPPPYYTSTCYEPLQNDLLHVMNVASWLCITNAIVQIIPSVAGCWYSKLIRK", "text": "FUNCTION: Plays a role in cuticle biogenesis (PubMed:15454573, PubMed:23028364, PubMed:25480962). In complex with doxa-1 and the dual oxidase bli-3, promotes the generation of reactive oxygen species (ROS) and tyrosine cross-linking of collagen, thus stabilizing cuticular extracellular matrix (PubMed:23028364). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
+{"protein": "MKTCNLTDRMEVKMIMLLFQILAISTLKSDSADIPEGYIQENVALRGRATQSAQLRGDHSGIAHASNAIDGNRDSVFYHGSCTHTEADKPWWRVDLLQVYTITSVTITNRGDCCEERISGARILIGKHLENNGINNPQCSVIGPMAAGETKTFRCPQPMIGRYVTVYLPKAESLHLCEVEVNVLFPAPC", "text": "FUNCTION: Acts as a defensive agent. Recognizes blood group fucosylated oligosaccharides including A, B, H and Lewis B-type antigens. Does not recognize Lewis A antigen and has low affinity for monovalent haptens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the fucolectin family."}
+{"protein": "MPGETEEPRSPEQQDQEGGPAAAADAASEELRPGAAAAPAAPAETASSRVLRGGRDRGRTAAAAAAAAAAVSRRRKAEYPRRRRSSPSNRPPDGPGHQPAAAKPPSPAQGKKSPRLQCIEKLTTDKDPKEEKEDDSVLPQEVSITTTRASRSWRSSSRTSISRLRDSENTRSSRSKTGSLQLVCKTEPITDQLDYDVPEEHQSPGGISSDEEEEEEEEMLISEEEIPFKDDPRDETYKPHLERETPKPRRKSGKVKEEKEKKEIKVEVEVEVKEEENEIREDEEPPRKRGRRRKDDKSPRLPKRRKKPPIQYVRCEMEGCGTVLAHPRYLQHHIKYQHLLKKKYVCPHPSCGRLFRLQKQLLRHAKHHTDQRDYICEYCARAFKSSHNLAVHRMIHTGEKPLQCEICGFTCRQKASLNWHMKKHDADSFYQFSCNICGKKFEKKDSVVAHKAKSHPEVLIAEALAANAGALITSTDILGTNPEPLTQPADGQGLPLLPEPLGNSTAGECLLLEAEGMSKSYCSGTERVSLMADGKIFVGSGSSGGTEGLVMNSDILGATTEVLIEDTDSTGP", "text": "FUNCTION: Atypical E3 ubiquitin-protein ligase that mediates 'Lys-63'- linked ubiquitination of MAP3K14/NIK, leading to stabilize and activate MAP3K14/NIK. It thereby acts as an activator of the non-canonical NF- kappa-B2/NFKB2 pathway. May also play an important role in cell proliferation and/or anti-apoptosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MLQAASALRHAKRILVITGAGLSADSGLPTYRGVGGLYNGETEDGLPIEMALSGPMLRRDPELCWKYIAELGKACLGGEPNVAHYAIAQLQRIKPECWVLTQNVDGYHRAAGSPPERLIEIHGQLSPLFCQSCAAQDPQLSEHLQRPLPPLCRLCGGILRPPVVLFQEMLPERALETLYEQLATGYDAVLSIGTTASFPYIHEPVIRTRVSGGFTAEINPQPTDHSAQMDVFLQCRAAHVMAELISHI", "text": "FUNCTION: NAD-dependent protein deacetylase which modulates the activities of several proteins which are inactive in their acetylated form. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sirtuin family. Class III subfamily."}
+{"protein": "MTQQPQEDFERSVEDAQAWMKVIQEQLQVNDNTKGPRAALEARLRETEKICQLESEGMVKVELVLRAAEALLATCQEGQKPEILARLRDIKSQWEETVTYMTHCHSRIEWVWLHWSEYLLAQDEFYRWFQKMVVALEPPVELQLGLKEKQWQLSHAQVLLHNVDNQAVLLDRLLEEAGSLFSRIGDPSVDEDAQKRMKAEYDAVKARAQRRVDLLAQVAQDHEQYREDVNEFQLWLKAVVEKVHSCLGRNCKLATELRLSTLQDIAKDFPRGEESLKRLEEQAVGVIQNTSPLGAEKISGELEEMRGVLEKLRVLWKEEEGRLRGLLQSRGDCEQQIQQLEAELGDFKKSLQRLAQEGLEPTVKTATEDELVAQWRLFSGTRAALASEEPRVDRLQTQLKKLVTFPDLQSLSDSVVATIQEYQSMKGKNTRLHNATRAELWQRFQRPLNDLQLWKALAQRLLDITASLPDLASIHTFLPQIEAALTESSRLKEQLAMLQLKTDLLGSIFGQERAATLLEQVTSSVRDRDLLHNSLLQRKSKLQSLLVQHKDFGVAFDPLNRKLLDLQARIQAEKGLPRDLPGKQVQLLRLQGLQEEGLDLGTQIEAVRPLAHGNSKHQQKVDQISCDQQALQRSLEDLVDRCQQNVREHCTFSHRLSELQLWITMATQTLESHQGDVRLWDAESQEAGLETLLSEIPEKEVQVSLLQALGQLVMKKSSPEGATMVQEELRKLMESWQALRLLEENMLSLMRNQQLQRTEVDTGKKQVFTNNIPKAGFLINPQDPIPRRQHGANPLEGHDLPEDHPQLLRDFEQWLQAENSKLRRIITMRVATAKDLRTREVKLQELEARIPEGQHLFENLLRLRPARDPSNELEDLRYRWMLYKSKLKDSGHLLTESSPGELTAFQKSRRQKRWSPCSLLQKACRVALPLQLLLLLFLLLLFLLPAGEEERSCALANNFARSFALMLRYNGPPPT", "text": "FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells (By similarity). SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass type IV membrane protein. Nucleus envelope. Rough endoplasmic reticulum. SIMILARITY: Belongs to the nesprin family."}
+{"protein": "DCQPCGHNVCC", "text": "FUNCTION: Causes reversible depression symptom in mice when injected intracranially. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MPSAISRGLLLLAGLCYLVFGIMAEDIQVAQVPSQHMPSHKVPRSLAHFAHSMHRVLTQQSNTSNIFFSPVSIATALAMVSLGAKGDTHTQILRSLEFNLTEIAEADIHDGFQNLLHTLNRPHSEHQLTTGNGLFLDQNLKLKEKFSGDVKTLYHAEAFPTNFSNPKEAEKQINAYVEKGTQGKIVDLVKDLGADTVLALVNYIFFRGKWEKPFDVKHTTQEDFHVDANTTVKVPMMKQQGMHKAFHCSTIQSWVLLLDYEGNVTALFLLPDEGKMQHLEETLTPELVFKFLRKTETMPAYVSLPKLSISGTYDLKEVLRDLGITNVFSGAADLSGITEDMPLKISKGLHKALLTIDEEGTEAAAATVLEATRTARPPRLSFNKPFFFLIIDHSTDTPLFVGKVMDPTKK", "text": "FUNCTION: Contrapsin inhibits trypsin-like proteases. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the serpin family."}
+{"protein": "METRGPGLAVRAESRRLVGIGPRAPPGRVGLQPSGRLDRRGGAGTMGYKDNDGEEEEREGGAAGPRGSRLPPITGGASELAKRKVKKKKRKKKTKGSGKGDDKHQSQSLKSQPLSSSFHDILSPCKERGPKPEHRQSKVEKKHLPSDSSTVSLPDFAEIENLANRINESLRWDGILADPEAEKERIRIYKLNRRKRYRCLALKGFHPDPEALKGFHPDPDALKGFHPDPEALKGFHPDPEALKGFHPDPEALKGFHPDPEALKGIHPDPEALKGIHPDPEALKGFHPDPEALKGFHPDPEALKGFHTDPEALKGFHIDPEALKGFHPDPKALKGFHPDPKALKGFHTDPEALKGFHPDPKALKGFHPDPEALKGFHPDPEALKGFHPDPEALKGFHTDPNAEEAPENLPYLSDKDGSSSHRQPTSKAECPNLCFEGNLTPKLLHSDLAPTLLE", "text": "FUNCTION: Participates in nucleolar liquid-liquid phase separation (LLPS) through its N-terminal intrinsically disordered region (IDR). May be involved in ATE1-mediated N-terminal arginylation. SUBCELLULAR LOCATION: Nucleus, nucleolus Cytoplasm Note=Shuttles between the cytoplasm and nucleoplasm, a significant portion localizes to the nucleolus."}
+{"protein": "MSTVTFENIFHGDSADLGKLRFNPVGFGWKAYQSEDNNPTTYNGSDIRHATWFRVARHFQLRLGMRNSEKPRISFDGFKRDDLDKIKRTLQEYFNITLETRDTSLKGWNWGEAQVKGSDLVFQVQGKTAFDVPLSQVANSNIAGKYEVALEFNPPSNYKFDPKDLNKRPPDEMVEMRFYIPGKSMKKAGSDAGSGGEETELDEEGNEVSAADAFHSLIKEKADIGAVVGDSIVVFEDCLILTPRGRFSIEVYADSIRLVGKSTDHRVPFTSIHRIFLLPKLDDLHVQLVLGLDPPIRQGATRYPFLVAQWPKDEVVNAELNLTDEELAQYPDLEKTYEATTFQVVSRVLKALTGKKVTPPGSLRNAQGLNGIRANVKAVQGELYFLEKGLIFISKQPILIDFSKTDSISFSRVGGGVASARTFDMRVVSKTGGADHVFSAINKQEVGPISSFLQSKNIRLKNEMEEAIVDIDEPFSDDDEEMESPSEDERPSKAKNDKSKTKPVKKAADDDEDESDDEDFEDESSDGGSPSESDSDDDSGMASDASDPMMEELRKKTQAKRTKAKETSGSGSEDEKPKKKKAKKDDDE", "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. SIMILARITY: Belongs to the SSRP1 family."}
+{"protein": "MTHCCSPCCQPTCCRTTCCRTTCWKPTTVTTCSSTPCCQPSCCVPSCCQPCCHPTCCQNTCCRTTCCQPTCVASCCQPSCCSTPCCQPTCCGSSCCGQTSCGSSCCQPICGSSCCQPCCHPTCYQTICFRTTCCQPTCCQPTCCRNTSCQPTCCGSSCCQPCCHPTCCQTICRSTCCQPSCVTRCCSTPCCQPTCGGSSCCSQTCNESSYCLPCCRPTCCQTTCYRTTCCRPSCCCSPCCVSSCCQPSCC", "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 (By similarity). SIMILARITY: Belongs to the KRTAP type 9 family."}
+{"protein": "MTTTTIEAPAIAGFHLSPEKVLGQVEPYSPGATDAASTLLQQNHEKWHMYFRDVAGHNHIPHAILTALPPMEAPTVGKMRDPAVFRQHMQRLDQYSNFLAFFEQELEQPGSSKEAVVSRYCFSRTPLADFMLAQLFEGLYHPIIHLGFGIEFHLPGLVAEGLAQAASHDPMKIDVFFQAAEALAGTGSLASKPLVELYRQVRASDTLRTAARLSDGPWKVRDGVLGRAFDEIVNVAAQFQVSSNEHDVQRATVEMMSCAAWACGGPHRPGKERKIDFFLMHCVTSSIFFTVLGRATWISIADKARLVEWKARLDLVWYAACAAPELRDENFLNYEPTLSRGMDWRQLYHALNRYHDDGHVAKFVRALKNAEEVALPFEQEHADILPVKGDAWFRIAQICYDSTASHTEAQKKWVWGVGFAPMWDLVPDFVTSS", "text": "FUNCTION: Baeyer-Villiger 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 AflY oxidoreductase family."}
+{"protein": "MTKGGLGIAAMSYVVIDYMRYVSPVWHSRLMPVLWSVLAIAVVTRVLFYKHWSKELRAAIPFLGSIVFLLCALLFEALCVRSVTAVLGLDWHRETPPLPDTGQWFLLALNESLPGTLVEILRAHIIGLHHFLMLFIMLGFSVVFDSVKAPGLGLGARYIFTMGVGRLLRAITFVSTILPSARPWCASARFNNVPSQPHRWAQKYYVPYANDPAAIRKLLHWDAAYADPGSYIGDYRADWGSMSFLSEFLRPSYSEGSSWFALLKKAGGGCNDLMYSGHMLVAVLTAMAWTEAYGGFSSAMIWLFVAHSAQREIRERHHYTVDCIVAIYVGILLWKMTGFIWSAERKTKQTKLEKIQNSLIHAAKDGDIETVRRLVEEIEVSSRVEKQSKVISNRTMTVFACATVITTLTIVILALTLTSDG", "text": "FUNCTION: Catalyzes the biosynthesis of sphingolipids with very long- chain fatty acid (VLCFA) (PubMed:31182845). Required for the formation of plasmodesmal cytoplasmic sleeve during the transition from type I to type II plasmodesmata to modulate post-sieve elements (SE) unloading and symplastic cell-to-cell molecular trafficking at the phloem pole pericycle (PPP)-endodermis interface in roots (PubMed:31182845). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sphingomyelin synthase family."}
+{"protein": "MELNSSSRVDSEFRYTLFPIVYSIIFVLGIIANGYVLWVFARLYPSKKLNEIKIFMVNLTVADLLFLITLPLWIVYYSNQGNWFLPKFLCNLAGCLFFINTYCSVAFLGVITYNRFQAVKYPIKTAQATTRKRGIALSLVIWVAIVAAASYFLVMDSTNVVSNKAGSGNITRCFEHYEKGSKPVLIIHICIVLGFFIVFLLILFCNLVIIHTLLRQPVKQQRNAEVRRRALWMVCTVLAVFVICFVPHHMVQLPWTLAELGMWPSSNHQAINDAHQVTLCLLSTNCVLDPVIYCFLTKKFRKHLSEKLNIMRSSQKCSRVTTDTGTEMAIPINHTPVNPIKN", "text": "FUNCTION: Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth-muscle contractile and hypotensive activity. Seems to mediate its action 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": "MDRAQKQESIESLKSVFADAGAVVVTHYMGLTVAEMTDLRLRLRKEGAAIKVVKNTLALKALDGKLGDKGDKLFTGPVAIAYGPDAVSAAKIAVQFAKENDKLKIVGGVLDQTNVLDEAGVRALATLPSLDELRGKLIGLIQAPATKIAGVLQAPAAQLARVFNAYATKDAA", "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. SIMILARITY: Belongs to the universal ribosomal protein uL10 family. SIMILARITY: Belongs to the universal ribosomal protein uL10 family."}
+{"protein": "MRSRLWLGLAWLLLARAPGAPGGYPHLEGDVRWRRLFSSTHFFLRVDLGGRVQGTRWRHGQDSIVEIRSVRVGTVVIKAVYSGFYVAMNRRGRLYGSRVYSVDCRFRERIEENGYNTYASRRWRHRGRPMFLALDSQGIPRQGRRTRRHQLSTHFLPVLVSS", "text": "FUNCTION: Plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis. Can stimulate cell proliferation (in vitro). May be involved in hair development. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the heparin-binding growth factors family."}
+{"protein": "MLRIGYRGFSTRSRVFKLSPQEYVNQVQQEKIENEQFKQALSQDQLEYNPKILSSHKLTKNRPIPINVELLKYKPLRLPKTHGDEVATLTIRGYDEDNLIRVGEFALRTAYYMGIPMSPLMALKTEKRLYTVIKSPFAQAKTKQNFHRVTYKKKLVAYDANPEIIDLWLSYINKNKFTDVEYKATVSSYESLNYHEELKSLKEFNLPDAYEGIEDPVAKKVQELLKSKSFKKHL", "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 uS10 family."}
+{"protein": "MSTLYDVVIVGGGLTGLNAAYQFKKAGLNVMVLKPKDRFGGRTESIKVEDYWFDLGGQWMGGTHKYLKELCDELGVKSFPQYDEGKHVLEINGKKVYYQGNISNLNKSYNLEGLFESISKIDELSAELNPDKPYAHSKSKEYDQLTVAQWVEKNVKGNDARSIIDWFCRVCVAAEPTEVSFLFFLHFIRTAGNYGLLADIHGGAQQDRLIGGSQQISEGLAKKIGEKHYTLNAPVRSIIQDANQCTIKTDNGSTYRSKYIVVAIPPTLAGRIHYSPSMPPRRDELTQRMPMGSVIKTITIYDEPFWRKEGYSAEAISDKGPIFICYDDSSHDDKKTAIVGFIAASAAKDWAEKSPEERKRAVLDCYARWWGPKALSPRIFLEKSWKEEEYSRGCYLGYTSPGTLYQCGEHLRAPVGRIHWAGTETASVWIGYMEGALESGFRVSKEIKDKLLNSKL", "text": "SIMILARITY: Belongs to the flavin monoamine oxidase family."}
+{"protein": "MPSVRSVTCCCLLWMMFSVQLVTPGSPATAQLSGQRTARGPGSAICNMACRLEHGHLYPFCHCRGKRD", "text": "FUNCTION: Highly inhibits both nicotinic acetylcholine receptors (neuronal (alpha-3/beta-4) and muscular (alpha-1/beta-1/epsilon/delta) subtypes) and the voltage-gated potassium channel Kv1.6/KCNA6 subtype. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin J superfamily."}
+{"protein": "MEIVNKQSFQDVLEYVRMYRLKNRIKRDMEDNNRKIRDNQKRILLLDNLNQYIRDDMTIAEVRGIIESMRDDYESRVDDYTIRNAELSKQRREASTKMKEQKKAHAELLKNAEK", "text": "SIMILARITY: Belongs to the UPF0265 family. SIMILARITY: Belongs to the UPF0265 family."}
+{"protein": "MALSVETESHIYRALRTASGAAAHLVALGFTIFVAVLARPGSSLFSWHPVLMSLAFSFLMTEALLMFSPESSLLRSLSRKVRARCHWVLQLLALLCALLGLGLVILHKEQLGKAHLTTRHGQAGLLAVLWAGLQCSGGMGLLYPKLLPRWPLAKLKLYHATSGLVGYLLGSASLLLGMFSLWFTATVTGGAWYLAVLCPILTSLVIMNQVSNAYLYRKRIQP", "text": "FUNCTION: Transmembrane reductase that may use ascorbate as an electron donor in the cytoplasm and transfer electrons across endoplasmic reticulum membranes to reduce monodehydro-L-ascorbate radical and iron cations Fe(3+) in the lumen of that compartment. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein."}
+{"protein": "MALVPTPVVNEGPMFAEVDMGDNSSTPTVRATVVQASTIFYDTPATLDKAERLLAEAASYGAQLVVFPEAFIGGYPRGSTFGVSIGNRTAKGKEEFRKYHASAIDVPGPEVDRLAAMAGKYKVYLVMGVIERDGYTLYCTVLFFDSQGHYLGKHRKIMPTALERIIWGFGDGSTIPVYDTPLGKIGAAICWENRMPLLRTAMYAKGIEIYCAPTADSRDVWQASMTHIALEGGCFVLSANQFCRRKDYPPPPEYVFSGTEDLTPDSIVCAGGSVIISPSGAVLAGPNYEGEALISADLDLGEIARAKFDFDVVGHYARPEVLSLIVRDHAVSPVSFTSTSSKAESSPK", "text": "FUNCTION: Highly specific for beta-cyano-L-alanine (Ala(CN)). Low activity with 3-phenylpropionitrile (PPN). Not associated with auxin production but may be involved in cyanide detoxification. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family."}
+{"protein": "MSRSQEELEATLQIAKVNPEDLRSTVHCLSFSSEFTSGDYSLMELDDTLCKQIEAGDSLVIRGDKSDHAVLCSQDKTYDLKIADTSNLLLFIPGCKLPDQLPADQQPLSVIHCEIAGFSNHYWELRRCRPKLKKLKKLLMENTYNGPENESESSQETSLYTTEDLLSVIQSSTEELMDHLKAIHACNIKGIWRLLDFDYEMKLLNHITQLIDSESWSFSKVPLQVCLQELRSLEPEEMIEHCLTCYGKRLMEEGGDCFALDEDKICRATALMLLQNAVKFNLAEFQEVWQQSVPDGMNTRLDQLKGLALVDRTSRPETIFLLQTEDLPEDTQERFNTLFGMREKWTEADIAPYIQDLCGEKQTIGALLTKYARSSMQNGIKLFNSRRPLS", "text": "FUNCTION: Loads pcna onto primed templates regulating velocity, spacing and restart activity of replication forks. May couple DNA replication to sister chromatid cohesion (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DCC1 family."}
+{"protein": "MATAPLAFRLPFPFSFPSASRPPPSRILAPPTPRRLPLRLAAAAARRFRPPTADDEPPEAAEDSSHGLTRYDQLARSVERARIRQPEITPDNPLFSSPSTAGGGGGGSYDPDDEFFDEIDRAIAEKREEFTRRGLIKPSPASPPPSQSQPEDEDLTDELSPEEVIDLDEIRKLQGLSVVSVADEEDEEVEGGEDEDDGLPLDEDGEGFDVAEELGLEGARMRQPAFRMTLAELLDESKLVPVAVTGDQDVALAGVQRDASLVAAGDLFVCVGEDGLAGLTEADKRGAVAVVADQDLNIEGTLACRALVIVDDILTALRVLPACLYSRPSMNMAIIGVTGTDGVTTTTHLVKAMYEAMGVRTGLVGVLGTYAFSSNKLDARPDASSDPIAAQKLMATMLHNGTEAVVLEKGTDGMPPSGVDSEIDYDIAVLTNVRHTDEENGMTYEEYMSRMASLFSRMVDPERHRKVVNIDDPSAPFFAAQGGHDVPVVTYSFENKKADVHTLKYQLSLFETEVLVQTPHGILEISSGLLGRDNIYSILATVAVGIAVGAPLEDIVRGIEEVDAIPGRCELIDEEQAFGVIVDHARTPEALSRLLDGVRELGPRRIVTVVGCCGEKERGKRPVMTKIAADKSDVVMLTSDNPANEDPLDILDDMLAGVGWTMEEYLKYGANDYYPPLPNGHRLFLHDIRRVAVRAAVAMGEQGDVVVITGKGNDTYQIEGDKNEFFDDREECREALQYVDQLHRAGIDTSEFPWRLPESH", "text": "FUNCTION: Required for the activity of the plastid-encoded RNA polymerase (PEP) and full expression of genes transcribed by PEP (PubMed:24246379). Required for the proper build-up and formation of the PEP-complex (PubMed:25599833). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the MurCDEF family. MurE subfamily."}
+{"protein": "MIAFIVLLSLAAVLQQSSGTVDFASESSNKKDYQKEIVDKHNALRRSVKPTARNMLRMKWNSRAAQNAKRWADRCTFAHSPPHTRTVGKLRCGENIFMSSQPFAWSGVVQAWYDEVKKFVYGIGAKPPGSVIGHYTQVVWYKSHLLGCASAKCSSTKYLYVCQYCPAGNIRGSIATPYKSGPPCADCPSACVNGLCTNPCKHEDDFSNCKALAKNSKCQTAWIKSKCPATCFCHNKII", "text": "FUNCTION: Blocks olfactory (CNGA2) and retinal (CNGA1) CNG channel currents. Does not affect neither depolarization- nor caffeine-induced contraction of smooth muscle (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
+{"protein": "MESDIEILSEADASMRKLRIFGIDDREDENGRRRIKDVEVYVPIVCGSIAFYLGKKATEYRTHKWTVYVRGATNEDLGVVIKRVIFHLHPSFNNPTRVVDAPPFALSECGWGEFKIDITVFFHTDVCEKKLELSHVLKLNPENAYGPIPKSIKIPVVAESYNEVVFPDPFESFVARVHNHPAIQISNIPDGLNLPPPGVADTYYLMEKGDTKEHPLSPWFLKFSEVEELFKLTAARQKVQADIAKLKRQLIMVDGQPEGLESSSGYEC", "text": "FUNCTION: Negative regulator of flowering controlling the H4K5 acetylation levels in the FLC and FT chromatin. Positively regulates FLC expression. Component of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. 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 a NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the YAF9 family."}
+{"protein": "MGACRIQYVLLIFLLIASRWTLVQNTYCQVSQTLSLEDDPGRTFNWTSKAEQCNPGELCQETVLLIKADGTRTVVLASKSCVSQGGEAVTFIQYTAPPGLVAISYSNYCNDSLCNNKDSLASVWRVPETTATSNMSGTRHCPTCVALGSCSSAPSMPCANGTTQCYQGRLEFSGGGMDATVQVKGCTTTIGCRLMAMIDSVGPMTVKETCSYQSFLQPRKAEIGASQMPTSLWVLELLFPLLLLPLTHFP", "text": "FUNCTION: Plays a role in fertilization by controlling binding of sperm to zona pellucida and migration of spermatozoa into the oviduct probably through molecule adhesion ADAM3 (PubMed:23633567, PubMed:23969891). May play a role in signal transduction and promote protein tyrosine phosphorylation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid- anchor, GPI-anchor Membrane raft Cytoplasmic vesicle, secretory vesicle, acrosome Secreted Cytoplasmic vesicle Note=Located on plasma membrane of spermatocytes, round and elongated spermatids, and testicular spermatozoa."}
+{"protein": "MSSGGLLLLLGLLTLWEVLTPVSSKDRPDFCELPADTGPCRVRFPSFYYNPDEKKCLEFIYGGCEGNANNFITKEECESTCAA", "text": "FUNCTION: Strongly inhibits plasmin (Ki=0.44 nM) and trypsin (Ki=0.42 nM). Has little effect on plasma (Ki=1870 nM) and tissue (Ki=12900 nM) kallikreins. In vivo, reduces bleeding in a small animal model. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family."}
+{"protein": "MLTTTILILLIVILMVSLHLYYRWYLLRSSPFNRTTAASTFFTDPSSTPGGLNPSIIKSLPIFTFSAVTALFAMECSVCLSEFKDNESGRVMPNCKHTFHVHCIDMWFHSHSSCPLCRSQIEPFAGGVKSSMDEVAISISDPVYGDTNHHEGTETTGDSVPEDSQRKPAAIEISQRNLGEIENDLSRSHSFRSPTDEPDDIFHSEFESRSGEVLLLLLLLSEFLIFCFRRSVACK", "text": "FUNCTION: May be involved in the early steps of the plant defense signaling pathway. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily."}
+{"protein": "MSELVMDSAFFGHVLQDMGALIEKERDYLTGLDSDIGDGDHGINLSIGFREVNKQLDELLTVSPDIATLLKKSGMILLGKVGGASGPLYGSFFMKCGADVPGKTEVNFDELCGMIINGAAAVQHRGKAELGDKTMMDAFLPGVEVLQNRDTNADPIETFSAFVDAMHAGAQSTIPLIAKKGRALRLGERAIGHLDPGSESSWMLMNVILENLKKAV", "text": "FUNCTION: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MRHRILTLLLGLAVLVTAGCGFHLRGTTQVPAELKKLQITSSDPYGPLARSVRQQLRLNNVTILEDGSADVPVLKLIDSSENKDTVSVFQDGKAAERQLTLNVNAQVIMPDGSVYPLRSRVDRSFFDNPLEALAKDAENEIINQEMREQAARRLVRQLLTVHNAEKQKAREKQVGQQAAQAQ", "text": "FUNCTION: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the LptE lipoprotein family."}
+{"protein": "MVILSLVSCSFSVFSPPISLRLHLPPVTSLCSHGTFPASSTFRSQLQPLLISCLNHREPALTFRCSCLSSPIESGSQIESLFSLFRDIGFIEEETEMILAKNPDIKSTSLDKIGARVASLQSLKINGFPLQGLIAKCPNLLTSEEFDLVISFLVDELEGRLDPELVERLLSVVDTSILLSFNQKVRLLLLHGIPKEKISHVLNKVYLNKLLYQKSVEDIERLISFLEPFGGIGIIARRPVILNSDLDSQLIPRVDFIRNLSGEDDFATGTVLRRLPAILSYSVEHMNGQVEFLKSFAGLTSEQVFKIVHVFPNVISTSKERKLRPRIEFLKECGFDSPGMFKFLSKAPLILALSENNLSHKLGFLVKIGYKHRTKELAFAMGAVTRTSSDNMQRVIGLYLSYGLSFEDILAMSTKHPQVLQYNYTSLEEKLEYLIEYMGREVEELLAFPAFLGYKLDSRIKHRYEEKLKSRGENMSLNKLLTVSAERFSKAADNIEMICL", "text": "FUNCTION: Transcription termination factor that is transcriptionally active in chloroplasts. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the mTERF family."}
+{"protein": "MVDDKEKNMKCLTFFLMLPETVKNRSKKGSKKANSSGGGGGGGSVGSGSSKLPPVCYEIITLKTKKKKKMAADIFPRKKPANSSSTTVQQQHQHNLCNNNLIPAPNWQGLYPTIRERNAVMFNNDLMADVHFVVGPPGGTQRLPGHKYVLAVGSSVFHAMFYGELAEDKDEIRIPDVEPAAFLAMLKYIYCDEIDLAADTVLATLYAAKKYIVPHLARACVNFLETSLSAKNACVLLSQSCLFEEPDLTQRCWEVIDAQAELALKSEGFCDIDFQTLESILRRETLNAKEIVVFEAALNWAEVECQRQDLALSIENKRKVLGKALYLIRIPTMALDDFANGAAQSGVLTLNETNDIFLWYTASKKPELQFVSKARKGLVPQRCHRFQSCAYRSNQWRYRGRCDSIQFAVDKRVFIAGFGLYGSSCGSAEYSAKIELKRQGVVLGQNLSKYFSDGSSNTFPVWFEYPVQIEPDTFYTASVVLDGNELSYFGQEGMTEVQCGKVTVQFQCSSDSTNGTGVQGGQIPELIFYA", "text": "FUNCTION: Acts as a key regulator of dendritic field orientation during development of sensory cortex. Also directs dendrites toward active axon terminals when ectopically expressed. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=Translocates from the cytosol to the nucleus in response to neuronal activity."}
+{"protein": "QAIGLPHTACIQCNRKTSSKCLSGQICLPYHMTCYTLYKPDENGELK", "text": "FUNCTION: This toxin may inhibit nicotinic acetylcholine receptor (nAChR). It has poorly reversible postsynaptic blocking activity in a chick muscle preparation and readily reversible inhibitory activity at a presynaptic site in the rat vas deferens prostatic segment most likely to prevent the release of neurotransmitters. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral subfamily. Boigatoxin sub-subfamily."}
+{"protein": "MAEAAVASTVTLPVSGGWTKHVTCRYFMHGLCKEGDNCRYSHDLTNSKPAAMICKFFQKGNCVFGERCRFDHCKPTKNEEFSSPQMLPPSSPSPSTDPESSQPAPRPKTQDWANAAEFVPGQPYCGRAESVKVEISIPLIEELDCDAAVDKEALRKQLCPYAAVGECRYGINCAYLHGDVCDMCGLQVLHPTDNSQRSQHTKACIEAHEKDMEISFAIQRSKDMMCGVCMEVVFEKANPSERRFGILSNCNHCYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEDKEDKQKLIQKYKDGMGRKPCRYFDEGRGICPFGANCFYKHAFPDGRLEEAQPQRRQTGSSSRNRLSEMLLMLLAAGD", "text": "FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins."}
+{"protein": "MAKLLLLTLLGASLAFVGERLLAFRNSFGAVQELEPVEPQNCVLIEGLENGSEDIDILPSGLAFISSGLKYPGMPNFAPDEPGKIFLIDMNEKNPRAQELEISNGFEKESFNPHGISTFIDKDHTVYLYVVNHPHMKSTVEIFKFEEQQRSLVHLKTIKHELLKSVNNIVVLGPEQFYATRDHYFTNYVLALLEMFLDLHWTSVLFYSPKEVKVVAKGFSSANGITVSLDKKYVYVADATAKNVHVMEKHDNWDLTELKVIHLDTLVDNLSVDPATGDILAGCHPNGMKLLNYNPEDPPGSEVLRIQNVLSEKPRVSTVYTNDGSVLQGSTVASVYQGKILIGTIFHKTLYCVL", "text": "FUNCTION: Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters (By similarity). 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": "MTFNKRQVKINHWPEKNDKEKQKYSKNRETVKLTLLTLLLLCSICFLFLTLNFPFTIEFTASIPRTCDHNFTVYVYDLPKEFNIGLLQNCRHLNIYTNMCPHVANNGLGQPLHRGRTSWFSTHQFIAEMIFHARVENHPCRTYEPDTADIFYVPFYGGLYASSVFREQNLTKRDELAVRLVNYISGQRWWKRSNGRDHFLAIGRTAWDFMRSSDTDFGANMLMQMPRVMNMSVLTVERQPWNGDNHFGIPYPSYFHPYTSAEMVTWQDKMKNVERPNLFSFVGGPRKGLEKAAIRDELIKQCAESSHCELLKCENGGSRCHNPMTVLGVMARSRFCLQAPGDSFTRRSTFDAMLAGCIPVFFSPHTMYTQYMWYLPDDKRSYSVFMDEKNNTHIEQELLRISENEVVQMREIVIDLIPRLTYAHPNSTNYDLPDAVDIALEALAKQARDNVVVSL", "text": "FUNCTION: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 47 family."}
+{"protein": "MDRINTSAAPPTSPDWERLRADFPLLQRHVHGKPLIYFDNANTAQKPQAVITATDTFYRRHNANISRAVHTLGTEATEAYEATRAALATLLNVPMHELVLCSGTTFAINLIAYSWALPRLRTGDVILVSRMEHHANIVPWQLIAERTGARIQVADILPNGTLDLDALHTLMTPQVKLLAITHVSNVLGTVNPIHDICRQARQRGITTVVDGSQAAPHRHINIPAIGCDFYAITGHKLYGPTGTGALWARREHLHIMPPFLGGGEMIKEVSFDGTLFNTPPHKFEAGTPNIAGFIGLSAAVDYVRRIGIDQIETRETELLAHLTEELQKIDGMRLFGTAPNKAAVVSFMIEGTHAHDLATLLDLEGVAVRSGQHCAHPLLQYYGVTATCRASLAFYNTHEEIERFITALLKVRKLLG", "text": "FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily."}
+{"protein": "MAFKLPNLPYAYDALEPYIDQRTMEFHHDKHHNTYVTKLNATVEGTELEHQSLADMIANLDKVPEAMRMSVRNNGGGHFNHSLFWEILSPNSEEKGGVIDDIKAQWGTLDEFKNEFANKATTLFGSGWTWLVVNNGKLEIVTTPNQDNPLTEGKTPILLFDVWEHAYYLKYQNKRPDYMTAFWNIVNWKKVDELYQAAK", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal ion at the active site. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
+{"protein": "MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEVDGSLKSWRESCDSALRAYVKDHYSNGFCTVYAKNIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSVTVSNEAQTAKEFIKIIEHAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA", "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 (PubMed:36071160, PubMed:25814576, PubMed:29420470, PubMed:33734450). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the F-actin-capping protein alpha subunit family."}
+{"protein": "MHAIAPRLLLLFVLSGLPGTRGGSGVPGPINPPNSDVVFPGGSPVAQYCYAYPRLDDPGPLGSADAGRQDLPRRVVRHEPLGRSFLTGGLVLLAPPVRGFGAPNATYAARVTYYRLTRACRQPILLRQYGGCRGGEPPSPKTCGSYTYTYQGGGPPTRYALVNASLLVPIWDRAAETFEYQIELGGELHVGLLWVEVGGEGPGPTAPPQAARAEGGPCVPPVPAGRPWRSVPPVWYSAPNPGFRGLRFRERCLPPQTPAAPSDLPRVAFAPQSLLVGITGRTFIRMARPTEDVGVLPPHWAPGALDDGPYAPFPPRPRFRRALRTDPEGVDPDVRAPRTGRRLMALTEDTSSDSPTSAPEKTPLPVSATAMAPSVDPSAEPTAPATTTPPDEMATQAATVAVTPEETAVASPPATASVESSPLPAAAAATPGAGHTNTSSASAAKTPPTTPAPTTPPPTSTHATPRPTTPGPQTTPPGPATPGPVGASAAPTADSPLTASPPATAPGPSAANVSVAATTATPGTRGTARTPPTDPKTHPHGPADAPPGSPAPPPPEHRGGPEEFEGAGDGEPPEDDDSATGLAFRTPNPNKPPPARPGPIRPTLPPGILGPLAPNTPRPPAQAPAKDMPSGPTPQHIPLFWFLTASPALDILFIISTTIHTAAFVCLVALAAQLWRGRAGRRRYAHPSVRYVCLPPERD", "text": "FUNCTION: Chemokine-binding protein that inhibits neutrophils' chemotaxis. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein G family."}
+{"protein": "MDRGVLPQAIALLLAVCSFGPTAGLAEGVQCDLQPVDPKVTYTTSQVSEGCVAHVPNATVGVHILFLEFSKEVSTLELTVQMTNPNGARPQEVLLILSVNKNIHLTLQVPEIPLHLAYDSKLVFLQEAPKAVITELPPSTTKNQLFLWANTKGSIISAAELDNPQSILLRLDQAPTSPSRCTLEPRKDMGHTLEWKSHTQASVLGCHLEGVTGHKEAHILRVLPGSEAWPRTVTVEVELSCALRDPEAVLILQGPPYVSWLIDANHNVKAWTTGEYSFKIFPGSNIQGVNLPDTRQGLLEEARKLNASVIASFVELPLASVISLQDRSCGSGLQPSPTTVQITPPGEGCNQDLLLSLIQPRCSDDVMTLVLRKDLISTLGCTITSLTFWDPSCQAEDTDDKFVLRGTYSSCGMKVAENVVISNEVVVNLLSSSSPQRKQVQCINLDSLSFQLGLYLSPHFLQASNTIELGQQGFVQVSMSPSIPELMTQLDSCQLNLGPDVEMVDLIQNQEAKSSCVSLLSPSPGGDMRFSFLLRGYVVPMPTAGILSCTVALRPRTWSLDVHKTASTRLNIVSPGLPDKGLVLPAVLGITFGAFLIGALLTAALWYIHSHTRHPGKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA", "text": "FUNCTION: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. Required for normal structure and integrity of adult vasculature. Regulates the migration of vascular endothelial cells (By similarity). Required for normal extraembryonic angiogenesis and for embryonic heart development (By similarity). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (By similarity). May play a role in the binding of endothelial cells to integrins (By similarity). Acts as TGF- beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:8294451). Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "GIGAILKVLATGLPTLISWIKNKRKQ", "text": "FUNCTION: Main toxin of bee venom with strong hemolytic activity and antimicrobial activity. It has enhancing effects on bee venom phospholipase A2 activity. This amphipathic toxin binds to negatively charged membrane surface and forms pore by inserting into lipid bilayers inducing the leakage of ions and molecules and the enhancement of permeability that ultimately leads to cell lysis. It acts as a voltage-gated pore with higher selectivity for anions over cations. The ion conductance has been shown to be voltage-dependent. Self- association of melittin in membranes is promoted by high ionic strength, but not by the presence of negatively charged lipids. In vivo, intradermal injection into healthy human volunteers produce sharp pain sensation and an inflammatory response. It produces pain by activating primary nociceptor cells directly and indirectly due to its ability to activate plasma membrane phospholipase A2 and its pore- forming activity. SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Alpha-helical peptides form toroidal pores in the prey. SIMILARITY: Belongs to the melittin family."}
+{"protein": "MGLKLSGRYIFLVLAVHLAYLLQAVKATGKCDAVFKGLSDCMLTLGDKVANYPQDLEEKKNLDTICSYWDDFHVCTVTALADCQEGAADIWEKLKRQSKNLNIQGSLFELCPGSAGAPGQRLLFPAFLPLLMVFLSTLFILVLQ", "text": "FUNCTION: Modulates postsynaptic dendritic arbor elaboration and synaptic maturation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the neuritin family."}
+{"protein": "MASSEQAEQPNQPSSSPGSENVVPREPLIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDLAFQQSGTASDEPSPVGPATPVVPVQPPHLISQPYSPGGSRWRDYGALAIILAGIAFGFHQLYKKYLLPLILGGREDRKQLERMAASLSELSGSVAQTVTQVQTTLASVQELLRQQQQKVQELAHELAAAKATTSTNWILESQNINELKSEINSLKGLLLNRRQFPPSPSAPKIPSWQIPVKSPSPSSPAAVNHHSSSDISPVSNESPSSSPGKDGHSPEGSTATYRLLGPQEEGEGVVDVKGQVRMEVQGEEEKREDEEGEEDEDDDVSHVDEEDVLGVQREDRRGGDGQINEQVEKLRRPEGASNESERD", "text": "FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (PubMed:19122147). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 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. Plays a key role for peroxisome movement through a direct interaction with tubulin (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peroxin-14 family."}
+{"protein": "MEDDFLFMTLLYDFYGALLTDKQREIFEMYYLNDYSLGEISEILDISRQGVYDALKRAEDSLEFYEEKLGLVKKHQEMMKKIEKIKECIKLIKEREKDEEILKIIEDMARELEELNP", "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 (By similarity). SIMILARITY: Belongs to the UPF0122 family."}
+{"protein": "MCALDRRERPLNSQSVNKYILNVQNIYRNSPVPVCVRNKNRKILYANGAFIELFSREDKPLSGESYIRLQVEIFLSSLELECQALGHGSAFCRRFNFHGEIYQIRMENVSFYNDESVVLWQINPFPDYPFFALNQSGSNTNTSDKLTIWNDLSPGTLVVFSFYMLGVGHATIARELGITDRASEDRIKPVKRKIKEFFEHV", "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": "MASGLGDLSVGVSSLPMRELAWRRVADDSHDLWCCCMDWKAHVEYAHPASELRPGSGGWPEHAEAQWRQQVHAAHDVWCNCGDWQGHALRSRSRTAESGRSSSSSSVSVLSDGDQQPWWRRLRVKRPKFPSWARRWTQRHDSEERASQQAENDSTS", "text": "SIMILARITY: Belongs to the herpesviridae US1 family."}
+{"protein": "MSPPAGGAAAAADPASPVVLLAVQAAVRLLGAGHEDEAQLRKLQLKADPERPGRFRLGLLGIEPGAVSLEWPLESICYTIRGPNQHELQPPPGGPGTFSVHFLNSEEAQQWAALVRDATAEGQNGNDSTAPVPTPAMCPTSPPCSSVTPTPKATQPEMDLPQGSGNLKKEELATHLAQAIAGGDEKAAAQVAAILAQHHVALNVQLLEAWFPRGPIRLQVTVEDATSVLSSSSSAHVSLQIHPHCSIAALQEQVFSEFGFPPAVQRWVIGRCLCMPERSLASYGVSQDGDPAFLYLLSAPREVSGHSPQHSKMDRKLGCLFPQSLELPHNLQASSSSLPSPPQPGWSCPSCTFINASNRPGCEMCSTQRPCAWDPLTATST", "text": "FUNCTION: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. SUBCELLULAR LOCATION: Cytoplasm Synapse Note=Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1."}
+{"protein": "MSSDKTSQQTFKLAPNNSVAQSNSIDQNKNKNNILSTIETMDKSISEDLYPKLQNIVSTVNLSTKLDLKQIALRARNAEYNPKRFAAVIMRLRDPKTTALIFASGKMVCTGAKTEEDSNRAARKYAKIIQKIGFPVQFKDFKIQNIVGSTDVKFPINLDHLEQDHKKFVQYEPEIFPGKIYREFNTKIVLLIFVSGKIVLTGAKTRENINKAFQKIYWVLYNYQKKDYRGANLHNQNLNIKPSIKN", "text": "FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TBP family."}
+{"protein": "MANFIEKITYLGTPAIKAGNEHLEMIVVPEWGSNVISLVDKTTNVQLLREPETAESFHDTPTLYGIPILFPPNRISDGTFSFRGRTYHFDINEKDKHNHLHGFLYHEKWNVVTTKQTDEGVIVETEIDLSELPHVQKQFPHHAVVRMTYTIKENTLFKHATVMNKGKEAFPWGIGYHTTFIFPAESSLFSLTADQQWELDERLLPTGKLMDVPYKEALHEGMDLRHKQLDDVFLSSYQKRGGENQAVIYHQHAHISIIYKADEQFKHWVVYNADGKQGYLCPEPYTWVTNAVNLDLPSSLTGLQVLEPGEETTAKSSITIELNHQ", "text": "SIMILARITY: Belongs to the aldose epimerase family."}
+{"protein": "LSCGDVATQMASCINYLRGAGPLPAACCNGVKNLKNSATTTQDRRTACKCLISASKTISGVNFGLAAGLPAKCGVSIPYKISPSTNCDQVN", "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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant LTP family."}
+{"protein": "MDPEGFTSGLFRWNPTRVMVQAPTPIPPPQQQSPATPQTAAFGMRLGGLEGLFGPYGVRFYTAAKIAELGFTASTLVGMKDEELEDMMNSLSHIFRWELLVGERYGIKAAVRAERRRLQEEEEEESSRRRHLLLSAAGDSGTHLALDALSQEDDWTGLSQEPVQHQDQTDAAGINGGGRGGYWEAGQTTIKKQQQRRRKKRLYVSETDDDGNEGEDDDGMDIVNGSGVGMERQREHPFIVTEPGEVARGKKNGLDYLFHLYEQCREFLLQVQTIAKDRGEKCPTKVTNQVFRYAKKSGANYINKPKMRHYVHCYALHCLDEEASNALRSAFKVRGENVGSWRQACYKPLVDIACRHGWDIDAVFNAHPRLSIWYVPTKLRQLCHLERNNAEAAAATLVGGISCRDRLRLDALGFN", "text": "FUNCTION: Controls floral meristem identity. Is required very early in flower development and may act here as a transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FLO/LFY family."}
+{"protein": "MDSFNYTTPDYGHYDDKDTLDPNTPVDKTSNTLRVPDILALVIFAVVFLVGVLGNALVVWVTAFEVKRTINAIWFLNLAVADFLSCLALPILFTSIVQHHHWPFGGAACRILPSLILLNMYASILLLATISADRFLLVFKPIWCQNFRGAGLAWIACAVAWGLALLLTIPSFLYRVVREEYFPPKVLCGVDYSHDKQRERAVAVVRLVLGFLWPLLTLTICYTFILLRTWSRRATRSTKTLKVVVAVVASFFIFWLPYQVTGIMMSFLEPSSPTFLLLKKLDSLCVSFAYINCCINPIIYVVAGQGFQGRLRKSLPSLLRNVLTEESVVRESKSFTRSTVDTMAEKTQAV", "text": "FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasmic vesicle Note=Phosphorylated C5aR colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MCMPCFTTDPNMANKCRDCCGGGKKCFGPQCLCNR", "text": "FUNCTION: Toxin with unknown function in healthy organisms. On glioma cells, interacts with chloride channels (probably ClC-3/CLCN3) and MMP2 at the surface of glioma cells. This complex is then internalized via caveolae, 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": "MTVVIGVLALQGAFIEHVRHVEKCIVENRDFYEKKLSVMTVKDKNQLAQCDALIIPGGESTAMSLIAERTGFYDDLYAFVHNPSKVTWGTCAGLIYISQQLSNEAKLVKTLNLLKVKVKRNAFGRQAQSSTRICDFSNFIPHCNDFPATFIRAPVIEEVLDPEHVQVLYKLDGKDNGGQELIVAAKQKNNILATSFHPELAENDIRFHDWFIREFVLKNYSK", "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": "MNKLILISLIASLYQVEVDAHGYMTFPIARQRRCSAAGGNWYPVGGGGIQDPMCRAAYQNVFNKVLNSNGGDVIDASEAANYMYTQDNEYAALAGPDYTNICHIQQRVVPSYLCAAGASDWSIRPFGDKSGMDLPGSWTPTIIQLSDNQQSNVVMELEFCPTAVHDPSYYEVYITNPSFNVYTDNVVWANLDLIYNNTVTLRPKLPESTCAANSMVYRFEVSIPVRPSQFVLYVRWQRIDPVGEGFYNCVDMKFKYSEGPDEEDIIEPEYEVDNEAECFAYRTNSGNVNVNPLQENKYMAYANKAIRNINTHSNGCSRNRNNKNNYNKYYSKTYNYNQNRK", "text": "FUNCTION: This protein is a spindle body protein."}
+{"protein": "MIFKKALYILLFLYIAIVKKGESKPGSKHPFLFKNLVIDKKKLDSSYYNKYDNIKWNGKIIAIGDIHGDIESLKLILRHSKLIGENDNWIGDNVLLVQNGDVFDRGIYGPIIYNFLFKLQKEAIKKNSRVILIMGNHEQLNLCGYFNYVNPKEIEMFFHNDANYRYHSFVNPYGEYHKRLIRLPPMVKVNNIIFTHGGLNLLISKLSINDINLKTRLQIENNCKPIKYDSFQNYLSRDGVLWSDAMSRNVPYYEKEKCSELFQILDKYDAKYLVVGHTRQPSHQIGSYCNNHYFLIDTGMSLFTNYGQPYPNYLKIDDHKIKAVRLIVEKKKKCPHTEIQLNTPNKIKYCVQESQTNLNPVL", "text": "FUNCTION: Phosphatase which plays an essential role in the development and differentiation of the ookinete and in the formation of ookinete micronemes. SIMILARITY: Belongs to the metallophosphoesterase superfamily. SLP family."}
+{"protein": "MGRKWTYCVVYAIIQIQFFRGAWEELFNAGDNNVYALPGSDVNLTCQTMEKDLMVQMQWSKVTDEIDMIVVYHPQYGFHYMQGVACESRVAAVETLKDATKWTLNLRNISSSLSGKYECSFTMYPTGTKTIVYNLIVEPYTQDEHNRTIEIETNRTLEIPCFQNTSSEISPRFTFSWLVEKDGVEDVLFTYDYHVSNSTAFKGRVGLGADYGLRLSPVQIQDDGRTFSCFLRISPLKVWKTSTTVKVFAKPEILMTVENTTMDVLGERVFTCLLKNVFPKASITWLIDGRLFQGNEEGIYITNEEKNSSSGFWELKSVLTRMHNRTSQSNNMTVWCMALSPGPGNKMWNTSSQPITFSLDSGTAPTKRLPNVTGSTLGAQTFPDAEVSPTRYLATSSMTIVDENVLTPDPTPQTSNSSMTTKDVNYSQPSSGTDAKNSSRAASSSDGGSRPFPSTSPPKWLSLPHTSTGPQEPDSAVSWIPTDAYTSGSSDASLTSHDVIIRTTKEFPDVLTTANGTTKIKHGHVTGITVNKPRDGMSWPVAVATLLFFCILLFGLGVRKWCQYQKEIMERPPPFKPPPPPIKYMCIQEPTGRGMPCHEMEVL", "text": "FUNCTION: May be involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. Promotes NK cell-target adhesion by interacting with PVR present on target cells. May function at a time after T and NK cells have penetrated the endothelium using integrins and selectins, when they are actively engaging diseased cells and moving within areas of inflammation (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MANDKGSNWDSALGCSYLLTEAECESDKENEEPGAGVELSVESDRYDSQDEDFLDNASVFQGNHLEVFQALEKKAGEEQLLNLKRKVLGSSENSSGSEASETPAKRQKAGAKRRLFSENEANRVLTPLQVQGGEWRQGFNEDQAISHRLLQLVKSKNATVFKLGLFKSLFLCSFHDLTRLFKNDKTTNQQWVLAVFGIAEVFFEASLELLKKQCSFVQMQKRSHEGGTCAVYLLCFNTAKSRETVRNLMANMLNVREECLLMQPPKIRGLSAALFWFKSSLSPATLKHGALPEWIRAQTTLHDSLATEKFDFGTMVQWAYDHKYAEESKIAYEYALAAGSDSNARAFLATNSQAKHVKDCATMVRHYLRAETQALSMPAYIKTRCKLATGEGSWKSILTFFNYQNIELITFINALKLWLNGIPKKNCLAFIGPPKTGKSMLCNSLIHFLGGSVLSFANHKSHFWLASLADARAALVDDATHACWRYFDTYLRNALDGYPVSIDRKHKAAVQIKAPPLLVTSNIDVQAEERYLYLHSRVQTFRFEQPCTDESGEQPFTITDADWKSFFVRLWGRLDLVDEEEDSEEDGDSMRTFTCSARNTNAVD", "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. 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": "MDSAISEIINALAILADDKNIQLTIKEAGKGAAICAGAALIGGLLLGPRGLALGGAIGGLTAYGLTEGNFKSLSEVILNDLTESQRRELEQHVIRAISEVRNVRVRDVARLILNNRHVQEVALEAVKSYITDRMGMTIVD", "text": "FUNCTION: Antiviral effector protein expressed downstream of Sting and Rel (Relish) signaling in response to viral infection. SIMILARITY: Belongs to the C19orf12 family."}
+{"protein": "MEQLFVDDPAFASSMSSLEADIFSGAGQLPSSPWLDLDLDDDVQDLSMAPTTANAVSSGYGSGGSGSHRKLSHNAYERDRRKQLNELYSSLRALLPDADHTKKLSIPTTVSRVLKYIPELQKQVENLERKKKELTTTSTTNCKPGVLGSQLMSEGMAPIVSATCINDMEIMVQVSLLSNVAGSVLPLSKCIKVLENEGLHFISSSTSSGFGNRTFYSIHLQRSEGTINEECPAFCERLEKVVRNKAKL", "text": "FUNCTION: Transcription activator that binds to the DNA motif 5'- CACGTGG-3' in the promoter of iron (Fe) deficiency-inducible genes as well as of genes involved in iron homeostasis, thus contributing to basal tolerance to iron deficiency, iron uptake from soil and iron transport, particularly during seed maturation and germination. Promotes the accumulation of mugineic acid family phytosiderophores (MAs). Required for ethylene-mediated signaling during iron deficiency responses. Improves growth and yield, especially in calcareous soil with low iron availability. Promotes iron concentration in shoots and grain. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bHLH protein family."}
+{"protein": "MTTSFGAAINIAVADDPNPKLQIHNFSGLKSTSNSLLLSRRLHVFQSFSPSNPSSIVRAVSTPAKPAAVEPKRSKVEIFKEQSNFIRYPLNEEILNDAPNINEAATQLIKFHGSYMQYDRDERGGRSYSFMLRTKNPGGEVPNRLYLVMDDLADQFGIGTLRLTTRQTFQLHGVLKKNLKTVMSTIIKNMGSTLGACGDLNRNVLAPAAPFAKKDYMFAKQTADNIAALLTPQSGFYYDVWVDGEKVMTAEPPEVVKARNDNSHGTNFPDSPEPIYGTQFLPRKFKIAVTVPTDNSVDIFTNDIGVVVVSNEDGEPQGFNIYVGGGMGRTHRMETTFPRLAEPLGYVPKEDILYAVKAIVVTQRENGRRDDRRYSRLKYLLSSWGIEKFRSVTEQYYGKKFQPCRELPEWEFKSYLGWHEAGDGSLFCGLHVDNGRVKGAMKKALREVIEKYNLNVRLTPNQNIILCNIRQAWKRPITTVLAQGGLLQPRYVDPLNLTAMACPAFPLCPLAITEAERGIPDILKRVRAIFERVGLKYSESVVIRITGCPNGCARPYMAELGLVGDGPNSYQIWLGGTPNQTSLAKTFKDKLKVQDLEKVLEPLFFHWRRKRQSKESFGDFTNRMGFEKLGEFVEKWEGIPESSSRYNLKLFADRETYEAMDALASIQDKNAHQLAIEVVRNYVASQQNGKSMD", "text": "FUNCTION: DNA-binding protein that binds to both double-stranded and single-stranded DNA without significant sequence specificity to reversibly repress the transcriptional activity of chloroplast nucleoids by promoting DNA compaction and possibly regulate DNA replication. FUNCTION: Essential protein with sulfite reductase activity required in assimilatory sulfate reduction pathway during both primary and secondary metabolism and thus involved in development and growth. SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid Plastid, chloroplast stroma Plastid stroma. SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family."}
+{"protein": "MEDSDKENTLLLPNNKYRNQNFIRNQDEDENENENNDNLENDNNKRNYISINNYEPYKEIDNNNNKNNNNNNIINNNNKINFYNNLIPRIKSYFQEIKPFLKYCSFSFLFSFDPSEPYLVDYFTNVLGINQTIVYQEIYPYWTYSYFVFLLIFGILGEIIGYKVIIIIGMVAKILTIGVLLSTNNIIWMILEQITEGLSYSAYTVFLAYIYFSLDTSEYQKMACRVNAGYLVGIVSSGLLGQLLVEQRLPLVYLLSIACGTNILALILALGFSNYKIDQKFSLKEVISDLFGTFKNADIVRWYIWSGIAISIHQIVITYWQNLFLQVNDEQSWNGYISASAYFFASFFAIIPSKLGNKINNIQGIILVLFGLLGGGLLVLMGFGGSTVVSALSFIIYNCCFEFVSPIVNVQIAKKLSSRIGVLFSFNIMVALTIQVLVQSAVGKQFLNLDIKTQFYYYGACLFFLSFGFAILFGFLFLKKKINSNSNSNSNVDVLIVNHNTQNQNSEEKKKKKELYYNANIIDFENNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNVGIGGNDNFK", "text": "FUNCTION: Folate transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter (TC 2.A.48) family."}
+{"protein": "MVATGSLSGKNPASISELLDCGYRPESLLSDFDYWDYVVPEPNLNEVIFEESTCQNLVKMLENCLSKSKQTKLGCSKVLVPEKLTQRIAQDVLRLSSTEPCGLRGCVMHVNLEIENVCKKLDRIVCDSSVVPTFELTLVFKQENCSWSSFRDFFFSRGRFSSGFRRTLILSSGFRLVKKKLYSLIGATVIEGS", "text": "FUNCTION: Inhibits cell growth by regulating the TOR signaling pathway upstream of the TSC1-TSC2 complex and downstream of AKT1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DDIT4 family."}
+{"protein": "MFPVAPKPQDSSQPSDRLMTEKQQEEAEWESINVLLMMHGLKPLSLVKRTDLKDLIIFDKQSSQRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLSRACHQQNKIKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAYLCKRVPHTVLDRQLLCLIDYYESKIRKIHTQRQYKEDESQSEEENDYRNLDASPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLETRPTQHELRLYKQQVKKLEKALKKNVKLQELINHKKAEDTEKKDEPSKYNQQQALIDQRYFQVLCSINSIIHNPRAPVIIYKQTKGGVQNFNKDLVQDCGFEHLVPVIEMWADQLTSLKDLYKSLKTLSAELVPWLNLKKQDENEGIKVEDLLFIVDTMLEEVENKEKDSNMPHFQTLQAIVSHFQKLFDVPSLNGVYPRMNEVYTRLGEMNNAVRNLQELLELDSSSSLCVLVSTVGKLCRLINEDVNEQVMQVLGPEDLQSIIYKLEEHEEFFPAFQAFTNDLLEILEIDDLDAIVPAVKKLKVLSY", "text": "FUNCTION: Plays a role in the organization of both preexisting and nascent microtubules in interphase cells. During mitosis, required for the organization and orientation of the mitotic spindle. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localized at the center of the radial microtubule array in interphase and at the spindle poles during various stages of mitosis."}
+{"protein": "MLRNTHLVLPFILYLLFRLSHFLLEVPTVRMIELAACHQHLRLDHGPLNEAACKTPPVQEHVSLVVGWKMTFDSIPGLMSILYFGTLADKSGHRAILRLCCVGYLLAILWVLITCLFHQVFPVELVLLSSLFLFIGGGQLVFAAVITAFVADLFPPPSRTKFLFLLAAMPHMDKVASPALATKLMEQNLFLPSLVSMAIVVICVALLQMSDVGRETAASKVVGSTSDQTEPFLRSSSNSSQESGTAAPAIDPEQARGPFRQLKNIICWVHREPVLFICYLCFFLKSNAMASEAFIFQYLSEKFGWPLRETTVMRLALSSGAVISTLIICPLANATLHNRGVASARINIGAVHASSIVLVASFIMAWQASSSTAFIFSMLAAGFGEGLEPALQGVLAAASQTKAKGSIFALMCTCSLLGDMTGGPLMSALMSIGRGGNGVSDGYCFLASALVFGAVIVLAHLLWALGAEEMLGED", "text": "FUNCTION: MFS transporter; part of the satratoxin SC3 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). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MDNLLPQSRFSYFKKYPIHAIRKYLSMLRNQKEEEQVARFQKIPNAENETMIPVLTSKKASELPVSEVASILQADLQNGLNKCEVSHRRAFHGWNEFDISEDEPLWKKYISQFKNPLIMLLLASAVISVLMHQFDDAVSITVAILIVVTVAFVQEYRSEKSLEELSKLMPPECHCVREGKLEHTLARDLVPGDTVCLSVGDRVPADLRLFEAVDLSVDESSLTGETTPCSKVTAPQPAATNGDLASRSNIAFMGTLVRCGKAKGIVIGTGENSEFGEVFKMMQAEEAPKTPLQKSMDLLGKQLSFYSFGIIGIIMLVGWLLGKDILEMFTISVSLAVAAIPEGLPIVVTVTLALGVMRMVKKRAIVKKLPIVETLGCCNVICSDKTGTLTKNEMTVTHIFTSDGLRAEVTGVGYNPFGEVIVDGDVVHGFYNPSVSRIVEAGCVCNDAVIRNNTLMGKPTEGALIALAMKMGLDGLQQDYIRKAEYPFSSEQKWMAVKCVHRTQQDRPEICFMKGAYEQVIKYCTTYHSKGQTLTLTQQQRDLYQQEKAQMGSAGLRVLALASGPELGQLTFLGLVGIIDPPRTGVKEAVTTLIASGVSIKMITGDSQETAVAIASRLGLYSKTSQSVSGEEIDAMDVQQLSQIVPKVAVFYRASPRHKMKIIKSLQKNGSVVAMTGDGVNDAVALKAADIGVAMGQTGTDVCKEAADMILVDDDFQTIMSAIEEGKGIYNNIKNFVRFQLSTSIAALTLISLATLMNFPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRKPPRNWKDSILTKNLILKILVSSIIIVCGTLFVFWRELRDNVITPRDTTMTFTCFVFFDMFNALSSRSQTKSVFEIGLCSNKMFCYAVLGSIMGQLLVIYFPPLQKVFQTESLSILDLLFLLGLTSSVCIVAEIIKKVERSREKIQKPVSSTSSSFLEV", "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 (By similarity). 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 (By similarity). Plays a primary role in the maintenance of Ca(2+) homeostasis in the trans-Golgi compartment with a functional impact on Golgi and post-Golgi protein sorting as well as a structural impact on cisternae morphology. Responsible for loading the Golgi stores with Ca(2+) ions in keratinocytes, contributing to keratinocyte differentiation and epidermis integrity (By similarity). Participates in Ca(2+) and Mn(2+) ions uptake into the Golgi store of hippocampal neurons and regulates protein trafficking required for neural polarity (By similarity). May also play a role in the maintenance of Ca(2+) and Mn(2+) homeostasis and signaling in the cytosol while preventing cytotoxicity (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein Note=During neuron differentiation, shifts from juxtanuclear Golgi position to multiple Golgi structures distributed over the neural soma with a predominance in the apical dendritic trunk. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily."}
+{"protein": "QGRPPGPPIPP", "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. 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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-potentiating peptide family."}
+{"protein": "MKLVFLFLLVTIPICCYASGSGCSILDEVIRGTINSTVTLHDYMKLVKPYVHDHFTANAVKQFKQCFLDQTNKTVENVGVMTEAIFNSESCQQPS", "text": "FUNCTION: Part of prostatein which is the major secretory glycoprotein of ventral prostate gland. Steroid-binding protein; can bind non-polar steroids, cholesterol and a group of small proline-rich peptides (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the secretoglobin family. Lipophilin subfamily."}
+{"protein": "MADLKSTFLDVYSVLKSDLLQDPSFEFTHESRQWLERMLDYNVRGGKLNRGLSVVDSYKLLKQGQDLTEKETFLSCALGWCIEWLQAYFLVLDDIMDNSVTRRGQPCWFRKPKVGMIAINDGILLRNHIHRILKKHFREMPYYVDLVDLFNEVEFQTACGQMIDLITTFDGEKDLSKYSLQIHRRIVEYKTAYYSFYLPVACALLMAGENLENHTDVKTVLVDMGIYFQVQDDYLDCFADPETLGKIGTDIEDFKCSWLVVKALERCSEEQTKILYENYGKAEPSNVAKVKALYKELDLEGAFMEYEKESYEKLTKLIEAHQSKAIQAVLKSFLAKIYKRQK", "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": "MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYGENGDEPDADPERDLLSMALINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQVEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGFITACQHHIAEKQRL", "text": "FUNCTION: Involved in the breakdown of putrescine via hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate. SIMILARITY: Belongs to the peptidase C26 family."}
+{"protein": "MGQLPGAGVFCRGGCGFSRLLAWCFLLVLSPQTPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPVAGVLVPPDGPGALNACNPHTNFTVPTVPGDWGSSVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSHPGAGDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQSRKQRQLKADAKKAIGRLQLRTQKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHVFHKTCVDPWLLEHRTCPMCKCDILKALGIEVDVEDGSVSLQVPVSNETSSNASPHEEDNRSETASSGYASVQGADEPPLEEHAHSANENLQLVNHEANSMAVDVVPHVDNPTFEEDESPDQETTVREIKS", "text": "FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down- regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. SUBCELLULAR LOCATION: Endomembrane system; Single-pass membrane protein Cytoplasm, cytoskeleton Cytoplasm, perinuclear region Note=Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A."}
+{"protein": "MKQFSAKFALALSAAAGQALAASTQGISEDLYNRLVEMATISQAAYANMCNIPSTITVGEKIYNAQTDINGWVLRDDSTKEIITVFRGTGSDTNLQLDTNYTLTPFSTFSECSGCEVHGGYFIGWSSVQDQVMSLVKEQADQYPDYTLTVTGHSLGASMATLAAAQLSGTYDNITLYTFGEPRSGNEAFASYMNDKFTATSADTTKYFRVTHSNDGIPNLPPAEQGYVHGGVEYWSVDPYSAQNTYVCTGDEVQCCEAQGGQGVNDAHTTYFGMTSGACTW", "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 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family."}
+{"protein": "MACLLETPIRMSVLSEVTASSRHYVDRLFDPDPQKVLQGVIDMKNAVIGNNKQKANLIVLGAVPRLLYLLQQETSSTELKTECAVVLGSLAMGTENNVKSLLDCHIIPALLQGLLSPDLKFIEACLRCLRTIFTSPVTPEELLYTDATVIPHLMALLSRSRYTQEYICQIFSHCCKGPDHQTILFNHGAVQNIAHLLTSVSYKVRMQALKCFSVLAFENPQVSMTLVNVLVDGELLPQIFVKMLQRDKPIEMQLTSAKCLTYMCRAGAIRTDDNCIVLKTLPCLVRMCSKERLLEERVEGAETLAYLIEPDVELQRIASITDHLIAMLADYFKYPSSVSAITDIKRLDHDLKHAHELRQAAFKLYASLGANDEDIRKKIIDTENMMDRIVTGLSESSVKVRLAAVRCLHSLSRSVQQLRTSFQDHAVWKPLMKVLQNAPDEILVVASSMLCNLLLEFSPSKEPILESGAVELLCGLTQSENPALRVNGIWALMNMAFQAEQKIKADILRSLSTEQLFRLLSDSDLNVLMKTLGLLRNLLSTRPHIDKIMSTHGKQIMQAVTLILEGEHNIEVKEQTLCILANIADGTTAKELIMTNDDILQKIKYYMGHSHVKLQLAAMFCISNLVWNEEEGSQERQDKLRDMGIVDILHKLSQSPDSNLCDKAKTALQQYLA", "text": "FUNCTION: 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. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MADKSHVNNVPMQGNGAYSSHAALQHEAMLKALPLFQAAAEVIANVDSTRISIVEYGSAHGNNSLEPMEAILKSIPTESLELLFSDRPENDFCTLSKTVTAWADGIVGNQLLNPLFISMIPRSFYQQVVPPKSAHLGFSLAALHHLDHVPQPTEDGQDESELLQQQAHVDLATFLKLRSQEIVSGGSLILSFVSQASAGYENYSGPVDACRNAMIEMVQQGKIPLSVAQAFRVPTYNRTLSDVKKVMDEFTQTWKVHDLFEDDVMHPAFHKLKIQSNPSLEASHKYAEVVIDWMMAVCSGYFTKALQVGSQGGYTKQEEEGLLQVWVTRTKEFFIRDYKDKEVICSFIYIRLERL", "text": "FUNCTION: Methyltransferase; 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 roles of the other FUS members are yet undetermined (PubMed:23932525). 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:23932525). 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 (PubMed:23932525). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (PubMed:23932525). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (PubMed:23932525). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (PubMed:23932525). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (PubMed:23932525). SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family."}
+{"protein": "MDPNPRAALERQQLRLRERQKFFEDILQPETEFVFPLSHLHLESQRPPIGSISSMEVNVDTLEQVEFIDLADQDGADVFLPCEESSPAPQMSGVDDHPEELSLLVPTSDRTTSRTSSLSSDSSNLRSPNPSDGGGDTPLAQSDEEDGDDGGAEPGPCS", "text": "FUNCTION: May modulate the activity of casein kinase-1. Inhibits CSNK1D autophosphorylation (in vitro) (By similarity). SIMILARITY: Belongs to the dysbindin family."}
+{"protein": "MVNEKKMLPKRIILMRHGESAGNIDAGAYATTPDHKIPLTEEGRAQAREAGKKMRALISTQSGGACGENWRVYFYVSPYERTRTTLREVGKGFSRKRVIGVREECRIREQDFGNFQVEERMRVVKETRERFGRFFYRFPEGESAADVYDRVSSFLESMWRDVDMNRHQVDPSSELNLVIVSHGLTSRVFLTKWFKWTVAEFERLNNFGNCEFRVMELGASGEYTFAIHHSEEEMLDWGMSKDMIDDQKDRVDGCRVTTSNDSCSLHLNEYFDLLDVTDDEE", "text": "FUNCTION: May play a role in carbohydrates metabolism. SIMILARITY: Belongs to the phosphoglycerate mutase family."}
+{"protein": "MGFPIPDPYVWDESFKVFYQLLDDKHKQIFQGVFDCAKDPSSAAKLQKLIEVTAKHFSDEENMMQQSKYSGYPPHKKAHEEFLGKLRGLRAPLDTAGLDYCKDWLVQHIKTIDFKYKGKL", "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": "MILVLASLFAVLILNVLLWRWLKASACKAQRLPPGPPRLPILGNLLQLGPLPHRDLASLCDKYGPLVYLRLGNVDAITTNDPDTIREILLRQDDVFSSRPKTLAAVHLAYGCGDVALAPMGPHWKRMRRICMEHLLTTKRLESFTTQRAEEARYLIRDVFKRSETGKPINLKEVLGAFSMNNVTRMLLGKQFFGPGSLVSPKEAQEFLHITHKLFWLLGVIYLGDYLPFWRWVDPSGCEKEMRDVEKRVDEFHTKIIDEHRRAKLEDEDKNGDMDFVDVLLSLPGENGKAHMEDVEIKALIQDMIAAATDTSAVTNEWAMAEAIKQPRVMRKIQEELDNVVGSNRMVDESDLVHLNYLRCVVRETFRMHPAGPFLIPHESVRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEDFRPERHWPVEGSGRVEISHGPDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFEWSSPGNIDTVEVYGMTMPKAKPLRAIAKPRLAAHLYT", "text": "FUNCTION: Involved in pollen wall development. Catalyzes the conversion of medium-chain saturated fatty acids to the corresponding monohydroxylated fatty acids, with a preferential hydroxylation of lauric acid at the C-7 position. In-chain hydroxylated fatty acids, together with omega-hydroxylated fatty acids, are key monomeric aliphatic building blocks for sporopollenin synthesis during exine formation. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MSANAEAQCGSISEDNTHSSTTCQGYVLPEGKIMPNTVFVGGIDIRMNEAEIRSYFEQYGTVKEVKIITDRTGVSKGYGFVSFLDNVDVQKIVESQISVHGKRLKLGPAIRKQQNLCSYMQPRPLAFNPPAPQFHSVWTNQNTETYVQPQAVVSPLTQYVQTYAYSSPAVLIQQQVPVGYQPAYNYQAPPQWVPGEQRNYVMPPVYTSVNYHYSEDPEFIQTECAVPEPTQMSGNSPQKKSVDRSIQTVVSCLFNPENRLRNTFVSQEDYFRERRAHHFRKGRAVLKSV", "text": "FUNCTION: RNA-binding protein, which probably plays a central role in gametogenesis in both males and females. Acts by binding to the 3'-UTR of mRNA, specifically recognizing GUU triplets, and promoting the translation of key transcripts (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RRM DAZ family."}
+{"protein": "MKFHLFFFILLFGATILTAKKSYPEYGSLDLRKECKMRRGHCKLQCSEKELRISFCIRPGTHCCM", "text": "FUNCTION: Has bactericidal activity. FUNCTION: Isoform 2 may play a role in the antimicrobial protection of sperm and urogenital tract epithelia. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "MRLEVFCQDRIGLARELLDLLVARSIDLRGIEVAASGRIYLNFSTLEFEQFSNLMAEIRRTPGVTDVRTVPYMPSEREHRVLSALLVAMPEPVFSVDLRTKVELANPAAQNLFNLDENKIRNFTADHLINGFNFARWLESERVQAQAQHVVIEGRDFLMEAHPIYLSEDNDQADQLVGAMVMLKSTARMGRQLQNLVVTDETEFDHIVAVTPRMRQVVEQARKLAMHDAPLLIIGDTGTGKDMLARACHLRSARGKMPFLALNCASLPDDVAESELFGHAAGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPTMQTKLLRFLNDGTFRRVGEEHEVHVNVRVICATQKNLFELVQRGEFREDLFYRLNVLTLNLPPLRERVQDIMPLTEIFVARFADEQGIPRPRLSSQLNAFLMRYNWPGNVRQLKNALYRALTQLEGHELRPQDIVLPEQALDVSLGEEAMEGTLDQITSRFERSILTRLYLSYPSTRKLAKRLGVSHTAIANKLREYGLGQKRGDNE", "text": "FUNCTION: Dual transcriptional regulator of the TyrR regulon, which includes a number of genes coding for proteins involved in the biosynthesis or transport of the three aromatic amino acids, phenylalanine, tyrosine and tryptophan. These three aromatic amino acids act as effectors which bind to the TyrR protein to form an active regulatory protein. Acts by binding specifically to TyrR boxes in the promoter region of the target genes. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MNGIHDTGGAHGYGPVYREPNEPVFRYDWEKTVMSLLPALLANANFNLDEFRHSIERMGPAHYLEGTYYEHWLHVFENLLVEKGVLTATEVATGKAASGKTATRVLTPAIVDDSSAPGLLRPGGGFSFFPVGDKVRVLNKNPVGHTRMPRYTRAKWGQWSSTMVCFVTPDTAAHGKGEQPQHVYTVSFTSVELWGQDASSPKDTIRVDLWDDYLEPA", "text": "FUNCTION: NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. SIMILARITY: Belongs to the nitrile hydratase subunit beta family."}
+{"protein": "MKGKKTLKRTIAAEESNGTSDVKKTKALPIVTHPSHGTVGGQVLTLGQGDVGQLGLGEDIMERKKPALVTLTEDIVQAAAGGMHTVCLGASGSIYTFGCNDEGALGRDTSEEGSEMQPGKVELAEKVVQVSAGDSHTAALTEDGRVFVFGSFRDNNGVIGLLEPMKKSMVPVQVQINTPVIKIASGNDHLVLLTVDGDLYTSGCGEQGQLGRVPERFTNRGGRKGLERLLVPQCIHLKAKGSGRVHFQDVFCGAYFTFAVSQEGHVYGFGLSNYHQLGTKNTQACYAPQNLTSFKNSTKSWIGFSGGQHHTVCVDSEGKAYSLGRAEYGRLGLGENAEEQSEPTPIPDLPKINSVASGASVSYAVSTDGCVFAWGMGTNLQLGTGEEEDVWSPEQMTGKHLEDREVLSVSSGGQHTVLLVRKRS", "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:2361953). 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": "MGGSESTGRKVSFGMDEEERVRVLRGVRLSDEVVNRMKDSDLPSKDQSTSAASGTASAPAAFPSKAGPSASHPASTSTGGAHKPTAAGVGQQYAEEDLYRRYEREQAIIQEELARLAKRERESAHEKLSASILLEKNSTNQERRKAEHLAKELEQKEAELQRLNTFYREQLSSIEKKNLEIYRLTAEQYHTAATNAELRVRQRSYDPVCMNLQADILKCYSENKQERLNCSNLAKEYRKCVSAAQKNLLFNHG", "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; Lipid-anchor. SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan Mic25 subfamily."}
+{"protein": "MPNLENLDWKNLGFSYIKTDFRFIATYKNGSWSQGELVSENALQLSEGSPVLHYGQACFEGLKAYRSQKGKALLFRPLENAKRLQTSCERLLMPKVSEELFLKACAEVIKANQKWLAPYKSGASLYLRPFVIGVGDNLGVKPASEYLFIVFCAPVGAYFKGGIEKGGARFITTAFDRAAPKGTGGVKVGGNYAASLLAHKIATEQGYDDCIYLDPTTHTKIEEVGAANFFGITHDDAFITPHSPSILPSVTRKSLMVLAKEHLKLKVEEREILIDELGAFKEAGACGTAAIITPIKEIAHNNKSYSFEAPGNITKQLYDLLLSIQQGEQEAPKDWIFEVG", "text": "FUNCTION: Acts on leucine, isoleucine and valine. SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MSANSPTGNDPHVFGIPVNATPSNMGSPGSPVNVPPPMNPAVANVNHPVMRTNSNSNANEGTRTLTREQIQQLQQRQRLLLQQRLLEQQRKQQALQNYEAQFYQMLMTLNKRPKRLYNFVEDADSILKKYEQYLHSFEFHIYENNYKICAPANSRLQQQQKQPELTSDGLILTKNNETLKEFLEYVARGRIPDAIMEVLRDCNIQFYEGNLILQVYDHTNTVDVTPKENKPNLNSSSSPSNNNSTQDNSKIQQPSEPNSGVANTGANTANKKASFKRPRVYRTLLKPNDLTTYYDMMSYADNARFSDSIYQQFESEILTLTKRNLSLSVPLNPYEHRDMLEETAFSEPHWDSEKKSFIHEHRAESTREGTKGVVGHIEERDEFPQHSSNYEQLMLIMNERTTTITNSTFAVSLTKNAMEIASSSSNGVRGASSSTSNSASNTRNNSLANGNQVALAAAAAAAAVGSTMGNDNNQFSRLKFIEQWRINKEKRKQQALSANINPTPFNARISMTAPLTPQQQLLQRQQQALEQQQNGGAMKNANKRSGNNATSNNNNNNNNLDKPKVKRPRKNAKKSESGTPAPKKKRMTKKKQSASSTPSSTTMS", "text": "FUNCTION: Transcription regulator. May recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. 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 SPT20 family."}
+{"protein": "MHGLLLAAGLLSLPLRALGHPNPNPQMHTLSRRGAVDLDAFRLGQNAEYSNTASVASNPPALSIRSTQSYVDVAKDLVKTTLPDATFRVVNDHYVGTNGVAHVHLRQTVHGIDVDNADFNVNVKDGKVFSFGNSFYKGKIPEENPMVKRDHADPVKALKGVVSALKLPVKTEKASAAISAQSQGQDAVVFKGTSGALSDPKGELVYLIKPDGELSLTWKVETDVGDNWLLSYIDAKDGKNIHGVVDYVADATYQVYPWGINDPTEGEREVFTDPWDGNASEFTWISDGRTRYPTTRGNNGIAQDNPSGGNQYENNYRPMSDDLRFEYPYSTDMSPPDSYIDASITQLFYTANVYHDLLYILGFTERAGNFEYNNNNQGGRGNDYVILNSQDGSGTNNANFATPPDGQPGRMRMYTWTTSRPNRDGSFEAGIVIHEYTHGLSNRLCGGPSNSRCLNALESGGMGEGWGDFMATAIRLKAGDTRETDYTMGEWAANQQGGIRQHPYSTNLQTNPLVYTTVNQYREVHDIGTVWASMLYEVLWNLIDKHGKNDGPKPELRDGVPTDGKYLTMKLVIDGMALQPCNPNFVQARDAILDADEALTGGENKCEIWAGFAKRELGTGARYDRSRRTGSTDVPQECQ", "text": "FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M36 family."}
+{"protein": "MAEAVWSTDTGEAVYRSRDPVRNLRLRVHLQRITSSNFLHYQPAAQMGKDLIDLATFRPPQAASGHRPDEEEEEEVVIGWQEKLFSQFEVDLYQNESACQSPLDHQYRQEILKLENSGGRKNRRIFTYTDSDRYTDLEEYCQKITTSASEVPSFLAERMANVRRRRQDRRGVEGSKLKSRIVTWEPSEDFIKNNHAINTPLQTMYIMADLGPYGKLGYKVHEHVLCILKVDSNGVITVKPDFTGIKGPYRIETEGEKQEHTSAWKYTIDNVSSLAQPEEEEREQRVFKDLYGRHKEYLSSLVGTDFEMIAPGALRLFVNGEVVSAQGYEYDNLYVHFFVELPAANWSSPPFQQLSGVTQACATKSLGMDKVAYFSFPFTFEAFFLHEDESAESLPEWPVLYCKVLSLDFWQRYRVEGYGAVVLPATPGSHTLTVSTWRPMELGLVAELRRFFIGGSLELEDPSYVRIPGTFKGERLSRFGFRTETTGTVTFRLHCLQQSRAFMESNSLQKQMRSVLDRLEGFSQQSSTHNVLEAFRRARRRMQEARESLPQDLVSPTGTLT", "text": "FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. 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. Required for cell branching morphology. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme."}
+{"protein": "MALDFSNATVKAWRRENGRVGVRNHVLILPVDDISNAACEAVANNVKGTLAIPHAYGRLQFGEDLELHFRTIIGTGANPNVAAVVVIGIEPEWTQVIVDGIAKTGKPVTGFSIEQKGDFETIRQAGWKAKEYVHWASELQKEDCPISDLWISTKCGESDTTTGLSSCPTVGNMYDKLLPQGIYGCFGETSEITGAEHICEKRAANPETARKFKEIWQAYSDDVIFAHQTDDLSDSQPTKGNILGGLTTIEEKALGNLEKIGRTSTYIDAMGPAETPSKGPGLYFMDSSSAAAECVTLMAAGGYVIHTFPTGQGNVVGNPIVPVIKISGNPRTLRTMSEHIDVDVTGVLTREMTIDQAGDALIEMIIRTANGRMTAAEALGHREFSMTKLYRSA", "text": "FUNCTION: Together with SuyA, desulfonates sulfolactate to pyruvate and sulfite. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UxaA family."}
+{"protein": "MWPFASVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASEKGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYPPLATDLRRRFDTFKAFDSAKNSWLNLCSAACCLPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLKSAKTSIDIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSLDALCVQNDLSVKVFTIQNNTKLLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI", "text": "FUNCTION: Major envelope protein that plays a role in the biogenesis of the viral double membrane and in egress of virus from the host cell. Produces the wrapped form of virus that is required for cell-to-cell spread. Acts as a lipase with broad specificity including phospholipase C, phospholipase A, and triacylglycerol lipase activities. SUBCELLULAR LOCATION: Virion membrane; Lipid-anchor Host Golgi apparatus, host trans-Golgi network Host endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side Note=Component of the inner side of the enveloped virion (EV) membrane. F13 is associated post-translationally with membranes. SIMILARITY: Belongs to the orthopoxvirus OPG057 family."}
+{"protein": "MMSDQENENEHAKAFLGLAKCEEEVDAIEREVELYRLNKMKPVYEKRDAYIDEIAEFWKIVLSQHVSFANYIRASDFKYIDTIDKIKVEWLALESEMYDTRDFSITFHFHGIEGDFKEQQVTKVFQIKKGKDDQEDGILTSEPVPIEWPQSYDSINPDLIKDKRSPEGKKKYRQGMKTIFGWFRWTGLKPGKEFPHGDSLASLFSEEIYPFCVKYYAEAQRDLEDEEGESGLSADGDSEDDDGSLGEVDLPLSDEEPSSKKRKV", "text": "FUNCTION: Histone chaperone which acts as a cofactor stimulating histone H3 acetylation by RTT109 (PubMed:21256037, PubMed:17320445, PubMed:31387991, PubMed:29300933, PubMed:19172748). Preferentially stimulates histone H3 'Lys-9' acetylation by RTT109 (PubMed:21256037, PubMed:31387991, PubMed:29300933). May also stimulate histone H3 'Lys- 56' acetylation by RTT109 (PubMed:17320445). Assembles nucleosomes (in vitro) (PubMed:19172748). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
+{"protein": "MEEYQHDNSTTPQRVSFLYSPISSSNKNDNTSDTNNNNNNNNSSNYGPGYNNTNNNNHHHQHMLFPHMSSLLPQTTENCFRSDHDQPNNNNNPSVKSEASSSRINHYSMLMRAIHNTQEANNNNNDNVSDVEAMKAKIIAHPHYSTLLQAYLDCQKIGAPPDVVDRITAARQDFEARQQRSTPSVSASSRDPELDQFMEAYCDMLVKYREELTRPIQEAMEFIRRIESQLSMLCQSPIHILNNPDGKSDNMGSSDEEQENNSGGETELPEIDPRAEDRELKNHLLKKYSGYLSSLKQELSKKKKKGKLPKEARQKLLTWWELHYKWPYPSESEKVALAESTGLDQKQINNWFINQRKRHWKPSEDMQFMVMDGLQHPHHAALYMDGHYMGDGPYRLGP", "text": "FUNCTION: May play a role in meristem function, and may be involved in maintaining cells in an undifferentiated, meristematic state, and its expression disappears at the same time the shoot apex undergoes the transition from vegetative to reproductive development (PubMed:11934861). Positive regulator of LATERAL ORGAN BOUNDARIES (LOB) (PubMed:11934861). Probably binds to the DNA sequence 5'-TGAC-3' (PubMed:11934861). Able to traffic from the L1 to the L2/L3 layers of the meristem, presumably through plasmodesmata (PubMed:12900451). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/KNOX homeobox family."}
+{"protein": "MKRKNNKFIEISIAFILGIALGLYGQNPDYFTNLISQKSLALSALQIKHYNISELSRSKVSTCFTPPAGCTKFIANQIDKAEESIYMQAYGMSDALITTALINAQARGVKVRILLDRSNLKQKFSKLHELQRAKIDVDIDKVPGIAHNKVIIIDKKKVITGSFNFTAAADKRNAENVIIIEDQELAESYLQNWLNRKASN", "text": "FUNCTION: Could be a virulence factor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase D family."}
+{"protein": "MDHQLTREESQRLMHLLKLPMEQYGNFPLMRKAFLRACKIVHPDKGGSDELSQELISLYRRLEESLPCLSTQDFIETDILQIPSYGTPEWDEWWKEFNKDFDLFCNEAFDRSDDEQEPQPDDSAPIILSPTYPARSQATPPKKKAKMDSPNDMPADLMEYLSCAILSNKTLPCFLIYTTLEKVELLYNKLSEEVLSPRFNQVDHKYGRKYVPIFIITGTKHRVSAVFNYCATYCSVSFIVVKGVIKEYPLYCHLCVEPYSVLQESIEELNSEFFDAPEDAAKNVNWVAISEYALKINCDDIYLLMGLYKEFQSPVPNCSKCENRMLTNHFKFHKEHHENAFYLQLVENQKTICQQAVDGVIATKTVDMAQMTRNEQLAARFDKLFERLEVILSAQSSYTISMFMAGIVWFENLFPGQSFKDLLLELLECMVSNIPKRRYWLFTGPVNTGKTTLAAAVLDLGGTIYISDCYLIELEVANSQIHGCVEVLAEKVKIRLPPGQGINNLDNLRDHLDGAVKVNLEKKHLNKKTQIFPPGIVTSNEYFIPFTLRVRFCKKLVFKFSKYQYLSLKKTECLGRYRILQNGCTLLLLLIYHCDLDDFAESIQGKVRAWKERVNSEISVSTYLEMRQCCLEGRYSVCTKYSNANTAQ", "text": "FUNCTION: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription. SUBCELLULAR LOCATION: Host nucleus."}
+{"protein": "MTLGSCCCEIMSSESSPAALSEPDADIDVVGGGSGGGELTARSGPRAPRDVLPHGHEPPPEEAEADVAEDEEESGGCSDCEPRALAPRGAAAAAGSPGPGVQAARGATGPGPGPGPPSGGAATRSPLVKPPYSYIALITMAILQSPKKRLTLSEICEFISGRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPESADMFDNGSFLRRRKRFKRQPLPPPHPHPHPHPELLLRGGAAAAGDPGAFLSSFAAYGAYGYGYGLALPAYGAPPPGPAPHPHPHPHAFAFAATAPCQLSVPPGRAAAPPPGPPTASVFASAASAPAPAPAPGSGPSPAGLPAFLGAELGCAKAFYPASLSPPAAGTAASLSTALLRQGLKTDAGGGAGGGGAGTGQRPSFSIDHIMGHGGGGAAPPGSGDGSPGSPFAAAAGPGGQAQVLAMLTAPALTPVAGHIRLSHPGDSLLSSGPSFASKVAGLSGCHF", "text": "FUNCTION: Probable transcription factor involved in embryogenesis and somatogenesis. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MQLTSFTDYALRTLIYLASLPDNEQTNITDVTELFGVSRNHMVKVINRLGQLNYIQTVRGKNGGIRLNRPAKTILVGEVVRDLEPLDLVNCSVEFCHITPACRLKERLYRAKLAFLAELDDCSIAELLDDNAELLILLQKA", "text": "FUNCTION: Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress. May require iron for activity."}
+{"protein": "MAAQGWSMLLLAVLNLGIFVRPCDTQELRCLCIQEHSEFIPLKLIKNIMVIFETIYCNRKEVIAVPKNGSMICLDPDAPWVKATVGPITNRFLPEDLKQKEFPPAMKLLYSVEHEKPLYLSFGRPENKRIFPFPIRETSRHFADLAHNSDRNFLRDSSEVSLTGSDA", "text": "FUNCTION: Chemotactic for neutrophils. Involved in lung-specific neutrophil trafficking during normal and inflammatory conditions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family."}
+{"protein": "MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP", "text": "FUNCTION: This potent antithrombotic agent acts in a calcium- independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
+{"protein": "MTSMYNFKRITCVPNAQELKDVVLSKTQRKTPTVVHRQYSIGRIRAFYARKIKFLQQTLHDKLTQIITEFPKMEEIHPFYSDLMNILYDRDHYKIALGQMNTARHLIDGIAREYVRLMKYADSLYRCKMLKRAALGRMVKLLKRQKSSFEYLEQVRQHLSRLPSIDPATRTLILCGFPNVGKSSFINNVTRADVEVQPYAFTTKALYVGHLDYRFLRWQVIDTPGILDQPLEDRNTIEMQAVTALAHLKASVLFMMDVSEQCDRSIEEQLHLFESIRPLFANKPVLIGLNKVDIRHRSDLPPEKAALLDQLEKEGIPIIETSTLTQEGVMGLRDRACDELLAQRVEAKIQAKKITNVEDCVLNRVFVAYPAPRDEKVRAPFVPPGLAAKRAQKKLQEAQELMETDGDEFAAKIPQKPGKIGKEKIAKGGSQSTDLGDLRDENTRRLEREIELEMQDDYILDLKKHYMLKNPDEKYDIVPEIWEGHNLADFVDPEIQSKLENLLREEELLEQAGEYESDLDSDDEETKEKLKLALQIREKEKLLTLDHAVNKRIAGRIGSRIHGSRKRDRSMSRLENELGELGVDVDTKKMKNLQGQCAKPQLGKKMKVGRSRSLSAVRPAPRDELAFPDEEKRAHVDKLRTKAMRGLRREAKKGEADRHVYDLKPKHLFCGKRGNGKTDWR", "text": "FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit (By similarity). Has a role in regulating longevity, growth and brood size (PubMed:24552710). May regulate fat storage via the insulin/IGF pathway (PubMed:24552710). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily."}
+{"protein": "MITHFRQAIEETLPWLSSFGADPAGGMTRLLYSPEWLETQQQFKKRMAASGLETRFDEVGNLYGRLNGTEYPQEVVLSGSHIDTVVNGGNLDGQFGALAAWLAIDWLKTQYGAPLRTVEVVAMAEEEGSRFPYVFWGSKNIFGLANPDDVRNICDAKGNSFVDAMKACGFTLPNAPLTPRQDIKAFVELHIEQGCVLESNGQSIGVVNAIVGQRRYTVTLNGESNHAGTTPMGYRRDTVYAFSRICHQSVEKAKRMGDPLVLTFGKVEPRPNTVNVVPGKTTFTIDCRHTDAAVLRDFTQQLENDMRAICDEMDIGIDIDLWMDEEPVPMNKELVATLTELCEREKLNYRVMHSGAGHDAQIFAPRVPTCMIFIPSINGISHNPAERTNITDLAEGVKTLALMLYQLAWQK", "text": "FUNCTION: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin (PubMed:10601204, PubMed:20038185). Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3 (PubMed:20038185). In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen (PubMed:20038185). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20 family."}
+{"protein": "MSSELLISNSKPRPEGLRKLCEGETVILPRDITPSKCAYFLKQNIVFISYIFIHIIITIILNRLALSAHGNTLIIILAALLITISLFLLLLLPYLSCSRYKLRCLDDDCKFKLLAEVITHKPNMDLSTWDRIAYDMNQFVYDRRICADRSFFYDGSYCYQVFKKLVATPYLVNSNMNSIYADLEMRSNGATNINDSGNSSLHIELGTYIFKALAVFRNSVDKYWEDKYPEMGVTV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DUP/COS family."}
+{"protein": "MESPKTFMRKLPITPGYCGFIPWLSCQESSSEDRMNPCVKAFQERTQRYKEDQQGLNCSVANTPPLKPICSEDTVLWVLHEYAKKYHPLTLECKNEKKPLQEPPIPGWAGYLPRARVTEFGYATRYTIMAKKCYKDFLDLVEQAKRAQLKPYEQTYDVRAAQPLSPSSKILQLQGLSPAFPEFSGPGQTPPSEDPQAPRPCGCAQWSSQSCSRNVYGEPPSLAKAFAES", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Located in the cytoplasm of spermatocytes and the nuclei of round spermatids and elongated spermatids."}
+{"protein": "MELSPRSPPEMLESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELRELRSDAVPSEVRDWLASTFTQQTRAKGRRAEEKPKFRSIVHAVQAGIFVERMFRRTYTAVGPTYSTAVHNCLKNLDLWCFDVFSLNRAADDHALRTIVFELLTRHSLISRFKIPTVFLMSFLEALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKSMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLADDDSKSKSQPSFQWRQPSLDVDVGDPNPDVISFRSTWTKYIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD", "text": "FUNCTION: Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily."}
+{"protein": "MFSIQQPLLVFSDLDGTLLDSHSYDWQPTALWLSRLREANVPVILCSSKTSAEMLYLQKTLGLQGLPLIAENGAVIQLAEQWQDIDGFPRIISGISHGEISQVLNTLREKEHFKFTTFDDVDDATIAEWTGLSRSQAALTQLHEASVTLIWRDSDERMAQFTARLNELGLQFMQGARFWHVLDASAGKDQAANWIIATYQQLSGKRPTTLGLGDGPNDAPLLEVMDYAVIVKGLNREGVHLHDEDPTRVWRTQREGPEGWREGLDHFFSAR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MPGP family."}
+{"protein": "MKTLCLLFAVLCLVTWTQARGAEVEENLTAQDGEVDIAGDNGDVQLTLNTDDFESFTLKTLTLGHPRVKRHSCVCRRICAARQVRKGRCSRRRRICCLY", "text": "FUNCTION: Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MSREAISNNELTEEQIAEFKEAFSLFDKDGDGTITTSELGTVMRSLGQNPTEAELHDMINEVDADGNGTIDFTEFLTMMAKKMKDTDNEEEIKEAFKVFDKDGNGFISAQELRHVMCNLGEKLTDEEVDEMIREADIDGDNQINYTEFVKMMMQK", "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. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. SIMILARITY: Belongs to the calmodulin family."}
+{"protein": "MAAEMALVKPITPKFINPMRTFSSSSKFSTIKMSATSQSNTTTTATKPSKKGNKKEINETLLTPRFYTTDFDEMETLFNTEINKKLNQSEFEALLQEFKTDYNQTHFVRNKEFKEAADKMQGPLRQIFVEFLERSCTAEFSGFLLYKELGRRLKKTNPVVAEIFSLMSRDEARHAGFLNKGLSDFNYALDLGFLTKARKYTFFKPKFIFYATYLSEKIGYWRYITIYRHLKENPEYQCYPIFKYFENWCQDENRHGDFFSALMKAQPQFLNDWKAKLWARFFCLSVYVTMYLNDCQRTAFYEGIGLDTKEFDMHVIIETNRTTARIFPAVLDVENPEFKRKLDRMVVINQKLQAVGETEDNSVVKNLKRVPLIAALVSEILAAYLMPPIESGSVDFAEFEPKLVY", "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) (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the AcsF family."}
+{"protein": "MPPSTVNQEVNSILFIKNLSFKITAEEMYDLFGRYGPVRQIRLGNTVQTRGTAFVVYENVQDARRACEKLSGYNFMDRYLVVHYYNPERAKVDGQDLAARYAALEQVKQKYGVQL", "text": "FUNCTION: Necessary for the splicing of pre-mRNA. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MELGKSKFSWKDLQYCDKAGTQNSPLRVVAHIDQDAFYAQVESVRLGLDHSVPLAVQQWQGLIAVNYAARAANISRHETVTEAKKKCPELCTAHVKTWKAGESEAKYHENPNPNYYKTCLDPYRHESVKILNIIKKHAPVVKKASIDECFIELTSDVKRIVLEEYPYLKIPSEDSNVALPQAPVLLWPAEFGMVIEEEVVDRTKEDYERDWDDVFLFYAAKIVKEIRDDIYLQLKYTCSAGVSFNPMLSKLVSSRNKPNKQTILTKNAIQDYLVSLKITDIRMLGGKFGEEIINLLGTDSIKDVWNMSMDFLIDKLGQTNGPLVWNLCHGIDNTEITTQVQIKSMLSAKNFSQQKVKSEEDAINWFQVFASDLRSRFLELEGMRRPKTICLTVVSRFLRKSRSSQIPMNVDISTQFIVEATSKLLRQLQQEFDVYPISNLSISFQNIIEVDRNSRGIEGFLKKSNDEIYMSTSVSPSIEGRAKLLNENMRENNSFELSSEKDIKSPKRLKRGKGKGIFDMLQQTAVSKPTENSADETYTCEECEQKITLSERNEHEDYHIALSISRKERYNNLVPPSHDKPKQVKPKTYGRKTGSKHYAPLSDETNNKRAFLDAFLGNGGNLTPNWKKQTPKAISNSSDNMTQLHLDLANSTVTCSECSMEYNSTSEEDILLHSRFHSRVLGGVTVSFQCSPIYRVNYGLSSDCIYSINSESSLIDQRKAEEALSFVNNELSSEPIETIGVDKYTTFLFISDKKCVGLLLAERISSAYIVDELELNNNNSTSSAVYIKNENLRKGFVLGISRIWVSASRRKQGIASLLLDNALKKFIYGYVISPAEVAFSQPSESGKQFIISWHRSRNNGSSKSLRYAVYES", "text": "FUNCTION: Probable acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. The relevance of acetyltransferase function remains unclear (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: In the C-terminal section; belongs to the acetyltransferase family. ECO subfamily. SIMILARITY: In the N-terminal section; belongs to the DNA polymerase type-Y family."}
+{"protein": "MLHHKFVYPFLFKWHLSCVEKCPPQITFIAKYATANDKNGNRKLTIRDEQWPELADPTPYDIFGIPKAGSGNPKLDKKSLKKKYHRYVKLYHPDHSDNIQIFSSEKVTNSDSKSPLLLTSSEKLHRFKVISQAYDILCDPKKKIVYDTTRQGWTTSYSPRSNVNTENYQYAGSYGYHSNAQYEYWNAGTWEDANSMKNERIQENINPWTVIGIICGLAICIEGTALLAKIQESLSKAEFTHDESGLHLIQSYTNYGLDTDKFSRLRRFLWFRTWGLYKSKEDLDREAKINEEMIRKLKAAK", "text": "FUNCTION: Probable chaperone. SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the DnaJ family."}
+{"protein": "MSTIQQLVRKRRKKIKKKKKLAALDSCPQKKCICLKVHTITPKKPNSALRKVTRVKIISISKMFTTAYIPGIGHNLQEHSMVLIRGGRVKDLPGVKYKVIRGCLDAAGVKNRKNGRSKYGVKRPK", "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. SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
+{"protein": "MPTYALLGATGATGSAILRCLLASPPPDLDLNILVRSKQKLLKSFPTLTTTISPRIHIIQGNSTDTIALQQCLEDASVAFMCVADNASNKGVSLTADTVTAIVTTLGMLRKLHGSAYNAPTILQLRSASLNPKLSCQVPRLVYNIVSFCLHYSHLDIVKACEHYEAAAAKGLLSYIYVDPPTIHDAFGPNRTGHKLISCKPDVCDKQETALSYADLGAGFVEIASRKEDFLNQPVGVTATGKAKETWGVLAGFLFDGAKGRARAWWEEERPMSKPQNLFLYCVMVSLAAVVLVQYTGTMNR", "text": "FUNCTION: Averufin oxidase A; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl- carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)- averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non-enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8- dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690). SIMILARITY: Belongs to the avfA family."}
+{"protein": "MERTFIAIKPDGVQRGLVGTIIGRFEQKGFKLVGLKQLKPSRELAEQHYAVHRERPFFNGLVEFITSGPIVAIVLEGEGVVAAARKLIGATNPLTAEPGTIRGDFGVNIGRNIIHGSDAIETAQQEIALWFSPAELSDWTPTIQPWLYE", "text": "FUNCTION: (Microbial infection) Catalyzes the phosphorylation of dZDP to dZTP, when the bacterium is infected by a phage that produces the substrate for the synthesis of dZTP (2- amino-2'-deoxyadenosine 5'- triphosphate), which is then used by the phage as a DNA polymerase substrate. 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. SIMILARITY: Belongs to the NDK family."}
+{"protein": "MKLIKVTLVFSLLALVFVAQTEAQNPIWENWLACNRIGTKALASLLRETIPTVRNLLNCIDFNPPTDIGNSYLSKLKLYYELVKRGALDKTQCLIVPLKESVRLLRPYVKSLETNKCLGE", "text": "FUNCTION: Responsible for physiological and behavioral changes in mated female flies. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MERYLPVSKKRNSSSSLEKITGSANGNGTLYSEEDTNLEENDFSWGDYLEETGTRAVPHVSFRHVEISIRSNFQPGMKLEVANKNNPDTYWVATIITTCGQLLLLRYCGYGEDRRADFWCDVIIADLHPVGWCTQNNKVLRPPDAIKDKYSDWTDFLIRELTGSRTAPANLLEGPLRGKGPIDLITVDSLIELQDSQNPFQYWIVSVTENVGGRLRLRYVGLEHTESYDRWLFYLDYRLRPIGWCQENKYRMDPPSDLYYLKLPFEWKCALEKALVLAAESPLPMEVFKDHADLQSHFFTVGMRLETLHISDPFHIYPASVTKVFNSKFFQVAIDDLRPEADKPTMLCHADSLGILPVQWCLKNGVNLAPPKGYSGQDFNWVDYHKQRQAEEAPHFCFKNAFSRGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMPDIIVDMDSMDIFPVGWCEANSYPLTTPYKASSKSKRKTVHFKMEKQLLSPVPIEKIPHELCLLPPQMDSPVGAINAKYCCPQLFVNHRCFSGPFLNKGRISELPQSVGPGMCVLVLKEILTLITNAAYKPGRVLRELQLVEDPEWNSQEEILKAKYGGKTYRAVVKIVRTADQVMNFCRQVCAKLECCPNLLSPVLISETCPENCSVHTKTRYTYYYGKRRRVIQSSLRVSNIETPPKSTRRRKRRKSVYVQKRRKSAIVVPAGVPAGVPAGVPEDIPAGIPEGIPASIPESIPEGIPESLPEAIPESIPKGSAQKTEQEKRETLDTARKKTGYHGPAYQTDTSAAQVPFARPRRAVTLRRNSEALKRPPVERARRVRTVPTTASSNNRVKGPLVRIVKPEDSSQSDEEKLILESNPLEWSVTDVVRFIKLTDCAPLARIFQEQDIDGQALLLLTLPTVQECMELKLGPAIKLCHQIERVKVAFYAQYAS", "text": "FUNCTION: Transcriptional repressor of HOXB13 gene. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MRFNHFSIVDKNFDEQLAELDQLGFRWSVFWDEKKILKDFLIQSPSDMTALQATAELDVIEFLKSSIELDWEIFWNIALQLLDFVPNFDFEIGKAFEYAKNSNLPQIEAEMTTENIISAFYYLLCTRRKTGMILVEHWVSEGLLPLDNHYHFFNDKSLATFDSSLLEREVLWVESPVDSEQRGENDLIKIQIIRPKSTEKLPVVMTASPYHLGINDKANDLALHDMNVELEEKTSHEIHVEQKLPQKLSAKAKELPIVDKAPYRFTHGWTYSLNDYFLTRGFASIYVAGVGTRSSDGFQTSGDYQQIYSMTAVIDWLNGRARAYTSRKKTHEIKASWANGKVAMTGKSYLGTMAYGAATTGVEGLELILAEAGISSWYNYYRENGLVRSPGGFPGEDLDVLAALTYSRNLDGADFLKGNAEYEKRLAEMTAALDRKSGDYNQFWHDRNYLINTDKVKADVLIVHGLQDWNVTPEQAYNFWKALPEGHAKHAFLHRGAHIYMNSWQSIDFSETINAYFVAKLLDRDLNLNLPPVILQENSKDQVWTMMNDFGANTQIKLPLGKTAVSFAQFDNNYDDETFKKYSKDFNVFKKDLFENKANEAVIDLELPSMLTINGPVELELRLKLNDTKGFLSAQILDFGQKKRLEDKVRVKDFKVLDRGRNFMLDDLVELPLVESPYQLVTKGFTNLQNQSLLTVSDLKADEWFTIKFELQPTIYHLEKADKLRVILYSTDFEHTVRDNRKVTYEIDLSQSKLIIPIESVKN", "text": "FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S15 family. SIMILARITY: Belongs to the peptidase S15 family."}
+{"protein": "MTTPLKKIVIVGGGAGGLEMATQLGHKLGRKKKAKITLVDRNHSHLWKPLLHEVATGSLDEGVDALSYLAHARNHGFQFQLGSVIDIDREAKTITIAELRDEKGELLVPERKIAYDTLVMALGSTSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANLGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYKGLTNEALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIEADLMVWAAGIKAPDFLKDIGGLETNRINQLVVEPTLQTTRDPDIYAIGDCASCPRPEGGFVPPRAQAAHQMATCAMNNILAQMNGKPLKNYQYKDHGSLVSLSNFSTVGSLMGNLTRGSMMIEGRIARFVYISLYRMHQIALHGYFKTGLMMLVGSINRVIRPRLKLH", "text": "FUNCTION: Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones (PubMed:6784762, PubMed:7009604, PubMed:7020757, PubMed:6362717, PubMed:3122832, PubMed:2679883, PubMed:10664466). Utilizes NADH exclusively, and electron flow from NADH to ubiquinone does not generate an electrochemical gradient (PubMed:3122832, PubMed:2679883). FUNCTION: It may also contribute to copper homeostasis and bacterial oxidative protection (PubMed:7487066, PubMed:10510271, PubMed:16759635, PubMed:21390523). Shows cupric reductase activity, and catalyzes the reduction of Cu(2+) to Cu(+) with NADH as electron donor (PubMed:10510271). Exhibits Cu(2+) reductase activity in the presence of either FAD or quinone, but is unable to reduce Fe(3+) (PubMed:10510271). Contains thiolate-bound copper (PubMed:12176061). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Note=Membrane-bound (PubMed:10664466). Interaction with the membrane is probably mediated by amphipathic helices and electrostatic interactions (PubMed:15581635). Copurifies with phospholipids (PubMed:7020757, PubMed:6362717). SIMILARITY: Belongs to the NADH dehydrogenase family."}
+{"protein": "MRVNLLIAMIIFALIWPVTALRAAVSKTTWADAPAREFVFVENNSDDNFFVTPGGALDPRLTGANRWTGLKYNGSGTIYQQSLGYIDNGYNTGLYTNWKFDMWLENSPVSSPLTGLRCINWYAGCNMTTSLILPQTTDTSGFYGATVTSGGAKWMHGMLSDAFYQYLQQMPVGSSFTMTINACQTSVNYDASSGARCKDQASGNWYVRNVTHTKAANLRLINTHSLAEVFINSDGVPTLGEGNADCRTQTIGSRSGLSCKMVNYTLQTNGLSNTSIHIFPAIANSSLASAVGAYDMQFSLNGSSWKPVSNTAYYYTFNEMKSADSIYVFFSSNFFKQMVNQGISDINTKDLFNFRFQNTTSPESGWYEFSTSNTLIIKPRDFSISIISDEYTQTPSREGYVGSGESALDFGYIVTTSGKTAADEVLIKVTGPAQVIGGRSYCVFSSDDGKAKVPFPATLSFITRNGATKTYDAGCDDSWRDMTDALWLTTPWTDISGEVGQMDKTTVKFSIPMDNAISLRTVDDNGWFGEVSASGEIHVQATWRNIN", "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. Tip pilus adhesin, which is required for assembly of EcpA into fibers (By similarity). SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the EcpD/MatE family."}
+{"protein": "MRTSYLLLFTLCLLMSEMASGDNFLTGLGHRSDHYNCVRSGGQCLYSACPIYTKIQGTCYHGKAKCCK", "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": "MDAKKNTGEANNDVLEEEAAIQLIAPGIARNLTQEVITGIFCNVVIYPLLLIYFVLTFRYMTTNIVPYEFIDEKFHVGQTLTYLKGKWTQWDPKITTPPGIYILGLINYYCIKPIFKSWSTLTILRLVNLLGGIIVFPILVLRPIFLFNALGFWPVSLMSFPLMTTYYYLFYTDVWSTILILQSLSCVLTLPFGPVKSIWLSAFFAGVSCLFRQTNIIWTGFIMILAVERPAILQKQFNTHTFNNYLKLFIHAIDDFSNLVLPYMINFVLFFIYLIWNRSITLGDKSSHSAGLHIVQIFYCFTFITVFSLPIWISRNFMKLYKLRIKRKPVQTFFEFIGIMLIIRYFTKVHPFLLADNRHYTFYLFRRLIGNKSRLIKYFFMTPIYHFSTFAYLEVMRPNQLTFHPITPLPIKEPVHLPIQLTHVSWTALITCTMVTIVPSPLFEPRYYILPYFFWRIFITCSCEPLIKDLKPAKEGENPITISSTKRLFMEFLWFMLFNVVTLVIFSKVSFPWTTEPYLQRIIW", "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": "MASSTALSLSWSSSPCWSHSFNGGANETLKVSERRFNFEVVSQKKAKKLRKVILKEDVTDLGKQGQLLDVKAGFFRNFLLPTGKAQLMTPLLLKELKMEDERIEAEKQRVKEEAQQLAMVFQTVGAFKVKRKGGKGKLIFGSVTAQDLVDIIKSQLQKDIDKRLVSLPEIRETGEYIAELKLHPDVTARVKINVFAN", "text": "FUNCTION: Binds to the 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
+{"protein": "MVKIKKTKGMRKQIRLNEVEEINLLKQWIESQKPDSGFNPLSLRPLPKDSKIGKSEDGKNGTVFSRYAGVRKFAQLPISDKTKRGLKDAKYVDMTDVQSAAIPHALCGRDILGAARTGSGKTLAFVIPILEKLHRERWSPEDGVGCIIISPTRELAAQTFGVLNKVGKFHKFSAGLLIGGREGVDVEKERVHEMNILVCAPGRLLQHMDETPNFECPQLQILILDEADRVLDSAFKGQLDPIISQLPKHRQTLLFSATQTKKVKDLARLSLRDPEYISVHAEAVTATPTSLMQTVMIVPVEKKLDMLWSFIKTHLNSRILVFLSTKKQVKFVHEAFNKLRPGIPLKSLHGKMSQEKRMGVYSQFIERQSVLFCTDVLARGLDFDKAVDWVVQVDCPEDVASYIHRVGRTARFYTQGKSLLFLTPSEEKMIEKLQEAKVPIKLIKANNQKLQEVSRLLAALLVKYPDLQGVAQRAFITYLRSIHKRRDKEIFDVSKLSIENFSASLGLPMTPRIRFTNLKTKKKGVYESSIAMEIENAQEYEAPLVVKKDLLGEDLEEEDFALKPRKEGKVVEKSTKEEEVLIPGNRVLKNKKLKINLHRPFGSRVVLDEEGNSLAPLASVAAEAGTEVALDEERMNDYYKKVGAEMRKADIEDKKVDKERRREKRMKQKIKRKRGAMEDEEEEEEEDHDGSGSSDDETGRNSKRAKKIVSDNEENGGKINTDSLSVADLEEMALKFITQ", "text": "SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4 subfamily."}
+{"protein": "MFSTFGSVPILTVVAIQLFLIRNVLSLNLTNAYLHHKCNNTQGIYKRGSAFEKNLNIALRTVIFNGDFRTGFRYGDVGEDPNTVFVMYQCRGDSYWSNCRTCVTTALSGLRKRCPGNKGAIIWYDQCLFEISTVDSYHKIDYENDFYLSNPKNVSNRELFNRETSALLEKLTTKATDKKNIDGANQLVLYAAGEKRIGTKKVYAMVQCTKDLVFTTCSSCLEWIFRMYSDCCDGKQGGRVLGTSCNFRYELYPFLRN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cysteine-rich repeat secretory protein family."}
+{"protein": "MKEKQFWNRILEFAQERLTRSMYDFYAIQAELIKVEENVATIFLPRSEMEMVWEKQLKDIIVVAGFEIYDAEITPHYIFTKPQDTTSSQVEEATNLTLYNYSPKLVSIPYSDTGLKEKYTFDNFIQGDGNVWAVSAALAVSEDLALTYNPLFIYGGPGLGKTHLLNAIGNEILKNIPNARVKYIPAESFINDFLDHLRLGEMEKFKKTYRSLDLLLIDDIQSLSGKKVATQEEFFNTFNALHDKQKQIVLTSDRSPKHLEGLEERLVTRFSWGLTQTITPPDFETRIAILQSKTEHLGYNFQSDTLEYLAGQFDSNVRDLEGAINDITLIARVKKIKDITIDIAAEAIRARKQDVSQMLVIPIDKIQTEVGNFYGVSIKEMKGSRRLQNIVLARQVAMYLSRELTDNSLPKIGKEFGGKDHTTVIHAHAKIKSLIDQDDNLRLEIESIKKKIK", "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). 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaA family. SIMILARITY: Belongs to the DnaA family."}
+{"protein": "MKRLVFISFVALSMTAGSAMAQQGDVKFFGNVSATTCNLTPQISGTVGDTIQLGTVAPSGTGSEIPFALKASSNVGGCASLSTKTADITWSGQLTEKGFANQGGVANDSYVALKTVNGKTQGQEVKASNSTVSFDASKATTEGFKFTAQLKGGQTPGDFQGAAAYAVTYK", "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. SIMILARITY: Belongs to the fimbrial protein family."}
+{"protein": "MAVPGVGLLTRLNLCARRRTRVQRPIVRLLSCPGTVAKDLRRDEQPSGSVETGFEDKIPKRRFSEMQNERREQAQRTVLIHCPEKISENKFLKYLSQFGPINNHFFYESFGLYAVVEFCQKESIGSLQNGTHTPSTAMETAIPFRSRFFNLKLKNQTSERSRVRSSNQLPRSNKQLFELLCYAESIDDQLNTLLKEFQLTEENTKLRYLTCSLIEDMAAAYFPDCIVRPFGSSVNTFGKLGCDLDMFLDLDETRNLSAHKISGNFLMEFQVKNVPSERIATQKILSVLGECLDHFGPGCVGVQKILNARCPLVRFSHQASGFQCDLTTNNRIALTSSELLYIYGALDSRVRALVFSVRCWARAHSLTSSIPGAWITNFSLTMMVIFFLQRRSPPILPTLDSLKTLADAEDKCVIEGNNCTFVRDLSRIKPSQNTETLELLLKEFFEYFGNFAFDKNSINIRQGREQNKPDSSPLYIQNPFETSLNISKNVSQSQLQKFVDLARESAWILQQEDTDRPSISSNRPWGLVSLLLPSAPNRKSFTKKKSNKFAIETVKNLLESLKGNRTENFTKTSGKRTISTQT", "text": "FUNCTION: Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion. SIMILARITY: Belongs to the DNA polymerase type-B-like family."}
+{"protein": "MPPPKKFRVQSKNYFLTYPQCSLSKEEALSQLQNLNTPVNKKFIKICRELHENGEPHLHVLVQFEGKYQCTNNRFFDLVSPTRSAHFHPNIQGAKSSSDVKSYIDKDGDTIEWGDFQIDGRSARGGQQSANDSYAKALNAGSVQSALAVLREEQPKDFVLQNHNIRSNLERIFAKAPEPWVPPFQVSSFTNVPDEMQEWADNYFGTGDAAPPDRPVSIIVEGDSRTGKTMWARALGPHNYLSGHLDFNGRVFSNDVQYNVIDDIAPHYLKLKHWKELLGAQKDWQSNCKYGKPVQIKGGIPAIVLCNPGEGASYKEFLDKAENTGLKNWTIKNAIFITLTAPLYQESTQASQETGNQKAQG", "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). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the geminiviridae Rep protein family."}
+{"protein": "MASEAEKTFNRFAAFGESSSSGTEMNNKNFSKLCKDCGIMDGKTVTSTDVDIVFSKVKAKNARTITFQQFKEAVKELGQKRFKGKSPDEVLESIYGLMEGKDPATTGATKATTVGAVDRLTDTSKYTGTHKERFDESGKGKGIAGREVMNDNTGYVSGYKGAGTYDKKTK", "text": "FUNCTION: Probable regulator of microtubule dynamics required for sperm motility (By similarity). In contrast to other members of the family, has no microtubule bundling activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell projection, cilium, flagellum Note=Present in the middle piece of sperm tail. SIMILARITY: Belongs to the TPPP family."}
+{"protein": "MFLTAVLLRGRIPGRQWIGKHRRPRTVSFQAKESMIRRLEVEAENHYWLSMPYMTAEQECGHAAERRAQAFEAIKAAATSKFPKHRYIADQLDHLNISKKWS", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL63 family."}
+{"protein": "MAMNGLSKMAVAAATALLLVLTIVPGAVAVTYTIEWTTGVDYSGWATGKTFRVGDILEFKYGSSHTVDVVDKAGYDGCDASSSTENHSDGDTKIDLKTVGINYFICSTPGHCRTNGGMKLAVNVVAGSAGPPATPTPPSSTPGTPTTPESPPSGGSPTPTTPTPGAGSTSPPPPPKASGASKGVMSYVLVGVSMVLGYGLWM", "text": "FUNCTION: Probably acts as an electron carrier involved in oxygen activation and/or lignin formation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor."}
+{"protein": "MFFTKPRLHRIITHNLHHLLSPHLLLSEISGSLGDLGTLLPLLLALSLQGSIDLPSTLLFSGLFNILTGLVFGVPLPVQPMKAIAAASLQENADLETTVAAGAWVGFAVLLLGGTGGLKRVMRWVPGAVVRGVQVGAGMSLVVAAGGGMVRPLGWLWTPEENENGHGGLGEWLDSRALAVLAFGGLVVGLGQQQQQQQQSGEKPQERRKKRSKMPVQVPYALVLFLVGIMFAVVRVSLSKDSPQSPPPPPHDQPTNSAPPWTWIWNPLNHIHPKVFRSLLNPQALSMAIAQLPLTTLNSIIAASALASDLFPPDSYPQLYADDESSDSPLSPSPSASSSSLSSAPPQTPSAETPKPLSSPTSAEEGPVPLTPLSLSISAMNLLSAPFGCMPLCHGSGGLAAQHRFGARSGTSIILLGLTKFLLGLFFPGPGLLGLLGKFPKAFLGVMVLGAGVELARVGVRNVEGEEQDRMVMLMTAGTILAFKNDGVGFLAGMGCYGGFRVAAWLGGGTEKGRGGEQGLLGEEEEEEEQGRVDEESPLLR", "text": "FUNCTION: Exports stored molybdate from the vacuole into the cytosol, making it available for molybdate cofactor (Moco) biosynthesis (PubMed:36240974). Plays a role in molybdate homeostasis as high cytosolic levels of molybdate are toxic to cells (PubMed:36240974). Not required for molybdate import into cells (PubMed:36240974). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family."}
+{"protein": "MIQEIIEKKLHSELQPSYLKVINESYMHNVPPGSESHFKVIVVSDSFAGQRLIGRHRQVHQILADELDNHIHALAIHTYTDEEWKREQDGAPDSPMCMGGGH", "text": "FUNCTION: Transcriptional regulator that plays an important role in general stress response. SIMILARITY: Belongs to the BolA/IbaG family."}
+{"protein": "MSHGSGLVRTTCSSGGALGPGQPSEGLLDRVYPLTHGALFKVAQMVTLLIAFICVRSSVPIDYGAHSFFEVVTMCDLIMILIFYLVHLFRFYRVLTCISWPLSELLHYLIGTLLLLIASIVIASKSYNQSGLVAGAIFGFLASFLCLASLWLSYKITCITQSSDASA", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chemokine-like factor family."}
+{"protein": "MPQTNPFHSLVPRKMTDTELARSIRLNIEAELDAINLYAAHIDATDNEDAKAILQHVMDEEREHAALFWELIARLDPEQAAHAKEAVEKYRLITSGASHEAVEAVGKEGAAPSPADVTPEKRLTVGSLRR", "text": "FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. May help nucleate Fe atoms in the interior of the encapsulin nanocompartment (Probable). Present in about 92 copies/encapsulin nanocompartment (PubMed:25024436). SUBCELLULAR LOCATION: Encapsulin nanocompartment Note=Probably lies against the interior face of the nanocompartment. SIMILARITY: Belongs to the ferritin-like superfamily."}
+{"protein": "MLEALKPAEGATFTYIKGRLIKQQAAVENPILPFPIFFLIKQNKVFLIKSFQSSQKCEFCGDFFANSHTCSVRRRDFYFHHINFKSSEWWSQISFQPIGSCDDTKRFFLTYDVETYTWHGKHGKQLVPFMLVFHLSGELELVSLSANIAEQQRWLAWDTPHTYYYVSPIKGEIGKAFKDLRYEIQKQVTRLLWDNFVGENPELAEIQERHHVNHIDDITAEMHKIKTKGSPQFIEIYVIGHNICGFDEIVLAAQVIHNRTDVLPAFKINRNFMPRNGKILFNDISFCLPNPKYEKRKDFADWECGKLTAADHKYQFVKFMVRDTFALTHTSLRNAAGAYELPVEKGSCPYEAVNEFYRIGSYQQDEDGFPSLRYWKSSEEYQLNKALWREKNVGAYDIIQQTLHYCVQDVLVTSALVNKLQESYKNFIASQVNLPDASFNIFQRPTISSNSHAIFKQILYREVRPNKANLDNVLLAPSHEMYDYVRQSIRGGRCYPTYIGIMEQPIYVYDICGMYASALTHPFPSGQPLNPYERALAATEWIRKLENLEQKIDYFDECLLPGIFTIDADPPDELFLDELPPFCSRKGGRLCWANEPLRGEVATSIDLITLHNRGWAVRILPDERTTIFPEWKCVAKEYVQLNIGAKEKADKEKNQTMRSIAKLLSNALYGSFATKLDNKKIVFSDQLEASASKTIARGNFSIKSSSFIETDNFSAEIMPEFVVTYPPAPSAELDESDENEEHTLFIPKDSHVTYKYKPITFLETEDDDICLHTLENNSPLIENNRYASHIASFVLAWTRVFVSEWAEFLYAEDRGKPLHQRTIKSVYGDTDSLFVTEEGHRLMEQRGKHRIKKNGGKLVFDPKNPSITWLVECETQCEKCKSDAFSSESVFLAPKLYALKNTVCTCCGHVGKGKLRAKGHATTELCYDTLAKCYLSDAQQGSQRFHTSRLSLKRTLATNQSNAAPFTVTETTLTRTVRPWKDKTLVDIDGHRLMPYSKSNPNPRNNDVCWMTLPWNM", "text": "FUNCTION: Eukaryotic-type DNA polymerase involved in viral genomic replication. DNA synthesis is protein primed, and acts in a strand displacement replication. Assembles in complex with viral pTP, DBP, host NFIA and host POU2F1/OCT1 on viral origin of replication. The polymerase covalently transfers dCMP onto pTP, thereby initiating complementary strand synthesis. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the DNA polymerase type-B family."}
+{"protein": "MNTYSITLPWPPSNNRYYRHNRGRTHISAEGQAYRDNVTRIIKNAMLDIGLAMPVKIRIECHMPDRRRRDLDNLQKAAFDALTKAGFWLDDAQVVDYRVVKMPVTKGGRLELTITEMGNE", "text": "FUNCTION: Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Corrects the defects in genetic recombination and DNA repair associated with inactivation of RuvAB or RuvC (By similarity). SIMILARITY: Belongs to the RusA family."}
+{"protein": "MTRFIMLSFVTGYRKSISCNRFSRNVVSPYFFMRTIIMTRFERNFLINSLMFLETILSVDKKLDDAIHHFTQGQYENPRYQINSRITNADDWSKEDKLKFTSAIAEAIALVSEKYENPTSETTEQIQSARNILLDNYVPLLTANTDPENRLKSVRENSSQIRKELIAKLKDEVPYKSQFENPYVLFPFVAATVAVAATAASVLFGNKP", "text": "FUNCTION: Virulence effector that is indispensable for endoplasmic reticulum (ER)-mediated remodeling of the Legionella pneumophila- containing vacuole (LCV) and lysosomal evasion (PubMed:33563829). Essential for intracellular replication in human monocyte-derived macrophages (hMDMs) and amoebae, as well as for intrapulmonary proliferation in mice (PubMed:33563829). SUBCELLULAR LOCATION: Secreted Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane; Single-pass membrane protein Note=Translocated into the host cell via the type IV secretion system (T4SS) (Probable). During infection, localizes to the poles of the LCV membrane (PubMed:33563829)."}
+{"protein": "NSLVIVVGGRPCKINVHRSLVLLYNSSSLLCSGTLINQEWVLTAAHCDSKNFKMKLGVHSIKIRNKNERTRHPKEKFICPNRKKDDVLDKDIMLIRLNRPVSNSEHIAPLSLPSSPPSVGSVCYVMGWGKISSTKETYPDVPHCAKINILDHAVCRAAYTWWPATSTTLCAGILQGGKDTCEGDSGGPLICNGLQGIVSGGGNPCGQPRKPALYTKVFDYLPWIESIIAGTTTATCP", "text": "FUNCTION: Snake venom serine protease that induces platelet aggregation through activation of protease-activated platelet receptors (PAR1/F2R and PAR4/F2RL3). On F2R, the cleavage occurs at Arg41-Ser42 (like thrombin cleavage), and Arg46-Asn47. In normal condition of hemostasis, the cleavage of the Arg41-Ser42 bond liberates a new N-terminus that functions as an agonist. However after envenomation, the cleavage of Arg46-Asn47 bond degrades this potential agonist. This may explain why the snake protease is less potent than thrombin in causing platelet aggregation and release reaction. On F2RL3, a thrombin-like activity has also been proven by calcium release from lung fibroblasts transfected with this receptor. Possesses amidolytic activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
+{"protein": "MGAKQSGPAANGRTRAYSGSDLPSGTGSGGGGADGARAARFAAPVSGAQQPSASAGAAAAAAAAASAPAAPRSRSLGGAVGSASGGRAAQSAFSIPSAGGGGGPYGSQDSVHSSPEDSVGARDRDRPAGGGPGGPRLVIGSLPAHLSPHLFGGFKCPVCSKFVPSDEMDLHLVMCLTKPRITYNEDVLSKDTGECAICLEELQQGDTIARLPCLCIYHKGCIDEWFEVNRSCPEHPSD", "text": "FUNCTION: May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. 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: Endosome membrane; Peripheral membrane protein Lysosome membrane; Peripheral membrane protein Presynaptic cell membrane; Peripheral membrane protein."}
+{"protein": "MREEVLKRILLIIGAILMAIICLFPFIWMIVVSFAEDPTFLGSPLVEYKSTLENYVRVLSDPTLHFPAYLKNSIIIASLVTLTTVSISSLAAYAVSRIEFKGRLLIPIFVLGLSMFPQISLVGYLFKFIEKLGWVNTYQALYFPYVAWTLPLSLWILLSYFSQLPKDLDEAAMIDGASRIKTLTTIILPLSAPALFSTALLVFIAAFNEFMFALLFTTDHRARTVPVGIALFQGVHGEIPWGSVMAASVISTIPLVIMALLFQKYIVSGLTAGALKGE", "text": "FUNCTION: Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. 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."}
+{"protein": "MVSTSKIKSVDFYRKIPRDLTEASLSGAGLSIIAALSMIFLFGMELNNYLAVSTSTSVIVDRSADGDFLRLDFNISFPSLSCEFASVDVSDVLGTNRLNVTKTIRKFSIDSNMRPTGSEFHAGEVLSLINHGDETGEEIVEDSVPLTGRNFDTFTHQFPILVVNFYAPWCYWCNLLKPSWEKAAKQIKERYDPEMDGRVILAKVDCTQEGDLCRRNHIQGYPSIRIFRKGSDLKDDNAHHDHESYYGDRDTESLVKMVVSLVEPIHLEPHNLALEDKSDNSSRTLKKAPSTGGCRVEGYMRVKKVPGNLMVSARSGSHSFDSSQMNMSHVVNHLSFGRRIMPQKFSEFKRLSPYLGLSHDRLDGRSFINQRDLGPNVTIEHYLQIVKTEVVKSNGQALVEAYEYTAHSSVAHSYYLPVAKFHFELSPMQVLITENSKSFSHFITNVCAIIGGVFTVAGILDSILHHSMTLMKKIELGKNF", "text": "FUNCTION: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein disulfide isomerase family."}
+{"protein": "MKKLICLFAVFLMLCGRAFALDANDLLPPEKAFVPELAVADDGVNVRFRIADGYYMYQAKIVGKTDPADLLGQPSFSKGEEKEDEFFGRQTVYHHEAQVAFPYAKAVGEPYKLVLTYQGCAEAGVCYPPVDTEFDISGNGTYHPQTDEPASAKDRFLQPSSQNGSGALPPPKGDEGGDSRFKLSWDTLNANLLAFFLAGLGLSFTACMYPLLPIVSSIVVGDKKAGKARAFVLSVVYVQGLSLTYTLVGIVAGLTGALLTVWLQQAWVVLAASALMVVLALSMFGLFNIQLPNAVQSYFQNQSSRLSGGKIVSVFIMGILSALIVGPCVAPPLAFALGYIGQTGDAVLGGLALYTLALGTGVPLIAIGTFGGHILPRAGDWMNAVKYAFGFILLAVAVYLATPHLPYYLVVALYTLLMLVPACMLLVNGRRQKRRPKAVAFALGGILLIGGAWFGWQGANGKTTALHHFLTLNPPAEAGKSSEHGKMFADTAALKAAMDTALKEHPDKPVVLDFYADWCISCKEMAAYTLNQPEVHQAVDMERFFQIDVTANTPEHQALLKEYGLFGPPGVFVVRSDGSRSEPLLGFVKADKFIEWYEQNR", "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 (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily."}
+{"protein": "VQPPHSHGDNFYIWT", "text": "FUNCTION: Hydrolyzes ester bonds of tannic acid to produce gallic acid and glucose. Exhibits no cytotoxicity in vitro in Vero cells or in vivo in a rat model. SIMILARITY: Belongs to the tannase family."}
+{"protein": "MANVLCNRARLVSYLPGFCSLVKRVVNPKAFSTAGSSGSDESHVAAAPPDICSRTVWPDETMGPFGPQDQRFQLPGNIGFDCHLNGTASQKKSLVHKTLPDVLAEPLSSERHEFVMAQYVNEFQGNDAPVEQEINSAETYFESARVECAIQTCPELLRKDFESLFPEVANGKLMILTVTQKTKNDMTVWSEEVEIEREVLLEKFINGAKEICYALRAEGYWADFIDPSSGLAFFGPYTNNTLFETDERYRHLGFSVDDLGCCKVIRHSLWGTHVVVGSIFTNATPDSHIMKKLSGN", "text": "FUNCTION: Involved in cobalamin metabolism and trafficking (PubMed:18385497, PubMed:23415655, PubMed:24722857, PubMed:26364851). Plays a role in regulating the biosynthesis and the proportion of two coenzymes, methylcob(III)alamin (MeCbl) and 5'-deoxyadenosylcobalamin (AdoCbl) (PubMed:18385497, PubMed:23415655, PubMed:24722857). Promotes oxidation of cob(II)alamin bound to MMACHC (PubMed:26364851). 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 (PubMed:27771510). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion."}
+{"protein": "MPCVQAQYGSSPQGASPASQSYSYHSSGEYSSDFLTPEFVKFSMDLTNTEITATTSLPSFSTFMDNYSTGYDVKPPCLYQMPLSGQQSSIKVEDIQMHNYQQHSHLPPQSEEMMPHSGSVYYKPSSPPTPTTPGFQVQHSPMWDDPGSLHNFHQNYVATTHMIEQRKTPVSRLSLFSFKQSPPGTPVSSCQMRFDGPLHVPMNPEPAGSHHVVDGQTFAVPNPIRKPASMGFPGLQIGHASQLLDTQVPSPPSRGSPSNEGLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKSPQEPSPPSPPVSLISALVRAHVDSNPAMTSLDYSRFQANPDYQMSGDDTQHIQQFYDLLTGSMEIIRGWAEKIPGFADLPKADQDLLFESAFLELFVLRLAYRSNPVEGKLIFCNGVVLHRLQCVRGFGEWIDSIVEFSSNLQNMNIDISAFSCIAALAMVTERHGLKEPKRVEELQNKIVNCLKDHVTFNNGGLNRPNYLSKLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPAIIDKLFLDTLPF", "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). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mostly nuclear; oxidative stress promotes cytoplasmic localization. SIMILARITY: Belongs to the nuclear hormone receptor family. NR4 subfamily."}
+{"protein": "MSVNNEVSADQHNPELEDDTFEHGPPVSLGEKKSLNEYMKMDAEDESLQKWKASLGITGTGYSPSNDRRTVVILKLSLLVDGRDPVDVNMEDAASVEQIRKKGFTIKEGSEFKIGVKFRVQHEVISGLRYVQTVRRRGFVVDKTSTMIGSYGPSETPYDFTSEPDEAPTGMLARGHYEANGKFVDDDKVVHHEFVWAFDVAKSWK", "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 Nucleus. SIMILARITY: Belongs to the Rho GDI family."}
+{"protein": "MKTPLLVSHLLLISLTSCLGEFTWHRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTNDRYSMVGGNLVINNPDKQKDAGIYYCLASNNYGMVRSTEATLSFGYLDPFPPEDRPEVKVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVESSDRGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDIYTMMGQNVTLECFALGNPVPDIRWRKVLEPMPTTAEISTSGAVLKIFNIQLEDEGLYECEAENIRGKDKHQARIYVQAFPEWVEHINDTEVDIGSDLYWPCVATGKPIPTIRWLKNGYAYHKGELRLYDVTFENAGMYQCIAENAYGTIYANAELKILALAPTFEMNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTEWLVNSSRILIWEDGSLEINNITRNDGGIYTCFAENNRGKANSTGTLVITNPTRIILAPINADITVGENATMQCAASFDPSLDLTFVWSFNGYVIDFNKEITNIHYQRNFMLDANGELLIRNAQLKHAGRYTCTAQTIVDNSSASADLVVRGPPGPPGGLRIEDIRATSVALTWSRGSDNHSPISKYTIQTKTILSDDWKDAKTDPPIIEGNMESAKAVDLIPWMEYEFRVVATNTLGTGEPSIPSNRIKTDGAAPNVAPSDVGGGGGTNRELTITWAPLSREYHYGNNFGYIVAFKPFDGEEWKKVTVTNPDTGRYVHKDETMTPSTAFQVKVKAFNNKGDGPYSLIAVINSAQDAPSEAPTEVGVKVLSSSEISVHWKHVLEKIVESYQIRYWAGHDKEAAAHRVQVTSQEYSARLENLLPDTQYFIEVGACNSAGCGPSSDVIETFTRKAPPSQPPRIISSVRSGSRYIITWDHVVALSNESTVTGYKILYRPDGQHDGKLFSTHKHSIEVPIPRDGEYVVEVRAHSDGGDGVVSQVKISGVSTLSSGLLSLLLPSLGFLVFYSEF", "text": "FUNCTION: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin family."}
+{"protein": "MAPPGVGVGVAYLWGKGRGGRKGTPVVVTMESPNYSVVEVDGPDAEAELRTAAVAMDKGGGRGRSRSRTARQLTWVLLLRARRAAGRLASFAAAAARRFRRSPADAADELGRGRGRLMYGFIRGFLALSLLALAVELAAYWNGWRLRRPELHVPEAVEIEGWAHSAYISWMSFRADYIRRPIEFLSKACILLFVIQSMDRLVLCLGCFWIKLRKIKPRIEGDPFREGSGYQHPMVLVQIPMCNEKEVYEQSISAACQLDWPREKFLIQVLDDSSDESIQLLIKAEVSKWSHQGVNIVYRHRVLRTGYKAGNLKSAMSCDYVKDYEFVAIFDADFQPTPDFLKKTIPHFEGNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEVEQQVNGVFLNFFGFNGTAGVWRIQALEESGGWLERTTVEDMDIAVRAHLNGWKFIFLNDVKVLCELPESYEAYRKQQHRWHSGPMHLFWLCLPDILTAKISSWKKANLILLFFLLRKLILPFYSFTLFCVILPLTMFVPEAELPVWVICYVPVCMSFLNILPSPRSFPFIVPYLLFENTMSVTKFNAMVSGLFKLGSSYEWIVTKKSGRSSESDLSTAVERDTKDLTLPRLQKQISESELIDLKMQKERQEKAPLGAKKANKIYKKELALSLLLLTAATRSLLSAQGIHFYFLLFQGVSFLFVGLDLIGEQID", "text": "FUNCTION: Probable beta-1,4-glucan synthase rather involved in the synthesis of the xyloglucan backbone than cellulose. Seems to work simultaneously with xyloglucan 6-xylosyltransferase. Xyloglucan is a noncellulosic polysaccharides of plant cell wall and consists of a glucan backbone substituted by xylose, galactose and fucose (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant cellulose synthase-like C subfamily."}
+{"protein": "MDDCGAILHNIETKWLYDFLTLEKCRNFSQAAVSRNVSQPAFSRRIRALEQAIGVELFNRQVTPLQLSEQGKIFHSQIRHLLQQLESNLAELRGGSDYAQRKIKIAAAHSLSLGLLPSIISQMPPLFTWAIEAIDVDEAVDKLREGQSDCIFSFHDEDLLEAPFDHIRLFESQLFPVCASDEHGEALFNLAQPHFPLLNYSRNSYMGRLINRTLTRHSELSFSTFFVSSMSELLKQVALDGCGIAWLPEYAIQQEIRSGKLVVLNRDELVIPIQAYAYRMNTRMNPVAERFWRELRELEIVLS", "text": "FUNCTION: Protects cells from HOCl (hypochlorite) stress but not peroxide or diamide stress. Decreases the intracellular load of reactive oxygen species by up-regulating genes involved in methionine and cysteine biosynthesis and down-regulating Fur-regulated genes involved in iron acquisition. Has also been suggested to down-regulate expression of the flagellar regulon, decreasing motility, but this activity was not confirmed in a second study (PubMed:22223481). SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MQSLRTTLLSLLLLLLAAPSLALPSGTGRSAPAATVCPEHCDPTRCAPPPTDCEGGRVRDACGCCEVCGALEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDAKTYTNLCQLRAASRRSEKLRQPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELYRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKNRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKAVTKKKYIGIRMMSLTSSKAKELKDRHRDFPDVLSGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVTANDVSDVIKKENTLNMVVRRGNEDIVITVIPEEIDP", "text": "FUNCTION: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF- binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, but it is unclear whether it leads to the proteolytic degradation of TGF-beta proteins themselves (PubMed:18551132) or not (PubMed:14973287). By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. SUBCELLULAR LOCATION: Cell membrane Secreted Cytoplasm, cytosol Note=Predominantly secreted. Also found associated with the plasma membrane. SIMILARITY: Belongs to the peptidase S1C family."}
+{"protein": "MYTSIYITDSKKNLVFEYLLTSQAPTFQQLCSKIAGRDAAMDAMVAISKDMSLYRQAVGPEKLWYWALCQACGDPLEPQMFLAQYHQVLIEYFDKEALTVKKLVNNADRLALLLHAMLDAGEVAVTDSNRLRQLVPLRNDLSTILNSATKTLANTVKYADSKQLFGAPVATGKVEAGQTVPWRTADCRYVNNEIYVDLVETVNATLRQKGSSLTLINGSLSGKIDVKCYLSGNPTVQLKLRTSGHPLDNSALHRCVELGEAGVATMNFVPPDGRFTLAEYAIDLSAISQAARRLTNLGLVTVSLASGLGQHRDEFEIKVIIGNSTQVAAIEDLRITVYFPDISDAAKIKILRTTHGGWESDLSRVRGVWAFDKQTAVGSVPVLRGCVENPESTPHAPPVFPSHLAVSYSHVGQLPSGIRVDTIALSDLPPGSKPFKGVKYTSRAGDYIVRA", "text": "FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole (By similarity). SUBCELLULAR LOCATION: Golgi apparatus Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. SIMILARITY: Belongs to the adaptor complexes medium subunit family."}
+{"protein": "MSDHVYKIVELTGSSPNGIEEAVNNAIARAGETLRHLRWFEVVDTRGHIEGGRVNHWQVTVKVGFTLEGG", "text": "FUNCTION: May function as a riboflavin storage protein that binds and sequesters riboflavin, thereby protecting cells against undesirable reactions mediated by free riboflavin. Protects bound flavin against light damage; flavin fluorescence is rapidly quenched by interaction with Trp-39. SIMILARITY: Belongs to the dodecin family."}
+{"protein": "MNRLDHIGIAVFSIKDARSFYENVLGLAFLHQETVEEQKVNVAFFQAGSVKLELIEPLTADSPVHLFLEKKGQGLHHIAFLCNCLSEQLQALSDQHVQLIDRFPRQGANGKKIAFISPRETNGVLVELCEPKGDQHNEHE", "text": "SIMILARITY: Belongs to the methylmalonyl-CoA epimerase family."}
+{"protein": "MMSQVSHSQEGSGRFWNKFKSSTKSLSTSLAHLSIKAEKDGDTVNTTLVHKGLVKFYENQHPFQGFPGWLGEKEDLPNERKILDTQVKHDMKKQNSRHFSPSFSNRRKASSEDPMGTPSSNGNTPEYTPASKSFQDIYNNHTSSSSATPRRASSRPTRPSAGQEFRASLGRSKTSNSFNTSSTPTPPPDASSGVMAMKDRLKRRNNDYGF", "text": "FUNCTION: Involved in secretion. Component of the secretory vesicle docking complex."}
+{"protein": "MTFPLEKALDVMVSTFHKYSGKEGDKFKLNRSELKELLMRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCVAMMCNEFFEGFPDKQPRKK", "text": "FUNCTION: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (By similarity). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Modulates also the pro-apoptotic function of TP53 by binding to its C- terminal transactivation domain within the nucleus and reducing its protein levels (By similarity). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (By similarity). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (By similarity). SUBCELLULAR LOCATION: Secreted Nucleus Cytoplasm. SIMILARITY: Belongs to the S-100 family."}
+{"protein": "MEFLGDSQNHDSSETEKKNKKKKRFHRHTPHQIQRLESTFNECQHPDEKQRNQLSRELGLAPRQIKFWFQNRRTQKKAQHERADNCALKEENDKIRCENIAIREAIKHAICPSCGDSPVNEDSYFDEQKLRIENAQLRDELERVSSIAAKFLGRPISHLPPLLNPMHVSPLELFHTGPSLDFDLLPGSCSSMSVPSLPSQPNLVLSEMDKSLMTNIAVTAMEELLRLLQTNEPLWIKTDGCRDVLNLENYENMFTRSSTSGGKKNNLGMEASRSSGVVFTNAITLVDMLMNSVKLTELFPSIVASSKTLAVISSGLRGNHGDALHLMIEELQVLSPLVTTREFCVLRYCQQIEHGTWAIVNVSYEFPQFISQSRSYRFPSGCLIQDMSNGYSKVTWVEHGEFEEQEPIHEMFKDIVHKGLAFGAERWIATLQRMCERFTNLLEPATSSLDLGGVIPSPEGKRSIMRLAHRMVSNFCLSVGTSNNTRSTVVSGLDEFGIRVTSHKSRHEPNGMVLCAATSFWLPISPQNVFNFLKDERTRPQWDVLSNGNSVQEVAHITNGSNPGNCISVLRGFNASSSQNNMLILQESCIDSSSAALVIYTPVDLPALNIAMSGQDTSYIPILPSGFAISPDGSSKGGGSLITVGFQIMVSGLQPAKLNMESMETVNNLINTTVHQIKTTLNCPSTA", "text": "FUNCTION: Probable transcription factor that acts as negative regulator of trichome branching in association with HDG11 (PubMed:16778018). Seems to promote cell differentiation (PubMed:25564655). May regulate cell differentiation and proliferation during root and shoot meristem development (PubMed:25564655). Acts as positive regulator of SCL18/LAS expression (PubMed:25358340). Involved, together with PDF2, in the regulation of flower organs development by promoting the expression of APETALA 3 (AP3) in the epidermis and internal cell layers of developing flowers (PubMed:23590515). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class IV subfamily."}
+{"protein": "MAEVHRRQHARVKGEAPAKSSTLRDEEELGMASAETLTVFLKLLAAGFYGVSSFLIVVVNKSVLTNYRFPSSLCVGLGQMVATVAVLWVGKALRVVKFPDLDRNVPRKTFPLPLLYFGNQITGLFSTKKLNLPMFTVLRRFSILFTMFAEGVLLKKTFSWGIKMTVFAMIIGAFVAASSDLAFDLEGYAFILINDVLTAANGAYVKQKLDSKELGKYGLLYYNALFMILPTLAIAYFTGDAQKAVEFEGWADTLFLLQFTLSCVMGFILMYATVLCTQYNSALTTTIVGCIKNILITYIGMVFGGDYIFTWTNFIGLNISIAGSLVYSYITFTEEQLSKQSEANNKLDIKGKGAV", "text": "FUNCTION: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar (PubMed:16965264, PubMed:17599910, PubMed:31423530). Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-galactosamine (UDP-GalNAc) and UDP-alpha-D- glucuronate (UDP-GlcA), which are used by ER glucosyltransferases as sugar donors for the synthesis of sugar chains of glycoproteins, glycolipids and oligosaccharides (PubMed:11322953, PubMed:16965264, PubMed:17599910, PubMed:31423530, PubMed:17952091). May couple UDP- GlcNAc or UDP-GalNAc efflux to UDP-GlcA influx into the ER lumen that in turn stimulates glucuronidation and subsequent excretion of endobiotics and xenobiotics (PubMed:16965264, PubMed:17599910). Plays a role in chondroitin sulfate biosynthesis, which is important for formation of cartilage extracellular matrix and normal skeletal development (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily."}
+{"protein": "MPSSPLRVAVVCSSNQNRSMEAHNILSKRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYTQNGILHMLDRNKRIKPRPERFQNCTDLFDLILTCEERVYDQVVEDLNSREQETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEEKSGRAFLHTVCFY", "text": "FUNCTION: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Predominantly in the cytosol. SIMILARITY: Belongs to the SSU72 phosphatase family."}
+{"protein": "MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLRDGEREGWGEISPLPGFSQETWEEAQTALLTWVNDWLQGNEGLPEMPSVAFGASCALAELTGILPEAADYRAAPLCTGDPDDLVLRLADMPGEKIAKVKVGLYEAVRDGMVVNLLLEAIPDLHLRLDANRAWTPLKAQQFAKYVNPDYRARIAFLEEPCKTRDDSRAFARETGIAIAWDESLREADFTFEAEEGVRAVVIKPTLTGSLDKVREQVAAAHALGLTAVISSSIESSLGLTQLARIAAWLTPGTLPGLDTLHLMQAQQIRPWPGSALPCLKREELERLL", "text": "FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- carboxylate (SHCHC) to 2-succinylbenzoate (OSB). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 1 subfamily."}
+{"protein": "MPYKRKLTSYFPQSKRFRGAKSGMAVVKTSASRRLYKKGKRKPDRIKTYTYAFSSICTDKGTIVYMNSWSLGLGPQQRSSDIEILKSMYIRLTVALSENAASQVKTYVVKWALIVDQVPGETLVGVADVYKTCPSPYPYVQCAYIADDNHSRFQVLRSGFLSLSGNGLAVGSSTRTGCPAMKNMASINKFCKNLNVRCVYDADSATGDIASIKRGAVYLVIWPDVEIRYGFSCTMYHRNGNA", "text": "FUNCTION: Encapsidates the viral genome into characteristic twinned ('geminate') particles. Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus. Plays a role in protection of the genome from degradation, virus acquisition and transmission by insect vectors, infectivity, and systemic movement. The CP of monopartite geminiviruses is absolutely essential for virus movement (By similarity). 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": "MSAATTADIDHYRTVLAGAFDDQVLEWTREAEARQRFPRELIEHLGARGVFSEKWCGGMLPDVGKLVELARALGRLSSAGIGVGVSLHDSAIAVLRRFGKSDYLRDICERAIAGQAVLCIGASEESGGSDLQIVRTEMSSRDGGFDIRGVKKFVSLSPIADHIMVVARSIDHDSASKHGNVALIAVPTSQASVQRPYAKVGAGPLDTAAVHIDTWVPADALVARAGTGLAAISWGLAHERMSIAGQIAASCQRAIGITLARMMTRRQFGRTLFEHQALRLRMADLQARVDLLQHGLNGIAAQGRLDLRAAAGVKVTAARLGEEVMSECMHIFGGAGYLVEETPLGRWWRDMKLARVGGGTDEVLWELVAAGMAADHGGYRSVVGASSA", "text": "FUNCTION: Catalyzes the dehydrogenation at the alpha-beta position of ACP-bound acyl chains. This results in the introduction of a double bond in the lipidic chain, which is further transferred to the epsilon- amino group of lysine residue in the mycobactin core by MbtK (By similarity). SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
+{"protein": "MENHLPNIFYFPNCVTAFPYRYTQKELDDMKPVDRERFKYAVFPLIKHRWCRAYVVRDNHTFKLNVETSKRLRRVAYPTLVPLVGVNAALREYVMEDGTKISFECYSYLICKRTTSLHDVDDSTIRGLVEGGNQLNIFTNSVGSVTNTVGIFGNPNPFAKVPLKSLHPSMQCKIFTSWARRVPVVLTGDTGVGKTSQVPKLLLWFNYLFGGFTDLSTLTFEVQEKPIVLSLPRVALVKLHSETLLTSLGFEEIHGSPVSLKFGNMQERFVNTRFSRYGIVFSTHKITLNTLFKYSTVILDEVHEHDQTGDIIIAVCRKYIRKLDSLFLMTATLEDDRRRIEEFFAESVFVHIPGGTLFSISEAYVKNSNDPLNRFMYIEEEKRNLANAIKTYTPPKQSSGIVFVSTVSQCEAYKQYLSERLPYKFYIIHGKVQNINDVLSDIYDNDGVSIIISTPYLESSVTVRNATHVYDTGRVYIPSPYGGCESFISKSMRDQRKGRVGRVNPGMYVYFYNVSELRPIKRIDFEFLHNYVLYAKVFDLQLPEDLFVKPTNVTRLHDVIEYIRSFDISDDVWTRLLSSYYIHILEYAKVYARGGSGALALDSFERTGNLTDDALDAIKSLNMRAKILSHKKASAHTYALRCKLLFGVYAGKVFTVYHKRPLTGYITMIAEHSFIPDY", "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. SUBCELLULAR LOCATION: Virion Note=Localizes to the virion core. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily."}
+{"protein": "MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPEGAVQQKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADLTASISACNGLKGHFMLQGEMYLIEPLKLSDSEAHAVFKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQSNLTPEQQRYLNAPKFVKLFLVADNIMYLKYGRSLTNVRTRMYDMANILNLIFRRMNIHVAVTDLEIWSDKDKIIVQPSADDTLKSFATWRESVLLKHKSHDNAQLLTGINFNGPTAGLAYLGGICDPMYSTAIVQDHNKIHHLVAIAMAHEMGHNLGIDHDKDTCTCAAKSCVMAGTLSCEASYLFSDCSRKEHRAFLIKNMPQCILKKPSKTDVVSPPVCGNYFVEMGEDCDCGSPATCRDPCCDAATCKLKQGAQCAEGLCCDQCRFKGAGTQCRAAMDECDMADLCTGQSADCTDRFQKNGQPCQNNNGYCYNGTCPTMIKQCTVFFGSNAAVSQDACFQFNLQGNNYGYCRKEQNTKIACEPQNVKCGRLYCTSPEKQNPCNIYYSPSNEDKGMVLPGTKCADGKACSNGQCVDVTTPY", "text": "FUNCTION: Strongly inhibits the collagen-induced human platelet aggregation. Hydrolyzes the Aalpha-chain of fibrinogen (FGA), without cleavage of Bbeta- and gamma-chains. Induces apoptosis and strongly inhibits proliferation of endothelial cells as well as adhesion of the cells to extracellular matrix proteins (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIc sub-subfamily."}
+{"protein": "MTKKVAIILSNEFEDIELTSPKEAIEEAGFETEIIGDTANAEVVGKHGEKVIVDVSIADAKPEDYDGLLIPGGFSPDHLRGDAEGRYGTFAKYFTKNDVPAFAICHGPQILIDTDDLNGRTLTAVLNVRKDLSNAGANVVDESVVVDKNIVTSRTPDDLDDFNREIVKQLQA", "text": "SIMILARITY: Belongs to the peptidase C56 family."}
+{"protein": "MTVATPNLTTVPVPPSDSRERVKQFMQTLQDEICAGLEALDGGGQFREDSWERPEGGGGRSRVIREGNVFEQGGVNFSEVWGEKLPPSILAQYPEAAGHGYFATGTSMVLHPRNPYIPTVHLNYRYFEAGPVWWFGGGADLTPYYPFAEDAKHFHSSFKAACDRHYPQFYDVFKLWCDEYFFLKHRGETRGIGGIFFDYQDGRGDLYNKGPAPSGPAGQKAAEVGIVSDLNWEKLFAFAQDCGRTFLPAYSPIVERRKDTPWGDRERQFQLYRRGRYVEFNLVYDRGTIFGLQTNGRTESILMSLPPLVRWEYMYQPEAGSREQELYDVFLKPQDWVNWPTA", "text": "FUNCTION: Involved in the heme and chlorophyll 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": "MAAPAAAAVEEGMEPRALQYEQTLMYGRYTQDLGAFAKEEAARIRLGGPEPWRSPPSPRTPPELLEYGQSRCARCRMCSVRCHKFLVSRVGEDWIFLVLLGLLMALVSWAMDYAIAACLQAQQWMSRGLNTNLLLQYLAWVTYPVVLITFSAGFTQILAPQAVGSGIPEMKTILRGVVLKEYLTLKTFVAKVIGLTCALGSGMPLGKEGPFVHIASMCAALLSKFLSLFGGIYENESRNTEMLAAACAVGVGCCFAAPIGGVLFSIEVTSTFFAVRNYWRGFFAATFSAFIFRVLAVWNRDEETITALFKTRFRLDFPFDLQELPAFAVIGIASGFGGALFVYLNRKIVQVMRKQKTINRFLMRKRLLFPALVTLLISTLTFPPGFGQFMAGQLSQKETLVTLFDNRTWVRQGLVEELEPPSTSQAWSPPRANVFLTLVIFILMKFWMSALATTIPVPCGAFMPVFVIGAAFGRLVGESMAAWFPDGIHTDSSTYRIVPGGYAVVGAAALAGAVTHTVSTAVIVFELTGQIAHILPVMIAVILANAVAQSLQPSLYDSIIRIKKLPYLPELGWGRHQQYRVRVEDIMVRDVPHVALSCTFRDLRLALHRTKGRTLALVESPESMILLGSIERTQVVALLAAQLSPARRRQSKQKRRVAHTSPPSCQESPPSPETSVCFQVKAEDAQGEPHKPLKPALKRGCSNSVNLGESPTGHVESAGIALRSLFCGSPPPEAASESEKSESSEKRKSKRVRISLASDSDLEGEMSPEEILEWEEQQLDEPVNFSDCKIDPAPFQLVERTSLHKTHTIFSLLGVDHAYVTSIGRLIGIVTLKELRKAIEGSVTAQGVKVRPPLASFRDSATSSSDTETTEVHALWGPRSRHGLPREGSPSDSDDKCQ", "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 (By similarity). 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 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC- 2/CLCN2 subfamily."}
+{"protein": "MMPGLKLYGALILCVLVLPFSRPSSQVLDCREVRSSFQFLYPGMKWTPETPVSGSDLQVCQPKGLTCCSRKMEERYLLIAKQNMESSLQATSAQLKGLIIQNAALFQEAFDMVLRLGRNSTLMVLREEFPGLGAGASGAVTQLFLDMSLYILGSDANVNDMVSTFFSRLFPLTYRRLLGNGAVAGISEECLRGAWKGSSAYGSFPKMMMTRLSRSLLATRVFLQALNLGIEVVNTTQHLRAGRDCGRSLLKLWYCPHCQSLLEARPCRPLCVSTMGACLGGTTEVQPHWRAYVDELGSLAAAMKGEQDIEAVVLRLHVIIRQALKQAVASKSKVSAQVSGMCVHAPPRVSRAVPVSAEHTSASTVNHNRPPMNFDPDETLFGRRREFISGLRGFSQFYSGLGEALCSKEPTSLNSSLCWNGQEMTDKFPGPGLKRVHPHGSESKQKTPEPVISQIIDKLKHINQLLRMVTLPEKRWRARQGGGGARRNPSGPGQTDEDEEGLESGDCDDEDECTGVSGLGPPPRRKRLRIFADLADNLAIDDLTLHELLLTPRLATDAHGGSSIPGAAHVPTAAFIFTITIIIFITLGLQ", "text": "FUNCTION: Cell surface proteoglycan (By similarity). Negatively regulates the hedgehog signaling pathway (By similarity). Positively regulates the canonical and non-canonical Wnt signaling pathways (By similarity). Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (By similarity). Inhibits the dipeptidyl peptidase activity of DPP4 (By similarity). Plays a role in limb patterning and skeletal development (By similarity). Modulates the effects of growth factors on renal branching morphogenesis (By similarity). Required for coronary vascular development (By similarity). Plays a role in regulating cell movements during gastrulation (PubMed:14610063). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. SIMILARITY: Belongs to the glypican family."}
+{"protein": "MQLFPVMLATLCIVLQLLIGSSALATTNRHVSNSHWLPAVATWYGSPNGDGSDGGACGYGTLVDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPGCSKTSTHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRRTACKYRGKNIAFHVNEGSTDFWLSLLVEFEDGEGDIGSMHIRQAGAREWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSAGKTLSATDVVPRNWAPKATYSSRLNFSPVL", "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 (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin B subfamily."}
+{"protein": "MRRAVGFPALCLLLNLHAAGCFSRNNDHFLAIRQKKSWKPVFIYDHSQDIKKSLDIAQEAYKHNYHSPSEVQISKHHQIINSAFPRPAYDPSLNLLAESDQDLEIENLPIPAANVIVVTLQMDITKLNITLLRIFRQGVAAALGLLPQQVHINRLIEKKNQVELFVSPGNRKPGETQALQAEEVLRSLNVDGLHQSLPQFGITDVAPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFIIIVTCLMIIYRLKERLQLSLRQDKEKNQEIHLSPIARQQAQSEAKTTHSMVQPDQAPKVLNVVVDPQGQCTPEIRNSTSTSVCPSPFRMKPIGLQERRGSNVSLTLDMSSLGSVEPFVAVSTPREKVAMEYLQSASRVLTRSQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNITDSLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVTGVTECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHALCLFESRLSPETVE", "text": "FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus. Isoform gamma may have a role in patterning and cellular proliferation of skeletal elements in the precartilaginous/cartilaginous skeleton. SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm. Note=Locates to the areas within the cytoplasm. SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm. Note=Locates to the areas within the cytoplasm. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Receptor class 7 subfamily."}
+{"protein": "MGKHRRNNSNATRKAVAASAVALGATAAIASPAQAAEVVVPGTGISVDIAGIETTPGLNNVPGIDQWIPSLSSQAAPTAYAAVIDAPAAEAQAAPAASTGQAIVDAARTKIGSPYGWGATGPNAFDCSGLTSWAYSQVGKSIPRTSQAQAAQGTPVAYSDLQAGDIVAFYSGATHVGIYSGHGTVIHALNSSTPLSEHSLDYMPFHSAVRF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C40 family."}
+{"protein": "MALETVPKDLRHLRACLLCSLVKTIDQFEYDGCDNCDAYLQMKGNREMVYDCTSSSFDGIIAMMSPEDSWVSKWQRVSNFKPGVYAVSVTGRLPQGIVRELKSRGVAYKSRDTAIKT", "text": "FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences. FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SPT4 family."}
+{"protein": "MSSLVTLNNGLKMPLVGLGCWKIDKKVCANQIYEAIKLGYRLFDGACDYGNEKEVGEGIRKAISEGLVSRKDIFVVSKLWNNFHHPDHVKLALKKTLSDMGLDYLDLYYIHFPIAFKYVPFEEKYPPGFYTGADDEKKGHITEAHVPIIDTYRALEECVDEGLIKSIGVSNFQGSLIQDLLRGCRIKPVALQIEHHPYLTQEHLVEFCKLHDIQVVAYSSFGPQSFIEMDLQLAKTTPTLFENDVIKKVSQNHPGSTTSQVLLRWATQRGIAVIPKSSKKERLLGNLEIEKKFTLTEQELKDISALNANIRFNDPWTWLDGKFPTFA", "text": "FUNCTION: Aldose reductase with a broad substrate specificity. Reduces the cytotoxic compound methylglyoxal (MG) to acetol and (R)- lactaldehyde under stress conditions. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation (PubMed:11525399). In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction (Probable) (PubMed:11722921). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MANKQDLIAKVAEATELTKKDSAAAVDAVFSTIEAFLAEGEKVQLIGFGNFEVRERAARKGRNPQTGAEIEIAASKVPAFKAGKALKDAVK", "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. 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 (By similarity). SIMILARITY: Belongs to the bacterial histone-like protein family."}
+{"protein": "ADVSYGINKDCLLPMDVGRCRAKFPRYYYNSSSRRCEKFNYGGCRGNANNFHTLEECEKVCGVRSRDSPKEN", "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": "MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL", "text": "FUNCTION: Binds to acetylcholine. Modulates neuronal synaptic transmission. SUBCELLULAR LOCATION: Synaptic cleft Note=Released in an acetylcholine-dependent manner in the synaptic cleft. SIMILARITY: To the extracellular portion of ligand-gated ionic channels family."}
+{"protein": "MASIGSQVRKAASSIDPIVTDYAVGYFNHLSGITFDAVQSKQVDLSTEVQFVSDLLIDAGASKAKVKELSESILKQLTTQLKENEAKLELTGDTSKRLLDINVLKSHNSKSDINVSLSMLGVNGDIEHTGRKMETRVDLKKLAKAEQKIAKKVAKRNNKFVKYEASKLINDQKEEDYDSFFLQINPLEFGSSAGKSKDIHIDTFDLYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHVEQELRGDDTKALQSVLDADVWRKQLLSEEAKINERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLDYYRGQDFDTFYTTKEERRKNAQREYDNQMVYRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPVLEPPEQDKTIDFKFPECDKLSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGTIYDYRDYILQSADAAGVVKKH", "text": "FUNCTION: Acts as a positive activator of the GCN2 protein kinase activity in response to in response to low amino acid, carbon, or purine availability (PubMed:7621831, PubMed:10733573). Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN20 helps GCN1 to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:10775272, PubMed:15722345). Participates in gene-specific mRNA translation activation, such as the transcriptional activator GCN4, by promoting the GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4- mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:15722345). SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily."}
+{"protein": "MKSLLFTLAVFMLLAQLVSGSWYVKKCLNDVGICKKKCKPEELHVKNGWAMCGKQRDCCVPADKRANYPAFCVQTKTTRTSTVTATTATRATTATTTTLMMTTASMSSMTPTPVSPTG", "text": "FUNCTION: Highly glycosylated atypical beta-defensin involved in several aspects of sperm function. Facilitates sperm transport in the female reproductive tract and contributes to sperm protection against immunodetection; both functions are probably implicating the negative surface charge provided by its O-linked oligosaccharides in the sperm glycocalyx. Involved in binding of sperm to oviductal epithelial cells to form a sperm reservoir until ovulation. Release from the sperm surface during capacitation and ovaluation by an elevation of oviductal fluid pH is unmasking other surface components and allows sperm to penetrate the cumulus matrix and bind to the zona pellucida of the oocyte. In vitro has antimicrobial activity and may inhibit LPS- mediated inflammation (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted by epididymal cells and is absorbed to the surface of sperm during transit through the epididymis. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "MKFFQAAALLLAMFAALANAEPVPQPGTVLIQTDNTQYIRTG", "text": "FUNCTION: Peptide which plays a role in the humoral immune response to a subset of filamentous fungi, including F.oxysporum and F.verticillioides. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAD", "text": "FUNCTION: 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. Thus, functions as a protein deglycase that 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 Schiff bases and advanced glycation endproducts (AGE). 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. Plays an important role in protecting cells from carbonyl stress. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C56 family. HchA subfamily."}
+{"protein": "MAQFPLFQKFQKAIQHPPALSLGLPIFLTVIFLLSQRYVWIEDDLELRSTALTNFELNRISFYPLVHATWFHLLLNLVALQPIVSQFERVNGTVRTGIVLNILAVVTAIPWCLLSIGFFPDEAVLGSSAWIFSFMGYWAIRESSKQPTTQLAPNLVVPTWLLPIIYLVVIAIVIPSSSFIGHLLGLIAGWMMALGYLDVLIEPSSKVVLWIENKISRVIDLIPSSIVTFYREEGALDTRAAARADTNRSLSVSGGNFLGFQANSSQADLEAGTRSRGNSSVDPTTSFPGTGQTLGTQ", "text": "FUNCTION: Probable serine protease. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase S54 family."}
+{"protein": "MIDENFKKKLAVSRERVEDLFYFENSKEIGRGTYGLVYKAVPKHSNGRFPNKEYALKMIEGQGFSMSACREIALFRELRHPNLICLQRVFLTNEKKVWLLLDYAEHDLWHVIKHHRTAKTKKVPIMVPRNMVKNILFQILSGMHYLHSNWVLHRDLKPANILLMGDGGPDMRGRVKIADLGFSRIFANPLKPMAELDPVVVTFWYRAPELLLGAKHYTKAIDVWAIGCIFAELLTAEPLFFCKEEDIKAQNPYHYDQVKRIFHLLGYPSDTDWPDMKKMPDHQRLLNDARNEGTPIQTFPNSLQRYFDKWKINSQSSPYRLLVKLLTVDPLKRVSCEEAMNDIYFRKMERPPRETDDVFNRYPIPYAKKEQQITIPIDQFQQQQQQQQQQQQQQQQQQQQQQQQQMQQPQIGPPQMMGQPQMGQPQMGQPQMGQPQMGQPQMGQPQMVPSQMGQPPMGGPHPGVVAPDGHAHQMMQQQHQSQHHMQYQQMHDSMQGGMDDGGPQAKMMRMGNVPVGRYGPMGPPYGPQDFHAPQGPPMMQMMPQPGPSGYYQQRPGQPPGPGPQGYMNPQMGMTMGMRPQGVPQQAYMPGRGMPPPQGPNPQQQQQWQQYHR", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in regulated gene 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 pre-initiation complex with RNA polymerase II and the general transcription factors. Phosphorylates the CTD (C- terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "MYFLSLPSLVIVIPVGYLLFHLGYNLFFHPLRGYPGPLLWRASSLPWKIALLRGTMHHDLMRFHQKYGDTVRIKPDEISYANAQAWRDIHAHVPGRPEFLKDPVRLPLAPNGVMSILVSDTKNHARFRSLFGHAFSDKGLRTQESTIVQYADLLVEVLREVADTGRSAEMVYYFNMAIFDSIGALSFGESFDSLKSRQLHPWVDAIHKNLKSVAISHVLRSMGIEFLTPYVLPKELRGKRQENYSYAVEKLNKRMKMEGDQGDFWDKVLVKSADDNQRGDGMSAGEMLNNAAVMVVAGSETTASALSGAMYLLCLSGKIEKATAEIRKSFASPEDIDLISVSHLPYLTAVIDETLRMYPAVPGQPPRVVPASGATVCGRFVPEETRVGVSHLATYFADYNFTHADKFIPERHLQKTEEPFKYDNYGAYQPWSVGLRNCIGRNLAYAEVRLTLAKLLWHFDFTLDVDKTGNFLDQKIWSIWAKRELYMFIKTRGTSSSSPQ", "text": "FUNCTION: Versicolorin B desaturase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:15094053, PubMed:8368837, PubMed:15006741). The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). Within the aflatoxin pathway, the versicolorin B desaturase aflL catalyzes the conversion of versicolorin B (VERB) to versicolorin A (VERA) (PubMed:8368837, PubMed:15006741). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'- hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'- oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 (PubMed:15006741). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MSKNTVSSARFRKVDVDEYDENKFVDEEDGGDGQAGPDEGEVDSCLRQGNMTAALQAALKNPPINTKSQAVKDRAGSIVLKVLISFKANDIEKAVQSLDKNGVDLLMKYIYKGFESPSDNSSAMLLQWHEKALAAGGVGSIVRVLTARKTV", "text": "FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). 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 (PubMed:29925947). 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) (PubMed:29925947). 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 Cell projection Nucleus. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection Nucleus. SIMILARITY: Belongs to the ARPC5 family."}
+{"protein": "MKTLLLTLVMVTIMCLDLGYTLTCYKGYHDTVVCKPHETICYEYFIPATHGNAILARGCGTSCPGGIRPVCCRTDLSNK", "text": "FUNCTION: Binds with high affinity to muscle nicotinic acetylcholine receptor (nAChR) and hinders acetylcholine binding to the receptor, thereby impairing neuromuscular transmission. Causes muscle paralysis, spasms and increased respiration. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type III alpha-neurotoxin sub-subfamily."}
+{"protein": "MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKTLDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQEEARRRRRQEQSPWNPRAGLDPRE", "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 (By similarity). 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": "MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNFVREIKKDMKKDLLSNKAPEKPMHDVSSGNALLSSETILRTNKRGERRRRRCQVAFSYLPQNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQLSKSRPEGFLPASLLPFPAHGAKGKTTFEGTILYRAAPGKTEGHRRYYSLRETTGSESDGGDSSSTKSEGANGTMATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEKTIGKKLPPATSTPDPSKTEMDSRTKTKDYCKVIFPYEAQNDDELTIKEGDIVTLINKDCIDVGWWEGELNGRRGVFPDNFVKLLPSDFDKEGNRPKKPPPPSAPVVKQGAGTTERKHEIKKIPPERPETLPNRTEEKERPEREPKLDLQKPSVPAIPPKKPRPPKTNSLNRPGALPPRRPERPVGPLTHTRGDSPKIDLAGSALSGILDKDLSDRSNDIDLEGFDSVISSTEKLSHPTTSRPKATGRRPPSQSLTSSSLSSPDIFDSPSPEEDKEEHISLAHRGIDVSKKTSKTVTISQVSDNKTSLPPKPGTMAAASSGPASLSSVASSPMSSSLGTAGQRASSPSLFSTEGKPKMEPAVSSQAAIEELKMQVRELRTIIETMKDQQKREIKQLLSELDEEKKIRLRLQMEVNDIKKALQSK", "text": "FUNCTION: Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may be inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3- kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration (By similarity). Has an essential role in the stimulation of B cell activation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cytoplasmic vesicle membrane; Peripheral membrane protein Synapse, synaptosome Cell junction, focal adhesion Note=Localized in endocytic vesicles containing clustered receptors. Colocalizes with ASAP1 in vesicular structures. Colocalized with actin microfilaments and focal adhesions (By similarity). Colocalized with MAGI2 in synaptosomes (By similarity). Translocation to EGFR containing vesicles upon EGF stimulation is inhibited in the presence of SH3KBP1 (PubMed:21830225). Colocalizes with ZFP36 in the cytoplasm (By similarity)."}
+{"protein": "GVDKPGCRYMFGGCVQDDDCCPHLGCKRKGLYCAWDGT", "text": "FUNCTION: Paralytic toxin that inhibits insect voltage-gated sodium (Nav) and calcium (Cav) channels in P.americana (American cockroach) dorsal unpaired median (DUM) neurons, and inhibits the B.germanica (German cockroach) Nav channel (BgNaV1) (PubMed:28475112). Also shows a delay in fast inactivation when tested on 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": "MNALLTNPFKERLRKGEVQIGLWLSSTTAYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAVAPYASHPVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTADQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQVNDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADLSASLGYPDNAGHQEVQRIIETSIRRIRAAGKAAGFLAVAPDMAQQCLAWGTNFVAVGVDTMLYSDALDQRLAMFKSGKNGPRVKGSY", "text": "FUNCTION: Catalyzes the reversible retro-aldol cleavage of 2-keto-3- deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde. SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDR aldolase subfamily."}
+{"protein": "MGTEKESPEPDCQKQFQAAVSVIQNLPKNGSYRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYITEMKLVAQKVIDTVPLGEVAEDMFAYFEPLYQVIPDMPRPPETFLRRVTGWKEQVVNGDVGAVSEPPCLPKEPAPPSPESHSPRDLDSEVFCDSLEQLEPELVWTEQRAASGEKRDPRNSPVPPTEKEAAAQAQCSAMAPWAPRARAALLPPVALRRPVALPNVSDPKEVTVSGGVSAAN", "text": "FUNCTION: Binds medium- and long-chain acyl-CoA esters and may function as an intracellular carrier of acyl-CoA esters."}
+{"protein": "SLFELGKMILQETGKNPAKSYGAYGCNCGVLGRGKPKEATQRCCYVHKCCYKKLTGCDPKKDRYSYSW", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that lacks enzymatic activity. Is myotoxic, induces edema, and causes systemic effects (renal changes that lead to proteinuria) on mice (PubMed:29170054). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (By similarity). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (By similarity). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (By similarity). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (By similarity). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily."}
+{"protein": "MSKAHPPEVKKYMDKRMMLKLNGGRAVTGILRGFDPFMNVVLDDTVEECKDNTKNNIGMVVIRGNSIVMVEALDRV", "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:18621711). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome (By similarity). 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 Sm proteins family."}
+{"protein": "SVAVAGAVIEGASLTFNVLQ", "text": "FUNCTION: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and 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. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects. 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": "MSAITRIIDKIGIVGTIVGSFSCAMCFPAAASLGAAIGLGFLSQWEGLFVQWLIPIFASVALLATLAGWFSHRQWQRTLLGSIGPVLALVGVFGLTHHFLDKDLARVIFYTGLVVMFLVSIWDMVNPANRRCATDGCETPAPRS", "text": "FUNCTION: Involved in mercuric ion uptake. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MLGLRRSATTLFDISQSLLRNVTFHGLRVQGIRVGNAEVPNNKPLKTGLQEVYGIGRRKSHQVLCHLGITNKLARDLTGKELIDLREEVGQHQHGDELRRRVGSEIQRLVEVDCYRGSRHRHGLPCRGQRTSTNARTKKGKAVAIAGKKKAPRK", "text": "FUNCTION: Located at the top of the head of the small subunit, it contacts several helices of the 18S rRNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS13 family."}
+{"protein": "MALNIASIRDTKWLTLEVCRQFQRGTCSRSDEECKFAHPPKSCQVENGRVIACFDSLKGRCTRENCKYLHPPAHLKTQLEINGRNNLIQQKTAAAMLAQQMQFMIPSTTMQHVQTFPVNQGLGSSAGLSYTPYLTPMSHSMGLVPTDILPSTPVIVPGSPPVSVTAGSSSNQKLLRTDKLEVCREFQRGNCARGETDCRFAHPSDSPMIDTSDNTVTVCMDYIKSRCSREKCKYFHPPAHLQAKVKAAQHQANQTAVAAQAAATAAAMTQSTAKAMKRPLEATVDLAFPHSGLQPLPKRPALEKSNGSSSLFNPSVLHYQQALANAQLQQPAFFPTGSVLCMTPASSLGRS", "text": "FUNCTION: Involved in pre-mRNA alternative splicing regulation. RNA- binding protein that binds to 5'ACACCC-3' core sequence (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the muscleblind family."}
+{"protein": "MRSPWADDVEYQKDPLFLNYEKRIWDNSTNQTTFSWHKDTREIASSSILALALVHDVWGPVIAACSIDARWAASDIYVIPTNSTVVFSNTTDSLMESLRHSNQGNREANIAKYGLSRNPIDIQLEWAEKLNRKYIFDLSVKPSQRMKAAPNEEINAIETFLMDIIPSMRVDPSVSTLLGLIVSDSISRTINTTRAPWGMVEEVDSNGSWNYSEVVRNSGNENRPNPDDDNGYVMRVIADRYGYGFALRVRFGVLYLESLPNGLVPIGDIFVLVWDLN", "text": "FUNCTION: 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). 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:28605916). These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing polyketide synthase clz14, followed by oxaloacetate extension and product release to generate a tricarboxylic acid containing product (PubMed:28605916). The phenylalanine ammonia lyase (PAL) clz10 and the acyl-CoA ligase clz12 are involved in transforming phenylalanine into benzoyl-CoA (PubMed:28605916). The citrate synthase-like protein clz17 is involved in connecting the C-alpha-carbons of the hexaketide chain and oxaloacetate to afford the tricarboxylic acid unit (PubMed:28605916). The potential hydrolytic enzymes, clz11 and clz13, are in close proximity to pks2 and may participate in product release (PubMed:28605916). On the other side, the tetraketide arm is synthesized by a the squalestatin tetraketide synthase clz2 and enzymatically esterified to the core in the last biosynthetic step, by the acetyltransferase clz6 (By similarity). The biosynthesis of the tetraketide must involve 3 rounds of chain extension (By similarity). After the first and second rounds methyl-transfer occurs, and in all rounds of extension the ketoreductase and dehydratase are active (By similarity). The enoyl reductase and C-MeT of clz2 are not active in the final round of extension (By similarity). The acetyltransferase clz6 appears to have a broad substrate selectivity for its acyl CoA substrate, allowing the in vitro synthesis of novel squalestatins (By similarity). The biosynthesis of SQS1 requires several oxidative steps likely performed by oxidoreductases clz3, clz15 and clz16 (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) clz20, suggesting a likely mechanism for self-resistance (Probable)."}
+{"protein": "MIKPCAYEKQGLIDHAIGSYRVLDGKISESYYKIISRRLERYGIVLDLNGVKEMVKDVVVLHDMGKAGEYYQNQFDDNCNPLKSNFSFIYHELGSALFFYYDYEPIDVEKAEEVKSLLTLAVLNHLNAIRVISDYLVNKFPDNFDERMIKLNKYGSIMLQNLRGVISKSLKVRDYTFDDYHDMLYAFSKKSDKYLKLYNLFLAPIMLGDNLDSSLVRNNGSKTGFVRILEGELNGGSTL", "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). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Acts as a dsDNA and dsRNA endonuclease (in a fusion with Alicyclus caldarius esterase to increase solubility). SIMILARITY: Belongs to the CRISPR-associated nuclease Cas3-HD family."}
+{"protein": "MVTFNCEVCNDTVPKKNTEKHYYRCPNAYYTCIDCSKTFEDGVSYKNHTSCISEDEKYQKALYKGNKKQKQKQQQKQQQKQHQHQPVATPAKKVEKPVIKKAEKVEKTSNGIELHKGKSLYKILKTMKDKGAKKTFLKSLVVDSEGQIRYAKE", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UPF0743 family."}
+{"protein": "GVRDAYIADDKNCVYTCASNGYCNTECTKNGAESGYCQWIGRYGNACWCIKLPDEVPIRIPGKCR", "text": "FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels. The toxin affect mammalian sodium channels Nav1.7/SCN9A (EC(50)=4.5 nM), Nav1.4/SCN4A (EC(50)=9.6 nM), Nav1.6/SCN8A (EC(50)=30 nM), Nav1.5/SCN5A (only at micromolar concentrations), and insect sodium channel para/tipE (EC(50)=80 nM) (PubMed:16038905, PubMed:16641312, PubMed:23527544). In vivo, intraplantar administration of this toxin elicits pain behaviors, including licking and flinching of the hind paw (PubMed:26999206). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
+{"protein": "MVLGWPLLLVLVLCPGVTGIKDCVFCELTDSARCPGTHMRCGDDEDCFTGHGVAQGVGPIINKGCVHSTSCGREEPISYMGLTYSLTTTCCSGHLCNKGTGLSTGATSLSLGLQLLLGLLLLLQYWL", "text": "FUNCTION: Sperm surface membrane protein that may be involved in sperm- egg plasma membrane adhesion and fusion during fertilization. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Cytoplasmic vesicle, secretory vesicle, acrosome Note=Expressed in acrosomal matrix and outer and inner acrosomal membranes. SIMILARITY: Belongs to the SPACA4/bouncer family."}
+{"protein": "MAEREQSNDSARTDVPAIVSLRTRELDTGEGRMQWASTLERLYCETDVAWPEPRRHFDAEWGGRPFGDLHVSTIRADAHTVVRSPAMIQSDSGEGYLVCLVTDGSVEVRQSGRATVVEPGSFALLDCAAPFVFHSPAPFRQVVVRSPREVLTSRLPGRIVEHGTARSIHGDTGAGGLVGRLFVDIADMDAPMSQGAAVSFASSAVDMLATALTEGLLATSAADLHRTEDLTRVQRVIEQNLHDADITLSDIAAAAGMSLRTVHKLFNAEGTTTRAWLYQARLEAARRYLLTTDLSVADVSECAGFRDVSHFSRLFRSTFGSSPGLYRKEHARIGS", "text": "FUNCTION: Transcriptional activator of nphA1 and nphA2 involved in the degradation of 4-nitrophenol (4-NP)."}
+{"protein": "MSAQAQMRAMLDQLMGTSRDGDTTRQRIKFSDDRVCKSHLLNCCPHDVLSGTRMDLGECLKVHDLALRADYEIASKEQDFFFELDAMDHLQSFIADCDRRTEVSKKRLAETQEEISAEVAAKAERVHELNEEIGKLLAKVEQLGAEGNVEESQKVMDEVEKARAKKREAEEVYRNSMPASSFQQQKLRVCEVCSAYLGLHDNDRRLADHFGGKLHLGFIEIREKLEELKRVVAEKQEKRNQERLKRREEREREEREKLRRSRSHSKNPKRSRSREHRRHRSRSMSRERKRRTRSKSREKRHRHRSRSSSRSRSRSHQRSRHSSRDRSRERSKRRSSKERFRDQDLASRDRDRSSRDRSPRDRDRKDKKRSYESANGRSEDRRSSEEREAGEI", "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": "MIGQRDTVNGAHFGFTDRWGGVSAVPYEELNLGGAVGDDPGAVTANRELAAKSLGVDPARVVWMNQVHGADVAVVDAPWGDRPVPRVDAVVTAERGLALAVLTADCVPVLLADPVSGVAAAAHAGRPGLVAGVVPAAVRAMAELGADPARIVARTGPAVCGRCYEVPEEMRAEVAAVEPAAYAETGWGTPALDVSAGVHAQLERLGVHDRAQSPVCTRESADHFSYRRDRTTGRLAGYVWLD", "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": "MFLCFCPCHVPIMSRLSPATGISSRLRFSIGLSSDGRLIPFGFRFRRNDVPFKRRLRFVIRAQLSEAFSPDLGLDSQAVKSRDTSNLPWIGPVPGDIAEVEAYCRIFRSAERLHGALMETLCNPVTGECRVPYDFSPEEKPLLEDKIVSVLGCILSLLNKGRKEILSGRSSSMNSFNLDDVGVAEESLPPLAVFRGEMKRCCESLHIALENYLTPDDERSGIVWRKLQKLKNVCYDAGFPRSDNYPCQTLFANWDPIYSSNTKEDIDSYESEIAFWRGGQVTQEGLKWLIENGFKTIVDLRAEIVKDTFYQTALDDAISLGKITVVQIPIDVRMAPKAEQVELFASIVSDSSKRPIYVHSKEGVWRTSAMVSRWKQYMTRPITKEIPVSEESKRREVSETKLGSNAVVSGKGVPDEQTDKVSEINEVDSRSASSQSKESGRFEGDTSASEFNMVSDPLKSQVPPGNIFSRKEMSKFLKSKSIAPAGYLTNPSKILGTVPTPQFSYTGVTNGNQIVDKDSIRRLAETGNSNGTLLPTSSQSLDFGNGKFSNGNVHASDNTNKSISDNRGNGFSAAPIAVPPSDNLSRAVGSHSVRESQTQRNNSGSSSDSSDDEAGAIEGNMCASATGVVRVQSRKKAEMFLVRTDGVSCTREKVTESSLAFTHPSTQQQMLLWKTTPKTVLLLKKLGQELMEEAKEAASFLYHQENMNVLVEPEVHDVFARIPGFGFVQTFYIQDTSDLHERVDFVACLGGDGVILHASNLFKGAVPPVVSFNLGSLGFLTSHPFEDFRQDLKRVIHGNNTLDGVYITLRMRLRCEIYRKGKAMPGKVFDVLNEIVVDRGSNPYLSKIECYEHDRLITKVQGDGVIVATPTGSTAYSTAAGGSMVHPNVPCMLFTPICPHSLSFRPVILPDSAKLELKIPDDARSNAWVSFDGKRRQQLSRGDSVRIYMSQHPLPTVNKSDQTGDWFRSLIRCLNWNERLDQKAL", "text": "FUNCTION: Involved in chlorophyll synthesis and chloroplast protection against oxidative damage. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the NAD kinase family."}
+{"protein": "MAQWPEKEEEEQPMFGEEYTGYIPSYLEKDEPCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYDCCCIIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRRLIEENRERRKKEEIVKTLQNRPEPTGAEWELIRMVTEAHRHTNAQGAQWKQKRKFLPDKIGQSPVAPTSDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSEQLPCEDQIILLKGCCMEIMSLRAAMRYDPESETLTLSGEMAVKREQLKNGGLGVVSDAIFDLGKSLAQFNLDDTEVALLQAVLLMSSDRSGLTCMDKIEKCQETYLLAFEHYINYRKHNIPHFWPKLLMKVTDLRMIGACHASRFLHMKVECPNELFPPLFLEVFEDQEV", "text": "FUNCTION: High affinity receptor for triiodothyronine. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
+{"protein": "MRRAALWLWLCALALRLQPVLPQIVTVNVPPEDQDGSGDDSDNFSGSGTGALPDITLSRQASPTLKDVWLLTATPTAPEPTSRDAQATTTSILPAAEKPGEGEPVLTAEVDPGFTARDKESEVTTRPRETTQLLITHWVSTARATTAQAPVTSHPHRDVQPGLHETSAPTAPGQPDQQPPSGGTSVIKEVAEDGATNQLPTGEGSGEQDFTFETSGENTAVAAVEPDQRNQPPVDEGATGASQGLLDRKEVLGGVIAGGLVGLIFAVCLVGFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA", "text": "FUNCTION: Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Secreted Secreted, extracellular exosome Note=Shedding of the ectodomain produces a soluble form. SIMILARITY: Belongs to the syndecan proteoglycan family."}
+{"protein": "MLTGVLQDWVWEAGETANESCPVGSLRTASAVNSCHQGRIPLFTVGVESTKQVQEAVRFARKHNLRLVIRNTGHDLAGRSSAPDSFQIHTHHLQEIQFHADMRLDGSNTSLGPAVTVGAGVMMGNLYAQAARHGYMVLGGDCPTVGVVGGFLQGGGISDFLSLNQGFGVDNVLEYEVVTADGELVVANALQNQDLFWALRGGGGGTFGVVTRATMRVFPDVPVVISEILLEAPQAISSSWTQGLSIVLTALQSLNRDNVGGQLVIAVLPKLAVQASIKFFFLDATEATVIDRRMKPFLTKLSRANVKYTYSSKNLPHFSSNYRQVPDIHSDNDYGVLGSTVAISQQLFDSPQGPEKVATALANLPVSAGDLIFTSNLGGRVISNGELAETSMHPAWRSASQLINYVHTVEPSIEGRAKARERLTNTQMPMLYALDPNLKLSYRNVGDPNEKDFQQIYWGPNYGRLSNIKKKWDTDDLFFSKLGVGSERWDSEEQLCLLHA", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4- dimethylallyl-L-tryptophan (PubMed:22403186). 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 (PubMed:22403186). 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:22403186). Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186). However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet (PubMed:22403186). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
+{"protein": "MTAAASDDAVYNKVADILRQCEDFHRLSTHIERFEREQASLNMHVKTELEKHVEAVELGKLALHDAQTKRVKLLQELHNMLTLCESAREMVDEFPLISRMSRIYKNCYATKQMISQLNNLVKETDVIEDMLREDLELDSDMPNLLRAHYKLSKLREFREEALYQASLEGQSDLPITLENSFSNLNTLSDNFDRLVLNFCRNIFQLVKSGHIKTIVQIFKIVEAEESSDEVLKSIRDAKSSLPDSQDGPFLSLQGMTRQLRNFRLRVLEEFQGAAAENFQRAWVSYLEDGSGELNLDFIFEDLKVAFYVLPDLTPPSYNIAKTFASIYQECLVGLVTKAVSLDTPAAVYLYLINFHREYRKFFEENAPFSVDEVEPGLEDGKDGILVREYTRLFTQKIREWSDKLFQSSVDTFMKRESEPELDSDGNYGLQGTIIFFQMITQQINIISHTNNSDVVGIVLSSIMYIMQSMQDQWKSVMRSELSQQLSGNPESVPPGLMEYLLAVANDNLKCAGFMDNTLLNTFELITSEREEDLREAFGKTVDGYILISDIGVSQIVAIISNDVKPALTSLFQPNWYQSSNMKLIVDTFRDYIVDCIEHMVPGLFDVFLLEASNALTISYLRSIFNKNACFDGDNAIQQIRSDIALAIRVFGEYMAAEHLRSTFEPIEKLLLGMLDADVETVSEYFHLLKEAYWDAPLSLVEAVLQNRTDLEKSIIKKMIDIVRHENDSLQIDTSQQPTVFSQVTSLSGSSIL", "text": "FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. SUBCELLULAR LOCATION: Nucleus Cell septum Cell tip Cytoplasm, cytoskeleton, spindle pole. SIMILARITY: Belongs to the SEC6 family."}
+{"protein": "MNHQEVADRVLNAIGKNNIQAAAHCATRLRLVIKDESKIDQQALDDDADVKGTFETNGQYQIIIGPGDVDKVYDALIVKTGLKEVTPDDIKAVAAAGQNKNPLMDFLKVLSDIFIPIVPALVAGGLLMALNNVLTAEHLFMAKSVVEVYPGLKGIAEMINAMASAPFTFLPILLGFSATKRFGGNPYLGATMGMIMVLPSLVNGYSVATTMAAGKMVYWNVFGLHVAQAGYQGQVLPVLGVAFILATLEKFFHKHIKGAFDFTFTPMFAIVITGFLTFTIVGPVLRTVSDALTNGLVGLYNSTGWIGMGIFGLLYSAIVITGLHQTFPAIETQLLANVAKTGGSFIFPVASMANIGQGAATLAIFFATKSQKQKALTSSAGVSALLGITEPAIFGVNLKMKFPFVFAAIASGIASAFLGLFHVLSVAMGPASVIGFISIASKSIPAFMLSAVISFVVAFIPTFIYAKRTLGDDRDQVKSPAPTSTVINVNDEIISAPVTGASESLKQVNDQVFSAEIMGKGAAIVPSSDQVVAPADGVITVTYDSHHAYGIKTTAGAEILIHLGLDTVNLNGEHFTTNVQKGDTVHQGDLLGTFDIAALKAANYDPTVMLIVTNTANYANVERLKVTNVQAGEQLVALTAPAASSVAATTV", "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 sucrose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MLATKMSVTFCFLLMLTTVMLPTEAKTVAGRTACTQHTSCDTPGAKYCCQNSDCCGGSEHFCASFGQCMRSF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the teretoxin H (TH) superfamily."}
+{"protein": "MSEEVVESSSQEASQVIPQEQEDWADDVVTTMPAQEVTEWPEIKLFGRWACDDISISDISLQDYIAVKEKFARYLPHSAGRYAAKRFRKAQCPIVERLTSGLMMKGRSNGKKLLACRIVKHAFEIIHLLTSENPLQVTVNAIVNSGPREDSTRIGRAGTVRRQAVDVSPLRRVNQAIWLICTGAREAAFRNIKTVAECLADELINAAKGSSNSYAIKKKDELERVAKSNR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
+{"protein": "MLKVEMLSTGDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDDLVTILRERSQHADVLIVNGGLGPTSDDLSALAAATAKGEGLVLHEAWLKEMERYFHERGRVMAPSNRKQAELPASAEFINNPVGTACGFAVQLNRCLMFFTPGVPSEFKVMVEHEILPRLRERFSLPQPPVCLRLTTFGRSESDLAQSLDTLQLPPGVTMGYRSSMPIIELKLTGPASEQQAMEKLWLDVKRVAGQSVIFEGTEGLPAQISRELQNRQFSLTLSEQFTGGLLALQLSRAGAPLLACEVVPSQEETLAQTAHWITERRANHFAGLALAVSGFENEHLNFALATPDGTFALRVRFSTTRYSLAIRQEVCAMMALNMLRRWLNGQDIASEHGWIEVVESMTLSV", "text": "FUNCTION: Does not have nicotinamide-nucleotide (NMN) amidohydrolase activity. SIMILARITY: Belongs to the CinA family."}
+{"protein": "MHRGTQEGAMASRLLHRLRHALAGDGPGEAAASPEAEQFPESSELEDDDAEGLSSRLSGTLSFTSAEDDEDDEDEDDEEAGPDQLPLGDGTSGEDAERSPPPDGQWGSQLLARQLQDFWKKSRNTLAPQRLLFEVTSANVVKDPPSKYVLYTLAVIGPGPPDCQPAQISRRYSDFERLHRNLQRQFRGPMAAISFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFVLPELRRAQSLTCTGLYREALALWANAWQLQAQLGTPSGPDRPLLTLAGLAVCHQELEDPGEARACCEKALQLLGDKSLHPLLAPFLEAHVRLSWRLGLDKRQSEARLQALQEAGLTPTPPPSLKELLIKEVLD", "text": "FUNCTION: Binds to membranes enriched in phosphatidylinositol 3- phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate. May be involved in several stages of intracellular trafficking. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the sorting nexin family."}
+{"protein": "MTPKLKLNNNINWTKRTIDSLFDLKKGEMLEKELITPEGKYEYFNGGVKNSGRTDKFNTFKNTISVIVGGSCGYVRLADKNFFCGQSNCTLNLLDPLELDLKFAYYALKSQQERIEALAFGTTIQNIRISDLKELEIPFTSNKNEQHAIANTLSVFDERLENLASLIEINRKLRDEYAHKLFSLDEAFLSHWKLEALQSQMHEITLGEIFNFKSGKYLKSEERLEEGKFPYYGAGIDNTGFVAEPNTEKDTISIISNGYSLGNIRYHEIPWFNGTGSIALEPMNNEIYVPFFYCALKYLQKDIKERMKSDDSPFLSLKLAGEIKVPYVKSFQLQRKAGKIVFLLDQKLDQYKKELSSLTVIRDTLLKKLFPDMTERTKSIKDY", "text": "FUNCTION: The specificity (S) subunit of a type I restriction enzyme; this subunit dictates DNA sequence specificity. This bacterium does not encode the associated endonuclease or methylase subunits. SIMILARITY: Belongs to the type-I restriction system S methylase family."}
+{"protein": "MKAISLGLISSIIFSIVLAKNSSGSGSSTGCFGCFRKKPKKKILATEVAKPVKAPETADFDPKLPNLKFIEEFEPITIEGCKSRLHELDEPFVSETDGMIIDKVTGFSRRENDSVLSGWYIRPYEEGYENMIKVNFIPLREYYKRMENRPPKQYDGPPPIPDMPQGYVPPKKEEIPVEQYVIQLSEEDPYLLQEEDALSLMEYDAETLNEGDAETLNEGDAETLNEYDAGTLNEEDAGTTNEAGEGTTNEEGEGAANEYDAETLNEYDADTLNEYDAGTLNEYDAGTLNEEEGSTTNEAGEGTSNEAGEGTANDDEELDEEVASIFDDDEHADDLSLLDYDENSNENQENVKKGNENEGEQKGNENEGEQKGKKKKAKEKSKKKVKNKPTMTTKKKKKKEKKKKKKEKEKKKEKKVKVEVIMDHFSEMEKMMNNKIKHWNK", "text": "FUNCTION: During infection, this phosphoprotein probably modulates the structure of the red cell membrane to the advantage of the parasite, although its precise function is not known. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Peripheral membrane protein on the cytoplasmic face of the host erythrocyte membrane."}
+{"protein": "MACLHETRTPSPSFGGFVSTLSEASMRKLDPDTSDCTPEKDLTPTQCVLRDVVPLGGQGGGGPSPSPGGEPPPEPFANSVLQLHEQDTGGPGGATGSPESRASRVRADEVRLQCQSGSGFLEGLFGCLRPVWTMIGKAYSTEHKQQQEDLWEVPFEEILDLQWVGSGAQGAVFLGRFHGEEVAVKKVRDLKETDIKHLRKLKHPNIITFKGVCTQAPCYCILMEFCAQGQLYEVLRAGRPVTPSLLVDWSMGIAGGMNYLHLHKIIHRDLKSPNMLITYDDVVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSSCPDGFKILLRQCWNRKPRNRPSFRQILLHLDIASADVLSTPQETYFKSQAEWREEVKLHFEKIKSEGTCLHRLEEELVMRRREELRHALDIREHYERKLERANNLYMELNALMLQLELKERELLRREQALERRCPGLLKSHTSRSLLHGNTMEKLIKKRNVPQKLSPHSKRPDILKTESLLPKLDAALSGVGLPGCPKAPPSPGRSRRGKTRHRKASAKGSCGDLPGLRAALPPHEPGGLGSPGGLGVGPTAWDASPPALRGLHHDLLLRKMSSSSPDLLSAALGARGRGATGGARDPGSPPPPQGDTPPSEGSAPGSTSPDSPGGAKGEPPPPVGPGEGVGLLGTGREGTTGRGGSRAGYQHLTPAALLYRAAVTRSQKRGISSEEEEGEVDSEVELPPSQRWPQGPNMRQSLSTFSSENPSDVEEGTASEPSPSGTPEVGSTNTDERPDERSDDMCSQGSEIPLDLPTSEVVPERETSSLPMQHQDDQGPNPEDSDCDSTELDNSNSIDALPPPASLPP", "text": "FUNCTION: Part of a non-canonical MAPK signaling pathway. Activated by APOE, enhances the AP-1-mediated transcription of APP, via a MAP kinase signal transduction pathway composed of MAP2K7 and MAPK1/ERK2 and MAPK3/ERK1. May be an activator of the JNK/SAPK pathway. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Behaves essentially as an integral membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily."}
+{"protein": "MTHQGIGCLVKWLYLVLIVHTLLCIGQLECRQQHHNRNNNNNNRRADSSSSEEGHGNTSDGLDNFADQDASFVGHGHQPRRGQRKKQQGGGGGGSGGGGGNGGGGGSRHNRNEESGISLWINEQQLKMLTALYFPQGYSERLYAIHNSRVTNDLRDTTLYNFLVIPSEVNYVNFTWKSGRRKYFYDFDRLQTMDESILKAPTLSIRKSGRIPQEQKNFSIFLPCTGNSSGTASFNVGLKIQTRHNKPLSGTPIRLNFKKECAHRGVYDIDASNPTSLTTLQECSLKCGKNGYCNEHHICKCNVGYTGQYCETAFCFPQCLNGGNCTAPSVCTCPEGYQGTQCEGGICKDKCLNGGKCIQKDKCQCSKGYYGLRCEYSKCVIPCKNEGRCIGNNLCRCPNGLRGDHCEIGRKQRSICKCRNGTCVSHKHCKCHPGFYGRHCNGRKRRHVHRNDDSKF", "text": "FUNCTION: Required for normal accumulation and movement of lipid- modified hedgehog (hh) morphogen. May act by stabilizing the interaction between heparan sulfate proteoglycans (HSPGs) and hh, HSPGs being required for diffusion of hh morphogen. Not involved in wingless (wg) morphogen movement, suggesting that it may provide HSPG specificity for Hh. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Note=Colocalizes with HSPG."}
+{"protein": "MNSNVENLPPHIIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGANGEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIHGGAGGPSGRAEAGRALASGTEASSTDPGAPGGPGGAEGPMAKKHAGERDKKLAAKKKTDKKRALRRL", "text": "FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed:22496338). Catalyzes 'Lys-11'-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 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 (PubMed:19820702, PubMed:19822757, PubMed:27259151). Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A (PubMed:16819549). In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination (PubMed:20061386, PubMed:20622874). SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "MALTTHSGKLIPELQFKAHHFIDKTTVLYGPSKTGKTVYVKHIMKILQPHIEQILVVAPSEPSNRSYEGFVHPTLIHYRLWLADKQKKNDNKGAERFLEAIWQRQTMMSSIYSRVNNIDMLKTLYHKLPIDIQQKENKNIAKVECLKAEQTDQKKEEKITSLYQQLLKKIIIQNIHMYKNLCLTEDEKFTLNYINLNPRLLLILDDCAAELHPLFTKEIFKKFFYQNRHCFISMIICCQDDTDLPANLRKNAFVSIFTNASICMSNFSRQSNRYSKQDKEYVEEISHIVFKGYRKLVYIREDENRQHFYHSTVPLPTAFSFGSKALLKLCKAVYSKEVVIDKSNPYWSKFRLNF", "text": "SIMILARITY: Belongs to the asfivirus B354L family."}
+{"protein": "MINIFIRRGGLIVRESLYSSDEQIKVFHEEDKILWIDLFRPSSDEVNYISQTYHLEVPTKEEREEIEQSARYWEDSGSITINTYFLVRSLESELHNETITFLLRKNILFTIRYSEFRVFDEIQQIVLATPKVFEDGFDLIGKIFEIRVEKDADLLESAAKNTRALRKRVFNSQVINYDEMLEELSSLQELNMSVRDSLFDKRRAITAVLKSDKADADVKKNITIVLKDLNSLVEFTAVNMHALDNIQTILTNQINIEQNKTIKLFTVVTVAMMPPTLIGTIYGMNFDNMPELHWDFSYPVALVIMILSTIFPIIYFKKKGWI", "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": "MDQADHSGVPDDAALEEAPNTVPIQEKSAQPHDTQPYCAFTKRSKLFIVLTVSLAGFFSPFAINIYIPALPQIAGMLHTSEAATNVTVTVYMIAQGLSPVIWAPLSDVFGRRPIYILTFFIFFIANLGLSFTNVYWLLVVLRMVQAAGACSAIAIGAGTIGDVTERKERGSYMGYYALAQYTGPAIGPVVGGALSQRWDYHATFFFLTAISGPFLLFMLLFLVETLRVIVGNGSAKTSGIYRPLVEPKLQRSIANAPRPGIKNPLHGTLDFGFHRPFLVFARPETSLAILAFSMVYASYYLSSGSLPYLFKQVYGLDELLIGVCFVPSGVGCAVGTVLAGKILDWDYRRALDKSKLGVKVTRARLQSAWIYLPCYCASLLAYGWCVRAHTHIAAPIVFQFTLGMFSTMYFTNVNTLIVDLYPGKAASATAAVNVGRCLLGAVAVAVVQPMIDAMGAGWTFTLGALLTLIVGLICQVLIYLYGEMWAARKHS", "text": "FUNCTION: MFS transporter; part of the gene cluster that mediates the biosynthesis of itaconic acid and 2-hydroxyparaconate (PubMed:26639528, PubMed:27750034). Cis-aconitate is secreted by the mitochondrial tricarboxylate transporter MTT1. In the cytosol cis-aconitate is converted into trans-aconitate via isomerization by the aconitate- delta-isomerase ADI1 (PubMed:26639528). Decarboxylation of trans- aconitate by the trans-aconitate decarboxylase TAD1 then leads then to the production of itaconic acid (PubMed:26639528). The cytochrome P450 monooxygenase CYP3 further converts itaconate to 2-hydroxyparaconate via oxidation of the double bond, leading to a transient epoxide, which can subsequently be lactonized to produce 2-hydroxyparaconate (PubMed:27750034). Secretion of itaconate and possibly 2- hydroxyparaconate into the medium is mediated by the major facilitator ITP1 (PubMed:26639528, PubMed:27750034). The glyoxalase domain- containing protein RDO1 is not involved in the biosynthesis of itaconate and 2-hydroxyparaconate, however, it might play a role in the further conversion of 2-hydroxyparaconate to itatartarate (PubMed:27750034). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MNSVGEACTDMKREYDQCFNRWFAEKFLKGDGSGDPCTDLFKRYQQCVQKAIKEKEIPIEGLEFMGHGKEKPENSS", "text": "FUNCTION: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. Likewise, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo). Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion intermembrane space. SIMILARITY: Belongs to the TRIAP1/MDM35 family."}
+{"protein": "MFALDSIVGKHINYALDKTQHLPNKIMNNITNTEITLQDYQYFVSRIFIGLKNLNSMLLFWDTGMGKTLTAVYIIKYIKELFPRWIILIFIKKSLYIDPWLNTIRSYISDTSNIKFIYYDSSSSLDKFNNIYRSIESSLNKKSRLLIIIDEVHKLISRTVKKDNNERNFTPIYKKLIKLANFENNKILCMSATPVTNNISEFNNLIGLLRPNVMNIKEEYINNGKLINFKELRETLLAICSYKRLIEADSLTETNYIDGYAKKNIFYHNIIMSDEQSKLYNMAEKYDYKTELGGLKTMRRLISSFAFYDLKIKGDLDNIEYNDMIKRKLAEFSEFTKNINFSESFIESFKNDNIKIKTNLPITDINNYNILYQYSCKYIETCKIILNSRGKVLIFEPLVNFEGISSLKCYFNCFNISYIEYSSKTLKTRDNELNEYNNYENNNGKKVKVCIFSYAGSEGISFKCINDIIILDMPWNESELKQIIGRSIRLNSHKDLPQEYRYVNVHFLISYTNNRKSVDKEILDIIKDKQGKINVIFDLLKSSSIESIHNTYKYIEPAENEIIFDTIRKTRMKEMNVSNVIINIKLYPISYCKDYDRATILKGLLNKDTNIVYKDNTAVAKLMIDKDNIPIFIIENDTLIYIADDYYE", "text": "FUNCTION: DNA-dependent ATPase required for providing the needed energy to achieve the termination of early transcripts. Acts in concert with the RAP94 subunit of the virion RNA polymerase and the capping enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex. NPH-I must bind ssDNA in order to exhibit ATPase activity (By similarity). SUBCELLULAR LOCATION: Virion Note=Virion core enzyme. SIMILARITY: Belongs to the helicase family. NPH I subfamily."}
+{"protein": "MGCNRNCGLIAGAVIGAVLAVFGGILMPVGDMLIEKTIKKEVVLEEGTIAFKNWVKTGTDVYRQFWIFDVQNPDEVTVNSSKIKVKQRGPYTYRVRYLAKENITQDPETHTVSFLQPNGAIFEPSLSVGTEDDTFTILNLAVAAAPQLYPNTFMQGILNSFIKKSKSSMFQNRTLKELLWGYTDPFLNLVPYPITTTIGVFYPYNNTADGIYKVFNGKDDISKVAIIDTYKGRKNLSYWSSYCDLINGTDAASFPPFVEKTRVLQFFSSDICRSIYAVFGAEINLKGIPVYRFILPSFAFASPFQNPDNHCFCTEKIISKNCTLYGVLDIGKCKEGKPVYISLPHFLHGSPELAEPIESLSPNEEEHSTYLDVEPITGFTLRFAKRLQVNMLVKPAKKIEALKNLKHNYIVPILWLNETGTIGDEKAEMFRNQVTGKINLLGLVEIVLLSVGVVMFIAFMISYCACRSKRVN", "text": "FUNCTION: Multifunctional glycoprotein that acts as receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor- ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (By similarity). Binds long- chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (By similarity). Mechanistically, binding of fatty acids activates downstream kinase LYN, which phosphorylates the palmitoyltransferase ZDHHC5 and inactivates it, resulting in the subsequent depalmitoylation of CD36 and caveolar endocytosis (By similarity). In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway (By similarity). Involved in oral fat perception and preferences (By similarity). Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions (By similarity). In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract (By similarity). Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis (By similarity). Receptor for thrombospondins, THBS1 and THBS2, mediating their antiangiogenic effects (By similarity). As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome. Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Membrane raft Golgi apparatus Apical cell membrane Note=Upon ligand-binding, internalized through dynamin-dependent endocytosis. SIMILARITY: Belongs to the CD36 family."}
+{"protein": "MKKKFLKGLCCAFVISITCLGASSKAYGWDGKKDGTGTHSMIVTQAVKVLENDMSKDEPEIVKQNFKILQDNMHKFQLGSTYPDYDPNAYKLFQDHFWDPDTDHNFSKDNLWYLSYSIKDTAESQVRKFTALARNEWEKGNYEKATWYFGQAMHYFGDLNTPYHAANVTAVDSIGHTKYEGFAEKRKDQYRINTTGIKTNEGFYADALKNSNFDSWSKEYCKGWAKQAKNLYYSHSTMKHTNEDWDYSASHALKNAQMGTAGCIYRFLYDVSKDLLPTENHKINGLMVVIKTANEIAAGTDDYVYFGIERKDGTVQEWTLDNPGNDFEANQEDTYILKIKKPSIKFSDINRMWIRKANFTPVSDDWKVKGIKVIADGSVQYEKQINKWIHGNEKYYIN", "text": "FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Binds to eukaryotic membranes where it hydrolyzes phosphatidylcholine, sphingomyelin and phosphatidylethanolamine. The diacylglycerol produced can activate both the arachidonic acid pathway, leading to modulation of the inflammatory response cascade and thrombosis, and protein kinase C, leading to activation of eukaryotic phospholipases and further membrane damage (By similarity). This enzyme is hemolytic against horse erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C family."}
+{"protein": "GLLDMVTGLLGNL", "text": "FUNCTION: Caeridins show neither neuropeptide activity nor antibiotic activity. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSAIQRLTGKTAVITGGATGIGFAAAKRFIEEGAFVFIFGRRQEKLDAATAALGPNSRAVQGSVTELADLDRLYEAVKAERGSLDIVMANAGAGMATPLGKITGEQCDIVFGTNLKGTIFTIQGALPLMAQAGGGSIILTGSSSGTTGAPPLSVYGASKAAIRNLARSWAGTLRDEGIRINVLSPASIATEIAKEALGEQGMKMFAQQNPLKRMGQPEEVGAVAAFLASSDSSFMTASEVSVDGGLAQI", "text": "FUNCTION: Oxidoreductase; 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 short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MLFQVGGEGTRPTFFEMAAAQQLPASLRAALTYSLGVFALRRSFLHKILDYEDEFFAALMLILEGHSLRTTDGSFAESLYGLRRKSARLRLRKDSARKDSSEEVQHSGLEKRQRILSVVFLVVLPYFKSKLHAIYNKEREARLRESLWGAEDQGFDEADFFTGDDSIVSREPSGNEELSVRVQLATKIKKFIAVCYPWIHASSEGLSFTYQLLYLLDATGFYSLGLQALGIQVCRATGQELMDTSSRISKIRNHERERLRGPPWLKTVQGALLSCSYAVLDYAQTGLIAAVFIFKMMEWWYQSAEERLSAPTVYPPPPPPPAPKMAKEGIPLPPDRSLCALCLQKRANPSVVTVSGFVFCYSCVFKYVSKYKRCPVTLIPASVDQIRRLFQDT", "text": "FUNCTION: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:16113209, PubMed:16813573, PubMed:17478547, PubMed:19594707, PubMed:20679226, PubMed:23336935). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (By similarity). When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the pex2/pex10/pex12 family."}
+{"protein": "MASLQCSFHFLGTNPKKYNPSSIFQSYSRTSFTKLSSRVSRQRFLRCTLSMNGCEADHKAPLGTVETRTLSTVPSPAAATERLITAVSDLKSQPPPFSSGIVRLQVPIEQKIGAIDWLHAQNEILPRSFFSRRSDSGRPDLLQDFSSDNGSSDHNPVSVAGIGSAVFFRDLDPFSHDDWRSIRRFLSSKSPLIRAYGGLRFDPTGKIAVEWEHFGSFYFTVPQVEFDEFGGSSMLAATVAWDNELSWTLENAIEALQETMLQVSSVIMRLRRESLGVIVVSKNHVPSEGAYYPAVNNALEIIKDKHSPLSKVVLARSSRIITDTDIDPIAWLARLQCEGQDAYQFCLQPPGAPAFIGNTPERLFHRKHLGVCSEALAATRPRGDSKVREMEIERDLLTSPKDDLEFSIVRENIREKLKTICDRVVVKPHKSVRKLARVQHLYSQLAGQLKREDDEFNILTALHPTPAVCGCPVEEARLLIKQIESFDRGMYAGPIGFFGGGESEFSVGIRSALVEKGLGALIYAGTGIVSGSNPSSEWNELELKISQFTKSLEHESALQPIN", "text": "FUNCTION: Isochorismate synthase involved in the synthesis of salicylic acid (SA) required for both local and systemic acquired resistance (LAR and SAR) while SA synthesized through the phenylalanine ammonium lyase (PAL) pathway seems to potentiate plant cell death. Also involved in phylloquinone (vitamin K1) synthesis. Has no isochorismate pyruvate lyase (IPL) activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the isochorismate synthase family."}
+{"protein": "MKHLKRWWSAGGGLLHLTLLLSLAGLRVDLDLYLLLPPPTLLQDELLFLGGPASSAYALSPFSASGGWGRAGHLHPKGRELDPAAPPEGQLLREVRALGVPFVPRTSVDAWLVHSVAAGSADEAHGLLGAAAASSTGGAGASVDGGSQAVQGGGGDPRAARSGPLDAGEEEKAPAEPTAQVPDAGGCASEENGVLREKHEAVDHSSQHEENEERVSAQKENSLQQNDDDENKIAEKPDWEAEKTTESRNERHLNGTDTSFSLEDLFQLLSSQPENSLEGISLGDIPLPGSISDGMNSSAHYHVNFSQAISQDVNLHEAILLCPNNTFRRDPTARTSQSQEPFLQLNSHTTNPEQTLPGTNLTGFLSPVDNHMRNLTSQDLLYDLDINIFDEINLMSLATEDNFDPIDVSQLFDEPDSDSGLSLDSSHNNTSVIKSNSSHSVCDEGAIGYCTDHESSSHHDLEGAVGGYYPEPSKLCHLDQSDSDFHGDLTFQHVFHNHTYHLQPTAPESTSEPFPWPGKSQKIRSRYLEDTDRNLSRDEQRAKALHIPFSVDEIVGMPVDSFNSMLSRYYLTDLQVSLIRDIRRRGKNKVAAQNCRKRKLDIILNLEDDVCNLQAKKETLKREQAQCNKAINIMKQKLHDLYHDIFSRLRDDQGRPVNPNHYALQCTHDGSILIVPKELVASGHKKETQKGKRK", "text": "FUNCTION: Activates erythroid-specific, globin gene expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. CNC subfamily."}
+{"protein": "MKIHYLLFAFILVMLSPLAAFSQLINSPVTCMSYGGSCQRSCNGGFRLGGHCGHPKIRCCRRK", "text": "FUNCTION: Has potent antibacterial activity against E.coli (ATCC 25922). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
+{"protein": "MGPGPPAAGAAAPPRPLSLSARLSYAVGHFLNDLCASMWFTYLLLYLHSVRAYSSRGAGLLLLLGHVADGLCTPLVGYEADRAAGRCVRCGPRKAWHLVGTVCVLLSFPFIFSPCLGCGPATPEWAALLYYGPFIVIFQFGWAATQIAHLSLIPELATNDHEKVELTALRYAFTVVANITVYAAAWFLLHLQGSPNVEMARDASDQLGIQDVQVFQNLSLLVIGVGAVFSLLFHLGTREGRRPQVEEPDENRPLLAPTTARPLLLWRHWLREPAFYQVGLLYMSTRLIVNLSQTYIAMYLTYSLSLPKKFIATIPLVMYLSGFCSSFLMKPVNKCIGRNLTYFTGLLVILAFAAWVALADRLGMAVYAAAVLLGSGCATILVTSLAMTADLIGPHTHSGAFVYGAMSFSDKVANGLAVMAIQSLYPCSLEICCRACMGFYRWVMVAATGGVGVAATLCLCSLLIWPIRLRSWDPGAQP", "text": "FUNCTION: Transporter that mediates the import of cysteine into melanosomes, thereby regulating skin/hair pigmentation. In melanosomes, cysteine import is required both for normal levels of cystine, the oxidized dimer of cysteine, and provide cysteine for the production of the cysteinyldopas used in pheomelanin synthesis, thereby regulating skin/hair pigmentation. Also catalyzes import of cysteine into lysosomes in non-pigmented cells. SUBCELLULAR LOCATION: Melanosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MSNRQTGTVKWFNDEKGFGFITPQSGDDLFVHFKAIQSDGFKSLKEGQQVSFIATRGQKGMQAEEVQVI", "text": "FUNCTION: Affects cell viability at low temperatures. FUNCTION: Affects cell viability at low temperatures. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MKQLIRRLSRVADSTQYSLLRSESQRGRTKKEKHKSWVPEGHVPVYVGHEMERFVVNAELLNHPVFVALLKQSAQEYGYEQQGVLRIPCHVLVFERILESLRLGLADRVT", "text": "FUNCTION: Plays a role in the regulation of cell expansion, root meristem patterning and auxin transport. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ARG7 family."}
+{"protein": "MRSHTGLRALVAPGYPLLLLCLLAATRPDPAEGDPTDPTFTSLPVREEMMAKYSNLSLKSCNISVTEKSNVSVEENVILEKPSHVELKCVYTATKDLNLMNVTWKKDDEPLETTGDFNTTKMGNTLTSQYRFIVFNSKQLGKYSCVFGEKELRGTFNIHVPKAHGKKKSLIAYVGDSTVLKCVCQDCLPLNWTWYMGNETAQVPIDAHSNEKYIINGSHANETRLKIKHLLEEDGGSYWCRATFQLGESEEQNELVVLSFLVPLKPFLAILAEVILLVAIILLCEVYTHKKKNDPDAGKEFEQIEQLKSDDSNGIENNVPRYRKTDSADQ", "text": "FUNCTION: Plays a role in targeting the monocarboxylate transporters SLC16A1 and SLC16A7 to the cell membrane (By similarity). Plays a role in the outgrowth of motoneurons and in the formation of neuromuscular junctions. Following muscle denervation, promotes nerve terminal sprouting and the formation of additional acetylcholine receptor clusters at synaptic sites without affecting terminal Schwann cell number or morphology. Delays the retraction of terminal sprouts following re-innervation of denervated endplates. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Synapse Note=Localizes to the neuromuscular junctions."}
+{"protein": "MLLCSLTLMLLWMVASGLECDTKEVCLGSPGIPGTPGSHGLPGRDGRDGIKGDPGPPGPMGPPGGMPGLPGRDGMTGAPGLPGERGEKGEPGERGPPGFPAYLDEELQGTLHEIRHQVLQSQGVLILQGSMLEVGEKVFSTNGQSLNFDAIKELCARAGGHIAAPRSPEENEAITSIVKKHNTYAYLGLAEGPTAGDFYYLDGAPVNYTNWYPGEPRGRGKEKCVEIYTDGQWNDKNCLQYRLAICEF", "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": "MSEQRVTFNGDTRVLYRQAVRTPLPNEDAERLFHENMMNIADAQERKADMLADPDISLLEAYETQLEGIAKSYKRRCRHIAGDDYEEIAMAYNRGARDDRVGALTAYYFEGLWRMQQRITVTDMLFFPIILRYPDCFTVNIRFASGHTTTESVLYESPEHSTEELDDEYAERYYNESLYSQKEAAEYIRDTAEIIREEFPSPDESTFEERQYGGITSAGGRKGPVFSSMLKRVEPDPNRFSEPVDQPTLVEEGKEARRTERELLPEGAIVL", "text": "FUNCTION: May be involved in swimming motility."}
+{"protein": "MWVFGYGSLIWKVDFPYQDKLVGYITNYSRRFWQGSTDHRGVPGKPGRVVTLVEDPAGCVWGVAYRLPVGKEEEVKAYLDFREKGGYRTTTVIFYPKDPTTKPFSVLLYIGTCDNPDYLGPAPLEDIAEQIFNAAGPSGRNTEYLFELANSIRNLVPEEADEHLFALEKLVKERLEGKQNLNCI", "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. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. ChaC subfamily."}
+{"protein": "MIDNGGRFFAMKHGRKIHRLSRPADQRRALLRGLTTQLLKHGRIKTTRAKASAMRKYVDKMITLAKEGSLHKRRQALGFIYEKQIVHALFAEVPERYGDRNGGYTRIIRTLPRRGDNAPMAYIELV", "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 bacterial ribosomal protein bL17 family."}
+{"protein": "MIIDRVEVETINSFSKLELFKEIYGLIWILPIFALLLGITIEVLVIVWLEREISASIQQRIGPEYAGPLGLLQAIADGTKLLLKEDILPSRGDIPLFSIGPSIAVISILLSFLVIPLGYRFVLADLSIGVFLWIAISSIAPIGLLMAGYSSNNKYSFLGGLRAAAQSISYEIPLTFCVLAISLLSNSLSTVDIVEAQSKYGFFGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKYGLFYLVSYLNLLVSSLFVTVLYLGGWNFSIPYISFFGFFQMNKIIGILEMVIGIFITLTKAYLFLFISITIRWTLPRMRMDQLLNLGWKFLLPISLGNLLLTTSFQLVSL", "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 1 family."}
+{"protein": "MQVLGMEEKPARRSVVLVPFPAQGHISPMMQLAKTLHLKGFSITVVQTKFNYFSPSDDFTHDFQFVTIPESLPESDFKNLGPIQFLFKLNKECKVSFKDCLGQLVLQQSNEISCVIYDEFMYFAEAAAKECKLPNIIFSTTSATAFACRSVFDKLYANNVQAPLKETKGQQEELVPEFYPLRYKDFPVSRFASLESIMEVYRNTVDKRTASSVIINTASCLESSSLSFLQQQQLQIPVYPIGPLHMVASAPTSLLEENKSCIEWLNKQKVNSVIYISMGSIALMEINEIMEVASGLAASNQHFLWVIRPGSIPGSEWIESMPEEFSKMVLDRGYIVKWAPQKEVLSHPAVGGFWSHCGWNSTLESIGQGVPMICRPFSGDQKVNARYLECVWKIGIQVEGELDRGVVERAVKRLMVDEEGEEMRKRAFSLKEQLRASVKSGGSSHNSLEEFVHFIRTL", "text": "FUNCTION: Possesses quercetin 3-O-glucosyltransferase and 7-O- glucosyltransferase activities in vitro. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MSDLFSFNKEKKNKLVDNNYSAKDIEVLEGLEPVRKRPGMYIGGTDSNAMHHLVSEVLDNAMDEAVAGFASIITITMHHDHSITIFDNGRGIPIDNHPKFPDKSALEVILTTLHSGGKFSNNVYHTAGGLHGVGISVVNALSKHLEIKVYKQGKLYSQSYSKGEKLTDLICEEASKRLRGTSINFTPDPEIFSEKLHFNPKKIYELARSKAYLYRGVTIEWACEVEVQSDIPKKALISFPNGLKDYLSSKITLDNLVIPGIFAGNIESKSDRIKLEWAICWQNNDSSAFVQSYCNTVPTPQGGTHEQGLKSAILRGLKAYGEMIGNKKAANLTIEDILETASVVLSIFIAEPSFQGQTKEKLVSNGVSKPVENIIKDHFDHFLSSDKALATNLLEHVISIAEFRISKKNEKNISRKNATQKLRLPGKLADCTRTSPEGTELFIVEGDSAGGSAKQARNRETQAVLPLWGKVLNVASSTLEKIVNNQAIQDLEIALACGSLKNYKKENLRYEKIIIMTDADVDGAHIASLLMTFFFLRMPKLVEEGHLYLAKPPLYRLTQSNKTYYAGDEEEKAKLMDKLLKASKAKIEVGRFKGLGEMMPAQLKETTMHPEKRSLLKVTLADFQNVDKIVDDLMGKKPEKRFQFIYEQALVKMDKIISELDI", "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": "MSTQSRKSNSSKQPHSTHKKLDPELKFKLETLTELFPDWTNDDLIDLVQEYEDLETIIDKITSGAATKWDEVKKPSKKERQREQQQQQQQQQQAQLAAQQATQPSSQSHHNNHTHISPSHDGDHSHSAQTSHNHHQSKSSKFSSRERDSSSRSHKKSSNNAAASGPNGSGNARRERASGASRVPATSAASAASANASAVQPDHLKTAVSAAKTASSTSWAAMASDKKAAKQSAQAKKAEEQQQEQQSPQQAQHESTAPSPQQEAEPQSQSQSKSQPQSDNKSAESVSSTSTPATEDLEKPKKMTWAAIVKPKTKPSVKKSEPLEELEDLKREAAQISTEEPEAAEKVIEQVIEQVEQTPEEVVEQVEVTVVPEEVSQESEEASAQQEETAEPAAPVVPAEPEAASSEEKAAPAQPEQGTYSPVAQQQQPQQQQQPQQQQQAQQQQQQPTAYSEDKQSQAQQAQSQQAQSFYQAQPQQYGSQTPQQTPQTLQQQNAAAAAAAAQQQYYMYQNQFPGYSYPGMFDSQSYPAGYGQQYAPQSQNGSQPQTASTQQSQSGQYGVPPGYASTGRDLGAASPMAAQVQLQQQQQQQPYGGSFMPYYHFYQQSFPYGQPQYGMAGQYPYQVPKAYNYMNQYQPQQGGQTPSSQSQQGEEAQQSAQQGQATASQGQAQGSGSQGQAQTNAQQQAQLQQYYQFQQQQQQQQAAAAAAAAQQGGVPYGYSGYDFSSQATRGFY", "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": "MVSSPCTQASSRTCSRILGLSLGTAALFAAGANVALLLPNWDVTYLLRGLLGRHAMLGTGLWGGGLMVLTAAILISLMGWRYGCFSKSGLCRSVLTALLSGGLALLGALICFVTSGVALKDGPFCMFDVSSFNQTQAWKYGYPFKDLHSRNYLYDRSLWNSVCLEPSAAVVWHVSLFSALLCISLLQLLLVVVHVINSLLGLFCSLCEK", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the L6 tetraspanin family."}
+{"protein": "MSTLFLIGIHEIEKSQTIVQNEHYFDRVIELQDLDSLMVALYKDRVSPFPNVHNFETGVSIVLYDPSKFQLSVRQLDVLFKRFFPSFNISAIDHTREENLQRLECVERENSICRNRITRINHWMYHHHDDTPDGINKNSYGTVNGNSVPTQACEANIYTLLLHLNDSKAQHLRKASVPRLIRNIEFMSFLSDPIEKISQEGSHYWNILSTWDFCALSLSTQELIWCGFTLIKKLSKDAKVLIADNKLLLLLFTLESSYHQVNKFHNFRHAIDVMQATWRLCTYLLKDNPVQTLLLCMAAIGHDVGHPGTNNQLLCNCESEVAQNFKNVSILENFHRELFQQLLSEHWPQLLSISKKKFDFISEAILATDMALHSQYEDRLMHENPMKQITLISLIIKAADISNVTRTLSISARWAYLITLEFNDCALLETFHKAHRPEQDCFGDSYKNVDSPKEDLESIQNILVNVTDPDDIIKDHPHIPNGQIFFINTFAEVFFNALSQKFSGLKFLSDNVKINKEYWMKHKKPQ", "text": "FUNCTION: Controls the level of cAMP in yeast cells, together with the low-affinity cAMP phosphodiesterase (PDE1). SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family."}
+{"protein": "MKRAFSSQLRSAYPASKSTHFGRVMASSGSEAKANYAPISTNEPVVSVDWLHSNLGDADIKVLDASWYMAHEQRNPIQEYQVAHIPGALFFDLNGIADRKTNLRHMLPSEEAFAAGCSALGIENNDGVVVYDGMGLFSAARVWWMFRVFGHDKVWVLDGGLPKWRASGYDVESSVSNDAILKASAATEAIEKIYQGQTISPITFQTKFRPHLVLALDQVKENIEDKTYQHIDARSKARFDGIAPEPWKGLPSGHIPGSKCVPFPLMFDSSQTLLPAEELKKQFEQEDISLDSPIAASCGTGVTACILALGLYRLGKTNVAIYDGSWTEWATAPNLPIVGSSS", "text": "FUNCTION: Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3- mercaptopyruvate > thiosulfate. Involved in embryo and seed development. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MASYQSINFRREAILSGRPYPYYYPYVSQIPCISNSCEDHRIQADPNIIYSYEGTQAFDWSNGQCHDPTHNRSTCISNVYYPTNPIFDYCYYGETPFQDPSYQLGFIVREIVVNIIDVPDLRDPVEYMETMAPIGNSESLQINFVLNNQNKLSENNQSNPQINSQINPQMNPRINSQINTQRDNLQPEIYTNNDEPTLSAPVKSVLYKDPIDRIRKVTNCPQVTQDPGLIEPRNLIIVCDTIWVCTPGFLRAYNLLGVPTGRKIGTFGIGGNNVYPSSIAYNDNQCLFPIQKGSKCASSTMIIATLDGTINAYNPIINPENSILVIDNSSRQAMYTGVAICGCRVYLTDFYNQQIDVYDDKFILLPEFSFVGDDECDPIPEYFSPYNIVNICDQLYVTFVQQDPYNNTLEFDGTGLGYINIYTPDGIFIRRFASGCVLNVPYGLIEAPSCYGYPSGSILVANYGSGNINVFDIHGKWISNLKDGFGTDLYIEGLRGITHASCCPKTVYWTSCVNHKINKLGTINTSTNNC", "text": "SIMILARITY: Belongs to the mimivirus R640 family."}
+{"protein": "MDFPQHSQHVLEQLNQQRQLGLLCDCTFVVDGVHFKAHKAVLAACSEYFKMLFVDQKDVVHLDISNAAGLGQVLEFMYTAKLSLSPENVDDVLAVATFLQMQDIITACHALKSLAEPATSPGGNAEALATEGGDKRAKEEKVATSTLSRLEQAGRSTPIGPSRDLKEERGGQAQSAASGAEQTEKADAPREPPPVELKPDPTSGMAAAEAEAALSESSEQEMEVEPARKGEEEQKEQEEQEEEGAGPAEVKEEGSQLENGEAPEENENEESAGTDSGQELGSEARGLRSGTYGDRTESKAYGSVIHKCEDCGKEFTHTGNFKRHIRIHTGEKPFSCRECSKAFSDPAACKAHEKTHSPLKPYGCEECGKSYRLISLLNLHKKRHSGEARYRCEDCGKLFTTSGNLKRHQLVHSGEKPYQCDYCGRSFSDPTSKMRHLETHDTDKEHKCPHCDKKFNQVGNLKAHLKIHIADGPLKCRECGKQFTTSGNLKRHLRIHSGEKPYVCIHCQRQFADPGALQRHVRIHTGEKPCQCVMCGKAFTQASSLIAHVRQHTGEKPYVCERCGKRFVQSSQLANHIRHHDNIRPHKCSVCSKAFVNVGDLSKHIIIHTGEKPYLCDKCGRGFNRVDNLRSHVKTVHQGKAGIKILEPEEGSEVSVVTVDDMVTLATEALAATAVTQLTVVPVGAAVTADETEVLKAEISKAVKQVQEEDPNTHILYACDSCGDKFLDANSLAQHVRIHTAQALVMFQTDADFYQQYGPGGTWPAGQVLQAGELVFRPRDGAEGQPALAETSPTAPECPPPAE", "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. 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. 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. Represses RB1 transcription; this repression can be blocked by interaction with ZBTB49 isoform 3/ZNF509S1 (PubMed:25245946). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MKKLKITGLSLIISGLLMAQAQAAEPVYPDQLRLFSLGQEVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGSASSTWCYPTNPATGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTSIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAINDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSPTTSLSQSVRPTVPAHSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLPTMQNNLAKVLRPVRAGITGDFSAESQFAGNIEIGAPVPVAAASHSSRARNLSAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ", "text": "FUNCTION: Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. SUBCELLULAR LOCATION: Secreted Host cell membrane Note=Secreted as a soluble precursor. SIMILARITY: Belongs to the aerolysin family."}
+{"protein": "MKMLRDPLFWLIALFVALIFWLPYSQPLFAALFPQLPRPVYQQESFAALALAHFWLVGISSLFAVIIGTGAGIAVTRPWGAEFRPLVETIAAVGQTFPPVAVLAIAVPVIGFGLQPAIIALILYGVLPVLQATLAGLGAIDASVTEVAKGMGMSRGQRVRKVELPLAAPVILAGVRTSVIINIGTATIASTVGASTLGTPIIIGLSGFNTAYVIQGALLVALAAIIADRLFERLVQALSQHAK", "text": "FUNCTION: Part of an ABC transporter complex involved in low-affinity glycine betaine uptake. 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. CysTW subfamily."}
+{"protein": "HADGVFTSDFSRLLGQLSAKKYLESLIXXXXXXXXXXXXXXXXXHSDAVFTDNYTRLRKQMAVKKYLNSILN", "text": "FUNCTION: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder. FUNCTION: PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin (By similarity). PHI also causes vasodilation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family."}
+{"protein": "MPKYTLYYFNSRGRAEICRMLFAAANIPYNDVRIDYSEWDIYRSKMPGSCLPVLEINDSIQIPQTMAIARYLARQFGFYGKHHLDMARVDFICDSFYDIFNDYMRMYHDQKGRVMFELMSQMREWYAARNENSGYEECYMQPSMAPSAQMSQEVDNSDTLADCSEMRSQDSMVEPPSQKLSPELESQSSLCSERPQCGPPDPMMGSDFERLSFNEGRMLEMRRRYDETCRRVLPFLEGTLKQRYGGDRYFMGEYMTMCDLMCYCALENPLLDNAYLLHPYPKLRGLRDRVSRNQRINSYFTLRNYTDF", "text": "FUNCTION: S-crystallins are structural components of squids and octopi eye lens. Contains relatively little if any GST activity. SIMILARITY: Belongs to the GST superfamily."}
+{"protein": "MAAPLELVLSADAAGQVANCTVWEPVTGSVLLTYRGGNTSHRGLAVLGGQYLLGGQLGKNYINVWELQRRDQLQQKIVCPGPVNCLSASPNGLYLVAGIAESIYLWEVSTGHLLAILNSHYQDVTCLTFTDDSSHIISGAKDSLVLVWGLYSVLQVETSRGPEPRYVWSRHSLPITDVQCGIGGPQARVATSSLDQTIKLWDICSGDLLVSVLFDVRITSVAFDPAEYHLFCGGSDGVIYQVDLYTTPEQRERPFHPEQEMVFKGHRNQVTCLSVSLDGSMLISGSHDETVCVWDIQSKQSLRSVPHRGPVTNVFIIAAPSNMLRAESKPSFPLPHFSKHLQGAEGCEGPESGGVILRLGKQQGSKENTYLQRADQLQSLLGESEGKNLSGLVEQLRSRTSELEEELNVVRKINKDLFDFSARIITKQ", "text": "FUNCTION: Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. 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). May play a role during development (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Cytoplasm Dynein axonemal particle Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. SIMILARITY: Belongs to the WD repeat IPI3/WDR18 family."}
+{"protein": "MGIEVVVLLTTLMLDAAVGEPPALLHPVVWYGKLISLLERAKFRKMLVEIFYGAFCCLIVITFALILSLLPFPYPLNFLWAVYLLFSSISVKSMVNHARVCVESGVDRKAVQMIVSRNTEELSEEQLCSAVIESVAENYVDGVVAPLFYFSIFGVAGAVVYRAVNTCDAMVGYRKGRYEAFGKFAARLDDILNYIPARLSLLFFELLKRGAFSYGLKRNVKLNGCAIAAMSYLLGVKLEKPGYYSLPGIEPSAADIERAIKAFVRLTVIAVIFTTIAVSIRIVLLTKLHF", "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": "MAAPMFSIIIPTLNVAAVLPACLDSIARQTCGDFELVLVDGGSTDETLDIANIFAPNLGERLIIHRDTDQGVYDAMNRGVDLATGTWLLFLGADDSLYEADTLARVAAFIGEHEPSDLVYGDVIMRSTNFRWGGAFDLDRLLFKRNICHQAIFYRRGLFGTIGPYNLRYRVLADWDFNIRCFSNPALVTRYMHVVVASYNEFGGLSNTIVDKEFLKRLPMSTRLGIRLVIVLVRRWPKVISRAMVMRTVISWRRRR", "text": "FUNCTION: Involved in glycosylation steps downstream of mono-O-methyl- glycosyl-p-hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl- rhamnosyl-phenolphthiocerol dimycocerosate (mycoside B) during the p- hydroxybenzoic acid derivatives (p-HBAD) and glycosylated phenolphthiocerol dimycocerosates (PGL) biosynthesis. FUNCTION: Involved in glycosylation steps downstream of mono-O-methyl- glycosyl-p-hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl- rhamnosyl-phenolphthiocerol dimycocerosate (mycoside B) during the p- hydroxybenzoic acid derivatives (p-HBAD) and glycosylated phenolphthiocerol dimycocerosates (PGL) biosynthesis. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
+{"protein": "MANSPKKPSDGTGVSASDTPKYQHTVPETKPAFNLSPGKASELSHSLPSPSQIKSTAHVSSTHNDAAGNTDDSVLPKNVSPTTNLRVESNGDTNNMFSSPAGLALPKKDDKKKNKGTSKADSKDGKASNSSGQNAQQQSDPNKMQDVLFSAGIDVREEEALLNSSINASKSQVQTNNVKIPNHLPFLHPEQVSNYMRKVGKEQNFNLTPTKNPEILDMMSSACENYMRDILTNAIVISRHRRKAVKINSGRRSEVSAALRAIALIQKKEEERRVKKRIALGLEKEDYENKIDSEETLHRASNVTAGLRAGSKKQYGWLTSSVNKPTSLGAKSSGKVASDITARGESGLKFREAREEPGIVMRDLLFALENRRNSVQTIISKGYAKIRD", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF4 family."}
+{"protein": "MRTQSLLLLGALLAVGSQLPAVFGRKKGEKSGGCPPDDGPCLLSVPDQCVEDSQCPLTRKCCYRACFRQCVPRVSVKLGSCPEDQLRCLSPMNHLCHKDSDCSGKKRCCHSACGRDCRDPARG", "text": "FUNCTION: Putative acid-stable proteinase inhibitor. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MAHFLETQEPLVFSGKKRNDRDDEDGDALVAKKSALAVCDADPAAAIANIRHEFGEHGGVNMSIEASATFTVMEPDTMRRMFTGELGPDNDFYVYSRHFNPTVLNLSRQMAALEGTQAAYCTSSGMSAISSVMLQLCSSGGHVVAASTLYGGTHALLSHFLPRTCNITTSFVDITDHGAVANAIVEGRTQVLYFESVANPTLTVADIPELSRMAHEKGVTVVVDNTFAPMVLSPAKLGADVVVHSISKFISGGADIIAGAVCGSENLVKEMMDLRGGSLMLLGPTMNAKVAFELSERIPHLGLRMREHSHRAQVYAERMRDLGMKVIYPGLETHPQHKLFKGMVNRDYGYGGLLSIDMETEEKANKLMAYLQNATQFGFMAVSLGYYETLMSCSGSSTSSELDPSQKEAAGISPGLVRMSVGYVGTLEQKWTQFEKAFLRM", "text": "FUNCTION: Catalyzes the degradation of L-methionine to alpha- ketobutyrate, methanethiol and ammonia. Exhibits a high activity toward L-methionine, L-ethionine, L-homocysteine and seleno-L-methionine, but not L-cysteine. Involved in an alternative cysteine biosynthesis pathway to the reverse trans-sulfuration pathway (methionine->homocysteine->cystathionine->cysteine) in which methanethiol is an intermediate. Mediates also an alternative isoleucine biosynthesis pathway in which 2-ketobutyrate is an intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
+{"protein": "MHFIYRVVLVLAAFALFKVDSISAGVTFNEEHLTIPRFTRPVEENLIKRQLRVMDDNERGFPSGPSLEKIEAMFQSLTNKITTKSKPSQRDVPDEKLSQLLGAAKPVNKAVEAAGRLKTLQTQKWLDEGKSTQEVFQLLELNKFMVPNFKKIEGTVFGLPDFNTWVNYVDDFNAKNPTKKESMIPTLRTIYSDEGLTRALELAKTYSTTNALATKLRKEQIQRWLDDAQTPKYVFEMFMIDDKVDGLLTNPRFIAWTKYVDDFNLQYPTSRASMEPPIAAHYGDDAVFAMLEAAKKVQLTENVASRLQAEQIKRLLNSNRSPEYVFEAFNLHETGDNLLSTPMFKTWFNYLESFNKKNTDKETLLAPIHRYYHDHGVAKIVAEGMKNPSTVELSKQLQIQRYKRWLHAERPPRDAFNTFILEKPGADVIIRYNERLDGKLYQVRLNKVSDGLLSSPEFQLWSKYLDDWNTKYPDQKQSMAKIFQALFTEDALAKMIMAARNNPSTQKIASLLENAFAKV", "text": "FUNCTION: Effector that enhances P.infestans colonization of Nicotiana benthamiana leaves. SUBCELLULAR LOCATION: Secreted Host cytoplasm. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MASVDLAKVGTILVKNALSGEMVELKSLWKEKTTVLLFLRRFGCQICRWIAKDIGKLKASCDAHQIRLVGIGPEEVGLKEFLEGNFFNGELYIDESKESYKTLGFKRYSALSVIPAALGKKVRDIVTKANADGVQGNFSGDLLQSGGMLIVSKGGEKVLLHFIQDSPGDYVPLESIVQTLGITANVTESQRPQCNDEVCTR", "text": "FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor. Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha) (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family. Prostamide/prostaglandin F synthase subfamily."}
+{"protein": "MYTMQSWSCIFLIICSMQSVCHCCDWIRHHYGHLSAEYLSLLDQMGGDITKQNAPVLFPTSLYRHIDDAEFEDKVIFLKETIYQITKLFDGNMKSVTWDKKNLDDFLNILERQLENLNSCVSPAMKPERRLKRYFKKLNSKVLRKMNYSAQAWELIRKEIKRHLQRLDILAAQMY", "text": "FUNCTION: Key player in antiviral response. Induces expression of TLRs, including that of TLR3, TLR9 and TLR8a1, and that of cytosolic pattern recognition receptors, including RIGI, IFIH1/MDA5 and DHX58/LGP2. Also induces MX1 and its own expression. In the presence of intracellular IFNAR2 (iIFNAR2) and IFNAR1B, intracellular isoform 3 may mediate STAT1 and STAT2 phosphorylation and induction of EIF2AK2, MX1 and RSAD2. SUBCELLULAR LOCATION: [Isoform 1]: Secreted. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol. SIMILARITY: Belongs to the alpha/beta interferon family."}
+{"protein": "MLEILLFLCVIIQRSHINAEITHVVSHLAETALRQDTNFQLLSQDIIAKKFPILDSSCVRRALSDFLPQCLQYGFETVPSDVRTQAAVKLSICELQASGVDNMPPECVGAVHFGACLRAMERTPQWWTTYSGNYQHLPSTCFENALPYEKEQLLSLFLNITDVYSNFQDDLVVDLEKYRANFEATVEASLRLMKASLMEGTHEIVNQLKDDLNYVNSKLADMGETITEHTDNVRTVFNDISDELNDYDMAGQIAHLKEDTMSLWQKINSDMGTYHDVQMSSLYNINAVFDTFYNRATESVQQVRTSVIESQLETLDLIADFNSLVRKSILPVLADELQPQLQEMSVSISRSLVGLSASYNEHLQAWSNRVNETLSEMESHLNNTMSQVEHMNDSIETLENKVFVLVSLGNALTTYVKWIYTFSRALISGYGIVTLIMSMLVVRYSIKLNSSWIKVLGRSTFILVAVVLGARTGSMLSY", "text": "FUNCTION: Required for nuclear membrane fusion during karyogamy. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Nucleus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KAR5 family."}
+{"protein": "MRNGTLVLAALLTLFVLAGSSSAADVGIELDKNMSDGSPIKPTYNSTIKIKAIVKAWNLDVQNATARVQLPEGLVVQDYYMSQGYYDLETGTWEIGDIPAYEERSLTFICLLNRTGSVTVNANVTADGDDNSANNNAELTFKVFGISDLEVNVTGNKETARIGDTVRITVKLKNRGPHDANNIKIGNFLSGGLVVQNFSYDAGYFDDITREWIFETLAAGEEAKSKP", "text": "SIMILARITY: To ORF5 in pFZ1."}
+{"protein": "MRIGIIFPVVIFITAVVFLAWFFIGGYAAPGA", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein Note=May be able to insert into the membrane in both orientations. Relies on YidC for insertion."}
+{"protein": "MSSKQAASPFTCKAEGEEEMTGDLASREMNECKDQIMASHLPLHPLNHNKPHSEELQSLVTTLPADLDWDSMISSQHRMDSESNKLRSLYSFRTSSTSPHKPDEGARERSDLMSSVNFGTPERRKGSLADVVDSLKQKKLEEMTRSEQEDSTCVEKILSKDWKDKMDRLNTSELLGEIKGTPESLAEKERQLSTMITQLISLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARQQQQLLQQQHKINILQQQIQVQGHMPPLMIPIFPHDQRTLAAAAAAQQGFLFPPGLSYKPGDNYPMQFIPSTMAAAAASGLSPLQLQQLYAAQLASMQVSPGAKIPTTPQPANAPGTLSPTGMKSEKRGTSPVAQIKDEAAQPLNLSARPKTADPIKSPTSPTQSFFPMSKTSPVSLSNKSGIPSPIRGPSLDILSSLNSPALFGDQDTVMKAIQEARKMREQIQREQLLTPHSIDGKLPINNMGLNNCRSDKMLLDAVTGKICIRSAHTERTHFENLGPQLTGKPNEDGKLGPGVIDLTRPEDVEGGATVVEARVYRDTRGRSSSEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKAMSNQEKQPYYEEQARLSKIHLEKYPNYKYKPRPKRTCIVDGKKLRIGEYKQLMRSRRQEMRQFFTVGQQPQIPISTPTGVVYPGTISMATTTPSPQMTSDCSSTSASPEPSIPVIQSTYGMKLDSGSLGGNDLMNGEDEMEMYDDFEDDPKSDYSSDNEANEAVSAN", "text": "FUNCTION: Transcription factor that plays a key role in several developmental processes, including neurogenesis, chondrocytes differentiation and cartilage formation. Specifically binds the 5'- AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis. Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: sox5 and sox6 cooperatively bind with sox9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate sox9's ability to transactivate. Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes. Binds to the proximal promoter region of the myelin protein MPZ gene, and is thereby involved in the differentiation of oligodendroglia in the developing spinal tube. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MFVLHSYSKLPNINEYAKAKSTPLDVFVWGTGSMCELGLGPSAKNKEVKRPRLNPYLTEEKLGGTKIVDFAVGGMHTLALDGKNRIWSWGGNDSEVLGRDTCQAKEVLKDIDGKNGNDDDDDDEDGDLNEAESTPALVENLPEGEIVQLAATDNLSAALLSNGDVYSWGCFRCNEGLLGFLRDEIKLQKTPLKIKELKKHCPIMRSVKIILLALDSKEWMPGVNGQQYQLGRRILERHRYRSLEPQQFGLYNIKYIASGDFHCFAIDHSHNVYAWGLNQYGQCALTGDNGELEDGSVLMKPTLIPELSHKGIKEIAAGEHHTLALTEDGQVYAWGRYDMKEIGIPKDKLPKSTFKINTGTHGSFSFLQNLFAVKIKTIGVGSHHSFAVTEDGVVYAWGFAETYGPGLGPSIDDVEKPTRIVNTATKNEDILLIGAGGQFSVSGGVKFEDEEKAEVRLDKYEDLE", "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 (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKVSAALLCLLLTVAAFSTEVLAQPDAINSQVACCYTFNSKKISMQRLMNYRRVTSSKCPKEAVIFKTILGKELCADPKQKWVQDSINYLNKKNQTPKP", "text": "FUNCTION: Acts as a ligand for C-C chemokine receptor CCR2 (By similarity). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (By similarity). Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinophils (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
+{"protein": "MSAPASTTQATGSTTSTTTKTAGATPATASGLFTIPDGDFFSTARAIVASNAVATNEDLSKIEAIWKDMKVPTDTMAQAAWDLVRHCADVGSSAQTEMIDTGPYSNGISRARLAAAIKEVCTLRQFCMKYAPVVWNWMLTNNSPPANWQAQGFKPEHKFAAFDFFNGVTNPAAIMPKEGLIRPPSEAEMNAAQTAAFVKITKARAQSNDFASLDAAVTRGRITGTTTAEAVVTLPPP", "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": "MFIGTIILVLSFLGFVFNRRNIILAFICLETMLLGINLILLRNSVLFDDISGSLFAIVIIILAGVESAIGLSLLVSYYRLRGVINSYGI", "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. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family."}
+{"protein": "MTAAVFFGCAFIAFGPALALYVFTIATEPLRIIFLIAGAFFWLVSLLISSLVWFMARVIIDNKDGPTQKYLLIFGAFVSVYIQEMFRFAYYKLLKKASEGLKSINPGETAPSMRLLAYVSGLGFGIMSGVFSFVNTLSDSLGPGTVGIHGDSPQFFLYSAFMTLVIILLHVFWGIVFFDGCEKKKWGILLIVLLTHLLVSAQTFISSYYGINLASAFIILVLMGTWAFLAAGGSCRSLKLCLLCQDKNFLLYNQRSR", "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. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the APH-1 family."}
+{"protein": "MRSVQAPVVCPAIRPRQVGACASLVNYTGLKPRSQFWGNRTKGVKSQGTTTTITLRLCNKSIKCVFSSHSDGNGSTAENFNENDEEYVNSSVVEAVEVKSGADGFMVKMRDGRQLRCVHNNPQGGHLPDYAPHPAIVLKMEDGTGLLLPIIVLEMPSVLLMAAMTNVQIARPTMYQVVKEMVDKMGYEVRLVRVTKRVHEAYFAQLFLSKVGNASECVSFDLRPSDAINIAVRCKIPIQVNKYLAYSDGMRVIESGKISTPAPASDGLLFTEQDRPNGQACLDTKEFNILSKMMQAVDEERYDEAAEWRDKLGQFRAKRNLRKYT", "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": "MFQATSTGAQIMHAAFPRSWRRGHVLPLRSAKIFKPLACLELRGSTGIGGFHEIELKVRDYELDQFGVVNNAVYANYCQHGRHEFMDSIGINCNEVSRSGGALAIPELTIKFLAPLRSGCRFVVKTRISGISLVRIYFEQFIFKLPNQEPILEAKGTAVWLDNKYRPTRVPSHVRSYFGHFQCQHLVD", "text": "FUNCTION: Acyl-ACP thioesterase involved in the production of fatty acids and beta-keto fatty acids. Can produce beta-keto fatty acids of medium chain (8:0 and 10:0) and small amounts of 8:0 fatty acid when expressed in a heterologous organism (E.coli). May play a role in suberin biosynthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family."}
+{"protein": "MRIPVIRSPLEIRDTERKGRGVFALEPIPAQTCIEISPVLMFSKEEYEQHGQYTVLNEYTYVWSEGKQGLALGLGSMFNHDRHPNVYWKKDNRNNYISYYTLREIKTNEELCISYGDHLWFEDEASSASRISPNEENEDFPLQNISL", "text": "FUNCTION: Histone lysine methyltransferase that specifically mono-, di-, and trimethylates 'Lys-37' of histone H3 to regulate sporulation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
+{"protein": "MSQNRPAAFNTLRMGEVIREKVQDGITGETRDLQYTQCKIVGNGSFGVVFQTKLSPSNEDAAIKRVLQDKRFKNRELQIMRIVRHPNIVQLKAFYYSNGERRDEVYLNLVQEFVPETVYRASRFFNKMKTTMPILEVKLYIYQLFRALAYIHSQGICHRDIKPQNLLLDPTTGILKLCDFGSAKILVENEPNVSYICSRYYRAPELIFGATNYTTKIDVWSTGCVMAELMLGQPLFPGESGIDQLVEIIKVLGTPTREQIRTMNPNYMEHKFPQIKPHPFNRVLRKADNNAIDLIARLLEYTPTERLGAIDAMVHPFFDDLRNPSTKLPDSRHQTGQVRDLPPLFDFNRHELSIAPQLNHQLVPPHVRPTLAAQGLDIDHFTPMRKEDMLARLD", "text": "FUNCTION: Protein kinase that acts downstream of the MPS1 MAPK cascade as a highly conservative signal modulator that dictates growth, conidiation and pathogenicity (PubMed:28424497). Phosphorylates HAT1 at 'Ser-8' to block its translocation from the nucleus to the cytoplasm where HAT1 positively regulates appressorium development and pathogenicity (PubMed:30776962). SUBCELLULAR LOCATION: Cytoplasm Note=Mainly localizes to the cytoplasm at the conidial stage. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily."}
+{"protein": "MGMKHSSRCLLLRRKMAENAAESTEVNSPPSQPPQPVVPAKPVQCVHHVSTQPSCPGRGKMSKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECSSISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWWENVYGFDMTCIRDVAMKEPLVDIVDPKQVVTNACLIKEVDIYTVKTEELSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRRGEEIYGTISMKPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR", "text": "FUNCTION: S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer (PubMed:16051612, PubMed:17925405, PubMed:26876602, PubMed:26529540). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS (PubMed:18320585). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily."}
+{"protein": "MEKELKVRTKLLTKEYSLAQTRIDKLKTLFSVFQNKVPTFWALKGVSLDVYSGETIGIIGLNGSGKSTLSNIISGITPQTSGELEINGEVSIISIGAGLNNNLTGRENIRMKCLMLGEKNKEIDAKIDDIIEFSELGVFIDQPVKTYSSGMRAKLGFSIAVHQNPDILVIDEALSVGDQTFYNKGLKKMLAFKEQGKTIFFVSHSIQQVEQICDRVAWMHYGDLRAFGETKHILKEYRAFLHRYNHFTEPQKESYQRDGKAKQRNFSLEQLQETILEKANQQVGSRRTTKEVIKFTTKNKIGDKMTLGTKSLLILLLCMIFYVSLTFVKGISLTTAFIHPAETIQRIFVPEKVAGKDTNAVKTTKTKPASTKESRQQEEVQPSPTNVPENNNSEQAVSTYTVEVGDSVSLIAENHGLTIEQLQTLNPEIIEVPIYPGQVLKLKEVTE", "text": "FUNCTION: Part of the ABC transporter complex TagGH involved in teichoic acids export. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Teichoic acids exporter (TC 3.A.1.104.1) family."}
+{"protein": "MENAGGAEGTESGAAACAATDGPTRRAGADSGYAGFWRPWVDAGGKKEEETPNHAAEAMPDGPGMTAASGKLYQFRHPVRLFWPKSKCYDYLYQEAEALLKNFPIQATISFYEDSDSEDEIEDLTCEN", "text": "FUNCTION: Plays a role in somitogenesis. Required for somite segregation and establishment of rostrocaudal polarity in somites (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ripply family."}
+{"protein": "MATDSWALAVDEQEAAVKSMTNLQIKEEKVKADTNGIIKTSTTAEKTDEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN", "text": "FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Note=Associates with the nuclear pore complex cytoplasmic fibrils. SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily."}
+{"protein": "MNGFNVRNENNFNSWKIKIQSAPRFESVFDLATDRQRCTPDEVKNNSLWSKYMFPKPFAPTTLKSYKSRFIKIVYCSVDDVHLEDMSYSLDKEFDSIENQTLLIDPQELCRRMLELRSVTKETLQLTINFYTNMMNLPEYKIPRMVMLPRDKELKNIREKEKNLMLKNVIDTILNFINDKIKMLNSDYVHDRGLIRGAIVFCIMLGTGMRINEARQLSVDDLNVLIKRGKLHSDTINLKRKRSRNNTLNNIKMKPLELAREIYSRNPTILQISKNTSTPFKDFRRLLEESGVEMERPRSNMIRHYLSSNLYNSGVPLQKVAKLMNHESSASTKHYLNKYNIGLDETSSEEENNNDDDDAQHNRNSSGSSGESLLYYRNE", "text": "FUNCTION: Plays a role in nucleocapsid assembly and serves an essential function during the final stages of the DNA packaging process. Participates in the processing of branched DNA molecules at the late stages of viral genome replication. SIMILARITY: Belongs to the 'phage' integrase family."}
+{"protein": "MQENLRFASSGDDIKIWDASSMTLVDKFNPHTSPHGISSICWSSNNNFLVTASSSGDKIVVSSCKCKPVPLLELAEGQKQTCVNLNSTSMYLVSGGLNNTVNIWDLKSKRVHRSLKDHKDQVTCVTYNWNDCYIASGSLSGEIILHSVTTNLSSTPFGHGSNQSVRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHNFDSVHKAPASGICFSPVNELLFVTIGLDKRIILYDTSSKKLVKTLVADTPLTAVDFMPDGATLAIGSSRGKIYQYDLRMLKSPVKTISAHKTSVQCIAFQYSTVLTKSSLNKGCSNKPTTVNKRSVNVNAASGGVQNSGIVREAPATSIATVLPQPMTSAMGKGTVAVQEKAGLPRSINTDTLSKETDSGKNQDFSSFDDTGKSSLGDMFSPIRDDAVVNKGSDESIGKGDGFDFLPQLNSVFPPRKNPVTSSTSVLHSSPLNVFMGSPGKEENENRDLTAESKKIYMGKQESKDSFKQLAKLVTSGAESGNLNTSPSSNQTRNSEKFEKPENEIEAQLICEPPINGSSTPNPKIASSVTAGVASSLSEKIADSIGNNRQNAPLTSIQIRFIQNMIQETLDDFREACHRDIVNLQVEMIKQFHMQLNEMHSLLERYSVNEGLVAEIERLREENKRLRAHF", "text": "FUNCTION: Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome."}
+{"protein": "MKSLMMNKLLFLQRITDSPSTTIISTFIVTIISIVFLYTVLLIRTTKNKQKIAAPKASGAWPFIGHLKLFMKQDTQFYRTLGTMSDKYGSVFTLRLGNQAILVVSNWEMVKECFTTNDKSFSNRPSTLSTKYMLNDTNSVVFSPYGTYWREMRKILVQKLLISNQRSEALKNLKTKEIDNSFVKLNDLCNNDVSGGGTKVRMDEWLADMMFNIIARITFGYQSGGGDAPGASTTSKNVERYKKTLDEMFVVLATRFAVSDIFPSLEFIDRLRGLVKDMKILGDELNSIAGCFIEEHRQKRRESLSSLLSLSNESVGDEQDFIDVLLSIMDQSRLPGDDPDFIIKIMILEAFAGGTDSLSATLTWVLSLLLNHPNVLKRAREEIDRHVENGKQVEVSDIPKLGYIDAIIKETMRLYPVGALSERYTTEECEVGRFNVPAGTRLLVNIWKIHRDPSVWENPSDFQPERFLCSDKVGVDLYGQNYELIPFGAGRRVCPAIVSSLQTMHYALARLIQGYEMKSASLDGKVNMEEMIAMSCHKMSPLEVIISPREPRRS", "text": "FUNCTION: Cytochrome P450 involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:25485687, PubMed:27378283, PubMed:29610307). Converts (S)-1-hydroxy-N- methylcanadine to (13S,14R)-1,13-dihydroxy-N-methylcanadine (PubMed:25485687, PubMed:27378283). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MAASTGYVRLWGAARCWVLRRPMLAAAGGRVPTAAGAWLLRGQRTCDASPPWALWGRGPAIGGQWRGFWEASSRGGGAFSGGEDASEGGAEEGAGGAGGSAGAGEGPVITALTPMTIPDVFPHLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQDKDAKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDEQAEALAVER", "text": "FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand- specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters (PubMed:12198491, PubMed:15870080, PubMed:17420247, PubMed:8248235). Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein, helicase Twinkle (TWNK) and the large ribosomal subunit protein bL32m. bL32m is protected from degradation by LONP1 when it is bound to a nucleic acid (RNA), but TWNK is not (PubMed:17579211, PubMed:28377575). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase S16 family."}
+{"protein": "MGAAISQGALIAIVCNGLVGFLLLLLWVILCWACHSRSADVDSLSESSPNSSPGPCPEKAPPPQKPSHEGSYLLQP", "text": "FUNCTION: Involved in the regulation of glucose homeostasis and lipid metabolism. FUNCTION: Involved in the regulation of glucose homeostasis and lipid metabolism. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIVVISILAAAVSLLYFSVVIIRSKYGWLSKDKKFQRYLARVTDVEATDTNNPSVNYGIVVDCGSSGSRIFVYCWPRHNGNPHDLLDIRQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLSFAAEHVPRAKHKETPLYILCTAGMRVLPESQQKAILEDLLTDIPVHYDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHIEEDDEAVVEVNIPGSESSEAIVRKRTAGVLDMGGVSTQIAYEVPQTVSFASSQQEEVAKNLLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRLFASTVQKNRLLGKQTGLTPDAPLLDPCLPLDIKDEIQQNGQTLYLQGTGDFDLCRETLQPFMNKTNETQTSLNGVYQPPIHFQNSEFYGFSEFYYCTEDVLRMGGDYNAARFTQAAKDYCATKWSILRERFDRGLYASHADLHRLKYQCFKSAWMFEVFHKGFSFPVTYKNLKTALQVYDKEVQWTLGAILYRTRFLPLRDIRQEVFRAGHAHWRGVSFVYNHYLFSGCFLVVLLSILLYLLRLRRIHRRAPRTGSLWMEEGLPSQKGPGPL", "text": "FUNCTION: [Isoform 1]: Catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner, with a preference for pyrimidines. Preferentially hydrolyzes UTP and TTP on UTP and TTP. AMP, ADP, ATP and UMP are not substrates. Preferentially activated by Ca(2+) over Mg(2+). FUNCTION: [Isoform 2]: Has a broad substrate specificity with the ability of cleaving all nucleotide di- and triphosphates with the exception of adenosine di- and triphosphate (ADP and ATP). Preferentially hydrolyzes CTP, UDP, CDP, GTP and GDP. Can use either Ca(2+) or Mg(2+) equally. SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GDA1/CD39 NTPase family."}
+{"protein": "MDTLLKTPNNLEFLNPHHGFAVKASTFRSEKHHNFGSRKFCETLGRSVCVKGSSSALLELVPETKKENLDFELPMYDPSKGVVVDLAVVGGGPAGLAVAQQVSEAGLSVCSIDPNPKLIWPNNYGVWVDEFEAMDLLDCLDATWSGAAVYIDDNTAKDLHRPYGRVNRKQLKSKMMQKCIMNGVKFHQAKVIKVIHEESKSMLICNDGITIQATVVLDATGFSRSLVQYDKPYNPGYQVAYGILAEVEEHPFDVNKMVFMDWRDSHLKNNTDLKERNSRIPTFLYAMPFSSNRIFLEETSLVARPGLRIDDIQERMVARLNHLGIKVKSIEEDEHCLIPMGGPLPVLPQRVVGIGGTAGMVHPSTGYMVARTLAAAPVVANAIIQYLGSERSHSGNELSTAVWKDLWPIERRRQREFFCFGMDILLKLDLPATRRFFDAFFDLEPRYWHGFLSSRLFLPELIVFGLSLFSHASNTSRFEIMTKGTVPLVNMINNLLQDKE", "text": "FUNCTION: Catalyzes the double cyclization reaction which converts lycopene to beta-carotene and neurosporene to beta-zeacarotene. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the lycopene cyclase family."}
+{"protein": "MSVEGLLSEVKHFNAHHLDAALGEQLFYGGKRVFSDVKPGTSSGGDHGCKGGKSELKGAIHNAKHAADKALNKEGGEDVSKLREEHSALAKKVDDLASLVAELQLQLSTLRQGQTSSVAAPAAAPAAAKEEAAGDDDFDLFGSEDEEEDEEKKKVVEERLAAYAAKKATKAGPIAKSSVILDVKPWDDETDLGEMEKLVRSIEMDGLVWGGAKLIPIGYGIKKLQIITVIEDLKVSVDDLIEKITGDFEDHVQSVDIVAFNKI", "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": "MSLEDPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGDLQERKVFVERMREAVQEMKDHMVSPTAVAFLERNNREILAGKPAAQKSPSDLLDASAVSATSRYIEEQQATQQLIMDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSDRRQWCAIAVLVGVLLLVLILLFSL", "text": "FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type IV membrane protein. SIMILARITY: Belongs to the syntaxin family."}
+{"protein": "MKIKAVGAYSAKQPLEPMDITRREPGPNDVKIEIAYCGVCHSDLHQVRSEWAGTVYPCVPGHEIVGRVVAVGDQVEKYAPGDLVGVGCIVDSCKHCEECEDGLENYCDHMTGTYNSPTPDEPGHTLGGYSQQIVVHERYVLRIRHPQEQLAAVAPLLCAGITTYSPLRHWQAGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSEAKREAAKALGADEVVNSRNADEMAAHLKSFDFILNTVAAPHNLDDFTTLLKRDGTMTLVGAPATPHKSPEVFNLIMKRRAIAGSMIGGIPETQEMLDFCAEHGIVADIEMIRADQINEAYERMLRGDVKYRFVIDNRTLTD", "text": "FUNCTION: Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
+{"protein": "DGLKLNYLRISEAKLTGIPKDLPETLNELHLDHNKIQAIELEDLLRYSKLYRLGLGHNQIRMIENGSLSFLPTLRELHLDNNKLSRVPAGLPDLKLLQVVYLHSNNITKVGVNDFCPVGFGVKRAYYNGISLFNN", "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": "MAALDSDSDEDLISYGTGLEPLDEGERPKKPIPLQDQTVRDEKGRYKRFHGAFSGGFSAGYFNTVGSKEGWTPSTFVSSRQNRADKSALGPEDFMDEEDLSEFGIAPKAIVTTDDFASKTKDRIREKARQLAAAAAPIPGATLLDDLITPAKLSVGFELLRKMGWKEGQGVGPRVKRKARRQKPDPGVKIYGCALPPGGSEESEDEDDDYLPDNVTFAPKDVMPVDFTPKDNVHGLAYKGLDPHQALFGMPGEHLNLFGGASEGTSHLLGDVGLSKGRKLGISGQAFGVGALEEEDDDIYATETLSKYDTVLKDEEPGDGLYGWTAPKQYKNQKEPERDLRYVGKILEGFSLASKPLSSKKIYPPPQLPRDYRPVHYFRPVVAATAENAHVLQVLSESSGKAGQDVGTHSRHQLNASKRGELLGEMPIQGSATSVLEFLSQKDKERIKEVKQATDLKAAQAKARSLAQSASSSRAQASTPDLGHSSWHLALGGGTVTTRANNFKPFAKDPEKQRRYEEFLVHMKKGQKDALERCLDPSMTEWERSREREEFARAAQLYVSSNSTLSSRFTHAKEEEDSDQVEVPRDQENDVSDKQSAVKMKMFGKLTRDTFEWHPDKLLCKRFNVPDPYPGSTLVGLPRVKRDKYSVFNFLTLPEPAPLPTAPVPSEKAPQQRGSDKSRKPSRWDTSKQEKKEDSISEFLSQARSKVGPPKQESSALGSKEEQAPEPRPDTTVDKAVDAQTDGEGSRPSMDLFKAIFASSSDEKSSSSEEEQDDSEDSQEHTEEASLKGSQEAAAGETSVVLAAEPEPCEPATPFPIQKAQIDEREEFGPRLPPVFCPNSRQKLEIPQKEKPKKSKERHKSKKEHRRKREKKKKHKKHKHKSKQKNKKSEKNSSSESTDSSDSGSDDGGPAELSPQELLRRLKCLPLRRQ", "text": "SIMILARITY: Belongs to the GPATCH1 family."}
+{"protein": "MPKGPKQQPPEPEWIGDGESTSPTDKVVKKGKKDKKTKKTFFEELAVEDRQAGEEEKVLKEKEQQQQHQQQQQKKKRDTRKGRRKKDVDDDDGEEKELMERLKKLSVPASDEEEEAPAPVPRGGKKNKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNRINKAVSQEQQPGPKGRKGKEEKSKGKAKPQNKFAALDDEEEQDEEEIKEKEPPKQGKEKAKKAEQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAADRLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTRGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFDDYKREVLEALGEVMVSRPRE", "text": "FUNCTION: Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Nucleus envelope. SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily."}
+{"protein": "MNNEETFYQAMRRQGVTRRSFLKYCSLAATSLGLGAGMAPKIAWALENKPRIPVVWIHGLECTCCTESFIRSAHPLAKDVILSLISLDYDDTLMAAAGTQAEEVFEDIITQYNGKYILAVEGNPPLGEQGMFCISSGRPFIEKLKRAAAGASAIIAWGTCASWGCVQAARPNPTQATPIDKVITDKPIIKVPGCPPIPDVMSAIITYMVTFDRLPDVDRMGRPLMFYGQRIHDKCYRRAHFDAGEFVQSWDDDAARKGYCLYKMGCKGPTTYNACSSTRWNDGVSFPIQSGHGCLGCAENGFWDRGSFYSRVVDIPQMGTHSTADTVGLTALGVVAAAVGVHAVASAVDQRRRHNQQPTETEHQPGNEDKQA", "text": "FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type I membrane protein; Periplasmic side. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type I membrane protein; Periplasmic side. SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family."}
+{"protein": "MAEETDTRPASAGSRGRPAPEDDDREEGEITDLACAPSPPATHPLEHSWTFWFDNPQSKSKQAAWGSSIRPIHTFSTVEEFWGLYNNINHPSKLIVGADFHCFKNKIEPKWEDPICANGGKWTISCGRGKSDTFWLHTLLAMIGEQFDYGDEICGAVVSVRGKQERIAIWTKNAANEAAQVSIGKQWKELLDYKDSIGFIVHDDAKKMDKGLKNRYTV", "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 (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). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the eukaryotic initiation factor 4E family."}
+{"protein": "MESISLPWTLPEPLQQVHLAHFSNLDPATQSAAIIDRIISASRLPSASPEQAQQADEERVKLDFAFLDPTKLCSKLHLLSAVTQAAVVCARSWDDDRQVFREGEASIGGMKSKTPHSEVIYMLNPGNNVGESLKRFGLSPTSSSLLLVKFSSPTADKQAILQSMIDLVSPSNLTSPPTAEAHTPIDIDHAIRYGSYPTTPSTTAQVTDWKQLNKIYKLQIPSTLLNNKQDNQWYEKYQDIICTSVAMKLVAA", "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": "MDVSAALSSDYSSGTPSPVAADADDGSSAYMTVSSAPPKRRAGRTKFKETRHPVFKGVRRRNPGRWVCEVREPHGKQRIWLGTFETAEMAARAHDVAALALRGRAACLNFADSPRRLRVPPIGASHDDIRRAAAEAAEAFRPPPDESNAATEVAAAASGATNSNAEQFASHPYYEVMDDGLDLGMQGYLDMAQGMLIDPPPMAGDPAVGSGEDDNDGEVQLWSY", "text": "FUNCTION: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates high salinity- and dehydration-inducible transcription (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily."}
+{"protein": "MAESSEPPVVLLHRPPSLTFMDEILTREFRTLITDTSSSESLPSFFPRHASSARAFVISGRLPVTDELLSHLPSLQILVCTSVGIDHIDLAACKRRGIVITNAGNAFSDDVADCAVGLLISVLRRIPAADRYVRSGNWAKFGDFQLGSKVSGKRVGIVGLGSIGSFVAKRLESFGCVISYNSRSQKQSSPYRYYSDILSLAENNDVLVLCCSLTDETHHIVNREVMELLGKDGVVINVGRGKLIDEKEMVKCLVDGVIGGAGLDVFENEPAVPQELFGLDNVVLSPHFAVATPGSLDNVAQIALANLKAFFSNRPLLSPVQLD", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate (HP) into glycolate and glycerate. Mostly active in the presence of NADPH and glyoxylate. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GyaR subfamily."}
+{"protein": "MASATASHTLCGIPATSSSTTNKAIAPSSARFLAKTPLRRLGFAGAAADSLFTNHVATKLRSLKSSSKPIRGVASMAKKSVGDLTAAELKGKKVFVRADLNVPLDDNQNITDDTRIRAAVPTIKHLMANGAKVILSSHLGRPKGVTPKYSLAPLVPRLSELLGIQVVKVEDCIGPEVEKLVASLPEGGVLLLENVRFYKEEEKNEPEFAKKLASLADLYVNDAFGTAHRAHASTEGVTKFLKPSVAGFLLQKELDYLVGAVSNPKRPFAAIVGGSKVSSKIGVIESLLEKCDILLLGGGMIFTFYKAQGLSVGSSLVEEDKLELATSLLEKAKAKGVSLLLPSDVVIADKFAPDANSKIVPASAIPDGWMGLDIGPDSVKTFNDALDTTKTVIWNGPMGVFEFDKFAVGTEAIAKKLADLSGKGVTTIIGGGDSVAAVEKVGVASVMSHISTGGGASLELLEGKVLPGVIALDEADAPVAV", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
+{"protein": "MDRSLGWQGNSVPEDRTEAGIKRFLEDTTDDGELSKFVKDFSGNESCHPPEAKTWASRPQVPEPRPQAPDLYDDDLEFRPPSWPQSSDNQQYFCAPAPLSPSARPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPPEVDRKKRKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSMTRLVVKERNRNKLTRESGTDLPIPAVPPGTDPETEKLIREKDEELRRMQEMLHKIQKQMKETY", "text": "FUNCTION: Filament-forming cytoskeletal GTPase (Probable). Pro- apoptotic protein involved in LGR5-positive intestinal stem cell and Paneth cell expansion in the intestines, via its interaction with XIAP (By similarity). May also play a role in the regulation of cell fate in the intestine (By similarity). Positive regulator of apoptosis involved in hematopoietic stem cell homeostasis; via its interaction with XIAP (By similarity). Negative regulator of repair and hair follicle regeneration in response to injury, due to inhibition of hair follicle stem cell proliferation, potentially via its interaction with XIAP (By similarity). Plays an important role in male fertility and sperm motility (By similarity). During spermiogenesis, essential for the establishment of the annulus (a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum) which is a requisite for the structural and mechanical integrity of the sperm (By similarity). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development (By similarity). Required for dopaminergic metabolism in presynaptic autoreceptors; potentially via activity as a presynaptic scaffold protein (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium, flagellum Cytoplasmic vesicle, secretory vesicle Cell projection, axon Cell projection, dendrite Perikaryon Synapse Note=In platelets, found in areas surrounding alpha-granules (By similarity). Found in the sperm annulus, a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum (By similarity). Expressed and colocalized with SLC6A3 and SNCA in axon terminals, especially at the varicosities (By similarity). SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
+{"protein": "MLPSATSLLRGPCLGLRAAALRLVRQQVPHVCAVRLMRCSSHRRGEALTGAPLDNAPKEYPPKIQQLVQDIASLTLLEISDLNELLKKTLKIQDVGLMPMGGMVPGAAPAPTAPEAAEEDVPKQKERTHFTVRLTEAKPVDKVKLIKEIKNYVQGINLVQAKKLVESLPQEIKANVAKAEAEKIKAALEAVGGTVVLE", "text": "FUNCTION: As a component of the mitochondrial large ribosomal subunit, it plays a role in mitochondrial translation. Associates with mitochondrial RNA polymerase to activate transcription. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family."}
+{"protein": "MGVISPTETLFLKSQHRLLQPRNYSYALAFHSTRRVANFPRNSFSSLGSCSVDFPLRSNPISQNSKSIHPWRRYVSESDSNELYHKKVSSIMETLKQAYSFIPHGILLSTILALVYPPSFTWFKPRYFVPGLGFMMFAVGINSNERDFLEALKRPDAIFAGYIGQYLIKPLLGYIFGVIAVSLFNLPTSIGAGIMLVSCVSGAQLSNYTTFLTDPSLAALSIVMTSISTATAVLVTPMLSLLLIGKKLPVDVFGMISSILQVVITPIAAGLLLNRLFPRLSNAIKPFLPALTVIDMSCCIGAPLALNIDSILSPFGATILFLVITFHLLAFVAGYFFTGFFFSKAPDVKALQRTISYETGMQSSLLALALATKFFQDPLVGVPPAISTVVMSLMGVSLVTIWKNRKE", "text": "FUNCTION: Plastidic transporter involved in the biosynthesis of aliphatic glucosinolates by translocating the biosynthetic intermediates of Met-derived glucosinolates across chloroplast membranes. Transports short chain (C2) alpha-keto acids, such as 4- methylsulfanyl-2-oxobutanoic acid, from the cytosol to the chloroplast where they are subjected to chain elongation cycles. Functions also in the transport of chain-elongated (C3 to C8) Met derivatives from the chloroplast to the cytosol. Does not seem to be involved in the transport of indole-derived glucosinolates. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Plastid, chloroplast envelope. SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family."}
+{"protein": "MTILIQQYTNDENKKLELNNISKLLQNRIILFSQTVDDEICNSIVGQLLYLENEDSTKDIRLFINSPGGSVTAGLSVYDTIQNLSVDVSTICFGLAASMGAVLLAAGVENKRFAFASSRIMIHQPLSKVEAPWSHLDIQIRNGAYFKNLLNNILSFHTKQELKQIETDTERDFFLSATEAKQYGIIDHIFINNN", "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, cyanelle. SIMILARITY: Belongs to the peptidase S14 family."}
+{"protein": "VIGGDECNINEHRSL", "text": "FUNCTION: Snake venom serine protease that cleaves fibrinogen Aalpha chain (FGA), partially cleaves Bbeta chain (FGB) and has no activity on gamma chain. Is less potent than A1 and A2 alpha-fibrinogenases. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
+{"protein": "MGEGKNHQSFSFKNADDEIDLSLSKFSLFKLKMAKSKIIKVFGQNDPVDPNNCYINMRSIKITTSSVLPESDPKYLIWEMSYKTDEEDHTLGQLAWKASYNGTFIVTTTYAMMVTGGELYTPYTAVIRSSDGNEIKGVKVKVTLSWDPANDRPSKARMGGFIQDMYCKTITNGKTQISPMVGWYIGQDERRYCKVLNKSALEFSSEGIYPLMELVSGADSVINPLINKLISGMLNDEEKRRVSLYTSTVGAGTSLTQSEKLLLKKLVESKTGSGLVQFLMRACKELGTDVYLEA", "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. Displays an RNA-binding activity (By similarity)."}
+{"protein": "MVVGQAKAAMGKISSAIGERSKRISGAMNEPLRKRKILLVIVCIAMLLDNMLYMVIVPIVPNYLETIRTYKLVYITIPSNGTNGSLLNSTQRAVLERNPNANEDIQIGVLFASKAILQLLSNPFTGTFIDRVGYDIPLLIGLTIMFFSTITFAFGESYAILFAARSLQGLGSAFADTSGIAMIADKYTEESERTQALGIALAFISFGSLVAPPFGGVLYQFAGKWVPFLVLSFVCLLDGILLLMVVTPFASRTRGNTLQGTPIHKLMIDPYIAVVAGALTTCNIPLAFLEPTISNWMKKTMNASEWQMGITWLPAFFPHILGVYITVKLAAKYPNYQWLYGAFGLVIIGVSSCTIPACRNFEELIIPLCALCFGIALVDTALLPTLAFLVDIRYVSVYGSVYAIADISYSVAYALGPIMAGQIVHDLGFVQLNLGMGLVNILYAPALLFLRNVCQMKPSLSERNILLEDGPKGLYDTIIMEERKAAKEPHGTSSGNHSVHAVLSDQEGYSE", "text": "FUNCTION: Involved in acetylcholine transport into synaptic vesicles. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Vesicular transporter family."}
+{"protein": "QVFGEGMFDYDLFPFLTSTVSPHYRHGLLRGFMDSGISEVRSDRDRFTINLDVKHFSPDDLTVKILDDFVEIHGKHSERQDDHGYISREFHRRYRLPSNLDQSSISCSLSADGILTFSGPKMMSNLVSSHSERPIPVSREEKPTSAPSS", "text": "FUNCTION: Contributes to the transparency and refractive index of the lens. May act as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates to the nucleus during heat shock. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MAKALEQPFDVANIPGPKMATLLEKGKPVANMIKKAKRPLLIVGPDMTDEMFERVKKFVEKDITVVATGSAITRFIDAGLGEKVNYAVLHELTQFLLDPDWKGFDGQGNYDLVLMLGSIYYHGSQMLAAIKNFAPHIRALAIDRYYHPNADMSFGNLWKKEEDYLKLLDEILAEL", "text": "FUNCTION: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation. SIMILARITY: Belongs to the CdhB family."}
+{"protein": "MLLWILLLETSLCFAAGNVTGDVCKEKICSCNEIEGDLHVDCEKKGFTSLQRFTAPTSQFYHLFLHGNSLTRLFPNEFANFYNAVSLHMENNGLHEIVPGAFLGLQLVKRLHINNNKIKSFRKQTFLGLDDLEYLQADFNLLRDIDPGAFQDLNKLEVLILNDNLISTLPANVFQYVPITHLDLRGNRLKTLPYEEVLEQIPGIAEILLEDNPWDCTCDLLSLKEWLENIPKNALIGRVVCEAPTRLQGKDLNETTEQDLCPLKNRVDSSLPAPPAQEETFAPGPLPTPFKTNGQEDHATPGSAPNGGTKIPGNWQIKIRPTAAIATGSSRNKPLANSLPCPGGCSCDHIPGSGLKMNCNNRNVSSLADLKPKLSNVQELFLRDNKIHSIRKSHFVDYKNLILLDLGNNNIATVENNTFKNLLDLRWLYMDSNYLDTLSREKFAGLQNLEYLNVEYNAIQLILPGTFNAMPKLRILILNNNLLRSLPVDVFAGVSLSKLSLHNNYFMYLPVAGVLDQLTSIIQIDLHGNPWECSCTIVPFKQWAERLGSEVLMSDLKCETPVNFFRKDFMLLSNDEICPQLYARISPTLTSHSKNSTGLAETGTHSNSYLDTSRVSISVLVPGLLLVFVTSAFTVVGMLVFILRNRKRSKRRDANSSASEINSLQTVCDSSYWHNGPYNADGAHRVYDCGSHSLSD", "text": "FUNCTION: It is involved in synaptogenesis and promotes excitatory synapse differentiation (PubMed:27273464, PubMed:27812321). Enhances neuronal dendrite outgrowth (PubMed:16224024, PubMed:19640509). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Secreted Synapse. SIMILARITY: Belongs to the SLITRK family."}
+{"protein": "MVQRDMSKSPPTAAAAVAQEIQMELLENVAPAGALGAAAQSYGKGARRKNRFKGSDGSTSSDTTSNSFVRQGSADSYTSRPSDSDVSLEEDREAVRREAERQAQAQLEKAKTKPVAFAVRTNVSYSAAHEDDVPVPGMAISFEAKDFLHVKEKFNNDWWIGRLVKEGCEIGFIPSPVKLENMRLQHEQRAKQGKFYSSKSGGNSSSSLGDIVPSSRKSTPPSSAIDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPFFKKTEHTPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFEGRISITRVTADISLAKRSVLNNPSKHAIIERSNTRSSLAEVQSEIERIFELARTLQLVVLDADTINHPAQLSKTSLAPIIVYVKISSPKVLQRLIKSRGKSQAKHLNVQMVAADKLAQCPPELFDVILDENQLEDACEHLADYLEAYWKATHPPSSSLPNPLLSRTLATSSLPLSPTLASNSQGSQGDQRTDRSAPIRSASQAEEEPSVEPVKKSQHRSSSSAPHHNHRSGTSRGLSRQETFDSETQESRDSAYVEPKEDYSHDHVDHYASHRDHNHRDETHGSSDHRHRESRHRSRDVDREQDHNECNKQRSRHKSKDRYCEKDGEVISKKRNEAGEWNRDVYIRQ", "text": "FUNCTION: Beta subunit of voltage-dependent calcium channels which contributes to the function of the calcium channel by increasing peak calcium current (By similarity). Plays a role in shifting voltage dependencies of activation and inactivation of the channel (By similarity). May modulate G protein inhibition (By similarity). May contribute to beta-adrenergic augmentation of Ca(2+) influx in cardiomyocytes, thereby regulating increases in heart rate and contractile force (PubMed:36424916). Involved in membrane targeting of the alpha-1 subunit CACNA1C (PubMed:17525370). SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the calcium channel beta subunit family."}
+{"protein": "MSEVTKNSLEKILPQLKCHFTWNLFKEESVSRDLEDRVCNQIEFLNTEFKATMYNLLAYIKHLDGNNEAALECLRQAEELIQQEHADQAEIRSLVTWGNYVWVYYHLGRLSDAQIYVDKVKQTCKKFSNPYSIEYSELDCEEGWTQLKCGRNERAKVCFEKALEEKPNNPEFSSGLAIAMYHLDNNPEKQFSTDVLKQAIELSPDNQYVKVLLGLKLQKMNKEAEGEQFVEEALEKAPCQTDVLRSAAKFYRRKGDLDKAIELFQRVLESTPNNGYLYHQIGCCYKAKVRQMQNTGESEASGNKEMIEALKQYAMDYSNKALEKGLNPLNAYSDCAEFLETECYQTPFNKEVPDAEKQQSHQRYCNLQKYNGKSEDTAVQHGLEGLSISKKSTDKEEIKDQPQNVSENLLPQNAPNYWYLQGLIHKQNGDLLQAAKCYEKELGRLLRDAPSGIGSIFLSASELEDGSEEMGQGAVSSSPRELLSNSEQLN", "text": "FUNCTION: IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exhibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin-dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Up-regulates CDKN1A/p21 by down-regulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion. SIMILARITY: Belongs to the IFIT family."}
+{"protein": "MKFTLVATVLLTFSLSAFAVEYPVLTTASPDQVGFDSQKLHRLDGWIQNQIDAGYPSINLLVIKDNHIVLQKAWGYAKKYDGSTLLAHPIRATTNTMYDLASNTKMYATNFALQKLVYEGKIDVNDLVSKYIPGFKDMPGDKIKGKNKLRIIDILHHVAGFPADPQYPNKNVAGKLFSQSKSTTLEMIKKTPLEYQPGSKHIYSDVDYMILGFIIESITAIPLDRYVETTIYKPLGLKHTVFNPLMKGFTPPQIAATELHGNTRDGVIHFPNIRTNTLWGQVHDEKAWYSMGGVSGHAGLFSDTHDMAVLMQVMLNGGGYGNVKLFDDKTVAQFTRRSPEDATFGLGWRVNGNASMTPTFGVLASPQTYGHTGWTGTLTSIDPVNHMAIVILGNRPHSPVANPKVNPNVFVSGLLPAATYGWIVDQIYGSLK", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S12 family. YfeW subfamily."}
+{"protein": "MKDMSIPLLAAVSSSTEETVRPIADFHPTLWGNHFLKSAADVETIDAATQEQHAALKQEVRRMITTTANKLAQKLHMIDAVQRLGVAYHFEKEIEDELGKVSHDLDSDDLYVVSLRFRLFRQQGVKISCDVFDKFKDDEGKFKESLINDIRGMLSLYEAAYLAIRGEDILDEAIVFTTTHLKSVISISDHSHANSNLAEQIRHSLQIPLRKAAARLEARYFLDIYSRDDLHDETLLKFAKLDFNILQAAHQKEASIMTRWWNDLGFPKKVPYARDRIIETYIWMLLGVSYEPNLAFGRIFASKVVCMITTIDDTFDAYGTFEELTLFTEAVTRWDIGLIDTLPEYMKFIVKALLDIYREAEEELAKEGRSYGIPYAKQMMQELIILYFTEAKWLYKGYVPTFDEYKSVALRSIGLRTLAVASFVDLGDFIATKDNFECILKNAKSLKATETIGRLMDDIAGYKFEQKRGHNPSAVECYKNQHGVSEEEAVKELLLEVANSWKDINEELLNPTTVPLPMLQRLLYFARSGHFIYDDGHDRYTHSLMMKRQVALLLTEPLAI", "text": "FUNCTION: Sesquiterpene cyclase catalyzing the production of beta- farnesene from farnesyl diphosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MRALVSVVSLFFLGIQAHSDWSYSGDDGVGESQWSEQYPSCGGERQSPIDVKTEEVMFNPSLKPLSLVNYEKENLEFTMTNNGHTVSIDLPPSMYLETSDGTEFISKAFHFHWGGRDWELSGSEHTIDGIRSIMEAHFVHFNKEYGTYENAKDQKNGLAVLAVLFKIDEYAENTYYSDIISALKNIEKPGETTTLKDTTIRNLLPKDVHHYYTYPGSLTTPPCTENVQWFVLRDKVTLSKAQVVTIENSVMDHNNNTIQNGYRSTQPNNHRVVEANFLNVQDMYSSYHLYLKNMQKEILQPKKQKKTKKNRHFWSRK", "text": "FUNCTION: Reversible hydration of carbon dioxide. Its role in saliva is unknown. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
+{"protein": "MQNHVISLASAAERRAHITDTFGVRGIPFQFFDALMPSERLEQAMAELVPGLSAHPYLSGVEKACFMSHAVLWKQALDEGLPYIAVFEDDVLLGEGAEKFLAEDAWLQERFDPDSAFIVRLETMFMHVLTSPSGVADYCGRAFPLLESEHWGTAGYIISRKAMWFFLDRFAALPSEGLHPVDWMMFGNPDDRERMPVCQLNPALCAQELHYAKFHDQNSALGSLIEHDRCLNSKQQRRDSPANTFKHRLIRALTKISREREKRRQRREQLIGKIIVPFQ", "text": "FUNCTION: Adds the second galactose to the lacto-N-tetraose chain in lipooligosaccharide (LOS). SIMILARITY: Belongs to the glycosyltransferase 25 family."}
+{"protein": "MVDGKKRPGKDLDRIDRNILNELQKDGRISNVELSKRVGLSPTPCLERVRRLERQGFIQGYTALLNPHYLDASLLVFVEITLNRGAPDVFEQFNTAVQKLEEIQECHLVSGDFDYLLKTRVPDMSAYRKLLGETLLRLPGVNDTRTYVVMEEVKQSNRLVIKTR", "text": "FUNCTION: Mediates a global response to leucine. Exogenous leucine affects the expression of a number of different operons; lrp mediates this effect for at least some of these operons. For example it is regulator of the branched-chain amino acid transport genes (By similarity)."}
+{"protein": "MNQTAILICCLVFLTLSGIQGIPLSRTVRCTCISISNQPVNPRSLEKLEIIPPSQFCPHVEIIATMKKKGEKRCLNPESKAIKNLLKAVSEKKSKRPP", "text": "FUNCTION: Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family."}
+{"protein": "MPSSISWGLLLLAGLSCLATGCLIEDSEKSDAPKHDQENSASHKIAPNLAEFAFSLYRVLAHESNTTNIFFSPVSIATALGSLSLGTKADTHTQIMEGVGFNLTEISEAEIHQGFQHLLQNLNKSNSQLQLTTGNGLFIDHNMKLLDKFLEDIKNLYHSEAFSTDFTNTEEAKKQINTYVEKGTQGKIVDLVKDLDRDSGLALVNYIFFKGTLEKPFKADHTMEQDFHVDEATTVRVPMMNRLGMFDLHYCPTLSSMVLKMKYLGDITAIFIMPKVGRMEYVEETLTKEFLDKLLKKDYTGKNTVHFPKLSISGTIDLKPVLTRLGITKVFSHEADLSGITEDAPLRVSQALHKAVLTIDEKGTEAERHTVKGPMALTLAPEVKFNRPFLVTLYDRSTKSPLFVGRVVNPTLH", "text": "FUNCTION: Inhibitor of serine proteases. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
+{"protein": "MKKFIFCFLCLWTLNIFAASKTYPNKLNRCKITRNIFNDYEPKVFETTNNLLRKTGRLSKFYGERILIKGKILDQNCVPVADAKVYLWQVGSGGKYPYEPLKTRVDKRRFTSKSDSSFTGSGIATTNNKGEYYFISMLPYKSSRYLRSANIRIEHPSLTTLETRLDLSDKNMCDNECGEVNPILIEPQENMPSYCFDLVLQGTTLKRY", "text": "SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family."}
+{"protein": "MAANSVGKMSEKLRIKVDDVKINPKYVLYGVSTPNKRLYKRYSEFWKLKTRLERDVGSTIPYDFPEKPGVLDRRWQRRYDDPEMIDERRIGLERFLNELYNDRFDSRWRDTKIAQDFLQLSKPNVSQEKSQQHLETADEVGWDEMIRDIKLDLDKESDGTPSVRGALRARTKLHKLRERLEQDVQKKSLPSTEVTRRAALLRSLLKECDDIGTANIAQDRGRLLGVATSDNSSTTEVQGRTNNDLQQGQMQMVRDQEQELVALHRIIQAQRGLALEMNEELQTQNELLTALEDDVDNTGRRLQIANKKARHFNNSA", "text": "FUNCTION: Essential for proper morphogenesis of the vacuole. May exist as structural reinforcement on the surface of the vacuolar membrane and be required for maintenance against rupture by osmotic pressure. SUBCELLULAR LOCATION: Vacuole."}
+{"protein": "MTLNNCASMKLEVHFQCKQDDDSEEEEQCTISSHWAFEQESKCGSLMGSSALLAPPSPSLLGTSSCESVLTELSAASLPAISASLSPESADQPLLGLVPSPSNQPFLSPPQGQEGSQDKVKKHYSRSFLKHLESLRRKEKGDSRQTEPEQCLATSEKATKASSFRTCRGFLSAGFHRAKNRVTTSARVRDGETQKAWEAWPVATFRHPQPIRRRDYLVHVPGDHKPGTFPRSLSIESLCPDEGRHLADWQSSRCWGYEGRRGSCGSTGSHASTYDNLPELYPAEPIQAEAEAEAEEGEGSYAHLDDILEHVWGLQQRVELWSQTMYPDLRPGDKEEEEEEEEEEEEATSSVEVATVEVEGQDEDLAQAESQAHRGFPTQVKEEVPLIVLDQAPNVVEPLVQAEAEAPAQAQDLEQEANSTAEPISASSLSVEEGHSISDTAVSSSELDSSGNSMNEADAADAPAGLQASVPRERRDSGVGASLTRPCRKLRWHSFQNSHRPSLNSESLEINRQFAGQINLLHKGSLLRLTGFMEKYTVPHKQAWVWSMPKFMKRNKTPDYRGHHVFGVPPLIHVQRTGQPLPQSIQQAMRYLRSQCLDQVGIFRKSGVKSRIQSLRQMNENSPDNVCYEGQSAYDVADLLKQYFRDLPEPIFTSKLTTTFLQIYQLLPKEQWLAAAQAATLLLPDENREVLQTLLYFLSDIASAEENQMTAGNLAVCLAPSIFHLNVSKKDSSSPRIKSKRSLVGRPGPRDLSENMAATQGLSHMISDCKKLFQVPQDMVVQLCGSYSAAELSPPGPALAELRQAQAAGVSLSLYMEESVQELLRDAAERFKGWTNVPGPQHTELACRKAPDGHPLRMWKASTEVAAPPAVVLHRVLRERALWDEDLLRAQVLEALMPGVELYHYVTDSMAPHPCRDFVVLRMWRSDLPRGGCLLVSQSLDPEQPVPESGVRALMLTSQYLMEPCGLGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVAKIRDSFPTLQAAGPETKL", "text": "FUNCTION: Accelerates GTPase activity of RHOA and CDC42, but not RAC1. Stimulates the hydrolysis of phosphatidylinositol 4,5-bisphosphate by PLCD1 (By similarity). SUBCELLULAR LOCATION: Cell junction, focal adhesion."}
+{"protein": "MGVRAQQKEKTRRSLVEAAFSQLSAERSFASLSLREVAREAGIAPTSFYRHFRDVDELGLTMVDESGLMLRQLMRQARQRIAKGGSVIRTSVSTFMEFIGNNPNAFRLLLRERSGTSAAFRAAVAREIQHFIAELADYLELENHMPRAFTEAQAEAMVTIVFSAGAEALDVGPEQRRQLEERLVLQLRMISKGAYYWYRREQEKMSHHSE", "text": "FUNCTION: Represses the transcription of fabB, involved in unsaturated fatty acid (UFA) biosynthesis. By controlling UFA production, FabR directly influences the physical properties of the membrane bilayer. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MPEIRVTPLGAGQDVGRSCILVSISGKNVMLDCGMHMGYNDDRRFPDFSYITQSGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGPIYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCILLETFWERMNLKVPIYFSTGLTEKANHYYKLFITWTNQKIRKTFVQRNMFEFKHIKAFDRTFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQMLEVKMQVEYMSFSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLRQKIEQEFRVSCYMPANGETVTLPTSPSIPVGISLGLLKREMVQGLLPEAKKPRLLHGTLIMKDNNFRLVSSEQALKELGLAEHQLRFTCRVHLQDTRKEQETALRVYSHLKSTLKDHCVQHLPDGSVTVESILIQAAAHSEDPGTKVLLVSWTYQDEELGSFLTALLKNGLPQAPS", "text": "FUNCTION: Catalytic 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 the snRNAs 3' cleavage. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. INTS11 subfamily."}
+{"protein": "MAFQAVCILVGVFVCSTYVKGSPQPQARVYLTFDELRETKTSEYFSLSQYPLDYRILLMDEDQDRMYVGSKDHILSLNINNISQEPLSVFWPASAIKVEECKMAGKDPTHGCGNFVRVIQAFNRTHLYVCGSGAFSPVCAYLNRGRRSEDQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNSRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLVCSVTDEDGPETHFDELEDVFLLEMDNPRTTLVYGIFTTSSSVFKGSAVCVYHFSDIQTVFNGPFAHKEGPNHQLISYQGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPVHRRPLIVRIGTDYKYTKIAVDRVNAADGTYNVLFLGTDRGTVQKVVVLPTNSSARSELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGLAQVSLHRCHIYGSACADCCLARDPYCAWDGHSCSRFYPTGKRRSRRQDVRHGNPLTQCRGFNLKAYRNAAEIVQYGVKNNTTFLECAPKSPQASIKWLLQKDKDRRKEVKLNERIIATSQGLLIRSVQDSDQGLYHCIATENSFKQTIAKINFKVLDSEMVAVVTDKWSPWTWASSVRALPFHPKDIMGAFSHSEMQMINQYCKDTRQQHQQGEESQKMRGDYGKLKALINSRKSRNRRNQLPES", "text": "FUNCTION: Binds to plexin family members and plays an important role in the regulation of developmental processes. Required for normal cardiovascular development during embryogenesis. Functions as attractant for growing axons, and thereby plays an important role in axon growth and axon guidance (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the semaphorin family."}
+{"protein": "MSKLFLDELPESLSRKIGTVVRVLPSSLEIFEELYKYALNENSNDRSGRHKKPRIDVSSDLLKTDEISETNTIFKLEGVSVLSPLRKKLDLVFYLSNVDGSPVITLLKGNDRELSIYQLNKNIKMASFLPVPEKPNLIYLFMTYTSCEDNKFSEPVVMTLNKENTLNQFKNLGLLDSNVTDFEKCVEYIRKQAILTGFKISNPFVNSTLVDTDAEKINSFHLQCHRGTKEGTLYFLPDHIIFGFKKPILLFDASDIESITYSSITRLTFNASLVTKDGEKYEFSMIDQTEYAKIDDYVKRKQMKDKSMSEELKAKSKSKGQATDGTADQPSILQEATRQMQDEKKAGVFSDDDEENDQNFEAESDLSDGSGQESSDGAEDGEEAEEDDEEDDEEEDKKGQSALNRDNSFASINGQPEQELQYKEFKEPLELEDIPIEIDNDDDEDDEDGSGVEYD", "text": "FUNCTION: Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to the promoter region of histones HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2,. SIMILARITY: Belongs to the RTT106 family."}
+{"protein": "MEPKVLSIQSWVCHGYVGNKCAVFALQHLGIEVDPINSVHLSNNTAYPTWKGESLTPNKLGDLFQGLEDNHLTSNYTHVLTGYNNSVQTLHTVLKIVKKLKSENPNLIYVCDPVLGDNNELYVPEDLVEVYKNEVIPNADYIFPNQTEVEFLTGIKIKNDQDALKAIDQFHKMGVKNVVITSLFFDTNPNDIIVIGSTINDDDNNNKYNQFKIKVGPKFNDYYTGTGDLLSSLLLGWSIREPTDLSLVCEKAISILYNIINETHNSKKSIPSNKEKQYYELRLVQSRKFIENSEIRFKSEKL", "text": "FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin B6. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the pyridoxine kinase family."}
+{"protein": "MLTYAPLNFIAIGIGATLGAWLRWVLGLRLNGAGWPWGTLTANLVGGYLIGVMVALIASHPEWPAWIRLAAVTGFLGGLTTFSTFSAETVDMLERGVYATAAAYAGASLAGSLAMTGLGLATVRLLLR", "text": "FUNCTION: Fluoride-specific ion channel (PubMed:23991286, PubMed:26344196). Important for reducing fluoride concentration in the cell, thus reducing its toxicity (By similarity). Is highly specific for fluoride ions and cannot transport chloride ions (PubMed:23991286). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Note=Exhibits a dual-topology architecture: the two subunits are oriented antiparallel to each other within the membrane. SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family."}
+{"protein": "EGDFTPRL", "text": "FUNCTION: Mediates visceral muscle contractile activity (myotropic activity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pyrokinin family."}
+{"protein": "MCPRHPEPVPLAHPLPVLKEALEKVDQILRQAMSAPGVAAMSAVVIHNDTVLWTGNFGKKNGSDPASGAPNEYTMYRISSISKIFPVLMLYRLWEEGIVASLDDPLERYASTFTINNPLGLASAEQQGLILRRMASQLSGLPRRLRSTSLLWKGSTQEALNLLKDDVLVVDPGTRCHYSTLAFSLLAHVLAAHTAQGDYQRWVSENVLEPLGMADTGFDLTPDVRARLAAGFYGSGRPAPLYDLGWYRPSGQMYSTAADLAKLAVALLGGGPRRLLRPDAAKTLLAPLLACPGAYFANETGTPWEFHAQRGYRVVRKDGDLDGYAATFSLVPPLRLGLVLLLAGPRPPGPDLVARAYDELLPALERALREAEPGPAPPPTAHPFAGYFTFANLTFYEVRAGPAGELRLRQFGPRVEALVPPAFRTLALRHLHGRVFQLHVAHEFPCALPLGDAWLSLEAQHGQLVNFYPLDHHGLSPGFDVPGLNTYRVLRLRGKPVFKT", "text": "SIMILARITY: Belongs to the beta-lactamase family."}
+{"protein": "MGGGGEDEYESLPTHSVPVHLTAGALAGAVEHCVMFPFDSVKTRMQSLCPCPETKCPTPVHSLMSIVKREGWLRPLRGVNAVAAGSMPAHALYFTVYEKMKGYLTGNSAGHSNTLAYGASGVVATLIHDAIMNPAEVVKQRMQMAFSPYGSSLECARCVYNREGVAAFYRSYTTQLAMNVPFQAIHFMSYEFWQHVLNPEHKYDPKSHLIAGGLAGGLAAALTTPMDCVKTVLNTQQAAEADPANRRIFLQARYRYRGISDAVRTIYSQRGLSGFSCGLQARVIFQVPATALSWSVYELFKFMLSFEGGHSS", "text": "FUNCTION: Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCAGSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFAAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDLPHYF", "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). SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. SIMILARITY: Belongs to the glutathione peroxidase family."}
+{"protein": "MPPLILHNVPDDELYVGDDGIQRPFAMVFPQQDGSLRSRKANLETGAFGKSTRRTRSKAATPAKREDPTIAAADKIFSNWLASQNQSAPQTSVPAPAQRKPNLIPSSSSQNLAQGHDESSAPSQTRFFRKQEPTEVILRGYRNAQHQYAAINHYEQIAGRICEDYPREPPVESRRYKSELRDPAFTHRRALTPEERAKVNRAMSGEHWVKVTFESAEAADKAVYSSPQLIQGHLVYAEYYKGVPPAQDEAIPDPSVAAFGAALSRTQTLRQRNRGSFSLSGTQEAGGPDASPTSSLTADTGTLASGVEISTSTSNTLNGGAAAGGAEKSQDDEFCRVIPTVRKAKLLPMEEALLPAPTFTQRIANHIPFLRWFNGAMIGSEVPRTETGEFDWVRASLFWKLMWWLDFLLGLFGGDIRDAEKDDKED", "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. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side Note=Symmetric distribution."}
+{"protein": "MQDVLGNPAGVSSAETWGSWSEKADLGLNIVIVDDQMSARTMLRHVIEDIAPELKVYDFGDPLDALSWCEAGRVDLLLLDYRMPGMDGLEFARRLRRLPSHRDIPIILITIVGDEPIRQAALEAGVIDFLVKPIRPRELRARCSNLLQLRQQSESVKQRALSLEQRLLASMNEVEERERETLSRLARAIEYRDGGTSAFLERMSHVAGLVAEQLGLSEEEVRIIEMAAPLHDMGKIAIPDSVLLKPGKLTEDEMNVMKRHPRIGYELLSGSQNRFIQVGALIALRHHERYDGSGYPDGLVGEAIPLEARIVAVADVFDALLSARPYKEAWTMDAALAYLYAQRGRLFDPRCVDALLRGRAQLEQICGQFSTASARPGV", "text": "FUNCTION: Member of the two-component regulatory system RpfG/RpfC, which is involved in the perception and response to the diffusible signaling factor (DSF), which is essential for cell-cell signaling (PubMed:11123673, PubMed:12960398). Detection of DSF leads to the positive regulation of biofilm dispersal and the production of virulence factors (PubMed:12960398). Activated RpfG degrades cyclic di- GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in DSF pathway. May also directly control genes involved in biofilm dispersal (PubMed:15158198, PubMed:17378922, PubMed:20231439). SUBCELLULAR LOCATION: Cytoplasm Note=Localizes predominantly at the cell poles."}
+{"protein": "MSDWKEYSLGDISRNISRRFDFNAYPNVVFINTGDVLNNKFLHCEISNVKDLPGQAKKAIKKGDILYSEIRPGNGRYLFVDNDLDNYVVSTKFMVIEPNANIVLPEFLFLLLISNETTEYFKMIAESRSGTFPQITFDSVSSLSLNIPDKETQQKILDIITPLDDKIELNTQINQTLEQIAQALFKSWFVDFDPVRAKAQALSDGMSLEQAELAAMQAISGKTPEELTALSQTQPDRYAELAETAKAFPCEMVEVDGVEVDGVEVPRGWEMKALSDLGQIICGKTPSKSNKEFYGDDVPFIKIPDMHNQVFITQTTDNLSVVGANYQSKKYIPAKSICVSCIATVGLVSMTSKPSHTNQQINSIIPDDEQSCEFLYLSLKQPSMTKYLKDLASGGTATLNLNTSTFSKIEIITPSKEIIYIFQKKVVSIFEKTLSNSIENKRLTEIRDLLLPRLLNGEI", "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 adenosines in the sequence 5'-RAACN(5)TAG-3'. Methylation protects against cleavage by HindI (PubMed:4591672) (Probable). 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 (Probable) (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 type-I restriction system S methylase family."}
+{"protein": "MGNSGSKQHTKHNSKKDDHDGDRKKTLDLPPLTKSDTTHSLKSSRSLRSLRSKRSEASLASNVQAQTQPLSRRSSTLGNGNRNHRRSNNAPITPPNNHYLTSHPSSSRRLSSSSRRSSMGNNNNSELPPSMIQMEPKSPILKNSTSMHSTSSFNSYENALTDDDDDRGDDGGESPSMAKVTRINTSSSADRGSKRTPLRRHNSLQPEKGVTGFSSTSSKLRRRSDNTLPASYPLNAEAGGNGSDYFSNRSNSHASSRKSSFGSTGNTAYSTPLHSPALRKMSSRDNDDSGDNVNGRGTSPIPNLNIDKPSPSASSASKREYLSAYPTLAHRDSSSSLSPRGKGQRSSSSSSSSQRIYVSPPSPTGDFVHGSCADGDNGSRTNTMVEMKRKKPVRPVDIDEIIQRLLDAGYAAKRTKNVCLKNSEIIQICHKARELFLAQPALLELSPSVKIVGDVHGQYADLLRLFTKCGFPPMANYLFLGDYVDRGKQSLETILLLLCYKIKYPENFFLLRGNHECANVTRVYGFYDECKRRCNIKIWKTFVDTFNTLPLAAIVTGKIFCVHGGLSPVLNSMDEIRHVSRPTDVPDFGLINDLLWSDPTDSSNEWEDNERGVSFCYNKVAINKFLNKFGFDLVCRAHMVVEDGYEFFNDRSLVTVFSAPNYCGEFDNWGAVMTVSEGLLCSFELLDPLDSTALKQVMKKGRQERKLANR", "text": "FUNCTION: Essential for the maintenance of cell size and integrity in response to osmotic stress. SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily."}
+{"protein": "MSDTADSLSARGIPKSELIEDVESWLTKEKLSIEEAEVVLREKYGKYKYVESSMLAQKVRMSEKIPEFENSLSIIDTLIAKRAADESFETTFLLSDDVYTKATVQKPEKVSIWLGANVMVEYDLENARKLLDKNRGSVQKVVDELTNELSYIKDQITTTEVNMSHIVNFGVNKRRAALAVNNGAK", "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 alpha family."}
+{"protein": "MEILCEDNISLSSIPNSLMQLGDDSRLYPNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLSSFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPTLAYKSSQLQVGQKKNSQEDAEPTANDCSMVTLGNQHSEEMCTDNIETVNEKVSCV", "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": "MSSDRQRSDDESPSTSSGSSDADQRDPAAPEPEEQEERKPSATQQKKNTKLSSKTTAKLSTSAKRIQKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSSDYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYLTNRAEHDRIARQWTKRYAT", "text": "FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination (By similarity). Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "MLIAVSTNIIFIVVNTICVILGKYSVQNKKNESYSIANINLAELLASMSLGHIISSATVLGLKSLNLIQ", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaG/PsaK family."}
+{"protein": "MNSEQLLHNYVSDSLLTTLISFQEFKQQLQSYTSDEQQLQHWYELLQARDARVTSELEARIKQFFITLRSRLLRFLESEQLSHSLSLETLIDALYKINDLLQQRLQILDDAIQEKTSELAEFENMVRSPSAGDNAIPGLLQIIQSYINLLEEN", "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: Nucleus Chromosome, centromere, kinetochore Note=Associated with kinetochores (PubMed:12408861). SIMILARITY: Belongs to the NKP2 family."}
+{"protein": "MAASGLRQAAVAASTSVKPIFSRDMNEAKRRVRELYRAWYREVPNTVHLFQLDISVKQGRDKVREMFKKNAHITDPRVVDLLVIKGKMELEETIKVWKQRTHVMRFFHETEAPRPKDFLSKFYVGHDP", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly. 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 LYR family."}
+{"protein": "MRKAFTRIRLRNNRYAAYIIGFSFLAVSIILGISCGSLHIPIPAVFRVFWHQGFGGSIGSDDPMYTNIMMNIRLPRVVLAALVGAALSIAGAAFQGLLKNPLADPYTLGVSSGASVGAVVTLFLGLHLPVIGGFTLPVLSVAAALATMAAVLFFSRLVHASMSVSTLILTGVITNSFLGAFISLIIALTGDNLLPIVHWLLGSVSMRGWSYVILFLPFFLLGTILLIINGRELNVMTYGEDKAKLLGVSVQQRKMMILIAGSLLTGSAVAVSGTIGFVGLVIPHITRLLWGTDHRHLLPLSALLGAGFLVLADLLSRTIIEPIELPIGIITSLAGAPVFALILIRQHRGGRSL", "text": "FUNCTION: Probably part of an ABC transporter complex. Probably 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. FecCD subfamily."}
+{"protein": "MPPLSLLIKPASSGCNLKCTYCFYHSLSDNRNVKSYGIMRDEVLESMVKRVLNEANGHCSFAFQGGEPTLAGLEFFEKLMELQRKHNYKNLKIYNSLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEIHNLNRKDCCGLDTFSKVERAAELFKKYKVEFNILCVVTSNTARHVNKVYKYFKEKDFKFLQFINCLDPLYEEKGKYNYSLKPKDYTKFLKNLFDFWYEDFLNGNRVSIRYFDGLLETILLGKSSSCGMNGTCTCQFVVESDGSVYPCDFYVLDKWRLGNIQDMTMKELFETNKNHEFIKLSFKVHEECKKCKWFRLCKGGCRRCRDSKEDSALELNYYCQSYKEFFEYAFPRLINVANNIK", "text": "FUNCTION: Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) 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) (PubMed:18408004, PubMed:16766528, PubMed:17335281, PubMed:19489556, PubMed:23477283). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys- type sulfatase in vivo, but this activity is not physiological (PubMed:18408004, PubMed:23477283). Converts threonyl peptides to the corresponding ketone product, and also allo-threonyl peptides, but with a significantly reduced efficiency (PubMed:23477283). SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family."}
+{"protein": "MPYPFKLPDLGYPYEALEPHIDAKTMEIHHQKHHGAYVTNLNAALEKYPYLHGVEVEVLLRHLAALPQDIQTAVRNNGGGHLNHSLFWRLLTPGGAKEPVGELKKAIDEQFGGFQALKEKLTQAAMGRFGSGWAWLVKDPFGKLHVLSTPNQDNPVMEGFTPIVGIDVWEHAYYLKYQNRRADYLQAIWNVLNWDVAEEFFKKA", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. 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": "MELENKLKKVTLGHEEGFGAPCLKCKEKCEGFELHFWRKVCRNCKCGQEEHSILSNNEDDRKVGKLFEDTKYTALIAKLKTDGIPTYKRNVMILTSPVAAKKDVSINTVTYEWAPPVQNQALARRYMELIPKDKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPNEVKQMEQFVKKYKNEVLGVGDVKLPKEVEAQACGAGRSTNGSLSTLTTVKGTEDKVAAQKESTYYCFRCKENMREGDPAVYAERAGYDKLWHPSCFVCFTCNELLVDMIYFWKNGKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAEGLNWHLKHFCCFDCDCVLAGEIYVMVNDKPVCKLCYVKNHAVSCQGCHNAIDPEVQRVSYNGFHWHAAPECFICSCCSKCLIGQKFMPIQGMVFCSVDCKKKMSS", "text": "FUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. May inhibit cell growth (By similarity). Regulates cranial neural crest migration. Acts together with prickle1 to control axial elongation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cell cortex Cell junction, focal adhesion Note=Detected along actin stress fibers. SIMILARITY: Belongs to the prickle / espinas / testin family."}
+{"protein": "MSPSTGVELYLDLLKRTVSNFIYQDATHVAGLITEAAFVEEARESGEDYPTVAHTMIGMKRLNNLQHCVESALRDGVPGDVLETGVWRGGACIFARGILKAYDVRDRTVWVADSFQGFPKITDDDHPMDAEMNLHQYNEAVDLPTSLATVQRNFSRYGLLDDQVRFLPGWFKDTMPTAPFERLAVLRMDGDSYGATMDVLTHAYPRLSPGGFAIIDDYCIPACREAVHEYRDRHGISDEIVEIDRQGVYWRRSA", "text": "FUNCTION: O-methyltransferase that catalyzes the conversion of mycinamicin III to mycinamicin IV in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic. SIMILARITY: Belongs to the methyltransferase TylF/MycF family."}
+{"protein": "MEFSSPSREECPKPSGRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGTIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ", "text": "FUNCTION: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta- D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose. Plays a central role in the degradation of complex lipids and the turnover of cellular membranes. Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation. Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol. GlcCer containing mono- unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)- sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4- enine). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D- glucoside to ceramide. Can also hydrolyze cholesteryl 3-beta-D- glucoside producing glucose and cholesterol. Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N- acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers. Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N-acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside. SUBCELLULAR LOCATION: Lysosome membrane; Peripheral membrane protein; Lumenal side Note=Interaction with saposin-C promotes membrane association. Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2. SIMILARITY: Belongs to the glycosyl hydrolase 30 family."}
+{"protein": "MARESRESTTLDSHSAEDQMELLVIKVEQEESSPLAEETSWLGSPGPDRSRQRFRAFRYPEAAGPRQALSRLRELCRQWLRPDMHSKEQILELLVLEQFLTILPGELQAWVREQHPDSGEEVVALLEYLDRQLDDTPPQVPDDDDGQELLCSKAVLLTSAQGSESSQMEPVEPLLKQESLGSLPSEVRVTHVGHCGEDGVTATRLTSELQGLLKMEDVAPVLSPRWTEQDSSQMNLYKDGMQEHSGSLVSLDQDMQTKVRDLPRAEEYRDQKPEQTVCFLGEDTVPIPTGAEASEQEGKLQAAQKSATGTRRFYCRECGKSFAQSSGLSKHKRIHTGLKPYECEECGKAFIGSSALIIHQRVHTGEKPYECEECGKAFSHSSDLIKHQRTHTGEKPYECDDCGKTFTQSCSLLEHHRIHTGEKPYQCNMCPKAFRRSSHLLRHQRTHTGDKDFFVPEPYWESQSRVESHWENIETPVSYQCNDCERSFSRITSLIEHQKVHTGEKPFECQTCGKGFTRPSYLIQHQRRHTGKKTSVTVTPAVHSEVGVQLSLN", "text": "FUNCTION: Transcriptional factor that binds to the consensus sequence 5'-[GT][AG][AGT]GGGG-3' and acts as a repressor of autophagy. Specifically represses expression of genes involved in autophagy and lysosome biogenesis/function such as MAP1LC3B, ULK1 or WIPI2. Associates with chromatin at the ITGB4 and VEGF promoters (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mainly localizes in the nucleus. Under starvation conditions translocates to the cytoplasm, allowing expression of target genes involved in autophagy and lysosome biogenesis/function (By similarity). SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
+{"protein": "MPATCLLHTMLTLPSPSTRNLRSIQMPRARTFSSPSRYRNGFEHAGCRCQGSTLSQIYSSLGYSGLQASQVNEGYEHLIHMLGHSREAMQLEAGAGVAIREGFKVVDQFLKDVQHYYNSEAFSVDFSKPEIAAEEINQFIAKKTNDKITNMVKDLDSDTVMMLINYMYFRGKWDKPFDAQLTHKADFKVDEDTTVQVDMMKRTGRYDIYQDPVNQTTVMMVPYKGNTSMMIIFPDDGKMKELEESISRHHLKNWHDKLFRSSVDLFMPKFSITATSKLKGILEDMGVTDAFGDTADLSGLTEEVKVKVSQVVHKAVLSVDEKGTEAAAATTIEIMPMSLPDTVILNRPFLVLIVEDTTKSILFMGKITNPTE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
+{"protein": "MGGVAAGTRWIHHVRRLSAAKVSADALERGQSRVIDASLTLIRERAKLKAELLRALGGVKASACLLGVPLGHNSSFLQGPAFAPPRIREAIWCGSTNSSTEEGKELNDPRVLTDVGDVPIQEIRDCGVEDDRLMNVVSESVKTVMEEDPLRPLVLGGDHSISYPVVRAVSEKLGGPVDILHLDAHPDIYDAFEGNIYSHASSFARIMEGGYARRLLQVGIRSITKEGREQGKRFGVEQYEMRTFSKDREKLESLKLGEGVKGVYISVDVDCLDPAFAPGVSHIEPGGLSFRDVLNILHNLQGDVVAGDVVEFNPQRDTVDGMTAMVAAKLVRELTAKISK", "text": "FUNCTION: Catalyzes the hydrolysis of L-arginine to urea and L- ornithine. The latter can be utilized in the urea cycle or as a precursor for the synthesis of both polyamines and proline (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the arginase family."}
+{"protein": "MRFCPKCGSFLKVKGNKMVCSKCGYSDHDVEKVILKENVAHENDKTIIADGETIEGRVAISLCPRCGSVRAILLNKKKRLYRCMTCNFVYNI", "text": "FUNCTION: A potent inhibitor of RNA polymerase (RNAP) probably involved in viral defense. Destabilizes the transcription pre-initiation complex of TBP, TFB, DNA and RNAP, inhibits abortive transcription initiation, productive initiation and transcription elongation. Increases the RNAP KM for NTPs about 50-fold. Overexpression of TFS1-tip4 (TFS1 with the active tip of this protein, phenocopies this protein) in S.acidocaldarius MW001 leads to severe growth inhibition (PubMed:29203770). When bound to RNAP induces conformational changes that widen the DNA-binding channel, probably destabilizing the interaction of DNA with RNAP (PubMed:34535646). SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family."}
+{"protein": "MGKCSMKKKGVGKNVGVGKKVQKKRSISTAERKRTKLQVEKLNKSSETMIPTLLREASTQEPAKLKAETTLKAEELIKDQEKDSKVREQIRTEKSKTNDSMLKQIEMISGFSL", "text": "FUNCTION: Transcriptional repressor which negatively regulates transcription of FYV5 by binding to the promoter on the sense strand. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ADF1 family."}
+{"protein": "MPLPVQGNYTNFARLTNEQKTVWSLQFWRQARNAAFINMFLGTDANSMIQQITELRRDEKGARAVITLIADMVGDGVVGDNQLEGNEEALTAFDTVIQLDQMRAANVHEGRMADQRSIVNFRTTSRDMLAYWLADRMDQLAFLSLAGVSYAYRTNGALRGSSPFPNLTFAADVTPPSANRRLRWDGTNKVLVPNAATSDVTAADTPSYALLVNLKAYAKTKYIRGLRGDGGEEMYHVFLDPLAMAKLKLDPDYIANLRSGYTRGNVNPLFKGGIVTVDGLVIHEFRHVYNTRGMAPGAKWGASGNVDGCSMLFCGAQALGFADIGNPRWVEKEFDYDNKHGISVAKILGFLKPQFPSIYEDGNTEDFGVINVYVAA", "text": "FUNCTION: Assembles to form an icosahedral capsid. SUBCELLULAR LOCATION: Virion."}
+{"protein": "MTSSGVLCLLGALSLQVLLLQPPGAQGAPNPDNSHSSSPAPPQTAQHLSQKSLKRETLKPAAHLVGDPSVQDSIHWRANTDHAFLRHGFSLSNNSLLVPTSGLYFVYSQVVFSGASCSEITPTLLYLSHEVLLFSSKYQVHVPLLSAQKSVCSGTQGPWMRSVYQGAVFLLTQGDRLSTYTDGVSHLLQSPSSVFFGAFAL", "text": "FUNCTION: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM (By similarity). In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo. SUBCELLULAR LOCATION: Secreted Membrane Note=The homotrimer is secreted. The heterotrimer is membrane- associated. SIMILARITY: Belongs to the tumor necrosis factor family."}
+{"protein": "MITVALIDDHLIVRSGFAQLLGLEPDLQVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQLPKGMATIMLSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTVATGGCYLTPDIAIKLASGRQDPLTKRERQVAEKLAQGMAVKEIAAELGLSPKTVHVHRANLMEKLGVSNDVELARRMFDGW", "text": "FUNCTION: Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. Activates the transcription of the uhpT gene. Acts by binding specifically to the uhpT promoter region. FUNCTION: Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. Activates the transcription of the uhpT gene. Acts by binding specifically to the uhpT promoter region. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLLKVKAKVRQCLRERRTVPILFASTVRRHPDKTALIFEGTDTLWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDAQLHCLTTSRARALVFGSEMASAICEIHASLDPSLSLFCSGSWEPNAVPTSTEHLDPLLKDAPKHLPICPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGICIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANDKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDARKGRYVPLDQEAYSRIQAGEEKL", "text": "FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes. Appears to be the principal fatty acid transporter in small intestinal enterocytes. 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 (By similarity). Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis (By similarity). Probably involved in fatty acid transport across the blood barrier (By similarity). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MTSYSYRQTSAMSSFGGTGGGSVRIGSGGVFRAPSIHGGSGGRGVSVSSTRFVTSSSGSYGGVRGGSFSGTLAVSDGLLSGNEKITMQNLNDRLASYLDKVRALEQANGELEVKIRDWYQKQGPGPSRDYNHYFKTIEDLRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVGGQVSVEVDSTPGVDLAKILSEMRSQYEIMAEKNRKDAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHYNNLPTPKAI", "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": "MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK", "text": "FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins such as maltotriose. FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins. SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
+{"protein": "MSGGWMAQVGAWRTGALGLALLLLLGLGLGLEAAASPLSTPTSAQAAGPSSGSCPPTKFQCRTSGLCVPLTWRCDRDLDCSDGSDEEECRIEPCTQKGQCPPPPGLPCPCTGVSDCSGGTDKKLRNCSRLACLAGELRCTLSDDCIPLTWRCDGHPDCPDSSDELGCGTNEILPEGDATTMGPPVTLESVTSLRNATTMGPPVTLESVPSVGNATSSSAGDQSGSPTAYGVIAAAAVLSASLVTATLLLLSWLRAQERLRPLGLLVAMKESLLLSEQKTSLP", "text": "FUNCTION: Receptor for transcobalamin saturated with cobalamin (TCbl) (PubMed:18779389). Plays an important role in cobalamin uptake (PubMed:18779389, PubMed:20524213). Plasma membrane protein that is expressed on follicular dendritic cells (FDC) and mediates interaction with germinal center B cells (PubMed:10727470). Functions as costimulator to promote B cell responses to antigenic stimuli; promotes B cell differentiation and proliferation (PubMed:10727470, PubMed:11418631). Germinal center-B (GC-B) cells differentiate into memory B-cells and plasma cells (PC) through interaction with T-cells and follicular dendritic cells (FDC) (PubMed:11418631). CD320 augments the proliferation of PC precursors generated by IL-10 (PubMed:11418631). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MAKLDETLTMLKDLTDAKGIPGNEREVRQVMKSYIEPFADEVTTDRLGSLIAKKTGAENGPKIMIAGHLDEVGFMVTQITDKGFIRFQTVGGWWAQVMLAQRVTIVTKKGEITGVIGSKPPHILSPEARKKSVEIKDMFIDIGASSREEALEWGVLPGDMIVPHFEFTVMNNEKFLLAKAWDNRIGCAIAIDVLRNLQNTDHPNIVYGVGTVQEEVGLRGAKTAAHTIQPDIAFGVDVGIAGDTPGISEKEAQSKMGKGPQIIVYDASMVSHKGLRDAVVATAEEAGIPYQFDAIAGGGTDSGAIHLTANGVPALSITIATRYIHTHAAMLHRDDYENAVKLITEVIKKLDRKTVDEITYQ", "text": "FUNCTION: Putative aminopeptidase. SIMILARITY: Belongs to the peptidase M42 family."}
+{"protein": "MEDFLLSNGYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKMGGPEEFIQRFLPRELQIVRTLDHKNIIQVYEMLESADGKIYLVMELAEGGDVFDCVLNGGPLPESRAKALFRQMVEAIRYCHGCGVAHRDLKCENALLQGFNLKLTDFGFAKVLPKSRRELSQTFCGSTAYAAPEVLQGIPHDSKKGDVWSMGVVLYVMLCASLPFDDTDIPKMLWQQQKGVSFPTHLGISTECQDLLKRLLEPDMILRPSIEEVSWHPWLAST", "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": "MARLRSRTATTEKDATESSKVPVPRRRRGQHEDTEEPDTYGLEDDEKSSGRPFRILEKLPCSAEPPRYDVLTHALSVRDSAVLYNSLLASRRTWIKAEMFELYWSKQYMNMKERERMLKEGIDPDDIDQSAAREKMHKLCDGILTGGPHTLPVRLFILKNDEIEQKWQFMQESRKKEKEVRRKREAEEKERRREERKRLQQLKKERKLKEVEHTKKEKIERKRENDTERDQLRKGRKDNKGPSVLSRMGTTIKSKGLTTFSKAQQQEIDNQKMIANLNLLAQRDPALNKLMIAVANGQAPPADVERFKVFIERARNMEPPPNWKPRLSSRPVIKRTEEPTVEQQESASQTPSTPLPRKASPESSQVDNLSSPPHGSDPNSSFTEASMSDSRGELSETKSGGSLVPDSTGSSGQALDKGPTDASGSANDLSRPGATLSSTDGAPPLKQETIPVRDMGDKNADKPLEAHGAISEKGTTITIKAEEGTAPRQKRKYTKRKKEVEDEDKSMQLTTFQQKYLNGADILFEYLENSNMRFLFPKDAILEQLENEESYLMSWIVVHNKKEIEQFKLKVLKGLNKNKPNEEETEVQPCLFNVYEHPNCPEVLYTPMTVTLSNIPKKFTPIILNSVNPAESVRAYMSTILARGRRLNGFNLWYQLDAYDDKDLAESLRCELKEYEQGFKSKRQKKQL", "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: Nucleus. SIMILARITY: Belongs to the SWC3 family."}
+{"protein": "MSYMPAQNRTMSHNNQYNPPDLPPMVSAKEQTLMWQQNSYLGDSGIHSGAVTQVPSLSGKEDEEMEGDPLMFDLDTGFPQNFTQDQVDDMNQQLSQTRSQRVRAAMFPETLEEGIEIPSTQFDPQQPTAVQRLSEPSQMLKHAVVNLINYQDDAELATRAIPELIKLLNDEDQVVVSQAAMMVHQLSKKEASRHAIMNSPQMVAALVRAISNSNDLESTKAAVGTLHNLSHHRQGLLAIFKSGGIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVRLAGGLQKMVTLLQRNNVKFLAIVTDCLQILAYGNQESKLIILASGGPNELVRIMRSYDYEKLLWTTSRVLKVLSVCSSNKPAIVDAGGMQALAMHLGNMSPRLVQNCLWTLRNLSDAATKVEGLEALLQSLVQVLGSTDVNVVTCAAGILSNLTCNNQRNKATVCQVGGVDALVRTIINAGDREEITEPAVCALRHLTSRHVDSELAQNAVRLNYGLSVIVKLLHPPSRWPLIKAVIGLIRNLALCPANHAPLREHGAIHHLVRLLMRAFQDTERQRSSIATTGSQQPSAYADGVRMEEIVEGTVGALHILARESHNRALIRQQSVIPIFVRLLFNEIENIQRVAAGVLCELAADKEGAEIIEQEGATGPLTDLLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSIELTNSLLREDNNIWANADLGMGPDLQVGSLQGASALILLLYIFSISPYRLFAGYDTLPIDSMQGLEISSPVGGGGATGNSGGVNSASAGSGAVVPPSGAPTSPYSMDMDVGEIDAGALNFDLDAMPTPPNDNNNLAAWYDTDC", "text": "FUNCTION: May associate with CadN and participate in the transmission of developmental information. Can associate with alpha-catenin. Accumulates through wg signaling; arm function in wg signal transduction is required early in development for determination of neuroblast fate. Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell junction, adherens junction Note=Inner surface of cell membrane and adherens junction. SIMILARITY: Belongs to the beta-catenin family."}
+{"protein": "MAHPFTLLVTVGSTLFPSLTSHVLLPTFLSLLQSLGVQRLVVQYGRAELKLQDDVKQTLNIDSQGDGIGVWSDNDGDRVRDEKQNGMVVEVMRFTNDFEGLVGKSDAVISHAGSGSILTVLRRAPPIPLLVVPNRSLMDDHQSELADALYKDGYVMVASVEDLEEKVQPFLKIWPSQAKLFPETRKEVFREVVDDLMGYD", "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": "MGVLDHVSEYFDCSHGSSKRHKSLQTVDVRVLIDCEGCERKVRRALEGMRGIRDVTIEPNAQKVTVVGYVEPNKVVARIIHRTGKRAELYPFVPYDVVAHPYASGVYDNRAPTGYVRNTEYDPHVSRLARASSTEVRYTTAFSDENASACVVM", "text": "FUNCTION: Heavy-metal-binding protein. Binds cadmium. May be involved in cadmium transport and play a role in cadmium detoxification. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the HIPP family."}
+{"protein": "SLVVAAAAASPYSGSHDFSGFQRDEPDGVPTAQKQHDINFLLHKLYEPLHEANLKALEDSFDPLTHTANMPDAGVAVNKLMQEVKTQHLEERHHWFSVFNATQREEALLLVKVLLQCQDWPTAIGNAVYFRKMMNEETYVYALYTAIKHSPLTKHVVLPPLYEIMPHFFTSSEVIQQAYRAKMIGQPGKFNMNFTGTQNNPEHKIAYFGEDIGLSTHYINWHIEYPFWWNETFGYQIERRGENYFWVHHQLVNRFEAERISNHLQKIEKLHWERNLHEGFDPHTSYKNGEHFPFRHDDIHIEDVDKVAEVRDMIVMENRIRDAIAHGYVIDKEGNKVDINNEHGIDILGEIIESCVYNPYNEYYGSLHNMGHMMLGHQGDPHAKYYDTPSVLEHYETTLRDPAFYKLHKYIDDLFRKHKDHLKPYSRKELLFPGIAINNIHIDGPLETYFEDYEYSLMNAMDDKEEMKWEDNMEISAIIPRLRHKDFSFKVNIMNNNDENKLATIRIFAWPHRDVNGVIMPFNEGRWHAIELDKFWKYLAPGENEVTRKCDESSVTVPDVPSLKSLHEQAEAAIAGISELNLEEFVSATGLPNRLLIPKGNAAGVEFKLVVAVTDGEADSVNDEINLTTKFHHYGHHGVYLDKKSHGYPLDRRVPDERLFHEIPNFGETIVKVFNHNEHVHRHE", "text": "FUNCTION: Does not function as a hemocyanin. SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily."}
+{"protein": "MAMARLTPNGVAAALAGDTNLKPVLQIVELRGVQVNGAGVTRGERFRAVVSDGTAASSALFAAQLSDHARSGALRRGSIVQLSEYVINEVGPRRIIVILNLEVLVSECEIIGNPTALSETGSPIPNPTRVEQFNGAPQYGLMAGNSSNTTTKPSDNVPLFQNSMAGNSSNFATRPSDKVPVFQPTVQPSYRPAPNYKNHGAIMKNEAPARIIPISALNPYQGRWAIKARVTAKGDIRRYHNAKGDGKVFSFDLLDSDGGEIRVTCFNALLDRFYEVVEVGKVYVVSRGNLRPAQKNYNHLNNEWEILLENGSTVDLCPDENSSIPTQRFDFRPINEIEDAQNNAILDIIGVVTSVNPCTTIQRKNGMETQKRTMNLKDMSGRSVEVTMWGDFCNREGSQLQGMVERGIFPVLAVKAGKVSDFSGKSVGTISSTQLFINPDSAEAHSLRQWFDSGGRDASTQSISRDITPGASRNEIRKTVAQIKDEGLGMGDKPDWITVKATVIFFKNESFFYTACPNMIGDRQCNKKVTKSTNGNWTCDKCDREFEECDYRYLLQFQIQDHSGTAWVTAFQEAGQELLGCSATELNALKEREDPRFADTMLNCLFQEYLLRLKVKEESYGDERKVKNTAVKVEKVDPSGESKFLLDLISKSSALH", "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. Plays an essential role in meiotic and somatic DNA repair, but is dispensable for DNA replication and homologous recombination. Is essential for normal progression through meiosis in pollen mother cells. Is involved in repair of double-strand DNA breaks (DSBs) induced by genotoxic stresses. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the replication factor A protein 1 family."}
+{"protein": "MALPSKAALVGLANTLSEQVKRYLATAGETKSPEDHKLCIESERTPSSNEHAQAWEIVRTCDRIGSLVHGPVPWLLSNALSHLDSACLAAATHLNLQDIIVDGPSPTSLDTIVAATGVSEDLLRRILRGCAQRFIFEEVAPDQYAHTDASKMLRVTGIHALVGFSCDEVMRSGASFSDFLQQTKGKPPSWNVPSPFSLAFDPTKGLFDYYSTVDEVRGRRFDLGMGGTEATKPLVEEMFDFSSLPEGSTVVDVGGGRGHLSRRVSQKHPHLRFIVQDLPAVIHGVEDTDKVTMMEHDIRRPNPVRGADVYLLRSILHDYPDAACVEILSNIVTAMDPSKSRILLDEMIMPDLLAQDSQRFMNQIDMTVVLTLNGKERSTKEWNSLITTVDGRLETEKIWWRKGEEGSHWGVQQLRLRK", "text": "FUNCTION: Sterigmatocystin 8-O-methyltransferase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8434913, PubMed:15006741). The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). Within the aflatoxin pathway, the O-methyltransferase aflP uses both sterigmatocystin (ST) and dihydrosterigmatocystin (DHST) as substrates to yield O- methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively (PubMed:8434913). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'- oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA- binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 (PubMed:15006741). SUBCELLULAR LOCATION: Cytoplasm Vacuole. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
+{"protein": "MNLFRKKVKEWVYSFSTEDHYAEYNSNDQFNMGMRSQGASHHDVEAHAQSANDNILSMEDDIDLDSMDGTPSEGVSEVLLAWRHIDTWTSEYNPDLNATLSDPCTANDIKHAEEDLEVVLPKALKASYRIHDGQEDLESMTGTSGLIYGLQLMTLDEIVAMTQRWRSVADKLNKQATMSKHSSVGVSNGSSMGSTASIGSSSQQQREKPRNKFKLPYIPEQKSIPPETVLPLYAHAMWIPVLTDNAGNHIGIDLSPARLGKHGQVIMFGRDFDTKYVVAENWGDFLLSFANDLEAGNWLLVDDSDDYLAGEGELVFRDKKSNGPIQDYLEVLKKRSWNKYQEQLRTNQETMQSGEPTLTSTRTHKKTSSFELDDDFDHTTTTTEHNGNEFIESSVPETNSDIPQIVKKEELDETAEETKEESNELDVKTEEIAPESTQIIEETPETKEEEVSEQPEEAVAEVTVDANIEEPEQQVEEQEVLLENEVTDSVNNADANTEAVPEVEEKKTEIETETPAEPIEEEEESTNVEAPQVEEEEDSTTAEPAETVSKSKKKKNKKKNKKKNKANQDDNVNELSHDFETVQL", "text": "SIMILARITY: Belongs to the KNR4/SMI1 family."}
+{"protein": "MAPLGEVGSYFGVQDAVPFGNVPVLPVDSPVLLSDHLGQSEAGGLPRGPAVTDLDHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSNLYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPDKVPELYKDILSQS", "text": "FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the heparin-binding growth factors family."}
+{"protein": "MLPADVANRHSCEKNLYVGACKLTLPMKQLWWAVYIIDTVLVIPFAIFFYESDQEKTVTQRVKNALLWVVILLTVFCLLLGILYAVIGYADFTMRSLSSTTMAFINDFSSLNAKASCLVSAGFSLFSNVTLMVSLFFYIFPFFIDLTTLCDSVQLICLDLWLKLSVTYVITLNTIIGSILFMMFGGVGMATLPLSLIFAFKNRPKCVITRAQYVKEATDLAKRSNELKTATLGLQREERGGKKGRMFRKNVKKVQQELVFLEDDVEALNEAFPQGEKTLTVLFYLAKLVFGIVGLALSIIWLLHIIVFMLVNPPAFPFLNQVFIQLDTVGGLLGTTTFAIFCYYLVMSVISGKMHLGMRLLFLSIHPMKYQGTLDPMWHENVIASGAQPSSAMDSSSWSADRPCRPWPWP", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LIMR family."}
+{"protein": "MSDFILISDGEDEATPPPSKRARKNRTPTDLNLDTEPSLQKQPPGSASTPFFLDETPLSDDVTVLKSSFGSGTGASSGRENNFFGKRVISLESDSEDSPGPESSKKYEPVYTDSWKKPCRLEFGSSDANSDDDPSWMRRASFQSSLSKDAIEVDSDHEKEDTGVEKMGRKKQTITSKSTSLSADSLPKKKMSKDEKTRAAEEKKLQKEQEKLQKAASKAEDAEHKKLEREKQKWAKEKDKALKCIVAWIDNKVLEGSFGGLLISGLKEKCITYHVTTNPIQRSIVWTMTLPEDIAQSLPLGSKIPYVLLLYEAEDFCNLVAKKELLENVYRVRDEYPSYTMCYLTNKLLSYVNKKERVEYKDPVNGCGWRKPPIDEAIAKLSTHYIGVHSRHCVDEAEVADHVVRLTSSLAHCQVRKKLTRLSVYADGTLMSKNAADKHLIRESIWLKVLVAIPKVQPRYAIAVSKKYPSLKSLLKVYMDPNISVHEKEFLLKDLKVENLVGRDTSVGEACSKRIYRVLMSLDGTIKTDDVENGAASFTLPPSDLI", "text": "FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks, nicked Holliday junctions and also intact Holliday junctions with a reduced efficiency. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. Plays a role in DNA repair and in genotoxic stress-induced homologous recombination (HR) in somatic cells. Mediates a subset of meiotic recombination events that are insensitive to crossover interference. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EME1/MMS4 family."}
+{"protein": "MAPTQAQKVLEAFEDFLKCLDLESYQEKYRPIKTVEQDLPRELNPLPDLYDHYWKPNGNTLHFPDFETFFDQWWEKRLRPLNEFIRKYFWGCSYEFVRLGLEARLYRTAVSIWTQFHFCYRWNASCQLRLTATWELDAQGIDAQIQAEDRLIGIQIKKETYRSEAREGNRFLRRREHSALLEVPYTLQSPEELERKAQRARTREEAYRLWVKIAHHLERLPNGFVIFRESYVKDLENFLKQNATTLSGLIPWDKVAREALTGP", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-TCGA-3' and cleaves after T-1."}
+{"protein": "MASPPAHRSSKAADEELPKASSTFHPSLWGSFFLTYQPPTAPQRANMKERAEVLRERVRKVLKGSTTDQLPETVNLILTLQRLGLGYYYENEIDKLLHQIYSNSDYNEKDLNLVSQRFYLLRKNGYDVPSDVFLNFKTEEGGFACAAADTRSLLSLYNAAYLRKHGEEVLDEAISSTRLRLQDLLGRLLPESPFAKEVSSSLRTPLFRRVGILEARNYIPIYEKEATRNEAVLELAKLNFNLQQLDFCEELKHCSAWWNEMIAKSKLTFVRDRIVEEYFWMNGACCDPPYSLSRIILTKITGLITIIDDMFDTHGTTEDCMKFAEAFGRWDESAIHLLPEYMKDFYILMLETFQSFEDALGPEKSYRVLYLKQAMERLVELYSKEIKWRDQDYVATMSEHLQVSAESIGANALTCSAYAGMGDMSITKETFEWALSFPQFIRTFGSFVRLSNDVVSTKREQTKDHSPSTVHCYMKEHGTTMDDACEKIKELIEDSWKDMLEQSLALKGLPKVVPQLVFDFSRTTDNMYRDRDALTSSEALKEMIQLLFVEPIPE", "text": "FUNCTION: Sesquiterpene synthase involved in the production after herbivore attack of a blend of volatiles that attracts natural enemies of herbivores (PubMed:15075399, PubMed:21607717). Converts farnesyl diphosphate to sesquithujene, (S)-beta-bisabolene, (Z)-alpha- bergamotene, sesquisabinene B and several minor products (PubMed:25940560, PubMed:15075399, PubMed:21607717). Can also act in vitro as a monoterpene synthase, converting geranyl diphosphate to (S)- (-)-limonene, beta-myrcene and 11 other monoterpenes (PubMed:25940560, PubMed:15075399). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MDVIGNITDLSPTVSGIPDECGLEPHDFLEVKFFLISVVGTLIGLFGLFGNATTALILTRPSMRNPNNLFLTALAVFDSCLLITAFFIYAMEYIIEYTAAFDLYVAWLTYLRFAFALSHISQTGSVYITVAVTIERYLAVCHPKSSKNMCGPGGAAWTILGVTTFAVVFNCTKFFELQVTVNPSCPDGSNWQSYILLPSAMASNPIYQQVYSLWVTNFVMVFFPFLTLLLFNAIIAYTIRQSLEKYDFHNQKSVVAALSASVNLPRNIAGISSRNELKEKSREATLVLVIIVFIFLGCNFWGFVLTLLERIMGQETLMVEHHIFYTFSREAINFLAIINSSINFVIYLLFGKDFRKELVVVYGCGIRGISLRLPVQDKFVIWRHWKRTKSRISMNTTNRTRHKISLPQTLVEHANLERLEETRFLAHHEDGVQTQVSPIHALRNGSTPKIDTLQDLTSNGRPCKTSIIDDNGTVVCTVTEFP", "text": "FUNCTION: G-protein coupled receptor (GPCR) that forms a heterodimer with daf-38 to control dauer formation and behavior (PubMed:22665789, PubMed:23509272). Receptor for the ascaroside pheromone ascr#2 (PubMed:22665789). Required for the response to dauer inducing pheromones, specifically the ascaroside ascr#2 (PubMed:22665789, PubMed:23509272). May serve neuronal specific roles in response to ascr#2 with expression in ASI neurons controlling dauer formation in larvae, and expression in ASK neurons playing a role in longevity and hermaphrodite repulsion (PubMed:22665789, PubMed:23509272). May function upstream of the daf-11, daf-7 and daf-2 signaling pathways (PubMed:22665789). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, cilium Golgi apparatus Note=Localizes to the cell membrane in the presence of daf-38, but localizes to the Golgi apparatus in the absence of daf-38. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDWKTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHFATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMVIVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGGFVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIVAKYHTLYIDALRKLFDQHKTKFGISETQELEII", "text": "FUNCTION: Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters (PubMed:15220349, PubMed:15671038, PubMed:16106050, PubMed:28420705). Shows a preference for medium chain acyl-CoAs from C12 to C16 in length and fatty alcohols shorter than C20, as the acyl donors and acceptors, respectively (PubMed:15220349, PubMed:15671038). Also possesses acyl- CoA retinol acyltransferase (ARAT) activity that catalyzes 11-cis- specific retinyl ester synthesis (PubMed:16106050, PubMed:24799687). Shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis- retinol, 13-cis-retinol, and all-trans-retinol substrates (PubMed:24799687). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the diacylglycerol acyltransferase family."}
+{"protein": "MLTRQQKELIVKEMSEIFKKTSLILFADFLGFTVADLTELRSRLREKYGDGARFRVVKNTLLNLALKNAEYEGYEEFLKGPTAVLYVTEGDPVEAVKIIYNFYKDKKADLSRLKGGFLEGKKFTAEEVENIAKLPSKEELYAMLVGRVKAPITGLVFALSGILRNLVYVLNAIKEKKSE", "text": "FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors (such as IF-2, EF-Tu, EF-G and RF3). SIMILARITY: Belongs to the universal ribosomal protein uL10 family."}
+{"protein": "CYFQNCPRGXXXAMSDLELRQCLPCGPGGKGRCFGPSICCGDELGCFMGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCNDESCVTEPECREGASFPRRA", "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": "MKKKCIAMLLAGGQGSRLRSLTKNIAKPAVPFGGKYRIIDFTLSNCTNSGIDTVGVLTQYQPLLLHSYIGIGSAWDLDRRNGGVTVLPPYSASSGVKWYEGTANAIYQNMNYIEQYDPDYVLVLSGDHIYKMDYQQMLDYHIAKQADATISVIEVPWEEASRFGIMNTNENMEIVEFAEKPANPKSNLASMGIYIFNWPLLREYLQIDNADPHSSHDFGKDVIPRLLRENKRLVAYPFKGYWKDVGTVKS", "text": "FUNCTION: Catalyzes the synthesis of ADP-glucose, a sugar donor used in elongation reactions on alpha-glucans. SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family."}
+{"protein": "MARQALDLFDEGFQELTPSEFFRKNKQMLGFTGKIRSLTIVFHELITNSFDAAEEAGILPEIKIDLKRIGKDHYILRHQDNGPGIPEKYIPKVFCTMFAGSKFRNIQSRGQQGLGCSGCVLLSQMTTGKPVKVISGTMENGELKGVKMTLKMDVKKNQGLILEKEEVEVDGTGVCIELHFKDVSYSLSEQGAYEYIRRTMIANPHARIVFNDPTGNRYVFNRASDVIPPMPKEVLPHPWGVTADDLIFMAKHTDKRRFGSMLKSNLSRMSSMKIKELEELTGIDLNKRPKDMKWEEAEQIVEAFKKMKFMSPPTSGLIPIGEEQIDKGMKEILQPEFTATVTRKPKTYRGGIAFIVEAGIAYGGNSGRLVGDQRKAEIMRFANRVPLTFDAGSCAITEGVKSLDWKRYGIRDLENAPISIFVNVVSTNVPYLSTGKQSVSPEPEILGEIRQATMIVARKLHKYLRKKKAAKEEAQRAKIFESYVPVIIKQAALLAEREEPDYRELLDTVTRRAKLEILGGITE", "text": "FUNCTION: Relaxes both positive and negative superturns and exhibits a strong decatenase activity. SIMILARITY: Belongs to the TOP6B family."}
+{"protein": "MNSSSTLTVLNLTLNASEDGILGSNVKNKSLACEEMGIAVEVFLTLGLVSLLENILVIGAIVKNKNLHSPMYFFVGSLAVADMLVSMSNAWETVTIYLLNNKHLVIADTFVRHIDNVFDSMICISVVASMCSLLAIAVDRYITIFYALRYHHIMTARRSGVIIACIWTFCISCGIVFIIYYESKYVIICLISMFFTMLFFMVSLYIHMFLLARNHVKRIAASPRYNSVRQRTSMKGAITLTMLLGIFIVCWSPFFLHLILMISCPQNVYCSCFMSYFNMYLILIMCNSVIDPLIYALRSQEMRRTFKEIVCCHGFRRPCRLLGGY", "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": "MGKNYKSLDSVVASDFIALGITSEVAETLHGRLAEIVCNYGAATPQTWINIANHILSPDLPFSLHQMLFYGCYKDFGPAPPAWIPDPEKVKSTNLGALLEKRGKEFLGVKYKDPISSFSHFQEFSVRNPEVYWRTVLMDEMKISFSKDPECILRRDDINNPGGSEWLPGGYLNSAKNCLNVNSNKKLNDTMIVWRDEGNDDLPLNKLTLDQLRKRVWLVGYALEEMGLEKGCAIAIDMPMHVDAVVIYLAIVLAGYVVVSIADSFSAPEISTRLRLSKAKAIFTQDHIIRGKKRIPLYSRVVEAKSPMAIVIPCSGSNIGAELRDGDISWDYFLERAKEFKNCEFTAREQPVDAYTNILFSSGTTGEPKAIPWTQATPLKAAADGWSHLDIRKGDVIVWPTNLGWMMGPWLVYASLLNGASIALYNGSPLVSGFAKFVQDAKVTMLGVVPSIVRSWKSTNCVSGYDWSTIRCFSSSGEASNVDEYLWLMGRANYKPVIEMCGGTEIGGAFSAGSFLQAQSLSSFSSQCMGCTLYILDKNGYPMPKNKPGIGELALGPVMFGASKTLLNGNHHDVYFKGMPTLNGEVLRRHGDIFELTSNGYYHAHGRADDTMNIGGIKISSIEIERVCNEVDDRVFETTAIGVPPLGGGPEQLVIFFVLKDSNDTTIDLNQLRLSFNLGLQKKLNPLFKVTRVVPLSSLPRTATNKIMRRVLRQQFSHFE", "text": "FUNCTION: Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:22353623). Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway (PubMed:22353623). Can also activate other fatty acids including heptanoate, octanoate and nonanoate (PubMed:22353623). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MNSNEDIHEERIEVPRTPHQTQPEKDSDRIALRDEISVPEGDEKAYSDEKVEMATTNASSNFGSNESAKDGESIGAFSNPHEALMQSKLREESQSKTILPSDDLSQQLETEESKVEEALKRITSPPLPPRADCIEESASALKSSLPPVLAGNKNDQAPLDRPQLPPRQVVNAETLHLKAPHGNATPSKSPTSAVGNSSSSTPPTLPPRRIEDPLDLAAQKHFLASTFKRNMLFYKSEDNSIKCDLDKNILNLKEDSKKINNNEIPEEVSSFWLKVIGDYQNILINDIETLHFQLSRGIPAAYRLVVWQLVSYAKSKSFDPIYETYLTEMAPFDVQEFENQLKMMDEVPSEYVKRISNVLKAYLLFDPECEFSTDIAYIINMILDVCEEEANAFGLLVRLMKVYGLRLLFLPSASEIDILCYKFDRLVEEFYPEIHNHMVEKGVRSSMFLPGFFTTLFQKKLPTEIQPRIGDMVFLEGIDSIMRILATLLSNSRDHLLKMGFDDMLELLKSGLLDAYIKQNDGTRGDTLLSNECMDKLLQDSMMKVAITPKTMKKYSSEYEEIHRLDNEKEVQYKSITEKNLHLQKHVRKLENDYTSLNREHVTIANELVKNRLNIESVLNENNGYKLQILDLKKKLDSEKKKQVLGVYVPNDLKKDLEETMKKNTQVMDENLKLQDRISELERLIEEIKTANKNGTLFEYSNSKNNPLGAGWSGFKKVFK", "text": "FUNCTION: Probable GTPase-activating protein which stimulates the GTP hydrolysis rate by GYP5 of YPT1 and SEC4. Involved in ER to Golgi trafficking and polarized exocytosis. SUBCELLULAR LOCATION: Cytoplasm Bud Bud neck. SIMILARITY: Belongs to the GYP5 family."}
+{"protein": "MSSSFFCFFLFCFQTCLIQNVYSQCLGRVGPGGPPLGPYGGPLGGPGYGPVGYGGCGGYGGSGIGNVAVAGELPVAGSAAVLGQVPVIGAVEFAGPACAVGSVSISGACGPTCGCGGSPYY", "text": "FUNCTION: This protein is one of many from the eggshell of the silk moth. SIMILARITY: Belongs to the chorion protein family."}
+{"protein": "MASHHQLLCLNILGFRKPGISTEDYRNYMVNVHAPLVAGLMEKYGFLHFTMSHASEQSPQLMDQLYDAQFANTASYDCCVQIVFPSIECFVNMKADPYFKQTVGPDHEKFADTKRSQMMIGWFSPLLINGQQTDSLSAAE", "text": "FUNCTION: Dehydratase; part of the gene cluster that mediates the biosynthesis of ustilaginoidins, dimeric gamma-naphthopyrones isolated from different fungal species (PubMed:31050129). The first step in the biosynthesis of ustilaginoidins is the production of gamma- naphthopyrone precursor YWA1 by the non-reducing polyketide synthase ustP, via condensation of one acetyl-CoA starter unit with 6 malonyl- CoA units (PubMed:31050129). YWA1 is then probably substrate of the ustZ to yield norrubrofusarin via a dehydration reaction (Probable). A key enzyme in the biosynthetic pathway is the laccase ustL, which catalyzes the oxidative dimerization of norrubrofusarin to ustilaginoidin A (PubMed:31050129). It can produce the M- and P- atropisomers in varying amounts, depending on the reaction conditions (PubMed:31050129). For the biosynthesis of 3-methylustilaginoid in derivatives such as chaetochromin A, a methylated derivative of YWA1 is required (Probable). The C-methylation is considered to be catalyzed by ustM, the phosphopantetheine attachment site of which indicates that it acts on the growing polyketide chain before release of the product (Probable). For the biosynthesis of chaetochromin A, it is assumed that saturation of the D2 double bond takes place before dimerization, and is probably catalyzed by an external reductase because no candidate gene was identified within the cluster (Probable). SIMILARITY: Belongs to the tpcK family."}
+{"protein": "MNLMINLKPLTFLPFFGRLVFLSGVIYNTAWANTVIPVDNSRPDETFSQTSPKQHLFSQKPKPTEPTSSASSQQISLTIEQLASRPDLVLRALIPALKNNDMRGVEILLPIYAKQSPDPFLLKWAQAVVARKQGKLNESVRLYRQIIAEKPNLQPARLQLAIALTQNRENEAAKAQFNQLRSENLPAPLLTLIDSYIDTINQRDSWNVYGGVNYLHENNVNNAPPKGTKAEGFTPSSQPEKAHGLSYFINLSKNWSLAHGFFTEFSADINGKYYWDNHKYDEFSTRLNLGGGYRNAKTEVKLMPFVEQFWYVGGENATKDARTLHRYSKSSGINLDVDYWLTPNWKISTVLEYTEQRYIQPQRQNSNGNSYSISNTLIYMPNSQQFWFVGLDYYQKNTRLKAYAFERQGIRLGWGQEWPKGISTRLQTSYATRTYRAPSAEKNMIFAPSFFKVVQKNHEYGVNFTIWHRSLHWLGITPKITWAYQKTTSNNPFSEYDRNRIYLTFSKTF", "text": "FUNCTION: Required for correct export to the cell surface of some cell outer membrane lipoproteins (tested with PM1514) upon heterologous expression in E.coli and probably also in Pasteurella. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Slam family."}
+{"protein": "MMFRLTSVSCFLLVIACLNLVVLTNACLRDGQSCGYDSDCCRYSCCWGYCDLTCLINGKRATFQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin I2 superfamily."}
+{"protein": "MSDFENLSGNDKELQEFLLIEKQKAQVNAQIHEFNEICWEKCIGKPSTKLDHATETCLSNCVDRFIDTSLLITQRFAQMLQKRGGGDL", "text": "FUNCTION: 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. The Tim8- Tim13 complex mediates the import of some proteins while the predominant Tim9-Tim10 70 kDa complex mediates the import of much more proteins (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the small Tim family."}
+{"protein": "MSSSSSSRIHNGEDVYEKAEEYWSRASQDVNGMLGGFEALHAPDISASKRFIEGLKKKNLFGYFDYALDCGAGIGRVTKHLLMPFFSKVDMEDVVEELITKSDQYIGKHPRIGDKFVEGLQTFAPPERRYDLIWIQWVSGHLVDEDLVDFFKRCAKGLKPGGCIVLKDNVTNHEKRLFDDDDHSWTRTEPELLKAFADSQLDMVSKALQTGFPKEIYPVKMYALKPQHTGFTNN", "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. SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family."}
+{"protein": "MDANNTFDSDLIHAIFKHIWARRFRERERSDAIDATEAEVALGTTKKNRLASANANALKLSCELLKSFVSEAVQRAAIIAEAEGMEKIEATHLERILPQLLLDF", "text": "FUNCTION: Acts in the same pathway as FANCM to restrain class II meiotic crossing over (CO), and acts with FANCM during meiosis to repair interstrand cross-links (ICLs). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CENP-X/MHF2 family."}
+{"protein": "MPFAQIYMIEGRTEAQKKAVIEKVSQALVEATGAPMANVRVWIQEVPKENWGIAGVSAKELGR", "text": "FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate. SIMILARITY: Belongs to the 4-oxalocrotonate tautomerase family."}
+{"protein": "MAEAEHTASTPGGESSRRDFLIYGTTAVGAVGVALAVWPFIDFMNPAADTLALASTEVDVSAIAEGQAITVTWRGKPVFVRHRTQKEIVVARAVDPASLRDPQTDEARVQQAQWLVMVGVCTHLGCIPLGQKAGDPKGDFDGWFCPCHGSHYDSAGRIRKGPAPLNLPVPPYAFTDDTTVLIG", "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 inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Rieske iron-sulfur protein family."}
+{"protein": "MLTATPLPHQLLATFLLVLASATQPAVPASTDRAALLAFRASLSPPSRAALSSWSGPLSPSWLGVSLHPATAPAPSVTTPSVAELSLRGLNLTGVIPAAPLALLRRLRTLDLSANALSGELPCSLPRSLLALDLSRNALSGAVPTCLPSSLPALRTLNLSANFLRLPLSPRLSFPARLAALDLSRNAISGAVPPRIVADPDNSALLLLDLSHNRFSGEIPAGIAAVRSLQGLFLADNQLSGDIPPGIGNLTYLQVLDLSNNRLSGSVPAGLAGCFQLLYLQLGGNQLSGALRPELDALASLKVLDLSNNKISGEIPLPLAGCRSLEVVDLSGNEISGELSSAVAKWLSLKFLSLAGNQLSGHLPDWMFSFPLLQWLDLSSNKFVGFIPDGGFNVSEVLNGGGGQGTPSESVLPPQLFVSASVDTVSWQLDLGYDVQATTGIDLSGNELCGEIPEGLVDMKGLEYLNLSCNYLAGQIPAGLGGMGRLHTLDFSHNGLSGEVPPGIAAMTVLEVLNLSYNSLSGPLPTTKFPGALAGNPGICSGKGCSENARTPEGKMEGSNHRGWLGGWHGENGWVSLGAFCISTMTSFYVSLATLLCSSNARNFVFRPVRVEY", "text": "FUNCTION: Receptor-like protein that regulates shoot meristem proliferation. Based on additive and synergistic phenotypes of double mutants, it is probable that unlike CLV1 and CLV2 in A.thaliana, FAE2 and TD1 do not function exclusively in a single pathway. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
+{"protein": "MHVLYIMGQDSGGLPHYTAELANSMSEYARVTVLKPNETSADEVLRDEITVINAFKPTDISMQNLFDLKLDVLDSIRGLFSFWNIKLINQIDPDIVHDPTDEFPQVNLFSWVHSVYEDRPYVVTSHETKHGGAGGVLRVVNPLLSLVPDFEKSAAIVHSADQRELLLNNHKAVDEVHVIPHGVYSFFRELDYDEQKEEDKHALFFGSLIPPKGIEYLIDAVPKVSEEVPGFSLTIAGSGSIPDECADVVEQYSDVINIRNEFIPNEEVGTLFSRAQVVVLPYRRGWQTGHSGTLSIAFAFGKPIITSEVGDFPELVGESGAGIVVEPESPEAIADGLIEVFSSDSALDQMSNASSRVADRLSWEKIAEQHFEVYQNLL", "text": "FUNCTION: Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn- 532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Together with Agl6, mediates the addition of sugars 1 and 2 to dolichol phosphate in the tetrasaccharide. SIMILARITY: Belongs to the glycosyltransferase group 1 family."}
+{"protein": "MKTLEKKLAEDFKIVFSDKELLETAFTHTSYANEHRLLNISHNERLEFLGDAVLQLTISHYLFDKYPQKAEGDLSKMRSMIVREESLAGFSRNCHFDRYIKLGKGEEKSGGRQRDTILGDLFEAFLGALLLDAGLKAVEAFLNQVVIPKVENNNYERVTDYKTALQELLQVDGDVLIDYEVLKESGPAHAKCFEVAVSMNHEKLSSGTGKSKKLAEQEAAKNALEKLQRGS", "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). In this organism endogenous ribonuclease 3 and Cas9 are required for correct coprocessing of pre-crRNA and the trans-encoded small RNA (tracrRNA). Cas9, crRNA and tracrRNA are required for cleavage of invading DNA (Probable). Complements pre-crRNA and tracrRNA coprocessing defects in an rnc deletion in S.pyogenes strain 370 (PubMed:24270795). 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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonuclease III family."}
+{"protein": "MEEEARPAVGDGEAATPARETPPAAPAQARAASGGVPESAPEPKRRQLGTLLQPTVNKFSLRVFGSHKAVEIEQERVKSAGAWIIHPYSDFRFYWDLIMLLLMVGNLIVLPVGITFFKEENSPPWIVFNVLSDTFFLLDLVLNFRTGIVVEEGAEILLAPRAIRTRYLRTWFLVDLISSIPVDYIFLVVELEPRLDAEVYKTARALRIVRFTKILSLLRLLRLSRLIRYMHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPMLQDFPSDCWVSMNRMVNHSWGRQYSHALFKAMSHMLCIGYGQQAPVGMPDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADTRQRIHEYYEHRYQGKMFDEESILGELSEPLREEIINFTCRGLVAHMPLFAHADPSFVTAVLTKLRFEVFQPGDLVVREGSVGRKMYFIQHGLLSVLARGARDTRLTDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDHFNAVLEEFPMMRRAFETVAMDRLRRIGKKNSILQRKRSEPSPGSSSGGVMEQHLVQHDRDMARGIRGLAPGTGARLSGKPVLWEPLVHAPLQAAAVTSNVAIALTHQRGPLPLSPDSPATLLARSARRSAGSPASPLVPVRAGPLLARGPWASTSRLPAPPARTLHASLSRTGRSQVSLLGPPPGGGGRRLGPRGRPLSASQPSLPQRATGDGSPRRKGSGSERLPPSGLLAKPPGTVQPSRSSVPEPVTPRGPQISANM", "text": "FUNCTION: Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel HCN family."}
+{"protein": "MADQVQDVHPMEWGPGKTPQGRARLPSSFDATVKDPVAAVHSENLVCRVPMHRIRHLESLVYDLMQNSSANVNQEQVGVTPSPGDQPHVPDYPTPSAAHAPSTNQEPASAAVSPADYGSMQSTGGGANYVGSAHWAAVLDGIAELKDHLDNEESHHSDSQGVDPPCLQVTGPQLLYGCPKPADKDEILSSIPARSVVDRLVSRYFNSFEMSPAVLHSVQFLKEYEEFWEDPQTTSPIWLGLLFTIMCLATQFEKSRLDPGVQSPAVLSMERELQEMVDTFRLRIPQCLVLGSYAKGGPFVLETLMLYIAAEIFLSNDAEIEIWILMGNTVQLALHMGYHRDPKHFKGLSPFTAEMRRRIWATIVEMDLGLSAQMGLPRMIKHWQTDTQEPSNFQDSDFDSATVEMPPSRLNTDLTPILYRLVKARLMTTIGYIWDFSADVRPYPYTEVQKMDDKLDQARKSIPECLKWHSMARNITDSPQHIMQKVILETVFYRAKIVLHRKYMFLPLAQSASSRRIVLESALKLLDYQHMLQEETQPFCQLYQERWRVSSLVNHDFLLATSILCYYLQHARGATPQLSESASFDETIMTSLSRSHDIWLQSSNSSKEARKVVRALAVILGRVNTPSADAAGESGLVFGLQSTYPPSTTNDYSQAPMITPTAEWQEMDGQSQWLPGPRVIQRLTYDMQRQQMRWGL", "text": "FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of Equisetin (PubMed:23614392). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLRKVFAVVSVLLVVSAAKVTKLVLDDHYVNRVVGGEVAKNGSAPYQVSLQVPGWGHNCGGSLLNNRWVLTAAHCLVGYEPSDLMVLVGTNSLKEGGELLKVDKLLYHSRYNRPQFHNDIGLMRLEQPVQFSELVQSVEYLEKAVPVNATVRLTGWGRTSTNGNVPTLLQSLNVVTLSNEDCKAKMGNPKNVDLGHVCTLTKAGEGACNGDSGGPLVYEGKLVGVVNFGVPCGRGFPDGFARVSYYHEWVRTTMANNS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
+{"protein": "MGVRDSHGEAAGTPDPVEKGIATLNTIRIGVKAMVHKDGALRKAEILSIKQRKDGLAFYVHYVDFNKRLDEWVASSRLDLSQEVEWPQPEKPEKKKSGPAKAPSKNKRVRAGSRDVSATPDTLTGKNTNVGKAQRPSKAGGKENRGDETPADLSMLASEAVSADGTPKAVSEDIDMMDASFTDAKEIKEEERALGLMSREEEIEKLRTSGSMTQNPTEVHRVRNLDRLQMGKYDIEPWYFSPYPASFSDAEVVYIDEFCLSYFDNKRAFERHRTKCTLTHPPGNEIYRDDNISFFEVDGRRQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMCTRDETGCHLVGYFSKEKESGEGYNLACILTLPQYQRRGYGRLLISFSYELSKREGKVGSPEKPLSDLGLLGYRQYWRETLVEILLDSGRETVSENELAMLTSMTEKDVHETLVTFKMLRYNKGQWIIVLTDEVIEERNKRLEKEKIKGSRKIDPARLQWKPPVFTASSRTWNW", "text": "FUNCTION: Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (By similarity). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity). The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination (By similarity). Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2- hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Following DNA damage, localizes to sites of DNA damage, such as double stand breaks (DSBs). SIMILARITY: Belongs to the MYST (SAS/MOZ) family."}
+{"protein": "MAGILAWFWNERFWLPHNVTWADLKNTEEATFPQAEDLYLAFPLAFCIFMVRLIFERFVAKPCAIALNIQANGPQIAPPNAILEKVFTAITKHPDEKRLEGLSKQLDWDVRSIQRWFRQRRNQEKPSTLTRFCESMWRFSFYLYVFTYGVRFLKKTPWLWNTRHCWYNYPYQPLTTDLHYYYILELSFYWSLMFSQFTDIKRKDFGIMFLHHLVSIFLITFSYVNNMARVGTLVLCLHDSADALLEAAKMANYAKFQKMCDLLFVMFAVVFITTRLGIFPLWVLNTTLFESWEIVGPYPSWWVFNLLLLLVQGLNCFWSYLIVKIACKAVSRGKVSKDDRSDIESSSDEEDSEPPGKNPHTATTTNGTSGTNGYLLTGSCSMDD", "text": "FUNCTION: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:17977534, PubMed:17609214, PubMed:23530041, PubMed:26887952, PubMed:31916624). Can use other acyl donors, but with less efficiency (By similarity). N- acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively (PubMed:17977534, PubMed:23530041, PubMed:26887952, PubMed:31916624). Ceramides generated by CERS6 play a role in inflammatory response (By similarity). Acts as a regulator of metabolism and hepatic lipid accumulation (By similarity). Under high fat diet, palmitoyl- (C16:0-) ceramides generated by CERS6 specifically bind the mitochondrial fission factor MFF, thereby promoting mitochondrial fragmentation and contributing to the development of obesity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
+{"protein": "MSTLKNTFFITPPDTPTQAGPENIFYDFNDGARVLLPEGKWHVRLLDADSENILFCCDVDKGWVTSSKKYFVRFRIQVFRQGEETPLLDETLKLKDRPVLISFPTGTLGDLLGWFPYAERFQSLHKCRLECTMSQDIIDLLAPQYPQIQFSTPDKPRTVAPYATYRVGLYFGGDTNNQPVDFRKVGFHRSAGYILGVDPREAPVRLDLSAPRVIQEPYVCIATQSTCQAKYWNNGTGWSEVIAHLKSLGYRVMCIDRDAHYGQGFVWNHIPWGAEDFTGKLPLQERVNLLRHASFFIGLPSGLSWLAWATRIPVVLISGFSLPNSEFYTPWRVFNSHGCYGCWDDTSLNFDHHDFLWCPRHKNTDRQFECTRLITGAQVNGVINKLHRSLTEQGVEATLKKGVSNE", "text": "FUNCTION: Glycosylates the TibA adhesin."}
+{"protein": "MTARYGFGSISFPNKCGIFLSTTKNFIAPNFPIHYWTAPAFELRGRMNPDLEKNTLTLKNAAAVAALDNLRGETITLPTEIDRRLKPLEEQLTRMAKVLDSLETAAAEAEEADAQSEECTRTEIIRNESIHPEVQIAKNDAPLQYDTNFQVDFITLVYLGRARGNNSPGIVFGPWYRTLQERLVLDRPVAARGVDCKDGRISRTFMNTTVTCLQSAGRMYVGDRAYSAFECAVLCLYLMYRTSNSVHEPQVSSFGNLIEHLPEYTETFVNYMTTHENKNSYQFCYDRLPRDQFHARGGRYDQGALTSHSVMDALIRLQVLPPAPGQFNPGVNDIIDRNHTAYVDKIQQAAAAYLERAQNVFLMEDQTLLRLTIDTITALLLLRRLLWNGNVYGDKLKNNFQLGLIVSEATGTPTNNVILRGATGFDGKFKSGNNNFQFLCERYIAPLYTLNRTTELTEMFPGLVALCLDAHTQLSRGSLGRTVIDISSGQYQDRLISLIALELEHRRQNVTSLPIAAVVSIHDSVMLQYERGLGMLMHQPRVRAALEESRRLAQFNVNSDYDLLYFVCLGVIPQFASTP", "text": "FUNCTION: Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. Participates in the interaction between the capsid and the tegument through interaction with the large tegument protein/LTP. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae CVC2 protein family."}
+{"protein": "MKVEFAPLNIPLARRLQTTAVFQWVFSFLLLAQCCIGIFICLVLARVWLLLALYVLWLYLDWETPQAGGRRWEWVRNWPVWKYFKDYFPIRLVKTCDLDPQHNYIMGFHPHGVLVAGAFGNFCTNYTGFKELFPGLTPYLHILPFWFRCPFFREYIMSVGLVSASKKSVNHVLSKEDGGNVSIIVTGGAEESLDAHPGSLTLNILKRKGFIKVALKRGAYLVPVFSFGENELFQQVSNPKGSLLRCVQERLQRIMGLAMPLFHARGIFQYSFGLMPYRMPIHTVVGRPIPVKETSHPTQEEIESLHQQYLGALQELFEEHKKRYGIPEHESLIFI", "text": "FUNCTION: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the diacylglycerol acyltransferase family."}
+{"protein": "MASVNSRSGFCNSNSTFYSKRTPIPLPPNPSLDVTTFISSQAHRGRIAFIDASTGQNLTFTELWRAVESVADCLSEIGIRKGHVVLLLSPNSILFPVVCLSVMSLGAIITTTNPLNTSNEIAKQIKDSNPVLAFTTSQLLPKISAAAKKLPIVLMDEERVDSVGDVRRLVEMMKKEPSGNRVKERVDQDDTATLLYSSGTTGMSKGVISSHRNLIAMVQTIVNRFGSDDGEQRFICTVPMFHIYGLAAFATGLLAYGSTIIVLSKFEMHEMMSAIGKYQATSLPLVPPILVAMVNGADQIKAKYDLSSMHTVLCGGAPLSKEVTEGFAEKYPTVKILQGYGLTESTGIGASTDTVEESRRYGTAGKLSASMEGRIVDPVTGQILGPKQTGELWLKGPSIMKGYFSNEEATSSTLDSEGWLRTGDLCYIDEDGFIFVVDRLKELIKYKGYQVAPAELEALLLTHPEITDAAVIPFPDKEVGQFPMAYVVRKTGSSLSEKTIMEFVAKQVAPYKRIRKVAFVSSIPKNPSGKILRKDLIKIATSNSKL", "text": "FUNCTION: Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors (PubMed:16963437, PubMed:18267944). Converts 12-oxo-phytodienoic acid (OPDA) and 3-oxo-2- (2'-pentenyl)-cyclopentane-1-octanoic acid (OPC-8:0) into OPDA-CoA and OPC-8:0-CoA, respectively (PubMed:16963437, PubMed:18267944). Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester (By similarity). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "IALQSPAGAARIRDYLYNELSK", "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). SIMILARITY: Belongs to the peptidase S14 family."}
+{"protein": "MKYINVRGCNGSGKTTLLRCLARDPLCRVINVIVPDHKPIPVTYAPDGIAIIGDYTPAAAGATTAGLDRIKTQAAAKAVAELVGRDPDVKAVLFEGVVVSTIYGPWQEWSKANGGMIWAFLDTPLEVCLKRIQERNGGKPIKEDQVADKHRTIARVRDKALADGETVRDIHWETALKDIKAVIENLG", "text": "FUNCTION: Phosphorylates 5-hydroxymethyluracil (5hmdU) into 5- phosphomethyl-2'-deoxyuridine (5-PmdU) on DNA as a step in the pathway leading to thymidine hypermodifications in the viral genome (PubMed:34522950). The phosphate is added internally to the DNA polymer (PubMed:34522950). Also transfers glutamate to 5- pyrophosphoryloxymethyldeoxyuridine (5-PPmdU) to produce 5-Nalpha- glyutamylthymidine (Nalpha-GluT). 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). SIMILARITY: Belongs to the thymidylate kinase family. 5-hmdU DNA kinase subfamily."}
+{"protein": "MRKVMLAEKAGFCFGVKRAVDMALLTQKEYNKKIYTLGELIHNNDVVDKLKDNNVYPIGIEDIDNLKENDVILIRSHGISEEIYKILLSKGLTVINATCPFVTKIQEKVKKYNELGYDIVIVGDKYHPEVIGINGWCDNKAIISKQGENLENITSESKVCIVSQTTEKLENWEKVLKEVKNRAIEVISFNTICNATSERQKIAKDLSNKVDFMVVIGGKQSSNTTKLYEICKSNCNETIHVENSGEIPENILKNKNCVIGVTAGASTPDWIIEEAISKMSENQISNETNNEMADAMKFIAENEGKIYVGASVTGEIIQVSEKEVFLNINYKRDGVIPKSEIDDDGKDLKELFTVGDKIVAKIIKLKDADNYVVLSVKELQREQGYKEIKEAFENKTTLNVVVKEDVKGGIIASYKGIRIFIPASHVELFHVDNLKEYIGKSFDVAIIEYSTKKRQTKIVASRRALLSKEKEKVEETVWNKLEEGQVVEGEVKRLTDFGAFVEIEGVDGLLHVSEISWGRVEKPADVLKIGDKIKVYVLSVDKENKKLSLSVKKLTENPWNNVEEKYPVGSVVLGKVIRFADFGAFVKLEPGVDGLVHISEISHKRIAKPSDALNVGEEIKAKILEVSSEEKKIGLSIREVEE", "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: In the N-terminal section; belongs to the IspH family."}
+{"protein": "MATKTAGVGRWEVVKKGRRPGVGAGAGGRGGGRNRRALGEANGVWKYDLTPAIQTTSTLYERGFENIMKRQNKEQVPPPAVEPKKPGNKKQPKKVATPPNQNQKQGRFRSLEEALKALDVADLQKELDKSQSVFSGNPSIWLKDLASYLNYKLQAPLSEPTLSQHTHDYPYSLVSRELRGIIRGLLAKAAGSLELFFDHCLFTMLQELDKTPGESLHGYRICIQAILQDKPKIATANLGKFLELLRSHQSRPAKCLTIMWALGQAGFANLTEGLKVWLGIMLPVLGIKSLSPFAITYLDRLLLMHPNLTKGFGMIGPKDFFPLLDFAYMPNNSLTPSLQEQLCQLYPRLKVLAFGAKPDSTLHTYFPSFLSRATPSCPPEMKKELLSSLTECLTVDPLSASVWRQLYPKHLSQSSLLLEHLLSSWEQIPKKVQKSLQETIQSLKLTNQELLRKGSSNNQDVVTCDMACKGLLQQVQGPRLPWTRLLLLLLVFAVGFLCHDLRSHSSFQASLTGRLLRSSGFLPASQQACAKLYSYSLQGYSWLGETLPLWGSHLLTVVRPSLQLAWAHTNATVSFLSAHCASHLAWFGDSLTSLSQRLQIQLPDSVNQLLRYLRELPLLFHQNVLLPLWHLLLEALAWAQEHCHEACRGEVTWDCMKTQLSEAVHWTWLCLQDITVAFLDWALALISQQ", "text": "FUNCTION: Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM214 family."}
+{"protein": "DPGSQGVGAEAENTGERTGGEAEAPAEGENGERSGGDAALGGESEGKAENESEGDIPAERRGDDEDEGEIQAEGGEVKGDEDEGEIQAGEGGEVEGDEDEGEIQAGEGGEVEGDEDEGEIQAGEGGEVEGDEDEGEIQAGEGGEVKDDEGEIQAGEAGEVEGEDGEVEGGEDEGEIQAGEGGEGETGEQELNAEIQGEAKDDEEGVDGEGGGDGGDSEDEEEEDEEEDEEEEEEEEEEEEEENEQPLSLEWPETRRKQAIYLFLLPIVFPLWLTVPDVRRLEAKKFFVITFLGSILWIAM", "text": "FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). Critical component of the visual transduction cascade, controlling the calcium concentration of outer segments during light and darkness. Light causes a rapid lowering of cytosolic free calcium in the outer segment of both retinal rod and cone photoreceptors and the light-induced lowering of calcium is caused by extrusion via this protein which plays a key role in the process of light adaptation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC24A subfamily."}
+{"protein": "MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVSALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA", "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": "MTLQKKIIELLGVKPAIIPEIEIKNCVDFLKKYLVNHVHIKSLIVGVSGGQDSTLTAKLCQMTAETLRKEKNDITYQFIALRLPYGIQYDEKDCQDAIRFIQPDQIFNVNIKKAVLSSEKSLKKSGVIISDYVRGNEKARERMKVQYSIAAMKQGLVVGTGHAAENITGFFTKYGDSGTDINPIAKLNKRQIRLLLKNLNCPKHLYLKKPMADLEDEHPQQDDESVLGVTYDAIDSYLEQKKIDIRSQKIIEALYLNTLHKRNLPITQ", "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. SIMILARITY: Belongs to the NAD synthetase family."}
+{"protein": "MKLTCMMIVAVLFLTAWTFVTAVPHSSNVLENLYLKARHEMENQEASKLNMRDDDCEPPGNFCGFPKIGGPCCSGWCFFACA", "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 family."}
+{"protein": "MQHRGFLLLTLLALLALTSAVAKKKDKVKKGGPGSECAEWAWGPCTPSSKDCGVGFREGTCGAQTQRIRCRVPCNWKKEFGADCKYKFENWGACDGGTGTKVRQGTLKKARYNAQCQETIRVTKPCTPKTKAKAKAKKGKGKD", "text": "FUNCTION: Secreted protein that functions as cytokine and growth factor and mediates its signal through cell-surface proteoglycan and non- proteoglycan receptors (PubMed:18469519, PubMed:12573468, PubMed:12122009, PubMed:10212223, PubMed:24458438, PubMed:15466886, PubMed:12084985, PubMed:10772929). Binds cell-surface proteoglycan receptors via their chondroitin sulfate (CS) groups (PubMed:12084985, PubMed:10212223). Thereby regulates many processes like inflammatory response, cell proliferation, cell adhesion, cell growth, cell survival, tissue regeneration, cell differentiation and cell migration (PubMed:12573468, PubMed:12122009, PubMed:10212223, PubMed:10683378, PubMed:24458438, PubMed:22323540, PubMed:12084985, PubMed:15466886, PubMed:10772929). Participates in inflammatory processes by exerting two different activities. Firstly, mediates neutrophils and macrophages recruitment to the sites of inflammation both by direct action by cooperating namely with ITGB2 via LRP1 and by inducing chemokine expression (PubMed:10683378, PubMed:24458438). This inflammation can be accompanied by epithelial cell survival and smooth muscle cell migration after renal and vessel damage, respectively (PubMed:10683378). Secondly, suppresses the development of tolerogenic dendric cells thereby inhibiting the differentiation of regulatory T cells and also promote T cell expansion through NFAT signaling and Th1 cell differentiation (PubMed:22323540). Promotes tissue regeneration after injury or trauma. After heart damage negatively regulates the recruitment of inflammatory cells and mediates cell survival through activation of anti-apoptotic signaling pathways via MAPKs and AKT pathways through the activation of angiogenesis (By similarity). Also facilitates liver regeneration as well as bone repair by recruiting macrophage at trauma site and by promoting cartilage development by facilitating chondrocyte differentiation (By similarity). Plays a role in brain by promoting neural precursor cells survival and growth through interaction with heparan sulfate proteoglycans (By similarity). Binds PTPRZ1 and promotes neuronal migration and embryonic neurons survival (PubMed:10212223). Binds SDC3 or GPC2 and mediates neurite outgrowth and cell adhesion (PubMed:12084985, PubMed:1768439). Binds chondroitin sulfate E and heparin leading to inhibition of neuronal cell adhesion induced by binding with GPC2 (PubMed:12084985). Binds CSPG5 and promotes elongation of oligodendroglial precursor-like cells (By similarity). Also binds ITGA6:ITGB1 complex; this interaction mediates MDK-induced neurite outgrowth (PubMed:15466886, PubMed:1768439). Binds LRP1; promotes neuronal survival (PubMed:10772929). Binds ITGA4:ITGB1 complex; this interaction mediates MDK-induced osteoblast cells migration through PXN phosphorylation (PubMed:15466886). Binds anaplastic lymphoma kinase (ALK) which induces ALK activation and subsequent phosphorylation of the insulin receptor substrate (IRS1), followed by the activation of mitogen-activated protein kinase (MAPK) and PI3-kinase, and the induction of cell proliferation (PubMed:12122009). Promotes epithelial to mesenchymal transition through interaction with NOTCH2 (PubMed:18469519). During arteriogenesis, plays a role in vascular endothelial cell proliferation by inducing VEGFA expression and release which in turn induces nitric oxide synthase expression. Moreover activates vasodilation through nitric oxide synthase activation (By similarity). Negatively regulates bone formation in response to mechanical load by inhibiting Wnt/beta- catenin signaling in osteoblasts (By similarity). In addition plays a role in hippocampal development, working memory, auditory response, early fetal adrenal gland development and the female reproductive system (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pleiotrophin family."}
+{"protein": "MGTNGVRVFVILYLLAVCGCIEYDVDDNVHICTHTNVSHINHTSWYYNDKVIALATEDKTSGYISSFIKRVNISLTCLNISSLRYEDSGTYKGVSHLKDGVIVTTTMNISVKANIVDLTGRVRYLTRNYCEVKIRCEITSFALNGSTTPPHMILGTVDKWKYLPFPTDDYRYVGELKRYISGNPYPTESLALEISSTFNRFTIVKNLNDDEFSCYLFSQNYSFHKMLNVRNICESKWKALNNNDNASSMPASHNNLANDLSSMMSQLQNDNDDNNDYSAPMNVDNLIMIVLITMLSIILVIIVVIAAISIYKRSKYRHIDN", "text": "FUNCTION: Plays a role in the spread of virus to neighboring cells ex vivo. SUBCELLULAR LOCATION: Host cell membrane; Single-pass membrane protein Note=May localize at the surface of cytoplasmic extensions at the periphery of the cell. SIMILARITY: Belongs to the orthopoxvirus OPG049 family."}
+{"protein": "MMRLTLKSKVLLLAMVPVLLFALVLSGGAVLILKKQADAEVKDTRERLLGDRRAELEHYVQIAMGSIQAEYDRSANGDLNARAEAIARLSKIKYGKDGYIFGYDSQVVRLFRGDSPVDVGKSFRDRRDPSGVYLNRELVEAGRNGSHYVTYTSPLPGNESVMVPKLSYTLYLPKWDMVIGSAINLDGVEAQLVEIKQDIDERIGTLIASIVGIAGVLLVVLLVIGLAVANAMLRPLHQIRQNLDDIAAGEGDLTRRLPVTSYDELGELAGSFNRFVEKIHGLVRQIAGMTGDLKQLVEQMSAQAERSEQAMERQRHETDQVATAINEMSAAAHEVAQSAQRAAEAAQQTDHEGQAAKRVVDGSIERIHALVDEIRDSGTSLDSLQQDVQSIVSVLGVIRSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRALASRTQQSTQEIQGMIDRLQQGTNAAVDAMRRSGEAGEGTSNQANQAGDSLDAIAQLIATINAMNAQIASAAEEQTAVAEEINRSVHQIAGAVDSVADEAQQGAQTARSLAQLGQGLGRLVGQFRI", "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 (Probable). Directly recognizes five C4-dicarboxylic acids: L-malic, citramalic, citraconic, bromosuccinic and methylsuccinic acids (PubMed:17933940, PubMed:29391435). Three of the identified ligands act as chemoattractants (L-malic, D,L-bromosuccinic and L-citramalic acids) whereas two of them (L-methylsuccinic and citraconic acids) behave as antagonists by inhibiting the downstream chemotaxis signaling cascade (PubMed:29391435). Antagonists compete with chemoattractants, thereby decreasing the affinity for chemoattractants and the subsequent chemotactic response (PubMed:29391435). Acts through the che chemosensory pathway (PubMed:29391435). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein family."}
+{"protein": "MDNGVETPQGQKTQPINLPPDRKRLRKHDGLGKGVKRKLFAEDSSPLKKQIPACSDMETLSSPVKFGCKSRSASALDESFGKCKHETACDCSAIEELLCHESLLDSPMKLSNAHTIFSSDKWKLELEKIIASKQIFLDMSENVELVAYGETLCNLRIFEKISSPFLFDVQSEERSYSVVYVPHNKELCGQFCQPEKTMARVLGVGAYGKVFDLDKVAIKTANEDESVISAFIAGVIRAKSGADLLSHDCVINNLLISNSVCMDHKVSLSRTYDVDLYKFEDWDVRNVMNYYSVFCKLADAVRFLNLKCRINHFDISPMNIFINHKKEIIFDAVLADYSLSEIHPEYNGTCAIAKEYDRNLQLVPISRNKFCDMFNPGFRPLVANAMILVNVCEAFDGENNPLRHCNLDLCAFAQVVLLCVLRMTDKRGCREAQLYYEKRLFALANEACRLNPLRYPFAYRDACCKVLAEHVVLLGLLFYRDVVDIYEKIYDFLDERGEFGLRDLFEATFLNNSKLTRRQPIRGGLASLQSSEYGEKLLHDLRALFLITSSADLDKDTSSLFQM", "text": "FUNCTION: Phosphorylates the antiviral nucleoside analog ganciclovir. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. HCMV ganciclovir subfamily."}
+{"protein": "MSKKSTNIFTCSGAQHKWIQVVNIDGNIFSIYVCFFVCFFFYLEPSSDDESYEVLDLTEYARRHHWWNRLFGRNSGPLTEKYSVATQIVIGGVSGWCAGFLFQKVGKLAATAVGGGFLLLQIASHGGYIQIDWKRVEKDVNKAKRKIKKEANKTPEINTVIEKSTDFFKKNIVVSGGFVGGFLIGLAS", "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": "MAGQAPNMLAPPTDDELLHAQADLWRHSLYFVTSMAFQCAVKLGIPTAIHRAGGTASLPDLVAALSLPPAKLPFLRRLMRLLVHSGVFAAADDTTGSAGTYRLTPLSWLLVEGEGGAPVVDGHPCQVPVVLAGTSRHFVEAAMGLAEWFRKDVPAAAPPSPFEEVHGAVLFDESMASLHPEVDTVFNQALAAYDHSGFATVLRECSEVFQGVQSLTDCRGGDGAAAKAIVEAFPHIKCTVLDFPRVIGNKRGDGVVNYVAGDMFRAIPPAQAVMLKLVLHHWSDEDCVKILTQCKKAIPARKDGGKVIIIDIVIGAPSGPLLEAQLLMDVGMMVATKGRQRDENDWRDLFKKAGFNNYKIVKKLRARAVFEVYP", "text": "SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
+{"protein": "MAAQLLEEKLTCAICLGLYQDPVTLPCGHNFCGACIRDWWDRCGKACPECREPFPDGAELRRNVALSGVLEVVRAGPARDPGPDPGPGPDPAARCPRHGRPLELFCRTEGRCVCSVCTVRECRLHERALLDAERLKREAQLRASLEVTQQQATQAEGQLLELRKQSSQIQNSACILASWVSGKFSSLLQALEIQHTTALRSIEVAKTQALAQARDEEQRLRVHLEAVARHGCRIRELLEQVDEQTFLQESQLLQPPGPLGPLTPLQWDEDQQLGDLKQLLSRLCGLLLEEGSHPGAPAKPVDLAPVEAPGPLAPVPSTVCPLRRKLWQNYRNLTFDPVSANRHFYLSRQDQQVKHCRQSRGPGGPGSFELWQVQCAQSFQAGHHYWEVRASDHSVTLGVSYPQLPRCRLGPHTDNIGRGPCSWGLCVQEDSLQAWHNGEAQRLPGVSGRLLGMDLDLASGCLTFYSLEPQTQPLYTFHALFNQPLTPVFWLLEGRTLTLCHQPGAVFPLGPQEEVLS", "text": "FUNCTION: E3 ubiquitin ligase that plays a role in several processes including innate immnity, autophagy or inflammation (PubMed:28594402, PubMed:34512673). Negatively regulates miRNAs by modulating the ubiquitination and stability of TNRC6A, a protein involved in RNA- mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (PubMed:24778252). This ubiquitination results in the suppressed expression of miR-138-5p leading to increased autophagy (PubMed:31160576). Upon enteroviral infection, promotes 'Lys-63'- mediated ubiquitination activation of IFIH1/MDA5 leading to innate signaling cascade (PubMed:28594402). Mechanistically, selectively recognizes MDA5 filaments that occur on dsRNAs (PubMed:33373584). Plays also a role in limitation of inflammation through different mechanisms. First, promotes 'Lys-48'-mediated ubiquitination of VCAM1 leading to its degradation and limitation of LPS-induced lung inflammation (PubMed:31310649). In addition, negatively regulates inflammasome activation by promoting 'lys48'-linked ubiquitination of NLRP3 which is critical for the inhibition of NLRP3 inflammasome activation in resting macrophages (PubMed:34512673). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRIM/RBCC family."}
+{"protein": "MAEVHIIGQILKAVDFAEPHLYCKWSLQSGNAWRLVQGEVQGQSHVASHRLQSSSDFAQPLDIHLSTASVQGWPRLLVEVYAVNVLQQSWPVGYGFVHVPSTPGTHRLEIGTWKVAPNGLWQSLRERFGGGGAALSKTDLLYSGVERYKLQTLSSGKVIVELNLIFRKFDEYGVEFK", "text": "FUNCTION: Probable component of the tectonic-like complex (also named MKS complex), a complex localized at the transition zone of primary cilia (PubMed:27646273, PubMed:25447994, PubMed:27577095). Has a role in ciliary structure and function (PubMed:27646273). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Note=Localizes at the transition zone (TZ), a region between the basal body and the ciliary axoneme (PubMed:27646273). In spermatocytes, localizes in the transition zone and the migrating base of the spermatid ciliary cap (PubMed:25447994, PubMed:27577095). Co-localizes with the tectonic-like complex (PubMed:27646273). SIMILARITY: Belongs to the B9D family."}
+{"protein": "MIINFLLNSIVGTVKLDENPNINLKNNINNNDNNKENSIEINDYLQTLVKEEDFKNQHTDPNFKFLALRSTKVPIDEYNPENYQLKFVQIITRHGRRTPESKRYPLTMWTCNSLDQLITNKDTSRPDCNMGQLTVLGIVDQINVGKAYRNLFINNLHFLDNKYNKDQIFIRSSNRERTISSARSFMHGLYGGSFADDQEKSPNHSSFLILDEKDENMYPRSSPKYNFLKGLLKKHKAVIEENEKSNLKEFTEKIKNIFEDSKFDTAFYVPSWRSYAGLVNSFDCFRNNGLPLPKGFTNDVIQRMYEESAKEFKSARLFPEMSILGIGRFVNDLTKQMYLKSVNDPSVKDLKLSLYSGHDTTLAALLVAYDMYEDNVHPVTSSALEYLLFQDKNYKEPEVVTKSNEKELINHQYVKVIFNHKPIHIGPCKDKEVDGMCPLSEFLKISQSIIPTNYDEQSKITDEEKNKYIQEST", "text": "SIMILARITY: Belongs to the histidine acid phosphatase family."}
+{"protein": "MSKIFVNPSAIRAGMADLEMAEETVDLINRNIEDNQAHLQGEPIEVDSLPEDIKKLDISEGRSKSLVDNPQDVECRMSEDFQMDEVEDPNIQFQSYLDNIGIQIVRKMRTGERFFKIWSQTVEEIISYVGVNFPSQSGKTTENKSTQTTPKKVKTEPSSTPAKRSDQLSKTEMAAKTASGPPALEWSTTNDEDDVSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKEAKSVPGVTSLARDGLRLPLRCILGWVGSSHSKKFQLLVGSEKLNKIMQDDLNRYMSC", "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": "MEIKYLLTVFLVLLIVSDHCQAFLFSLIPNAISGLLSAFKGRRKRNLDGQIDRFRNFRKRDAELEELLSKLPIY", "text": "FUNCTION: Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). 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": "MNFNDIDNQMYGNLEEDAELLAELAAIQEEEMGRVSRPAAPARGAPPAARGRPAPAAPANVPGLDPRLLAAALADNHGDGGDEELEMDEDLLNELNGLVGGGGGGGAAPTVPTRAAPRAPGPSGPPPSASAPNSQLGHLKQLHVYYMKAHKSAEQAGEGPKARRYKRAVDKLVELIRAVERGKTIDESEIPVAPPNFSSAAAEPLPPPAPTAQPAHHPPAPPIRQAAHAAESSPPPIPQRKSSAPAPTAAAPPATKEPTDPKKAAIYRILHHRRDLHKQNARAAIADKDKESAKESVEMAKAFDQAIAALNECSADEMDMNDVPPSPPPYRKPAPPQPQAPPTSAGPLGFIEELQQRQQRFQKMAEKAKTEGNERKMKMNMRLAGQFDEAIKEAKRGKLVNVGELPSLPDMGPLPPQTAPGQAAPKLHQRPPPQEVGPLAPSGVEGKSRNQGQLEFLLERQAQFKQAAIHAKSRGDVEAAKKYLVEMKGFDKMIQAAQAGLPVSIKATPIPPQAQTASTTLQPRIQSAAASSSTGVENRGEKLSLLEKTLIEQVRSAETNQMRFTRLGDVGKVRLFEGWGKVAKQDLLLVREVAKRGLQVPKFHYEMRQIPSADLFPDLADDVIELTIVSCRDVPLPSGYETHHANLFIKYTFPAVVNDLPQTGKTKLIAGTASPDFGESIMLNIGSGKSRNSKLQRTFKRGGLKFEVFQKGGFMRSDKLLGTCEWKLEKLEHSAEMEESLPLKDGRKAVGGLLSAKVRIRQPIGDAKAQHIAQKWLILDN", "text": "SIMILARITY: Belongs to the CC2D1 family."}
+{"protein": "MWSVRLYPLALTLLFQCVSPAAARPSGCVDDVEVVQEIGSKEIQAPVVRFEISLTTQSIDAAGIGFREAIFINDAFIGPTLYAKQGDRIEFVVHNYMQQDTSIHFHGIDQRSTPWSDGVPGLTQSQIRPGASFLYNWTAHDAGTYFYHSHAKSQMMDGLYGAVVIAPDDEAPRPFHLISSGEADQAAMLAAEKLMRPIFVSDWSQYTSAEYHGIQHAANIDFSCMDSILVQGVGSQYCLSEEELDDMTNPIVLQLLKELAGGHMTPKGCIPPLQMFNGDFELHLENVPELAYNKCKGGQSSKGNYTIDVDTSIGWAALTFVNPGGLYPLQLSIDSHELYVYAVDGQYVYPIVADRVLVNTGSRISVMIKLDQEKARHVVRVANDYLNQILGGFAELAYDGATNAPKHPHPKTNYGGKLISSEMVSFVPEDSSPYPALRPAQSADSTFKLRLKKLGQPYRAYEWTQTGSLGYNISHEHDDPPLLLQNVEDVPATELTLKTQIGDWVDLVLVTAGPFAQAHPMHKHGNKVFLIGSGSGSFPWESVEEAIPHLPEGTFNFQDPPYLDTFNTVEMEGQANDTWTAVRYKAEYAGAWLFHCHVQTHLSGGMGMVVLDGVDAWPEVPLAYQEWNGFEPPALS", "text": "FUNCTION: Multicopper oxidase; 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 multicopper oxidase family."}
+{"protein": "MKVAVVVALLCFVCYTAAETCSADGDCKNTICDASHDLECHRGQCTCVNHATACSSAADCSGSCTIFGRHGRWHCVDAKCRCFFV", "text": "FUNCTION: Slow-binding inhibitor of serine proteases. The inhibitor rapidly binds to the protease forming a weak enzyme-inhibitor complex, and this is followed by a slow isomerization forming a tight-binding enzyme-inhibitor complex. Active against subtilisin A with a dissociation constant of 0.18 nM. Active against perkinsin. Not active against thermolysin, papain or pepsin. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MDARKEGLLRKPRFSAQPRVGMGLLPFFLACAVYLLVRNADQPPWVNVLLKILPVLYLAGFLGTAHPGGGYRALLQGALLCSAVGDACLVWPEALRYGMAAFGLAHLLYLRAFGLTPLKPGLLLPLLLVSALYFRVLHPHMPPQVVWPLLAYSIVLVAMLWRGLARGGSAHWGALLFVLSDSVLAWNIFTYLVPHGHLLVMTTYYSAQMLITLSAFQNPRLKSH", "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": "MSYRELRNLCEMTRSLRYPRLMSIENFRTPNFQLVAELLEWIVKKFEPESNLDAHEVQTEADRVAFIKNAVLLMLQNSRIKMNPKKLYQADGHAVQELLPAMKILYQAKAEDPNTDNSPKWTQVKNKLSSKMQEVRITRQLSSQLPETGALLSELLSRQEFISQQHERAASRAVPLAEAEKVLQATVQNIAQETEQLSNKLNNVASDEAELDEKIERKKREYEQLQKRFAKLQSFRPQYMDEYERFEERLKKLYEVYVLNFRNLSYLRKVHDDLARSERQRQEELEKAMRMAVEKMRLEQEKKDAIGLHDDDGSDAPLVDRRQSVRKVYGNMMGGDASDDDEDDEDDEDDEIIRMDDNVAQHHKRELHRQEEDEERSEADYMVGITTAHVADDAKSDLSSGDDF", "text": "FUNCTION: Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium (PubMed:28479320). May be required for ciliary entrance and transport of specific ciliary cargo proteins such as che-3 which are related to motility (PubMed:28479320). Required for sensory cilia biogenesis (PubMed:15713455). SUBCELLULAR LOCATION: Cell projection, axon Cell projection, cilium Cell projection, dendrite. SIMILARITY: Belongs to the CLUAP1 family."}
+{"protein": "MDNRKRLAYAIIQFLHGQLRHGGLSSDAQESLEVAIQCLETAFGVTLEDSDLALPQTLPEIFEAATASKEMPQDPRGPDRTPPSEEDSAEAERLKTEGNEQMKLENFEAAVHLYGKAIELNPANAVYFCNRAAAYSKLGNYVGAVQDCERAIGIDPGYSKAYGRMGLALSSLNKHAEAVAYYKKALELDPDNDTYKSNLKIAELKLREAPSPTGGVGSLDIAGLLNNPHFITMASSLMNSPQLQQLMSGMISGGHNPLGTPGSSPQHSDLASLIQAGQQFAQQMQQQNPEFVEQIRSQVVRSRTPSASHEEQQE", "text": "FUNCTION: Co-chaperone that binds misfolded and hydrophobic patches- containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states. Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex (By similarity). Binds directly to HSC70 and HSP70 and regulates their ATPase activity (PubMed:12878599). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis. SIMILARITY: Belongs to the SGT family."}
+{"protein": "MSSIKSYTIGNELGRGSFATVYKGEHVASGSPVAIKSVLRAKLNRKLLENLGSEISILKQMKHPHVVELLDFQETPTHFHLVMEYCSLGDLSFFLKKKKELSETLPLVASLLRRYPSNTRGLHEELVRHFVHQLSAALEFLRQKNLVHRDIKPQNLLLCPPSLSEMDAQNANLYGRWELPILKIADFGFARILPASALAETLCGSPLYMAPEILRYEKYNAKADLWSVGAVTYEMVVGKPPFKANNYVELLKTIEQSNDVIGFGREPPSEDMQDFVRCLLKKNPADRIGFKEYFEHPIIANKQVIGSGEELDRSQLDPRMYISEYIQEADLPKLDLDREMDSFSQKRSTQKSSPKNSTNKTLSSTVKNPLLELTSPSPGSSLLLTRKNESLFLESEYVVVEKRQVEVNTLADELAREPDERRPSSERRFSLTYGAPTGAMARALSMASARLLGEKKNGAGHGSGNGSRNGSGNGSGNGARLSAGAALSGTSSGTSTTGKSPPVPATTTPSLSEREIVETLEEIAAKARSIALLADVKYSQIQDDVDNPDMNLPDSVSSSIAEEAMLLYVKTLSLLSLAMDQAGAWWSNNHKDNKMVSSHFNEIIQWTRSAFNESLERAETVKKKVSSGTTHTTAEKLIFDRALEMSRDAAVQEISGDFTGCESAYTTSIWMLEALLEDDEDGLGEEDRRIVERFISSITKRLVILRGQQE", "text": "FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. 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. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER- associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8. SUBCELLULAR LOCATION: Cytoplasm Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily."}
+{"protein": "MDRVTRYPILGIPQAHRGTGLVLDGDTSYTYHLVCTGPEASGWGQDEPQTWPTDYKAQQGVLRQGVSYSVRAYPGQPSPRGLHLETGEDEGLKVYRLGARDAHQGRPTWAVHPEDGEDEEMKTYRLDAGDAVPRGLCDLERERWAIIQGQAVRKSGTVATLQAAPDHGDPRTPGPPRSTPLEENVVDREQIDFLAARQQFLSLEQANKEVPHSSPARGTPAGPSPGVSQAPKAFNKPHLVNGHVVPTKPQGKGVFREENKVRAVPAWASVQVADDPGSLAPVESPGTPKETPIEREIRLAQEREADLREQRGLRRAADHQELVEIPSRPLLTKVSLITAPRRERGRPSLYVQRDMVQETQREEDHRREGLHVGRASTPDWVSEDPQPGLRRALSSDSILSPDSILSPAPDARAADPAPEVRKVNRIPPDAYQPYLSPGTPQLEPSAFGAFSKPSGLSTVDTEAATSPKATMSPRHLSESSGKPMSTKQEPWKLPRGSPQANRGVVRWEYFRLRPLQFRAPDEPQQAQVPHVWGWEVAGAPALRLQKSQSSDLLERERESVLRREREVAEERRNALFPEVFSPTPDESCDQNSRSSSQASGITGSYSVSESPFFSPIRLHSSLAWTVEDPVDSAPPGQRKKEQWYAGINPSDGINSEVLEAIRVTRHKNTMAERWESRIYASEEDD", "text": "FUNCTION: Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus (By similarity). SUBCELLULAR LOCATION: Cell junction, focal adhesion Cytoplasm, cytoskeleton Cytoplasm, cell cortex Note=Predominantly localizes to cortical actin structures during interphase and mitosis. Present in retraction fibers, which are formed at former adhesion sites during mitosis, and at spicular membrane protrusions in re-attaching cytokinetic cells. Partially colocalizes with cytoplasmic F-actin. Not detected at microtubules at interphase, nor at spindle during mitosis (By similarity). SIMILARITY: Belongs to the MISP family."}
+{"protein": "MDSYVIQTNVNDSLPSVLDVRVNIGGRSSVQGRAKGRKARWNVRPSDMSNKTFNPIRAIVDNMKVKPNPNKTVISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGYLSSREEVASYYHCPEAPLEAKDVILTSGCSQAIELCLAVLANPGQNILIPRPGFSLYRTLAESMGIEVKLYNLLPEKSWEIDLKQLESLIDEKTACLVVNNPSNPCGSVFSKRHLQKILAVAERQCVPILADEIYGDMVFSDCKYEPMATLSTNVPILSCGGLAKRWLVPGWRLGWILIHDRRDIFGNEIRDGLVKLSQRILGPCTIVQGALKSILQRTPQEFYQDTLSFLKSNADLCYGALSAIPGLQPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLIAEQSVHCLPATCFEYPNFFRVVITVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK", "text": "FUNCTION: Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity for phenylalanine. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MSHYTKPKSRRPATLPSSHSHATTSNSRSLTEDQRGEIKEAFELFDVDKDGAIDYHELKVAMRALGFDVKKGEVMKLLKEHGGEDGLMDFLAFERIMTEKILARNPEHELRRAFELFDDDRTGKISLKNLRRVARELGETLGEEELQAMIDEFDLDQDGEINLEEFLAIMLDGE", "text": "FUNCTION: Calmodulin-like protein which plays a role in the activation of calcineurin (CNA1)."}
+{"protein": "MAALRWLSAVVAVSTTVLAITPEQMLSAPRRGEAIPNPSGNVALFSASQYSFDTKEKSSSWNLLNLKTGDITLLTDDANVSEIVWLGGDDTSLLYINGTNAEIPGGVELWVSSVKDFSKGYKAASLGASFSGLKAVRTRSGDIKFAVNAQSYANGTAYNEELATKYASTARIYDSIYVRHWDTYLTTTFNAVFAGTLKKGKHQYASAGPLKNLVAPVKNAESPYPPFGDSTDYDVSPDGKWVAFKSKAPDVPRANYTTAYIYLAPHDGSSTATPINGPDSPGTPEGVQGDANYPVFSPDSRHLAYFQMAHKSYESDRRVLYVYTLGSKTTTPAVAGDWNRSPDSAKWLDNKHLILGSEDHARVRLFGPVPIDADDDFKPQNFTDGGAVSSYHVLPDKTVLVTGTAIWTSWNVYTASPKKGVIKTIASANKIDPGLAGLGPEDISEFYYDGNWTKIQSWIIYPENFDSSKKYPLFFYIHGGPQSATPDSWSTRWNAKVFADQGYVVVAPNPTGSTGFGQELTDAIANNWGGAPYEDLVKAWEYVDKNLPYVDTENGVAAGASYGGFMINWIQGSDLGRKFKALVCHDGTFVADAKISTEELWFIEHDFNGTFWGARDNYRRWDPSAPERILQFSTPQLVIHSDQDYRLPVAEGLAMFNVLQERGVPSRFLNFPDENHWVLKQENSLVWHQQMLGWLNRYSGIEEANPDAVSLDDTIIPVVNYNP", "text": "FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S9C family."}
+{"protein": "MSEDMEFENWGSTQSSVEKFCYKWTISNFSFCMGGIQRRITSPVFSSEENKEVAWCLRVYPKGADKESKDYLSVYLVLLSHLQIPVWAKFKFWIINSQGEKYQKIKSPTVECFLTNEQNGFKKFLPRDLLLSHRNCLLPEDQLTICCKVTILGRKYNMPSQNITPAIKDPRHLLTDDLGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMKESLKTPIKIHNLNPQVFKEMMGFIYTGKAPHLHSHSMACDVLPAADKYGLVSLKVLCEDALCRNLSVKNATHTLILADLHSTEKLKTQALDFIAYYASEVCETSEWKSILESHPHLVAEAFQSLASAQCSFLEPKVISGSNQL", "text": "SIMILARITY: Belongs to the Tdpoz family."}
+{"protein": "MFLVGLTGGIASGKSTVVSILRELGCAVIDADLIARQVVRLGTPAYSQIVQHFGDGVLLVSGELDREKLGAIIFSDPEKRCVINSITHPQIRREMLRQTLWYFFLGYRYVILDIPLLFESRSMTRYMKHTMLVYCDPQTQLERLMRRNSLSRDEATKRIAAQLPLDSKLPLADHVIDNSGDRDNTRRQVLQLHARLESSLAYLPVRITAATVATGLVVLACGLLRRLWQ", "text": "SIMILARITY: Belongs to the CoaE family."}
+{"protein": "MLKTYHIALACVILAVVVLLFGGESLSLEEWQEVCLNVKNHFLHNEELSSLSVIILEIRLPRVILALLVGASLSGSGVVMQTILRNPLVDPFLLGISSGAMLGVAMAIAVVESNIAILAFFGAILPSLAVLAMNRVLGNSVLSLVLSGVVLSAFLSALAGAIKFFVIPQKAQAIVVWLLGSLSLSSYKDCLIAFIGLSLGFIPLFLLRWRINLLSLSDAQSLSLGINPVLLRSLCLVCVSVASALAVSVSGTIGWIGLVIPHVARLFFGANLQKLLLSSLLMGAFFLLLADVVAKTITPYDLPVGIATSVLGAPFFLWLLFRTRGV", "text": "FUNCTION: Part of a binding-protein-dependent transport system for an iron chelatin; 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. FecCD subfamily."}
+{"protein": "MAEINRMQYEIDYTEGISQRMRVPEMLKVAPGNLGANLKAQQDMPIPGVVMEVPERIVVAGQSEESPFSRPSDLDFISGTNIGTLALKTPPRVLTLSERPLDFLDLEGLTPATPQSEEIRSSGHLKRDKFSSENALRQNGQLVRHDSMSAMSTLDTTLDATADDLALADAASLRRQIIKLNRRLLLLEEENKERVKHEMTMYSIIIIFGLLNSWLWLRR", "text": "FUNCTION: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein Peroxisome Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. SIMILARITY: Belongs to the Tango11 family."}
+{"protein": "MATWLAIIFIVAALILGLIGGFLLARKYMMDYLKKNPPINEEMLRMMMMQMGQKPSQKKINQMMTMMNKNMDQNMKSAKK", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0154 family."}
+{"protein": "MPLLLYTCLLWLSTSGLWTVQAMDPNTTYVNMSNHHRGLASANVDFAFSLYKHLVALSPKKNIFISPVSISMALAMLSLGTCGHTRAQLLQGLGFNLTGRSETEIHQGFQHLHQLFAESDTSLEMTMGNALFLDGSLELLESFSADIKHYYESEVLAMNFQDWATASRQINSYVKSKTQGKIADLLSGLDSPAILVLVNYIFFKGTWTQPFDLASTREENFYVDETTVVKVPMMLQSSTISYLHDSELPCQLVRLNYVGNGTVFFILPEKGKMNTVIAALSRDTINRWSAGLTSSQVDLYIPKVTISGVYDLGDVLEEMGIADLFTNQANFSRITQDAQLKSSKVVHKAVLQLNEEGVDTAGSTGVTLNLTSKPIILRFNQPFIIMIFDHFTWSSLFLARVVNPA", "text": "FUNCTION: Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
+{"protein": "MKLSNIPQRYVIVFLTFLSTCVCYIERVGFSIAYTVAADAAGINQSSKGTILSTFFVGYACSQVPGGWAAQKIGGRKVLLLSFVLWSSTCFLVPLDPNRVGLLVVARLLVGVAQGFIFPSIHTVLAQWVPPHERSRLVSITTSGMYLGAALGMWLLPALVELRGPESVFLAEALAGVIWSLLWIRYATDPPRSEHPKAAAAGFGGALLPTNVNHHKVTHIPWKKIMLSLPVWAIVVNNFTFHYALYVLMNWLPTYFELGLQISLQGMDSSKMVPYLNMFVFSIVGGFIADYLITKRILSVTRTRKFLNTVGFLIASAALMVLPMFRTENGVILCSSVALGFLALGRAGFAVNHMDIAPRYAGIVMGVSNTAGTLAGIIGVDLTGKLLEASKLVYSDLSHPESWRVVFFIPGLLCIFSSVVFLLFSTGERIFD", "text": "FUNCTION: Inorganic phosphate and probable anion transporter. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter (TC 2.A.1.14) family."}
+{"protein": "MSAEQIAGTGVIHGRFQPLHLGHLEYLLAGAERCRTLVVGITNPDPWTTTEETTDPERGLPESNPCTFYERYLMVEGALTEAGVSHERLRIVPFPHSFPERLAHYAPADARYFVTVYDDWGDAKLDRFHALGLRTEVMWRRTDKPVSGGRVRRSIAEGQPWEHLVPPAVARVVKECGIDERIRA", "text": "FUNCTION: Catalyzes the displacement of the beta- and gamma-phosphates of CTP by phosphonoformate to produce CMP-5'-phosphonoformate, an intermediate in the biosynthesis of phosphinothricin tripeptide (PTT). PTT is both a natural-product antibiotic and potent herbicide."}
+{"protein": "QPSQDFMRF", "text": "FUNCTION: Has modulatory actions at skeletal neuromuscular junctions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
+{"protein": "MDSRSPSLPDDRPDPPEQHLDARAGATLRGTAGPRGVRRILPFLGPAVIASIAYMDPGNFATNIEGGARYGYSLLWVILAANLMAMVIQNLSANLGIASGRNLPELIRERWPRPLVWFYWIQAELVAMATDLAEFLGAALAIQLLTGLPMFWGAVVTGVVTFWLLNLQKRGTRPLELAVGAFVLMIGVAYLVQVVLARPDLAAVGAGFVPRLQGPGSAYLAVGIIGATVMPHVIYLHSALTQGRIQTDTTEEKRRLVRLNRVDVIAAMGLAGLINMSMLAVAAATFHGKNVENAGDLTTAYQTLTPLLGPAASVLFAVALLASGLSSSAVGTMAGDVIMQGFMGFHIPLWLRRLITMLPAFIVILLGMDPSSVLILSQVILCFGVPFALVPLLLFTARRDVMGALVTRRSFTVIGWVIAVIIIALNGYLLWELLGG", "text": "FUNCTION: H(+)-stimulated, divalent metal cation uptake system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP family."}
+{"protein": "MSEREVKQIHEDQEAANAPAGLAQENAQVEETANENGSEDVSSAKKRDPEEDVTKADEPDKKKKKKRRTYDDDDDKEEKDGEEVKGKEAAKEKDSEGKEKVDADDDDEDEEDEEAEVVLGEDDEDDDDDDDEDDDEEYDESRADVGEEDDEEEDELNEIDQSNIISSGRRTRGKQIDFNEAAEKLDRENGLLEEDGEEEN", "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": "MMLLLAILHKNDADYFIAEAMGVKIIEEEAYKKISKETFEEALKELKNSDVVVYTDFPIGEMNELNLKLIEEAKNLKKRMIFYEDDISVLKEI", "text": "SIMILARITY: To B.subtilis YdcN C-terminal region."}
+{"protein": "RNTPGPHGLTPYEILYGAPPPLVNFHDPDMSELTNSPSLQAHLQALQTVQREIWRPLAEAYRDRLDQPVIPHPFRTGDSVWVRRHQTKNSEPRWKGPYTVLLTTPTALKVDGIAAWIHAAHVKAATTPPAGTASGPTWKVQRSQNPLKIRLTRGAP", "text": "FUNCTION: Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step that requires cell division, the PIC enters cell nucleus. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The last step is viral DNA integration into host chromosome (By similarity)."}
+{"protein": "MKVVATILYLVVLAICGLGIHGAHPTHSAPPTVYPSVSFNLTEANSNEYRHFLQELRGKVILGSHRAFDLPVLNPESKVSDSDRFVLVRLTNPSRKKVTLAIDVVTFYVVAFAQNDRSYFFSGSSEVQRENLFVDTTQEDLNFKGDYTSLEHQVGFGRVYIPLGPKSLAQSISSLSTYKSSAGDNKRLARSLLVVIQMVSEAARFRYIQLRIQASITDAKEFTPDLLMLSMENKWSSMSSEIQQAQPGGAFAQVVKLLDQRNHPIDVTNFRRLFQLTSVAVLLHGCPTVTKMPAYIIKMPVFNGGEDEERCSVVEEVTRRIGGRDGFCAEVKNGDEKDGTPVQLSSCGEQSNQQWTFSTDGTIQSLGKCLTTSSSVMIYNCKVVPPESTKWVVSIDGTITNPRSGLVLTAPKAAEGTLVSLEKNVHAARQGWIVGNVEPLVTFIVGYEQMCLETNPGNNDVSLGDCSVKSASKVDQKWALYGDGTIRVNNDRSLCVTSEGKSSNEPIIILKCLGWANQRWVFNTDGTISNPDSKLVMHVDQNDVPLRKIILSHPSGTSNQQWIASTHPA", "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). Agglutination is inhibited by Neu5Ac(alpha2,6)lactose, and N-linked glycoproteins such as fetuin and orosomucoid. SIMILARITY: In the N-terminal section; belongs to the ribosome- inactivating protein family. Type 2 RIP subfamily."}
+{"protein": "MDYNRMNSFLEYPLCNRGPSAYSAHSAPTSFPPSSAQAVDSYASEGRYGGGLSSPAFQQNSGYPAQQQPSALGVPFPSSAPSGYAPAACSPSYGPSQYYPLGQSEGDGGYFHPSSYGAQLGGLSDGYGAGGAGPGPYPPQHPPYGNEQTASFAPAYADLLSEDKETPCPSEPNTPTARTFDWMKVKRNPPKTAKVSELGLGSPSGLRTNFTTRQLTELEKEFHFNKYLSRARRVEIAATLELNETQVKIWFQNRRMKQKKREREGGRVPPAPPGCPKEAAGDASDQSTCTSPEASPSSVTS", "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 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family. Labial subfamily."}
+{"protein": "MASGRDPREARPGELEIWDLSREPWDEWLRDMLEDINQEAKMHFGRELLFQVWNYCQEEGERNRTPMLERAYKYYKLVQKALFVHFRCGCRRRQPFEPYEERRDGQGGGRAGRVPPGLD", "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": "MGDERPHYYGKHGTPQKYDPTFKGPIYNRGCTDIICCVFLLLAIVGYVAVGIIAWTHGDPRKVIYPTDSRGEFCGQKGTKNENKPYLFYFNIVKCASPLVLLEFQCPTPQICVEKCPDRYLTYLNARSSRDFEYYKQFCVPGFKNNKGVAEVLQDGDCPAVLIPSKPLARRCFPAIHAYKGVLMVGNETTYEDGHGSRKNITDLVEGAKKANGVLEARQLAMRIFEDYTVSWYWIIIGLVIAMAMSLLFIILLRFLAGIMVWVMIIMVILVLGYGIFHCYMEYSRLRGEAGSDVSLVDLGFQTDFRVYLHLRQTWLAFMIILSILEVIIILLLIFLRKRILIAIALIKEASRAVGYVMCSLLYPLVTFFLLCLCIAYWASTAVFLSTSNEAVYKIFDDSPCPFTAKTCNPETFPSSNESRQCPNARCQFAFYGGESGYHRALLGLQIFNAFMFFWLANFVLALGQVTLAGAFASYYWALRKPDDLPAFPLFSAFGRALRYHTGSLAFGALILAIVQIIRVILEYLDQRLKAAENKFAKCLMTCLKCCFWCLEKFIKFLNRNAYIMIAIYGTNFCTSARNAFFLLMRNIIRVAVLDKVTDFLFLLGKLLIVGSVGILAFFFFTHRIRIVQDTAPPLNYYWVPILTVIVGSYLIAHGFFSVYGMCVDTLFLCFLEDLERNDGSAERPYFMSSTLKKLLNKTNKKAAES", "text": "FUNCTION: [Isoform 1]: Choline/H+ antiporter, mainly in mitochodria (PubMed:10677542, PubMed:20665236, PubMed:33789160, PubMed:23651124). Also acts as a low-affinity ethanolamine/H+ antiporter, regulating the supply of extracellular ethanolamine (Etn) for the CDP-Etn pathway, redistribute intracellular Etn and balance the CDP-Cho and CDP-Etn arms of the Kennedy pathway (PubMed:33789160). FUNCTION: [Isoform 3]: Does not exhibit choline transporter activity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Mitochondrion outer membrane; Multi-pass membrane protein Note=Mainly expressed in mitochondria. SIMILARITY: Belongs to the CTL (choline transporter-like) family."}
+{"protein": "MEDGELDFSNQEVFSSSEMGELPPSNCSMDSFFDGLLMDTNAACTHTHTCNPTGPENTHTHTCFHVHTKILPDESDEKVSTDDTAESCGKKGEKRPLGNREAVRKYREKKKAKAASLEDEVARLRAVNQQLVKRLQNQATLEAEVSRLKCLLVDLRGRIDGEIGSFPYQKPMAANIPSFSHMMNPCNVQCDDEVYCPQNVFGVNSQEGASINDQGLSGCDFDQLQCMANQNLNGNGNGSFSNVNTSVSNKRKGGHRASRAV", "text": "FUNCTION: Transcription factor involved in the response to zinc ion deficiency. Binds to the consensus sequence 5'-[AG]TGTCGACA[CT]-3' also called zinc deficiency response element (ZDRE). The ZDRE sequence is conserved in the plant kingdom and present in the promoters of genes that constitute the primary response to zinc deficiency, comprising additional ZIP metal transporter genes (PubMed:20479230, PubMed:26306426). Required for zinc accumulation in roots. Mediates the expression of the zinc transporters ZIP3, ZIP4, ZIP5 and ZIP9 during growth in zinc-deficient conditions. ZIP9 transporter is involved in zinc uptake in roots (PubMed:26306426). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MSQLFSHKIAPSPIPDNISVVDLIDNYFTAYNSARLREICHLLAQKVMQPGVTVGLSLSGAMTPTGLGISALAPLVRAGLIDYIISTGANLYHDLHYALGMDLYASHPFVDDVKLRQESRIRIYDIIFDYDVLLETDAFIREVLRAEPFQRRMGTAEFHHLLGQYARAAEVELGRSHSSLLATAYECGVPIYTSSPGDSSIGMNVAALALEGSQLVLDPALDVNETAAIAYFARESDIPDQEGKSAALIIGGGSPKNFLLQTQPQIHEVLGLEERGHDYFIQITDARPDTGGLSGAVPSEAVSWGKVDPNGLRDTVVCYTDSTIALPILTAYVLNQCAPRPLKRLYDRRPAMIEELQRLYLQAQFKQQAEAKLGKEQMPEPQSTEPVATYPCGTPIKGRK", "text": "SIMILARITY: Belongs to the deoxyhypusine synthase family."}
+{"protein": "MNDPTDTLYHQTAIHKLAEIGKNCKHLGIIFIHGGAWVDPLNTSNDFKGIAGEISKVIENNNTQGFNISMFGIEYRLSPSVKHPIHITDVITNTYKLINEYKIDILYIVGHSVGATLGLQLATDNRDYLIKYSSQLHLIRSTIQGLFLLDGIYSLQELLKEYPTYDSFISKAFTNYELEFQDPKEYLDKEQQFIKNLSFYIIHSFQDELLTLRQTDYLVELLKAKEISFNLSISDYGRHNDVYINDRVAKLIIFNILSNIN", "text": "FUNCTION: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites. SIMILARITY: Belongs to the kynurenine formamidase family."}
+{"protein": "MKPLVSPGLAKACTGLSLIGIVFLLVLSYLFSIEAETLMHDLVGSGLTGKQVAKTCLGAVVIYAVFFLFCGSQVIVSRYQKPVRI", "text": "FUNCTION: Accessory component 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: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
+{"protein": "DAPASPLADIEKHAAEFQKTISEQFNSLVNSKNTQ", "text": "FUNCTION: Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects (By similarity). Has hemagglutinating activity towards rabbit erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insect apolipophorin-3 family."}
+{"protein": "MKNKLIAKSLLTIAAIGITTTTIASTADASEGYGPREKKPVSINHNIVEYNDGTFKYQSRPKFNSTPKYIKFKHDYNILEFNDGTFEYGARPQFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLVR", "text": "FUNCTION: Extracellular fibrinogen-binding protein that plays an important role in virulence (PubMed:7934883). By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non- functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N-terminal (By similarity). FUNCTION: Extracellular fibrinogen-binding protein that plays an important role in virulence. By interacting with the alpha chain of fibrinogen and its derivative fibrin, enhances a non-functional interaction between fibrinogen and platelets and is responsible for repression of fibrinogen-dependent platelet aggregation. In addition, assembles a fibrinogen protective shield around the bacteria which results in impaired phagocytic clearance by the host. Mechanistically, interacts with host complement C3b deposited on the surface of the bacterium via its C-terminal and then recruits fibrinogen via its N- terminal. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSLRKRSAQTQMWESPVMSQGKQSLLELPLKESPPKDSGLKAVPSTHTLYVSHLNPQFSVPVLACLLRDTLERLELPVARGQIEVVRRPRNTYALVQVAAPKAVLASLPWRLQMALEEQLILKELTARGKELVLSEALESLHHREQEDSGPSPSHSPGPSPGPSPGLRHPPLPQLADPSPIWGSAGRRQISQNRPSGVRSDSAIVHHKILGQEQLFQGAFLGSETRNMEFKRGSGEYLSLAFKHHVRRYVCAFLNSEGGSLLVGVEDSGLVQGIHCSHRDEDRTRLLVDSILQGFKPQVFPDAYTLTFIPVISTTTTSTPLKVLRLTVHTPKAQGEPQLYETDQGEVFLRRDGSIQGPLSVGAIQDWCRQKWAMELGKLEEKVKVLTLEKEQLQQQLRQRQPLSCSCCVL", "text": "SIMILARITY: Belongs to the Schlafen family. Subgroup I subfamily."}
+{"protein": "MTHNIHDNISQWMKSNEETPIVMSSRIRLARNLENHVHPLMYATENDGFRVINEVQDALPNFELMRLDQMDQQSKMKMVAKHLISPELIKQPAAAVLVNDDESLSVMINEEDHIRIQAMGTDTTLQALYNQASSIDDELDRSLDISYDEQLGYLTTCPTNIGTGMRASVMLHLPGLSIMKRMTRIAQTINRFGYTIRGIYGEGSQVYGHTYQVSNQLTLGKSELEIIETLTEVVNQIIHEEKQIRQKLDTYNQLETQDRVFRSLGILQNCRMITMEEASYRLSEVKLGIDLNYIELQNFKFNELMVAIQSPFLLDEEDDKSVKEKRADILREHIK", "text": "FUNCTION: Catalyzes the specific phosphorylation of arginine residues in proteins (By similarity). Is required for stress tolerance and virulence in S.aureus. Acts as a modulator of the repressor activity of CtsR upon heavy metal and oxidative stress caused by these metal ions (PubMed:22902728). FUNCTION: Catalyzes the specific phosphorylation of arginine residues in proteins. SIMILARITY: Belongs to the ATP:guanido phosphotransferase family."}
+{"protein": "MWNDTQMTEIVIPPVDWRVATQLSIIFGWASVLLVIALFVPRSRTRIVGYLAMVGAMVAAAVGIPLWGVNAETFSGMLRLDSYSLTLNWLFLAAAAITMVLSLDYLPRQGIERSEYYVLVLFATGGMMLLAQGADLIILFLGLELLSIVLYVLTGFAYPRNASEEAGMKYLLIGAFAGGFVVFGIALLYGATGSMNLRAIGETLAQQTLTLEERIYLLAGAALVVVGFGYKVAMAPFHMWAPDVYEGAPTPIAGLLSVGSKAAGFAALLRFLVEALAGEWQIWAPVLAVLAIATLAVGNIGALTQRNVKRMLAYSSIGHAGYILFGVIAAGAPGGIAGQRGVEGVLLYLIAYTFTNLGAFGVLIALEHRGEAAWDMSDLAGLWSRRPWLAVAMAVCMLSLAGVPPTGGFWGKFYVFTAAWLSGMGWITVIGVIVAAIAAFYYLRIVAQMFMAEPAREVPLPMDRALRAGLALATLGVLILGFLPTPAIDLVQRVVLGG", "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": "MINPNPKRSDEPVFWGLFGAGGMWSAIVAPVIILLVAILLPLGLFPGEALGYERVLAFASSFIGRVFIFLMIVLPLWLGLHRIHHAMHDLKIHVPNGKWVFYGLATILTVVTLVAIVTI", "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": "MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLQDVIATDKEEIAFKDLDVAVLVGSMPRREGMERKDLLKANVKIFKSQGTALEKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKSQIALKLGVTADDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAIADHIRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKELTEEKETAFEFLSSA", "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": "MATTAAPAGGARNGAGPEWGGFEENIQGGGSAVIDMENMDDTSGSSFEDMGELHQRLREEEVDADAADAAAAEEEDGEFLGMKGFKGQLSRQVADQMWQAGKRQASRAFSLYANIDILRPYFDVEPAQVRSRLLESMIPIKMVNFPQKIAGELYGPLMLVFTLVAILLHGMKTSDTIIREGTLMGTAIGTCFGYWLGVSSFIYFLAYLCNAQITMLQMLALLGYGLFGHCIVLFITYNIHLHALFYLFWLLVGGLSTLRMVAVLVSRTVGPTQRLLLCGTLAALHMLFLLYLHFAYHKVVEGILDTLEGPNIPPIQRVPRDIPAMLPAARLPTTVLNATAKAVAVTLQSH", "text": "FUNCTION: Involved in the maintenance of the Golgi structure. May play a role in hematopoiesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasm. Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. Note=Localization to the cytoplasm or to the cell membrane is developmentally and ontogenetically regulated. SIMILARITY: Belongs to the YIP1 family."}
+{"protein": "MAGERPPLRGPGPGPGEVPGEGPPGPGGTGGGPGRGRPSSYRALRSAVSSLARVDDFHCAEKIGAGFFSEVYKVRHRQSGQVMVLKMNKLPSNRGNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIARGLRYLHSKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGARKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGDDCPLPFLLLAIHCCNLEPSTRAPFTEITQHLEWILEQLPEPAPLTRTALTHNQGSVARGGPSATLPRPDPRLSRSRSDLFLPPSPESPPNWGDNLTRVNPFSLREDLRGGKIKLLDTPSKPVLPLVPPSPFPSTQLPLVTTPETLVQPGTPARRCRSLPSSPELPRRMETALPGPGPPAVGPSAEEKMECEGSSPEPEPPGPAPQLPLAVATDNFISTCSSASQPWSPRSGPVLNNNPPAVVVNSPQGWAGEPWNRAQHSLPRAAALERTEPSPPPSAPREPDEGLPCPGCCLGPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS", "text": "FUNCTION: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (By similarity). Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Positively regulates integrin- mediated cell spreading, via phosphorylation of cofilin (PubMed:15584898). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (PubMed:25849865). Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, lamellipodium Note=Colocalizes with SPRY4 in vesicular spots in the cytoplasm (PubMed:15584898). Localized to F- actin-rich lamellipodia at the cell periphery following fibronectin- mediated cell adhesion of Schwann cells (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family."}
+{"protein": "MISGLFIFNLKGDTLICKTFRHDLKKSVTEIFRVAILTNTDYRHPIVSIGSSTYIYTKHEDLYVVAITKGNPNVMIVLEFLESLIQDLTHYFGKLNENTVKDNVSFIFELLDEMIDYGIIQTTEPDALARSVSITAVKKKGNALSLKRSHSSQLAHTTSSEIPGSVPWRRAGIKYRKNSIYIDIVERMNLLISSTGNVLRSDVSGVVKMRAMLSGMPECQFGLNDKLDFKLKQSESKSKSNNSRNPSSVNGGFVILEDCQFHQCVRLPEFENEHRITFIPPDGEVELMSYRSHENINIPFRIVPIVEQLSKQKIIYRISIRADYPHKLSSSLNFRIPVPTNVVKANPRVNRGKAGYEPSENIINWKIPRFLGETELIFYAEVELSNTTNQQIWAKPPISLDFNILMFTSSGLHVQYLRVSEPSNSKYKSIKWVRYSTRAGTCEIRI", "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 (Potential). 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": "MSSKRKVELCDSLLTWMQTFQVSGPCSSYEDLTGGVAIAQVLNRIDPSWFNEAWLVRVKKDTTENWRLKVSNLKRILQSVLEYYQDVLGHPVSDDHIPDVALIGEFSNDTELRKMVQLVLGCAISCDKKEEHIQQIMTLGESVQQAVMESIQELLSKAPSDAVTSESFINYDSQSRKYYFLSEDNDEKNEILQRCHDLEQQVSLLMEEKKNMMGENRTLKEQQEQSGMGTPQLFNKKLLLLQSQIEQLQEENYRLESSRDDYRQRCQELDRDVQELQQRNQDLTGLAHESQALRDEMDVLRHSSDRVGKLESLVDSYKKKLEDLGDLRRQVKLLEERNTMYMQRTFQLEEDLHKANASRGQVESLSRQVQELHKKHSTESLRAEKWQFEFQTLKEKFEALQKERERLIAERDSLRETNDELRCSHLQQTCLGQADLLLSGSSPPLENLAAEIVPAELRETVIRLQQENKMLCAQEASYHERLCDLQNFLEESNRSKNRLESESRLQQQQIKGLKAQVEELQKQLREQGNRAEDSSQLKRKLEEHLEMLHDAHSELQKKREYIETLEPKADLNMSRKVDELQQILHQKEEDMRAMEERYKRYVDKARTVIKSLDPKQQNYIPPEIQALKNQLQEKDTRIRHLETDYEKTKVQRDQEEKLIISAWYNMGMALHQKSTDEKTQPPNGAQSFLAQQRLATNARRGQISRSHTLLPRYTDKRQSLS", "text": "FUNCTION: May function to promote vesicle trafficking and/or fusion. May contribute to the establishment and maintenance of centrosome function (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the hook family."}
+{"protein": "MNKNIPAFHRRCHGLVQGLARTLLLAPVLLALSVPAAQAQTWPSRPIRMVVAAGAGSSVDVFARLVSERLSKALGQAVIVDPRPGANGTIAAQAVASAKPDGYTLLYAGNSALVVAPLMTKDLPYDAEKDLEPVAPVVYVPLAIAVGAKSAIQNIQELVAGAKTDEVFFATPGAASLSRLIGESINQKAGTRLVNIAYPSSPPAHTDIIGGQVPILIDGLGGIAPHAKSGRMRLLAVSTASRFAGFPDVPSISEAVPGLATPSMNIVMAPAGTPAEVLDLLNRHINEITADPAIASRFIPMGGESAQGSRQDTAAMLREQRVEFRKLMQTANIKP", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the UPF0065 (bug) family."}
+{"protein": "MSGPSSWRRAATVMLAAGWTHSSPAGFRLLLLQRSQNQRFIPGAHVFPGGVLDAADSSPDWVRLFAPRHTPPRFGLGPEPPRQPPFPGLSHGDADPAALPDDVALRICAIRETFEEAGVLLLRPRDADPASQEPSQALSPPAGLAEWRSRVRSDPRCFLQLCAHLDCTPDIWALHDWGGWLTPYGRITRRFDTTFLLCCLRDTPRVEPDLAEVVGYQWLSPSEATECFLSKEIWLAPPQFYEIRRLDNFASLSALYRFCSDRPLEGGEKWLPIILLTSDGTIHLLPGDELYVKDSDFLEKNMSTDKKTEEIVKEGKVLNRVVIHSPYVYEIYMTLPSENKHVYPRNYVVNKRCTAHL", "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": "MTKRTKKAGIVGKYGTRYGASLRKQIKKMEVSQHSKFFCEFCGKFAVKRKAVGIWGCKDCGKVKAGGAYTLNTPSAVTVRSTIRRLREQTEG", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL43 family."}
+{"protein": "MIELRHEVQGDLVTVNVVETPEDLEGFRNFIRAHLNCLAVDTETTGLDIYSDTFECRLVQFGTQDEAWVVPVELGDVFIEDVRIAIGALKRMVLQNASFDLQVLDQCFGIEMEGLWPRVLDTQILAKLVDPRPFEAGGFGHSLEELIAKFISEDQAENVKKLMAKLAAEHKTTKAKIWSTIDLFHPEYLLYAGMDTIFTARVCKSLTPLVPDVSRSLVPYEHKISEICSYIDRQGFLLDVEYSRSLAEKWLADQEVWEAIAFTEYGVEKVNSTEDLAEGLEEMGVKITGRTETGKRQVNAALLDKLVEDGNELAAIAQEAKKLGKWRKTWVQKFIDTRDSEDRCHTFINPLQARTSRMSITGIPAQTLPSSDWIVRRCFIAEPGDVMASVDYQAQELRVLAALSGDRNMIEAFENGADLHQMTADAAQVPRKVGKTANFQKVYGGGAKALAEAVGISIPVAKRVHEAFSATYPGVERLSKKLAMEAGRNGYIVNAMGRRLPVDSSRTYSALNYMIQSSSRDVTCRALIRLHEAGYTPYLRLPIHDEIVASLPASEAERAAAHIGHLMQEQMGPVLVGTDPEVGKRSWGSLYGADY", "text": "FUNCTION: Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction. SIMILARITY: Belongs to the DNA polymerase type-A family."}
+{"protein": "MCGRFTLFSEFDDIIEQFNIDQFLPEGEYHPSYNVAPSQNILTIINDGSNNRLGKLRWGLIPPWAKDEKIGYKMINARAETLSEKPSFRKPLVSKRCIIPADSFYEWKRLDPKTKIPMRIKLKSSNLFAFAGLYEKWNTPEGNPLYTCTIITTKPNELMEDIHDRMPVILTDENEKEWLNPKNTDPDYLQSLLQPYDADDMEAYQVSSLVNSPKNNSPELIESH", "text": "FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross- link with DNA: forms a stable thiazolidine linkage between a ring- opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue (By similarity). May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). SIMILARITY: Belongs to the SOS response-associated peptidase family."}
+{"protein": "MEASSGTAGPAVLLLILALLLTESQGSRSQGTHTLRYDVTACFLEGSEQTRLLVLIYVDDELFLRYNGDRRSAKPWACWIKGHGGDETCTREAENLPKEEERLREMMADMINQKGHDKGPYTLQATLDCELQRNGSTRGFWHLGYEGRNLLTFDQKTLTWTMDVPFTQQKKTFEPRAPKADLVKTFLDETCPARLQRHLASLSNVLPDTGSPVVIVTCRNYPVGRITLTCRAFNLSSRVATLLWLRDGKPVQQDVFGPGTILPSGDGTYQTWVSIRVLPGQEPQFACNLRHSNRTIMQTAVSGESMGWPSASWATRQEAEGPHRTHNDHVVDGGLVTGNANKDSPDASSCATASAISAFPVVVLSVALPRAN", "text": "FUNCTION: Binds to heparan sulfate proteoglycans on the surface of fibroblast cells. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the MHC class I family."}
+{"protein": "MPRSSRMNLWPHCFPCFDDGDRSGNRFSTVCNFPDDLLPSLGATAHQPPKLRKYLVSPYDPRYKVWETFLIILVVYSAWICPLEFAFLRYLPSAPFVVDDVVNGFFAVDIMLTFFVPFVDKKSYLLVNDPKKIAVRYLSSWFVFDVCSTVPFHSISLLFNEHGHDLGFKFLNVLRLWRLRRVSSMFARLEKDIRFNYAVIRCTKLISVTLFAIHCAGCINYLIADRYPDPRRTWIGAVMPNFREDGLWIRYVTAMYWSITTLTTTGYGDLHAENAREMLFGICYMLFNLWLTAYLIGNMTNLVVHSTSRTRDFRDVVQAASEFAARNQLPQQIEEQMLNHICLRYKTDGLKQQETLDVLPKAMRSSISHYLFFRVVQGAYLFKGVSSRFIQQLVTEMQAEYFAPKEDIILQNDSPSDLYLLVSGAVDILVFLDGTEQVYRRAAEGELLGEIGVLCNKPQSFTFRTTKLSQILRISRTKLLGIIQENREDGDIIRSNLQQVNV", "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": "MLSSTLRVAVVCVSNVNRSMEAHSILRRKGLSVRSFGTESHVRLPGPRPNRPVVYDFATTYKEMYNDLLRKDRERYTRNGILHILGRNERIKPGPERFQECTDFFDVIFTCEESVYDTVVEDLCSREQQTFQPVHVINMEIQDTLEDATLGAFLICEICQCLQQSDDMEDNLEELLLQMEEKAGKSFLHTVCFY", "text": "FUNCTION: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SSU72 phosphatase family."}
+{"protein": "MDGSCDCIEPLWQADDLLVKYQYISDFFIALAYFSIPLELIYFVKKSAFFPYRWVLIQFGAFIVLCGATHLINLWTFAIYTKTIAVVLTVAKAATAVVSCITALMLVHIIPDLLNVKLRERFLKDKADELDREMGIIRTQEETGRHVHMLTHEIRSTLDRHTILRTTLVELGRTLVLAECALWMPTRSGSALQLSHTIYNSAAIGSVVPINLPIVSKVFNSNRVVKIPHTSPLASITADKSRYVPPEVVAIRVPLLHLTNFQINDWPELSAKSFAVMVLMLPPDSAREWRPHERELVEVVADQVAVALSHAAILEESMRARDLLMEQNIALDAARREAEMAICARNDFLAVMNHEMRTPMRAIVSLSSLLLETNLSAEQRLMVETILKSSDLLATLTNDVLDVSKLENGSLELEIAPFNLHSTFTDVVNLIKPVAACKRLSVMVTLAPELPLHAIGDQKRLMQIILNVAGNSIKFTKEGHVSITASMARPDALRGPHEPDYHPVVSDGFFYLAVQVKDTGCGISPQDMPHTFRKFAHPENAGKWNSGSGLGLALSRRFVSLMEGNIWLESEGVGKGCTAMFFVKLGMPEKPNANLRRMAPHPLQPNQGAGGPDALSISIMDSNPRVPRVRYQSSV", "text": "FUNCTION: Ethylene receptor related to bacterial two-component regulators. Acts as negative regulator of ethylene signaling. May play a role in the regulation of flowering by up-regulating GI (GIGANTEA) and RCN1 and regulate starch accumulation by down-regulating the alpha- amylase AMY3D. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ethylene receptor family."}
+{"protein": "MANMQGLVERLERAVSRLESLSAESHRPPGNCGEVNGVIGGVAPSVEAFDKLMDSMVAEFLKNSRILAGDVETHAEMVHSAFQAQRAFLLMASQYQQPHENDVAALLKPISEKIQEIQTFRERNRGSNMFNHLSAVSESIPALGWIAVSPKPGPYVKEMNDAATFYTNRVLKDYKHSDLRHVDWVKSYLNIWSELQAYIKEHHTTGLTWSKTGPVASTVSAFSVLSSGPGLPPPPPPPPPPGPPPLLENEGKKEESSPSRSALFAQLNQGEAITKGLRHVTDDQKTYKNPSLRAQGGQTRSPTKSHTPSPTSPKSYPSQKHAPVLELEGKKWRVEYQEDRNDLVISETELKQVAYIFKCEKSTLQIKGKVNSIIIDNCKKLGLVFDNVVGIVEVINSQDIQIQVMGRVPTISINKTEGCHIYLSEDALDCEIVSAKSSEMNILIPQDGDYREFPIPEQFKTAWDGSKLITEPAEIMA", "text": "FUNCTION: May have a regulatory bifunctional role. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CAP family."}
+{"protein": "MKGILGVKVGMTRIFRDDRAVPVTVILAGPCPVVQRRTPEKDGYTAVQLGFLPQNPKRVNRPLKGHFAKAGVEPVRILREIRDFNPEGDTVTVEIFKPGERVDVTGTSKGRGFAGVMKRWNFAGGPDSHGAHKIHRHPGSIGNRKTPGRVYKGKKMAGHYGAERVTVMNLEVVDVIPEENLLLVKGAVPGPNGGLVIVRETKKAAK", "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. 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. SIMILARITY: Belongs to the universal ribosomal protein uL3 family."}
+{"protein": "MVKSKIYIDKIYWERVQLFVEGHSENLDLEDSNFVLRNLTETRTMKANDVKIDGNQFVCRFNVAILDNGYYLPEDKYLLVNEQELDYIAQLNPDVINDAYQNLKPEQEEEYNELETQNGKINFLLQTYLKEFRKGGISKKTVYTVTPEISSDVNEFVLDVVVTTPEVKSIYIVRKYKELRKYFRKQSFNTRQFIFKAIFNTTKFFHLKKGNTVLFTSDSRPTMSGNFEYIYNEMLRQNLDKKYDIHTVFKANITDRRGIIDKFRLPYLLGKADYIFVDDFHPLIYTVRFRRSQEVIQVWHAVGAFKTVGFSRTGKKGGPFIDSLNHRSYTKAYVSSETDIPFYAEAFGIKEKNVVPTGVPRTDVLFDEAYATQIKQEMEDELPIIKGKKVILFAPTFRGSGHGTAHYPFFKIDFERLARYCEKNNAVVLFKMHPFVKNRLNIADKHKQYFVDVSDFREVNDILFITDLLISDYSSLIYEYAVFKKPMIFYAFDLEDYITTRDFYEPYESFVPGKIVQSFDALMDALDNEDYEGEKVIPFLDKHFKYQDGRSSERLVRNLFGS", "text": "FUNCTION: Responsible for the polymerization of the main chain of the major teichoic acid by sequential transfer of ribitol phosphate units from CDP-ribitol to the second glycerol phosphate attached to the disaccharide linkage unit. Synthesizes polymers of more than 40 ribitol phosphate units in length. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase family."}
+{"protein": "MHAPLTAEQRDVYDKYKFATYARSVALTRAQLDQWRDNKVIVPEPVSRAETLRVEAATRGQSKNALWNLLRLDRSTASRSSGGVALRSSALAFGNAQENRLKLANGELFERLGRLAAERAGCPVAETVLDCGMFISAFGLHSASPDAYFAMADGSCVPVEIKCPFNYRDTTVDQMRLELGKANRKYRVKHTALLVNKAGPAQFEVVKTHDHYRQMQRQMYVMRNAPVCFYVVRFKHNLVALAVPRDDDFCRKEAAAEGAAFVAFATENAGRVQFKRGDRRRASFAQNAADHGYNAAQVDALVRRGLYLSYGQLRCGHCDAFALDGPRAFELAMARPHEQCDGLALQEHEFDNVAFLDFTKRYTSLVDKRCDDARALRVDGFYVDDAGAVKTFCCGVHGSNASRRHLPTCSYYLAMGVNKIQNNM", "text": "FUNCTION: May play a role in maturation and encapsidation of viral replicated genome, by promoting DNA homologous recombination. Exhibits endonuclease and 5'->3' exonuclease activities. The endonuclease activity displays a specificity for ssDNA in vitro (By similarity). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the baculo-herpesviridae alkaline nuclease family."}
+{"protein": "MSVKKLENGQYQVDVSFGFDPITGERIRTRPVASTRKEALELEAKLRREFQEERARKSRSVSFPTLISIYLASCEIDSKPNYYQNQKYIINKHISDYFLKSDIQKITHREITDFRKHLMETGLSNKSVNNIMTSLSKIFDTAVHEEILKRNPCDNVKRLPLTRKKMKFWRPEEFKKFISLIPQDQLLFKTFYTVAFLTGLRCGEMLALQWKDIDKILLEIDVHKSCTWLDGQFVVTTPKTKNSIRRVSINKKLLKLLERWKEAQEELFNELGIRHSHDTYIFQYKDTPSRKDIFSRKIKYFCKDSDLTPIRLHDFRHSHVALLIHQGEDYITIKERLGHGSVKTTIDVYGHLYPNKQKEMADKLDDLL", "text": "FUNCTION: Putative integrase that is involved in the insertion of the integrative and conjugative element ICEBs1. Required for the excision of ICEBs1 from the donor cell genome and subsequent integration in the recipient cell genome. Appears not to be transferred through the mating pore. Integration of ICEBs1 involves an attachment site in the chromosome, attB, and a site in the circular form of ICEBs1, attICEBs1. SIMILARITY: Belongs to the 'phage' integrase family."}
+{"protein": "MSFTRKKGFYKQDVNKTAWELPKTYVSLTHIGSGAYGSVCSAIDKRSGEKVAIKKLSRPFQSEIFAKRAYRELLLLKHMQHENVIGLLDVFTPASSLRNFHDFYLVMPFMQTDLQKIMGMEFSEDKIQYLVYQMLKGLKYIHSAGVVHRDLKPGNLAVNEDCELKILDFGLARHTDVEMTGYVVTRWYRAPEVILSWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGAEFVQKLNDKAAKSYIQSLPQSPKKDFSQLFPRASPQATDLLEKMLELDVDKRLTASQALAHPFFEPFRDPEEETEAQQPLEDSLEREKLIVDEWKQHIYKEIVNFSPIARKDSRRRSGMKLQ", "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": "MSEAALVPPALSTNQTEETFNFQQYELLRQDRAAHLGPGITDLASLKERIRSYYAIESLADHLNSHAEYRSITLQFPDDLLFDSALVAEELQALLPDLQCARTDAPAQADTTCSCGTQKTCADSKDSADGRKIWILADTAYSPCCVDEVAAEHVQADVVVHFGDTCLNPVETLPVVYIFGEPYLDRAKVISLFTERYDKDAKVCLMANAPYSRHLESLSGELSQLGYSNLVFTDVALPDTPNAAATILGVSDSHPISHKLYASGDRVYYGAKEQLLCEEQLQSFELFHIGLPPDPRLLFLSTKFQGVTAYDTQKRQIAKGPFPAMMRRYRFMHVARTASTIGILVNTLSLKSTRSLISSLVELIRSCGKKHYMFVVGKPNVAKLANFEPVDVWCVLGCGHGGIVLDHANEFYKPIVTPYELTLALAPELSWTGAWVVDFNTVIDGISADLGLQAGAIPAENVPEFDAVTGKYVGNSRPLRELNHLEIESPQESITTGSTELVKKFSGALTIGSTVSTSAQFLQARQWTGLGSDFNAEDSYEEEGATVEEGLSGVARGYQYDVSNAEHTDADVPKTSGRVMNT", "text": "FUNCTION: 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 similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily."}
+{"protein": "MSNVQNASRSSAFAAVEGDHWVESLDDGRHVLIRPLREEDRERERQFINRLSPATRHFRFLGEIKEASPALLDQLMDIDYQQSMAFVALVHEDGELREVGISRYAACCEEGQCECAVTIADDYQGLGLDAVLMRHLIDVARRNGFRQMYSVDSAANRAMRDLCCALGFVGQRDPDDSTQVIHRLAL", "text": "FUNCTION: Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It prefers the antibiotic chloramphenicol."}
+{"protein": "MAHQCARFHFFLCGFICYLVHSALASNSSSTLCFWFPLAHGNTSFELTINYTICMPCSTSQAARQRLEPGRNMWCKIGHDRCEERDHDELLMSIPSGYDNLKLEGYYAWLAFLSFSYAAQFHPELFGIGNVSRVFVDKRHQFICAEHDGHNSTVSTGHNISALYAAYYHHQIDGGNWFHLEWLRPLFSSWLVLNISWFLRRSPVSPVSRRIYQILRPTRPRLPVSWSFRTSIVSDLTGSQQRKRKFPSESRPNVVKPSVLPSTSR", "text": "FUNCTION: Minor envelope protein. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host endoplasmic reticulum membrane; Single- pass type I membrane protein Host Golgi apparatus membrane; Single-pass type I membrane protein Secreted Note=Only a small fraction of GP3 synthesized in infected cells ends up in virions. The transmembrane region probably functions as an uncleaved signal (By similarity). SIMILARITY: Belongs to the arteriviridae GP3 protein family."}
+{"protein": "MLGVGAGVVAVLVALVMFMGKEPSELLYSNLDLKEASEVTQALDQAGIKYETKGDGSTIMVPRDKVASARLMVAGKGLVSSGSIGYEIFDTNNALGQTDFVQQLNRQRALQGELERTIKAMQGVNSVRVHLVLPKRQLFEEDAEQPSAAVTIGVGSREPSSDMVRAIQNLVSSSVPNMKAEKVAVIDQHGKTLSAPSDESLAGKMAQDRKSEVEARIAKTVKDMIEGVLGPGKARVNVTAELDLNRVTTQEERFDPDGQVIRSESTTEASSQENKNDDNAGVTAAANVPGGQGANGFQQLGSRTGQNDAVTNYEISKSVTTTVQEPGTIKKIAVAVAIDGVSAPMAADGKPGAYTPRTAQEIQQIEELVKTAVGFDAERGDQVRVTNIKFPQPEDQGLEEQGLLAGFDKNDIMRAAELGVLAVVALLILLFAVRPFIKNLSAPAPGQIALAGPSGGPPVTRLVTLADGTQQQVVVDQSGEPIALAGPPVSDIDQRIDIAKIEGQVKASSIKRVSEFVEKHPDESVAILRNWLHEST", "text": "FUNCTION: The M ring may be actively involved in energy transduction. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Bacterial flagellum basal body. SIMILARITY: Belongs to the FliF family."}
+{"protein": "MGDSKELVWNGSINVQIKLDSRLLVDGVPEGRRLVNIRVPRESHIAIYTPLVLERLRNVLRSDIEELLPKVWYSYKDISLPWSIPFGTLFDIYNGAHKGISGSRDNYINVWKLNLVTDEKFPINVIPIIEGQDQLRKFMMQSWKQCCFILNGSSKRVMSLSLQDSLEVWEGVTERDYAKYSGVIKRILPRTPRRIPVAIHAANGGPIVQTTEPTLTDTSFSQAVEGIVKADFVVCQGIVMYLRDFSDTSLYDVYDKLHSIDGYLHLIANL", "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": "MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL", "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 (PubMed:17494869, PubMed:11877457, PubMed:11877461, PubMed:12952931, PubMed:14617351, PubMed:25653444). Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1 (PubMed:17494869). Preferentially, may phosphorylate substrates on threonine residues (PubMed:11877457, PubMed:18657069). Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes (PubMed:12952931). Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes (PubMed:18657069). Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (PubMed:21464124). FUNCTION: (Microbial infection) By regulating clathrin-mediated endocytosis, AAK1 plays a role in the entry of hepatitis C virus as well as for the lifecycle of other viruses such as Ebola and Dengue. 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. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MSDVLSQYKGCSVRDLPTPNFVINEEKFDKNCTTMLNNVEKLSQECGVPIKFRAHVKTHKTAKGTLKQLGHGLPLAKRTTRAILVSTLKEAEELLNYQDRQCSDYIDDITYSLPCCVPEFIPLLSNLSRRVNNFQVFVDNIEHLENLKNFGRPASGKKWSVFIKVDMGTKRAGLAFDSPEFLSLLKKLTSSEIKEVIEPYGFYAHAGHSYSSTSINDTQNLLMEEVKAVNSAAKVLCSVDPQFDPSKLTLSVGATPTSNSLKLDNKSTLVKFITTQLVSTLEIHCGNYCMYDLQQVATGCVQDHELSGFVLGTVLSSYPSRGELLSNTGVMCLTREASSIKGFGICADLEHVLKSESFSREWYVARVSQEHGILRPIRNWNETTPLKLGSKIAVLPQHACITMGQFPYYFVVNSEGIVNDVWLPFQKW", "text": "FUNCTION: Catalyzes the conversion of D-serine to pyruvate and ammonia (PubMed:17869212, PubMed:17937657). May play a role in D-serine detoxification (PubMed:17869212, PubMed:17937657). SIMILARITY: Belongs to the DSD1 family."}
+{"protein": "MISFCPDCGKSIQAAFKFCPYCGNSLPVEEHVGSQTFVNPHVSSFQGSKRGLNSSFETSPKKVKWSSTVTSPRLSLFSDGDSSESEDTLSSSERSKGSGSRPPTPKSSPQKTRKSPQVTRGSPQKTSCSPQKTRQSPQTLKRSRVTTSLEALPTGTVLTDKSGRQWKLKSFQTRDNQGILYEAAPTSTLTCDSGPQKQKFSLKLDAKDGRLFNEQNFFQRAAKPLQVNKWKKLYSTPLLAIPTCMGFGVHQDKYRFLVLPSLGRSLQSALDVSPKHVLSERSVLQVACRLLDALEFLHENEYVHGNVTAENIFVDPEDQSQVTLAGYGFAFRYCPSGKHVAYVEGSRSPHEGDLEFISMDLHKGCGPSRRSDLQSLGYCMLKWLYGFLPWTNCLPNTEDIMKQKQKFVDKPGPFVGPCGHWIRPSETLQKYLKVVMALTYEEKPPYAMLRNNLEALLQDLRVSPYDPIGLPMVP", "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": "MAGDSRNAMNQDMEIGVTSQDHKKIPKQARDYIPIATDRTRLLTEGKKPRQRYMEKTGKCNVHHGNVQETYRYLSDLFTTLVDLKWRFNLLVFTMVYTITWLFFGFIWWLIAYVRGDLDHVGDQEWIPCVENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQAILGSIVNAFMVGCMFVKISQPKKRAETLMFSNNAVISMRDEKLCLMFRVGDLRNSHIVEASIRAKLIKSRQTKEGEFIPLNQTDINVGFDTGDDRLFLVSPLIISHEINEKSPFWEMSRAQLEQEEFEVVVILEGMVEATGMTCQARSSYMDTEVLWGHRFTPVLTLEKGFYEVDYNTFHDTYETNTPSCCAKELAEMKRSGRLLQYLPSPPLLGGCAEAGNEAEAEKDEEGEPNGLSVSQATRGSM", "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. Can be blocked by external barium. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ5 subfamily."}
+{"protein": "MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGKYKVIKGIISPVGDAYKKKGLISAYHRVIMAELATKNSKWVEVDTWESLQKEWTETAKVLRHHQEKLEASICDPQQNSPVLEKPGRKRKWAEQKQDISEKKSLEQTKTKGVPKVKLLCGADFLESFGVPNLWKSEDITKILGDYGLICITRAGNDAQKFIYESDVLWKHQNNIHLVNEWITNDISSTKIRRALRRGQSIRYLVPDLVEEYIEKHNLYSSESEERNVGVVLAPLQRNTTEVKA", "text": "FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (By similarity). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency (By similarity). Can use triazofurin monophosphate (TrMP) as substrate (By similarity). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (By similarity). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively (By similarity). Involved in the synthesis of ATP in the nucleus, together with PARP1, PARG and NUDT5 (By similarity). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Also acts as a cofactor for glutamate and aspartate ADP- ribosylation by directing PARP1 catalytic activity to glutamate and aspartate residues on histones. Protects against axonal degeneration following mechanical or toxic insults. Delays axonal degeneration after axotomy. Results in a >10-fold increase in intact neurites 72 hours after injury (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family."}
+{"protein": "MLSRKLSPEQLVARRLKIRDWNHKIGAVVAPHYSPTLSIRNPAPPSQLSLPLLLSSGAHLGHSTSIWNPYTQPFIYGKREGIHIISLDQTMVYLRRAISVVRSIAKENGIILFIGTRNGQKDSVVAAAKRARGYHIFDRWLPGLLTNAREVQGKLGGSILCKDNRGKLIQTDKKPSYVFPDLMVILNPLENKSACLEAQKTHVPTIGIIDTDADPRMVTYPIPANDDSLRCTDLIAGLLSRVAEQEYQKANQAFEKDKFTLPL", "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 uS2 family."}
+{"protein": "MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFGNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFGNTWAEMYRNRYWKEHHFEGIALVEKALQAAYGASAPSMTSATLRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLEPAVVDAFNQAWHLVTHECPNYFR", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily."}
+{"protein": "MHFSTITAALALLGLGAATPTDYSTSSYSKNQGLAQAWTSKGRQYIGTALTIRDDPVEQGIIQSRTDFNSITPENAMKWESTEPQRNNFTFAGADAVADFADRYNKEMRCHTLVWHSQLPAWVSQGNFDNKTLISIMENHIKKVAGRYKNKCTHWDVVNEALNEDGTYRSSVFYNTIGEAFIPIAFRFAEKYAGSKTKLYYNDYNLEYGSAKALGAQRILKLVQSYGVQIDGVGLQAHLSSEATASTGGGVTPDVQTLTNVLKLYTDLGVEVAYTELDVRFTTPATDAKLKAQADAYARVVQSCINVKRCVGITVWGVSDKYSWIPGVFPTEGAALLWDENFNKKPAYSSVLKTIQSFRKS", "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. Hydrolyzes birch-wood xylan, with a similar activity toward oat-spelt xylan. Also shows weak activities toward pNP-beta-D- cellobioside and pNP-beta-D-xylopyranoside, but no detectable activity toward carboxymethyl cellulose and pNP-beta-L-arabinofuranoside.-. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family."}
+{"protein": "MIPLLFILFYFANGIEWHKFETSEEIISTYLLDDVLYTGVNGAVYTFSNNKLNKTGLTNNNYITTSIKVEDADKDTLVCGTNNGNPKCWKIDGSDDPKHRGRGYAPYQNSKVTIISYNECVLSDINISKEGIKRWRRFDGPCGYDLYTADNVIPKDGLRGAFVDKDGTYDKVYILFTDTIGSKRIVKIPYIAQMCLNDEGGPSSLSSHRWSTFLKVELECDIDGRSYRQIIHSRTIKTDNDTILYVFFDSPYSKSALCTYSMNTIKQSFSTSKLEGYTKQLPSPAPGICLPAGKVVSHTTFEVIEKYNVLDDIIKPLSNQPIFEGPSGVKWFDIKEKENEHREYRIYFIKENSIYSFDTKSKQTRSSQVDARLFSVMVTSKPLFIADIGIGVGMPQMKKILKM", "text": "FUNCTION: Acts as a semaphorin-like protein and binds to host plexin C1 receptor. May alter the movement of host plexin C1-expressing cells including dendritic cells, monocytes, or granulocytes in the proximity of infected cells. May also regulate host cell cytoskeleton of neighboring cells to improve viral infection (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the semaphorin family."}
+{"protein": "MEGISALEKNVAELTVMDVYDIASAVGQEFERVIDQYGCEVIGRLMPKVVRVLEILEVLVSRNHINPEMEELRLELDRLRLERMDRIEKEKKHLKELELVEDVWRGEAQDLLNQISQLQEENKQLLTNLSHKDVNLTEEEFQKHEGMSERERQVMKKLKEVVDKQRDEIRARDRELVLKNEDVEALQQQQSRLIKINHDLRHRVTVVEAQGKALIEQKVELEAYLQTKEQEAASMRIEIGKLRDKLKGEHHTNGEEIKTETLNEECIFETEKFSLDLKDSNRPRFTLQELRDVLHERNELKAKVFMLQEELAYYKSEEAEEENKLPQSLPVINSKAPIPQESGIKRLFSFFSRDKKRMPMMQKNVHFQESFGEWTNYNRDDVYTEQGQEALQHM", "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": "MRGREFPLVLLALVLCQAPRGPAAPVSVGGGTVLAKMYPRGNHWAVGHLMGKKSTGESPYAYEGGNMKEQLREYIRWEDATRNLLSLLEAKGIGSHQPPQWEPLGIRQSTWDSKDGSNFKDMGPRLKVDGLSAPGSQHEGRIPQLN", "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 (PubMed:496973). 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: Secreted Cytoplasmic vesicle, secretory vesicle lumen 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": "MDLYPEENTQSEQSQNSENNMQIFKSETSDGFSSDLKISNDQLKNISKTQLTLEKEKIFKMPNVLSQVMKKAFSRKNEILYCVSTKELSVDIHDATGKVYLPLITKEEINKRLSSLKPEVRRTMSMVHLGAVKILLKAQFRNGIDTPIKIALIDDRINSRRDCLLGAAKGNLAYGKFMFTVYPKFGISLNTQRLNQTLSLIHDFENKNLMNKGDKVMTITYIVGYALTNSHHSIDYQSNATIELEDVFQEIGNIQQSEFCTIQNDECNWAIDIAQNKALLGAKTKTQIGNSLQIGNIASSSSTENELARVSQNIDLLKNKLKEICGE", "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 tubules structures that increase the size exclusion limit (SEL) of plasmodesmata, thereby allowing viral ribonucleocapsids to spread directly to neighboring cells (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma. Note=Assembles in tubules that are embedded within modified plasmodesmata. SIMILARITY: Belongs to the caulimoviridae movement protein family."}
+{"protein": "MALIDVAISCLNSIREIEEDVKDAIVYIDAGCTESFQFVGAFPLFLELGARAVCSLENMTSLDAVADWNSKSDCAKRIVIMTSRLLNDAHRYMLRCLSTHEGVQRCTVFTSISEGSHSAIPDSPLGPDAYREYETLLVQDYNEHTKKSDKISKDKGVSKFSSALESLTMEPIESENVDISSGGAQGLVVSVHHFPLIICPFTPRAFVLPSQGSVAEASLSRQHEDSLSFGLPPISTGSMSDTDDVPPGATLTAHFLYQLALKMELKLEIFSLGDQSKNVGKILTDMSSVYDVARRKRSAGLLLVDRTLDLITPCCHGDSLFDRIFSSLPRAERFSSQAQLKQGVPSINRPSLDVQVPLGELLNEEPSKIRDSGLPEGIEAFLRGWDSYTSAPQNVGLFNECDKKSTTNWTELLNGSLVATECFRGTPYLEAMIDRKTKDGSVLVKKWLQEALRRENISVNVRARPGYATKPELQAMIKALSQSQSSLLKNKGIIQLGAATAAALDESQSAKWDTFSSAEMMLNVSAGDTSQGLAAQISDLINKSAVAELQAKKNEKPDSSSRGLLSFRDALLLTIVGYILAGENFPTSGSGGPFSWQEEHFLKEAIVDAVLENPSAGNLKFLNGLTEELEGRLNRLKSEETKEIPSDDQLDIDALDDDPWGKWGDEEEEEVDNSKADESYDDMQLKLDLRDRVDSLFRFLHKLSSLRTRNLPLREGSLASESSFPGEPSGNKGLVYRLITKVLSKQEIPGLEYHSSTVGRFIKSGFGRFGLGQAKPSLADQSVILVFVIGGINGIEVLEAQEAVSESGRPDINLVIGGTTLLTPDDMFELLLGQFSHF", "text": "FUNCTION: Required for proper maturation of seed storage proteins. Forms a complex with MAG2, ZW10/MIP1 and MIP2 on the endoplasmic reticulum that may be responsible for efficient transport of seed storage proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family."}
+{"protein": "MGSTLKHLLLLLLVLIRHVDSAAIVKSLPGLEGRLPFELETGYIGIGEEEDIQLFYYFIKSENNPKEDPLLLWLDGGPGCSSLGGLLFENGPVALKSAVYNGSNPSLFSTTYSWTKMANIIYLDQPVGSGFSYSRTPIGKSSDTSEVKRIHEFLQKWLSKHPQFFSNPFYVTGDSYSGMIVPALVQEISKGNYICCKHLINLQGYVLGNPITYAEHEKNYRIPFSHGMSLISDELYESLKRNCKGNYENVDPRNTKCVRLVEEYHKCTDKINTQHILIPDCDKKGHGITSPDCYYYLYFLIECWANNERVREALHVTKGTKGQWQRCNWTIPYDNNIISSVPYHMDNSINGYRSLIYSGDHDITMPFQATQAWIKSLNYSIVDDWRPWMINDQIAGYTRTYSNKMTFATVKGGGHTAEYLPNESSIMFQRWISGQPL", "text": "FUNCTION: Involved in the biosynthesis of sinapoylated anthocyanins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S10 family."}
+{"protein": "MGNGQGRDWKMAIKRCSNVAVGVGSKSKRFGEGNFRWAIRMANVTTGREPGDIPETLEQLRSIICDLQDRREHYGSSKEIDMAITTLKVFAVAGILNMTVSTATAAENMYAQMGLDTRPSVKESGGKEEGPPQAYPIQTVNGAPQYVALDPKMVSIFMEKAREGLGGEEVQLWFTAFSANLTSTDMATLIMSAPGCAADKEILDETLKQMTAEYDRTHPPDGPRPLPYFTAAEIMGIGLTQEQQAEPRFAPARMQCRAWYLEALGKLAAIKAKSPRAVQLKQGAKEDYSSFIDRLFAQIDQEQNTAEVKLYLKQSLSIANANPDCKRAMSHLKPESTLEEKLRACQEVGSPGYKMQLLAEALTRVQTVQTKGPRLVCFNCKKPGHLARQCKEAKRCNNCGKPGHLAANCWQGGRKTSGNEKVGRAAAPVNQVQQIVPSAPPMEEKLLDL", "text": "FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. FUNCTION: Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. FUNCTION: Nucleocapsid protein p13 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). SUBCELLULAR LOCATION: [Nucleocapsid protein p13]: Virion. SUBCELLULAR LOCATION: [Matrix protein p15]: Virion. SUBCELLULAR LOCATION: [Capsid protein p24]: Virion. SIMILARITY: Belongs to the feline lentivirus group gag polyprotein family."}
+{"protein": "MADSRDPASDQMKHWKEERAAQKPDVLTTAGGNPVGDKLNIMTVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFAYFEVTHDITKYCKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEEGIWDLVGNNTPIFFIRDALLFPSFIHSQKRNPQTHLKDPDMMWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNGSGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFQQAQSFPFNPFDLTKIWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRTRVANYQRDGPMCVTDNQGGAPNYYPNSFSAPVEQRQALEHTSRCSGDVGRYNSTDDDNVTQVRAFYTQVLNEEQRRRLCENIAGHLKDAQLFIQKKAVKNFMDVHPDYGNRIQTLLDKYNVEKPKNAIHTFVQDGSHLSAKEKANL", "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": "MGRLQMLKHKNEPLTPGYHGFPTRDSQGNQEPTTTPDAMVQPFTTIPFPPPPQNGIPTEYGVPHTQDYAGQTSEHNLTLYGSTQAHGEQSSNSPSTQNGSLTTEGGAQTDGQQSQTQSSENSESKSTPKRLHVSNIPFRFRDPDLRQMFGQFGKILDVEIIFNERGSKGFGFVTFENSADADRAREKLHGTVVEGRKIEVNNATARVMTNKKMVTPYANGWKLSPVVGAVYGPELYAASSFQADVSLGNDAAVPLSGRGGINTYIPLIIPGFPYPTAATTAAAFRGAHLRGRGRTVYGAVRAVPPAAIPAYPGVVYQDGFYGADLYGGYAAYRYAQPATATAATAAAAAAAAYSDGYGRVYTADPYHALAPAASYGVGAVASLYRGGYSRFAPY", "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. Seems to act as a coregulatory factor of ER-alpha (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MSSSQNNNSSWIDWFLGIKGNQFLCRVPTDYVQDTFNQMGLEYFSEILDVILKPVIDSSSGLLYGDEKKWYGMIHARYIRAERGLIAMHRKYMRGDFGSCPNISCDRQNTLPVGLSAVWGKSTVKIHCPRCKSNFHPKSDTQLDGAMFGPSFPDIFFSLLPNLTSPLDDPRT", "text": "FUNCTION: Unknown. In males lacking the Y chromosome, its strong overexpression leads to the appearance of proteinaceous star-shaped crystals in the primary spermatocytes causing meiotic drive, possibly by interfering with normal casein kinase 2 activity. SIMILARITY: Belongs to the casein kinase 2 subunit beta family."}
+{"protein": "MRMQRRHLLKNAAAALAALGLPALPQWALAAKAVGLRRLGQPQPFDYAWLKGRARELAKAPYKSHKQVLPGPLEALNWDQYQSIRYRQDHALWADGNGKFQAKFFHLGLYFHTPVHIYDIVDGKAQQLAYDPAAFDYGKSGLGGKQLPKDLGFAGFRLNTRKDTERDFSAFLGASYFRAVGKEGQYGQSARGLAIDTGTGGPEEFPDFIAYYLEQPAADSNTVVVYGLLDSPSIAGAYRFAITNGDVLLMDIDSALYPRKTIERLGIGPCTSMYQVGENDNRMDWDWRPEIHDTDGLAMWTGGGEWIWRPLCNPPHVRFNMFVDENPRGFGLLQRDRNFDHYQDDGVFYEKRPCLWVEPKSGWGKGSVQLVEIPTVDETFDNIVAFWNPQAKPQPGQELLMGYRLYWGVQPPASAPLAHCVATRTGLGGIVGQKRSHFSWRFAVDFAGGELAALAKDPKAKVEAVLQVSRGTTEIVSARPLHELKGYRAMFDLVPPDEGTQQIDIRLYLRANGKPLTETWLYQWTPLAASERKN", "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": "MASVQSGKMIVGLDIGTSKVVALVGEVTADGQLEVVGIGTHPSRGLKKGVVVNIESTVQSIQRAIDEAQQMAGCRIHSAFVGIAGNHIRSLNSHGIVAIRDREVNPADIERVLDAAQAVAIPADQRVLHTLAQDYVIDNQEGVREPLGMSGVRLEAKVHVVTCAVNASQNIEKCVRRCGLEVDDIILEQLASAYSVLTEDEKELGVCLVDIGGGTTDIAIFTEGAIRHTAVIPIAGDQVTNDIAMALRTPTQYAEEIKIRYACALAKLAGAGETIKVPSVGDRPPRELSRQALAEVVEPRYDELFTLVQAELRRSGYEDLIPAGIVLTGGTSKMEGAVELAEEIFHMPVRLGVPYSVKGLTDVVRNPIYSTGVGLLMYGLQKQSDGMSMSVSGSSYSSDEPKAPVLERLKRWVQGNF", "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": "MDGESPEIMPVECPDPEPASSESGDDHDIPEPLSSRLSVPSGELNLYRAAVALRLVLLAAFFRYRVTRPVADAHALWVTSVACELWLAASWLIAQLPKLSPANRVTYLDRLASRYEKGGEASRLAGVDVFVAAADAAREPPLATANTVLSVLAADYPAGGVACYVHDDGADMLVFESLFEAAGFARRWIPFCRRHGVEPRAPELYFARGVDYLRDRAAPSFVKDRRAMKREYEEFKVRMNHLAARARKVPEEGWIMSDGTPWPGNNSRDHPAMIQVLLGHPGDRDVDGGELPRLFYVSREKRPGFRHHGKAGAMNALLRVSAVLTNGAYVLNLDCDHCVNNSSALREAMCFMMDPVAGNRTCFVQFALRDSGGGDSVFFDIEMKCLDGIQGPVYVGSGCCFSRKALYGFEPAAAADDGDDMDTAADWRRMCCFGRGKRMNAMRRSMSAVPLLDSEDDSDEQEEEEAAGRRRRLRAYRAALERHFGQSPAFIASAFEEQGRRRGGDGGSPDATVAPARSLLKEAIHVVSCAFEERTRWGKEIGWMYGGGVATGFRMHARGWSSAYCSPARPAFRRYARASPADVLAGASRRAVAAMGILLSRRHSPVWAGRRLGLLQRLGYVARASYPLASLPLTVYCALPAVCLLTGKSTFPSDVSYYDGVLLILLLFSVAASVALELRWSRVPLRAWWRDEKLWMVTATSASLAAVFQGILSACTGIDVAFSTETAASPPKRPAAGNDDGEEEAALASEITMRWTNLLVAPTSVVVANLAGVVAAVAYGVDHGYYQSWGALGAKLALAGWVVAHLQGFLRGLLAPRDRAPPTIAVLWSVVFVSVASLLWVHAASFSAPTAAPTTEQPIL", "text": "FUNCTION: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant cellulose synthase subfamily."}
+{"protein": "MGGRVFLAFCVWLTLPGAETQDSRGCARWCPQNSSCVNATACRCNPGFSSFSEIITTPTETCDDINECATPSKVSCGKFSDCWNTEGSYDCVCSPGYEPVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSYTCQCLPGFKFIPEDPKVCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTVCEDVDECSSGQHQCDSSTVCFNTVGSYSCRCRPGWKPRHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDSKTSSAEVTIQNVIKLVDELMEAPGDVEALAPPVRHLIATQLLSNLEDIMRILAKSLPKGPFTYISPSNTELTLMIQERGDKNVTMGQSSARMKLNWAVAAGAEDPGPAVAGILSIQNMTTLLANASLNLHSKKQAELEEIYESSIRGVQLRRLSAVNSIFLSHNNTKELNSPILFAFSHLESSDGEAGRDPPAKDVMPGPRQELLCAFWKSDSDRGGHWATEGCQVLGSKNGSTTCQCSHLSSFAILMAHYDVEDWKLTLITRVGLALSLFCLLLCILTFLLVRPIQGSRTTIHLHLCICLFVGSTIFLAGIENEGGQVGLRCRLVAGLLHYCFLAAFCWMSLEGLELYFLVVRVFQGQGLSTRWLCLIGYGVPLLIVGVSAAIYSKGYGRPRYCWLDFEQGFLWSFLGPVTFIILCNAVIFVTTVWKLTQKFSEINPDMKKLKKARALTITAIAQLFLLGCTWVFGLFIFDDRSLVLTYVFTILNCLQGAFLYLLHCLLNKKVREEYRKWACLVAGGSKYSEFTSTTSGTGHNQTRALRASESGI", "text": "FUNCTION: Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor E5 subunit alpha]: Secreted, extracellular space. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily."}
+{"protein": "MDALVEDDICILNHEKAHKRDTVTPVSIYSGDESVASHFALVTAYEDIKKRLKDSEKENSLLKKRIRFLEEKLIARFEEETSSVGREQVNKAYHAYREVCIDRDNLKSKLDKMNKDNSESLKVLNEQLQSKEVELLQLRTEVETQQVMRNLNPPSSNWEVEKLSCDLKIHGLEQELELMRKECSDLKIELQKAKQTDPYQEDNLKSRDLQKLSISSDNMQHAYWELKREMSNLHLVTQVQAELLRKLKTSTAIKKACAPVGCSEDLGRDSTKLHLMNFTATYTRHPPLLPNGKALCHTTSSPLPGDVKVLSEKAILQSWTDNERSIPNDGTCFQEHSSYGRNSLEDNSWVFPSPPKSSETAFGETKTKTLPLPNLPPLHYLDQHNQNCLYKN", "text": "FUNCTION: Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity (PubMed:14560022, PubMed:21931631). Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization (PubMed:14560022, PubMed:21931631). Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1 (PubMed:14560022, PubMed:21931631). Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B (PubMed:14560022, PubMed:21931631). Participates in IFNB promoter activation via TICAM1 (PubMed:15611223). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MAEWKTKRTYDEILYETYNGIAKITINRPEVHNAFTPKTVAEMIDAFADARDDQNVGVIVLAGAGDKAFCSGGDQKVRGHGGYVGDDQIPRLNVLDLQRLIRVIPKPVVAMVSGYAIGGGHVLHIVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEQLEEETIKWCEEMLEKSPTALRFLKAAFNADTDGLAGIQQFAGDATLLYYTTDEAKEGRDSFKEKRKPDFGQFPRFP", "text": "FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2- naphthoyl-CoA (DHNA-CoA). SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB subfamily."}
+{"protein": "MSKQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEVWLENTQPMLSHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFLENQDRFRG", "text": "FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4- dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily."}
+{"protein": "MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAGQEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD", "text": "FUNCTION: Accessory component of the DNA polymerase epsilon complex (PubMed:10801849). Participates in DNA repair and in chromosomal DNA replication (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKAILLLAIFSVLTVAICGVSQNYGNVRYNYTELPNGEYCYIPRRRCVTTEQCCKPYDTVNNFAACGMAWPEDKKRKVNKCYICDNELTLCTR", "text": "FUNCTION: Probable neurotoxin with ion channel impairing activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 27 (Jztx-72) family. ICK-72 subfamily."}
+{"protein": "MAAHKRLQKEITDMLKTPPSWCSAHLVDDNLQKWKATVQGPEGSPFEKGVFSMDIDIPADYPFKPPTLKFTTKIYHPNIKTSDGAICAEVFSTWSPQLKILDVLTTIRSILTDPNPDNPLETEIAQQFKTDRNAFNKTAKEWTKKYAK", "text": "FUNCTION: Involved in protein ubiquitination and degradation during development. Mediates protein ubiquitination at the mound and finger stage required for subsequent development and may be an essential component of the developmental transition between the induction of postaggregative gene expression and subsequent cell-type differentiation and morphogenesis. ubcB and ubpB differentially control ubiquitination/deubiquitination and degradation of mkkA protein in a cell-type-specific and temporally regulated manner. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "MKQIPIEYQVSPYMVFFLIITIQMGVGMLGFERISAKLVGNDAWISTLLFGISVNVMIWIIYQILNQGNGDIIAINQNVLGKWIGGLLNFIFLSYIVLLGATTLHTYIEVVHVWMFPSISSWVIAGAFLGLCYYIVTGGFRVVAGIGFFGIVIPSILIFTFFYPLQYADFRNLFPIAQHSFLEIMKGMKGNMFSFFGFEMLLLYYPFIKKARTSQKYAHYANLVTTIVYTYLMILTLAFFSEKQLANAIWAYLSMIKIIQFPFIERFEYIIVSVWAFFILPNVSFTLWGVSRGIKEALGIKQKYVLPVIILFIFILSFFLNNRNKINLLNTWTGQIGFVYIYVYLPVLWLIQTAKIKLRR", "text": "FUNCTION: Required for the germination response to inosine. Has no role in L-alanine germination. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Spore germination protein (SGP) (TC 2.A.3.9) family."}
+{"protein": "METRETKPVIFLFPFPLQGHLNPMFQLANIFFNRGFSITVIHTEFNSPNSSNFPHFTFVSIPDSLSEPESYPDVIEILHDLNSKCVAPFGDCLKKLISEEPTAACVIVDALWYFTHDLTEKFNFPRIVLRTVNLSAFVAFSKFHVLREKGYLSLQETKADSPVPELPYLRMKDLPWFQTEDPRSGDKLQIGVMKSLKSSSGIIFNAIEDLETDQLDEARIEFPVPLFCIGPFHRYVSASSSSLLAHDMTCLSWLDKQATNSVIYASLGSIASIDESEFLEIAWGLRNSNQPFLWVVRPGLIHGKEWIEILPKGFIENLEGRGKIVKWAPQPEVLAHRATGGFLTHCGWNSTLEGICEAIPMICRPSFGDQRVNARYINDVWKIGLHLENKVERLVIENAVRTLMTSSEGEEIRKRIMPMKETVEQCLKLGGSSFRNLENLIAYILSF", "text": "FUNCTION: Glycosylates the amino acid-related molecules isoleucic acid (2-hydroxy-3-methylpentanoic acid) and valic acid (2-hydroxy-3- methylbutyric acid). Acts as a negative regulator of salicylic acid (SA)-dependent plant defense in the absence of pathogens and promotes the jasmonate (JA) response. Negatively influences the onset of senescence. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "MEPSACEDLKAFERRLTEVVSSYRPSTFRWRKLLAVVLSAMSMCTAISAWYWLRDPRTTVVPLTESLWIHPVFTVATLTLVVLFILGIQKLVIAPQIITSRTRMVLGDFNMSCDDTGKLILKPRQSNNNST", "text": "FUNCTION: May form with the serine/threonine protein phosphatase l(1)G0269 an active complex dephosphorylating and activating lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels (By similarity). SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein Cytoplasm. SIMILARITY: Belongs to the CNEP1R1 family."}
+{"protein": "MEVSMPLPQIYVEKTLALIKPDVVDKEEEIQDIILGSGFTIIQRRKLHLSPEHCSNFYVEQYGKMFFPNLTAYMSSGPLVAMILARHKAISYWKELMGPSNSLVAKETHPDSLRAIYGTDELRNALHGSNDFAASEREIRFMFPAVIIEPIPIGQAAKDYINLYVAPTLLQGLTELCKEKPPDPYLWLADWLMKNNPNKPKLCHFPVTEEP", "text": "FUNCTION: Functions as part of axonemal radial spoke complexes that play an important part in the motility of sperm and cilia (PubMed:36417862). Does not seem to have NDK kinase activity. Confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. May play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species (PubMed:12788088). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the NDK family."}
+{"protein": "MDLIPNFSMETWLLLVISLVLLYLYGTHSHGIFKKLGIPGPKPLPFLGTILAYRKGFWEFDKYCHKKYGKLWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTNRRNFGPVGILKKAISISEDEEWKRIRALLSPTFTSGKLKEMFPIINQYTDMLVRNMRQGSEEGKPTSMKDIFGAYSMDVITATSFGVNVDSLNNPQDPFVEKVKKLLKFDIFDPLFLSVTLFPFLTPLFEALNVSMFPRDVIDFFKTSVERMKENRMKEKEKQRMDFLQLMINSQNSKVKDSHKALSDVEIVAQSVIFIFAGYETTSSALSFVLYLLAIHPDIQKKLQDEIDAALPNKAHATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGVFIPKGTVVMIPTFALHKDPHYWPEPEEFRPERFSKKNQDNINPYMYLPFGNGPRNCIGMRFALMNMKVALFRVLQNFSFQPCKETQIPLKLSKQGLLQPEKPLLLKVVSRDETVNGA", "text": "FUNCTION: This isozyme seems to be implicated in olfaction. Active in the demethylation of erythromycin as well as benzphetamine. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "FKFRQSPSSPRFRLNSRNWALNVTTPLTVDSSSSPPIEEEPKTQRFDPGAPPPFNLADIRAAIPKHCWVKNPWKSMSYVVRELAIVFALAAGAAYLNNWLVWPLYWIAQGTMFWALFVLGHDCGHGSFSNDPRLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPMSEKIYKSLDKPTRFFRFTLPLVMLAYPFYLWARSPGKKGSHYHPDSDLFLPKERNDVLTSTACWTAMAVLLVCLNFVMGPMQMLKLYVIPYWINVMWLDFVTYLHHHGHEDKLPWYRGKEWSYLRGGLTTLDRDYGLINNIHHDIGTHVIHHLFPQIPHYHLVEATEAAKPVLGKYYREPDKSGPLPLHLLGILAKSIKEDHFVSDEGDVVYYEADPNLYGEIKVTAE", "text": "FUNCTION: Chloroplast omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 16:3 and 18:3 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; Peripheral membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
+{"protein": "MAMKFIAPMAFVAMQLIIMAAAEDQSAQIMLDSDIEQYLRSNRSLRKVEHSRHDAINIFNVEKYGAVGDGKHDCTEAFSTAWQAACKKPSAMLLVPGNKKFVVNNLFFNGPCQPHFTFKVDGIIAAYQNPASWKNNRIWLQFAKLTGFTLMGKGVIDGQGKQWWAGQCKWVNGREICNDRDRPTAIKFDFSTGLIIQGLKLMNSPEFHLVFGNCEGVKIIGISITAPRDSPNTDGIDIFASKNFHLQKNTIGTGDDCVAIGTGSSNIVIEDLICGPGHGISIGSLGRENSRAEVSYVHVNGAKFIDTQNGLRIKTWQGGSGMASHIIYENVEMINSENPILINQFYCTSASACQNQRSAVQIQDVTYKNIRGTSATAAAIQLKCSDSMPCKDIKLSDISLKLTSGKIASCLNDNANGYFSGHVIPACKNLSPSAKRKESKSHKHPKTVMVKNMGAYDKGNRTRILLGSRPPNCTNKCHGCSPCKAKLVIVHRIMPQEYYPQRWMCSRHGKIYHP", "text": "SUBCELLULAR LOCATION: Secreted Plastid, amyloplast Secreted, cell wall. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
+{"protein": "MAESTNLRLRLPLICIILEVILIILFGVLVEYNDDTDAKKWNKNNSTDPATNEFYYRYPSFQDVHVMIFVGFGFLMTFLQRYGFSSMGFNFLIAAFSLQWATLMQGFFHGMHHGKIHVGVTSMINADFCTGAVLISFGAVLGKTSPVQLLVMAILEVTLFAVNEYILLSILGANDAGGSMTIHTFGAYFGLMVTRILHRPNLDKSKHKNSSVYHSDLFAMIGTIFLWMFWPSFNSAITQYGDPQHRTAANTYYSLAACTLATFGFSSLVNPEGKLDMVHIQNAALAGGVAVGTAGEMMLTPFGSMIVGFLAGTISVLGYKYLTPFMESKLKIQDTCGIHNLHGMPGILGAIVGAVTAALASRDVYGNGLDKVFLEAADNSQWSAQTKGGFQAISLAVTLGIALIGGLITGFLLKLPIYGTPPDTQCFEDAVYWEVPGEEEDHHELNEVSTQNEVEKLNS", "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": "MPIGGDVKADQETSGSRSIKRIGFGFIGGIGYDITPNITLDLGYRYNDWGRLENVRFKTHEASFGVRYRF", "text": "SIMILARITY: Belongs to the opacity porin family."}
+{"protein": "MVRKCLLAVLMLLSVIVLPGCWDKRELTDLAIISAIGIDRTNDSNYVLHLQIINPGNVAGGLQGGGAGDRPPVSVYSIEGNNITEALRKASMKVSRRLYFAHTNLVVINEKLAKEEGLDFVLDNLDRDTEFRTTATFVVAHKTKAENIVKILTPIDKIPSNKVNKTLDFTEAQYGRVVKINIQDVLKTLAANTMAPVIPGYMMIGDDKKGVSMENTQATDPKAILQADGLAVFDKAGYLKYWLEDDESVGAVWLMNKIQHTFINADWGKTKDAVSLQVTHQDTKLVPKMRNGRPYIHVKVSVEGIIDAVKYPFQLSDPKVLAAIEKALNKELEKEISHTVKKIKKNKIDFIGFGDTIYRKYPEQWEKMKDTWDKEYLPELPIDVKAETYIRRTGLRNNPIKHQFKDD", "text": "FUNCTION: Involved in the germination response to the combination of glucose, fructose, L-asparagine, and KCl. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the GerABKC lipoprotein family."}
+{"protein": "MISVATAECFTHGKIGIKIHKMACGYREFEKDPNYSIINGNVFVIASMFLPSKKGIESILDVKLPEPDYVFKYSKAYNQENDILVAKMVANALKNKLNCDIAISSTAGVGNGAICILTDKNEYNFTSDIYGDLIKGENILKRQDNGVNKAFNTFVEILKKEYGLK", "text": "SIMILARITY: Belongs to the UPF0254 family."}
+{"protein": "MSETILITGSSRGIGKAIALRLAQAGFDIVVHCRSRIEEAEAVAQAVRELGQNARVLQFDVSCRSEAADKLTADVEAHGAYYGVVLNAGLTRDNAFPALTDEDWDRVLRTNLDGFYNVLHPIMMPMIRRRKAGRIVCITSVSGLIGNRGQVNYSASKAGIIGAAKALAVELAKRKITVNCVAPGLIDTDILDENVPIDEILKMIPAGRMGDPEEVAHAVNFLMGEKAAYVTRQVIAVNGGLC", "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": "MQVSYFHVAADVPDAIGSVEGPDAAVVIDVLRATTTIAWALHNGAEAVQAFADLDELRLQSRNWPEQTRLLLGERGGRMLEGFDLGNSPVAVIPEVVQGKRLFMSTTNGTRALQRVRDVSVVMTVALPNRQAVAQRLLRDQPERVWMVGSGWEGTYSLEDSLAAGALADALVAAGAQVANDELQAALALWAQWKHDPEACLRVASHGQRLTRLGNHDADFSCCAGLDQLSVVPTQTEPGVLRAIRV", "text": "SIMILARITY: Belongs to the ComB family."}
+{"protein": "MMMRDLALAGMLISLAFLSLLPSGCPQQTTEDACSVQILVPGLKGDAGEKGDKGAPGRPGRVGPTGEKGDMGDKGQKGTVGRHGKIGPIGAKGEKGDSGDIGPPGPSGEPGIPCECSQLRKAIGEMDNQVTQLTTELKFIKNAVAGLRETESKIYLLVKEEKRYADAQLSCQARGGTLSMPKDEAANGLMASYLAQAGLARVFIGINDLEKEGAFVYSDRSPMQTFNKWRSGEPNNAYDEEDCVEMVASGGWNDVACHITMYFMCEFDKENL", "text": "FUNCTION: Lectin that plays a role in innate immunity, apoptosis and embryogenesis. Calcium-dependent lectin that binds self and non-self glycoproteins presenting high mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope. Primarily recognizes the terminal disaccharide of the glycan. Also recognizes a subset of fucosylated glycans and lipopolysaccharides. Plays a role in innate immunity through its ability to bind non-self sugars presented by microorganisms and to activate the complement through the recruitment of MAPS1. Also plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding. Finally, plays a role in development, probably serving as a guidance cue during the migration of neural crest cells and other cell types during embryogenesis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the COLEC10/COLEC11 family."}
+{"protein": "MAVLVVLLFFLVAGALGNEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVMVKGVDKLALPAGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSLLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILEAKQENTQSPYNLAYKYNLEYSVVFNLVLWIMIGLALAVIITSYNIWNMDPGYDSIIYRMTNQKIRID", "text": "FUNCTION: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (By similarity). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin- angiotensin system (RAS) (By similarity). Through its function in V- type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (PubMed:26376863, PubMed:29127204, PubMed:30985297). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Cytoplasmic vesicle, autophagosome membrane; Single-pass type I membrane protein Cell projection, dendritic spine membrane; Single-pass type I membrane protein Cell projection, axon Endosome membrane; Single-pass type I membrane protein Cytoplasmic vesicle, clathrin-coated vesicle membrane; Single-pass type I membrane protein Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type I membrane protein."}
+{"protein": "MKKIQLNSIASSCSLSGQRLDLVLSKLFREYSRSYLKKLIIMNQVLVNESIVNQPDKKILGGETLTIHPFSKDLLVDIPENIFLDIVYEDSDILIINKPAGLVVHPGSGNKSGTILNALLYHYKNSKDLPRAGIVHRLDKDTSGLMVIAKNIFSYNHLLLLLKEKKIIREYEGIVHGKMIAGGTINKPIMRHYNRRTCMMVHHLGKPSVTHYKVLSRFKFHTHIAIRLETGRTHQIRVHMLHIKYPLVGDPCYSGFKIQSNYRKDKKTNKIYKFPRQALHANHLSLHHPIKKNVMSWTVPLPQDIQELLLKI", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RluA family."}
+{"protein": "MRLRVRLLKRTWPLEVPETEPTLGHLRSHLRQSLLCTWGYSSNTRFTITLNYKDPLTGDEETLASYGIVSGDLICLILQDDIPAPNIPSSTDSEHSSLQNNEQPSLATSSNQTSMQDEQPSDSFQGQAAQSGVWNDDSMLGPSQNFEAESIQDNAHMAEGTGFYPSEPMLCSESVEGQVPHSLETLYQSADCSDANDALIVLIHLLMLESGYIPQGTEAKALSMPEKWKLSGVYKLQYMHPLCEGSSATLTCVPLGNLIVVNATLKINNEIRSVKRLQLLPESFICKEKLGENVANIYKDLQKLSRLFKDQLVYPLLAFTRQALNLPDVFGLVVLPLELKLRIFRLLDVRSVLSLSAVCRDLFTASNDPLLWRFLYLRDFRDNTVRVQDTDWKELYRKRHIQRKESPKGRFVMLLPSSTHTIPFYPNPLHPRPFPSSRLPPGIIGGEYDQRPTLPYVGDPISSLIPGPGETPSQFPPLRPRFDPVGPLPGPNPILPGRGGPNDRFPFRPSRGRPTDGRLSFM", "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 and plays a role in several biological processes such as cell cycle, cell proliferation, or maintenance of chromosome stability (PubMed:15145941, PubMed:34791250). Recognizes and ubiquitinates BIRC2 and the cell cycle regulator DLGAP5 (PubMed:15145941, PubMed:16510124, PubMed:22212761). Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination. Mediates the ubiquitination and proteasomal degradation of UXT isoform 2, thereby impairing the NF-kappa-B signaling pathway (PubMed:33010352). Inhibits NF-kappa-B pathway also by promoting the ubiquitination of TRAF2 (PubMed:22212761). Affects the assembly state and activity of the proteasome in the cells including neurons by ubiquitinating the proteasomal subunit PSMA2 via 'Lys-63'-linked polyubiquitin chains (By similarity). Promotes 'Lys-48'-linked polyubiquitination SIRT7, leading to the hydrogen peroxide-induced cell death (PubMed:36646384). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion Cytoplasm, cytosol Note=Predominantly cytoplasmic (PubMed:16096642). A minor proportion is detected in the nucleus (PubMed:16096642). Relocates from the cytosol to depolarized mitochondria (PubMed:23933751)."}
+{"protein": "MGDPSKQDILTIFKRLRSVPTNKVCFDCGAKNPSWASITYGVFLCIDCSGSHRSLGVHLSFIRSTELDSNWSWFQLRCMQVGGNASASSFFHQHGCSTNDTNAKYNSRAAQLYREKIKSLASQATRKHGTDLWLDSCVVPPLSPPPKEEDFFASHVSPEVSDTAWASAIAEPSSLTSRPVETTLENNEGGQEQGPSVEGLNVPTKATLEVSSIIKKKPNQAKKGLGAKKGSLGAQKLANTCFNEIEKQAQAADKMKEQEDLAKVVSKEESIVSSLRLAYKDLEIQMKKDEKMNISGKKNVDSDRLGMGFGNCRSVISHSVTSDMQTIEQESPIMAKPRKKYNDDSDDSYFTSSSSYFDEPVELRSSSFSSWDDSSDSYWKKETSKDTETVLKTTGYSDRPTARRKPDYEPVENTDEAQKKFGNVKAISSDMYFGRQSQADYETRARLERLSASSSISSADLFEEPRKQPAGNYSLSSVLPNAPDMAQFKQGVRSVAGKLSVFANGVVTSIQDRYGS", "text": "FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Note=Also found on peripheral punctate structures likely to be endoplasmic reticulum-Golgi intermediate compartment."}
+{"protein": "MTSWLCASNMKFRINKFKIEKFQIDNSDIVGKIMGLDINTCDLLTKAVVVDHECEYYWDSKVCICGKDPLTKLKQLEKVECLDFSKIAQEITGGIISSESLRDMYDYISRMLYDSETFEFPLEWDFTFANRYILVPRSYENNSQIEMIKGFCFFADELPFIKPLIVKFFTEKNPTIVY", "text": "SIMILARITY: Belongs to the mimivirus L39/R874 family."}
+{"protein": "MTKADFISLVAQTAGLTKKDATTATDAVISTITDVLAKGDSISFIGFGTFSTQERAAREARVPSTGKTIKVPATRVAKFKVGKNLKEAVAKASGKKKK", "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. 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": "MAFMEKIFPDILEAIRNEEIIKESKKIPMPYFGLFALVIFDKVKELGSETSLYEIGEEFGKMLSPKNIEELKKIFKLMNFGDLEIDENKILLKNPPYKIKLSNPPYQWVSKEEPIHDFIAGILAGCLEEIFKKKFVVNEVECVSQGKDKCVFEVKEVDELNK", "text": "SIMILARITY: Belongs to the M.jannaschii MJ0150/MJ0739/MJ0745/MJ1460/MJ1642 family."}
+{"protein": "MDLVDPSQSAAAAAGTQTVKDEVSEKCQKLFQDFLEEFRGSDGELKYQSDAEELIRPERNTLLVSFIDLEQFNQQLATTIQEEFYRVYPYLCRAVKAFARDHGNVPQNKEFYVAFQDLPTRHKIRELTTPRIGSLLRISGQVVRTHPVHPELVSGTFLCLDCQTLVRDVEQQFKYTQPSICRNPVCANRRRFMLDTNKSRFVDFQKVRIQETQAELPRGSIPRSVEVILRAEAVESCQAGDRCDFTGSLIVVPDISQLATPGVRAETSARVGGTEGYQAEGVQGLRALGVRDLSYKLVFLACYVCPTNPRFGGKDLHEEDMTAESIKNQMSVKEWEKVFEMSQDKNLYHNLCTSLFPTVHGNDEVKRGILLMLFGGVPKTTMEGTSLRGDINVCIVGDPSTAKSQFLKHVEEFSPRAVYTSGKASSAAGLTAAVVKDEESHEFVIEAGALMLADNGVCCIDEFDKMDTKDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPVGGRYDRAKSLKQNINLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYTLDEVRRYLLFARQFKPKISKESEDFIVEQYKRLRQRDGTGVTKSAWRITVRQLESMIRLSEGMARMHCSDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEDEHEAEEEPQEVINGDASVPSGVNGHVNGMNGHAEEPNAATPKPSLRLNFAEYKRISNLLVLQLRKMEDEDETSQRKSELINWYLKEIESEIDSEEELVTRKQIIDKVVHRLVHYDQILIELTQTGLKGTGDEEVPKEEDPYLVVNPNYILED", "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. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development. May replace mmcm6 in the mcm2-7 complex (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. SIMILARITY: Belongs to the MCM family."}
+{"protein": "MLVTLLETFSVVFQVANGDGNCVPRFQDDVEFCDNYILEAVTEASKMIAPRAREQKLCCGFNKFTHCVTTASKKCSEAADRVKRVLDTKMTSLGVHCPDTNKVCNGGVNTSVSANTVTVYLLFSLGYFFYMNKL", "text": "FUNCTION: Probable secreted venom toxin. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "LCVAHGITREKIEENGSMRENIIDVTKTNRVFMQHIDVLENSLGFK", "text": "FUNCTION: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females (By similarity). Acts as a shuttle for pheromonal communication between individuals of the same species. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
+{"protein": "MADTGKGSSVAGCNDSCGCPSPCPGGNSCRCRMREASAGDQGHMVCPCGEHCGCNPCNCPKTQTQTSAKGCTCGEGCTCASCAT", "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) (PubMed:18287486). Plays a role in storing and distributing Zn ion in seed (PubMed:22014117). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane. SIMILARITY: Belongs to the metallothionein superfamily. Type 15 family."}
+{"protein": "MGSIRGDLQPLFVMPPPPLDEDCDDIFNSDESSWGLLSLSCFGIIMGLWFFASVCLIFGVYGSETVWLGPNSSILVKPSSIFVKSINAKELDFSKPGLQLYGFNGQSTPSGYFVNWTESRVLSVSQNSYKGWPYYLNRGTHMNISYNILPKGSAVRLVITEGMPFFYRSSLKDIAFRDTAWSWNLIQGSGMIQLDISKSKGYYLTVANLKRKDVEVELDIDVKVVLYDTKQSSYNCSFSNGECSFKMNERSPVENYAVVTSPALGQGVSIDDEWYIELSYQPRLIAYGSFTGVLLSFMLVAIHFCNKLKCCGGEGFLSEDDSVRTCLLADKGDNDCCNDVEASNKSLCAICFDAPRDCCFLPCGHCVSCYQCGTKIKRTKGRCPICRKKIMHVKRIYTA", "text": "FUNCTION: Involved in pollen mitosis II (PMII) regulation during male gametogenesis. SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Vacuole membrane; Multi- pass membrane protein."}
+{"protein": "MRMGKIAVGYGFLLLLVFQLGVRASTLFNKYNVQELSSLKDLLERLEEKLSPGEESDVYAGSEDLVNDPEEDADLILDNVRKQAEKEFYKPAGFRDENLQRGRLRSIATSARSMNGCFGNRIERIGSWSSLGCNNSRFGSKKRIF", "text": "FUNCTION: Exhibits natriuretic and vasodepressor activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family."}
+{"protein": "MKPAYPPLLLQMSPAYTPRPLKNLFTANQCWAHLLEEGGLRDIEVETVTKMLACGTSILGVKHYTCGNHSCPHVKYLCNTCHCRACPSCGKKATDQWITVQNNRLPDCPWQHLVFTLPDTLWPLFFYNRWLLDALFRLAADNLIYAAKRRGLRVGIFGALHTYGRRLNWHPHVHLSVTAGGLDEQGVWKNLSFHKEALRRRWMWLVRDYLLGQPLSQLTMPPPLAHILCESDWRRLILAAGGQHWHIHLSKKTKNGRKTVNYLGRYLKKPPISGSRLAHYTNGATLRFTYLDHRTQAYQQETLSQADMLFRVVQHIPEKHFRMIRYFGFLANRVCGQYLPKVYEALKMATPGPTPKLYFAPMAKAFLNVDPFRCVLCGARMVYTAAISGLTVQGLNLNAQAIAQMRYVKP", "text": "FUNCTION: Involved in the transposition of the insertion sequence. SIMILARITY: Belongs to the transposase 32 family."}
+{"protein": "MKVKAVRGIANPLGTIDAHGTVIESIANAGDGVDILNRHREKIGSGFVHLEGDNVILTGYVDEEQYTAEKIEETGLSVGFNANGVKAREIDGVGYYKDVTITEVSLTPLPSNKGAKVTKVREENKGEQEQMGANETQEIMKQAIEAGVKVRELEAKVEELNKEREELKKEREASIPSEKPEDAERKFMRELGSKMAEMPEQGFLREFANGADLNVVNSLGSITSKYARKSGIYDGAMKARFQGLTLAEDGVDDTFISGTFKAGTDKNKSQTATKRSLRPQMAEAYLQMDKATVRGVNDSGALSEYVMSEMVNRVIQKVEYNMILGSVDGSNGFYGLKTATDGWTKQIEYTDLFEGITDAVAECSISDAITIVMSPQTFAELRKAKGTDGHSRFNELATKEQIAQSFGAVNLETRVWMPKDEVAVYNHDEYVLIGDLNVENYNDFDLRYNVEQWLSETLVGGSIRGKNRSAYLKKKGSLGV", "text": "FUNCTION: Assembles to form a prolate capsid about 56 nm in length and 41 nm in width. SUBCELLULAR LOCATION: Virion."}
+{"protein": "MSDQFNSREARRKANSKSSPSPKKGKKRKKGGLFKKTLFTLLILFVLGVVGGAVTFAVMVSDAPSLDESKLKTPYSSTIYDKNGKEIAEVGAEKRTYVSIDEIPDVVKEAFIATEDARFYEHHGIDPVRIGGALVANFKDGFGAEGGSTITQQVVKNSLLSHQKTLKRKVQEVWLSIQLERNYSKDEILEMYLNRIYFSPRAYGIGKAAEEFFGVTDLSKLTVEQAATLAGMPQSPTAYNPVKNPDKAEKRRNIVLSLMKKQGFISDSQYNKAKKVAVKDEGVVSQKEYEKASTNKYSAFVEEVMKEIDEKSDVDPSADGLKIYTTLDTKAQDKLDELMDGDTVGFTEGMQGGVTLLDTKNGEVRAIGAGRNQPVGGFNYATQTKAQPGSTIKPILDYGPVIENKKWSTYEQIDDSAYTYSNGKPIRDWDRKYLGPISMRYALAQSRNIPALKAFQAVGKDTAVDFANGLGLGLTKDNVTEAYSIGGFGGNDGVSPLTMAGAYSAFGNNGTYNEPHFVKSIEFNDGTKLDLTPKSKSAMSDYTAFMITDMLKTAVKTGTGQLAQVPGVEVAGKTGTTNFDDNEVKRYNIASGGARDSWFVGYTPQYTAAVWTGMGENEAGKKSLSAEEQKVAKRIFAQLIADVDDGSGSFEKPDSVVEATVEKGSNPAKLAGPNTPSDKKLTEYFVKGTAPSTVSKTYEKEEKEETAKLSGLNVKYDKDNQSLTLSWNYDGDATFAVKQSVDGGSYSEIQNSSAKEAVISGVQPGSVYKFEVTAVSDDGKSTASTSYEVPKAEDDEDKKDQQQTDDEKQDDEKTQDDTQTDDSQKDDGQTDQDQTDDSTNDQDKKQDNTNTNPSDNNNQDQSNDNDNDNSNNQDTSDGDSNSGKNDSTGSDTNKNKTDTSNKTQTNSSSIEKTN", "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) (Probable). Required for vegetative growth (Probable). Has a partially redundant function with PBP-2A (pbpA) during spore outgrowth (PubMed:9851991). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Forespore inner membrane; Single-pass type II membrane protein Note=Probably found all over the whole cell at low concentrations. Also localizes to the division site in vegetative cells. SIMILARITY: In the C-terminal section; belongs to the transpeptidase family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 51 family."}
+{"protein": "MEKDTKQVDIIFRSKLPDIYIPNHLPLHSYCFENISEFSSRPCLINGANKQIYTYADVELNSRKVAAGLHKQGIQPKDTIMILLPNSPEFVFAFIGASYLGAISTMANPLFTPAEVVKQAKASSAKIIVTQACHVNKVKDYAFENDVKIICIDSAPEGCLHFSVLTQANEHDIPEVEIQPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYIHSEDVMLCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVSFLELIQRYKVTIGPFVPPIVLAIAKSPMVDDYDLSSVRTVMSGAAPLGKELEDTVRAKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFEIKSGACGTVVRNAEMKIVDPKTGNSLPRNQSGEICIRGDQIMKGYLNDPEATARTIDKEGWLYTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSTITEDEVKDFISKQVIFYKRIKRVFFVDAIPKSPSGKILRKDLRAKLAAGLPN", "text": "FUNCTION: Major enzyme of the phenylpropanoid pathway that mediates the production of several precursors for numerous metabolites and regulates carbon flow (PubMed:26412334). Catalyzes the formation of CoA thioesters using 4-coumarate, ferulate, caffeate, and cinnamate as substrates (PubMed:8819324, PubMed:26412334). Follows a two-step reaction mechanism, wherein a (hydroxy)cinnamate substrate first undergoes adenylation by ATP leading to an acyl-AMP, followed by a thioesterification in the presence of CoA to yield the final (hydroxy)cinnamoyl-CoA product (PubMed:26412334). Almost inactive toward sinapate (PubMed:8819324, PubMed:26412334). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
+{"protein": "MPAELRRLAVLLLLLSARAALAQPWRNENYERPVDLEGSGDDDPFGDDELDDIYSGSGSGYFEQESGLETAVSLTTDTSVPLPTTVAVLPVTLVQPMATPFELFPTEDTSPEQTTSVLYIPKITEAPVIPSWKTTTASTTASDSPSTTSTTTTTAATTTTTTTTISTTVATSKPTTTQRFLPPFVTKAATTRATTLETPTTSIPETSVLTEVTTSRLVPSSTAKPRSLPKPSTSRTAEPTEKSTALPSSPTTLPPTEAPQVEPGELTTVLDSDLEVPTSSGPSGDFEIQEEEETTRPELGNEVVAVVTPPAAPGLGKNAEPGLIDNTIESGSSAAQLPQKNILERKEVLIAVIVGGVVGALFAAFLVMLLIYRMKKKDEGSYTLEEPKQANVTYQKPDKQEEFYA", "text": "FUNCTION: Cell surface proteoglycan that may bear both heparan sulfate and chondroitin sulfate. The multiple functional domains provide potential sites for mediating the adhesive cell-matrix interactions and cytoskeletal reorganization involved in limb chondrogenesis. Interaction with other matrix ligands as well as phosphorylation and shedding of the ectodomain might be involved in cell shape changes that occur during chondrogenesis. Furthermore, shedding of the ectodomain might break the adhesive interactions that promoted condensation, thus facilitating the deposition of cartilage matrix molecules. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the syndecan proteoglycan family."}
+{"protein": "EHGYLLDKYTGCKVWCVINNESCNGECNKRRGGYYGYCYFWKLACYCQGARKSELWNYKTNKCKS", "text": "FUNCTION: Has a toxic effect on insects and mammals. On German cockroach larvae, it provokes contraction, paralysis and lethality (PubMed:26109302). Intracerebroventricular injection into mice causes severe neurotoxic symptoms (PubMed:26109302). It fully competes with the binding of the iodinated Css4 (AC P60266) on rat brain synaptosomes, with moderate affinity and in a concentration-dependent manner (EC(50)=25 nM). It may act on both site 3 and site 4 of voltage- gated sodium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family."}
+{"protein": "MKILTYNQLQEAFRDYAPRDFAVSRDDAFRVMRIYYNEGGGNLVAFCNAQLGGRLAQFYFVMKMDLYSYKPCHNSHIFATCRNRCSSYNTFVAPGVKNVYMDKINVIKFKRNGSSFGEKTMALDKFLHNANRVHMQTPVIEGTYLRFRRAQRCRNNCVADDARPFALERFSDDFEVLDPSTLTTNIAPVMACYDIETHSDGHNSSKPECDVIMCIGLAVFKNDRFEKVCFVYHSEAVEIPQASDDTYVVVFNNENHMITAFFEFLKTVNPDVILDYNGDVFDLPYIRGRLKGDKPLLRRYDLPAMQPNTKLFITKIGNRTDTYYFNYYIHIDLYKYFGVDANKRDVENFQLNTLSQYYLGDAKVDLNWQTMVEMYNNKQLGTIIKYNVQDCLLPIRLFNKLKLTDFMYSQCIMYRLCTDDFICNISHLISSTFFHLALTNTRADPATGLTVSDPYFFNKDDLGLMSSKGSAGLTTGMSRLRRRRIPLKDVPATAIRLGAIDENVKYEGGKVLQPRAGVYEFAFSLDFNSLYLTIMIDICACLTNLILCEDGNVYLNQDKQAINVQLLLQLLKQRSELKKCRDSQTESEFLYDLYDQMQNLSKRTANSIYGYYGIFCKLLANHITRVGREKLTAAIGTVEGLSNDPDLLREFGLSTLTFKVLYGDTDSTFVLPVFRREEIPEEGRMATLGRICAAVEARVNGLFTNGYKMAFENLMSVLILLKKKKYCYINNNNKIVFKGWLVKKDMPVFMRVAFRAAIEQVLRHQDLSKCLDSLKANMLMYLDAFGITKPLTDYSFSMTYNDGAGKTAADDDEAAPPKRRVITVARHCREILVNKATDFVPGNGDRIPYVLLDMQGNVTQKAYPLRLFDAQTMRISWLKHMTILNTFMNELLEIFGDEHKDALAECYSAILEKYMQHQAYDKKRAALVKIATKRKAPSASDASGKRARKGAAPSDDESGSSEDEDAPCEPKCANNTFKFCLYKAQ", "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": "MILNKVAKCYGKQIGFFGNKTTQFIKPNQTIFLIGGTKRLFTTQQQQSPKKEEPKSEQQKKVEDKTEEKEKEKDEEENENEKEKENEDGEGQKKKSKFNVPPIVTSVTSTFFAGVLVASTFGYLTYNFKKDISEEERYRLNSVESKFYHSIAEPFREFFDNIFENLRTKYEFFDMLFGPGKIHKVLPPPLPGGKKYTLVIDIDALTEITKTSKYPTLYKRAGLDFFLDHLRKDYEIYLYFNGNIPQNKYEQLQFKIDTNGKYFTGLLYPETGIKERNQFSKKIEMLDRDPSKVIFIDAASPYDHPNVINIGKFKSNSKDKLLIELLPVLESFSRKNLDDVRPEISQFQNISKQSLTKNLEDYLSTHNINSRQKK", "text": "FUNCTION: Component of the mitochondrial import inner membrane translocase that mediates the translocation of transit peptide- containing proteins across the mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM50 family."}
+{"protein": "MSEDSDMEKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALQHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRKKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDGIYIHDHENGTEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDALQSFSWNGRGFTDKVDRLKLAEVVKQVIEEQTLPHEPQ", "text": "FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
+{"protein": "MAAMECRDKAVVPPRRLVQARLPFKRLNPVPKEKHDAEAEGKKGKCSKSGLGQSKDSSTDTLHASTDNMENDCQLNSDVNFVPKLVNGKGPLDHFIQKSTKDNTDEIIVIIDSVDESNQRLSDDVDHVSFDSKASSAALTNGMLGKDMNKLSCLNSTQNSQTDDSMQTDVPCEAIANKGEDLVDGIQSCSGLTERNNLENTKVNQSELKDVIFEGKMPVVLLEDIMAAKSPQVTSLDGSVTSENETVELSHEGDSVLTNSSLSSLSVSSPEAQPVAETKRNTSPLAVSTPVRKVSQKLHKSSAEKEKLRLQRDQERADKLQKLQAEREEKGRLKEEAKAAKERAKEEAKKKKEEEKELKERERREKKEKEEKEKAEKLRVKEEKRKERQEALEAKLEEKRKKEEEKRLKEEEKRINAQKAEITRFFQKPKTPQAPKILAGSCGKFAPFEIKENMVLAPLCRIALYPDFLEQLDRLLRAQNSEVSFLRDLKCRKPRKTGPTFVNSSTDTVNSDVVVVDNCKTDAVPERGKFGRMKLLQFCENHRPAYWGTWNKKTTMIRPRNPWSKDSKLLDYEVDSDEEWEEEEPGESLSHSEGDDEEEGEDEDDDDGFFIPHGYLSEDEGVTEECDPENQKVRQKLKAKEWDELMAKGKRLHVLQPVKIGCIWESAQNDSGTNADLKILQQFTACILDSSVAEEEQQIQKCSKKRAKDQQILGQLLPLLHGNVNGSKVIIQEFQECCRQGLFSDVTAATDCGDTSPVSPNTSRPQTPVGEDSGVPSKARLKRIISENSVYEKRPEYRMCWYVHSEVLKSFDQEHLPVPCQWNYITQVPSSGKEDGGSVPGVAPVQSTPVSVKRKSTGSMCITKFMKRPRDAEQAEAMEMDGFQADTEEDEDDDDCMIVDVQPCKDSTLTVTETAPESRGTTAAHQDASMVSPSNTV", "text": "FUNCTION: Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. SUBCELLULAR LOCATION: Nucleus Note=DNA replication foci. SIMILARITY: Belongs to the CHAF1A family."}
+{"protein": "MADAKSTIAKDVTELIGNTPLVYLNRVVDGCVARVAAKLEMMEPCSSVKDRIGYSMISDAENKGLITPGESVLIEPTSGNTGIGLAFIAAAKGYRLIICMPASMSLERRTILRAFGAELVLTDPARGMKGAVQKAEEIKAKTPNSYILQQFENPANPKIHYETTGPEIWRGSGGKIDALVSGIGTGGTVTGAGKYLKEQNPNIKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPGVLDVNLLDEVIQVSSEESIETAKLLALKEGLLVGISSGAAAAAAIRIAKRPENAGKLIVAVFPSFGERYLSTVLFESVKRETENMVFEP", "text": "FUNCTION: Produces L-cysteine from O-acetyl-L-serine and hydrogen sulfide. Can also use pyrazole and 3,4-dihydroxypyridine instead of the hydrogen sulfide to produce two plant specific non-protein amino acids beta-pyrazolylalanine and L-mimosine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family."}
+{"protein": "MIEVKHLKTLQALRNCGSLAAAAATLHQTQSALSHQFSDLEQRLGFRLFVRKSQPLRFTPQGEILLQLANQVLPQISQALQACNEPQQTRLRIAIECHSCIQWLTPALENFHKNWPQVEMDFKSGVTFDPQPALQQGELDLVMTSDILPRSGLHYSPMFDYEVRLVLAPDHPLAAKTRITPEDLASETLLIYPVQRSRLDVWRHFLQPAGVSPSLKSVDNTLLLIQMVAARMGIAALPHWVVESFERQGLVVTKTLGEGLWSRLYAAVRDGEQRQPVTEAFIRSARNHACDHLPFVKSAERPTYDAPTVRPGSPARL", "text": "FUNCTION: Control of the last step in methionine biosynthesis; MetR is a positive activator of the metA, metE and metH genes. It is also a negative regulator of its own expression (By similarity). FUNCTION: Control of the last step in methionine biosynthesis; MetR is a positive activator of the metA, metE and metH genes. MetR is also a negative regulator of its own expression. Binds homocysteine as an inducer. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
+{"protein": "MGVIELCNTSSICIGRANPSCCSIERNQRRRIICMASSVPVQEESQQKQRVTGDAFIRPHLLKLSPYQPILPFEVLSTRLGRKPEDIVKLDANENPYGPPPEVIEALGAMKFPYIYPDPESRTLRAALAEDSGLESEYILAGCGADELIDLIMRCVLDPGDMIVDCPPTFTMYEFDAAVNGAHVIKVPRNPDFSLDVERIAEVVEHEKPKCIFLTSPNNPDGSIIDDETLLKILDLPILVILDEAYVEFSGMESKMKWVKKHENLIVLRTFSKRAGLAGLRVGYGAFPKSIIEFLWRAKQPYNVSVAAEVAACAALKNPAYLENVKVALVQERERLFNLLKEVPFLDPYPSYSNFILCKVTSGMDAKKLKEDLATMGVMIRHYNSKELKGYVRVSVGKPEHTEALMKCLKHFY", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily."}
+{"protein": "MPITIGRGFLKSEMFSQSAISQRSFFTLLWEKIKDFFCDTQRSTADQYIKELCDVASPPDAQRLFDLFCKLYELSSPSCRGNFHFQHYKDAECQYTNLCIKDGEDIPLCIMIRQDHYYYEIMNRTVLCVDTQSAHLKRYSDINIKASTYVCEPLCCLFPERLQLSLSGGITFSVDLKNIEETLIAMAEKGNLCDWKEQERKAAISSRINLGIAQAGVTAIDDAIKNKIAAKVIENTNLKNAAFEPNYAQSSVTQIVYSCLFKNEILMNMLEESSSHGLLCLNELTEYVALQVHNSLFSEDLSSLVETTKNEAHHQS", "text": "FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. SUBCELLULAR LOCATION: Secreted Host cytoplasm Note=Secreted via type III secretion system 2 (SPI-2 TTSS), and delivered into the host cytoplasm. Localizes to the Salmonella-containing vacuole (SCV) at early time points following invasion and subsequently traffics away from the SCV along Salmonella-induced filaments (Sifs) in epithelial cells. SIMILARITY: Belongs to the Sif family."}
+{"protein": "MAGVMKLACLLLACMIVAGPITSNAALSCGSVNSNLAACIGYVLQGGVIPPACCSGVKNLNSIAKTTPDRQQACNCIQGAARALGSGLNAGRAAGIPKACGVNIPYKISTSTNCKTVR", "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. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the plant LTP family."}
+{"protein": "MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEEELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA", "text": "FUNCTION: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A- mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Associated with microtubules."}
+{"protein": "MSATKPRLRSTQWFGTNDKNGFMYRSWMKNQGIPDHEFDGRPIIGICNTWSELTPCNAHFRKLAEHVKRGISEAGGFPVEFPVFSNGESNLRPSAMLTRNLASMDVEEAIRGNPIDAVVLLAGCDKTTPALLMGAASCDVPAIVVSGGPMLNGKLEGKNIGSGTAVWQLHEALKAGEIDVHHFLSAEAGMSRSAGTCNTMGTASTMACMAEALGVALPHNAAIPAVDSRRYVLAHMSGIRIVEMALEGLVLSKILTRAAFENAIRANAAIGGSTNAVIHLKAIAGRIGVPLELEDWMRIGRDTPTIVDLMPSGRFPMEEFYYAGGLPAVLRRLGEGGLLPNPDALTVNGKSLWDNVREAPNYDEEVIRPLDRPLIADGGIRILRGNLAPRGAVLKPSAASPELLKHRGRAVVFENLDHYKATINDEALDIDASSVMVLKNCGPRGYPGMAEVGNMGLPPKLLRQGVKDMVRISDARMSGTAYGTVVLHVAPEAAAGGPLAAVRNGDWIELDCEAGTLHLDITDDELHRRLSDVDPTAAPGVAGQLGKGGYARLYIDHVLQADEGCDLDFLVGTRGAEVPSHSH", "text": "FUNCTION: Catalyzes the dehydration of L-arabonate to L-2-keto-3- deoxyarabonate (L-KDA). Is involved in a degradation pathway of L- arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. To a lesser extent, can also use D-xylonate as substrate, but not D-galactonate, D-arabonate, and D-gluconate. SIMILARITY: Belongs to the IlvD/Edd family."}
+{"protein": "MAASYEEERDIQKNYWIEHSADLTVEAMMLDSRASDLDKEERPEVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESINGHYKNVKFMCADVTSPDLKITDGSLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGYIFFRESCFHQSGDSKRKSNPTHYREPRFYSKVFQECQTRDAAGNSFELSMIGCKCIGAYVKNKKNQNQICWIWQKVSSENDRGFQRFLDNVQYKSSGILRYERVFGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCSVEFEVADCTTKHYPDNSFDVIYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPKTPSAEFSEYIKQRGYDLHDVQAYGQMLKDAGFTDVIAEDRTDQFMQVLKRELDRVEKEKEKFISDFSKEDYDDIVGGWKSKLERCASDEQKWGLFIANKN", "text": "FUNCTION: Catalyzes N-methylation of phosphoethanolamine, phosphomonomethylethanolamine and phosphodimethylethanolamine, the three methylation steps required to convert phosphoethanolamine to phosphocholine. Required for root system development and epidermal cell integrity through its role in choline and phospholipid metabolism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. PEAMT family."}
+{"protein": "MGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSSRGRVYEYSNNNIKSTIDRYKKASSDSTNGGSTMEINAQYYQQESAKLRQQIQMLQNSNRHLMGDSLASLTVKELKQLENRLERGITRIRSKKHELLLAEIEYLQKREIELENESVYLRTKIAEVERLQQANMVSTHEFNAIQALVSRNFFQPNMIEGGSTGYPLPDKKVLHLG", "text": "FUNCTION: Probable transcription factor involved in seed development (PubMed:21447172, Ref.1, PubMed:29853599). Plays a role in seed morphogenesis by promoting the correct development of endotesta cell layer, which directs the further development of the seed coat, the endosperm, and consequently the embryo (Ref.1, PubMed:29853599). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MAANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEESKQPGVSEQQRHQLKHRELFLSRQFESLPATHIRGKCSVTLLNETDILNQYLDKEDCFFYSLVFDPVQKTLLADQGEIRVGCKFQAEIPDRLAEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQRNGYDLAKAMSTLVPQGGPVLCRDEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKTTDRYIQQKRLKAAEADSKLKQVYIPTYTKPNPNQIISVGSKPGMNGAGFQKGLTCESCHTTQSAQWYAWGPPNMQCRLCASCWIYWKKYGGLKTPTQLEGAARGTTEPHSRGHLSRPEAQSLSPYTTSANRAKLLAKNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLVRLPLATIVKDLVAQAPLKPKTPRGTKTPINRNQLTQNRGLGGIMVKRSYETMAGAGVPFSANGRPLASGIRSSSQPAAKRQKLNPADAPNPVVFVATKDTRALRKALTHLEMRRAARRPNLPLKVKPTLMTVRPPVPLPASSHPASTNEPIVLED", "text": "FUNCTION: May function as a transcriptional coregulator (By similarity). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MEDIIKTLPQHTCSFLKQRFTLYKYQDVWNHQEFLEGRMLSEQTFKAHPNDVFLASYPKSGTTWLKALAFAIITREKFDDSTSPLLTTMPHDCIPLLEKDLEKIQENQRNSLYTPISTHFHYKSLPESARTSNCKIVYIYRNMKDVIVSYYHFLRQIVKLSVEEAPFEEAVDEFCQGISSCGPYWEHILGYWKASLEKPEIFLFLKYEDMKKDPVPSVKKLADFIGHPFTPKEEEAGVIENIIKLCSFEKLSSLEVNKSGMHRPEEAHSIENRLYFRKGKDGDWKNYFTDEMIEKIDKLIDEKLGATGLVLK", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of quercetin, rhamnetin and isorhamnetin but not kaempferol. O-sulfation of position 3 of flavonol. May play a role in auxin transport. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sulfotransferase 1 family."}
+{"protein": "MNIVYSLANQLKDSLRDLLPVVLVMGFFQLVVIRQPLPDSLALLDLVLGLVFVVVGLTLFIKGLELGLFPLGENLARAFVKKGSVAWLLIFAFALGFGSTVAEPALIAVAARAGEVVSESGLIADTSAAQASFAFTLRMVVALSVGTAVVVGVLRIFKGWPLHLMIIAGYIIVLLLTLFAPNELIGIAYDSGGVTTSTITVPLVTALGVGLASTIKGRNPMLDGFGLIAFASVMPIIFVLLFGIFGLSLVTGST", "text": "FUNCTION: Part of a two-component antiporter that catalyzes the efflux of Na(+), Li(+) and K(+) in exchange for external protons. Shows a preference for Na(+), followed by K(+) and Li(+). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UmpA/UmpB family."}
+{"protein": "MNSKFQLILSTFVVIAAFTLLPRPCASIEFHRKLSSWSNGGATWYGAANGAGSDGGACGYQAAVDQAPFSSMIAAGSPSIYKSGLGCGSCYQVKCSGNSACSGNPVTVVLTDECPGGPCLSEPVHFDLSGTAFGAMANPGQADQLRAAGVLQIQYNRVPCNWGGVMLTFAVDAGSNPSYFAVLVKYENGDGDLSGMDLMQTGAGAAWTPMQQSWGAVWKLSAGAALQAPLSIRLTSSSGKTLVASNVIPSGWKPGASYTSTVNY", "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": "MVSNWNWNGMKRRRTPRRGYGRPYKPVVPITRVVVHQSALLKKDEVVGCEIKPDGDVARYKMMKVMLTCTLRMPPGELVNYIIVKSSSPIANWSAAFTTPALLVKESCQDMISIIAKGKVESNGVAGTDCTKSFNKFIRLGAGISQTQHLYVVMYTSVALKLVLEHRVYIEL", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the nanoviridae capsid protein family."}
+{"protein": "MAVAYADKPNHFINFPLTQFQGFVLNYKGLQFQLLDEGVDCKIQTAPHISLAMLDIQPEDYRSVDVAIQEVIDDMHWGEGFQIKFENPHILGRCIVLDVKGVEELHDDLVNYIRDKGCVDDQSRKWIGHCTIAQLTDAALSIKGNVDFINSMQFNYKITINPSSPARLEIVKLGAEKKDGFYETIASHWMGIRFEYNPPTDKLAMIMGYCCLEVVRKELEEGDLPENDDDAWFKLSYHYENNSWFFRHVYRKSSYFRKSCQNLDCNCLGFYESSVEED", "text": "SIMILARITY: Belongs to the coronaviruses ns2a protein family."}
+{"protein": "MADTVEEPQLQNGAAPAESETEQNPIPEPQLQTEPKLTGEIPEIEADLTPEEVQSEVTDAKPEEVQSEVKPEEVKTVVTDAKPEEAQSEVKPEEVQSVVTDTKPDLTDVDLSPGGSEEIPIRSTEVEQESTTSVLKKDDDGNKTFTMRELLSELKSEEGDGTPHSSASPFSRESASQPAENNPAMDLINRIQVNDEEGRSRQRVLAFAARKYASAIERNPDDHDALYNWALILQESADNVSPDSVSPSKDDLLEEACKKYDEATRLCPTLYDAYYNWAIAISDRAKIRGRTKEAEELWEQAADNYEKAVQLNWNSSQALNNWGLVLQELSQIVPAREKEKVVRTAISKFRAAIRLQFDFHRAIYNLGTVLYGLAEDTLRTGGSGNGKDMPPGELYSQSAIYIAAAHSLKPSYSVYSSALRLVRSMLPLPHLKVGYLTAPPVGNSLAPHSDWKRTEFELNHERLLQVLKPEPREMGRNLSGKAETMSTNVERKTVKVNITEIVSVTPCADLTLPPGAGLCIDTIHGPVFLVADSWESLDGWLDAIRLVYTIYARGKSDVLAGIITG", "text": "FUNCTION: Component of the endomembrane trafficking machinery that is involved in protein recycling to the plasma membrane. Forms a complex with BIG5/MIN7/BEN1 and actin to modulate the function of the trans- Golgi network /early endosome at the intersection of the exocytic and endocytic pathways. May be linking post-Golgi traffic with the actin cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm Endomembrane system Golgi apparatus, trans-Golgi network Early endosome."}
+{"protein": "MDVKAEAPNGPAPVKNENQNQPKPQRENMNMNKNQNQNQNNNMGGGGGPNKRNNMNMNKNFQNRGGKGGPGMGPRGPMKNEDFIVNSKLKNLAGPTHDLPELVCEEIKFSGRNRLYIGNLTSDVTEEELKELFSPYGEISEAFINAEKNFAFLKIDYRANAERAKKDLDGRMRKNKPIRIRFAPNATTIRVKNLTPFVSNELLFKSFEVFGQVERAVIIVDDRGKTTGEGIVEFARKSGAMSALKYCSEKCYFLTSSLRPCVVETFDHIDETDGFPEKSLMRKSNDYYKARQNGPRFAEMGSFEHEFGTKWKQMYDMYKQKHDALKREMQLEEEKLEAQMEYAKFEHETESLREQLRKREQDRDRQKKEWEDRERQADESRIRDEQQMRRQQDDMQMRMQRQDEEMRRRQQENSLFMQAQQLSNMLDQQEMNHQGGGGGGGNGGNGNNQGGGGNQGGGRRNYNNDRNNDRNQNFDMMNQGGGNHGGNQYQGNQHYQGNQDQGNRFDGPPQRGNVRPWNNNDRGHRDDFQNKRRRY", "text": "FUNCTION: Component of nuclear connecting fibers associated with the transport of ribonucleoprotein particles from either the chromosome to the nuclear pore complex or their transient retention in the nucleoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus."}
+{"protein": "MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKCAISDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFETA", "text": "FUNCTION: Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M38 family."}
+{"protein": "MAAVPPENGVDGDDEREEEEEDEEEEEEEEEEENGDEAEEEPRLKYQRMGGNVPALLSNDAASCIAVAARMIALGTHDGTVRILDLLGNQVKEFRAHTAPVNDINFDTEGEYIGSCSDDGSVVINSLFTDDEKMKFDYHRPMKAISLDPDYTKKQSKRFVAGGLAGHLYMNSKKWFGNKDQVLHSGEGPIHSVKWRGSLIAWANDVGVKVYDTAKDQRVTFIEKPRGSPRPEALLPHLVWQDDTLLVIGWGTSVKIASIKSDQQQTGTFRQIQMSSLTQVDIVASFQTSYYISGIAPFGDSLVILAYIPIEGDGEKEFSSTTTLSRQGNAQRPEIRIVSWNNDELTMDALPVHGFEHYKAKDYSLAHAPFPGSSYAGGQWAAGDEPLYYIVSPKDVVIAKPRDAEDHINWLLQHGFHEKALAAVEASEGRTELIDKVGAGYLDHLIVERKYAEAASLCPKLLRGSASAWERWVFHFAQLRQLPVLVPYMPTDNPRLKDTVYEVALVALATNPSYHKELLSAVKSWPRSVYSALTVISAIEPQLNTSSMTDALKEALAELYVIDGQYQKAFSLYADLLKPEVFDFIEKYSLHEAIRGKVVQLMLLDCKRATVLFIQNRDLIPPSEVVPQLLKAGKNPQVLKAGKKCDSRYYLYLYLHALFEVSHDTGKDFHDMQVELYAEYDTKMLLPFLRSSQHYKLEKAYELCVKKDFLREQVFVLGRMGNAKQALAVIINKLGDIEEAVEFVSMQHDDDLWEELIKQCLNKPEMVGLLLEHTVGNLDPLYIVNMVPNGLEIPRLRDRLVKIVTDYRTETSLRHGCNDILKTDIVNLLVKCFNEARRGVCLSHEDDDSRAKREDNNRSSFSQRMVVDKSLSIKMTEVKSKTRGDTRCCMCFDPVSIRGDTVVVFFCCHAYHETCLMDAAFSNNNHKTTKGSSGYEYSYDNGVDEEEEDEEEDEDGDGDRPGRSRLRCILCTTAAAASAR", "text": "FUNCTION: Required for vacuolar assembly and vacuolar traffic. SIMILARITY: Belongs to the VPS41 family."}
+{"protein": "MGLISYFASFLPDVPWHFWGSVDSLLQGLVGACAVSVLYNLMKVHLYIVCLNDPDKQKEAAQLRAQSPIMDFLHLSLLSLLFSLLGPRVGALVVLEFSLRAVSMVLSANKGAQSSQLFLLCQFSLGCGVSCSLDYLHEGAPHRTWNLLLAVGLSGLILWQSRRMCRHVGILYQLHSGERYCGVCLSLLACWRDIPPFLWRALKVAFWVSDLAAVAVINRDFLSTSEAMRFWTPLTICYTLLVIYMQEEQHQNPSEQMAYQTVFVRMGGLLILMMTVGRWADILHIFISLTGELWCLLHAGVMLRLCREQDFAERMSNPRKYPVSRAPKSTREGRTLQRETSLEE", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM82 family."}
+{"protein": "MSPPAEIQADTLKRFIAGWGGWTMESFFATLSDDFTQKPLPLSCGEPARGREQLYPLLSSLMTMMTNFKLTIHNTIHDPSNKAAVVYAVADGDTPFGPYHNEQAVFIWFNSKGDKVDRIEELFDTAFMAEFKPKFKKWALENPGAAAGRPPPANTST", "text": "FUNCTION: Monooxygenase; part of the ergochrome gene cluster responsible for the typical purple-black color of the ergot sclerotia (Probable). The ergochrome gene cluster produces several ergot pigments including the yellow ergochrome secalonic acid and its derivatives, as well as the red anthraquinones endocrocin and clavorubin (PubMed:28955461). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) CPUR_05437 (By similarity). The atrochrysone carboxyl ACP thioesterase CPUR_05436 then breaks the thioester bond and releases the atrochrysone carboxylic acid from CPUR_05437 (By similarity). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (By similarity). The next step is performed by the anthrone oxygenase CPUR_05434 that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving CPUR_05427, CPUR_05428, CPUR_05429 and CPUR_05430 (By similarity). The short chain dehydrogenase/reductase CPUR_05418 then catalyzes the C-5 ketoreduction to give the xanthone skeleton of the monomeric units (PubMed:32105084). Ergochromes formation requires further dimerization steps of different xanthone units, probably catalyzed by the cytochrome P450 monooxygenase CPUR_05419 (PubMed:28955461). CPUR_05425, CPUR_05426 and CPUR_05431 are unique to Claviceps, thus it is likely that they are involved in further modification of xanthone units or in their dimerization (PubMed:28955461). The yellow ergochromes and the red anthraquinone pigments endocrocin and clavorubin are products from the same PKS derived precursors and the latter are likely shunt products in the pathway of xanthone biosynthesis (PubMed:28955461). It is proposed that atrochrysone carboxylic acid released from the PKS CPUR_05437 can also be converted to endocrocin anthrone which is further oxidized into endocrocin by CPUR_05435 (By similarity). Endocrocin could be then modified to clavorubin, possibly by CPUR_05423 and CPUR_05431 (PubMed:28955461). Clavorubin is the principal anthraquinone metabolite produced by the cluster with a much higher yield compared to endocrocin (PubMed:28955461). SIMILARITY: Belongs to the avfA family."}
+{"protein": "MAAGGPCPAAAGGGPGGASCSVGAPGGVSMFRWLEVLEKEFDKAFVDVDLLLGEIDPDQADITYEGRQKMTSLSSCFAQLCHKAQSVSQINHKLEAQLVDLKSELTETQAEKVVLEKEVHDQLLQLHSIQLQLHAKTGQSVDSGTIKAKLSGPSVEELERELEANKKEKMKEAQLEAEVKLLRKEDEALRGHIAVLQAEVYGARLAAKYLDKELAGRVQQIQLLGRDMKGPAHDKLWNQLEAEIHLHRHKTVIRACRGRNDLKRPMQAPPGHDQDSLKKSQGVGPIRKVLLLKEDHEGLGISITGGKEHGVPILISEIHPGQPADRCGGLHVGDAILAVDGVNLRDTKHKEAVTVLSQQRGEIEFEVVYVAPEVDSDDENVEYEDESGHRYRLYLDELEGGGNPGASCKDPSGEIKVLQGFNKKAVTDTHENGDLGTASETPLDDGASKLDDLHTLYHKKSY", "text": "FUNCTION: Plays a role in intracellular protein trafficking and degradation (By similarity). May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels (By similarity). May also regulate the intracellular trafficking of the ADR1B receptor (By similarity). May play a role in autophagy (By similarity). Together with MARCHF2 mediates the ubiquitination and lysosomal degradation of CFTR (By similarity). Overexpression results in CFTR intracellular retention and degradation in the lysosomes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Synapse Postsynaptic density Cell projection, dendrite Note=Enriched in synaptosomal and postsynaptic densities (PSD) fractions. Expressed in cell bodies and dendrites of Purkinje cells. Localized at the trans-Golgi network (TGN) of spermatids and the medulla of round spermatides (By similarity)."}
+{"protein": "MEVSGPEDDPFLSQLHQVQCPVCQQMMPAAHINSHLDRCLLLHPAGHAEPAAGSHRAGERAKGPSPPGAKRRRLSESSALKQPATPTAAESSEGEGEEGDDGGETESRESYDAPPTPSGARLIPDFPVARSSSPARKGMGKRPAAAAAAGSASPRSWDEAEAQEEEEAGVDGDGDADVDGEDDPGHWDADAADASFGVSAGRAHPRALAAEEIRQMLEGKPLADKMRPDTLQDYIGQSRAVGQETLLRSLLEANEIPSLILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFFKRKTILFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEAMVTILMRAINSLGIHVLDSSRPTDPLSHSSNCSSEPSVFIEDKAVDTLAYLSDGDARTGLNGLQLAVLARLSSRKVFCKKSGQTYSPSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKAMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFASEDIGLADPSALAQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRSHQGPLPPVPLHLRNAPTRLMKDLGYGKGYKYNPMYSEPVDQDYLPEELRGVDFFKQRRC", "text": "FUNCTION: Functions as a modulator of initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. In the presence of ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is decreased. Also plays a role in the innate immune defense against viruses. Stabilizes the RIGI dsRNA interaction and promotes RIGI 'Lys- 63'-linked polyubiquitination. In turn, RIGI transmits the signal through mitochondrial MAVS. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Colocalizes with WRN in granular structures in the nucleus. SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily."}
+{"protein": "MATTAAAAAAALSAAATAKTGRKNHQRHHVLPARGRVGAAAVRCSAVSPVTPPSPAPPATPLRPWGPAEPRKGADILVEALERCGVSDVFAYPGGASMEIHQALTRSPVITNHLFRHEQGEAFAASGYARASGRVGVCVATSGPGATNLVSALADALLDSVPMVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVLDVEDIPRVIQEAFFLASSGRPGPVLVDIPKDIQQQMAVPVWDTSMNLPGYIARLPKPPATELLEQVLRLVGESRRPILYVGGGCSASGDELRWFVELTGIPVTTTLMGLGNFPSDDPLSLRMLGMHGTVYANYAVDKADLLLAFGVRFDDRVTGKIEAFASRAKIVHIDIDPAEIGKNKQPHVSICADVKLALQGLNALLQQSTTKTSSDFSAWHNELDQQKREFPLGYKTFGEEIPPQYAIQVLDELTKGEAIIATGVGQHQMWAAQYYTYKRPRQWLSSAGLGAMGFGLPAAAGASVANPGVTVVDIDGDGSFLMNIQELALIRIENLPVKVMVLNNQHLGMVVQWEDRFYKANRAHTYLGNPECESEIYPDFVTIAKGFNIPAVRVTKKSEVRAAIKKMLETPGPYLLDIIVPHQEHVLPMIPSGGAFKDMILDGDGRTVY", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TPP enzyme family."}
+{"protein": "MGMSWWLACAAAFSALCVLKASSLDTFLAAVYEHAVILPKDTLLPVSHSEALALMNQNLDLLEGAIVSAAKQGAHIIVTPEDGIYGVRFTRDTIYPYLEEIPDPQVNWIPCDNPKRFGSTPVQERLSCLAKNNSIYVVANMGDKKPCNTSDSHCPPDGRFQYNTDVVFDSQGKLVARYHKQNIFMGEDQFNVPMEPEFVTFDTPFGKFGVFTCFDILFHDPAVTLVTEFQVDTILFPTAWMDVLPHLAAIEFHSAWAMGMGVNFLAANLHNPSRRMTGSGIYAPDSPRVFHYDRKTQEGKLLFAQLKSHPIHSPVNWTSYASSVESTPTKTQEFQSIVFFDEFTFVELKGIKGNYTVCQNDLCCHLSYQMSEKRADEVYAFGAFDGLHTVEGQYYLQICILLKCKTTNLRTCGSSVDTAFTRFEMFSLSGTFGTRYVFPEVLLSEVKLAPGEFQVSSDGRLVSLKPTSGPVLTIGLFGRLYGKDWASNASSDFIAHSLIIMLIVTPIIHYLC", "text": "FUNCTION: Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. BTD/VNN family."}
+{"protein": "MSFYSNLPSAGQSSRGSSTSGRNGVGLEPLYPTIFEIMSSQEIDSLLPASIRYLLANHLVANFPNRYTLRLNKYFFEWFQAIKGFVEWYHLKTYNSTFIDRFYGLQLFSSRDRNLALTQCLNPKGQSEWPQGLQLNQQQKSVIFLEKIILPYITAKLDEILEKISMNNIFSSDETENKWPKRAFLRIYPFIKKLLALSNLLVKLLFLTKRTGSVSLLQYLFKIEYTTVRPLSSELSGLKETKGMDNRLRKTNISSIFALMQGQLSIIPRFLTFMGSQFFPTFIFVLRVYQWWTTQDMTTKLQKRVNDLDEDIPRPPFSSHSDKTEDKEGVSEACPVCEKTVQNPCVLETGYVACYPCAISYLVNNEGHCPVTNKKLLGCTYNKHTNKWEVVTGIRKLLI", "text": "FUNCTION: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:9090384, PubMed:19687296, PubMed:22471590, PubMed:11370741, PubMed:35768507). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (PubMed:35768507). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (PubMed:35768507). When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (PubMed:35768507). SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the pex2/pex10/pex12 family."}
+{"protein": "MVIPELFSAGLILLLLFITGFVGMKMKIPDVVIFILLGIAVGGLLSGSHLLHFAGEVGIVLLFFMLGMEFPLKQLMSIAKKVLRAGILDVALSFGVTMAICMMMGLDVITSLIIGGVAYATSSSITAKMLESSKRMANPESEFMLGLLIFEDLVAPILVAVLVGLTAGMALTAGSMSLLVVKVVALVAGAVILGVFLFRKLGSFFDRHMKHDLFILFVIGLALMYGGLALYLDLSEVLGAFLAGIMLAEVKRTHELELMVVRFRDLLLPLFFLYFGTTISFSEGIPMIPLLILVLVWSVIAKVIVGVLGGRWYGLTKKVSLRAGLSLTQRGEFSIIIASLAAGSIKAFSSVFILASAMIGILLFQFAPSIANKFYGKKAKTSVKQHVGSA", "text": "FUNCTION: Ammonium/proton antiporter that mediates the efflux of ammonium ions. Can also transport potassium or rubidium, but not sodium or lithium. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family."}
+{"protein": "MSEMTARFSEIVGNANLLTGDAIPEDYAHDEELTGPPQKPAYAAKPATPEEVAQLLKAASENGVPVTARGSGCGLSGAARPVEGGLLISFDRMNKVLEVDTANQVAVVQPGVALTDLDAATADTGLRYTVYPGELSSSVGGNVGTNAGGMRAVKYGVARHNVLGLQAVLPTGEIIRTGGRMAKVSTGYDLTQLIIGSEGTLALVTEVIVKLHPRLDHNASVLAPFADFDQVMAAVPKILASGLAPDILEYIDNTSMAALISTQNLELGIPDQIRDSCEAYLLVALENRIADRLFEDIQTVGEMLMELGAVDAYVLEGGSARKLIEAREKAFWAAKALGADDIIDTVVPRASMPKFLSTARGLAAAADGAAVGCGHAGDGNVHMAIACKDPEKKKKLMTDIFALAMELGGAISGEHGVGRAKTGYFLELEDPVKISLMRRIKQSFDPAGILNPGVVFGDT", "text": "SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
+{"protein": "MPKRKVAASRGGREEVPKRRSARLSAKPVPDKAEPKAKALAAKDKSENKKAQSKGKKGPKGKQTEETNQEQIKDNLPAENGETKSEETPASDAAVEKEEVKSE", "text": "FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HMGN family."}
+{"protein": "MFPFALLYVLSVSFRKIFILQLVGLVLTYDFTNCDFEKIKAAYLSTISKDLITYMSGTKSTEFNNTVSCSNRPHCLTEIQSLTFNPTAGCASLAKEMFAMKTKAALAIWCPGYSETQINATQAMKKRRKRKVTTNKCLEQVSQLQGLWRRFNRPLLKQQ", "text": "FUNCTION: [Isoform 1]: Cytokine that induces the release of T-cell- attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells. FUNCTION: [Isoform 2]: May act as an antimicrobial peptide in the oral cavity and on the skin. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MTALSRTPVFDAADTAALLDYPALLATLARTVADYAAGEIVSPERLVVPLQAGGVMLSMPSSAHDLAIHKLVNVCPGNAARGLPTILGQVIACDATTGEMRFVLDGPTVTGRRTAAVTALGVQALHGTPREILLIGTGKQAANHAEAFTALFPDARLHVRGSRAASAAEFCAAHRAHAPQLMPLDGDAIPDAIDVVVTLTTSRTPVYRDAAREGRLVVGVGAFTADAAEIAADTVRRSRLVVDDPAGARHEAGDLIVANVDWQQVASLADVLNGTFARGGPMLFKTVGCAAWDLAACRTARDALAAREQR", "text": "FUNCTION: Catalyzes the reduction of Delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, using NADPH as the electron donor. May be involved in a degradation pathway that converts trans-3-hydroxy-L- proline (t3LHyp) to L-proline. SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin family."}
+{"protein": "MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS", "text": "FUNCTION: Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co- chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Cytoplasm Microsome Nucleus Cytoplasm, perinuclear region Mitochondrion Note=Primarily associated with microsomes. A minor proportion is associated with mitochondria (By similarity). Primarily cytoplasmic. A minor proportion is associated with nuclei."}
+{"protein": "MSVEDTQPLITHLIELRKRLLNCIISVIVIFLCLVYFANDIYHLVSAPLIKQLPQGSTMIATDVASPFFTPIKLTFMVSLILSAPVILYQVWAFIAPALYKHERRLVVPLLVSSSLLFYIGMAFAYFVVFPLAFGFLANTAPEGVQVSTDIASYLSFVMALFMAFGVSFEVPVAIVLLCWMGITSPEDLRKKRPYVLVGAFVVGMLLTPPDVFSQTLLAIPMYCLFEIGVFFSRFYVGKGRNREEENDAEAESEKTEE", "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 inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family."}
+{"protein": "MDPEVSLLLLCPLGGLSQEQVAVELSPAHDRRPLPGGDKAITAIWETRQQAQPWIFDAPKFRLHSATLVSSSPEPQLLLHLGLTSYRDFLGTNWSSSASWLRQQGAADWGDKQAYLADPLGVGAALVTADDFLVFLRRSQQVAEAPGLVDVPGGHPEPQALCSGGIPRHKDLPGLLVVRELFSSVLQEICDEVNLPLHTLSQPLLLGIACNETSAGRASAEFYVQCSLTSEEVRSYYLSGGPEAHESTGIIFVETQRVQRLQETEMWAQLCPSAKGAILLYNRHPPLQSGVGKSHLSHPSAPALSLQL", "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": "MRIHYLLFAFLLVLLSPPAAFSKKINNPVSCLRKGGRCWNRCIGNTRQIGSCGVPFLKCCKRK", "text": "FUNCTION: Antimicrobial activity against Gram-negative bacteria E.coli and P.aeruginosa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family. LAP/TAP subfamily."}
+{"protein": "MPITLPATLPAFDVLTHEGVMVMTPERAARQDIRPLRIGLLNLMPKKIQTENQFARLIGATPLQIDFQLIRMTEHQTKNTAAEHMEAFYRPFQEVKHEKFDGLIITGAPIEHLDFADVTYWDELCEVMDWTQTNVQSTFGVCWGGMAMIYHFHRVQKHRLQAKAFGCFRHRNVAPTSPYLRGFSDDFVIPVSRWTEMRQAEIDAAPGLRTLLASDEAGPCLVEDPGHRALYIFNHFEYDSDTLKQEYDRDVANGKPINVPANYYPDDDPSKPPLNRWRSHAHLLYGNWINEIYQSTPYDPQQIGR", "text": "FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. 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": "MPSKKSSSPLSVEKLHRSEPLELNGATLFEGDALSVLRRLPSGSVRCIVTSPPYWGLRDYGIDEQIGLESSMTQFLNRLVTIFSEAKRVLTDDGTLWVNIGDGYTSGNRGYRAPDKKNPARAMAVRPDTPEGLKPKDLIGIPWRLAFALQEDGWYLRSDIVWNKPNAMPESVKDRPTRSHEFLFMLTKSEKYYYDWEAVREEKDSGGFRNRRTVWNVNTKPFAGAHFATFPTELIRPCILASTKPGDYVLDPFFGSGTVGVVCQQEDRQYVGIELNPEYVDIAVNRLQGEDTNVIRIAAA", "text": "FUNCTION: A beta subtype methylase, recognizes the double-stranded sequence 5'-CCCGGG-3', methylates C-2 on both strands, and protects the DNA from cleavage by the Cfr9I endonuclease. SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4) subfamily."}
+{"protein": "MGCVQCKDKEAAKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL", "text": "FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta- catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane Perikaryon Note=Present and active in lipid rafts (By similarity). Palmitoylation is crucial for proper trafficking (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily."}
+{"protein": "MSSGGLLLLLGLLTLWAELTPISGQDRPKFCNLAPESGRCRGHLRRIYYNPDSNKCEVFFYGGCGGNDNNFETRKKCRQTCGAPRKGRPT", "text": "FUNCTION: Serine protease inhibitor that inhibits trypsin. FUNCTION: Serine protease inhibitor. Inhibits activated protein C (APC) with an IC(50) of 3.5 nM in the presence of heparin (to which it strongly binds) and an IC(50) of 88.9 nM in its absence. Other targets are also significantly inhibited in presence of heparin: trypsin (PRSS1) (45%), coagulation FXIa (F11) (40%), and plasmin (PLG) (70%). In vivo, synergizes with RVV-X in promoting coagulation in mice and by extension in Russell's viper bite patients. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family."}
+{"protein": "RDPTGCEVDQVIMVKRHGERYPSPSAGK", "text": "FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from phytate. SIMILARITY: Belongs to the histidine acid phosphatase family."}
+{"protein": "AECKVDVDSTDQMSFNTKEITIDKSCKTFTVNLTHSGSLPKNVMGHNWVLSKSADMAGIATDGMAAGIDKDYLKPGDSRVIAHTKIIGSGEKDSVTFDVSKLTAGESYEFFCSFPGHNSMMKGAVVLK", "text": "FUNCTION: Transfers electrons from cytochrome c551 to cytochrome oxidase. SUBCELLULAR LOCATION: Periplasm."}
+{"protein": "METPDTTENYDMITEFDYGDATPCHKVNERAILAQLLPPLYSLVFVIGVVGNLLVVLVLVQYKRLKNMTNIYLLNLAISDLLFLFTLPFLIYYKSTDDWIFGDAMCKILSGFYYTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIIIWALAILASSPLMYFSKTQWNIVRHSCNLHFPYESFQQWKLFQALKLNLFGLVLPLLVMIVCYTGIIKILLRRPNEKKSKAVRLIFVIMIIFFLFWTPYNLTELISVFQEFLFTHLCEQNRQLDLAMEVTEVIANMHCCVNPVIYAFAGERFRKYLRQLFHRRVAVHLVKWLPFLSGDRLERVSSTSPSTGEHELSAGL", "text": "FUNCTION: Receptor for a C-C type chemokine. Binds to MIP-1-alpha, RANTES, MCP-3 and, less efficiently, to MIP-1-beta or MCP-1 and subsequently transduces a signal by increasing the intracellular calcium ions level. Responsible for affecting stem cell proliferation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MALLKVKFNQKKRVKLAQGLWLMNWFSVFAGIIVFSMGLFLKIELRKRSEVMDNSESHFVPNSLILMGILSCAFNGFAGKICYDSLDPAKFAKWKPLLKPYLALCFFFNILLFFVALICFLMRGSLESTLAQGLKNSMKFYRDTDTPGRCFMKKTIDMLQIEFKCCGNNGFKDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRYLVDGVPFSCCNPSSPRPCIQYQVTNNSAHYSYDYQTEELNLWGRGCREALLHYYSSMMSSMGAVVLLVWLFEMSVMVGLRLLHTSLESIANPEDPECESEGWILENSLKDTLKSALESLKKIGKFNQVEAGAEGAEGEEAGKTPAITTVS", "text": "FUNCTION: May be involved in the morphogenesis of retina outer segment disks and the development and maintenance of the retina ultrastructure. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the PRPH2/ROM1 family."}
+{"protein": "MAKVAILGAGNLALTLAGDLARRLGQTPSIWAPISNRSSFNDVRCLGSLELVGPDYGGDFQPRLEDDLGTAISGAAFIFLTVPTLGQQGILRELAKFNLSNSVLVALPGSATSLACKQTLVPTFAPIAVIESTTSPYACRRVKARVLMLGVKATFEVATTQPLSEEVKGRFEVLFPNPPQWYQHPASIFFSNTNPVAHPAGILAARDSIEQGILPVPKFYRQFVPQAITRVIAIDEERLSIVDALGLESETDFSYSKKWYGGHACNAREFYETYEGYAEIETPKTMNHRYLTEDVKHILVLWVEIAEAIGVQVPEMKSVVQEASDVLNENLLRTGRGLSSLNLGGANANAIVRALNGV", "text": "FUNCTION: Reductive condensation of pyruvate and arginine, lysine, histidine, or octopine to form octopine, lysopine, histopine, or octopinic acid, respectively. NADPH is the preferred cofactor, but NADH can also be used. SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine dehydrogenases family."}
+{"protein": "MSSGGLLLLLGLLTLWGVLTPVSSKDRPKKPGLCPPRPQKPCVKECKNDWSCSGQQKCCNYGCIDECRDPIFVN", "text": "FUNCTION: Damages membranes of susceptible bacteria. Has no hemolytic activity. Not toxic to mice. Does not inhibit the proteinases elastase and cathepsin G. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom waprin family."}
+{"protein": "MADSGPASFWTRANAILRKNLTYQKRNIWSNVRLIMIPFYLCIVLVFIQALFDSQVNNSLDNQCGCQCIDKLGDGKCQMTCGLEYSTRDQGFFCAIPKPQPWPPLILIPRPEYRALDANFTNDSCRRKNSCPVTILFTGNNHSLGAVLSRNLLRRPFAMNSSDLLFSLANNVLATTFKGSATNYLDAGIVSDGSIYNIQPRCPPNSNFSISIGQSPLNFTKDMRCVQGLNLWRNNSIEVNLELFEGYHKGNSDGMINEIVAAYDLFDTNMTNFNVNIWFNATYKDEARNQPYKVVRVPRLVNWVSNAYLQYLQGPRTKMLFEFVKEMPKPETKLRLDIASLIGPIFFTWVILLLLPVILNSLVYEKQQRLRIIMKMHGLGDGPYWIISYAYFLALSTFYIIFLMIFGSVIGLKFFLLNDFSLQFSFYFVYINLQISIAFLLSSAFSKVETASVAAYLYVFGSGLLGMFLFQFLLEGLSFPRRWIFVMELYPGFSLYRGLYEFSQNAYQGNLNGKDGMKWKYFSDNAIDEVFYIIIVEWFVALIATYYIDKMSSSGKDLLFFLKNQNPFKISHSLQKQVSAISVEMEKLDVIHESEKVAQLMLESSTSHAIVCDKLRKVYPGRDGNPPKKAVRVLSLAVPSGECFGMLGPNGAGKTSFINMMTGLVKPTSGAAFVQGLDICKDMDRVYTSMGVCPQHDLLWETLTGREHLLFYGRLKNLKGVDLNQAVEESLRSVNLFHGGVADKPAGKYSGGMKRRLSVAISLIGNPKVVYMDEPSTGLDPASRKNLWTVIKNAKRHTAIILTTHSMEEAEFLCDRLGIFVDGRLQCIGNPKELKGRYGGSYVLTMTTSSEHEKDVEMLVQEVSPNVKKIYHIAGTQKFEIPKDEVRISEVFQVVEKAKSNFKVFAWGLADTTLEDVFIKVARTAQAFNVFS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family. CPR flippase (TC 3.A.1.211) subfamily."}
+{"protein": "MPIINKTMLITYADSLGKNLKELNENIENYFGDAVGGVHLLPFFPSTGDRGFAPIDYHEVDSAFGDWDDVKCLGEKYYLMFDFMINHISRQSKYYKDYQEKHEASAYKDLFLNWDKFWPKNRPTQEDVDLIYKRKDRAPKQEIQFADGSVEHLWNTFGEEQIDLDVTKEVTMDFIRSTIENLAANGCDLIRLDAFAYAVKKLDTNDFFVEPEIWTLLDKVRDIAAVSGAEILPEIHEHYTIQFKIADHDYYVYDFALPMVTLYSLYSSKVDRLAKWLKMSPMKQFTTLDTHDGIGVVDVKDILTDEEITYTSNELYKVGANVNRKYSTAEYNNLDIYQINSTYYSALGDDDQKYFLARLIQAFAPGIPQVYYVGFLAGKNDLELLESTKEGRNINRHYYSSEEIAKEVKRPVVKALLNLFTYRNQSAAFDLDGRIEVETPNEATIVIERQNKDGSHIAKAEINLQDMTYRVTENDQTISFE", "text": "FUNCTION: Intracellular catabolism of sucrose (PubMed:2971020). Being intracellular, probably not involved in synthesis of extracellular polysaccharides (Probable). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose phosphorylase subfamily."}
+{"protein": "MATVHYSRRPGTPPVTLTSSPSMDDVATPIPYLPTYAEAVADAPPPYRSRESLVFSPPLFPHVENGTTQQSYDCLDCAYDGIHRLQLAFLRIRKCCVPAFLILFGILTLTAVVVAIVAVFPEEPPNSTT", "text": "SUBCELLULAR LOCATION: Host Golgi apparatus membrane; Single-pass membrane protein. SIMILARITY: Belongs to the varicellovirus ORF0 protein family."}
+{"protein": "MREFTPTTLSEEERQELLGQLRRKEGRWLAWARACQTLLKNGLNPQTLFEATGFEPIQQNQITVAMQVYDSILRQDPPAHVRETYQEWGSDLLYELRELDQEQRSLCAQLALERKLDADQIREVAKATKDFCRLPKQPENFDRHPGDAVAHQCWRLAQERTDLTERSRLIARGLQFAQSAGARALIEALLLDLSGVPSRKPPMLPIYRLETEEDLPRLLPFAGTLPLSSSQIEAIAAVEAEGPFGLVSSPQGQQWLALPGWQAILTAEDPIACLEQIDRLPNAPEGPTEAVVLVVDRADRDWDADHFFLVEQAEGARIQWSPSAIAAPILGRLVLILRPKRVLDEAAIATPWQFEE", "text": "FUNCTION: A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL). Cooperates with RbcX in RbcL folding, plays the major role in assembly of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces Raf1, leading to holoenzyme formation. FUNCTION: It has been suggested that Raf1 and RbcX are partially functionally redundant (Probable). Other evidence suggests they are antagonistic in mediating RuBisCO assembly (PubMed:32636267). FUNCTION: The Raf1 dimer brackets an RbcL dimer, leading to RbcL(8)- Raf1(8) complex formation. RbcS displaces Raf1, resulting in holoenzyme formation (PubMed:26237510, PubMed:32636267). Probably plays a role in early carboxysome assembly; in its absence CcaA, CcmM, CcmN, RbcL and RbcS colocalize in small patches while the shell proteins CcmK2, CcmK3 and CcmK4 are found diffused in the cytoplasm (PubMed:32636267). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RAF family."}
+{"protein": "MMIHGFQSSHQDFSFGPWKLTASKTHIMKSADVEKLADELHMPSLPEMMFGDNVLRIQHGSGFGIEFNATDALRCVNNYQGMLKVACAEEWQESRTEGEHSKEVIKPYDWTYTTDYKGTLLGESLKLKVVPTTDHIDTEKLKAREQIKFFEEVLLFEDELHDHGVSSLSVKIRVMPSSFFLLLRFFLRIDGVLIRMNDTRLYHEADKTYMLREYTSRESKIANLMHVPPSLFTEPNEISQYLPIKEAVCEKLVFPERIDPNPVDSESAPSE", "text": "FUNCTION: May be a allosteric regulator of serine/threonine-protein phosphatase 2A (PP2A). Inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase activity. Acts as negative regulator of serine/threonine-protein phosphatase 4 probably by inhibiting the formation of the active PPP4C:PPP4R2 complex; the function is proposed to implicate it in DNA damage response by promoting H2AX phosphorylated on Ser-140 (gamma- H2AX). May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TIP41 family."}
+{"protein": "MNDLKSKSNIKLMKRVLTTYELRKYLKKYFCLTLDNYLVLAYLDVFKNDEGKYFMRDIISYIGIDQSRIVKSVKELSKKGYLNKCRDPHDSRNVIIVVSVKQHNYIKNLLSEININET", "text": "FUNCTION: Transcriptional regulator acting as an intermediary between major regulators SarA and agr and virulence genes. Represses alpha- hemolysin (hla) gene expression (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SarA family."}
+{"protein": "MIFPIRCFSCGNVISEVYEEYRTRLKNGENPEEILNDLEIKKYCCRRMFASHRLDNDRELFDDIVEYK", "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 Rpo10/eukaryotic RPB10 RNA polymerase subunit family."}
+{"protein": "MNFKYIIAVSFLIASAYARSEEYDIQSLSQRDVLEEESLRKIRGIGSAILSAGKSIIKGLAKGLAEHFGKRTAEDHEVMKRLEAAMRDLDSLDYPEEASERETRGFNQEEKEKRIIGPVLGLVGKALGGLLG", "text": "FUNCTION: [Bombinin H-BO1]: Has no antimicrobial activity at concentrations up to 161 uM. Has moderate hemolytic activity towards human erythrocytes at a concentration of 40.3 uM. FUNCTION: [Bombinin-BO1]: Has antimicrobial activity against Gram- negative bacterium E.coli (MIC=26.3 uM), Gram-positive bacterium S.aureus (MIC=26.3 uM) and yeast C.albicans (MIC=52.5 uM). Has moderate hemolytic activity towards human erythrocytes at a concentration of 52.2 uM. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
+{"protein": "MGLMTRIADKTGALGSVVSAMGCAACFPALASFGAAIGLGFLSQYEGLFISRLLPLFAALAFLANALGWFSHRQWLRSLLGMIGPAIVFAATVWLLGNWWTANLMYVGLALMIGVSIWDFVSPAHRRCGPDGCELPAKRL", "text": "FUNCTION: Involved in mercuric ion uptake and binding. MerC-mediated Hg(2+) uptake does not require MerP. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "MRNNIAGPPITPVQATVKVTRVRQMDPTDLMSMKILLNILLRRTFESSLGMLNIRSGFYDLRNPSIHAIQIDGRGYDICWIPGFRLTTATLRGKLGLQILPETTKVRSKSMNELLTERRGNIHPSALAVITVMAMHNGKVFRVHSIVQGQTIVSPLANGNETDYFTYYSTRYRDKIDSAGLSLLRHNDYCNSVMQQDKFILKLTPLKRTQNGKVVRPCNVPSSLCIIISDNEIAPYGVSKLSTNRAAVALSTMSPDALLEKATAFAARLAEDTELQSLLGDYGFGFTSNPLELETFVCKPPKLMMDNTSRIVTIEDDSGGVFHNLLQSPGVSPIYYSNNNQPATGMPVWAIMVPRNLGNDYARRLRKELTERVRSLAGTTAPNIGDPPLIAVELSNQRREMYRVEPYKDAFKALLNKLRLEYKDARESEIVAKIQLVVIVIPGPKQDRGDLYKGIKQFYTHMGIVTQCLLAPKSSQNELQWYDQAVLRSVCQQIYAKAGGAVWAPVLPPQNVYSKSTMLCALDISRPKKTVGRPAEVPISTAGFISTYDGSFEYIYSQKKTLVPNRLNHGGELQQQTLMEAFIKNSCNVYLAFNNRILPDHIVIFRDGVSDSQISATLEVEIKSLYECLRQIYHKSNRPMCDLKVIVAQKTCAMRFSAVGGTVLRSGYYVINRSPDNRQQGSEFLMASQAIVHGTTPKPIRYKIIFDSMEASVDNDSFNQLIELTNAMAYGYVNWPQAISLPHVLHMAHHLSKFCGEVLRNGDDLFESCAIFGLQYRPFFI", "text": "FUNCTION: Plays an essential role in growth and, with Dicer, also involved in microRNA (miRNA)-mediated translational repression. The RNA interference pathway is implicated in antigenic variation having a role in regulation of variant-specific surface protein (VSP)-coding gene expression. Several VSP genes are transcribed but only transcripts encoding the VSP to be expressed accumulate. Antisense RNAs corresponding to the silenced VSP genes are detected. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argonaute family. Ago subfamily."}
+{"protein": "MGLPQNKLSFFCFFFLVSVLTLAPLAFSEIFLEEHFEGGWKSRWVLSDWKRNEGKAGTFKHTAGKWPGDPDNKGIQTYNDAKHYAISAKIPEFSNKNRTLVVQYSVKIEQDIECGGAYIKLLSGYVNQKQFGGDTPYSLMFGPDICGTQTKKLHVIVSYQGQNYPIKKDLQCETDKLNHFYTFILRPDASYSVLVDNKEREFGSMYTDWDILPPRKIKVKNAKKPEDWDDREYIDDPNDVKPEGFDSIPREIPDRKAKEPEDWDEEENGLWEPPKIPNSAYKGPWKAKRIKNPNYKGKWKNPWIDNPEFEDDPDLYVLKSIKYAGIEVWQVKAGSIFDNILICDDPAYARSIVDDYFAQHRESEKELFAEAEKERKAREDEEARIAREEGERRRKERDHRYGDRRRRYKRPNPRDYMDDYHDEL", "text": "FUNCTION: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the calreticulin family."}
+{"protein": "MKIVEVKNLTYRINDFEILKNVTFSVEEGEFVGIIGPNGAGKTTLVRILVGDIKNYEGKVEVRGKIGYLPQLHQVQREFPITVKEFAAMGMYGRYRKIDWEKVRSTLKDVGILHKENDPIKNLSGGEFQRLSLARALLSDPDILVLDEPEAGVDEMGKASFYELLNRLRKEKNITVIMVSHDIGMVFKECSTIMCLNRTLHCHGPTETINPEDLKKIFTDFDIWIRGTRHYEIYHGRERD", "text": "FUNCTION: Part of an ATP-driven transport system TM_0123/TM_0124/TM_0125 for a metal. Probably responsible for energy coupling to the transport system. SIMILARITY: Belongs to the ABC transporter superfamily."}
+{"protein": "MTISILGARVIDPKTGLDQVTDLHLDGGRIAAIGAAPAGFSASRTIQADGVVAAPGLVDLGVSLREPGYSRKGNIRSETRAAVAGGVTSLCCPPQTRPVLDTLAVAELILDRAREAANSKVYPIGALTKGLEGEQLAELVALRDTGCVAFGNGLKQIPNNRTLARALEYAATFDLTVVFHSQDRDLAEGGLAHEGAMASFLGLPGIPESAETVALARNLLLVEQSGVRAHFSQITSARGAQLIAQAQELGLPVTADVALYQLILTDESVRQFSSLYHVQPPLRTAKDRDGLRAAVKSGVIQAISSHHQPHERDAKLAPFGATEPGISSVELLLPLAMTLVQDGLLDLPTLLARLSSGPAAALRVPAGELKVGGAADLVLFDPQASTVAGEQWSSRGENCPFIGHCLPGAVRYTLVDGHVCHGPE", "text": "FUNCTION: Non-functional DHOase. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. PyrC' subfamily."}
+{"protein": "MVGFKATEVPPTATVKFLGAGTAACIADLITFPLDTAKVRLQIQGERRGPVQAAASAQYRGVLGTILTMVRNEGPRSLYNGLVAGLQRQMSFASVRIGLYDSVKHFYTKGSEHAGIGSRLLAGSTTGALAVAVAQPTDVVKVRFQAQARAGGGRRYRSTVDAYKTIAREEGLRGLWKGTSPNVARNAIVNCAELVTYDLIKDTLLKADLMTDDLPCHFTSAFGAGFCTTVIASPVDVVKTRYMNSAPGQYSSAGHCALTMLQKEGPRAFYKGFTPSFLRLGSWNVVMFVTYEQLKRALMAARASREAPF", "text": "FUNCTION: Antiporter that exports dicarboxylate intermediates of the Krebs cycle in exchange for phosphate plus a proton across the inner membrane of mitochondria, a process driven by mitochondrial motive force with an overall impact on glycolysis, glutaminolysis and glutathione-dependent redox balance. Continuous export of oxaloacetate and related four-carbon dicarboxylates from mitochondrial matrix into the cytosol negatively regulates the oxidation of acetyl-CoA substrates via the Krebs cycle lowering the ATP/ADP ratio and reactive oxygen species (ROS) production (By similarity). Proton transporter activity is debated, but if it occurs it may mediate inducible proton re-entry into the mitochondrial matrix affecting ATP turnover as a protection mechanism against oxidative stress. Proton re-entry may be coupled to metabolite transport to allow for proton flux switching and optimal ATP turnover (By similarity). Regulates the use of glucose as a source of energy. Required for glucose-induced DRP1-dependent mitochondrial fission and neuron activation in the ventromedial nucleus of the hypothalamus (VMH). This mitochondrial adaptation mechanism modulates the VMH pool of glucose-excited neurons with an impact on systemic glucose homeostasis. Regulates ROS levels and metabolic reprogramming of macrophages during the resolution phase of inflammation. Attenuates ROS production in response to IL33 to preserve the integrity of the Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity). Can unidirectionally transport anions including L-malate, L-aspartate and phosphate (By similarity). Does not mediate adaptive thermogenesis (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MNPYETEIYKVVPIPNKGMGMIAKVKIPVGTRIFAETPLIRTKSDAKEIEEALSTKTKEEQEAFHRLFNAHPDTMGPFLGPFYSNALTIDETKGGMFLLGSRMNHDCSPNVKHTWNPRLDQVTVHAVRDIEAGEEILTTYIDLHKSHTERQKILLEHFGFKCYCSVCSVEERKIRKISDLRRKQLAYYDRTMAKMCIVNPRGALRALRHRIHIAHEELLFGRLDIIALLDAFRLCVIHGDFERASIFAKKGTKAISLYEGTDSEKYLKISKYVENPRSHALAEGVPALPLFLEEDDELSDLEDNLWGCKLEEDVYSDTD", "text": "SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
+{"protein": "MADKKLVVVFGATGAQGGSVARTLLEDGTFRVRVVTRDPGQRAAKQLRLQGAEVVQGDQDDEASMELALSGAHATFIVTNYWENCSQEQEVKQGKLLADLAKRLGLRYVVYSGLENIKKLTAGRLTVGHFDGKGEVEEYFRDIGVPMTSVRLPCYFENLLSYFLPQKAPDGRSYLLSLPMGDVPIDGMSVADLGPVVLSLLKTPEEYVGRNIGLSTCRHTVEEYAALLTKHTGKAVRDAKTSPEDYEKLGFPGAQDLANMFRFYALKPDRNIELTLKLNPKARRLDQWLEQHKEDFAGL", "text": "FUNCTION: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios (By similarity). SIMILARITY: Belongs to the NmrA-type oxidoreductase family."}
+{"protein": "MASCPDSDNSWVLAGSETLPVETLGPESRVDPESEEAPQALQDSSKADGKESAGTLNGEEMLFQTESSQGEGAALPEESEAKGALGGDDGHGTKRPGDTAVQEDLQETPMVTSLGPDTQDLERNIHPQNLPSSPRAVWKEHGCSSSDDDTDVDVEGLRRRRGREPSPPQPTAAVDGEDQAKGEGIGELGISLNMCFLGALVLLGLGILLFSGALLEPETEPVEEAELQVFPETELVQTVGNRQDEVEQLQASVPPDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRGVDGVCLNWGGSPQGGKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQWQLLGSVHRNLQRGLQDAGQGAPAHAGLAELGHMLAQTLQGLESQGINTGRSSNDSEAWHQKKPRFQHPREWSGREKWRGGQRDQKAEHWKLKKEESGQDRKKSWRDEGREFTGHWKENRPRAEESGSRKDSKRQDPKVHPRKSGNSHSGERQKHSWGKDNSPDSVSWEELLRRKYRPPQGCSGVADCARQEGLALFGVELAPVRQQELASVLREYLARLPWAGQLTKELPLSPAYFGEDGIFRHDRLRFRDFVDALEDSLEEVALKQTGDDDEVDDFEDFIFSHFFGDKALKRRSKKKEKQPWNHRAVGPREEHSRHPHHYHQG", "text": "FUNCTION: Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor- alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus Note=Shuttles between the nucleus and the cytosol. Mainly localized in the cytoplasm, associated with microtubules. Detected in small amounts in the nucleus."}
+{"protein": "MGKPPGARNPAEAEADGDDAVFLELSRELKEEGTRLFNRRDFEGAAFKYDKAVQLLPAGRRVEAAHLRASIAHCYMRMSPAEFHHAIHECNLALEAVPRYSRALLRRAACFEALGRPDLAWGDIRTVLRWEPGNRAARQISDRVRTALEDKGISVALDVLPEDENEIASAKGEERKKSRNKRFDSVAGGREGENGIALLESASTEKQAGPRQTNGTGNHQDHTEDSESNGLEKLEQSTETGEKDMGKKRGAHAAGKKPRCGESKQQKHSAVNHCQDNIGAKEEVMKDVKLVFGEDIRCAQMPANCSLPQLREIVQNKFPSLKAFLIKYKDKEEDLVTITLSEELSWASNLAVSQVPIRFYVVEVNHVQELGVDGVRRRPSFATLERNRDIMLDNGTIGHDVEHKHYADDWMVQFAQIFKNHVGFSSDAYLDLHDLGLRLHYEAMEDTIQREEAQEIFEVAESKFKEMAALALFNCGNVHMSRARRRPCLAEDPLQEFILEKVNVSYDWACTEYAKAGAMFEEAVKTKSDFFEGLIALGQQKFEQAKLSWYYALACKINMETEVLELFNHAEDNMEKGMDMWERMETLRLKGLSKPSKEKVVLEKMVLEGFVKDISADEAFEQASSIRSHINILWGTILYERSVVEFNLGLPSWEESLTVAMEKFKIGGASQADINVIVKNHCANETTQEGLSFKVEEIVQAWSEMHDAKNWRSGPLYFRLQPVFRRRAPKLHHILEHMHYA", "text": "FUNCTION: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain."}
+{"protein": "MSGGDGIPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGQIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTARVTYKNVPNWHRDLARVCENIPIVLCGNKVDVKDRKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLLGDPNLEFVAMPALAPPEVQMDPAMIAEYEKDLDNAAKADLPDDDDDL", "text": "FUNCTION: Ran GTPase system comprises ran-1, ran-2 and ran-3 and is essential in nucleocytoplasmic transport. Ran-1 is a GTP-binding protein that mediates the interaction between mitotic chromosomes and kinetochore microtubules. Plays a crucial role in nuclear envelope assembly at the end of each cell division. Required for the import of protein into the nucleus and also for RNA export. RCC1 (ran-3)/Ran (ran-1) complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Chromosome Note=At interphase, ran-1 is localized to the nucleus and the nuclear envelope. At prometaphase, ran-1 is still localized to the nuclear envelope. When the nuclear envelope begins to disassemble at M phase (early metaphase), ran-1 is localized throughout the entire cell. At late metaphase, ran-1 localizes to the kinetochore regions, this persists until anaphase. At telophase, ran-1 is localized around the decondensing chromosomes. SIMILARITY: Belongs to the small GTPase superfamily. Ran family."}
+{"protein": "MTLTNLDAIVVGAGFSGILAVYRLRKLGFRVQGFERQERLGGVWRENAYPGAAVDSLFPFYQFYDAELLQDWEWGEQFPTRAEMLRYFDHVDKRWEISASFEFGVSVSAARYSETTQRWTVTLEDGRRAEARWFIPAVGFSSVLNIPRIPGMSRFRGAIYHTAKWPHDAVSMRGKRVAVIGTGPSGVQIIQSVGKIAKAMTIFQQSPCLTLRKYGSPNQTATALCMRPDDHREALRLGLQTSNGFGYVPRDQDTLDVPIEERNHFYQQRYLAGGWAFWMAGFRDLCQNIQANRDAYDFWARRTRARIGDVTKRELLVPQIPSFAFGIKRPCLEEDLYEIMDQPHVKIIDISNQQIELITETSIRVHGQTVECEAIIFATGFGDEASGLRSLHIRGRNGIRLEDAWSDGVESHLGMAIHSFPNMFFLYGPQCPTLLVNSPAVITVQVEWLCEIISKCQQAGICQLEATSKSHCQWEKKMSLLWDKTLYHTHARKSKKTAEANKEEKTWVGGLILYRRELENCLANNLEGFQAWYVEETALL", "text": "FUNCTION: FAD-binding 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). SIMILARITY: Belongs to the FAD-binding monooxygenase family."}
+{"protein": "MSVALFCGPPPAVSFGCKDGRGRKGMVRSKDIVRQTVKPPAHACRLIGWNKYPGSVVPTNSSLSPSPTALDDEIELDLSPFLIIYKDGRIERLKGTTVIPACPEVATKDVIIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKSGLLIVSVNYRLAPEHPIPASFDDCMAGFNWVVSHSAGPAPEPWLARHGDLTQILISGDSAGGTVTHYVLLRADAGVIEGAALVHPYFLGSKRLENQTEEDFEFHEKLWRLSTPDTEGLDDPLINPLAPGAPSLAGLKCKRAVVFVAELDFLVERGRMYYDALVKSGWGGEAELVHQKGVGHVFHLSDYSGDVSVDMMAKMVAFLRGE", "text": "FUNCTION: Lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide A > 6-tuliposide B. SUBCELLULAR LOCATION: Plastid, amyloplast. SIMILARITY: Belongs to the AB hydrolase superfamily."}
+{"protein": "MAQLYYKKVNYSPYRDRIPLQIVRAETELSAEEKAFLNAVEKGDYATVKQALQEAEIYYNVNINCMDPLGRSALLIAIENENLEIMELLLNHSVYVGDALLYAIRKEVVGAVELLLSYRKPSGEKQVPTLMMDTQFSEFTPDITPIMLAAHTNNYEIIKLLVQKRVTIPRPHQIRCNCVECVSSSEVDSLRHSRSRLNIYKALASPSLIALSSEDPILTAFRLGWELKELSKVENEFKAEYEELSQQCKLFAKDLLDQARSSRELEIILNHRDDHSEELDPQKYHDLAKLKVAIKYHQKEFVAQPNCQQLLATLWYDGFPGWRRKHWVVKLLTCMTIGFLFPMLSIAYLISPRSNLGLFIKKPFIKFICHTASYLTFLFMLLLASQHIVRTDLHVQGPPPTVVEWMILPWVLGFIWGEIKEMWDGGFTEYIHDWWNLMDFAMNSLYLATISLKIVAYVKYNGSRPREEWEMWHPTLIAEALFAISNILSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYETRAIDEPNNCKGIRCEKQNNAFSTLFETLQSLFWSVFGLLNLYVTNVKARHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFDEGGTLPPPFNIIPSPKSFLYLGNWFNNTFCPKRDPDGRRRRHNLRSFTERHADSLIQNQHYQEVIRNLVKRYVAAMIRNSKTNEGLTEENFKELKQDISSFRYEVLDLLGNRKQPRRSLSTSSTELSQRDDTNDGSGGARAKSKSVSFNLGCKKKACHGPPLIRTMPRASGAQGKSKAESSSKRSFMGPSLKKLGLLFSKFNGHMSEPSSEPMYTISDGIVQQHYMWQDIRYSQMEKGKAEACSQSEINLSEVELGEVRGAAQSSECPLTCSSSLHCASSICSSNSKLLDSSEDVFETWGEACDLLMHKWGDGQEEQVTTRL", "text": "FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G- protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion (By similarity). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with PLSCR1 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC subfamily. TRPC5 sub-subfamily."}
+{"protein": "TKKDGEEKVA", "text": "FUNCTION: Strongly inhibits trypsin and plasma enzyme(s) activity. SIMILARITY: Belongs to the serpin family."}
+{"protein": "MVCIPCIVIPVLLWIFKKFLEPYIYPVVSRIWPKKAVQQSGDKNMSKVDCKGAGTNGLPTKGPTEVSDKKKD", "text": "FUNCTION: May activate the NF-kappa-B signaling pathway. SUBCELLULAR LOCATION: Endoplasmic reticulum Lipid droplet. SIMILARITY: Belongs to the UPF0729 family."}
+{"protein": "MAFSPNVLLGGRVCAAVARSGFATRRVTIPGSTSREPDPDFDWEPEERELQEVESALKRQKKAIRFQKIRRQMEASGAPPRTLTWEAMEQIRYLHREFSESWSVPRLAEGFDVSTDVIRRVLKSKFIPTLEQKLKQDQKVLKKIGLARSIPELPGPGDSSKPLSAGQSVSGSLLIPGDEASSRGHGHSTALKAIELNTQSTNITTRQTERNKGVQGLEEGKDFVPVAAGHPTSTCRGARGIDSDGLPSDKRLEELKAGEAGDQIFSKRVVQRGREFFDSNGNFLYRI", "text": "FUNCTION: Plays an essential role in mitochondrial ribosome biogenesis. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation of core subunits of the oxidative phosphorylation system. SUBCELLULAR LOCATION: Nucleus Secreted Mitochondrion membrane. SIMILARITY: Belongs to the neugrin family."}
+{"protein": "MKNKLINLRSKHIYKLIIIIFFCIILKYYKWCDFKNKVFFIQLVYSFAKKSVCTSSLDDSTCHTVTFGELDVSNNSVVRLKVMRKGGKGYFLTIRRDYVTVSYYLKYVKDIPLEFREIIDIFNNHKFEQYTQEQINKYTYTCNVRKIEDIDKYDEKNPTKFHEYTRGEACRCQTYNYFKDDEFIKRAKLKCIYYNMLFTESATVYSRHCPIIDLMHFAVYDIEYPPIFNTIVNITIEEYYYNDVSSVLNNKSDLVTKEKKYQLNDTITEIRDDYFDLWLFLKGETHGKRTLVNLSNDYIVIPSSPINNRDVIASDITRNCGLSQNSPLLKGCNYSSICNIMHPCLRKAMMLPKYMFDLSGKTCGKLGVSLNTWRKSEGNFCGSEAGYCISNNLKKYYDIHNSASIKDGISLSKYKIKNIYNSEPQTKIYESYKLPDYLKDKIKNNNHAEMDENDLDNKIFYKPNVAAHSQFIDYKYNGNHSVEIKFETDAIEVYEIRPVSIATITHVTIPNDCASNNSNSNECVLIIHVWNNSKFVGSNFSCSIACTNKETDQLASHINPIAPVRAFIGPNKNYAFYFIIKFLINKEITTLCKAIVKDSNGKECSIEEFELQSKESVHIVESEVDETTDQVVVEHHTQSPDIKNPDEYVCKCTINLLCYVINFKTCSNYYINTVKTLIGKFAIIAILIILAPALIPLLPFFLNFFFLFISTILKLYQSIISTIGQIRIRNNDKPIIYKKKIHDMKTNYLSVSSYSSLSDSSSIYSTDSVSSMRKNKKKFNKNNISSNIKHKKGGKKVKQKEPNRNSNHTSHEYADTSPSGKSKIPPLR", "text": "FUNCTION: During fertilization, required on male gametes for their fusion with female gametes, and for subsequent ookinete formation in the host (PubMed:18403203, PubMed:18367645, PubMed:21209845, PubMed:29212032). Thereby, required for mosquito-mediated transmission to other animals (PubMed:18403203, PubMed:18367645, PubMed:29212032). Probably initiates the fusion of gamete cell membranes by inserting part of its extracellular domain into the cell membrane of a female gamete (PubMed:20080406). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the HAP2/GCS1 family."}
+{"protein": "MGDKPPGFRGSRDWIGCVEASLCLAHFGGPQGRLCHVPRGVGLHGELERLYSHFAGGGGPVMVGGDADARSKALLGVCVGSGTEAYVLVLDPHYWGTPKSPSELQAAGWVGWQEVSAAFDPNSFYNLCLTSLSSQQQQRTLD", "text": "SIMILARITY: Belongs to the peptidase C78 family."}
+{"protein": "MGSCVSRDLFTSAHKNCPMPQGADPLNPDLPSGRTPTVAPDCVIGKDKQMDFCWDPWQRCFQTTNGYLSDSRSRPGNYNVAALATSSLVGVVQSIKDHITKPTAMARGRVAHLIEWKGWSAQPAGWELSPAEDEHYCCLPDELREARFAAGVAEQFAITEATLSAWSSLDEEELHPENSPQGIVQLQDLESIYLQDSLPSGPSQDDSLQAFSSPSPSPDSCPSPEEPPSTAGIPQPPSPELQHRRRLPGAQGPEGGTHPPGSLPSMDSGSLWEEDEVFYN", "text": "SIMILARITY: Belongs to the FAM131 family."}
+{"protein": "MSFSHSFIFIVIFCMQSLAALLQNGFMATVLGREWVRSQGLPAGDMIMACLAASRFCLHGIAVLNNFLASAMFWTIKNYFSILWDFTNTVNFWFTTWLAIFYCVKISSFSHPIFFWIKWRISRSVPRLLLGSLIIGGLSAISSATGNTIALQMAACENYTIYYKMMAFYLYYFRCHAMLMWVIPFFLFLLSIILLMFSLYRHLEQMRYHRPRTHDYSTQAHIMALKSLAFFLIFYTSYTLLLTVSVAHVINVHGSWHWAWEVVTYMGISLHSTILILSNTKMRKALKIKFPDLCIPRS", "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": "MAQNFSTVGDGKQMLLERDSSKRVLTGCFLSLLIFTTLLGNTLVCVAVTKFRHLRSKVTNFFVISLAISDLLVAILVMPWKAATEIMGFWPFGEFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKVACLMISVAWTLSVLISFIPVQLNWHKAQTASYVELNGTYAGDLPPDNCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQKQIRRISALERAAESAQNRHSSMGNSLSMESECSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCEADDTTDFPCISSTTFDVFVWFGWANSSLNPIIYAFNADFRKAFSILLGCHRLCPGNSAIEIVSINNTGAPLSNPSCQYQPKSHIPKEGNHSSSYVIPHSILCQEEELQKKDGFGGEMEVGLVNNAMEKVSPAISGNFDSDAAVTLETINPITQNGQHKSMSC", "text": "FUNCTION: Receptor for dopamine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MKLRNTGQMAFRSPFSNLHVRRSSHKPSHPAFVRQNRSMHYYFRDALNIGAFGIIFGLPCLLYAFTFFCNDISGCPAPSLLHPSTLSIDKLEQEVGWPEDGIKALYDTQVTMWVLSYYLLSLLMQVFLPGTEVEGTELACGGRLKYKFNAFLSAVLILSGCAVGTYLYGTEFALWTFLWDNYVQVITANLIICTAIAIFVYLRSFSVPAPGQLNPELRQLAPGGHTGNVLYDFFIGRELNPRIKLPIPFVGETARTIDIKVWCEMRPGLLGWIILDLSNIAHQYRTYGYITDSIVLTTAFQAFYVLDALYMEPALLTTMDVIMDGFGFMLSFGDMVWVPFLYNFQTRYLSVYPSELGLSGILIVLAVTAAGYVIFRGANNQKNRFRTDPNDPRVKHLKYIETKTGSKLLISGWWGCARHINYLGDWIMSWSYCLPTGVAGYAIIESINPASGEMQKQAVQTPESRGWGMIFTYFYMIYFGVLLLHRERRDEEKCKRKYGADWNRYTSLVRSRIIPGIY", "text": "FUNCTION: Delta(14)-sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:33475797). Catalyzes the reduction of the C14=C15 double bond within 4,4,24-trimethyl ergosta-8,14,24(28)-trienolto produce 4,4-dimethylfecosterol (PubMed:33475797). 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. SIMILARITY: Belongs to the ERG4/ERG24 family."}
+{"protein": "MRGAFLAAAAAVAGTAMADVAHMRRHGHDSFHHNRAYQPEVPAEGDENCECTTKVITITGPPTLVPINTPAPEPSSSSSSEVPSVPSSESSVVTSEAVTTLHSTSTATVTVVTTPGVDATGAQTPTGGVPGTPEASSPAGTPEASTPAVPATSESPLPTPGVTSFSSTGIYTIPATTVTVRDTTTVCGATTTELPSGTHTFGGVTTVVSTATTVTCPVATVEPSGSTVTSKIYTTTYVCPSAGTYTIAPTTTYVPTSTVVVYPTPATITPGTYTQDEQTVTVTRTDFTYVCPFTGNDQPTSAPVASTSAVPVTTTAAPSTTSAVASSSASASSTATAVPTGVSGQQMGMTYSPYTNEGGCQSKDQVLKDVALIKQKGFTHVRVYSTDCNGLEYIGEAARENGLKMIIGVFISSTGISGAQEQVTAITKWAQWDLVTLVVVGNEAIQNGYTDASSLAGFISSCKSSFQASGYSGQVTTTEPINVWQQSGSALCGAVDILGANLHPFFNADVTPDQAGSFVRAQIKDLEAVCNKDVINLETGWPSAGNANGKAVPGTAQQAAAIKALVEEVGSQSVFFSYSNDLWKDAGEFDVERYWGCIDQFK", "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": "MPAESHTVYPAYRFSIAPMLDWTDRHCRYFLRLLSRNTLLYTEMVTTGAIIHGKGDYLAYSEEEHPVALQLGGSDPAALAQCAKLAEARGYDEINLNVGCPSDRVQNGMFGACLMGNAQLVADCVKAMRDVVSIPVTVKTRIGIDDQDSYEFLCDFINTVSGKGECEMFIIHARKAWLSGLSPKENREIPPLDYPRVYQLKRDFPHLTMSINGGIKSLEEAKAHLQHMDGVMVGREAYQNPGILAAVDREIFGSSDTDADPVAVVRAMYPYIERELSQGTYLGHITRHMLGLFQGIPGARQWRRYLSENAHKAGADINVLEHALKLVADKR", "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. Specifically modifies U20 and U20a in tRNAs. SIMILARITY: Belongs to the Dus family. DusA subfamily."}
+{"protein": "MRPLKQATPTYSSRTADKFVVRLPEGMREQIAEVARSHHRSMNSEIIARLEQSLLQEGALQDNLGVRLDSPELSLHERELLQRFRQLTHRQQNALVALIAHDAELAQA", "text": "FUNCTION: Functions as both a transcriptional activator and repressor of multiple genes encoding virulence factors as well as genes involved in environmental adaptation (PubMed:16352829, PubMed:26549743, PubMed:22511872). Plays a role in alginate production via the activation of AlgD which is the first gene in the alginate biosynthetic operon (PubMed:16352829, PubMed:10476040). Regulates also the transcription of genes responsible for type IV pili localization and twitching motility (PubMed:16352829). Mediates transition of P.aeruginosa biofilm infections from colonizing to chronic biofilms through repression of the psl operon (PubMed:23354748). Represses also its own transcription by binding to two sites on amrZ promoter, amrZ1 and amrZ2 (PubMed:15968052)."}
+{"protein": "MACSSSLSSKWASWGASSRPHPSVQPFVTRKNVVRYHKPTSELSYSPLTTTLSSNLDSQFMQVYETLKSELIHDPSFEFDDDSRQWVERMIDYNVPGGKMVRGYSVVDSYQLLKGEELTEDEAFLACALGWCTEWLQAFILVLDDIMDGSHTRRGQPCWFRLPEVGVVAINDGVLLRNHVHRILKKYFQGKPYYVHLLDLFNETEFQTISGQMIDTICRLAGQKDLSKYTMTLNRRIVQYKGSYYSCYLPIACALLMFGENLEDHVQVKDILVELGMYYQIQNDYLDTFGDPDVFGKTGTDIEECKCSWLIAKALELANEEQKKILSENYGINDPSKVAKVKELYHALDLKGAYEDYETNLYETSMTSIKAHPNIAVQAVLKSCLEKMYKGHK", "text": "FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Catalyzes the condensation of two molecules of dimethylallyl diphosphate to produce chrysanthemyl diphosphate (CPP), a monoterpene with a non-head-to-tail or irregular c1'-2-3 linkage between isoprenoid units (PubMed:11287653, PubMed:25378387). In a second step, hydrolyzes the diphosphate moiety of CPP to form chrysanthemol (PubMed:25378387). With a lower efficiency, can also converts dimethylallyl diphosphate into lavandulyl diphosphate (LPP), and subsequently LPP into lavandulol (PubMed:25378387). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
+{"protein": "MASPGSGFWSFGSEDGSGDPENPSTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGGSEPPRATSRKAACACNQKPCSCPKAEVNYAFLHATDLLPACDGERPTLAFLQDVMDILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMLIARFKMFPEVKEKGMAAVPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMVPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHIDKCLELAEYLYSIIKNREGYEMVFDGKPQHTNVCFWYVPPSLRVLEDNEERMNRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL", "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": "MSNVGTPRTAQEIQQDWDTNPRWNGITRDYTAEQVAELQGSVVEEHTLAKRGAEILWDAVSAEGDDYINALGALTGNQAVQQVRAGLKAVYLSGWQVAGDANLAGHTYPDQSLYPANSVPNVVRRINNALLRADEIARVEGDTSVDNWLVPIVADGEAGFGGALNVYELQKGMITAGAAGTHWEDQLASEKKCGHLGGKVLIPTQQHIRTLNSARLAADVANTPTVVIARTDAEAATLITSDVDERDRPFITGERTAEGYYHVKPGLEPCIARAKSYAPYADMIWMETGTPDLELAKKFAEGVRSEFPDQLLSYNCSPSFNWSAHLEADEIAKFQKELGAMGFKFQFITLAGFHSLNYGMFDLAYGYAREGMPAFVDLQNREFKAAEERGFTAVKHQREVGAGYFDTIATTVDPNSSTTALKGSTEEGQFH", "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": "MRRTVRALATRVHGRVCAVPLVVGMLLATALYGGGPAAADPAAPDNLATLVAKVASADQKLQELGAAIQTQQETVNKAIVDVQAARDAAAAAQRELEAGQRGVADANAAIEAAQKRFDSFAAATYMNGPSRSYLTATDPADIVNTTATGQALIASSQQVMAKLQRARTEQVNRESAARLAKEKADQAARDAESSQDNAVAALKQAQQTFNAQQGELERLAAERAAAQAELDSVRKVSATGNAAPAAAPAAAPAPAAAPAPVPNSAPAPVPGAQPNPQAAAGNWDRAPSGPASSGQNWAVWDPTLPAIPSAFVSGDPIAIINAVLGIASTSAQVTADMGRSFLQKLGILPTPTGFTNGAIPRVYGREAVEYVIRRGMSQIGVPYSWGGGNAAGPSRGIDSGAGTVGFDCSGLMLYMFAGVGIKLDHYSGSQYNAGRKIPSSQMRRGDMIFYGPNASQHVAMYLGNGQMLEAPYTGSHVKVSPVRTSGMTPYVTRLIEY", "text": "FUNCTION: Peptidoglycan endopeptidase that cleaves the bond between D- glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan. Required for normal separation of daughter cells after cell division and for cell wall integrity (By similarity). SUBCELLULAR LOCATION: Secreted. Note=Localizes to the septa. SIMILARITY: Belongs to the peptidase C40 family."}
+{"protein": "MSKGLPETRTDAAMSELVPEPRPKPAVPMKPIGINPNLLGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIHYETYRAKRLNDNGGLPPGEGLLGTVLPPVPATPCPTAE", "text": "FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton Synapse. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
+{"protein": "MLGTSTKCSKRDCNYAKENISRIMPTIGLGYKQNFEKKTADTQSSCKLLLVALLESFCKHSDQTPEQSKQMFLYVAHSLQNSGIIDFEFSEELEPIRNAYADSLHNLLSKAFRSTLPMSSTKDSKKSRYSSPDGVLAKTASFLSVLSDGGYEDDVMNVKPSVNVLSNRLNHLPVEALESCFPQTTLESSTFADFCEHKDGTGNLSFSNFDSFPTVQRSRYASDFEELELLGKGGYGSVYKARNKFDGVEYALKKIPLRLRSFSTSSNIFRESRTLARLNHPNVIRFFSSWVELLPSSEKQIEEEPLASADETLSQSADIDNFMFDMDTGLLQHTYPSSVQILFQEDSVADDLTPCYSTKNSTCNLTDLFKKEADQDYAESHDCSSTTSQVDTLGKLAPTKSASEMLLMDSFLSEREEDECSNIPSFDQQPLCLYIQMALCEETLEKHINRRNKHIHGVMSKGLRNCYILLFARILEGVLYLHDAMHLVHRDLKPRNIFLSSGVHSEPCSVCLPNFSDEDNVEVSNAYEPVNQRTLCVVPKIGDFGLVLSQSDNLEEGTNSSAESSFVGTSTYAAPELFSKHMRSVMNNNSSTDIYALGILFFELLYPFNTRMERASAIANLKKGIFPHDFLDSMPEEASLIRSMLSSSNKRPTAAQLLTSNLFHDLVVNELHVYQALLEDAEKRNNNLKAELNILRVLNPNYDC", "text": "FUNCTION: Mediates down-regulation of protein synthesis in response to stress conditions by the phosphorylation of the alpha subunit of eIF-2 (tif211) on 'Ser-52'. Protein synthesis is inhibited at the level of initiation. Activity is inhibited in the presence of heme. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily."}
+{"protein": "MEKLAAGLAGLRWSMGAFPLDLIVSRCRLPTLACLGPGEYAEGVSERDILLIHSCRQWTTVTAHTLEEGHYVIGPKIDIPLQYPGKFKLLEQARDVREPVRYFSSVEEVASVFPDRIFVMEAITFSVKVVSGEFSEDSEVYNFTLHAGDELTLMGQAEILCAKTTKERSRFTTLLRKLGRAGALAGIGGPGSMGATGGGGGAARPVKSKMPCLICMNHRTNESLSLPFQCQGRFSTRSPLELQMQEGEHTVRAIIERVRLPVNVLVPSRPPRNPYDLHPVREGHCYKLVSIISKTVVLGLALRREGPAPLHFLLLTDTPRFTLPQGLLAGDPRVERLVRDSASYCRERFDPDEYSTAVREAPAELSDDCASPRHARLCLPAPRAPGAVRAPGPPGRLGPALPAPGDSDQDYVSPDWAGVSEPAGGCAEIPYEELWVHQAPESRADARARPLAGPDLISFGIVGPPRHEPEAPPPPVPPKSEAVKEECRLLHAPPVPPRGGGSCSKLTGSPPVLPHFPKLQPVHSPSSSLSYYSSGLQDGAGSRSGSGSPSPDAYSLYCYPCTWGDCKASESSSRPPPGPLPSTTTQPSQASRGLSEPLSGRTPSLLGADTPVVKNYHSCPPLFKSSRPQKSFAPFGALNPFSGPAHPSGAPAASSSGSISTSGVLATSSPTHSPGPGPGPQGQGYSAAPSSSLSSSEWQEPALEPLDPFELGQASPPELELVRCQEPRAAGAPGSGPCLSPLGQPKAFEPEGLVLRQVPASLSPAALQGPEAGGTLLFLTQGCLEGPPGSPREGATGAGVRDASSWQPPADLSALSLEEVSRSLRFIGLSEDVVSFFARERIDGSIFVQLSEDILADDFHLTKLQVKKIMQFIKGWRPKI", "text": "FUNCTION: Probable adapter protein that provides a critical link between cell surface epidermal growth factor receptor and the MAPK/ERK signaling pathway. SIMILARITY: Belongs to the GAREM family."}
+{"protein": "MDANTKTILFFVVFFIDLFSPNILFVYAREIGNKPLFTYKQKTEKGPAEWGKLDPQWKVCSTGKIQSPIDLTDERVSLIHDQALSKHYKPASAVIQSRGHDVMVSWKGDGGKITIHQTDYKLVQCHWHSPSEHTINGTSYDLELHMVHTSASGKTTVVGVLYKLGEPDEFLTKILNGIKGVGKKEIDLGIVDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVQKRVLYFFCFCYRLIIFVTPYINIFWIFVFVFWCMLM", "text": "FUNCTION: Reversible hydration of carbon dioxide. SUBCELLULAR LOCATION: Plastid, chloroplast stroma Note=Targeted to the chloroplast via a protein-targeting pathway that uses the secretory system. SIMILARITY: Belongs to the alpha-class carbonic anhydrase family."}
+{"protein": "MADSLLLLKRVPSRHTWLRARKARPQLMLSRRPRRRLRNLRWRSRRRLRRRLLQAQAAGADWLQGGCLVSGDAALQRLKTSARRRASSPEPAEDPVPSGPAILPIPPVRPAGSGRAVLLLPLGQGFTFSGICCVTCLYGQVQVFGFTISQGQPAQNVFSTYTHSRLTINAVHYSVHEKSKKEMKREARVLLRPYLNQDDRYCLMSSFSPLCSIVLLERLKTSTVNFIISHPGLSYIFVQEVRTFQINSEYFALRSVGIRREKKKTGLRLTESAFAVMEELVSISSEEADSCPVILVCGCQDIGKSTFNRYLINQLLNSVSCVDYLECDLGQTEFTPPGCISLLNITEPVLGPPFTHQRTPQKMVYYGKTSCKNNFENYIEVIKYVFSSYKRESPLIINTMGWVADQGLLLLIDLIRLLSPSHVVQFSSDRSKYMPDLTPDFVDDMDGLYTRRRSRVRNRGFHLPEFAESLEFADEEKEGPVMSTGYKLMFVKSEFVTGKTSRNRESHNRILRELAVLGYLSQLQPPVPKPLRALHGLTPYQVPFNAVALRIIHADVAPTHILYAVNASWVGLCKILDDVRGYASGPILLAQSPICDCVGFGICRGIDMEKKLYHILTPVPPEELRHVNCLLVGAVNIPQCVLKSQGGLEGTIPYVTTDYNFKLPGASEKIGARESGATYKEKGHPKPKFYRKTY", "text": "FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. The kinase activity is required for the processing of the 32S precursor into 5.8S and 28S rRNAs, more specifically for the generation of the major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase activities. Probably binds RNA (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Note=Colocalizes with pre-60S rRNP particles. SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily."}
+{"protein": "MGRMHSAGKGISSSAIPYSRNAPAWFKLSSESVIEQIVKYARKGLTPSQIGVLLRDAHGVTQARVITGNKIMRILKSNGLAPEIPEDLYYLIKKAVSVRKHLERNRKDKDAKFRLILIESRIHRLARYYRTVAVLPPNWKYESATASALVN", "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": "MSIKYLMLLFAAMIIRSLADSGNAIETTSPEITNATTDIPAIRLCGPEGDGYCLHGDCIHARDIDGMYCRCSHGYTGIRCQHVVLVDYQRSGKPDTTTSYIPSLGIVLVLVGIIITCCLLSVYMFTRRTKLPIQDMVVLYFL", "text": "FUNCTION: [Viral epidermal growth factor]: Stimulates cellular proliferation (hyperplasia)and mobility around infected cells to promote rapid and efficient spread of infection. This effect is beneficial for virus replication in vivo, because poxviruses replicate possibly better in proliferating cells than in quiescent cells. Acts by binding host EGFR, inducing its dimerization, autophosphorylation and leading to activation of several cellular pathways regulating cell proliferation or cell survival. The activation by host EGFR of mitogen activated protein kinases (MAPK) and extracellular-signal regulated kinases (ERK) are essential for the positive effect of vaccinia growth factor on poxvirus virulence in vivo. SUBCELLULAR LOCATION: [Pro-Viral epidermal growth factor]: Host membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Viral epidermal growth factor]: Secreted. SIMILARITY: Belongs to the orthopoxvirus OPG019 family."}
+{"protein": "MPMTLGYWDIRGLAHAIRLFLEYTDTSYEDKKYSMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLGRKHNLCGETEEERIRVDVLENQAMDTRLQLAMVCYSPDFERKKPEYLEGLPEKMKLYSEFLGKQPWFAGNKITYVDFLVYDVLDQHRIFEPKCLDAFPNLKDFVARFEGLKKISDYMKSGRFLSKPIFAKMAFWNPK", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Mu family."}
+{"protein": "MEESEQVLPLLTNPKDLTNPSYASSSSSSSEPRDETEDLLLPISDENEEEEEENSPIRQVALTVPTTDDPSLPVLTFRMWVLGTLSCILLSFLNQFFWYRTEPLTISAISAQIAVVPLGRLMAAKITDRVFFQGSKWQFTLNPGPFNVKEHVLITIFANAGAGSVYAIHVVTVVKAFYMKNITFFVSFIVIVTTQVLGFGWAGIFRKYLVEPAAMWWPANLVQVSLFRALHEKEERTKGGLTRTQFFVIAFVCSFAYYVFPGYLFQIMTSLSWVCWFFPSSVMAQQIGSGLHGLGVGAIGLDWSTISSYLGSPLASPWFATANVGVGFVLVIYVLVPICYWLDVYKAKTFPIFSSSLFSSQGSKYNITSIIDSNFHLDLPAYERQGPLYLCTFFAISYGVGFAALSATIMHVALFHGREIWEQSKESFKEKKLDVHARLMQRYKQVPEWWFWCILVTNVGATIFACEYYNDQLQLPWWGVLLACTVAIIFTLPIGIITAITNQAPGLNIITEYIIGYIYPGYPVANMCFKVYGYISMQQAITFLQDFKLGHYMKIPPRTMFMAQIVGTLISCFVYLTTAWWLMETIPNICDSVTNSVWTCPSDKVFYDASVIWGLIGPRRIFGDLGLYKSVNWFFLVGAIAPILVWLASRMFPRQEWIKLINMPVLISATSSMPPATAVNYTTWVLAGFLSGFVVFRYRPNLWQRYNYVLSGALDAGLAFMGVLLYMCLGLENVSLDWWGNELDGCPLASCPTAPGIIVEGCPLYT", "text": "FUNCTION: Involved in the translocation of tetra- and pentapeptides across the cellular membrane in an energy-dependent manner. May also transport cadmium complexes. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the oligopeptide OPT transporter (TC 2.A.67.1) family."}
+{"protein": "MALIEGVGDEVTVLFALVLFFMVLMLAWVSTHTTERAPTHWIRPEPAQGGASSNSQRDFHPGPSQTLTNADPNSETVDSSDSTQSSREFQNAGATPHSEVAFSSSGSTVSTGGSVEYTGAAADSPPDGESHPNFTVSSRDPQAGASSSLRYRGLGDGTTAQSAEEAGTIHLRLKFLNDTERLVTVRLSDTIMYIKRTYFPGQELRVRLIFQGQLLRDDSQTVSSLQLRDGSVLHCHISQHASVPGVGADQANVPLNVGNLLVPLLFLIVMLLWYCQFQYPSLFTGTATACLGGFTLLISAIAFSSYHR", "text": "FUNCTION: May contribute to the regulation of translation during cell- cycle progression. May contribute to the regulation of cell proliferation (By similarity). The membrane form is involved in sterol- regulated ubiquitination and degradation of HMG-CoA reductase HMGCR. May be involved in centrosome assembly. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Cytoplasm Nucleus."}
+{"protein": "MAPFAPLASCILLLLWVTAPSRACTCAPPHPQTALCNSQIVIRAKFVGTAEVNQTDLNRRYEIKMTKMFKGFSALGNASDIRFVDTPALESVCGYLHRSQNRSEEFLVAGNLRDGHLQINTCSFVAPWSSLSTAQRRGFTKTYAAGCEGCTVFTCSSIPCKLQSDTHCLWTDHFLTGSDKGFQSRHLACLPREPGICTWQSLRPRMA", "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": "LKCNKLVPLF", "text": "FUNCTION: Shows cytotoxic activity against Ehrlich ascites carcinoma (EAC) model in mice. Also shows effect on apoptotic features such as nuclear fragmentation, caspase activity, pro- and anti-apoptotic protein levels on treated EAC cells. Increased levels of antioxidant enzymes and cytokine levels observed in toxin-treated EAC mice. Cardiotoxic towards guinea pig auricle. Has no cytotoxicity towards macrophages in vivo in EAC bearing mice or in vitro in normal human lymphocytes. SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily."}
+{"protein": "MHNMSDIIEQYIKRLFEEADEDVVEIQRAHIAQRFDCVPSQLNYVIKTRFTNEHGYEIESKRGGGGYIRITKIENKDATGYINHLLQLIGPSISQQQGYYVIDGLLDKGLINEREAKMIQTIIDRETLKMDVVARDIIRANILKRLLPVINYY", "text": "FUNCTION: Negative regulator of clpC, clpB and clpP transcription by binding directly and specifically to their promoter region. SIMILARITY: Belongs to the CtsR family."}
+{"protein": "MGLLSIGTPLSWDESKKYNNHVRTNGITQLINIFKQHGYRENDVFLWGDEVEYMLVDFDETKKTARLSIDKDYIINDLNDPDKLLPIAEKQDVSYHPEYGRFMVEATPAKPYNGNLLSDYLYIEKNMIIRRQLCEDNLPSHIKLLTLTTFPRMGCNIFTSPPSKPDGIASQSLFLPDEIINRHARFPTLTANIRKRKGHKVAINLPIYPDKSTKLLDDTIPQNRELFDSDKEPWIGASKPGFIYMDSMGFGMGSSCLQITMQTKNISQARYLYDSLAPIAPIMLSLSAAAPIFKGFLVDQDVRWNVVSGAVDDRTFIEKGQEPYSGYHLFGGLDIDAQDKLRINNHQINQQGDLLDLYTKDGKPIQRVPQSRYDSIDNYLNDNYYDTKYFQDEYNDLNAPINEQVYQRLIDEGKLDKYMANHFAHLFIRDPLVIFSERINQDNNLENDHFENIQSTNWQTLRFKPPALYTKDTDLTTKPGWRVEFRPMEIQLTDFENAAYSSFITLLSKAILKFQPNFYIPLSKVEINMKLAHKVDSTLKDKFWFRSFELWNIDPQEFDDYGFEWFDQFINGNQQQNGHVNNNNNNDKKTKNDPIIVNGSTTTTNGTNSGSGITETNGTMLPKGCEGKTVEEINDVDDNGIDQRYTICQLINGSGEFPGFIKLVIKLIATDLVPQALNNSTISKEQLIEN", "text": "SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family."}
+{"protein": "MKIKAISIDIDGTITYPNRMIHEKALEAIRRAESLGIPIMLVTGNTVQFAEAASILIGTSGPVVAEDGGAISYKKKRIFLASMDEEWILWNEIRKRFPNARTSYTMPDRRAGLVIMRETINVETVREIINELNLNLVAVDSGFAIHVKKPWINKGSGIEKASEFLGIKPKEVAHVGDGENDLDAFKVVGYKVAVAQAPKILKENADYVTKKEYGEGGAEAIYHILEKFGYL", "text": "FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate (By similarity). Has phosphatase activity towards p-nitrophenylphosphate (in vitro). SIMILARITY: Belongs to the archaeal SPP-like hydrolase family."}
+{"protein": "MGLKWTDSREIGEALYDAYPDLDPKTVRFTDMHQWICDLEDFDDDPQASNEKILEAILLVWLDEAE", "text": "FUNCTION: May function as iron donor in the assembly of iron-sulfur clusters. FUNCTION: May function as iron donor in the assembly of iron-sulfur clusters. SIMILARITY: Belongs to the IscX family."}
+{"protein": "MAEMEKEGRPPESKRSRKPAHPVKREINAEMKVPSNRPLPGAGQAGNLHGNSPYLMSFAENTMNELLGWYGYDKVELRDSDDIEIRNYPDGEMRQHISVLKENSLPKASTLENSSGSPPHANSSGSTPTSRNGVTAESSVNPSSSKEHGGLPIIVPLIPPPLIKAPAEEDSSNVQIMCAWCQKVGVKRYSLSMGSELKSFCSEKCFAACRRAYFKRNKLGYVRNCSAREEEGVPTHSLSKDTPRLVLKTNSDVLVCDWCKHIRHTKEYLDFGAGERRLQFCSAKCLNQYKMDIFYKETQAALPGGLCNPPLPTSDTKSESGAGVQLLTPESWSAPLSELRSRKAPSPVGATIAGPSGSTSGSPSEAGTVCSSSSSSSSSSSSTKIPTPRPHESPSLPPPHPPPISGLHPALGMPPGSPPMVMTPRGPVPFPIFMEHQMMQQMRPPFLRPPGPNSPHSNPMIPGIGPPPPPRTLCPPSSPMHRPLLSPHLHPSSTPTLSGNPPGIMPPHPAAHMPGLPFPPVNMMPSGPIPVPPIMNIGMPSLAPLVPPPTLLVPYPVIVPLPVPIPIPVPIPYNPQRSGDRPGNDGTLPNTANEQKDSKAPPSFSSRGEERDFQKAPPNSDTLSPEFSKQTEQGRTNMADLMVKMENSGKGSSEHSHKDTPADGVIDLTTSHRSRQQLVIQRAVTCVQVKAEPGLSPPPALLGETELDGSTSISTGTAKDDHRDTYSNAESPLASVALPCADPSYCSGTPPLSQPITCSASIIPSNITTAKTEPGSATPCNVIVNGSCNLPPTESLIRTPPLEQRPQVDTCRRTATVCDEPAGADLEGEDLKENSCLATEKDSAGKRCSNDQSAITTGTGDDKSQSPEDDPSGEDHAYALPLMPKPGCVIQPVPKPAEKTAAILPCGLTAPLTGTVPMEMEPPLKRRCLRIRNQNK", "text": "FUNCTION: Implicated in development of the cochlea. SIMILARITY: Belongs to the SOBP family."}
+{"protein": "MTIEEVSGETPPSTPPSSSTPSPSSSTTNAAPLGSSVIPIVNKLQDIFAQLGSQSTIALPQVVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSRANGGSDDEWGEFRHLPETRFYDFSEIRREIEAETNRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQPSDIEARIRTMILSYIKQDTCLILAVTPANTDLANSDALQIASIVDPDGHRTIGVITKLDIMDKGTDARKLLLGNVVPLRLGYVGVVNRCQEDILLNRTVKEALLAEEKFFRSHPVYHGLADRLGVPQLAKKLNQILVQHIKVLLPDLKSRISNALVATAKEHQSYGELTESRAGQGALLLNFLSKYCEAYSSLLEGKSEEMSTSELSGGARIHYIFQSIFVKSLEEVDPCEDLTDDDIRTAIQNATGPRSALFVPDVPFEVLVRRQISRLLDPSLQCARFIFEELIKISHRCMMNELQRFPVLRKRMDEVIGDFLREGLEPSEAMIGDIIDMEMDYINTSHPNFIGGTKAVEAAMHQVKSSRIPHPVARPKDTVEPDRTSSSTSQVKSRSFLGRQANGIVTDQGVVSADAEKAQPAANASDTRWGIPSIFRGGDTRAVTKDSLLNKPFSEAVEDMSHNLSMIYLKEPPAVLRPTETHSEQEAVEIQITKLLLRSYYDIVRKNIEDSVPKAIMHFLVNHTKRELHNVFIKKLYRENLFEEMLQEPDEIAVKRKRTQETLHVLQQAYRTLDELPLEADSVSAGMSKHQELLTSSKYSTSSSYSASPSTTRRSRRAGDQHQNGYGF", "text": "FUNCTION: Involved in the control of mitochondrial and peroxisomal division and morphology. In association with PEX11C, PEX11D, PEX11E and FIS1B, is involved in cell cycle-associated constitutive self- replication of preexisting peroxisomes. SUBCELLULAR LOCATION: Mitochondrion Peroxisome. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
+{"protein": "MDEYDEDPGRRASKLMETLSIYDVYQDGMYGEPNPDMEKTKRMNGSSSTPGNKVYSAAPVRSVNGNRASVPLDFCSPQREAVYPDPDVYCTKSEVALPCYSGASDRLRRYTHAEVQGHRYSTGCAYDGLVLGKQVAVSGARSNSLCMSSPDGRYTATSPRSSLASSHSSQDQSKHTSPRSSISSPRSSLVSPGQGEGTSVISPRSSYASTASDTSKHSSPRTSLNSYDCGSKPSSNRTSGISMGYDQRHISPRSSTTSPRSSYSDSRFTPAGGHDPESAAVHGIPMASPRSSICSQPAVAANCVVSPRSSISSHSSRSSRSSRGSMSAYPELQLPMLGPGLPEDALLQDFTEPNGLHNNRVHLQTFPVLEEPQQQNSEVNIGFNYCKAGAGGQRFKLPYQVTPSRDSGPSQAERRLEALTLELEKELEIHMKKEYFGICVKCGKGVYGASQACQAMGNLYHTNCFTCCSCGRRLRGKAFYNVNGKVYCEEDFLYSGFQQTAEKCFVCGHLIMEMILQALGRSYHPGCFRCVICKEGLDGVPFTVDVENNIYCVKDYHTVFAPKCASCNQPILPAQGSEETIRVVSMDKDYHVDCYHCEDCGLQLNDEEGHRCYPLEGHLLCHRCHLHRLKTPLAPHPPPSYPLHVTEL", "text": "FUNCTION: May monitor slit diaphragm protein assembly, a specialized adherens junction characteristic of podocytes. In case of podocyte injury, it shuttles into the nucleus and acts as a transcription regulator. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Acts as a transcriptional corepressor for snai1 and snai2/slug and plays a role in regulating neural crest development (By similarity). SUBCELLULAR LOCATION: Cell junction, adherens junction Nucleus. SIMILARITY: Belongs to the zyxin/ajuba family."}
+{"protein": "MWMFSWLCAILIILAIAGMNTIAKTTPHTKFTKKSEEREMPKGLKPSSGPPPEEEETLFTEMAEMAEPITKPSALDSVFGTATLSPFENFTLDPADFFLNCCDCCSPVPGQKGEPGETGQPGPKGEAGNLGIPGPPGVVGPQGPRGYKGEKGLKGERGDQGVPGYPGKPGAQGEPGPKGDKGNIGLGGVKGQKGSKGDTCGNCTKGEKGDQGAMGSPGLHGGPGAKGEKGEMGEKGEMGDKGCCGDSGERGGKGQKGEGGMKGEKGSKGDSGMEGKSGRNGLPGAKGDPGIKGEKGELGPPGLLGPTGPKGDIGNKGVRGPTGKKGSRGFKGSKGELARVPRSAFSAGLSKPFPPPNIPIKFEKILYNDQGNYSPVTGKFNCSIPGTYVFSYHITVRGRPARISLVAQNKKQFKSRETLYGQEIDQASLLVILKLSAGDQVWLEVSKDWNGVYVSAEDDSIFTGFLLYPEETSGISP", "text": "FUNCTION: Collagen-like protein specifically expressed in the inner ear, which provides an organic scaffold for otoconia, a calcium carbonate structure in the saccule and utricle of the ear. Acts as a scaffold for biomineralization: sequesters calcium and forms interconnecting fibrils between otoconia that are incorporated into the calcium crystal structure. Together with OC90, modulates calcite crystal morphology and growth kinetics. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Note=Localized in both the surrounding otoconial matrix and otoconia. SIMILARITY: Belongs to the OTOL1 family."}
+{"protein": "MESQLWNWILPLLISSLLISFVAFYGFFVKPKRNGLRHDRKTVSTVTSDVGSVNITGDTVADVIVVGAGVAGSALAYTLGKDKRRVHVIERDLSEPDRIVGELLQPGGYLKLLELGIEDCVEEIDAQRVYGYALFKNGKRIRLAYPLEKFHEDVSGRSFHNGRFIQRMREKAASLPNVQLEQGTVLSLLEENGTIKGVRYKNKAGEEQTAFAALTIVCDGCFSNLRRSLCNPQVEVPSCFVGLVLENCNLPYANHGHVVLADPSPILMYPISSTEVRCLVDVPGQKVPSIANGEMKNYLKTVVAPQMPHEVYDSFIAAVDKGNIKSMPNRSMPASPYPTPGALLMGDAFNMRHPLTGGGMTVALADIVVLRNLLRPLRDLSDGASLCKYLESFYTLRKPVAATINTLANALYQVFCSSENEARNEMREACFDYLGLGGMCTSGPVSLLSGLNPRPLTLVCHFFAVAVYGVIRLLIPFPSPKRIWLGAKLISGASGIIFPIIKAEGVRQMFFPATVPAYYYKAPTVGETKCS", "text": "FUNCTION: Catalyzes the stereospecific oxidation of squalene to (S)- 2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis. Can produce not only oxidosqualene, but also 2,3:22,23-dioxidosqualene. Main squalene epoxidase in the root. Sqe1 mutants may show defects in membrane lipid rafts, impairing the correct localization of RHD2 NADPH oxidase and the proper polarized production of ROS. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the squalene monooxygenase family."}
+{"protein": "MATMVPSVLWPRACWTLLVCCLLTPGVQGQEFLLRVEPQNPVLSAGGSLFVNCSTDCPSSEKIALETSLSKELVASGMGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVYRLPERVELAPLPPWQPVGQNFTLRCQVEDGSPRTSLTVVLLRWEEELSRQPAVEEPAEVTATVLASRDDHGAPFSCRTELDMQPQGLGLFVNTSAPRQLRTFVLPVTPPRLVAPRFLEVETSWPVDCTLDGLFPASEAQVYLALGDQMLNATVMNHGDTLTATATATARADQEGAREIVCNVTLGGERREARENLTVFSFLGPIVNLSEPTAHEGSTVTVSCMAGARVQVTLDGVPAAAPGQPAQLQLNATESDDGRSFFCSATLEVDGEFLHRNSSVQLRVLYGPKIDRATCPQHLKWKDKTRHVLQCQARGNPYPELRCLKEGSSREVPVGIPFFVNVTHNGTYQCQASSSRGKYTLVVVMDIEAGSSHFVPVFVAVLLTLGVVTIVLALMYVFREHQRSGSYHVREESTYLPLTSMQPTEAMGEEPSRAE", "text": "FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2) (PubMed:1448173). ICAM3 is also a ligand for integrin alpha-D/beta-2. In association with integrin alpha- L/beta-2, contributes to apoptotic neutrophil phagocytosis by macrophages (PubMed:23775590). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family."}
+{"protein": "MIKQDVQKCVDALQDFVDKEIGESVNLFSCKSRANNELLLNIDEKFQLKDKDELHQLGEQKIENQNKLQEIRNKVEYYEKLLTELEEAQKELEVRYKLVSKSK", "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": "MGRRLGRVAALLLGLLVECTEAKKHCWYFEGLYPTYYICRSYEDCCGSRCCVRALSIQRLWYFWFLLMMGVLFCCGAGFFIRRRMYPPPLIEEPTFNVSYTRQPPNPAPGAQQMGPPYYTDPGGPGMNPVGNTMAMAFQVQPNSPHGGTTYPPPPSYCNTPPPPYEQVVKDK", "text": "FUNCTION: Increases the transcriptional activity of NFKB1 by facilitating its nuclear translocation, DNA-binding and associated apoptotic response, when overexpressed. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass type I membrane protein Note=When overexpressed, localizes in the nucleus and perinuclear regions. SIMILARITY: Belongs to the VOPP1/ECOP family."}
+{"protein": "MKKTQTWIITCIYLQLLLFNPLVKTKEICGNPVTDNVKDITKLVANLPNDYMITLNYVAGMDVLPSHCWLRDMVIQLSLSLTTLLDKFSNISEGLSNYSIIDKLGKIVDDLVLCMEENAPKNIKESPKRPETRSFTPEEFFSIFNRSIDAFKDFMVASDTSDCVLSSTLGPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAAKAPEDSGLQWTAMALPALISLVIGFAFGALYWKKKQSSLTRAVENIQINEEDNEISMLQQKEREFQEV", "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: [Soluble KIT ligand]: Secreted. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Cytoplasm, cytoskeleton Cell membrane; Single-pass type I membrane protein Cytoplasm, cytoskeleton Cell projection, lamellipodium Cell projection, filopodium. SIMILARITY: Belongs to the SCF family."}
+{"protein": "MLPTAIVLTILLGIIAYIWGYPHWLDWREKQLFQRPLPPHWQAILGDRLPFYAQLSPQQRQKLEAKIQLFLQQKQFIGCNDFVLTDEVRLVIAAQACYLALELGSNPYPRLDTILVYPDAFQVRQITSPDGYVVEEEDTVRAGESWDRAGQLILAWGTIAWDLERWQDGHNVIFHEFAHQLDMGDGAMNGVPKLGRRNDYQRWQSIFASEYQQLLSQLENNLPTVIDPYGATNPCEFFAVVTETFFEKGQELQHNHGQLYQVLRKYYCLEPLINC", "text": "SIMILARITY: Belongs to the MtfA family."}
+{"protein": "MISITSAEVGMKINEWHRHIQKFNVTDAEMLKAEIERDIEVMEEDQDLLIYYQLMAFRHKIMLEYTLPSDENRMELSEYLNKIEGHKKKLDNMRAYYYNFFRGMYEFRNGEYTRAITYYKKAERKIPTISDKIEKAEFYFKLSEVYYHMKMTHISMHYAELSYNIYKKHELYSVRRIQCHFVIAGNYDDLENHEKALPHLQEALKGAELLKSKNTHIYATAFFNLGNCYHKMDNLNKAARYIEQALVQYRKINSDVLPQAYHDLALIYFKQGKKEQAMDCFRKGIRSAVDFKDELFMNLFEALDVLYIRNGDTPKLLNIFSRLENGKGYPYLEELALLGGNLFDYNGKIEDSIICFKKMVYAQKQISKGECMYEI", "text": "FUNCTION: Involved in the regulation of sporulation (PubMed:10629174). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:10629174). Probably plays a dispensable role in the overall context of sporulation initiation (PubMed:10629174). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rap family."}
+{"protein": "MGAWASRGRAARVPAPEPESEPEEALDLSQLPPELLLVVLSHVPPRTLLGRCRQVCRGWRALVDGQALWLLILARDHSATGRALLHLARSCQSPARNARPCPLGRFCARRPIGRNPCGQGLRKWMVQHGGDGWVVEENRTTVPGAPSQTCFVTSFSWCRKKQVLDLEEEGLWPELLDSGRIEICVSDWWGARHDSGCMYRLLVQLLDANQTVLDKFSAVPDPIPQWNNNACLHVTHVFSNIKMGVRFVSFEHWGQDTQFWAGHYGARVTNSSVIVRVHLS", "text": "FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Able to recognize and bind complex-type oligosaccharides."}
+{"protein": "MKLNKLNPRWDAYDRRDSFWLQLLCLKYLGLWPPEDTDQATRNRYIAYGWALRIMFLHLYALTQALYFKDVKDINDIANALFVLMTQVTLIYKLEKFNYNIARIQACLRKLNCTLYHPKQREEFSPVLQSMSGVFWLMIFLMFVAIFTIIMWVMSPAFDNERRLPVPAWFPVDYHHSDIVYGVLFLYQTIGIVMSATYNFSTDTMFSGLMLHINGQIVRLGSMVKKLGHDVPPERQLVATDAEWKEMRKRIDHHSKVYGTMYAKVTECVLFHKDILSFGDEVQDIFQGSIFAQVCASVIIICMTLLQATGDDVTMADLLGCGFYLLVMTSQVFIFCYVGNEISYTTDKFTEFVGFSNYFKFDKRTSQAMIFFLQMTLKDVHIKVGSVLKVTLNLHTFLQIMKLSYSYLAVLQSMESE", "text": "FUNCTION: Odorant receptor which plays a critical role in the anthropophilic host-seeking behavior; establishes the host preference to transmit malaria. May participate in the phenomenon of decreased host-seeking behavior in disease vector mosquitoes after blood feeding. 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": "MPRARKGNTPRKGGQRRGGGARSSAQADSGSSEDEAASEARSTTSECPSLLSTTAEDSLGGDTVDEQGPQEDLEEKLKEYVDGLTDKSAKTRQGALESLRLALASRLLPDFLLERRFTLADALEKCLKKGKGEEQALAAAVLGLLCVQLGPGPKGEELFHSLQPLLLSVLSDSTASPAARLHCASALGLGCYVAAADVQDLVSCLACLEGVFSRSCGTGSSTSHVAPASLHGVCCAALQAWALLLTICPSAHISHILDRQLPRLPQLLSSESVNLRIAAGETIALLFELARDLEEDFVYEDMEALCSTLRTLATDSNKYRAKADRRRQRSTFRAVLHYVEGGECEEETVRFGLEVLYVDSWARHRVYTSFKEALGSGLHHHLQNNELLRDIFGLGPVLVLDATALKACKISRFEKHLYNAAAFKARTKARSRVRDKRADIL", "text": "FUNCTION: Ribosome-binding protein that acts as an inhibitor of mRNA translation by promoting ribosome inactivation (PubMed:30355441). Associates with the P- and E-sites of the ribosome and inserts a C- terminal helix into the mRNA exit channel to preclude translation (PubMed:30355441). SIMILARITY: Belongs to the IFRD family."}
+{"protein": "MMPLAGIAWNLMLLFSAVQGLPLQDGEGTQHPDLLNNPPKGSVEPVALEQLVHQAILKKDFLAQDVFFPGTTAIPTRAAPISLTEGVSDASGVLTTAVGGAFSLPPQLSTLIPPSPAPTGGPGPSPEAEEETTTTLITTTTVTTVHSPVLCNNNISESEGLLEAPEYGGSTFFGGLDCTYSVSVYLGYGVEIRVERLNLSKEEALSIEGLEEDRRFLLANETLMAEGQVIRSPTNHVAVRFQTYRATSPGAFRLRYQAFVLSCVFPPRPENGEVTVTDLHPGGAANFRCSAGFTLKGGESLVCLNISRPEWSGKPPVCAASCGGVIRNATVGRIVSPDISTSHSNNHGNNLSCHWLIEAAEGQRLHLHFERVSLDEDNDRLVVRSGSSPLSPVIYDSDIDDVPERGLLSDAQSLYIELISDNPAVPLLLSLRYEVFSESRCYEPFLAHGNFTTTDPLYSPGSLVSFFCNAGYMLEQGPPVIECVDPADPHWNESEPVCKALCGGEISEPAGVILSPDWPQNYGKGQDCVWGIHVQEDRRVLLEIEILNIRRSDALTVYDGDDLTARVLGQYMGVHQRFNLFSSANDVTLQFQSDSNDPVFSLSQGFIIHFKEVPRNDTCPALPEVPNGWKTSSHPDLIRGTVVTYQCEPGYDISGSDILTCQWDLSWSNAPPTCEKILNCADPGEIANGVRRASDPRFPIGSHVQYSCNEGYTLEGSRTLTCYNRDTGTPKWSDRIPKCVLKYEPCLNPGVPENGYQTLYKHHYQAGEALRFFCYEGFELIGEVTITCAPGHPSQWTSQPPLCKVAYEELLDDRKLEVTQTTDPSHQMEGGNIALAIFLPIILVILLIGGIYIYYTKFQGKSLFGFSFPASHSYSPITVESDFNNPLYEAGDTREYEVSI", "text": "FUNCTION: May play a role in cell-cell recognition and in neuronal membrane signaling. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the SEZ6 family."}
+{"protein": "MLGLTQHAQKVWRMKPFSPEVSPGSSPATAGHLLRISTLFLTLLELAQVCRGSVVSNRPFITVWNGDTHWCLTEYGVDVDVSVFDVVANKEQSFQGSNMTIFYREELGTYPYYTPTGEPVFGGLPQNASLVTHLAHTFQDIKAAMPEPDFSGLAVIDWEAWRPRWAFNWDSKDIYRQRSMELVQAEHPDWPETLVEAAAKNQFQEAAEAWMAGTLQLGQVLRPRGLWGYYGFPDCYNNDFLSLNYTGQCPVFVRDQNDQLGWLWNQSYALYPSIYLPAALMGTEKSQMYVRHRVQEALRVAIVSRDPHVPVMPYVQIFYEMTDYLLPLEELEHSLGESAAQGVAGAVLWLSSDKTSTKESCQAIKAYMDSTLGPFIVNVTSAALLCSEALCSGHGRCVRHPSYPEALLTLNPASFSIELTHDGRPPSLKGTLSLKDRAQMAMKFRCRCYRGWRGKWCDKRGM", "text": "FUNCTION: May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth. SUBCELLULAR LOCATION: Secreted Lysosome. SIMILARITY: Belongs to the glycosyl hydrolase 56 family."}
+{"protein": "DKLIGSCVWGATNYTSDCNAECKRRGYKGGHCGSFWNVNCWCEE", "text": "FUNCTION: Has antibacterial activity against the Gram-positive bacterium S.lutea (MIC=1.9 uM). Lacks antibacterial activity against the Gram-positive bacteria L.monocytogenes and M.luteus, and the Gram- negative bacteria E.coli D31, E.coli ATCC 25922, and S.typhimurium. Has antifungal activity against A.niger (MIC=2.9 uM), C.albicans (MIC=2.9 uM), C.fructus (MIC=2.9 uM), C.wickerhamii (MIC=2.9 uM), P.pastoris (MIC=2.9 uM), P.stiptis (MIC=2.9 uM), P.tannophilus (MIC=2.9 uM), T.harzianum (MIC=2.9 uM), and Z.marxianus (MIC=2.9 uM), but lacks antifungal activity against C.albidus, F.oxysporum, and S.cerevisiae. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the invertebrate defensin family. Type 2 subfamily."}
+{"protein": "MARLGLAVCAASFHLFLLLASTSSLRRAPTEADTANHARRTAYHFQPAKNWQNDPNGPMYHNGMYHLFYQYNPHSALWDIGNLSWGHSVSGDLLNWAALDTALDPTSPFDANGCWSGSATILPGALPAILYTGIDASKEQVQNVAFAKNPSDPLLREWEKPAYNPVIALPADVPGDKFRDPSTAWLGRDGLWRIAVSAEVDGVASTLVYRSKDFVRWERNAAPLHASRAAGMVECPDLFPVAERGEDGLDTSANGAGGVRHVLKLSVMDTLQDYYMVGTYDDAADAFSPAEPERGDDCRSWRRLDYGHLYASKSFFDVRKNRRVLWAWANESDSQADDVARGWSGVQTFPRKMWLAKDGKQLLQWPIEEIETLRRKRAGLWRGTRLGVGAVQEIVGVASSQADVEVVFKIPSLEEAERVDDPNRLLDPQKLCGEKGAAVRGGVGPFGLLVMASGDLHEHTAVFFRVFRHHDKYKLLMCTDLTKSSTRAGVYKPAYGGFVDMDIDDHKTISLRTLIDHSVVESFGGGGRACITARVYPEHVATSSSHLYVFNNGSDAVKVAKLEAWDLATATVNVVVGDHHGLVAPALELEPTRTTQ", "text": "FUNCTION: May play a role in sucrose partitioning during seed development. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast Secreted, cell wall Note=Associated to the cell wall. SIMILARITY: Belongs to the glycosyl hydrolase 32 family."}
+{"protein": "MAEVNRIHYELEYTEGISQQMRIPERLKIASGSSEEPPGLLNASHSTMMLVPERIVIAGDDNDARFGRPRDLDLIQSTPLETVELKTPPRVLTLNDQPLDFLEPEPAANSTAQPREEMKSHFRSRREQCRSENSTMRRNGQINKHDFASPSPSRAPVRVCPPLISPEDSQNLNSASGVLNYIKSTTRRAYQQVLEVLDDSQRGRASLVTFDASVENTPDDAGLTDAASLRRQIIKLNRRLQLLEHENKERAKREMVMYSLTVAFWLVNSWIWLRR", "text": "FUNCTION: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein Peroxisome. SIMILARITY: Belongs to the Tango11 family."}
+{"protein": "MPYSNLHPSIPRPRSYRFKLAAFVLLVGSLMSLWMTGEPPSHTLHYLALHVASQQLGLLLKKLCCLAEELCHVQSRYQGSYWKAVRACVGSPICFMALILLSFYFYCSLENTSDLRLAWHLGILVLSKSLSMTLDLQSLAPAEVSAVCEEKNFNVAHGLAWSYYIGYLKLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDDLSVADPNIRFRDMLPQQNTDRAGVKNRAYSNSVYELLENGQPAGACILEYATPLQTLFAMSQDGKAGFSREDRLEQAKLFCRTLEEILADVPESRNHCRLIVYQESEEGNSFSLSQEVLRHIRQEEKEEVTMSGPPTSVAPRPSLLSQEPRLLISGMEQPLPLRTDLI", "text": "FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:26669264). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (PubMed:26669264). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). Exhibits 2',3' phosphodiester linkage- specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'- cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26669264). The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation (By similarity). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cytoplasm, perinuclear region Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein Mitochondrion outer membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. SIMILARITY: Belongs to the STING family."}
+{"protein": "MRTRRVYLPLKGELSMDWHDYLGPLGRGAWVTIQFTLYSMFFGAVCSFAFGIGKLSKNPFVKGFSILYIEIFRGTSLLVQLFWLFFALPIAGDMMGIDLRLSPVVAGVLALSLNLGAYGAEIVRGAIQAVSPSQYEAATALNFSSSQALWRVALPQAIPEMMPSFSNLAIAALKDTSLVSLITLHDLTFAAEQLRNFYQDSTTVYTMVLLMYFGIALVLSFFMRLIESSVTRWRGHRR", "text": "FUNCTION: Probably part of the binding-protein-dependent transport system y4tEFGH 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": "MPTLPRGLRFGSNGEVLNDFEALWFPERHTVDLSNGTCKLTGYITNLPGYSDIFPNKGVTAARTPYRSTVPVNHLGYRPVTTVEYIPDGTYVRLDGHVKFEGDLVNGSVDLTNFVISLAAQGGFDYQSVIGPRFSARFSAFSTKYGVLLGEGRETLKYLLLVVRRMREGYRAVRRGDLKRLRNVISTFEPSTIKGKRARAEFSQTYRDKLTGNKVEVRPSEGKWNSSSASDLWLEFRYGLMPLFYDIQSVMEDFMRVHKKIAKIQRFSAGHGKLETVSSRFYPDVHFSLEVTAVLQRRHRWGVIYQDTGSFATFNNGRLVPVKDWKTAAFALLNPAEVAWEVTPYSFVVDWFVNVGDMLEQMGQLYRHVDVVDGFDRKDIKLKSVSVRVLTNDVAHVASFQLRQAKLLHSYYSRVHTVAFPQISPQLDTEIRSVKHVIDSIALLTQRVKR", "text": "FUNCTION: Induces host cell lysis. Inhibits host MurA activity thereby blocking the synthesis of murein precursors necessary for the host cell wall biosynthesis. May be responsible for the attachment to the host pilus. SUBCELLULAR LOCATION: Virion Note=A single copy of the maturation protein is present in the virion. SIMILARITY: Belongs to the Leviviricetes maturation protein family."}
+{"protein": "MERPAPLAVLPFSDPAHALSLLRGLSQLRAERKFLDVTLEAAGGRDFPAHRAVLAAASPYFRAMFAGQLRESRAERVRLHGVPPDMLQLLLDFSYTGRVAVSGDNAEPLLRAADLLQFPAVKEACGAFLQQQLDLANCLDMQDFAEAFSCSGLASAAQRFILRHVGELGAEQLERLPLARLLRYLRDDGLCVPKEEAAYQLALRWVRADPPRRAAHWPQLLEAVRLPFVRRFYLLAHVEAEPLVARCPPCLRLLREARDFQAARYDRHDRGPCPRMRPRPSTGLAEILVLVGGCDQDCDELVTVDCYNPQTGQWRYLAEFPDHLGGGYSIVALGNDIYVTGGSDGSRLYDCVWRYNSSVNEWTEVAPMLKAREYHSSSVLNGLLYVVAADSTERYDHATDSWEALQPMTYPMDNCSTTACRGRLYAIGSLAGKETMVIQCYDPDTDLWSMVNCGQLPPWSFAPKTVTLNGLMYFVRDDSAEVDVYNPTKDEWDKIPSMNQVHVGGSLAALGGKLYVSGGYDNTFELSDVVEAYDPETRAWSVVGRLPEPTFWHGSVSIFRQFMPQTPAGGRGFELNSGSSDVDAGHHRLPQNPEELQ", "text": "FUNCTION: Substrate-specific adapter of BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Note=Localizes to the spindle midzone and targets CUL3 to this region."}
+{"protein": "MPSMGIDLGTTYSCVGVCNEKGRIEIIANDQGNRTTPSYVSFNNRECLIGDDAMNQVAMNPVNTIFDVKRLFGRKYSDSVVQSDMKLWPFKVIANKFDDKPLIQVDFKGETKTFSPEEISSMVLSKMKEIVEQHLGEPVTDAVITVPAYFNDRQRHATKYAGTISNLNVLRIINEPTATAIAYGLHRRGIDDMKVLIIDLGGGTFDVSLFNIEDGIYEILLSGGDNHLGGADFNNRLMNHFIDEFKLKHKKDITNNQRAIFRLRTACERAKRTLSISSLASIEIDSLYDGIDFYSTITRTHFEKLCSDLFHSCIDHVETILNKCKLDKSLVDEIVLAGGSTQIPKIQRMFKEYFNGKEFNNSINPDEVVAYGAAVQSGVISGKGSNFPQLIFLNVTPLSMGIETVGGIMTNLVERNTHIPIKKTQTFSTQYDNQTNVLIQIYEGERTMTKDNNLIGTFELNGIPPAPRGVTQIEVCFDVDIDGILTVSAEDKTTKKVQKITISNINDHLSKVEIEKMIVDGEKFKQQDQQQKKELIESNYKIYCGDENTLDFEITQKLLGSAQSTEMNE", "text": "FUNCTION: May function in protein folding and assembly, and disassembly of protein complexes. SIMILARITY: Belongs to the heat shock protein 70 family."}
+{"protein": "MVLKTELCRFSGAKIYPGRGIRFIRGDSQVFLFVNSKCKRYFHNRLKPSKLTWTAMFRKQHKKDAAQEAVKKRRRATKKPYSRSIVGATLEVIQKKRTEKPEVRDAAREAALREIKERIKKTKDEKKAKKAEVASKAQKSQGKGNVQKGALPKGPKMGGGGGKA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family."}
+{"protein": "MKFAISTLLIILQAAAVFAAFPISDITVVSERTDASTAYLSDWFVVSFVFSTAGSDETIAGDATIEVSIPNELEFVQYPDSVDPSVSEFFTTAGVQVLSTAFDYDSHVLTFTFSDPGQVITDLEGVVFFTLKLSEQFTESASPGQHTFDFETSDQTYSPSVDLVALDRSQPIKLSNAVTGGVEWFVDIPGAFGDITNIDISTVQTPGTFDCSEVKYAVGSSLNEFGDFTPQDRTTFFSNSSSGEWIPITPASGLPVESFECGDGTISLSFAGELADDEVLRVSFLSNLADDVLEVQNVVNVDLTTADSRKRALTSFVLDEPFYRASRTDTAAFEAFAAVPADGDITSTSTAITSVTATVTHTTVTSVCYVCAETPVTVTYTAPVITNPIYYTTKVHVCNVCAETPITYTVTIPCETDEYAPAKPTGTEGEKIVTVITKEGGDKYTKTYEEVTYTKTYPKGGHEDHIVTVKTKEGGEKVTKTYEEVTYTKGPEIVTVVTKEGGEKVTTTYHDVPEVVTVITKEGGEKVTTTYPATYPATYTEGHSAGVPTSASTPPQATYTVSEAQVNLGSKSAVGLLAIVPMLFLAI", "text": "FUNCTION: Putative adhesion protein. May be involved in cell-cell interaction, interacting with other proteins by salt bridges and hydrogen bonds. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Secreted, cell wall Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer."}
+{"protein": "MSRVLSRRDIADRIAKGQTIVIYEDSVLNLDKWIKFHPGGDKSIYHMIGRDATDEMNAYHDDQTITKFKIWKIGRIDYPWENMLPPIQGGRFSKIDERDDIGDYDINLTSKWRSVDESNQYTKIPKNDRLASEAEVKIYPKIPQGVVPSLDLKEAYEKKIVVDPAIVSENYDNERVYEDLTNFPSLDVKNQEWIASEYRKLHGEITAAGLYQCNYVRYLKEFLRIGTLFGISFYLLSLKWFAISAICLGFAWQQLVFIAHDAGHISITHNYQVDNIIGMTVASWIGGLSLGWWKRNHNVHHLVTNDPVHDPDIQHLPFFAVSTRLFHNVYSTYYDKFLWFDKFAQKVVPIQHYLYYPILCFGRFNLYRLSWMHVLLGQGPRRGKAAWFRYYELAGLSFFNYWFFYLIIYKQMPTNAERFKYVMISHIATMIVHVQITLSHFAMSTSDLGVTESFPMRQLRTSMDVDCPRWLDFFHGGLQFQVIHHLFPRLPRHNLRDAQSLVIKFCDKVGIKYSIYGFAAGNDVVISHLQQIAQQAHTMLECAKTMKKEATDTEFHTNKHVLAANVNEKRKQE", "text": "FUNCTION: Delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides. Required for the formation of the di-unsaturated sphingoid base (E,E)-sphinga- 4,8-dienine during glucosylceramide (GluCer) biosynthesis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
+{"protein": "MNLRNNKLHSSFIQRKAIKVISGINNFNVGQIFKIIHACEISKATYVDVARNPKIVSFIKSISSIPVCVSSIDPRALYESVLAGADLVEIGNFDCFYTNGVYLSNDQIIAIVKQVKYLLPYTDICVTIPHILKLHEQIYLAQKLESLGINLLQTEGSITNFSNEKLLEAKKINDNILYSTSMACCALSSVYSISKVVSLPVIASSGINGISASVALSYGASGIGIRSSVSKLGNIIDMSNYIDEMIFSTSKKLYDIDQNNLLYMATSNLSLNKCSII", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf23 family."}
+{"protein": "MQIEMEEKFEDWRGKEAISGKHGGIKAAFIACVVETMENMVFLACSTNFMMYFTKSMNYSTPKAATMVTNFVGTSFLLTIFGGFVADSFLTRFAAFVLFGSIELLGLIMLTLQAHITKLQPQGGKKPSTPQSTVLFTGLYAIAIGVGGVKGSLPAHGGDQIGTRNQRLISGFFNWYFFSVCLGGFLAVTLMVWIEENIGWSSSFTISTAVLASAIFVFVAGCPMYRFKRPAGSPLTRIVNVFVSAARNRNRFVTDAEVVTQNHNSTDKSIHHNKFKFLNKAKLNNKISATQVEETRTFLALLPIFGSTIIMNCCVAQMGTFSVQQGMVTNRKLSRSFEIPVASLNAIPLLCMLSSLALYELFGKRILSNSERSSSFNLKRIGYGLALTSISMAVAAIVEVKRKHEAVHNNIKISVFWLELQFVMLSLSDMLTVGGMLEFFFRESPASMRSMSTALGWCSTAMGFFLSSVLVEVVNGITGWLRDDLNESRLELFYLVLCVLNTLNLFNYIFWAKRY", "text": "FUNCTION: Involved in (+) and (-)-abscisic acid transport (ABA) and in gibberellin import. 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": "MGFTEKQEGLVKESWEVLKQDIPHSSLRFFSLILEIAPGAKNMFSFLRESEEIPQNNPKLKAHAVKVFKMTCESAIQLREKGEVVVADTTLKYLGTVHVKSGVKDPHFEVVKEALLRTIEEAIGEEKWNEEMKNAWGEAYDQLAEAIKAEMKNHHDETA", "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": "MVSRMVSTMLSGLLFWLASGWTPAFAYSPRTPDRVSEADIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPVGKTDDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGERRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE", "text": "FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro. SUBCELLULAR LOCATION: Secreted Note=Neuroendocrine and endocrine secretory granules. SIMILARITY: Belongs to the 7B2 family."}
+{"protein": "MEMIGGDDTDTEMYGALVTAQSLRLRHLHHCRENQCTSVLVKYIQAPVHLVWSLVRRFDQPQKYKPFISRCTVNGDPEIGCLREVNVKSGLPATTSTERLEQLDDEEHILGINIIGGDHRLKNYSSILTVHPEMIDGRSGTMVMESFVVDVPQGNTKDDTCYFVESLIKCNLKSLACVSERLAAQDITNSIATFCNASNGYREKNHTETNL", "text": "FUNCTION: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane Note=Localizes at the plasma membrane in the presence of a CAR protein. SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular receptor family."}
+{"protein": "MAASPGSGSANPRKFSEKIALHTQRQAEETRAFEQLMTDLTLSRVQFQKLQQLRLTQYHGGSLPNVSQLRNSAPEFQPSLHQADNVRGTRHHGLVERPARNRFHPLHRRSGDKPGRQFDGNAFAASYSSQHLDESWPRQQPPWKEEKHPGFRLTSALNRTNSDSALHTSALSTKPQDPYGGGGQSAWPAPYMGFCDGENDGHAEVAAFPGPLKEENLLNVPKPLPKHLWESKEIQSLSGRPRSCDVGGGNAFPHNGQNTGLSPFLGTLNTGGSLPDLTNLHYSAPLPASLDTSDHLFGSMSVGNSVGNLPAAMTHLGIRTSSGLQSSRSNPSIQATLSKMALSSSLKCHPQPSVANASALHPSLRLFSLSNPSLSTTNLSGPSRRRQPPVSPLTLSPGPEAHQGFSRQLSATSPLNPYPASQMVTSEQSPLSFLPTDAQAQVSPPPPYPTPQELPQPLLQQPHAQEPPTQQPQAAPSLPQSDFQLLTAQGSALTSFFPDVRFDQQPMRPSPAFPQQVPLVQQSHREPQDSFHLRPNPYSSCGSFPGTILTEDTNSNLFKGLSGGLSGMPEVSLDMDTPFPLEEELQIEPLSLDGLNMLSDSSMGLLDPSVEETFRADRL", "text": "FUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites (PubMed:29211348, PubMed:30611118). Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated (PubMed:29211348). Acts independently of CREB1 'Ser-133' phosphorylation (By similarity). Enhances the interaction of CREB1 with TAF4 (By similarity). Regulates the expression of specific CREB- activated genes such as the steroidogenic gene, StAR (By similarity). Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Appears to be mainly nuclear. Translocates to the nucleus following adenylyl cyclase or MAP kinase activation (PubMed:30611118). SIMILARITY: Belongs to the TORC family."}
+{"protein": "MGSCQSNENSEGNARNKEIEKQLNADKRAGSSIVKLLLLGAGECGKSTVLKQMQILHSNGFTEEEVNEKRAIVYNNTVSAMCTILRAMDGVLHLPLENGQKEAEKAIVMKVQENGEEGEALTEEVSRAIQSLWADPGVKKAFEMRSEYQLPDSAKYFLDNCQRISEPGYRPNDQDILYSRVATTGVVEVKFKIKELDFRVFDVGGQRSERRKWIHCFDNVESIIFITAISEYDQVLFEDETTNRMIESMQLFNSICNSTWFLSTAMILFMNKKDLFMEKIQRVNITTAFPDYEGGQNYEEAVAFIKQKFAELNLNPDKKTIYMHETCATDTNQVQLVISSVIDTIIQKNLQKAGMM", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. This specific G-alpha subunit plays an important role in olfaction and in cilia morphogenesis. Involved in chemotactic responses to attractants diacetyl, pyrazine, 2,4,5-trimethylthiazole, benzaldehyde, isoamyl alcohol, butanone and 2,3-pentanedione. Displays a redundant function with gpa-3 in chemotactic responses. Involved in avoidance responses to copper, sodium dodecyl sulfate and linoleic acid. Involved in osmotic avoidance and mechanosensory responses. Involved in specifying fan-like morphology of cilia of head sensory neurons AWC (By similarity). SUBCELLULAR LOCATION: Cell projection, cilium Cell projection, dendrite Note=In amphid neurons also weakly expressed in cell body. In phasmid neurons found only in cilia. SIMILARITY: Belongs to the G-alpha family."}
+{"protein": "MTDQDSKPRVTIALGTSSSSSSFKTKKPSRPTHTRRHHARASSNHYSSESEDDDDETGGQRTGRVQAITEISTYGDDNELENRDRSDRRRDRSRDRDRDRNRDGDRNRDRRRDNRSQDRDRHNNRSSRPSRDDDASRSRRRSTSRSRDRDHKPKDPKDLQEPETAPPKWGLTINPKSTTTATSSFHHQRQPRSPSPEEKPPQTLEEQALSSLLSLDNKGSSTASKRKRSHSPSSHDRDRSPDHSDYRAVPIDDFGATLLKQFGWDGKMRGKVKEVTHKHANLAGLGAKDAKGAEELDAWNQKISGRGGGDSRGRDSRPVRLEDYRREENKKKQRMEYRHGESSYKQERERERERRGDR", "text": "FUNCTION: Involved in spliceosome maturation and the first step of pre- mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SPP2 family."}
+{"protein": "MGQKESQFKVLWQLQTHEEYMKQTSSFLRDFNALERYNLKENFEALSSFDNGEKIWVEDAFTTFFGIPDVIQLSPFFYRSACSFGRDLNINRQRLTFSALARFLASYTGRHKDVWSDFESNLMIIASWCDSFPKFRVEVLKNSKQISRLIHSDVQNISNFFDQNFGIRRSNIYQLCLLLLCISKLKPGESVGCHINSFLDSMFVKEQKAAFYVLQGISPDISSNIIKPSYLLHFLESNPYFLKSLGSLFELALFPHSAHNQKVQDDVSPLNDFAILSPLIHAQICFFLPKSVWQVNGLTSLFRASFHGYSMYALERKMCNYHNPSILLIKAKKINANHKSSSRPISLDATIPRKYPPHCIGTDKAVPQKFGADFHNENILLGAYISTRWRQSHMGFFGDHSTLLFQLQPIHQVYYASNLDKNYCMFDKNVGLGFGLSRHKVTNKVQYDVPGVCMYIDDGLEYGLFRHAGDGAFKPATNYENFEYEERFLIQDLEVIGVDTTKPVEPIHIGL", "text": "FUNCTION: May be involved in a process influencing telomere capping. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the RTC5 family."}
+{"protein": "MNTADQARVGPADDGPAPSGEEEGEGGGEAGGKEPAADAAPGPSAAFRLMVTRREPAVKLQYAVSGLEPLAWSEDHRVSVSTARSIAVLELICDVHNPGQDLVIHRTSVPAPLNSCLLKVGSKTEVAECKEKFAASKDPTVSQTFMLDRVFNPEGKALPPMRGFKYTSWSPMGCDANGRCLLAALTMDNRLTIQANLNRLQWVQLVDLTEIYGERLYETSYRLSKNEAPEGNLGDFAEFQRRHSMQTPVRMEWSGICTTQQVKHNNECRDVGSVLLAVLFENGNIAVWQFQLPFVGKESISSCNTIESGITSPSVLFWWEYEHNNRKMSGLIVGSAFGPIKILPVNLKAVKGYFTLRQPVILWKEMDQLPVHSIKCVPLYHPYQKCSCSLVVAARGSYVFWCLLLISKAGLNVHNSHVTGLHSLPIVSMTADKQNGTVYTCSSDGKVRQLIPIFTDVALKFEHQLIKLSDVFGSVRTHGIAVSPCGAYLAIITTEGMINGLHPVNKNYQVQFVTLKTFEEAAAQLLESSVQNLFKQVDLIDLVRWKILKDKHIPQFLQEALEKKIESSGVTYFWRFKLFLLRILYQSMQKTPSEALWKPTHEDSKILLVDSPGMGNADDEQQEEGTSSKQVVKQGLQERSKEGDVEEPTDDSLPTTGDAGGREPMEEKLLEIQGKIEAVEMHLTREHMKRVLGEVYLHTWITENTSIPTRGLCNFLMSDEEYDDRTARVLIGHISKKMNKQTFPEHCSLCKEILPFTDRKQAVCSNGHIWLRCFLTYQSCQSLIYRRCLLHDSIARHPAPEDPDWIKRLLQSPCPFCDSPVF", "text": "FUNCTION: Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus- associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIIC subunit 4 family."}
+{"protein": "MKDVTKVALLIARAMCASSGTFVFELAFSITEYTGRPLGGGRSKYARRRRAISIARCHRCYRLWPPTVFTTRCDNKHCVPGISYNVRVAQFIDEGVTEVIPSVINKRE", "text": "FUNCTION: Suppressor of viral-induced RNA silencing. Increases the accumulation of viral RNA and enhances viral cell-to-cell movement by inhibiting RNA silencing. SIMILARITY: Belongs to the carlaviruses nucleic acid-binding protein family."}
+{"protein": "MATMKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTHTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQRYPTVPTVMMDWAPFDGDSDLIQDNSLLGGDLATQYLIDKGHTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMRQLLSHPLRPQAVFTGNDAMAVGVYQALYQAELQVPQDIAVIGYDDIELASFMTPPLTTIHQPKDELGELAIDVLIHRITQPTLQQQRLQLTPILMERGSA", "text": "FUNCTION: Transcriptional repressor for the ribose rbsDACBK operon. RbsR binds to a region of perfect dyad symmetry spanning the rbs operon transcriptional start site. The affinity for the rbs operator is reduced by addition of ribose, consistent with ribose being the inducer of the operon. FUNCTION: Transcriptional repressor for the ribose rbsDACBK operon. RbsR binds to a region of perfect dyad symmetry spanning the rbs operon transcriptional start site. The affinity for the rbs operator is reduced by addition of ribose, consistent with ribose being the inducer of the operon (By similarity)."}
+{"protein": "MTDTKQLFIEAGQSQLFHNWESLSRKDQEELLSNLEQISSKRSPAKLLEDCQNAIKFSLANSSKDTGVEISPLPPTSYESLIGNSKKENEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDMVKDKKVEIPWYIMTSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKHFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAKDKDGLLKLRAGNIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDSVTGKYTKPTEPNGIKLEQFIFDVFDTVPLNKFGCLEVDRCKEFSPLKNGPGSKNDNPETSRLAYLKLGTSWLEDAGAIVKDGVLVEVSSKLSYAGENLSQFKGKVFDRSGIVLEK", "text": "FUNCTION: UDP-N-acetylglucosamine pyrophosphorylase that utilizes N- acetylglucosamine-1-phosphate as substrate (PubMed:9603950). Together with AGM1, is involved in the production of UDP-N-acetylglucosamine from N-acetylglucosamine-6-phosphate (PubMed:9603950). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UDPGP type 1 family."}
+{"protein": "MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI", "text": "FUNCTION: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. 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": "MADDLKRFLYKKLPSVEGLHAIVVSDRDGVPVIKVANDNAPEHALRPGFLSTFALATDQGSKLGLSKNKSIICYYNTYQVVQFNRLPLVVSFIASSNANTGLIVSLEKELAPLFEELRQVVEVS", "text": "FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V- ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2 (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the LAMTOR3 family."}
+{"protein": "MVADPPKGDPKGLAAVEPTANGAPAQDPLEDSGAAVGRCCSSRDQVRRCLRANLLVLLTVVAVVAGVALGLAVSGAGGALALGPARLIAFAFPGELLLRLLKMIILPLVVCSLVGGAASLDPSALGRLGAWALLFFLVTTLLASALGVGLALALQPGAAFAAMNASLSSTGAVEQTPSKQVLDSFLDLLRNIFPSNLVSAAFRSYSTSYEEKNFNGTLVKVPVAHEEEGMNILGLVVFAIVFGVALRKLGPEGEPLIRFFNSFNDATMVLVSWIMWYAPVGILFLVASKIVEMDDVGVLFASLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGILTPLAMAFGTSSSSATLPLMMKCVEERNGVAKHISRFVLPIGATVNMDGAALFQCVAAVFIAQLNRQSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAVSLPVSEISLILAVDWLVDRSCTIINVEGDAFGAGLLQHYVDRTEQRGSEPELTQVKSEVPLGSLPAPNEEGNPLLRHSPGAAGDAGACEKESVM", "text": "FUNCTION: Sodium-coupled antiporter of neutral amino acids. In a tri- substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (By similarity) (PubMed:9227483). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (By similarity). The transport cycle is usually pH-independent, with the exception of L- glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (By similarity). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (By similarity). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Melanosome. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. SLC1A5 subfamily."}
+{"protein": "GLWSTIKQKGKEAAIAAAKAAGQAALGAL", "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). FUNCTION: Has antibacterial activity against the Gram-positive bacteria S.aureus (MIC=5.7 uM), S.dysgalactiae (MIC=5.7 uM), Nocardia sp (MIC=22.9 uM) and S.uberis (MIC=5.7 uM), and the Gram-negative bacteria P.aeruginosa, E.coli and A.calcoaceticus. Has antiprotozoal activity against T.cruzi. Has antifungal activity against the yeasts C.tropicalis (MIC=0.37 uM), C.guilliermondii (MIC=22.9 uM), C.albicans (MIC=5.7 uM) and C.albicans ATCC 1023 (MIC=5.7 uM). Lacks hemolytic activity against human and murine erythrocytes. Does not cause morphological changes in murine liver, spleen and kidney. Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes. FUNCTION: Has antibacterial activity against the Gram-negative bacterium E.coli and the Gram-positive bacterium S.aureus (PubMed:16844081). Has antiprotozoal activity against L.amazonensis (PubMed:16844081). Has antifungal activity (By similarity). Has no hemolytic activity (PubMed:16844081). SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
+{"protein": "MSDPIRTKPKSSMQIDNAPTPHNTPASVLNPSYLKNGNPVRAQAQEQDDKIGTINEEDILANQPLLLQSIQDRLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFFNFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKLIPRAVDWFTGAALEFEFEEDEEEADEDEDEEEDDDHGLEDDDGESAEEQDDFAGRPEQAPECKQS", "text": "FUNCTION: Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Bud neck. Note=Phosphorylation by CK2 promotes the import into the nucleus. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
+{"protein": "MIGKVAGTAAIAGISFLAGKYSNDDLPIFRNVQSATNVPMNQIQVSEPMTVKPASLNADAMGPSRSAEIMKHGYPGFTNVRTYEDFVLSYDYKTRTAHWVCEHLTPERLKHAEGVDRKLCEFKPDITFPQKFLSQNTDYKCSGFDRGHLAAAGNHRKSQLAVDQTFYLSNMSPQVGRGFNRDKWNDLEMHCRRVAKKMINSYIITGPLYLPKLEGDGKKYIKYQVIGDNNVAVPTHFFKVALFEVTPGKFELESYILPNAVIEDTVEISKFHVPLDAVERSAGLEIFARLDPKSIVKENGAKKGGLLW", "text": "FUNCTION: Endonuclease important for programmed cell death; it mediates apoptotic DNA fragmentation. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family."}
+{"protein": "MKASVVLSLIGYLVVPSDTAVLGRCVVAKKLHEGGLSDFEGYSLENWVCLAYFESKFNPMAVYENSRSDFIGYGLFQIRNHDWCDHGRNRCHMSCSALLNPDLKKTIECAKTIVKGKRGMGAWPSWTLNCQHSDTLARWLDGCKL", "text": "FUNCTION: May be involved in fertilization (By similarity). Has no detectable bacteriolytic and lysozyme activities in vitro (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasmic vesicle, secretory vesicle, acrosome Cell projection, cilium, flagellum Note=Found in the principal piece of sperm tail. SIMILARITY: Belongs to the glycosyl hydrolase 22 family."}
+{"protein": "MSGRRELCTPLRTIMTPGPVEVDPRVLRVMSTPVVGQFDPAFTGIMNETMEMLRELFQTKNRWAYPIDGTSRAGIEAVLASVIEPEDDVLIPIYGRFGYLLTEIAERYGANVHMLECEWGTVFDPEDIIREIKKVKPKIVAMVHGETSTGRIHPLKAIGEACRTEDALFIVDAVATIGGCEVKVDEWKIDAAIGGTQKCLSVPSGMAPITYNERVADVIAARKKVERGIATQADRAALSGNRPITSNYFDLSQLEDYWSERRLNHHTEATTMLYALREGVRLVLEEGLETRFERHRHHEAALAAGIKAMGLRLFGDDSCKMPVVTCVEIPGGIDGESVRDMLLAQFGIEIASSFGPLAGKIWRIGTMGYSCRKENVLFVLAGLEAVLLRHNAGIEAGKALQAALDVYENAGRQAAV", "text": "FUNCTION: Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MLFTASLLLLLPWASAAPANLPIVDLGYQRHQAISFNSTGQYYSFTNIRYAEPPLGSRRFAPPVAPHGRSKNIVNGTGLGYKCPQALACWFNVQNKFTSAAAAGTPFDFNAAYEEVYTKDACTEPAKQDPLQSEDCLFLDVYVPQDVWQKGPQAAHQKGGAPVLVYLQDGAYVGGSKSDQNPAGLIARSREEGSSGMIYVGINYRLGVFGWLSGRKFTSSGGKPNAGLLDQRLALEWIQRHIHLFGGDPSRVTVMGVSAGGGSIIMQMTAYGRGISPPFAQVITQSPAWEPGTKTPAIEDDLFDTFLASLNVTSLDQARRLPSHALTDANYRLVASRPYGAGVLGPAIDGDFIPDSPKRLLLQGKANPGVRVLTSYTAAEGFGIAPANITDEASFQRYVGLMLAGTDASVRTHAATVLYPAVFDGSMPYRTQHDRASLLWADLAASCNTRYLHAAVRTPGYAIEYSVPPALHLSDTPSVFYNGPVADPTVNGTIAELLQRQIVRFVKTGNPNGEPDPEVPVYDGRDLLDLGDDGVLVRPDSTDNARCEYWQKVHF", "text": "FUNCTION: Carboxylesterase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (By similarity). The function of patB in patulin synthesis has still to be characterized (By similarity). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (PubMed:19383676) (Probable). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
+{"protein": "MFVVRRSIVFQQSRRQFSGSIAWLQACSSCGIKLQSKNPALIGYYTKPKPLEVGKVETLEDVKYMLFSQDIQKIKEIEDGTTLEDEKNRIPHSLICKRCSDAVHQNKYDVMDFKNCSLKEVIRSVPNDKPIVSIASLPEFPFHVNKNILENEKESVLVFTKADQVLKTSSATSTRLPIFFKDYFKYHLGLQVNKVLAVSSLKKWNLSGLLSNLRNNSYFLGNPNVGKSTLMNSLIQRYNGTKLDFNSNISDDMVNDAQHKHLRKAQLAGVSHIPNLTRECQGYQVDKKRIYDLPGYSENVDELPLERIVKSNWLEWVRKTNLFDTKKVKKKPYITIKGTENGRCYTIGGLFFLQPPPYSINQIIKFIPGEPYIFKNVTRALETFKSVYGNDTPHPLEKYCGINDEYCDITKYQRHVIPPFQGSIEIVFKDIGYILLRSTGRYSFNGLYEIWVPKGISVCIREPLEKLIEEGYVQYTESKNKISSCPKGRPLVSSTYIMDPNEEDTFAKIREMYLDRTENEISVRRLVKEDPLEVVSNKHDTPPNLYWHYKW", "text": "FUNCTION: May be involved in the mitochondrial lipid metabolism. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. GEP3 subfamily."}
+{"protein": "MHLSRYIAVLLSASSFVSALPLQNDVISDDGSKPIDAIMATAMEHKVVNPENLDATPATPENPEDLDKRFYYTGYKRNAETPEDLDKRFYYTGYKRNAETPEDLDKRFYYTGYKRNAETPEDLDKRFYYTGYKRNAETPEDLDKRFYYTGYKRNAETPEDLDKRFYYTGYKRNAETPDDLDKRFYYTGYKRNAETPDDLDKRFYYTGYKRNAETPEDLDKRFYYTGYKRNAETPEDLDKRFYYTGYKRNAETPEDLDKRFYYTGYKRNAETPEDLDK", "text": "FUNCTION: Ribosomally synthesized cyclic peptide asperipin-2a precursor; part of the gene cluster that mediates the biosynthesis of the asperipin-2a, a bicyclic peptide that possesses two macrocyclic ether rings consisting of 14- and 17-membered paracyclophans (PubMed:26703898, PubMed:30516224). The aprA translated product contains a 11-fold repeated peptide embedding the hexapeptide Phe-Tyr- Tyr-Thr-Gly-Tyr, that is converted into asperipin-2a (PubMed:30516224). After being excised from the precursor peptide by kexin proteases, the core peptides are cyclized and modified post-translationally by enzymes encoded within the corresponding gene cluster (PubMed:30516224)."}
+{"protein": "METPRLMCTQHPDSTVKVPVQEEVEEAVRSFLVYGCDEVMSDYEGKLTPYAQPKEIVVKAGELGVPVGEGFYVTVRAPNPRLEDFDRVDLALEAAVLANYYSYKRLGVQAVRWVVLPMTDSAETVRLVQRLLARKTRVLCEEVGQPCEQAQLVPLLEDVDSLLRVREILRDLHSALAELGSDPGVLRVFLGKSDSALKAGHIASALSLLYALGESAKAGEELGLEVKPILGGGSPPFRGGVNNPRLVGVEVQRYRGYSTVTVQSAVRYDASFSEYQEVRSKLLGGAGGEPGDAGGRVAELARLAASMYRSLASKYLDFVNEYARSVPTTRDRVSWREYGRALELEDKLFSAPRAIVYTAAWYSLGVPPTFLDADFVLEAYRGDFLDEVLGYLPGLEEEWRYDAQFYLPRLAGERLGEELVKKVDEALDAMGLRPEPLEPYEKLARTAPAELRALLLGKVRGFLG", "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": "MECYRMSNIVTCQPWEKFCYKEVTMFFPNHPVHLSGCASECTETNSKFCCTTDKCNGAGSG", "text": "FUNCTION: Shows no cytotoxicity and does not inhibit the binding of alpha-bungarotoxin to nicotinic acetylcholine receptors of muscle and alpha-7/CHRNA7 types. However, it potentiates the binding of alpha- bungarotoxin to the acetylcholine-binding protein from Lymnaea stagnalis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily."}
+{"protein": "MFEARLVQGSILKKVLEALKDLIDEACWDITSSGISLQSMDSSHVSLVQLTLRSDGFDTYRCDRNQSIGVKMSSMSKILKCAASDDIITLRAEDNADTVTMVFESPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVIKMPSGEFARICRDLSQIGDAVVISCAKDGVKFSASGELGTGNVKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSPTVILSMSADIPLVVEYKIADMEHVKYYLAPKIEDEEAS", "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. Promotes 3'-5' nuclease activity of the DNA- endonuclease apex2.L in response to DNA damage (PubMed:28028224, PubMed:29361157). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PCNA family."}
+{"protein": "MKCPYCSSAQGRCTTTSSGRSITECSSCGRVMEERQTQNHHLFHLRAQDTPLCLVTSDLQTAAQPSPEDEEDPFEPTGFITAFSTWSLEPSPIFARSSLSFSGHLAELERTLELASSTSNSNSSTVVVDNLRAYMQIIDVASILGLDCDISEHAFQLFRDCCSATCLRNRSVEALATACLVQAIREAQEPRTLQEISIAANVQQKEIGKYIKILGEALQLSQPINSNSISVHMPRFCTLLQLNKSAQELATHIGEVVINKCFCTRRNPISISAAAIYLACQLEDKRKTQAEICKITGLTEVTLRKVYKELLENWDDLLPSNYTPAVPPEKAFPTTTISTTRSTTPRAVDPPEPSFVEKDKPSAKPIETFDHTYQQPKGKEDKQPKFRQPWLFGTASVMNPAEMISEPAKPNAMDYEKQQLDKQQQQQLGDKETLPIYLRDHNPFPSNPSPSTGISTINWSFRPSVVPGSSSNLPVIHPPKLPPGYAEIRGSGSRNADNPHGDF", "text": "FUNCTION: Plant-specific TFIIB-related protein that may be involved in an intracellular signaling pathway between plastids and the nucleus (PubMed:12697827). May act as general transcription factor (GTF) of RNA polymerase I-dependent transcription and rRNA synthesis. Forms a ternary complex with TBP2 and the rDNA promoter region (PubMed:18668124). SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane; Peripheral membrane protein; Cytoplasmic side Nucleus Note=Localizes to the nucleus under conditions of proteasome inhibition."}
+{"protein": "MSQGPPAGGVLQSSVAAPGNQPQSPKDDDRKVRRREKNRVAAQRSRKKQTQKSDKLHEEHESLEQENSVLRREIAKLKEELRHLTEALKEHEKMCPLLLCPMNFVQLRPDPVASWSAHDAPDHPSFIWLGTLV", "text": "FUNCTION: AP-1 family transcription factor that controls the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes. Required for development of CD8- alpha(+) classical dendritic cells (cDCs) and related CD103(+) dendritic cells that cross-present antigens to CD8 T-cells and produce interleukin-12 (IL12) in response to pathogens (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
+{"protein": "MMKCLFLLCLCLFPILVFSSTFTSQNPINLPSESPVPKRVLDTNGKKLNPNSSYRIISTFWGALGGDVYLGKSPNSDAPCPDGVFRYNSDVGPSGTPVRFIPLSGANIFEDQLLNIQFNIPTVKLCGSYTIWKVGNINAHLRTMLLETGGTIGQADSSYFKIVKSSKFGYNLLYCPLTRHFLCPFCRDDNFCAKVGVVIQNGKRRLALVNENPLDVLFQEV", "text": "FUNCTION: Inhibitor of cathepsin D (aspartic protease). May also inhibit trypsin and chymotrypsin (serine proteases). Protects the plant by inhibiting proteases of invading organisms. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz- type inhibitor) family."}
+{"protein": "MSQQHTLPVTLSPALSQELLKTVPPPVNTQQEQMKQPTPLPPPCQKVLGELPVEVPSKQEEKHMTTVKGLPEQECEQQQQEPQEQELQQQHWEQHEEHQKAENPEQQLKQEKAQRDQQLNEHLEEEKKLLDQQLNQELIKRDEQLGIKKEQLLELTEQQEGQLEHLEQQEGQLELPEQQEGQLEHLEQQEGQLKHLDQQGKQPELPEQQVAQLKHLEQQEGQLKHLEHQKGELQVPEEQVGQLKYLEQQEGQLKHLDQQEKQPELPEQQVGQLKHLEQQEGQLEHMEHQEGQLGLPEQQVGQLKQLEEQEGQPKHLEEEEGQLKHLVQQEGQLEHLVQQERQLEQQEGKVQHLEQQVEQLKHLEEQEGQLKHLEQQQGQLEVSEQQVGQPKHLEQEGKQLELPEQQEGQLKHLEKQEAQLELPEQQVGQPKHPEQQEKQLEHPEQQEGQLKHLEQQEGQLKDLEQQKGQLEQQQGQLEQPVFAPAPGQVQDIQPVLPTKGEALLPVEQQQQKQEVQWPPKHK", "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": "MVSILSNIGMMVVTFKRPSLFTSLRRRSANNIIITKHSHPISTTRRSGNYKPTMWDFQFIQSLHNPYEGDKYMKRLNKLKKEVKKMMMTVEGSHDEELEKLELIDNLERLGVSYHFKDEIMQIMRSINININIAPPDSLYTTALKFRLLRQHGFHISQDILNDFKDENGNLKQSICKDTKDILNSSKDEHDNLKQSTCNNTKGLLKLYEASFLSIENESFLRNTTKSTLAHLMRYVDQNRCGEEDNMIVELVVHALELPRHWMVPRLETRWYISIYERMSNANPLLLELAKLDFNIVQATHQQDLRILSRWWKNTGLAEKLPFSRDILVENMFWAVGALFEPQHSYFRRLITKVIVFISIIDDIYDVYGTLDELELFTLAIQRWDTKAMEQLPDYMKVCYLALINIINEVAYEVLKNHDINVLPYLTKSWADLCKSYLQEAKWYHNGYKPNLEEYMDNARISIGVPMVLVHSLFLVTNQITKEALDSLTNYPDIIRWSATIFRLNDDLGTSSDELKRGDVSKSIQCYMNEKGASEEEAIEHIEFLIQETWEAMNTAQSKNSPLSETFIEVAKNITKASHFMYLHSDVKSSISKILFEPIIISNVAFALK", "text": "FUNCTION: Involved in monoterpene (C10) biosynthesis in glandular trichomes (PubMed:17440821). Converts geranyl diphosphate to linalool in glandular trichomes in response to jasmonate (JA) (PubMed:17440821). Can convert farnesyl diphosphate to nerolidol in vitro (PubMed:17440821). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily."}
+{"protein": "MASKSSFMATFNIVTLMLMVASSTVTARPLMKPSMGTSSPTTSLVYRLKLDEDTGYCWDSLMQLQHCSGELILFFLNGETYIGPGCCSAIRTIGRKCWPTMIGVLGFTAQEGDMLQGYCDGNDSDNNGEDHALASSTLPLSVNFKTTVVRSSASPSNP", "text": "FUNCTION: Involved in the regulation of gamete interactions during the double fertilization and to prevent multiple-pollen tube attraction; mediates the redistribution of the gamete fusogen HAP2/GCS1 to the cell surface after secretion upon sperm arrival. SUBCELLULAR LOCATION: Cytoplasmic vesicle Secreted Note=Secreted via vesicle exocytose upon sperm arrival, especially in the apical region of the degenerating synergid cell. SIMILARITY: Belongs to the plant egg cell-secreted peptide family."}
+{"protein": "MTGGRLVALLLLVAASLGLGQQPHPEPGLPGLQYSYDCGMRGMQLVVLPRPGRTIRFKVVDEFGNRFEVNNCSICFHWVSAEPQAPAVFSADYKGCHVLEKEGHSHLTVFIEAMLPDGHVEVAQEAVLICPKPGHTWAVGSHQVPPTTPSPTTPHALPFHLSSAHTFPIPLYLEHSLMLPTPAGPSLGPGPTPAVLAQVERWEVDKPDAVGSHLPQEWCQVASGHIPCIVQSSSKEACEQAGCCYDSAREVPCYYGNTATVQCFRNGYFILVVAQEMALAHRITLANVHLAYAPTRCPPAQKTSAFVIFHVPLTHCGTTVQVLGSQLFYENQLVSDIDVREGPQGSITRDSSFRLLVRCIFNASDFLPIQASIFSPPLPAPVTQAGPLRLELRIARDETFSSFYEEEDYPLVRLLREPVHVEVRLLQRTDPSLVLELHQCWATPSANPVQQPQWPLLSDGCPFKGDSYRTRVLALDRAELPFRSHYQRFTVATFTFLDSGAQRALRGLVYFFCSASACHPSGPETCSSTCSSRTAKRRRSSGYHDGTPRALDIVSSPGPVGFQDSHRQEPTLESTGSGRNSNPKPLLWVVLLLLAIALVLGIGVFVGLSQAWAHKLREGHRLTDQAQ", "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. ZP1 ensures the structural integrity of the zona pellucida (By similarity). SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 1]: Zona pellucida. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the ZP domain family. ZPB subfamily."}
+{"protein": "MSINRNLLNIIIILCICLNLGCNDGAQERETDSHTIQVSSLLPSSSSSCVLSPRASTTKSSLHVTHRHGTCSRLNNGKATSPDHVEILRLDQARVNSIHSKLSKKLATDHVSESKSTDLPAKDGSTLGSGNYIVTVGLGTPKNDLSLIFDTGSDLTWTQCQPCVRTCYDQKEPIFNPSKSTSYYNVSCSSAACGSLSSATGNAGSCSASNCIYGIQYGDQSFSVGFLAKEKFTLTNSDVFDGVYFGCGENNQGLFTGVAGLLGLGRDKLSFPSQTATAYNKIFSYCLPSSASYTGHLTFGSAGISRSVKFTPISTITDGTSFYGLNIVAITVGGQKLPIPSTVFSTPGALIDSGTVITRLPPKAYAALRSSFKAKMSKYPTTSGVSILDTCFDLSGFKTVTIPKVAFSFSGGAVVELGSKGIFYVFKISQVCLAFAGNSDDSNAAIFGNVQQQTLEVVYDGAGGRVGFAPNGCS", "text": "FUNCTION: Probably not redundant with AED1 and not involved in restriction of salicylic acid (SA) or systemic acquired resistance (SAR) signaling. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MSSSMCLARCSASLSAGNFPSRMFMGRLHAQRRTRTLQLRCAASLLPDQPTLAASSAISPVPSDLPEVLGDALHRLGAIYVLADASASTAAAAVMPTAVDSAAGAAPQRAGGWVAPVADALEQVLYALQEGLDKLHVPYSYGYSIILLTLIVKLLTYPLTKQQVESAMAVQALKPRIDLIKDRFGEDKDKIQKETSVLYEQAGVNPLAGCLPTLATIPIFIGLFSSLTNVANDGLLDTQGFYFVPSLAGPTTMAMRQSGLGTSWLWPLGPDGAPPIGWEDAAAYLTLPLLLVAVQYASSSVTSPPIDPKDENANTQRALLVFLPLMVGWFSLNVPAGLSLYYLANTVLSSAIQIYLKKLGGANVVMNELGPVTKPGSGRRNGVAAGEWSVWKPATVLTTAEAAKARAEAEEAVERAREAAEEAAAAAAFDNASVSLSVDDSTAAIAGTATMAVTAGAPAAAMDPSKVNRRCKRRRLTSLVQDGSTASAAVAGASA", "text": "FUNCTION: Required for the insertion of some light-harvesting complexes (LHC) proteins into the chloroplast thylakoid membrane. Essential for the assembly and activity of LHC I and II. Its function is probably partly distinct from that of ALB3.2. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC (TC 2.A.9.2) family."}
+{"protein": "MYLRRALIAGGSAAAAILGVVAAGKSKGGSDSEILSVAPPATGQWDRNWDRREPISMVNLSKINAETGEEELQLHLNKHKPKATRHIFLIRHSQYKLDGKTDFDRVLTPLGREQADLTGQRLASLGHKYNHIVYSTMTRAKETTEIISKYLPDVNKSSSDLLREGAPIRPEPQVCHWKPDFVYYEDGPRIEAAFRHFIHRADPKQEEDSYEILICHANVIRYVVCRALQFPPEAWLRISLNNGSITYLVIRPNGNVSIRMLGDSGFMPAEKISRT", "text": "FUNCTION: Displays phosphatase activity for serine/threonine residues. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics (By similarity). May be a central mediator for programmed necrosis (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
+{"protein": "MTANVTVSSMYLFTVLLLLFNVYVNSQDTDAQLCQMCEGTIRHDSPVWSFCITKGYVKGHCCFKNNTSDVDTIIGLDLSNCSISHVEHLYNSSTALIIDLSNNPISNLSDYVFQGFSQLTQLLLPSKLECPGGRASWEKVEVKSITRICEGQKNACNQTVQMPLVCPENSLCSPYGPGFFECSCLNNFHGYKCMRQGEFPLVKVLGILTASTVVVSSVLWFTQRRKVKNT", "text": "FUNCTION: Involved in osteoblast cell differentiation. May play a role in inducing the cell cycle arrest (By similarity). SUBCELLULAR LOCATION: Nucleus envelope Cell membrane; Single-pass membrane protein Lysosome membrane; Multi-pass membrane protein Note=Colocalizes with NELL1 on the nuclear envelope and the perinuclear region."}
+{"protein": "MKFLVSSDDTGVVKEVICNRGTDTSKQDATQPISVKNFCTEPNCSRKNRIIHMINYQEKYLVAIRIGGELSVYEIADDEYEIEDEYKYNLLHNYKLEVSSSDKPISLFTVDILEAVAVAFSSGKVFFVNFNDDKFDKEPVLVQLPGGKEIAEFSKNPSVEGIFGYGGEENDVRIVKLYESDITSEIFDTENVENNFKSEVVFTAKNVKNDHLDLRVPVWITKIRFFTEQPEKGYKFITATHYGQIRVYDTNHGRRPVRDFTVCQKPILTLTFANEEESEVIISDSHNLIAKHSLIQVDDKASKTHSASAGDIIKPVAKLLGRFVDQFGATYGVEVGEGLLVTGGLDRYLRVFDLASREIVAKVYVGVEVSSVVVLDYEEEESQEEIVGDVELLKKSEKRKRTLPVVEREESDEEDLWNQLEEKDIKRKKS", "text": "FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NSA1 family."}
+{"protein": "LECKDLGISIDDDNNRRLAVKEGDPLVVQFVNADREGN", "text": "FUNCTION: Inhibition of trypsin. SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz- type inhibitor) family."}
+{"protein": "MSSSYNTIALSSTPTFLLSSAAAGPGPNNFNRQEAAMTMVQQQPTSSVAPPPKKRRNQPGNPNPDAEVIALSPKTIMATNRFLCEVCNKGFQREQNLQLHRRGHNLPWKLKQKSNKEVRRKVYLCPEPSCVHHDPARALGDLTGIKKHYYRKHGEKKWKCDKCSKRYAVQSDWKAHSKTCGTKEYRCDCGTIFSRRDSYITHRAFCDALIQESARNPTVSFTAMAAGGGGGARHGFYGGASSALSHNHFGNNPNSGFTPLAAAGYNLNRSSSDKFEDFVPQATNPNPGPTNFLMQCSPNQGLLAQNNQSLMNHHGLISLGDNNNNNHNFFNLAYFQDTKNSDQTGVPSLFTNGADNNGPSALLRGLTSSSSSSVVVNDFGDCDHGNLQGLMNSLAATTDQQGRSPSLFDLHFANNLSMGGSDRLTLDFLGVNGGIVSTVNGRGGRSGGPPLDAEMKFSHPNHPYGKA", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Plastid, chloroplast."}
+{"protein": "MFARVFKAMPARASALTSVNASIPARFMATVRQQRPAHERATFTIRDGPIFHGKSFGARTNISGEAVFTTSLVGYPESLTDPSYRGQILVFTQPLIGNYGVPSAERDEHGLLKYFESPNLQAAGVVVADVAEQYSHWTAVESLGEWCAREGVPAISGVDTRAIVTYLRERGSSLARITVGEEYDADQDEAFTDPEQIHLVRQVSTKAPFHVSAADPQCHVAVIDCGVKENILRSLVSRGAGITVFPFDYPIHKVAHHFDGVFISNGPGDPTHCQETTYHLRRLMETSQVPIFGICLGHQLLALAAGARTIKLKYGNRAHNIPALDLSTGRCHITSQNHGYAVDASTLPSDWKPYFVNLNDSSNEGMIHKSRPIFSTQFHPEAKGGPLDSSYLFDIYIDSVKKYKASQAAFYPQRDSLPSPLLVDLLAKERVGVQPTIGMQNIAAAATAAAAAA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CarA family."}
+{"protein": "MRITDTAGFHAWFAERGAAHRYRITRTPLHDLEGWYTDPASGDVRHRSGRFFSIEGLRYGRQEPDGPAWTQPIIRQPETGVLGVLIKWFDGVPHLLMQAKMEPGNINTLQVSPTVQATFSNYTRVHHGSPVRYIDHFLTPGAGDRVHYDALQSEQGSWFLGKRNRNIVVETTGEIPVHEDFCWVPRPVMAELLRVDNLVNMDSRTVLAGLPDDPGEGSVPRRAVEKPLHDTAALLHWFTGAKVRHRPERTTIPLSRVGGWRRDDDRGEIVHETGRYFRIIGVDVEADSREVTSWSQPMLAPVGRGVVAFVSKEIHGERHLLVQARAEAGTFDAVELGPTVQCNPGNLPDGAPRPPYLDTVLTARPEQVLFDTVHSEEGGRFYHAENRYLVLDGDDVPVDVPEDYTWMTVRQLTRAGRIGNLVDVEARTLLACVRTLPDHGASR", "text": "FUNCTION: Involved in the biosynthesis of the 2,6-deoxysugar, dTDP-L- rhodinose, attached to the benzoisochromane quinone chromophore to produce the aglycone antibiotics granaticin and granaticin B. Catalyzes the removal of the hydroxyl group at position C-2 of the hexose ring of dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose, and the oxidation of the hydroxyl group at position C-3 to form a carbonyl functionality. The product of the reaction, dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose, is a highly unstable diketosugar, which spontaneously forms dTDP-3,4- didehydro-2,6-dideoxy-alpha-D-glucose. SIMILARITY: Belongs to the hexose 2,3-dehydratase family."}
+{"protein": "MAAVVPVTVELGFVEEAPAWRLRSEQFPSKVGGRPAWLALAELPGPGALACARCGRPLAFLLQVYAPLPGRDEAFHRSLFLFCCREPLCCAGLRVFRNQLPRKNAFYSYEPPSETGASDTECVCLQLKSGAHLCRVCGCLAPMTCSRCKQAHYCSKEHQTLDWQLGHKQACTQSDHLDHMVPDHNFLFPEFEIVTETEDEIGPEVVEMEDYSEVIGSMEGVPEEELDSMAKHESKEDHIFQKFKSKIALEPEQILRYGRGIKPIWISGENIPQEKDIPDCSCGAKRIFEFQVMPQLLNHLKADRLGTSVDWGILAVFTCAESCSLGIGYTEEFVWKQDVTETP", "text": "FUNCTION: May be a DNA-binding protein with a regulatory function. May play an important role in cell death and/or in regulation of cell proliferation. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MVATIDSIEMPALPTAVEAHPMKGGDDSHSYSQNSCYQKGVIDAAKAVIVEAVNEKLDLENNPIFDPIKPFRIADFGCSTGPNTFHAMQNIVESVETKYKSLQKTPEFHVFFNDHVNNDFNVLFRSLPPNREFFAAGVPGSFYTRVFPKNSIHFAHCSYALHWLSKVPKEIQDKNSLAYNKGRIHYTGTEKHVVKAYFGQFQRDFEGFLKARAQEIVVGGLMVIQIPGLPSGEVLFSRTGAGLLHFLLGTSLMELVNKGIINEESVDSFNLPQYHPSVEDLEMVIEMNDCFTIERVGTLPHPMKNLPFDVQRTSLQVRAIMECILTEHFGENILDPLFEIYTKNLQENFHVFDKEIRKDADLYLVLKRKGN", "text": "FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine and ajmalicine) biosynthesis pathway. Catalyzes the methylation of loganic acid (6S,7R) to produce loganin (PubMed:29399933, PubMed:18326827, PubMed:24104568). Weak activity with secologanic acid as substrate. Inactive on deoxyloganic, dehydrologanic, epiloganic and loganetic acid (PubMed:18326827). SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family."}
+{"protein": "MRVNVTLACTECGDRNYITTKNKRNNPERVEMKKFCSRENKQTLHRETK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
+{"protein": "MGLFRGFVFLLVLCLLHQSNTSFIKLNNNGFEDIVIVIDPSVPEDEKIIEQIEDMVTTASTYLFEATEKRFFFKNVSILIPENWKENPQYKRPKHENHKHADVIVAPPTLPGRDEPYTKQFTECGEKGEYIHFTPDLLLGKKQNEYGPPGKLFVHEWAHLRWGVFDEYNEDQPFYRAKSKKIEATRCSAGISGRNRVYKCQGGSCLSRACRIDSTTKLYGKDCQFFPDKVQTEKASIMFMQSIDSVVEFCNEKTHNQEAPSLQNIKCNFRSTWEVISNSEDFKNTIPMVTPPPPPVFSLLKISQRIVCLVLDKSGSMGGKDRLNRMNQAAKHFLLQTVENGSWVGMVHFDSTATIVNKLIQIKSSDERNTLMAGLPTYPLGGTSICSGIKYAFQVIGELHSQLDGSEVLLLTDGEDNTASSCIDEVKQSGAIVHFIALGRAADEAVIEMSKITGGSHFYVSDEAQNNGLIDAFGALTSGNTDLSQKSLQLESKGLTLNSNAWMNDTVIIDSTVGKDTFFLITWNSLPPSISLWDPSGTIMENFTVDATSKMAYLSIPGTAKVGTWAYNLQAKANPETLTITVTSRAANSSVPPITVNAKMNKDVNSFPSPMIVYAEILQGYVPVLGANVTAFIESQNGHTEVLELLDNGAGADSFKNDGVYSRYFTAYTENGRYSLKVRAHGGANTARLKLRPPLNRAAYIPGWVVNGEIEANPPRPEIDEDTQTTLEDFSRTASGGAFVVSQVPSLPLPDQYPPSQITDLDATVHEDKIILTWTAPGDNFDVGKVQRYIIRISASILDLRDSFDDALQVNTTDLSPKEANSKESFAFKPENISEENATHIFIAIKSIDKSNLTSKVSNIAQVTLFIPQANPDDIDPTPTPTPTPTPDKSHNSGVNISTLVLSVIGSVVIVNFILSTTI", "text": "FUNCTION: May be involved in mediating calcium-activated chloride conductance. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Apical cell membrane Secreted Note=The C-terminus 30 kDa form is anchored to the membrane. The N-terminus 110 kDa form is released from the membrane triggered by an unknown stimulus. SIMILARITY: Belongs to the CLCR family."}
+{"protein": "MLVALAAIGVTVLLFLIKALGSGAKKAPVTLLDPNAKYPLPLIEKQEISHDTKKFRFGLPSAEHVLGLPVGQHIYLSAKVNGSLVVRAYTPVSSDEVKGHVDLVVKVYYKNVNPKFPDGGKMSQHLDSLKIGETIDFRGPNGLLVYKGKGKFAIRPDKKAEPKIKVAKHVGMLAGGTGITPMLQLIRQITQDPNDNTKCYLIFANQTEDDILLRYELETVAKSHPEQFKLWYTLDRPPQGWKYGSGFVTADMIKEHLPPPSEDVLVLMCGPPPMIQFACQDNLTKLGYPEAGRFAY", "text": "FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis and drug metabolism. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family."}
+{"protein": "MNKIFSSHVMPFRALIDACWKEKYTAARFTRDLIAGITVGIIAIPLAMALAIGSGVAPQYGLYTAAVAGIVIALTGGSRFSVSGPTAAFVVILYPVSQQFGLAGLLVATLLSGIFLILMGLARFGRLIEYIPVSVTLGFTSGIGITIGTMQIKDFLGLQMAHVPEHYLQKVGALFMALPTINVGDAAIGIVTLGILVFWPRLGIRLPGHLPALLAGCAVMGIVNLLGGHVATIGSQFHYVLADGSQGNGIPQLLPQLVLPWDLPNSEFTLTWDSIRTLLPAAFSMAMLGAIESLLCAVVLDGMTGTKHKANSELVGQGLGNIIAPFFGGITATAAIARSAANVRAGATSPISAVIHSILVILALLVLAPLLSWLPLSAMAALLLMVAWNMSEAHKVVDLLRHAPKDDIIVMLLCMSLTVLFDMVIAISVGIVLASLLFMRRIARMTRLAPVVVDVPDDVLVLRVIGPLFFAAAEGLFTDLESRLEGKRIVILKWDAVPVLDAGGLDAFQRFVKRLPEGCELRVCNVEFQPLRTMARAGIQPIPGRLAFFPNRRAAMADL", "text": "FUNCTION: Responsible for the aerobic transport of succinate from the periplasm to the cytoplasm at acidic pH. FUNCTION: Responsible for the aerobic transport of succinate from the periplasm to the cytoplasm at acidic pH (PubMed:23278959). Can transport other C4-dicarboxylic acids such as aspartate and fumarate (PubMed:23278959). May also play a role in the regulation of C4- dicarboxylic acid metabolism at pH 7, via regulation of expression and/or activity of DctA. May act as a co-sensor of DcuS (PubMed:23278959). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family."}
+{"protein": "MSKLGTLGARLHHGEVGYDFVKNRKIWYGISILITITAIVGLAVRGLHMGIEFQGGAVFTTPKNMSASVAQTETWAEEASGHDAIVQKLGDGSLRIQIAGTDTQQSDQIKEDLSKNLDVSAEKINADLVGPSWGDQIANKAWQGLGIFMVLVVIYLAIAFEWRMALAAFVALIHDITITVGIYALVGFEVTPGTVIGLLTILGYSLYDTVVVFDSLKEQTRDITKQTRWTYAEIANRSINSTLVRSINTTVVALLPVAGLLFIGGGVLGAGMLNDISLSLFVGLAAGAYSSIFIATPLVADLKEAEPQMKALKKRVLAKRAQGAAKGESAESAADEGAYDADEPDDAAPAVVGPRNQPASRGRGRGRPSGKRR", "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": "MRYAFAAEATTCNAFWRNVDMTVTALYEVPLGVCTQDPDRWTTTPDDEAKTLCRACPRRWLCARDAVESAGAEGLWAGVVIPESGRARAFALGQLRSLAERNGYPVRDHRVSAQSA", "text": "FUNCTION: Acts as a transcriptional regulator. Probably redox- responsive. The apo- but not holo-form probably binds DNA (By similarity). FUNCTION: Acts as a transcriptional regulator. Probably redox- responsive. The apo- but not holo-form probably binds DNA (By similarity). The apo-form has been shown to act as a protein disulfide reductase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the WhiB family."}
+{"protein": "MASAERVPVSFNKPGRVPFGEVQGYAPGHIPAYSNKHDHFFSGERSIDDNVFCGFKYQCVEFARRWLLERKGLVLPDVNWACHIFKLKNVKDAATAEEVPVIAVRNGTEAKPEPDTLIIYPSSDVNTVGHVGAITEVGDDYVCIADQNYRFHKWEASYSYKLKLQHKDGVWTIIDDIDPNDVEIPLGWVTFPGYENRPEGAAPPALHPSLHFQPPEEPYLVRKTYEPTETKANWLDLNDPAEKLFVEEFGMDVSRSRLEETTVNYYECDHEFHLRCIAYGTQLHDYFMEATAQVINDDERLRIFKIPEELWPRMRHSWKYQQTYISGRFDFAYNNETHQMKCFEYNADSASTLLECGRIQQKWAESVGLDKEGTRGSGWAVERNLRTAWATCGATGRVHFLVDDEKEEQYTALYCLQAAEAVGLEGKLCVMYDEFRFNEEGYVVDSDGVRVRNIWKTWMWESAISDYFAAQAERGADWKATPADKVRLCDLMLGKDWDILYFEPMWKLIPSNKAILPIIYHNHPDHPAILRAEYELTDELRAVGYARKPIVGRVGRNVTITDGTGEVHAESGGNFGERDMIYQELFSLTKQDGYYAIIGGWMLGDAFSGTGIREDKSIITGLDSPFAAIRIKINAIPRPLTHKDLDKLAEDE", "text": "FUNCTION: Conjugates glutathione (gamma-Glu-Cys-Gly) and glutathionylspermidine to form trypanothione (N(1),N(8)- bis(glutathionyl)spermidine), which is involved in maintaining intracellular thiol redox and in defense against oxidants. SIMILARITY: In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family."}
+{"protein": "MKPKLVFLPFLIFITVFIEESEAVHPVVLETKLGDIRGNEFFFLSKKIRTFFGVPFAEPPVEEFRFRKPREKKQWKKLFDATKPANACFQTRDNYNTSFWGSEMWNANTQISEDCLYLNIWAPADAYNLTVMVWFFGGGFYSGSPSLSIYDGRALAATQHVIVVNINYRLGPFGFLYLDHPDAPGNMGLLDQQLALHWIRQNIVSFGGNPDKVSVFGQSAGAASIVAHLIAPGSRGLFKNAILQSGSLENTWAINSPFRAKQKSEKLLELVGCNKTTVENSMSCLRLVSPEQLSLSTWNISLTYLEFPFVIVSRDKHFFGHLDARAALREGDFNRDVNLMIGMNKDEGNYWNIYQLPQFFDKAEPPELTRHQFDNLIDSTFSIQPDIIRSAAKYIYSDPNCTDHGRKTRFYAGQMNQIVGDYFFSCDSLWLADQFFLFLQICSTPNGSLKNPPKVFVYYFTQSSSANPWPKWTGAMHGYEIEYVFGVPLSYSKIYKRREQIFSRKIMQFWASFAKNGTPRLRVLKNSEHWPEFNEHNNYRWMQLRSGSNIRPIKRRKETECQFWRRVKDTEYTAYLTQEYSSSCHINSYRILLFIPFFFIFSAF", "text": "FUNCTION: Rapidly hydrolyzes choline released into the synapse. SUBCELLULAR LOCATION: Synapse Secreted Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
+{"protein": "MTTKNLETKVTVTSSPIRGAGDGMETEEPPKSVEVTSGVQSRKHHSLQSPWKKAVPSESPGVLQLGKMLTEKAMEVKAVRILVPKAAITHDIPNKNTKVKSLGHHKGEFLGQSEGVIEPNKELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDLQYHFERLAREKNQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQEMIATQKLLEELLVSLQWGREQTYSPSVQPHSTAELALTNHKLAKAVNSHLLGNVGINNQKKIPSTVEFCSTPAEKMAETVLRILDPVTCKESSPDNPFFESSPTTLLATKKNIGRFHPYTRYENITFNCCNHCRGELIAL", "text": "FUNCTION: Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface. SUBCELLULAR LOCATION: Golgi apparatus membrane. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus Note=Detected in the nucleus upon heterologous expression. Not detected in the cytoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Note=Not detected in the nucleus."}
+{"protein": "MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD", "text": "FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (By similarity). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (By similarity). Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (By similarity). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (By similarity). May counteract a default induction of apoptosis in G2/M phase (By similarity). The acetylated form represses STAT3 transactivation of target gene promoters (By similarity). May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). Essential for the maintenance of mitochondrial integrity and function (By similarity). FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:9859993, PubMed:21364656, PubMed:20627126, PubMed:25778398, PubMed:28218735). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (PubMed:16322459). Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (PubMed:20826784). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (PubMed:20929775). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (PubMed:18591255). May counteract a default induction of apoptosis in G2/M phase (PubMed:9859993). The acetylated form represses STAT3 transactivation of target gene promoters (PubMed:20826784). May play a role in neoplasia (PubMed:10626797). Inhibitor of CASP3 and CASP7 (PubMed:21536684). Essential for the maintenance of mitochondrial integrity and function (PubMed:25778398). Isoform 2 and isoform 3 do not appear to play vital roles in mitosis (PubMed:12773388, PubMed:16291752). Isoform 3 shows a marked reduction in its anti- apoptotic effects when compared with the displayed wild-type isoform (PubMed:10626797). SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome Chromosome, centromere Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore Midbody Note=Localizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the midbody during telophase and cytokinesis. Accumulates in the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor (By similarity). Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody (PubMed:11084331). Colocalizes with AURKB at mitotic chromosomes (PubMed:14610074). Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export (PubMed:20826784). SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome Chromosome, centromere Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore Midbody Note=ocalizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the midbody during telophase and cytokinesis. Accumulates in the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor (By similarity). Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1- mediated nuclear export (By similarity). SIMILARITY: Belongs to the IAP family."}
+{"protein": "MQFQTLLVVAGSLVASTLAVNSTVTEHHTTEITITHCSDNKCATSVAPAVQSVNTVTIEGVVTEYTTYCPLTASEHKHKESSSPSSVAPVASTESVVTTTISGVHTSYTTYCPLSGSSEASTVITPGTVAGESSSSSEEVSYVDVTSTPVVESTTDVELTLTAQSTLFTSYANSTGSSSSSSVVPSANVTTFEGGAVGGASNQITVGFAAIAGLAAILL", "text": "FUNCTION: Probable cell wall protein that participates directly in adhesive cell-cell interactions. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Lipid-anchor, GPI-anchor Note=Covalently- linked GPI-modified cell wall protein (GPI-CWP). SIMILARITY: Belongs to the flocculin family."}
+{"protein": "MKMEMGLVFLTVFMAVMSSTMVSAQSSCTNALISMSPCLNYITGNSTSPNQQCCNQLSRVVQSSPDCLCQVLNGGGSQLGINVNQTQALGLPRACNVQTPPVSRCNTGGGGGGSTSDSPAESPNSSGPGNGSKTVPVGEGDGPPSSDGSSIKFSFPLIAFFSAVSYMAIF", "text": "FUNCTION: Lipid transfer protein involved in seed and ovule maturation and development, probably by regulating the fatty acids homeostasis during suberin and sporopollenin biosynthesis or deposition (PubMed:24460633). Contributes to pre-invasive defense against some non-host powdery mildew pathogens by preventing the penetration of the epidermal cell wall by the fungal agents (e.g. Blumeria graminis f. sp. hordei (Bgh)) (PubMed:30102837). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the plant LTP family."}
+{"protein": "MSRLKINLDAIERDGASATEGFCADGVRIGSLLVSSEGVRDNQGNLCVLSLSDLEVVPETEGGFLGKGSSGSVRRAVHRGSNKVVALKEIKVTGQTHINEIRRELETLHAGDFATPYLVSFYGAFAHEGSVFIAMEAMDGSLHELYKPVPPPVLACITRLMLKGLTYLHRNRHLIHRDLKPSNVLYNSRTGDIKISDFGVSSNLECTKADAHSFVGTVTYMSPERLRGEHYSYGADIWSLGLVVAELAVGVCPYAGLRGGSSEARFWALLQHLNGDGTALELPPEMDSDLADFISACVVKSPDRRPTCTELLRHPFIVRYTGAAPEAEAKPFSTTTPTVLAPGGLSSLLNRASPAAGSALPLASEGGTPKATSPSPAPVSPLTLSCPLERHDGETDADIADRTVVARWIHAVMKRAVLHKARGHGREELHQEPLAAVSASVATDSGEGGGAAGVSAASLDNGQAAQHREFRAERNLDGHSGDGGSAPVEEDCTAGVRSLTCDDLRWTSTGEPSVNLDDELNRLLF", "text": "FUNCTION: Protein kinase which phosphorylates and activates MPK4 in vitro. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily."}
+{"protein": "MAANQNVTKKKKAVIGGIFKAELNNFLMKELAEDGYSGVEVRSTPARAEVIIMATRTQNVLGERGRRIKELTSVVQKRFGFEEGSVELYAEKVSNRGLCAVAQCESLRYKLVGGLAVRRACYGVLRFIMESGAQGVEVIVSGKLRGQRAKAMKFVDGLMIHSGHPVNDYIQQAVRHVQLRQGVIGIKVKIMLPYDPRGQNGPRNALPDHVQIVEPQEEVLPKEPHSQHKEEKKDVQVPAAQPVAPVQ", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
+{"protein": "MSLSKVSVENSLKPEKFVKISWVDKLLPNYFSILKYLSITDFSVVKAQSYESLVPVKLLRGVDLTKHLYVTLLGVVVSGVWNVPESCRGGATVALVDTRMHSVAEGTICKFSAPATVREFSVRFIPNYSVVAADALRDPWSLFVRLSNVGIKDGFHPLTLEVACLVATTNSIIKKGLRASVVESVVSSDQSIVLDSLSEKVEPFFDKVPISAAVMARDPSYRSRSQSVSGRGKRHSKPPNRRLDSASEESSSVSFDDGLQSDHT", "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. Forms a ribonucleoprotein complex with viral RNA. Binds microtubules and modulates microtubule stability. Can bind double- stranded DNA. SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton Host cell junction, host plasmodesma. SIMILARITY: Belongs to the tobamovirus movement protein family."}
+{"protein": "MHDAGLDYYGRRLATCSSDKTIKIFEIEGETHRLVETLKGHEGAVWCIAWAHPKFGTILASSSYDGKVLIWREQHQNTTSPVAVNTWTKVFDFSLHTASVNMVSWAPHESGCLLACASSDGHVSVLEFQDNSWTHQIFHAHGMGVNSISWAPAASPGSLISANPGPGQQRRFVTGGSDNLLKIWDYNSETKSYNLSQTLEGHSDWVRDVAWSPSILSKSYIASASQDKTVRIWTSDVSNPGQWASQQLEFDTVLWRVSWSPSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE", "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": "MTVKPAKAASLARNLAKRRRTYLGGAAGRSQEPEVPCAAVLPGKPGDRNCPEFPPPDRTLGCWATDAAPAAGLCGAGSEPSIAPTSCAGNLPSRPPPLLSPLLASRNPCPWHYLHLSGSHNTLAPTCFKAKLHRKRGSQPPDMASALTDRTSRAPSTYTYTSRPRALPCQRSRYRDSLTQPDEEPMHYGNIMYDRRVIRGNTYALQTGPLLGRPDSLELQRQREARKRALARKQAQEQLRPQTPEPVEGRKHVDVQTELYLEEIADRIIEVDMECQTDAFLDRPPTPLFIPAKTGKDVATQILEGELFDFDLEVKPVLEVLVGKTIEQSLLEVMEEEELANLRASQREYEELRNSERAEVQRLEEQERRHREEKERRKKQQWEIMHKHNETSQKIAARAFAQRYLADLLPSVFGSLRDSGYFYDPIERDIEIGFLPWLMNEVEKTMEYSMVGRTVLDMLIREVVEKRLCMYEHGEDTHQSPEPEDEPGGPGAMTESLEASEFLEQSMSQTRELLLDGGYLQRTTYDRRSSQERKFMEERELLGQDEETAMRKSLGEEELS", "text": "FUNCTION: Functions as part of axonemal radial spoke complexes that play an important part in the motility of sperm and cilia (By similarity). Functions as a protein kinase A-anchoring protein that scaffolds the cAMP-dependent protein kinase holoenzyme. May serve as a point of convergence for MAPK and PKA signaling in cilia (PubMed:19684019). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the flagellar radial spoke RSP3 family."}
+{"protein": "MNSQFAGLTREACVALLASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQTFIKDVHLMVADQWAAAQACVKAGAHCITLQAEGDIHLHHTLSWLGQQTVPVIDGEMPVIRGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLYERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDDRLVENTRSWRAMFKVAGDTTFLPSTA", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family."}
+{"protein": "MNNAIILGIIWHLVGAASAACFYAPFKQVKKWSWETMWSIGGLVSWLILPWTVSYLLLPDFWQYYGSFSIATLLPVFLFGAMWGIGNINYGLTMRYLGMSMGIGIAIGITLIIGTLMTPILQGRFDVLLGTPGGRMTLLGVFVALIGVAIVSYAGLLKERAMGIQAEEFNLKKGLILAVMCGIFSAGMSFAMDAAKPMHEAASALGINSLYVALPSYVIIMGGGAIINLSYCFIRLATLKNLSVKADFSVAKPLLITNILFSALAGLMWYLQFFFYAWGHAKIPQQYDYMSWMLHMSFYVLCGGIVGLLLKEWKCSTKKPVAVLCIGCLVIILAANIVGLGMAA", "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": "MATAQLSHSIKIHKASKETVFPSQITNEHESLIMVKKLFATSISCITYLRGLFPESSYGERHLDDLSLKILREDKKCPGSLHIIKWIQGCFDALEKKYLHMAVLTLYTNPKEPEKVTEIYQFKFKYTKEGATMDFDSYSSSASFESGTNSEDIKKASILLIRKLYILMQNLGPLPNDVILTMKLHYYNAVTPHDYQPPGFKEGVNSHLLLFEGEPVNLQVGLVSTGFHSMKVKVTTEVTRVSDLENNLFQENSTTEIAHQGLDFDEEEEECNNHVRQSCSESPLIASVKKKRKKDFPIYFFYEFRK", "text": "FUNCTION: Essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity. 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. Required for the DNA double-strand break- independent, BRCA1-dependent activation of ATR on the sex chromosomes that is essential for normal sex body formation (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Preferentially localizes to unsynapsed or desynapsed chromosomal regions during the male and female prophase I stage of meiosis. TRIP13 is required for depletion from synapsed chromosomes (By similarity)."}
+{"protein": "MTILPKKKPNSSVGVSDHPDDPDRRTGSDPHQHQHQHSHGVRPGARPRASPPPWSYQAAPPASREDRRTESSSRPQQASPPPVGAGSSGGPGDATGMACVSGNRAELSGGVGCGGGMGGCCSGPGLSKRRRQATCSGGVAGGGTGPGAAGGGGGGGGGGGVGGPSPEQEEGAGYNSEDEYENASRLQSEDPATVEQQEHWFEKALQEKKGFVIKKMKEDGACLFRAVADQVYGDQDMHEVVRKHCMDYLMKNADYFSNYVTEDFTTYINRKRKNNCHGNHIEMQAMAEMYNRPVEVYQSGTEPINTFHGIHQNNDEPIRVSYHRNIHYNSVVNPNKATIGVGLGLPAFKPGFADQSLMKNAIKTSEESWIEQQMLEDKKRATDWEATNEAIEEQVARESYLQWLRDQEKQARQPRKASATCSSATAAASSGLEEWNARSPRQRSSAPSPEIPDPAHSDTAAKPPSPAGALALSKPPSPCAPGPSNQACVGPDRPTSSSLVSLYPALGYRAIMQEMSPTAFGLTDWEDDEILASVLAVSQQEYLDSMKKNAMHREPSPDSS", "text": "FUNCTION: Deubiquitinating enzyme that may function as negative regulator of the innate immune system. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro) (By similarity). SIMILARITY: Belongs to the peptidase C85 family."}
+{"protein": "MAEGLRAPPPPGNGSECPDGARWVLRLLGECARDGRDVGSALLGLLSIGCFAAAALPQFYQACKTGIMDRALSIYFLLGWLGGDLLNLIGSFLANQLPLQVYTAVYYVLADLVMLSLYGYYKAKNWGTGATASINAACLFCLLGTATTLTVLSHDTGPAPNPAAFGGRSLLSLGLEGPGPEPISKTEIIGFAIGSISSVLYLCSRLPQIYTNYRRKSTAGVSFLLFALVMLGNLLYGTSVLLKNPEPGQSEGDYILHHLPWLIGSLGVLSLDVIISFQFLAYRTGQPSAGEEREALLAEHGDS", "text": "FUNCTION: Amino acid transporter that specifically mediates the pH- dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the laat-1 family."}
+{"protein": "MALTSRFYNERYPEIEDVVMVNVLSIAEMGAYVHLLEYNNIEGMILLSELSRRRIRSINKLIRVGKTEPVVVIRVDKEKGYIDLSKRRVSPEDVEKCTERFAKAKAINSLLRHVADILGFEGNEKLEDLYQKTAWHFEKKYNNKTVAYDIFKQSVTDPTVFDECNLEPETKEVLLSNIKRKLVSPTVKIRADIECSCYGYEGIDAVKASLTKGLELSTEELPIRINLIAPPLYVMTTSTTKKTDGLKALEVAIEHIRAKTSEYDGEFKVIMAPKLVTAIDEADLARRLERAEAENAQVAGDDDEEDGADQEGMQFDPEKEFNHKGSGAGRANEEDEEEEED", "text": "FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This preinitiation complex mediates ribosomal recognition of a start codon during the scanning process of the leader region. SIMILARITY: Belongs to the eIF-2-alpha family."}
+{"protein": "MVMAHFVENFWGEKNNGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQAIQNITQALQKSKENYNAKCVEQERLKKEGATPREIEKAAVKSKKATDTYKLYVEKYALTKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAIKEIHLQIGQVHEEFINNMANTTIESLIQKFAESKGTGKERPGLIEFEECDPASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDEEGFSIKPEANQNDTKENHFYSSSDSDSEDEEPKRYRIEIKPVHPNNVHHTMASLDELKVSIGNITLSPAVSRHSPVQMNRNSSNEELTKSKPSSLPTEKGTNDLLAWDPLFGSSLESSSAPLTSSSSARPTTPLSLGTIVPPPRPASRPKLTSGKLSGINEIPRPFSPPITSNTSPPPTAPLARAESSSSISSSASLSAANTPTVGVSRGPSPVSLGNQDTLPVAIALTESVNAYFKGADPTKCIVKITGDVTISFPSGIIKVFTSNPSPAVLCFRVKNISRLEQILPNSQLVFSDPSQCDSNTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVLSNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSGISEKSDSGGSGSLRAKFDLSEGPSKPATLAVQFLSEGNTLSGVDIELVGTGYRLSLVKKRFATGRYLADC", "text": "FUNCTION: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2- dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor (By similarity). SUBCELLULAR LOCATION: Membrane, clathrin-coated pit; Peripheral membrane protein; Cytoplasmic side Note=Associated with forming but not mature clathrin- coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2 (By similarity). SIMILARITY: Belongs to the FCHO family."}
+{"protein": "MPRFSHLIGCVWQVLFVSAGAQAMASSFVVPSTAQMAGQLGIEATGSGVCAGPAEQANALAGDVACAEQWLGDKPVSWSPTPDGIWLMNAEGTGITHLNRQKEGEYTGRTPSGADVTLQRTN", "text": "FUNCTION: Inhibitor of the alkaline protease. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the protease inhibitor I38 family."}
+{"protein": "MSSGANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSTPADRNGGQDQCRAQIRDWQDLQEGEFLLQALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPDSAQGVDEAHGPPQAAVYYTPDQLPPENASFMERCFRCRLRCLLDNSSGFLAMNFQGRLKYLHGQNKKGKDGALLPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGQLILGYTEVELCTRGSGYQFIHAADMLHCAESHIRMIKTGESGMTVFRLFAKHSRWRWVQSNARLIYRNGRPDYIIATQRPLTDEEGREHLQKRSTSLPFMFATGEAVLYEISSPFSPIMDPLPIRTKSNTSRKDWAPQSTPSKDSFHPSSLMSALIQQDESIYLCPPSSPAPLDSHFLMGSVSKCGSWQDSFAAAGSEAALKHEQIGHAQDVNLALSGGPSELFPDNKNNDLYNIMRNLGIDFEDIRSMQNEEFFRTDSTAAGEVDFKDIDITDEILTYVQDSLNNSTLMNSACQQQPVTQHLSCMLQERLQLEQQQQLQQPPPQALEPQQQLCQMVCPQQDLGPKHTQINGTFASWNPTPPVSFNCPQQELKHYQLFSSLQGTAQEFPYKPEVDSVPYTQNFAPCNQPLLPEHSKSVQLDFPGRDFEPSLHPTTSNLDFVSCLQVPENQSHGINSQSTMVSPQAYYAGAMSMYQCQPGPQRTPVDQTQYSSEIPGSQAFLSKVQSRGIFNETYSSDLSSIGHAAQTTGHLHHLAEARPLPDITPGGFL", "text": "FUNCTION: Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed:10639156, PubMed:10973493, PubMed:1314586, PubMed:7961644, PubMed:7969080, PubMed:8806883, PubMed:9427285, PubMed:33436590). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) (By similarity). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (PubMed:20106950, PubMed:28396409). Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) (PubMed:10639156, PubMed:10973493, PubMed:1314586, PubMed:7961644, PubMed:7969080, PubMed:8806883, PubMed:9427285). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons (By similarity). Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists (By similarity). Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands (By similarity). Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity (By similarity). Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 (By similarity). Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 (PubMed:20106950). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28396409). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus."}
+{"protein": "MDKYKVAGKFGLPDITVAEMESLASFCEAVLPSVQPPPEELSGEGDNHRNKEALRSFYSTSGSKTPVLRQSIELVTKRGTIEAYIATRLILFLLATRLGTLLICGTECLVSRWPFVEKFSELSLEKRERVLQKQFKNWILTPIRAAFVYIKVAFLFCFFSRVNPNGENPAWEAIGYRVNPDENKPSETHNERPLEKGIVETMEETEQTLLESLAHKGLEAVLDTEHDAIRIKCDVVVVGSGSGGGVAASVLAKSGLKVVVLEKGSYFTPSEHRPFEGPGLDKLYENGGILPSVDGSFMVLAGATVGGGSAVNWSACIKTPKSVLQEWSEDQNIPLFGTKEYLTAMEVVWKRMGVTEKCELESFQNQILRKGCENLGFNVENVPRNSSESHYCGSCGYGCRQGDKKGSDRTWLVDAVGHGAVILTGCKAERFILEKNGSNKGGKQMKCLGVMAKSLNGNIAKMLKIEAKVTVSAGGALLTPPLMISSGLRNRNIGKNLHLHPVLMAWGYFPDKESSNISFKGNSYEGGIITSVSKVLSEDSEVRAIIETPQLGPGSFSVLTPWTSGLDMKKRMARYSRTASLITIVRDRGSGEVKTEGRINYTVDKTDRDNLKAGLRESLRILIAAGAEEVGTHRSDGQRLICKGVNENSIQEFLDSVSTEEGAKGMTEKWNVYSSAHQMGSCRIGENEKEGAIDLNGESWEAEKLFVCDASALPSAVGVNPMITVMSTAYCISTRIAKSMTTGLSH", "text": "FUNCTION: Long-chain fatty alcohol oxidase involved in the omega- oxidation pathway of lipid degradation. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the GMC oxidoreductase family."}
+{"protein": "MQKNQTIFLNTWKFLITLHQKPWSTFFTKIPDFPHVLLKDIAKVGVGLVSGFDEAFLLNEDDISKLNEDEKQLIKNFVKAKNCKRFVVEGFVQYILIEDNLKDEEIFKTKYPNIYKKLLKFKDRMENRYLPKNKKWFNWQALRNYKFLIKNLNKKRIYVPTLDRKPYNRFSLGDDELLPSGDVIFIQPYNDDDIYFLLGYLNSSFFRNYYLANGGRRGGRVAFTQKLLENAKIPTFSDEVKEKIKNIVKDIIYNLKNGKDIENLERQIDYIIVSAINNNQFKGYQTTLKNLLKPKLKG", "text": "FUNCTION: A methylase that recognizes the double-stranded sequence 5'- GTNNAC-3', methylates A-5 on both strands, and protects the DNA from cleavage by the MjaIV endonuclease."}
+{"protein": "MALIMTQQNNPLHGITLQKLLTELVEHYGWEELSYMVNINCFKKDPSIKSSLKFLRKTDWARERVENIYLKLQRHKERNQ", "text": "FUNCTION: Binds double-stranded DNA (dsDNA)."}
+{"protein": "MNNTRVSFRSTKSLLAAIIATSMMTWSVNRATLQTTKATEAASTGWATQGGTTGGAKAASAKIYAVKNISEFKAALNGTDTDPKIIQVTGAIDISGGKAYTSFDDQKARSQISVPSNTTIIGIGSNGKFTNGSLVIKGVSNVILRNLYIETPVDVAPHYEEGDGWNAEWDAAVIDNSTRVWVDHVTISDGSFTDDKYTTKNGEKYVQHDGALDIKKGSDYVTISSSRFELHDKTILIGHSDSNGSQDSGKLRVTFHNNVFDRVTERTPRVRFGSIHAYNNVYLGDVKNSVYPYLYSFGLGTSGTILSESNSFTLSNLKSIDGKNPECSIVKQFNSKVFSDNGSLVNGSSTTKLDTCAVTAYKPTLPYKYSAQTMTSSLASSINSNAGYGKL", "text": "FUNCTION: Involved in maceration and soft-rotting of plant tissue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLBC subfamily."}
+{"protein": "MQKWFSAFDDAIIQRQWRANPSRGGGGVSFTKEVDTNVATGAPPRRQRVPGRACPWREPIRGRRGARPGGGDAGGTPGETVRHCSAPEDPIFRFSSLHSYPFPGTIKSRDMSWKRHHLIPETFGVKRRRKRGPVESDPLRGEPGSARAAVSELMQLFPRGLFEDALPPIVLRSQVYSLVPDRTVADRQLKELQEQGEIRIVQLGFDLDAHGIIFTEDYRTRVCDCVLKACDGRPYAGAVQKFLASVLPACGDLSFQQDQMTQTFGFRDSEITHLVNAGVLTVRDAGSWWLAVPGAGRFIKYFVKGRQAVLSMVRKAKYRELLLSELLGRRAPVVVRLGLTYHVHDLIGAQLVDCISTTSGTLLRLPET", "text": "FUNCTION: Serine/threonine-protein kinase that acts as a key regulator of NRAS signaling by mediating phosphorylation of NRAS at 'Ser-89', thereby enhancing NRAS-binding to its downstream effectors. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the STK19 family."}
+{"protein": "MMKVLVVVALLVTLISYSSSEGIDDLEADELLSLMANEQTRAKACTPRYYDCSHDRHSCCRSSMFKDVCTCFYPEGGDNKEVCTCQQPKHLKYMEKATDKIKNLFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 02 (D7) subfamily."}
+{"protein": "MEDRLHMDNGLVPQKIVSVHLQDSTLKEVKDQVSNKQAQILEPKPEPSLEIKPEQDGMEHVGRDDPKALGEEPKQRRGSASGSEPAGDSDRGGGPVEHYHLHLSSCHECLELENSTIESVKFASAENIPDLPYDYSSSLESVADETSPEREGRRVNLTGKAPNILLYVGSDSQEALGRFHEVRSVLADCVDIDSYILYHLLEDSALRDPWTDNCLLLVIATRESIPEDLYQKFMAYLSQGGKVLGLSSSFTFGGFQVTSKGALHKTVQNLVFSKADQSEVKLSVLSSGCRYQEGPVRLSPGRLQGHLENEDKDRMIVHVPFGTRGGEAVLCQVHLELPPSSNIVQTPEDFNLLKSSNFRRYEVLREILTTLGLSCDMKQVPALTPLYLLSAAEEIRDPLMQWLGKHVDSEGEIKSGQLSLRFVSSYVSEVEITPSCIPVVTNMEAFSSEHFNLEIYRQNLQTKQLGKVILFAEVTPTTMRLLDGLMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYYSDLMKIGGVLVNSTLMGETFYILIGCGFNVTNSNPTICINDLITEYNKQHKAELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIVGLDDSGFLQVHQEGGEVVTVHPDGNSFDMLRNLILPKRR", "text": "FUNCTION: Biotin--protein ligase catalyzing the biotinylation of the 4 biotin-dependent carboxylases acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, and methylcrotonyl-CoA carboxylase. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion. SIMILARITY: Belongs to the biotin--protein ligase family."}
+{"protein": "MRRRVALSTAIALLVGAQLCVAAEVEVAGAGGGVVRRRSLHQPFFPIEWSPPPPMSGSEAVPPPPPAAAASATTGGGRSTTTVMNTVAIALSAGLVALAVASYSCCLLLRRRRREEEDDGDRAAKRAVGAAAAVAARVPSDVGSSSRQHRSPPPSSTASDAIYLDPLTTLVEVRQHEKSPDLRPLPLLKQPSPDLRPLPPLKRPESQPPPPPPSTPPLTTTGYSTDEEDQATYYTAPKTAMSSFSRSTSQHSTLEQTAMPPMAAPAPPQTNPPRPVRPPPPPPPPRQRLLRPLPAESPPPAALANLELTGSPVKPAVEDRGGENSGAARPPKPPHLKPLHWDKLRAISGRTTVWDQVKNSDTFRVDEEAMESLFLNSGGGGAGSSDPAARRGGSGKQERRLLDPKRLQNVAIMLKSLNVAADEVIGALVRGNPEDLGSEFYETLAKMAPTKEEELKLKGYSGDLSKIDPAERFLKDVLGVPFAFERVDAMLYRANFDNEVNYLRKSFGTLEAACEELRSSKLFLKLLDAVLKTGNRMNDGTNRGEARAFKLDTLLKLADIKSTDGRTTLLHFVVKEIIRSEGFDSDQSAVNPGSGSKEQFKRDGLKLLAGLSSELSNVKRAATLEMDTLSGNILRLEADLEKVKLVLQLKETCSDQGASENFFQAMVVFLRRAEAEIKNMKTAEENALRLVKETTEYFHGDATKEEPHPLRIFVVVDEFLLILDRVCRDVGRTPERVMMGSGKSFRVPAGTSLPPHRNENRRVLSSSDEDSSSS", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the formin-like family. Class-I subfamily."}
+{"protein": "MTMRASLAIENFLEMMSAERGAAQNTLESYRRDLEAAAEELAAKGVNLAEAETGHIRMTLDTMAAQGFAPTSQARRLSALRQFFRFLYSEGFRQDDPTGILYAPKKQKPLPKIMSVENVGKLLDRAALEANEAAEPGERIKALRLHALLETLYATGLRVSELVGLPVTVARTDHRFLLVRGKGSKDRMVPLSRKARDALQKFLTLRDSLPGSDDNPWLFPAFSESGHLARQVFARELKGLAARAGLAASSASPHVLRHAFASHLLQNGADLRTVQQLLGHADISTTQIYTHVLEERLHKLVSEHHPLAD", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily."}
+{"protein": "MARGPGPLGRPRPDTVAMPKRGKRLKFRAHDACSGRVTVADYANSDPAVVRSGRVKKAVANAVQQEVKSLCGLEASQVPAEEALSGAGEPCDIIDSSDEMDAQEESIHERTVSRKKKSKRHKEELDGAGGEEYPMDIWLLLASYIRPEDIVNFSLICKNAWTVTCTAAFWTRLYRRHYTLDASLPLRLRPESMEKLRCLRACVIRSLYHMYEPFAARISKNPAIPESTPSTLKNSKCLLFWCRKIVGNRQEPMWEFNFKFKKQSPRLKSKCTGGLQPPVQYEDVHTNPDQDCCLLQVTTLNFIFIPIVMGMIFTLFTINVSTDMRHHRVRLVFQDSPVHGGRKLRSEQGVQVILDPVHSVRLFDWWHPQYPFSLRA", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TMEM183 family."}
+{"protein": "MGQAATHVDANYTLINYTEEVIEDDRDACAVADDPKYPSSFGITLAVPEWEAICTAIVLTLIIISTIVGNILVILSVFTYKPLRIVQNFFIVSLAVADLTVAILVLPLNVAYSILGQWVFGIYVCKMWLTCDIMCCTSSILNLCAIALDRYWAITDPINYAQKRTLERVLLMIGVVWVLSLIISSPPLLGWNDWPDVFEPDTPCRLTSQPGFVIFSSSGSFYIPLVIMTVVYFEIYLATKKRLRDRAKATKISTISSGQNKYNNKDDHHDQDSVSSEANHNEHQGVTRLVSDNEKKKRTRKLTPKKKPKRKYWSKDDKSQNKLIIPILSNENSVTDMGENLENRNTSSESNSKETHEDDLIEVNETVPVKTHHKKPKPNQQSAVYQFIEEKQRISLTRERRAARTLGIIMGVFVVCWLPFFVIYLVIPFCASCCLSNKFINFITWLGYCNSALNPLIYTIFNMDFRRAFKKLLCMKP", "text": "FUNCTION: Receptor for octopamine. Octopamine (OA) is a neurotransmitter, neurohormone, and neuromodulator in invertebrates. 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": "MPIRAYCTICSDFFDNARDVAAITCGHTFHQECLLQWFHSAPHRTCPQCRIQVSSRQIINKLFFDIGGEEETVLDAESLKNEVDRIKASLLVKEKEKRECQGLVDSLREMLDVRNVTIQSQQKELGDMEMLCSTLKKQIKFLDKQQSETKAAKDEARKLRNKLKTMESIEVLLQSQRSEVEEMIRDMGSGQAAVEQLAIYCVSLKKEYENLKEVRKSSAEMTEKLRKELFSSNHKAQKAELELTKVREELSASQKELHSADKEIMSLKKKVEFLQKTLTTPTASNEAISRLIFESPAPIGLERPKLRPPMMGNDINLDVTFDIDTPEHNTQKSVVAPFKKMKFDNKEHPLSSPTKNPLQESKGLMSWAGGRTGADEDDDLTLPSFIKNSLLHKKPVGSLLGLRQNTGAVRTGFDGLGGRTKFIQPSNLTEIRPLHQKMKRKKVSRPTACTSSLANQPRLEDFLK", "text": "FUNCTION: E3 ubiquitin ligase required to protect genome stability in response to replication stress (PubMed:30979826, PubMed:30849395, PubMed:30842657). Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription (PubMed:30979826, PubMed:30849395, PubMed:30842657). Controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of mcm7 subunit of the CMG helicase complex (PubMed:30842657). Short ubiquitin chains on mcm7 promote recruitment of DNA glycosylase neil3 (PubMed:30842657). If the interstrand cross-link cannot be cleaved by neil3, the ubiquitin chains continue to grow on mcm7, promoting the unloading of the CMG helicase complex by the vcp/p97 ATPase, enabling the Fanconi anemia DNA repair pathway (PubMed:30979826, PubMed:30842657). Only catalyzes ubiquitination of mcm7 when forks converge (PubMed:30842657). Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: promotes ubiquitination of DPCs, leading to their degradation by the proteasome (PubMed:30595436). Also acts as a negative regulator of innate immune signaling by inhibiting activation of NF-kappa-B mediated by TNF (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus Chromosome Cytoplasm Note=Localizes to DNA damage sites in response to replication stress. SIMILARITY: Belongs to the TRAIP family."}
+{"protein": "MRASTHSWLLLVVVLSLSSFTVNAVILEGLIPPRSHLAPSTFQQPFALSSYLQKLFGTSLRALYGAEQNRQTSVKTFGLREAYHQGIGDKAHERARATFDFRITANDVQADQANIDFIPAIRTVRQRITRAKDPKKYVEVRGQSYRDAMCAASTELDWEDVDVEAPDVTERTTVLAFAKMASAAYKNDTSDWDGIGGFDPTNSFGWEGDGIRGHIFTTHDNDTIVVALKGTSNVFLGGGDTARRDKTNDNLLFSCCCARVSWSWSTVCDCYQGHGDQCGQTCVERALIEKSLYYPAITDLFNNVSYAYPDSQIWITGHSLGGALSSLLGMTFGVPTVTFQAPGERMAAMRLHLPLPPAKHADESPVAALPIVHVYNNADPIATGTCNGAASVCSNFGYAMESKCHSGKSIVYDTVGKLGWSMTINAHRINTLVDDVLTEDWSEKVRKKKAKLRSIGSRGGQISTRGWRWPWHRGDSADDDGDSDEDTDEDDKLAVPKARSEERCQDCTNWHFTDETL", "text": "FUNCTION: Lipase which is essential for lysis of subvacuolar cytoplasm to vacuole targeted bodies and intravacuolar autophagic bodies. Involved in the lysis of intravacuolar multivesicular body (MVB) vesicles. The intravacuolar membrane disintegration by ATG15 is critical to life span extension (By similarity). SUBCELLULAR LOCATION: Endosome, multivesicular body membrane; Single-pass type II membrane protein Prevacuolar compartment membrane; Single-pass type II membrane protein Note=From ER, targeted to vacuolar lumen at the MVB vesicles via the Golgi and the prevacuolar compartment (PVC). SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
+{"protein": "MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKATGEMKEQTEWHRVVLFGKLAEVASEYLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQMLGGRQGGGAPAGGNIGGGQPQGGWGQPQQPQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFDDDIPF", "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. Acts as a sliding platform that migrates on DNA via reptation. SSB or its 10 C-terminal amino acids stimulates the ATPase activity of RadD (PubMed:27519413). 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": "MSGSAVSKRYASALFDIANESAQLNQVEEELIVVKQVFQNEKALNDVLNHPKVPAAKKKELIQNAFGSLSQSVLNTIFLLIDRHRAAIVPELTDEFIKLANVARQTEDAIVYSVKPLTDAEMLPLSQVFAKKAGVASLRIRNEVQTDLIGGIKVRIGNRIYDGSVSGKLQRIERQLAGENR", "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 Membrane raft; Peripheral 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. SIMILARITY: Belongs to the ATPase delta chain family."}
+{"protein": "MSEEQLKAFIAKVQADTSLQEQLKAEGADVVAIAKAAGFSITTEDLEKEHRQTLSDDDLEGVAGGFFCVQGTANRFTINVC", "text": "FUNCTION: Lanthionine-containing peptide (lantipeptide) with unknown function (Probable). Does not show antibiotic activity against Lactococcus lactis 117 and Bacillus subtilis 6633 bacteria (PubMed:20479271). 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": "MPKTRKQRSRRPRNQRPSTPWPISQVSDRAFSTGTLSTFSATVYRPIGAPFLGGFVPLGYTAMPCWPRAPNIRLPGTPSMDALSAQLYNTLSLGSPPSPPKELPAPSRFSPPQPLLRPPRFLHPSSTPLKNTPPSETIASSSPWESSCQPCPSPTLGSGPKTSTPYGAAPSCVSTSISSPPP", "text": "FUNCTION: Rex escorts unspliced gag-pro-pol and singly spliced env mRNAs out of the nucleus of infected cells. These mRNAs carry a recognition sequence called Rex responsive element (RxRE or XRE) located at the 3' region of the long terminal repeat (LTR). This function is essential since most HTLV proteins are translated from unspliced or partially spliced pre-mRNAs that 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 (NLS) and nuclear export (NES) signals leads to continuous shuttling between the nucleus and cytoplasm. SIMILARITY: Belongs to the deltaretrovirus Rex protein family."}
+{"protein": "MSDKVLVIGAGPNRIGQGIEFDYCTVHAVWAIQEEGYKAIIVNNNPETVSTDYDTSDKLYFEPITLEDVLNIVEKERPIGVLTQFGGQTSVNLTVPLAERGVRVLGTDPDDVDRLEDRDRFSKLLKKLGIPQPESGTANDPEEAVEVAEDIGYPVLVRPSYVIGGRAMEIVYDEEDLRRYIEEAAKVSPEHPILIDRFIEGGIECEIDGARDEAGNVLIPGIMEHIEEAGVHSGDSACVVPPQTLPEHAQETVLEYAEDIAEGANVIGLINIQFVYDPEEDEVYVIEANPRASRTVPFISKAVGIPLAKIGTKAILGREIPEVLDEMGLEPPDGDPGIVAVKEAVFSFEKWPGVDPVLGPEMKATGEVMGIDRTFGAAYWKAQLAAGHELPLEGTAVISVADRDKPDIVPIARKLQRLGFDLLATRGTASHLREHGIECEVVRKVSEGSPNIVDLIREGEIDLIINTPTEGKDARRDGYAIRRAAVKFKVPYITTIAAAKAAVEAIELVKEKGVTVNCLHDIHKGDWTPREVKPEELTRYGG", "text": "SIMILARITY: Belongs to the CarB family."}
+{"protein": "MKPLHYTASALALGLALMGNAQAVTTIPFWHSMEGELGKEVDSLAQRFNAENPDYKIVPTYKGNYEQNLSAGIAVFRTGNAPAILQVYEVGTATMMASKAIKPVYDVFKEAGIQFDESQFVPTVSGYYSDSKTGHLLSQPFNSSTSVLYYNKDAFKKAGLDPEQPPKTWQDLADYSAKLKASGIKCGYASGWQGWIQLENFSAWNGLPFASKNNGFDGTDAVLEFNKPEQVKHIAMLEEMNKKGDFSYVGRKDESTEKFYNGDCAMTTASSGSLANIREYAKFNYGVGMMPYDADAKDAPQNAIIGGASLWVMQGKDKETYTGVAKFLDFLAKPENAAEWHQKTGYLPITKAAYDLTREQGFYEKNPGADTATRQMLNKPPLPFTKGLRLGNMPQIRVIVDEELESVWTGKKTPQQALDTAVERGNQLLRRFEKSTKS", "text": "FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn- glycerol-3-phosphate (G3P) import. Binds G3P. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
+{"protein": "MFRSCVPKAITSSRCFARMYSKDVRFGSGVRAMMIRGVDILADAVAVTMGPKGRSVIVERPWTSPKITKDGFTVARSIALKDQHMNLGAKLVQDVADNTNESAGDGTTTATVLARAIAKEGFNQITMGANPVEIRRGVMLAVDVVKDKLKEMSKAVETREEIQQVATLSANGDTEIGRLIGEATDKVGPRGTITVKDGKRLKDELNIIQGLRFDNGYVSPFFVNSSKGSKVEFANALVMISLKKITGLSQIVKGLEQSLRQRRPLIIIAEDISGEALNALVLNKLRLGLQVCAVKSPSYGHHRKELIGDISAATGATIFGDDINYSKMEEAKLEDLGQVGEAVISKDSTMLLQGKPKTGLLEMRIQQIQDELAEKQIKPEQRDRLRQRLSALTKGVAVLHIGGGSEVEVNEKKDRVVDALNATRAAIEEGIVPGGGTAFLRCIPYLQELKTESADLQKGVDIVCNALRMPCQTIAQNAGVDGPMVVAKVLNGSEDYGYDAMGDEYCRLVEKGIIDPTKVLRTAITDAAGVASLLSTTEVVITDSRNDDLLSKLSGAGGGMDDGLDMNMGGLEELAALSGLGGMGGMGGMGGMGGMGGMGGGFGGMGAGGGMSASASNDGPTAEEMNEMVKAIPGMEQVEVRDIDSGMM", "text": "FUNCTION: Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the chaperonin (HSP60) family."}
+{"protein": "MRAHPGGGRCCPEQEEGESAAGGSGAGGDSAIEQGGQGSALAPSPVSGVRREGARGGGRGRGRWKQAARGGGVCGRGRGRGRGRGRGRGRGRGRGRPQSGGSGLGGDGGGGAGGCGGGSGGGVAPRRDPVPFPSGSSGPGPRGPRATESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYFSPSGKKFRSKPQLARYLGNAVDLSSFDFRTGKMMPSKLQKNKQRLRNDPLNQNKGKPDLNTTLPIRQTASIFKQPVTKFTNHPSNKVKSDPQRMNEQPRQLFWEKRLQGLSASDVTEQIIKTMELPKGLQGVGPGSNDETLLSAVASALHTSSAPITGQVSAAVEKNPAVWLNTSQPLCKAFIVTDEDIRKQEERVQQVRKKLEEALMADILSRAADTEEVDIDMDSGDEA", "text": "FUNCTION: Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides (PubMed:9774669). Binds hemimethylated DNA as well (By similarity). Recruits histone deacetylases and DNA methyltransferases to chromatin (By similarity). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). Acts as transcriptional repressor and plays a role in gene silencing (By similarity). Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression (By similarity). May enhance the activation of some unmethylated cAMP-responsive promoters (By similarity). Selectively represses transcription activity of methylated rRNA promoters (PubMed:14610093). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Nuclear, in discrete foci. Detected at replication foci in late S phase. Localizes to methylated chromatin. Localizes to sites of DNA damage in a manner partially dependent on ZMYND8."}
+{"protein": "MATVAFHTLGCKVNHYETEAIWQLFKEAGYERRDFEQTADVYVINTCTVTNTGDKKSRQVIRRAIRQNPDGVICVTGCYAQTSPAEIMAIPGVDIVVGTQDREKMLGYIDQYREERQPINGVSNIMKARVYEELDVPAFTDRTRASLKIQEGCNNFCTFCIIPWARGLLRSRDPEEVIKQAQQLVDAGYKEIVLTGIHTGGYGEDMKDYNFAKLLSELDTRVEGVKRIRISSIEASQITDEVIEVLDRSDKIVNHLHIPIQSGSNTVLKRMRRKYTMEFFADRLNKLKKALPGLAVTSDVIVGFPGETEEEFMETYNFIKEHKFSELHVFPYSKRTGTPAARMEDQVDENVKNERVHRLIALSDQLAKEYASQYENEVLEIIPEEAFKETEEENMFVGYTDNYMKVVFKGTEDMIGKIVKVKILKAGYPYNEGQFVRVVEDEITEHMRLSS", "text": "FUNCTION: Catalyzes the methylthiolation of N6- threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methylthiotransferase family. MtaB subfamily."}
+{"protein": "DLVEFGFMIRCANRNSQPAWQYMDYGCYCGKRGSGTPVDDVDRCCQTHNECYDEAAKIPGCKPKWTFYFYQCGSGSQFTCRKSKDVCRNVVCDCDFKAALCLTGARYNSANYNIDIKTHCR", "text": "FUNCTION: Snake venom oligomeric phospholipase A2 that has potent presynaptic neurotoxicity. Chain B is not itself neurotoxic, but it is essential for the neurotoxicity of textilotoxin. Subunit B possesses a very low phospholipase activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. N49 sub-subfamily."}
+{"protein": "MDPALRSYHQRLRLYTPVAMGINLAASSQPLDPEGPIAVTPRPPIRPSSGKAPHPEAPRRSPNWATAGEVDVGDELIAISDERGPPRHDRPPLATSTAPSPHPRPPGYTAVVSPMALQAVDAPSLFVAWLAARWLRGASGLGAVLCGIAWYVTSIARGA", "text": "SUBCELLULAR LOCATION: Host nucleus, host nucleolus. SIMILARITY: Belongs to the HHV-1 US8.5 protein family."}
+{"protein": "MEVAPEQPRWMAHPAVLNAQHPDSHHPGLAHNYMEPAQLLPPDEVDVFFNHLDSQGNPYYANPAHARARVSYSPAHARLTGGQMCRPHLLHSPGLPWLDGGKAALSAAAAHHHSPWTVSPFSKTPLHPSAAGAPGGPLSVYPGAAGGSGGGSGSSVASLTPTAAHSGSHLFGFPPTPPKEVSPDPSTTGAASPASSSAGGSVARGEDKDGVKYQVSLSESMKMEGGSPLRPGLATMGTQPATHHPIPTYPSYVPAAAHDYGSSLFHPGGFLGGPASSFTPKQRSKARSCSEGRECVNCGATATPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTCCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNVNRPLTMKKEGIQTRNRKMSSKSKKSKKGAECFEELSKCMQEKSPPFSAAALAGHMAPVGHLPPFSHSGHILPTPTPIHPSSSLSFGHPHPSSMVTAMG", "text": "FUNCTION: Transcriptional activator which regulates endothelin-1 gene expression in endothelial cells. Binds to the consensus sequence 5'- AGATAG-3'. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MRLGNAYAYCKPSQNVGLKLDLLRGLPGYVGHATSRINRLENQDNYSIKMMRSWPNAYGSALNCSVFDGHGEKGAQLSQLLADKLCSSLDFPEPSWDKQDLKKLVQEYARRFPEGNYWKHKLSTFEKFYNKFIKNCNSKQELLLMKEGDSAILGQNGGRMIFDKMGNIIDKIALLTELDRLRLFYGFARFDLDQCCGLGTAAGSTASSIFLYPYDDPNAPIDEGKDDDSWIISHSGLLKLIVTQVGDSKIILCDQDGIAHALTTTHHINSSRERHRLSIDPSRLDPDAFGETRFLNNFANTRSFGDVAGKPYGISSEPDIFSFLVGNTLHLPRSERSKLPFNGDECFLALVTDGITNKLADQEVVDLITSTVNSWGLKKATPQFVAEETIKFIQAIATKHSDNATCVVVRLSNWGNWPNVDRTGPQRETKLMNAQSNETKLN", "text": "FUNCTION: Protein phosphatase that shows typical type 2C protein phosphatase (PP2C) activity (PubMed:17002782). Catalyzes the dephosphorylation and concomitant reactivation of the E1 alpha subunit (PDA1) of the pyruvate dehydrogenase complex (PubMed:18180296). Required for efficient mitophagy in stationary phase cells (PubMed:17166847). SUBCELLULAR LOCATION: Mitochondrion intermembrane space Mitochondrion matrix."}
+{"protein": "MIEVPEDNRSSQTKRKNTEKNCNELMVDEKMDDDSSPRDEMKDKLKGTKSLIIRKSELMAKKYDTWQLKAIFLFSAFICTFAYGLDSSIRGTYMTYAMNSYSAHSLISTVSVIVLMISAVSQVIFGGLSDIFGRLTLFLVSIVLYIVGTIIQSQAYDVQRYAAGAVFYYVGLVGVMLQVVLMLSDNSSLKWRLFYTLIPSWPSIITTWVSGSVVEAANPLENWSWNIAMWAFIFPLCCIPLILCMLHMRWKVRNDVEWKELQDEKSYYQTHGLVQMLVQLFWKLDVVGVLLFTAGVGCILVPLTLAGGVSTNWRNSKIIGPFVLGFVLVPGFIYWESRLALVPFAPFKLLKDRGVWAPLGIMFFICFVYQMAAGYLYTILVVAVDESASSATRIINLYSFVTAVVAPFLGLIVTRSSRLKSYIIFGGSLYFITMGLFYRYRSGQDADGGIIAGMVIWGLSSCLFDYPTIVSIQSVTSHENMATVTALNYTVFRIGGAVAAAISGAIWTQSLYPKLLHYMGDADLATAAYGSPLTFILSNPWGTPVRSAMVEAYRHVQKYEVIVALVFSAPMFLLTFCVRDPRLTEDFAQKLPDREYVQTKEDDPINDWIAKRFAKALGRS", "text": "FUNCTION: Involved in the transport of siderophore triacestylfusarinine C and so has a role in iron homeostasis. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MNSVSAAERLKSFGDAGPVCNKSIIFPSRVVTLANSFEKKDRSWYVKSQIPTDLSIQVNDITFKAHKFPLISKCGYISSIELKPSTSENGYHLKLENFPGGADTFETILKFCYNLPLDLNPLNVAPLRCASEYLYMTEEFEAGNLISKTEAFITFVVLASWRDTLTVLRSCTNLSPWAENLQIVRRCCDLLAWKACNDNNIPEDVVDRNERCLYNDIATLDIDHFMRVITTMKARRAKPQITGKIIMKYADNFLPVINDDLEGIKGYGLGKNELQFSVNRGRMEESNSLGCQEHKETIESLVSVLPPQSGAVSCHFLLRMLKTSIVYSASPALISDLEKRVGMALEDANVCDLLIPNFKNEEQQERVRIFEFFLMHEQQQVLGKPSISKLLDNYLAEIAKDPYLPITKFQVLAEMLPENAWKCHDGLYRAIDMFLKTHPSLSDHDRRRLCKTMNCEKLSLDACLHAAQNDRLPLRTIVQINTQVLFSEQVKMRMMMQDKLPEKEEENSGGREDKRMSRDNEIIKTLKEELENVKKKMSELQSDYNELQQEYERLSSKQKSSHNWGLRWQKVKKSFQTKREDEETRERTRRRSSTGQRTSFRRRMSMS", "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 (By similarity). Involved in leaf vasculature patterning (PubMed:18643975). SIMILARITY: Belongs to the NPH3 family."}
+{"protein": "MKCEHCTRKECSKKSKTDDQENVSSDGAQPSDGASPAKESEEKGEFHKLADAKIFLSDCLACDSCVTVEEGVQLSQQSAKDFLHVLNLNKRCDTSKHRVLVVSVCPQSLPYFAAKFNLSVTDASRRLCGFLKSLGVHYVFDTTIAADFSILESQKEFVRRYHQHSEEQRELPMLTSACPGWVRYAERVLGRPIIPYLCTAKSPQQVMGSLVKDYFARQQNLSPEKIFHVVVAPCYDKKLEALREGLSTTLNGARGTDCVLTSGEIAQIMEQSDLSVKDIAVDTLFGDMKEVAVQRHDGVSSDGHLAHVFRHAAKELFGEHVEEITYRALRNKDFHEVTLEKNGEVLLRFAAAYGFRNIQNMIQKLKKGKLPYHFVEVLACPRGCLNGRGQAQTEDGHTDRALLQQMEGIYSGIPVRPPESSTHVQELYQEWLEGTESPKVQEVLHTSYQSLEPCTDGLDIKW", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NARF family."}
+{"protein": "MATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN", "text": "FUNCTION: Component of several N-terminal acetyltransferase complexes (PubMed:20154145, PubMed:29754825, PubMed:32042062). Inhibits the N- terminal acetylation activity of the N-terminal acetyltransferase NAA10-NAA15 complex (also called the NatA complex) (PubMed:29754825, PubMed:32042062). Has chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT in neuronal cells probably while associated with the NatA complex (PubMed:17947297, PubMed:20154145). May play a role in the NatA complex-mediated N-terminal acetylation of PCNP (PubMed:20154145). FUNCTION: Component of several N-terminal acetyltransferase complexes (By similarity). Inhibits the N-terminal acetylation activity of the N- terminal acetyltransferase NAA10-NAA15 complex (also called the NatA complex) (By similarity). Has chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT in neuronal cells probably while associated with the NatA complex (By similarity). May play a role in the NatA complex-mediated N-terminal acetylation of PCNP (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Within the NatA/HYPK complex, may localize to ribosomes. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Within the NatA/HYPK complex, may localize to ribosomes."}
+{"protein": "MALCQTSVLKVYHAVIEDVITNVRDAFLDEGVDEQVLQEMKQVWRNKLLASKAVELSPDSGDGSHPPPIVANNPKSHKAANAKAKKAAAATAVTSHQHIGGNSSMSSLVGLKSSAGMAAGSGIRNGLVPIKQEVNSQNPPPLHPTSAASMMQKQQQAASSGQGSIPIVATLDPNRIMPVNITLPSPAGSASSESRVLTIQVPASALQENQLTQILTAHLISSIMSLPTTLASSVLQQHVNAALSSANHQKTLAAAKQLDGALDSSDEDESEESDDNIDNDDDDDLDKDDDEDAEHEDAAEEEPLNSEDDVTDEDSAEMFDTDNVIVCQYDKITRSRNKWKFYLKDGIMNMRGKDYVFQKSNGDAEW", "text": "FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIA subunit 1 family."}
+{"protein": "MLKAVQILGWSSGLTISQRLTKTRKSSTVSFISSSLNLSSVTSSSPRRIFSFKPTRMSSSLPGSDPVANSPTFVSVQSAGDVRKIKFCQWCGGPTKHEIPDGEEKLRAICTHCGKIAYQNPKMVVGCLIEHEGKVLLCKRNIQPSHGLWTLPAGYLEVGESAAQGAMRETWEEAGATVEVISPFAQLDIPLIGQTYVIFLAKLKNLHFAPGPESLECRLFALDEIPFDSLAFSSIYVTLNLYLEDLKKGKLKFHYGTINKRPGSSPSDIRAFSLDYHLQP", "text": "FUNCTION: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use FAD and ADP-ribose as substrates. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Nudix hydrolase family."}
+{"protein": "RDSTTHQSHFRGGVGVTKISFKPHGFRAIRASVMPSEGQQQSSLGDSLVNSPHRNDVVDVIRKSAISNCLSETNLHNTVPGLVSKTRGKVRDIYDAGDYLVLVTTDRQSAFDRILASIPFKGQVLNETSLWWFERTKQIVPNAVVSAPDKNVTIAKKCSVFPVEFVARGFVTGSTDTSLWTVYNKGARNYCGNVLPDGMVKNQKLSENILTPTTKAADHDVPVTPDEIIERGLMTRSDYEEVSEKALSLFEYGQQVASEHGLILVDTKYEFGKANDGSIMLIDEVHTPDSSRYWIASSYPERFQNGLEPENIDKEFLRLWFKSHCNPYEDEVLPDAPEDLL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the SAICAR synthetase family."}
+{"protein": "LYRHIVTIAVFIILLFVLCLCVCLVLCCLLPLLLSQYVFAAALLLILCFWFVVATSQLTTFFVYLIFFYLPCLLLHLYTFLLLQ", "text": "SIMILARITY: Belongs to the papillomaviridae E5 protein family."}
+{"protein": "MKIYVDGREVIINDNERNLLEALKNVGIEIPNLCYLSEASIYGACRMCLVEINGQITTSCTLKPYEGMKVKTNTPEIYEMRRNILELILATHNRDCTTCDRNGSCKLQKYAEDFGIRKIRFEALKKEHVRDESAPVVRDTSKCILCGDCVRVCEEIQGVGVIEFAKRGFESVVTTAFDTPLIETECVLCGQCVAYCPTGALSIRNDIDKLIEALESDKIVIGMIAPAVRAAIQEEFGIDEDVAMAEKLVSFLKTIGFDKVFDVSFGADLVAYEEAHEFYERLKKGERLPQFTSCCPAWVKHAEHTYPQYLQNLSSVKSPQQALGTVIKKIYARKLGVPEEKIFLVSFMPCTAKKFEAEREEHEGIVDIVLTTRELAQLIKMSRIDINRVEPQPFDRPYGVSSQAGLGFGKAGGVFSCVLSVLNEEIGIEKVDVKSPEDGIRVAEVTLKDGTSFKGAVIYGLGKVKKFLEERKDVEIIEVMACNYGCVGGGGQPYPNDSRIREHRAKVLRDTMGIKSLLTPVENLFLMKLYEEDLKDEHTRHEILHTTYRPRRRYPEKDVEILPVPNGEKRTVKVCLGTSCYTKGSYEILKKLVDYVKENDMEGKIEVLGTFCVENCGASPNVIVDDKIIGGATFEKVLEELSKNG", "text": "FUNCTION: Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2) (PubMed:19411328). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2) (PubMed:19411328). The alpha subunit contains the catalytic H-cluster (PubMed:19411328). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MQQHPDQLKLEEEPYLKGTVNTVIYHNDTNLYTVLKVKVTETSEAIEDKAVSVTGYFPALQEEETYTFYGKIVTHPKFGLQFQAEHFKKEIPTTKEGIIQYLSSDLFEGIGKKTAEEIVKKLGDSAINKILADASVLYDVPRLSKKKADTLAGALQRHQGLEQIMISLNQFGFGPQLSMKIYQAYESETLEKIQENPYQLVKDVEGIGFGKADELGSRMGLSGNHPERVKAAILYTLETTCLSEGHTYIETEQLIIDTQSLLNQSAREGQRITEMDAANAIIALGENKDIVIEDGRCYFPSLFYAEQNVAKRVKHIASQTEYENQFPESEFLLALGELEERMDVQYAPSQKEAIQKALSSPMLLLTGGPGTGKTTVIRGIVELYGELHGVSLDPSAYKKDEAFPIVLAAPTGRAAKRMSESTGLPAVTIHRLLGWNGAEGFTHTEDQPIEGKLLIIDEASMLDIWLANHLFKAIPDHIQIIIVGDEDQLPSVGPGQVLRDLLASQVIPTVRLTDIYRQAEGSSIVELAHQMKNGLLPNNLTAPTKDRSFIRCGGSQIKEVVEKVVANALKKGYTAKDIQVLAPMYRGKAGINELNVMLQDILNPPKEKRRELKFGDVVYRTGDKILQLVNQPENNVFNGDIGEITSIFYAKENTEKEDMAVVSFDGNEMTFTKKDFNQFTHAYCCSIHKSQGSEFPIVVLPVVKGYYRMLRRNLLYTAITRAKKFLILCGEEEALEWGVKNNDATVRQTSLKNRLSVQVEEMDAELEALQKELPFSVHDANIGMEGITPFDFMKEEQQ", "text": "FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity. SIMILARITY: Belongs to the RecD family. RecD-like subfamily."}
+{"protein": "MAEAQIKKNIFTISSSPHVRCDESVSKIMWSVCLALTPAAVFGVFNFGIHALEVIITGIIAAVVTEYFVEKVRNKPITITDGSAFLTGLLLSMCLPPDIPPYMVAIGSFIAIAIAKHSMGGLGQNIFNPAHIGRAALMVSWPVAMTTWSKLSASGVDAVTTATPLGILKLQGYSKLLETFGGQGALYKAMFLGTRNGSIGETSTILLVLGGLYLIYKKYINWQIPVVMIGTVGILTWAFGGTTGIFTGDPVFHMMAGGLVIGAFFMATDMVTIPMTIKGQIIFALGAGALTSLIRLKGGYPEGVCYSILLMNAVTPLIDKFTQPVKFGTRR", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Couples electron transfer from reduced ferredoxin to NAD(+) with translocation of H(+) out of the cell. Essential for energy conservation during autotrophic growth. Contributes to ATP synthesis during heterotrophic growth. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrB/RnfD family."}
+{"protein": "MARLLKAVTVCALAGIAHAFNYDQPYRGQYHFSPQKNWMNDPNGLLYHNGTYHLFFQYNPGGIEWGNISWGHATSEDLTHWEEQPVALLARGYGSDVTEMYFSGSAVADVNNTSGFGKDGKTPLVAMYTSYYPVAQTLPSGQTVQEDQQSQSIAYSLDDGLTWTTYDAANPVIPNPPQPYQAQYQNFRDPFVFWHDESHKWVVVTSIAELHKLAIYTSDNLKDWKLVSEFGPYNAQGGVWECPGLFKLPLDGGSSTKWVITSGLNPGGPPGTVGSGTQYFVGEFDGTTFTPDADTVYPGNSTANWMDWGPDFYAAAGYNGLSIKDHVHIGWMNNWQYGANIPTYPWRSAMAIPRHLALKTINNKTTLVQQPQEAWSSISSKHPLYSRTYSTFSEGSTNASTTGETFRVDLSFSATSKASTFAIALRASANFTEQTLAGYDFAKQQIFLDRTKSGDVSFDNTFASVYHGPLVPDSTGMVRLSIFVDRSSVEVFGGQGETTLTAQIFPSNDAVHARLVSTGGATEDVRVDVHNITSTWN", "text": "FUNCTION: Exo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. Splits off terminal fructose units successively from the non-reducing end of the inulin molecule, and also hydrolyze sucrose and raffinose. FUNCTION: Exo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. Splits off terminal fructose units successively from the non-reducing end of the inulin molecule, and also hydrolyze sucrose and raffinose. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 32 family."}
+{"protein": "MTQSNLLPKTFRTKSGKEISIALGTGTKWKQAQTINDVSTELVDNILLGLKLGFRHIDTAEAYNTQKEVGEALKRTDVPREDIWVTTKYSPGWGSIKAYSKSPSDSIDKALAQLGVDYVDLFLIHSPFFTTEQTHGYTLEQAWEALVEAKKAGKVREIGISNAAIPHLEKLFAASPSPEYYPVVNQIEFHPFLQNQSKNIVRFCQEHGILVEAFSPLAPLARVETNALAETLKRLAEKYKKTEAQVLLRYTLQRGILPVTTSSKESRLKESLNLFDFELTDEEVNEINKIGDANPYRAFFHEQFKDL", "text": "FUNCTION: NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. Reduces ketopantoyl lactone (2-dehydropantolactone), isatin and camphorquinone. Does not act on menadione, p-nitrobenzaldehyde and pyridine-3-aldehyde. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MSLREQMGADTLIAEYTPPDVIQKFMTGGDVGHDKDGSVLRIEPWGYLDMKGIMYSCKKSDLEKSKLLQCEKHLKDLEAQSEKVGKPCTGLTVVFDMENVGSKHMWKPGLDMYLYLVQVLEDNYPEMMKRLFVINAPTLFPVLYKLVKPLLSEDMKNKIFVLGGDYKDTLLEYIDAEELPAYLGGTKSEGDEKCSELICHGGEVPKEFYLENTDDFETMETITVGSGDKIYVEYEIENENTYIKWEYKTEEHDIGFGLFRKNGDEWEEVVPIERTDCSIMTLDGSHKCKDPGTYALCFDNSFSMMTSKNVRYTAEVMDPEVDSEDINKMIKDSTWDELSAQIS", "text": "FUNCTION: Shuttles 11-cis- and all-trans-retinals between rhodopsin and retinochrome and regenerates the photoproducts of both pigments. Also binds weakly to retinol."}
+{"protein": "MESNNVVLLDFSGSSFGMRLRIALALKGIKYEAKEENLSDKSPLLLEMNPVHKKIPILIHNGKPICESLNILEYIDEVWHEKCPLLPSDPYQRSQARFWANYIDNKIYSTGRRVWSGKGEDQEEAKKEFIEIFKTLEGELGNKTYFGGDNLGFVDVALVPFTSWFYSYETCANFSIEAECRKLVVWQNCMENERVSKSLPHPHKIYDFVLELKHKLGLA", "text": "FUNCTION: May play an important role in hormonal and growth regulatory responses. SIMILARITY: Belongs to the GST superfamily. HSP26 family."}
+{"protein": "MPGKPVNLASPNERKLNFWERLYLPAVVQGLAYTWRKMRSPRYTFQYPDELWYPPDSYRGRPVLVEENGRPRCVACGLCARACPPLAISMQAKEVDDVKEREPAWFEINMLRCIYCGYCEEVCPEEAIVMSKEYDLTFQSRDEAIFGLEKLLVPAERLKDRLEWLDRYKDPQYGQHWEFRKENNLHSLKDRPFLKWLLEEEGMEELKSTHLRPEEPVAAERSWGGVRAEG", "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. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 23 kDa subunit family."}
+{"protein": "MLSAKGVSLGLGLGLGAWGPVLLGVVGVAGAIALYGYYKNRNAEPAAAEAV", "text": "FUNCTION: Might be involved in magnetite crystal growth. SUBCELLULAR LOCATION: Magnetosome membrane; Single-pass membrane protein Note=Tightly associated with magnetite crystals. SIMILARITY: Belongs to the magnetosome MamD/Mms5 family."}
+{"protein": "MRLFVLLAYIIPFILCQLTPVLVASHKLVRGLKEEINPSNTLPHNVTSVTNMLKKLITECSSDAYLLINQPGLTYADLTTEKKDNWPFLRNYLYMSSTIVGLPRVENPIDLDFLEQYIISNCDAETINVWHDSEDEVVDYYDIRKRVIRIDLSPLSISNHDDRVKEIFEHDQLIRKILRKLPSAHYTIILTSLEPGIIHPVPRFLMEETPASFEIFDDIINDPFHNREIEKNDRFHKVEPNWNPIRDSNDRYYRNKKKDEIHLFDYELWEKNEKLITTIFVMVLSLFMMKIISFFNYLKQKIIQKKQQKSKRGIIADDKKLD", "text": "FUNCTION: Required for normal beta-1,6-glucan synthesis, for hyphal morphogenesis, adhesion and virulence. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the BIG1 family."}
+{"protein": "MRVRLGALAGAAALSGALSFVLLAAAIGTDFWYIIDTERLERSSQRMRDQGPANRSQQEPLSSHSGLWRTCRVQSSCTPLMNPFWQENVTVSDSSRQLLTMHGTFVILLPLSLIVMVFGGMTGFLSFLLRAHLLLLLTGILFLFGAMVTLTGISIYIAYSAVAFREAVCLLEERALLDQVDIRFGWSLALGWISFVSELLTGVVFLAAARALSLSQRQDQAI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=N- glycosylation at Asn-54 and Asn-88 is required for plasma membrane localization."}
+{"protein": "MSKTVNFRATKNFYLQFVSVSSRDTSCIPCIHLFFDSKRYVFGSVGEGCQRAILSQQLRLSKIKDVFLMQGSSISSPDTYDSSSSSSTTSVSDMLQLDDRDKVIVSERNSMCSTVNYPTWWDSCGGFPGFLLSLNDISEPGETGEASPFVLHGPSEVHQFLSSMRHFTYHTNVNLTVQGYTSAEAPVFVDENICVTPVVVSLVKNSFKKRKHENINRGTNARPLKEDRANTSPHWYSHVSNDTSFVVENAMYNTPAPLEPDKPELFISYIVQSHPTPGKFDAAKAKSLGITKGLDCGRLARGEPVTLENGKTVYPKEVIGPSIPGSSFFIIHCPNELVIDLVIENHKWTNAPKPVCVIHSVTPEVYKNPRYQSWISSFPSEVSHLIASTEVNEVINYPRSAVAIATLNLLDSKVFPLGFNCYEVKNVQKNNRIAFAKPKLRFAFGKKTGIDDSEVGVSIEELKDKILKEKPDYKSFVEEAQKYVSDKPKAPSFAGSDIQICTLGTGSAMPSLYRNVSSTYVRIPVDKKCMEDSAISMKNILLDCGEGTLGRLSRQYGDNLKYEIASLRWIYISHMHADHHAGVIGVLKAWTKYSDGRSKLFITAPPQFEFWLLEYSRIDYLPLSNIVFISNSALRTDRKPSALESSRLSSLFKEFDLVSFRTVPAIHCPYSYCMEITNSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAKKAGTKNVILTHFSQRYPKLPDIDISTEDLHIALAFDGMTLKISDISLFRYFGKPLAYLFNEENLKEESDPLKF", "text": "FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. May be involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RNase Z family."}
+{"protein": "MAFKFKTFAAVGALIGSLALVGCGQDEKDPNHIKVGVIVGAEQQVAEVAQKVAKDKYGLDVELVTFNDYVLPNEALSKGDIDANAFQHKPYLDQQLKDRGYKLVAVGNTFVYPIAGYSKKIKSLDELQDGSQVAVPNDPTNLGRSLLLLQKVGLIKLKDGVGLLPTVLDVVENPKNLKIVELEAPQLPRSLDDAQIALAVINTTYASQIGLTPAKNGIFVEDKDSPYVNLIVTREDNKDAENVKKFVQAYQSDEVYEAANKVFNGGAVKGW", "text": "FUNCTION: This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the NlpA lipoprotein family."}
+{"protein": "MAASRAPRRRLEDLSVDEFLASGFESGSESELEGAAEERRARGAAWNRERRGARTSPGPAGRLRKGRASEHKDQLSRLKDRDPEFYKFLQENDRSLLDFSDSDSSAEEEEPFHSLPDTLEEASETEEDGGEDSDALPRGLRSKKNEPVPVTLAMVERWRQGSRHHLTPRLFHEVVQAFRAAVATTQGEQEAAETCRFQVADSAVFNALVTFCIRDLCGCLQKLLFGKTPKDSNRLLLPSSSPLWGKLRVDVKSYLSAVVQLAACLAEATVSAAVLQHISSLVPYFLTFPKQCRMLLKRMVVLWSTGEESLRVLAFLVLIRVCRHKKEAFLGPILKQMYIMYVRNCKFTSPSTLPLISFMQRTLTEMLALDPSVSYQHAFLYIRQLAVHLRNAMTTGKKETHQSVYNWQYVHCLYLWCRVLSTLGSSEILQPLLYPLSQIIIGCIKLLPTARFYPLRMHCVRALTLLSQTIGTFIPVLPFILEIFQQVDFNRRPGRMSSKPINFSVILKLSSTNLQEKAYRDGLLEQLCDLILEYLHSQAHSIAFPELVLPTVLQLKSFLRECKVANYCRQVRQLLEKVQENARHIESLRQSATFSVSDRTAVDAWEKQVREEGTPLTRYYGHWKKLRDREIQLEISGKERLEDLNFPEIKRRKVEDRKDEDRKELKDLFELDSSEGEDSTDFFERGVPRLPEAHQGLKEDQEEEDKEEGDSDSEDGDTDTGVDLSELWQLAQGAQDELEDLQLSEED", "text": "FUNCTION: Acts as an inhibitor of histone acetyltransferase activity; prevents acetylation of all core histones by the EP300/p300 histone acetyltransferase at p53/TP53-regulated target promoters in a histone deacetylases (HDAC)-independent manner. Acts as a transcription corepressor of p53/TP53- and TP63-mediated transactivation of the p21/CDKN1A promoter. Involved in the regulation of p53/TP53-dependent apoptosis (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus Note=Translocates from the nucleoli to the nucleoplasm in presence of several stressors like ultraviolet irradiation and actinomycin-D. Predominantly detected in the nucleoli in non-mitotic cells. Predominantly detected in nucleoplasma in cells undergoing mitosis (By similarity). SIMILARITY: Belongs to the NOC2 family."}
+{"protein": "MALEKIIRESLTGFIQCHIPHADLSALDEVFYAYATGVLEELGSQNSSEEDFEMESFVEMLEAYIPGFSEISSGKVYDMLFELSRRLSEARGKENVSPKPTAEVSFMTPTSSSTESSKKIETEPLEGAVAQEKDDAKNGIDLLLEIFPSCTVSQAQTALSMAKGDLEDAVQIIVDGKVIADNHSGSKDLQGAPKTDDLKDFILQKYMLVDTEDDKKTYRPVAPKEAPKKMIRYIDNQVVSTKGERYKDIKKPESEEMKKTYINLKPARKYKFH", "text": "FUNCTION: May play a role in targeting proteins for ubiquitination and subsequent proteasomal degradation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CUEDC2 family."}
+{"protein": "MSITQKVRNWVEEFDVIVARSAFGRWFRLEGCGHPRERKGSRFSLEISAGLTTFFAMAYILAVNATILVDTGGTCECTEANRDDCDKLDDYVLCKEDFHRDLVTATAAISALASFCMGLFANMPVGMAPGMGLNAYFAYQVVGYNGTGRVSYREALLAVFVEGFIFTGLTVIGLRQWLARVIPASLKFATGAGIGLYLTIIGLSPSAGLGVIGHSSSDIVALGGCPPEYLNADYSCNGHQLQSGRMWVGIFCGGVLTAILMMYKFKGAVLAGIALVTITSWPRRSLVTMFPHTLTGDYNFDFFKKVVSFRKINRILVAQQWNVTGGQFAIALITFLYVDIMDMTGTLYSMANYAGLVDPRTQDFEGSAVAYIVDALSISIGSLFGCSPVTAFIESGSGISAGGRTGILGMVVGICFFISLFFAPIFSSIPVWATGSTLVLVGSMMMKSTTLINWSYLGDSIPAFITIALMPFTYSIAYGLIAGIICYALLNSIIYAIDKMSRGRLVPADYNQKEAWTWRVEGGLLPQWVRRLFKGNRRFWEDPDDRKAMDNATLEMATSRSYSEDGKNEKTTHEDVTMKETSLKKMDDERISVDEAVGESESFSNRQQDFRTPYAGIDMDTDDRI", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily."}
+{"protein": "MEDQRRGQGEEEDDSGSLPSPPLLPAHRNTDFFIDNILRPDFGCKRERERVTRDSGVRPTALPDSRSDGVSSSASSTVSSPVSSRQSNKVEQGSSKSSSPSKDSQKQILWPAWVYCTRYSDRPSSGPRTRKLKKKNNNTESDDKRPRTAFTAEQLQRLKAEFQTSRYITEQRRQALARELGLNESQIKIWFQNKRAKIKKSSGFKNALAMQLMAQGLYNHSTTTIQEEEDN", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the engrailed homeobox family."}
+{"protein": "MGRIGTPVFLAFLSALTCSLQVHAQVRDLKQCSNDPEFGRYCPTTCGVADVLSKYAKGVDEDSSFIDSVLTQLAAKHGIVEGNVNIVNEDVRITRDEAQIIKDSGQKTVQKILEEVRILEQIGVSHDAQIQELSEMWRVNQQFVTRLQQQLVDIRQTCSRSCQDTTANKISPITGKDCQQVVDNGGKDSGLYYIKPLKAKQPFLVFCEIENGNGWTVIQHRHDGSVNFTRDWVSYREGFGYLAPTLTTEFWLGNEKIHLLTGQQAYRLRIDLTDWENTHRYADYGHFKLTPESDEYRLFYSMYLDGDAGNAFDGFDFGDDPQDKFYTTHLGMLFSTPERDNDKYEGSCAEQDGSGWWMNRCHAGHLNGKYYFGGNYRKTDVEFPYDDGIIWATWHDRWYSLKMTTMKLLPMGRDLSGHGGQQQSKGNSRGDN", "text": "FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MPRRPPFWLTLLIILIGLPLCLPFLYVILRATEVGLTRSVELLFRPRMAELLSNTMLLMVCVTIGAISLGTFCAFLLERYRFFGKAFFEVAMTLPLCIPAFVSGFTWISLTFRVEVFWGTIGIMTLSSFPLAYLPVSAILKRLDRSLEEVSLSLGKSPVYTFWYAISPQLKPAIGSSILLIALHMLVEFGAVSILNYQTFTTAIFQEYEMSFNNSTAALLSAVLMAICILIVFGEIFFRGKQTLYHSGKGVTRPYLVKTLSFGKQCLTFGFFSSIFILSIGVPVIMLIYWLIVGTSLESAGDFSEFLSAFSNSFIISGLGALLTVMCALPLVWAAVRYRSYLTIWIDRLPYLLHAVPGLVIALSLVYFSIHYANDLYQTFFVIIIAYFMLYLPMAQTTLRASLEQLSDQIEKVGQSLGRNPFYIFRTLTLPAILPGVAAAFALVFLNLMKELTATLLLTSNDIKTLSIAVWEHTSDAQYAAATPYALMLVLFSGIPVFLLKKYAFK", "text": "FUNCTION: Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1) involved in Fe(3+) ions 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. FbpB subfamily."}
+{"protein": "MNKLIYYFGNNGSDGNASMNNILGNKGAGLAEMSNLKLPIPNGFTITTELCNYFYKHNNNFPKNFQNELQQAISKLEVTTGKIFGSTTSNPLLLSVRSGSTVSMPGMMDTILNLGMNNEVCNALADACGNKLFALDSYRRFLEMYGSTVLSIPSDLFEQIYENHKIQADIYKDSDITVELLEKIIDDFKRLHIKYDKQLINDPYEQLESAIKAVLYSWKNNRAIIYRKLNNISEDFGTAINIQEMVFGNLGKTSATGVAFTRSPSTGEKKLFGEFLINAQGEDIVSGTRTPMPIIANDSNSMQAMMPEVFKELSQIAKKLEEHYLDMQDIEFTIENNKLYILQTRTAKRTAIAAINIAVQMVKEKLISKEQALMRIDPESLNQLLHTRIDYSKGLTSIAEGLPASPGAATGIVVFSPYDAEKLSHHHKVILVRHDTSPEDINGMHVSSGILTIRGGMTSHAAVVARGMGKPCVCGTNNLSIDEQKQILIAGDIVIKQGDIITIDGGSGKIFLGEMPLIQPTFSEESKLILDWADEISSLKVRANAETVNDALVSIKFGAQGIGLCRSEHMFFDKNKIPLVREMIIAPDIERRQCALQKLLPLQTEDFKSLFRVMKNKPVNIRLLDPPLHEFLPTTEEDKKNLANSLNLPLSMIHQRLHAMHEVNPMLGHRGCRLGICLPEIYQMQIEAIFTAIFELHKKEHIESNLELMIPLISNVAEIKKLKMYIYEVVQELEQRYSYKFSFTLGTMIELPRAALESKKIAKEVDYFSFGTNDLTQTTYGISRDDIASFLPYYLEEKIFESDPFTTLDEEGVGELIEIAIKRGKSSNANLKLGACGEHAGNPTSIAFFHKANLNYVSCSPYRIPIARIAAAQAKIKQGS", "text": "FUNCTION: Catalyzes the reversible phosphorylation of pyruvate and phosphate. SIMILARITY: Belongs to the PEP-utilizing enzyme family."}
+{"protein": "MSAAAAIASPIPAAIAVVQQQRRGRSRGGGSGAAAVRCSAVAPTSAIAPILADLRLRCAAPLPVLRRVADAMASGMRAGLADDGAGELKMIPSHVYSLPTGNETGLFYALDLGGTNFRVLRVQLGGKDKRIIDTEFEQVSIPREIMHGITEDLFDFIASGLSRFVATEGDKFHLPQGRKRELGFTFSFPVNQTSIDSGILIKWTKGFAVSGTAGKDVVACLNAAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYIQRTEAIPKLQHLKLETGNTIINTEWGAFSDGLPLTEFDREMDDESINPGEQIFEKTISGMYLGEIVRRVLVKMAEVSDLFGHSFPKKLAEPFVLRTPHLCAMQQDTSDNLGEVESILSDVIGVSQASLLARRVTVEVSDCIIRRGGRLAGAGIVGILEKMENDSRGHIFGRRTVVAMDGGLYEKYPQYRRYMKEAVAELLGPERSNRIAIEHTKDGSGIGAALLAAANSKYAAAQISTR", "text": "FUNCTION: Fructose and glucose phosphorylating enzyme. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the hexokinase family."}
+{"protein": "MTKKRKLEGEESNEAEEPSQKLKQTPEEEQQLVIKNQDNQGDVEEVEYEEVEEEQEEEVEDDDDEDDGDENEDQTDGNRIEAAATSGSGNQEDDDDEPIQDLLEPFSKEQVLSLLKEAAEKHVDVANRIREVADEDPVHRKIFVHGLGWDTKTETLIEAFKQYGEIEDCKAVFDKISGKSKGYGFILYKSRSGARNALKQPQKKIGSRMTACQLASKGPVFGGAPIAAAAVSAPAQHSNSEHTQKKIYVSNVGAELDPQKLLMFFSKFGEIEEGPLGLDKYTGRPKGFCLFVYKSSESAKRALEEPHKTFEGHILHCQKAIDGPKPGKQQQHHHNPHAYNNPRYQRNDNNGYGPPGGHGHLMAGNPAGMGGPTAQVINPAIGQALTALLASQGAGLAFNPAIGQALLGSLGTAAGVNPGNGVGMPTGYGTQAMAPGTMPGYGTQPGLQGGYQTPQPGQGGTSRGQHGVGPYGTPYMGH", "text": "FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein that acts as component of a complex regulating the turnover of mRNAs in the nucleus. Binds with high affinity to RNA molecules that contain U- rich sequences in 3'-UTRs. May function in complex with UBP1 and contribute to the stabilization of mRNAs in the nucleus. However, unlike UBP1, UBA2A does not stimulate pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus Note=Relocalizes into nuclear speckles in response to abscisic acid (ABA)."}
+{"protein": "MAEQSTKSVLFVCLGNICRSPIAEAVFRKLVTDQNISENWRVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHVARQITREDFATFDYILCMDESNLRDLNRKSNQVKTCKAKIELLGSYDPQKQLIIEDPYYGNDSDFETVYQQCVRCCRAFLEKAH", "text": "FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates with differences in substrate specificity between isoform 1 and isoform 2. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein phosphatase family."}
+{"protein": "MACLGPSAQVPELPEKNCGYREVQYWDQRYQGAADSAPYEWFGDFSCFRDLLEPELRPLDRILVLGCGNSALSYEIFLGGFPDVTSVDYSSVVVAAMRARYAHVPTLRWETMDVRALGFPSGSFDVVLEKGTLDALLTGEQDPWTVSSEGVHTVDQVLNEAGFRKRTSRLLGLHTQLELVLAGVSLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTQRFYLSCLQVERIEELGAQPLRDLIDKIGGWNVTGPWDQDNFMEVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGQPTSTREQMRQVLELEIQLANITVPQDQRRDEEKIYHKMSIAELQALAPSMDWLEFLSFLLSPLELGDSEPVVVYGTDYLQQVSELINRTEPSVLNNYLIWNLVQKTTSSLDHRFESAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRAAFEEALGHLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYTCNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACIEEQYSQYQVNGEKLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNSGQLCEVW", "text": "FUNCTION: Converts big endothelin-1 to endothelin-1 (PubMed:7797512). May also have methyltransferase activity (Probable). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Cytoplasmic vesicle, secretory vesicle membrane. SIMILARITY: In the N-terminal section; belongs to the methyltransferase superfamily. SIMILARITY: In the C-terminal section; belongs to the peptidase M13 family."}
+{"protein": "NFDEIDRSGFGFN", "text": "FUNCTION: Myotropic peptide, enhances both the frequency and amplitude of spontaneous hindgut contractions. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MAYGAPQCAQHLPPIGTPTLRQRSVSCYHFFRHSRGFLWFVLCNLLLTPNISDAQLLINVQNQGGEVIQESITSNIGEDLITLEFQKTDGTLITQLIDFRNEVQILKALVLGEEERGQSQYQVMCFATKFNKGDFISSDAMAKLRQKNPHTIRTPEEDKGRETYTMSSWVQLNRSLPITRHLQSLCAEATDATYVRDVDLKAWAELPGSSISSLEAATEKFPDALSTRCNEVSSLWAPCLCTLETCIGWYPCGLKYCKGKSVGGDTSGTQQQQQQTNYRCGIKTCRKCTQFTYYVRQKQQCLWDE", "text": "FUNCTION: Vital for proper neuronal development and hatching. SIMILARITY: Belongs to the OAF family."}
+{"protein": "MSFLIDSSIMVTSQVLFFGFGWLFFMRKLFKDYEVRQYVVQVIFSVTFAFSCTMFELIIFEILGVLNSSSRYFHWKLNLCVILLILVFMVPFYIGYFVVSNIRLLHRQKLLFACVLWLTFMYFFWKLGDPFPILSPKHGILSIEQLISRVGVIGVTLMALLSGFGAVNCPYTYMSYFLRNVTDADILALERRLLQTMDMIISKKKRIAVAHRTMFQRGEVHNKPTGFWGMIKSVTTSVAGSENLSLIQQEVDALEELSRQLFLETADLHATKERIEYSKTFQGKYFNFLGYFFSIYCVWKIFMATINIVFDRVGKTDPVTRGIEITVNYLGIQFDVKFWSQHISFILVGIIIVTSIRGLLITLTKFFYAISSSKSSNVIVLLLAQIMGMYFVSSVLLIRMSMPLEYRTIITEVLGELQFNFYHRWFDVIFLVSALSSILFLYLAHKQAPEKHMAL", "text": "FUNCTION: Voltage dependent anion channel required for acidification and functions of the Golgi apparatus that may function in counter-ion conductance (By similarity). Plays a role in lymphocyte development (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Golgi pH regulator (TC 1.A.38) family."}
+{"protein": "MGVVYGSQQNLSEYFYSSVNMAEVPDTFEENRGHSFEGVTLQRRHVKGMKSYGSDITPRRPKQLGLPKEVNTSECIDQGSWRKPSAFESLRSYSRKFSKRIFSFIGVESKSTVQRNASGADSTSLSHFTANEINKGNCKKTALSNEFNSANKGSKASGVGAELPSVNGFIEGELHDDNETDSFRINELAKQIQETSLGATTQEDESSDGICWDELSTTSPESSKVSEPIIQDNTQTTHINNDSSDIRFSSRCDLFADDADSDWEQDFNVKFDSPLIIPETVNSAGHTVREQLFEVKEFTRSIKDLKDLYEKANSKDIYDKDSEILGEAKAILRLADPANYSDLKDEDAQNILSKYKVKLEGDSSLDFDASMLPGLNDHVHYLMSQLQLLLH", "text": "FUNCTION: Involved in septation."}
+{"protein": "MEEEGEAQGRAVPGGRLNMSHGFVHHIRRNQLARDDYDREVKQAKEKQKKRYTPGPTRQKKPDLQVYHPRQREKAHTTETLKDEPNDNGTQLFCLDFEADGGEVTSIIVYEDDDAEQLATMISNQNQLEGDMREALKQRIQEEISKRRVQR", "text": "SIMILARITY: Belongs to the UPF0561 family."}
+{"protein": "MRGVVKELNDDGFGVLGNVLVPFSAPGDEVEILKIEKVKKAKIASKWKLIKSSPLRVGARCKVFGRCGGCSLQHLSYDYQLEFKGERIRRLLGVDVEVIPSPRIFGHRNRIDLAVTVEGIGFRERGKWWKIVDIQECPVFGKTSRKAIERLREFIEEERISVWNVKKDEGFLRYMVLREGKFTGEVMVNLVTKEGKLPDPSKYFDFATSIYWSVNRTKSDVSYGEVESVWGREFITEKLDDVIYLIHPNSFFQTNSYQAVNLVKKVSELVEGERVLDMYSGVGTFGIYLAKRGFKVVGFDSNEFAIEMARKNAKINKVDAVFDVATDREVEVNGFDTVIVDPPRVGLHPKLIKKLNREKPEVIVYVSCNPKTFARDIEKLEYKIDEIVALDMFPHTPHLELVAKLIV", "text": "FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in tRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family."}
+{"protein": "MDRVESEEPMDGFESPVFSENTSSNSGWCSDAFSDSYIAYNPALLLKNDLLFSELLFASHLINVPRAIENNVTYEASSAVGVDNEMTSSTTEFIEEIGDVLALDRACLVCRTLDLYKRKFGLTPEWVADYAMLCMKSLASPPCAVVTFSAAFEFVYLMDRYYLCRYNVTLVGSFARRTLSLLDIQRHFFLHVCFRTDGGLPGIRPPPGKEMANKVRYSNYSFFVQAVVRAALLSISTSRLDETETRKSFYFNQDGLTGGPQPLAAALANWKDCARMVDCSSSEHRTSGMITCAERALKEDIEFEDILIDKLKKSSYVEAAWGYADLALLLLSGVATWNVDERTNCAIETRVGCVKSYWQANRIENSRDVPKQFSKFTSEDACPEVAFGPILLTTLKNAKCRGRTNTECMLCCLLTIGHYWIALRQFKRDILAYSANNTSLFDCIEPVINAWSLDNPIKLKFPFNDEGRFITIVKAAGSEAVYKHLFCDLLCALSELQTNPKILFAHPTTADKEVLELYKAQLAAQNRFEGRVCAGLWTLAYAFKAYQIFPRKPTANAAFIRDGGLMLRRHAISLVSLEHTLSKYV", "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. Note=Mainly cytoplasmic in transfected cell culture. SIMILARITY: Belongs to the herpesviridae UL32 protein family."}
+{"protein": "MDSSREPTLGRLDAAGFWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDDTVMKANLHKVKQQFMTTQDASKDGRIRMKELAGMFLSEDENFLLLFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLARILALQENFLLQFKMDACSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVNKDGKIQKSELALCLGLKINP", "text": "SUBCELLULAR LOCATION: Cytoplasm. Secreted Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=Predominantly cytoplasmic. A small proportion is associated with secretory granules and membrane fractions (By similarity). Detectable in human serum after ischemic neuronal damage."}
+{"protein": "ELVSQLCLKKERVCEGSSLTISCPQKGAGISIARAIYGRTKTQVCPSDGATSNVNCKASNALNVVRDLCRGKSSCTVEASNDVFGDPCMHTYKYLELSYDCSK", "text": "FUNCTION: Rhamnose-binding lectin. Also binds alpha-D-melibiose, alpha- D-lactose, beta-D-lactose, methyl-alpha-D-galactopyranoside, methyl- beta-D--galactopyranoside and D-galactose but not D-arabinose, L- fucose, D-glucose, D-mannose, D-maltose, D-sucrose, N-acetyl-D- galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-mannosamine-D-xylose or by glycoproteins orosomucoid, thyroglobulin, ovomucoid and porcine stomach mucin. Shows cation-independent hemagglutinating activity against rabbit and human erythrocytes. Agglutinates cells of Gram- positive bacterial species S.aureus but not those of Gram-negative E.coli."}
+{"protein": "MPREDRATWKSNYFMKIIQLLDDYPKCFVVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCDVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHKRFLEGVRNVASVCLQIGYPTIASVPHSIVNGYKRVLAVAVETDYTFPLAEKVKAFLADPSAFVAAAPVVVETAAPAAAAAPAKEAPKEESEESDEDMGFGLFD", "text": "FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL10 family."}
+{"protein": "MEKERETLQVWKQRVGQELDSVIAFWMEHSHDQEHGGFFTCLGRDGQVYDHLKYVWLQGRQVWMYCRLYRTFERFRRVELLDAAKAGGEFLLSYARVAPPGKKCAFVLTQDGRPVKVQRTIFSECFYTMAMNELWKVTGEMHYQREAVEMMDQIIHWVREDPAGLGRPQLSGTLATEPMAVPMMLLNLVEQLGEEDEEMTDKYAELGDWCAHRILQHVQRDGQVVLENVSEDGKELPGCLGRHQNPGHTLEAGWFLLQYALRKGDPKLQRHIIDKFLLLPFHSGWDPEHGGLFYFQDADDLCPTQLEWNMKLWWPHTEAMIAFLMGYRDSGDPALLNLFYQVAEYTFHQFRDPEYGEWFGYLNQEGKVALTIKGGPFKGCFHVPRCLAMCEQILGALLQRLGPAPLGSLPAVPTREGSK", "text": "FUNCTION: Catalyzes the interconversion of N-acetylglucosamine to N- acetylmannosamine. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family."}
+{"protein": "MHQQKRQPELVEGNLPVFVFPTELIFYADDQSTHKQVLTLYNPYEFALKFKVLCTTPNKYVVVDAAGAVKPQCCMDIVIRHRDVRSCHYGVIDKFRLQVSEQSQRKALGRKEVVATLLPSAKEQQKEEEEKRIKEHLTESLFFEQSFQPENRTVSSGPSLLTVFLAVVCITALMLPTLGDVESLVPLYLHLSVNQKLVAAYILGLITMAIFRT", "text": "FUNCTION: Plays a role in differentiation and/or proliferation of mesenchymal stem cells. Proposed to be involved in epithelial-to- mesenchymal transition (EMT). However, another study suggests that it is not required for EMT or stem cell self-renewal and acts during later stages of differentiation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein."}
+{"protein": "MKVYCLLLVLLVGLVSQAHGQLDKKCQMVCTMDYRPVCGSDGRTYPNKCTLTSTACMSQRSITVFHDGEC", "text": "FUNCTION: Acts as a neurotoxin by inhibiting an ion channel (By similarity). May also act as a serine protease inhibitor, since it possess the kazal serine protease inhibitor signature. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conopeptide P-like superfamily."}
+{"protein": "MEGPTHPKPSKDKTFSWDLMILVGVLLRLDVGMANPSPHQIYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDQPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSITGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITLPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGNRLINLVQGTYLALNVTNPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSDPQHKLTISEVSGQGSCIGTVPKTHQALCKKTQKGHKGTHYLAAPSGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFDKTVRLRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFGQLQMAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIKQYDPDQP", "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 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). 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). SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane; Peripheral membrane protein Note=The R-peptide is membrane-associated through its palmitate."}
+{"protein": "MRFSTLHFAFLATLSSIFTVVAASDTTTCSSSKHCPEDKPCCSQFGICGTGAYCLGGCDIRYSYNLTACMPMPRMSTFQESFDSKDKVKEIELQSDYLGNSTEADWVYTGWVDYYDNSLLIQMPNHTTGTVVSSTKYLWYGKVGATLKTSHDGGVVTAFILFSDVQDEIDYEFVGYNLTNPQSNYYSQGILNYNNSRNSSVNNTFEYYHNYEMDWTEDKIEWYIDGEKVRTLNKNDTWNETSNRYDYPQTPSRIQFSLWPGGDSSNAKGTIEWAGGLINWDSEDIKKYGYYYAHIKEIYATAYDIPNDVKLDGNSTKESDYHAFLYNSTDGDASNIMLTTKKTWLGSDDATGFDPQNDDEDSSSNKAQETTITSVSGSSTITSVKTDSTKKTANVPAQNTAAAAQATAKSSTGTNTYDPSAGVGGFVQDSKSTDSGSSGSSSQGVANSLNESVISGIFASICLGILSFFM", "text": "FUNCTION: Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, filamentation, and adherence to host cells. Plays a role of cell surface antigen in acute candidemia patients. 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 16 family. CRH1 subfamily."}
+{"protein": "MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM", "text": "FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'- linked polyubiquitination. Mediates the selective degradation of short- lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by RIGI in response to viral infection. Essential for viral activation of IRF3. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
+{"protein": "MALFRLSAAIVVIFLYIWSPSQRIQCRCRSFERCWPSQQDWSALNNSISGHLVNPRPVAYVCHDPDFDHDACEHVRYMANNSLWRASMPGALQNTVWESSLVSTQTCLPFSAREQPCNQGRIPLYAAVVESKKEVQTAVRFARKYNLRLVIRNTGHDGAGSSSGPESFQIFTHRLNSILYHSNFCPGGSHSKYQTCAGPAVSIGAGVMFRDLYARGAERGFVVTGGDSGTVGAAGGFIQGGGVPAFMGYTWGLAVDNVLEFEVVVATGQLVIANADENADLFWALRGGGGGSFGIVVRVTMRTYPDLPTLKGELTVSGNRHDPSFWTEDIAGLLNALRAFNHLDAPGVFRLIQTSAKGSISAVLEVYLLNRTLAEDLTRMMGPILGTSRRKYNISPITVGKISSFANPNEPTITEFFGSTILSRNFFESPNGPLVMAKRMAAINLDPGDGLLTSNLGGRINNENSDLPLHPAWRSSAHLVSLVVNVDTSLRARERAMVRLTDELMPMLYAIDSSQWVSYSNMGNPNEPDFKERYWGMRNYRRLVSIKKKWDPKDLFIARVGVRSDGWDSEGMCRT", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). Within the pathway, asqF performs FAD-dependent dehydrogenation of the dimethylallyl quinolone peniprequinolone to yield the conjugated aryl diene yaequinolone E (By similarity). The first step of the pathway is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin. 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate- dependent dioxygenase asqJ. AsqJ also converts its first product 4'- methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI. 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B. The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain. The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin. Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (Probable). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
+{"protein": "MKLFTGLIFCSLVLGVHSQWLSFLGEAYEGAKDMLRAYSDMREANFKNSDKYFHARGNYDAAQRGPGGAWAAKVISDARENVQRVTDWLKHGDSGHGVEDSRADQAANEWGRSGKDPNHFRPPGLPDKY", "text": "FUNCTION: Major acute phase reactant. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SAA family."}
+{"protein": "MNGPADGEVDYKKKYRNLKRKLKFLIYEHECFQEELRKAQRKLLKVSRDKSFLLDRLLQYENVDEDSSDSDATASSDNSETEGTPKLSDTPAPKRKRSPPMGGAPSPSSLSLPPSSGFPLQTSGAPSPYLSSLASPPYPPFPSDYLALQLPEPSPLRPKLEKRPRLPRKLKMAVGPPDCPVGGPLAFPARGSGASVGAALTPLPPPKMPPHTILSTVPQQMFSDAGSGDDALDGDDDLVIDIPE", "text": "FUNCTION: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MNFAKILSFVFALVLALSMTSAAPEPRWKIFKKIEKMGRNIRDGIVKAGPAIEVLGSAKAIGK", "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": "MKYVIVSGGVISGVGKGIVSSSIGALLKSRGHVVTHFKIDPYLNYNAGRMHPYEHGEVYVLDDGHECDMDFGNYERFNGIKLSGANSIPGGRLLHDIVKCEREGSFLGKTLQINPHIIDEVIRRIRAVADTPVESFGGGQAAVPDVVVVELGGTVGEYESSIYTEALAKFQYVVGKANCAFVSVDYIVELETGEQKTKGIQMGCRNFRRFGLNYDIVICRGRREPNMETRRKISTSCWVKEENVLGLPNLESVYLAPMFLEKHGIVEALNRILGLDDKGMDRRMLDIFSMVGRRHRDGVRIGIVGKYAPEFDSYTSLVNALKFSGAHIGVNVEIVWINSESYSVCDFERCDGVVIPGGFGARGISGKIEAIRHARENGVPLLGICLGYQLSVIEMCRNILGMSDAFSEEFQPSGKNLVVRFISDENGVVDKRLRVGGYGVELRDGLVKKLYGGVETVRERHRHRFEVAQEKVRGLLQHGVRFVGFSSGGKKINVFEVESHPFFVGVQFHPEFNARPDRPHPLITGLVSASYERSK", "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": "MFSPADNIFIILITGEFILGILGNGYIALVNWIDWIKKKKISTVDYILTNLVIARICLISVMVVNGIVIVLNPDVYTKNKQQIVIFTFWTFANYLNMWITTCLNVFYFLKIASSSHPLFLWLKWKIDMVVHWILLGCFAISLLVSLIAAIVLSCDYRFHAIAKHKRNITEMFHVSKIPYFEPLTLFNLFAIVPFIVSLISFFLLVRSLWRHTKQIKLYATGSRDPSTEVHVRAIKTMTSFIFFFFLYYISSILMTFSYLMTKYKLAVEFGEIAAILYPLGHSLILIVLNNKLRQTFVRMLTCRKIACMI", "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. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor T2R family."}
+{"protein": "MANLPILQFEEKIVETVEKNSVVVIIGETGSGKSTQLSQILHRHGYTKSGVIAITQPRRVAAVSVARRVAQELDVPLGEDVGYAIRFEDRTTSKTRIKYLTDGVLLRESLSNPMLDDYSVIILDEAHERSLNTDILLGLVKRLVRIRASNFKVLITSATLDGEKVSEFFSGCPVLNVPGKLYPVEILYSKERPVSYIESSLKVAIDIHVREPEGDILIFMTGQDDIEKLVSRLEEKVRSLAEGSCMDAIIYPLHGSLPPEMQVRVFSPPPPNCRRFIVSTNIAETSLTVDGVVYVIDSGYVKQRQYNPSSGMFSLDVIQISKVQANQRAGRAGRTRPGKCYRLYPLAVYRDDFLDATIPEIQRTSLAGSVLYLKSLDLPDIDILKFDFLDAPSSESLEDALKQLYFIDAIDENGAITRIGRTMSDLPLEPSLSRTLIEANETGCLSQALTVVAMLSAETTLLPARSKPSEKKRKHDEDSNLPNGSGYGDHIQLLQIFESWDRTNYDPVWCKENGMQVRGMVFVKDVRRQLCQIMQKISKDRLEVGADGRKSSSRDDYRKLRKALCVGNANQIAERMLRHNGYRTLSFQSQLVQVHPSSVLSADNDGMMPNYVVYHELISTTRPFMRNVCAVDMAWVAPIKRKIEKLNVRKLSGGPAPSFKVPEEKTELSKNNAETPAVSENVESRIEAARERFLARKGQK", "text": "FUNCTION: May be involved in pre-mRNA splicing. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. PRP22 sub-subfamily."}
+{"protein": "MVVINGYSFKTQQLLTQQPDHSQLTQFVQPQSQSTHSVHPGPSPGQQQAGGSMTMPSSSTGKGKREWDINDAIVPHVPDQEFDEFNEWSDGHVRHIYSLHNEEAKKHISGWAMRNTNNHNVNILKKSCLGVLVCSQHCTLPNGSKINLRPAICDKARRKQEGKACPNKSCRGGRLEIKPCRGHCGYPVTHFWRHSGNAIFFQAKGVHDHLRPDPKNSSVSKRAFGRVPLAGKSANGSVAKKSVIAGLVKQAKQQHSLISKVLKRPAVSNPLAHTALDIYQYNACGKCAGYSHCTCSYLDDSTTARSHQLSQSSNYGTNSWPLSGSESSAPCETAANVFTVNHQHITYNYPIYHATPAAATAAPSKSPSLPYACSISELAAYQQSSSGNSFAMGVPVHGHTQCQAVAYDSSPQLATPEPEFINYSQIKHLGGGGGQEEISCKAEPGPTIKYNATVETQPYVEDNYDYYYSPKAEYEMQQHHHQQQQSHQQFGGNQTAGHHYYESSSGYNGVSYFDTGTTTAPGNTATGNGLEVGYGGYYDHYTSYEQQMAVAGGFATAGGSTAPTVAAPPGHPPPPPPPPTLTYHHHHHHHLHHPAAATGLAPSVTH", "text": "FUNCTION: Transcription factor with a minor role promoting glial cell differentiation and a more significant role in hematocyte differentiation. Gcm2, together with gcm, is required for the proliferation of plasmatocyte precursors, the expression of Croquemort protein, and the ability of plasmatocytes to convert into macrophages. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MIKMWRLQIVLVPPSAQDIITFLEARLNTPQSVSPMVQYNEDIITHNNSINNCSDPSPTSPSSQNSIQSNRSSDFINYLPNCKKFLHFTDGDNTLLQLSNEILTKFDRLYPNFKESIEIVSLQDRHGCDLDSEFIIKDVFENDGVVLVILKDELDWSRNQHISLLQLARQRRRQDNKPSTKSIVTEKRKKISKEDLSSISNKDTMHLIAKSSLKNNFINKSRVSTPLMNEILPLASKYDALNKEKCPMPLTSTVVASNVHKDVKDHARAKEGVVTQGSDNNKENIPSSTQQQKNDGAKRAESKDLDLLRNSSEDADYEPADENSPQISFDSIDTDFQLSTTSHTNSDMHIQYSNPSSGAHSPRKSSLEIKVQNKKGDDLPLNDKDIGENCRRIEAFSDEEDFNETDNDRADSFINNSKKASMGFRDINSDLDSVSFNSDIENAVQSTQSTKNVVSPPFFPEKELNNRLHQSQGKEALFRLVEKEFPDKSLGAASSTSHAKDVKIQETIRKLNRFKPTGETKVQKRNSITEPYYGKFGIMKKDKPKSITSKGVSLETKHFDDPNTIISGEKFAKFGKIKVKRKTDDVGSKVIEFKRKRNMGNRSLKDIFANAGKPPNAASTIKVVKLMRDPVDNSKDKVEATSNSTAQEQEQVSPKLPVMNSTPGKRKNGQAIPSSLERTPQLKKVKVTRSHSSPSSSSSMSLESSLDSSSSDDSDDDSDSRNVQVKKINFKTSHGPAGNSNGKPMLDVDDNEINTKKYQTPKYVESDEDDQ", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: To yeast YJL076w."}
+{"protein": "MAAARAAVPIAVFLLLVLAEADPAAATRSPSAFVQNAIYSNRITIFSKTYCPYSMRAKRIFRDLKENPYIVELDLREDGREIQSVLLDLVGRHTVPQVFVNGQHVGGSDDTANAHSNGQLQKLLGNSQSQR", "text": "FUNCTION: May only reduce GSH-thiol disulfides, but not protein disulfides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily."}
+{"protein": "GIPCGESCVFIPCISTVIGCSCKNKVCYRN", "text": "FUNCTION: Probably participates in a plant defense mechanism. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily."}
+{"protein": "MAGMALARAWKQMSWFYYQYLLVTALYMLEPWERTVFNSMLVSIVGMALYTGYVFMPQHIMAILHYFEIVQ", "text": "FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1- SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA (PubMed:19416851). Plays a role in MBOAT7 location to mitochondria-associated membranes (MAMs), may me involved in fatty acid remodeling phosphatidylinositol (PI) (PubMed:23510452). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SPTSS family. SPTSSA subfamily."}
+{"protein": "MESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLGAVKGELLIDIGSGPTIYQLLSACESFTEIIVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRMKGPEKEEKLRRAIKQVLKCDVTQSQPLGGVSLPPADCLLSTLCLDAACPDLPAYRTALRNLGSLLKPGGFLVMVDALKSSYYMIGEQKFSSLPLGWETVRDAVEEAGYTIEQFEVISQNYSSTTSNNEGLFSLVGRKPGRSE", "text": "FUNCTION: Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1- methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway (PubMed:26168293, PubMed:29483571). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases (By similarity). Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3. In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (By similarity). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis (PubMed:24717514, PubMed:26168293). In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway (PubMed:24717514). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (PubMed:26168293). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family."}
+{"protein": "MFLKVQLPWNVMIPAENMDAKGLMLKRAILVELLEAFASKKATKELGYYVAVTTLDKIGEGKIREHTGEVLFPVMFSGMTFKIFKGEIIHGVVHKVLKHGVFMRCGPIENVYLSYTKMPDYKYIPGENPIFMNEKTSRIQVETTVRVVVIGIKWMEVEREFQALASLEGDYLGPLSEE", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase V involved in RNA-directed DNA methylation- dependent (RdDM) silencing of endogenous repeated sequences, including transposable elements. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family."}
+{"protein": "MRGLLCWPVLLLLLQPWETQLQLTGPRCHTGPLDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQGTMTGLAIQYAMNVAFSVAEGARPPEERVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLDEHVFLVESFDLIQEFGLQFQSRLCGKDQCAEGGHGCQHQCVNAWAMFHCTCNPGYKLAADNKSCLAIDLCAEGTHGCEHHCVNSPGSYFCHCQVGFVLQQDQRSCRAIDYCSFGNHSCQHECVSTPGGPRCHCREGHDLQPDGRSCQVRDLCNGVDHGCEFQCVSEGLSYRCLCPEGRQLQADGKSCNRCREGHVDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERGTMTGLALRHMVEHSFSEAQGARPRALNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAELHVSYAPDFGTMTHLLENLRGSICPEEGISAGTELRSPCECESLVEFQGRTLGALESLTLNLAQLTARLEDLENQLANQK", "text": "FUNCTION: Major component of the extracellular matrix of cartilage. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MSSDALKALLQWGASFGVIVPEELKFLYTDLKGIICVCEKDIDNPSIKIPPEIVISRNLPMKFFGLSESTKNINGWLKLFFAKIKFDRDNDTIVDNVRVNDKFKPYLDALPSRLNSPLVWNPSELKRLSSTNIGNSIHEKFEGIFKEWFELVSSSDMFDLERVADDVQTFHNLDELTYEALYEKILKITELQRPTIWYSFPAFLWSHLIFISRAFPEYVLNRNCPDNSIVLLPIVDLLNHDYRSKVKWYPENGWFCYEKIGTASQSRELSNNYGGKGNEELLSGYGFVLEDNIFDSVALKVKLPLDVVSTILETEPSLKLPLLSDYTTYAFENKDCVQQEKKATRSATDYINGVTYFINIQNEQCLEPLLDLFTYLSKAEEEDLHDLRARLQGIQMLRNALQSKLNSITGPPATDDSYAIDPYRVYCADVYTKGQKQILKEALTRLKKLEKTMLSENKHQLLTMSKILKNDPAFAETELPSLFSNEDGEEVIFESTYDLLILWILLKTKKNSYPTKYEWVGQQYTNFKQTAYISDDAKAFHTAYFEKQDDVDLAEVDHAIQFVVDNSFTRTSSTTEETILVRK", "text": "FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that monomethylates ribosomal protein S18 (RPS18A and RPS18B) at 'Lys-48' and dimethylates ribosomal protein L23 (RPL23A and RPL23B) at 'Lys-106' and 'Lys-110'. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM1 family."}
+{"protein": "MAATSGTDEPVSGELVSVAHALSLPAESYGNDPDIEMAWAMRAMQHAEVYYKLISSVDPQFLKLTKVDDQIYSEFRKNFETLRIDVLDPEELKSESAKEKWRPFCLKFNGIVEDFNYGTLLRLDCSQGYTEENTIFAPRIQFFAIEIARNREGYNKAVYISVQDKEGEKGVNNGGEKRADSGEEENTKNGGEKGADSGEEKEEGINREDKTDKGGEKGKEADKEINKSGEKAM", "text": "SIMILARITY: Belongs to the PBDC1 family."}
+{"protein": "MAAVRTPLSLWRFQLGSRRARRVCTRATAQRHPDALLATRPQPFEVGQPRRLLSSEAESGSSEVKKPAFMDEEVQRILTKITGLDLQKTFRPAIQPLKPPTYKLMTQAQLEEATRLAVEAAKVRLKMPPVLEERKPINDVLAEDKILEGTETNKYVFTDISYNIPHRERFIVVREPSGTLRKASWEERDRVIQIYFPKEGRRVLPPVIFKDENLKTMYSQDRHADVLNLCVAQFEPDSAEYIKVHHQTYEDIDRHGKYELLRSTRHFGGMAWYFVNKKKIDGLLIDQIQRDLVDDATSLVQLYHMLHPDGQSAQEAKEQAAEGVDLIKVFAKTEAQRGAYIELALQTYQEIVTSHSAAS", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mS22 family."}
+{"protein": "MANSEQAYWLAWSQVKGVGPVLLKRLAQHFELLENAWKARPIALGEVEGFGHKMIEKIIGQRNNLNPFQFLEEHQQKNPQFLTPDDPDYPRLLWEIPSPPPVLYYLGRLDHRESQGQIPGVGIVGTRYPTDHGSRWTRKISQALVKSGFTIVSGLAAGIDADAHSSCLRVNGRTIAVLGTGLDLIYPPQNRQLFEQIAAEGLILSEYPVGSKPERGNFPARNRIIAGLSRAVLVMEAPPKSGALITAKYANEFNRDVFSLPNSPDVQEAHGCLNLIHNGAEVILSENQLLASLGAIPLLDQGQEQKILPGDRQIGYLDQTNVPTLTTGARGKQPLTEPPEDLEPTLKKILAAVQEEPTALDQIVAVTALAIGDVSAGLLQLEILGLVSQEPGMRYQRR", "text": "FUNCTION: May help load RecA onto ssDNA (By similarity). SIMILARITY: Belongs to the DprA/Smf family."}
+{"protein": "MTHAAIDQALADAYRRFTDANPASQRQFEAQARYMPGANSRSVLFYAPFPLTIARGEGAALWDADGHRYADFIAEYTAGVYGHSAPEIRDAVIEAMQGGINLTGHNLLEGRLARLICERFPQIEQLRFTNSGTEANLMALTAALHFTGRRKIVVFSGGYHGGVLGFGARPSPTTVPFDFLVLPYNDAQTARAQIERHGPEIAVVLVEPMQGASGCIPGQPDFLQALRESATQVGALLVFDEVMTSRLAPHGLANKLGIRSDLTTLGKYIGGGMSFGAFGGRADVMALFDPRTGPLAHSGTFNNNVMTMAAGYAGLTKLFTPEAAGALAERGEALRARLNALCANEGVAMQFTGIGSLMNAHFVQGDVRSSEDLAAVDGRLRQLLFFHLLNEDIYSSPRGFVVLSLPLTDADIDRYVAAIGSFIGGHGALLPRAN", "text": "FUNCTION: Aminotransferase that acts exclusively on beta-amino acids and exhibits a broad substrate range in vitro, accepting meta-, para- and, to a lesser extent, ortho-substituted beta-phenylalanine derivatives as amino donors, and 2-oxoglutarate or pyruvate as amino acceptors. Is highly enantioselective toward (S)-beta-phenylalanine (is not active with (R)-beta-phenylalanine) and derivatives with different substituents on the phenyl ring, allowing the kinetic resolution of various racemic beta-amino acids to yield (R)-beta-amino acids with >95% enantiomeric excess (ee). Highly prefers aromatic beta-amino acids over aliphatic beta-amino acids; cannot use beta-alanine or beta- glutamate as substrate. Is likely involved in the beta-phenylalanine degradation pathway that allows V.paradoxus strain CBF3 to use beta- phenylalanine as a sole nitrogen source. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MVLFLLLVALLSPAGEAGKIIGGHEAKPHSRPYMAFLQIKISGKSYRCGGFLVHEDFVLTAAHCLGSSISVTLGAHNIVDRERTQQVIQVRRAIPHPHYNDKTLANDIMLLQLTRKAEMSDAVSPINLPRSLEKVKPGMMCSVAGWGQLGVNMPSADKLQEVNLEVQSEEECIARFKNYIPITQICAGDSTKRKNSFSGDSGGPLVCNGVAQGIVSYGKDDGTTPDVYTRISSFLSWIQRTMRRY", "text": "FUNCTION: Has a chymotrypsin-like and trypsin-like activity. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory granules. SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily."}
+{"protein": "MPTLEPSVLDQLFHEARTHNVWLDNPVDDELLHTLYDTVKYGPTAANSTPARFVFVKSAAAKEQLVPCMSAGNQEKTRQAPVTVIVAYDTQFHEQLPKLFPHVDARSWYAGDQARINAAALMNSSLQGGYLVIAARALGLDCGPMGGFDADKVNATFFPDGQWKVNFICNLGYGDTSKVHPRNPRLTFEEACRVL", "text": "SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily."}
+{"protein": "MASRFMTDPHAMRDMAGRFEVHAQTVEDEARRMWASAQNISGAGWSGMAEATSLDTMAQMNQAFRNIVNMLHGVRDGLVRDANNYEQQEQASQQILSS", "text": "SUBCELLULAR LOCATION: Secreted Note=Probably secreted via the ESX-5 / type VII secretion system (T7SS). SIMILARITY: Belongs to the WXG100 family. CFP-10 subfamily."}
+{"protein": "MTESTTDPARQNLDPTSPAPATSFPQDRGCPYHPPAGYAPLREGRPLSRVTLFDGRPVWAVTGHALARRLLADPRLSTDRSHPDFPVPAERFAGAQRRRVALLGVDDPEHNTQRRMLIPTFSVKRIGALRPRIQETVDRLLDAMERQGPPAELVSAFALPVPSMVICALLGVPYADHAFFEERSQRLLRGPGADDVNRARDELEEYLGALIDRKRAEPGDGLLDELIHRDHPDGPVDREQLVAFAVILLIAGHETTANMISLGTFTLLSHPEQLAALRAGGTSTAVVVEELLRFLSIAEGLQRLATEDMEVDGATIRKGEGVVFSTSLINRDADVFPRAETLDWDRPARHHLAFGFGVHQCLGQNLARAELDIAMRTLFERLPGLRLAVPAHEIRHKPGDTIQGLLDLPVAW", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MINLKKYIPEGSRDILFEECTIKNNIENILRNSYINVGYEEVRSPTLEFYDVYNLENQPISQEKMYKLFDNTGRILVLRPDMTTPIARICATKLKNRVYPLKLSYTGNIYRMNKALNGKISEITQSGIEILGFSSLKADAEVIITAIKAILKTGLKNFKIEIGQVEFFKSIISDTALKEQDTEKLRNFIENKNFSKVEEFILRNSDLIGETSSKVLMNLPNLFGGKEVIEKAEQLTSNKQAIEALKKVRDLYDIVKRAGFGEYILIDLGMVQHINYYTGLIFRGYAHGIGDDLLSGGRYDKLLGQFGYDIPATGLAINVDNLVAALDDCVRENLYSRDRYVVFASSCNIEKAYEAVSKLNSEGKRAEVSLFDNIEETKKYCIENKISKIFNADTGKTIVEENYYGQK", "text": "FUNCTION: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily."}
+{"protein": "MKTETGSNNNNTTVVNMDFDMYPSISGKQQDPVREVVMKYIDYFLPDASGTSAVAIDNKIEQAMDLVKSHLMIAVREEVEVLKERISELMDKINKLELENSILKSNIPQETLQQLQLQLQLAAPPATPAIQAAPAVQSVVAPAAAGQAVQQQAAGAVAVTGVATSPASAVVPTSIPNGSAENGSSAVESAAVSVEQQVQQVTSAAAAAASVVTANGPMS", "text": "FUNCTION: Probable transcription factor required for peripheral nervous system morphogenesis, eye development and oogenesis. May be required for the transmission of the dpp signal and for a morphogenetic movement of the medulla in the brain that reorients the second optic lobe relative to the first. Plays a role in determining proper dorsal cell fates leading to the formation of the dorsal appendages. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TSC-22/Dip/Bun family."}
+{"protein": "MAFSPNPLSLSVPDPAFESWLRDSGYLELLDHRTSAAAAAASSSASVSSSAAATSAASDDVVSSITGGFFASLLSRLVTVSSLLTINPFSKLSADDFSGDTTPWTTGFIGNCDSYSFPSSSQQARMRVHENIKRFARNYATLFIVFFACALYQMPLALVGLLGSLALWELFKYCSDKWKFDRHPSMRKLSIGIGQCATAVLLTFLNVQMALFSALAISYSVMILHAGFRKLTPSKKPTRGR", "text": "FUNCTION: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PRA1 family."}
+{"protein": "MGGDKENLDLSDLNASLPAAAAALSAEDRAGLVNALKDKLQSLAGQHTDVLEALSPNVRKRVEYLREIQGQHDEIELKFFEERAALEAKYQKLYEPLYTKRYNIVNGVVEVDGGNDEPASENAAEGKDADAKGVPDFWLTAMKTNEVLSEEIQERDEPALKYLKDIKWARIDDPKGFKLDFFFDTNPFFKNSVLTKTYHMVDEDEPILEKAIGTEIEWYPGKNLTQKILKKKPKKGSKNAKPITKTEVCESFFNFFSPPQVPDDDEDIDEDTADELQGQMEHDYDIGTTIRDKIIPHAVSWFTGEAVQAEDFDDMEDDEEDDEDDDEDEEEEEEDEDEDEDDEEEKSKPKKKSAGKPKLPSKGGAQGGADQPADCKQQ", "text": "FUNCTION: May modulate chromatin structure by regulation of nucleosome assembly/disassembly. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
+{"protein": "METSMPEYYEVFGDFHGFLMDKLFTKYWEDVETFSARPDDLLVVTYPKSGSTWIGEIVDMIYKEGDVEKCKEDAIFNRIPYLECRNEDLINGIKQLKEKESPRIVKTHLPAKLLPASFWEKNCKIIYLCRNAKDVVVSYYYFFLIMKSYPNPKSFSEFVEKFMEGQVPYGSWYDHVKSWWEKSKNSRVLFMFYEDMKEDIRREVVKLIEFLERDPSAELVDRIIQHTSFQEMKNNPCTNYSMLPETMIDLKVSPFMRKGIVGDWKNHFPEALRERFEEHYQQQMKDCPVKFRAEL", "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": "MEEDFSSQMKKMALAMGTSLSDKDIELLPTDMRHHGSFNYLKFFKHIRKLHASGQLDDAIHTAFQSLDKDKSGFIEWNEIKYILSIIPSSGPTTPLTDEEAEAMIQAADTHGDGRINYEEFSELIKKEKIPKKK", "text": "SIMILARITY: Belongs to the parvalbumin family."}
+{"protein": "MDIDRNRLRTGLPQVGVQPYRQVHAHSTGNRNSTVQNEADYHWRKDPELGFFSHVVGNFRIMQVGPVNNGSWDVGGGWNAETYAAVELIESHSTKEEFMADYRLYIELLRNLADEAGLPKTLDTDDLAGIKTHEYCTNNQPNNHSDHVDPYPYLASWGISREQFKQDIENGLSAATGWQKNGTGYWYVHSDGSYSKDKFEKINGTWYYFDGSGYMLSDRWKKHTDGNWYYFDQSGEMATGWKKIADKWYYFDVEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADKPEFTVEPDGLITVK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family."}
+{"protein": "MPRAPAPLYACLLGLCALLPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEDFGSPRSITSRCDLRANLVKNGCGGEIESPASSFHVLRSLPLSSKGSGSAGWDVIQMTPQEIAVNLRPGDKTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLDNIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLALLGEKLAENNINLIFAVTKNHYMLYKNFTALIPGTTVEILDGDSKNIIQLIINAYNSIRSKVELSVWDQPEDLNLFFTATCQDGVSYPGQRKCEGLKIGDTASFEVSLEARSCPSRHTEHVFALRPVGFRDSLEVGVTYNCTCGCSVGLEPNSARCNGSGTYVCGLCECSPGYLGTRCECQDGENQSVYQNLCREAEGKPLCSGRGDCSCNQCSCFESEFGKIYGPFCECDNFSCARNKGVLCSGHGECHCGECKCHAGYIGDNCNCSTDISTCRGRDGQICSERGHCLCGQCQCTEPGAFGEMCEKCPTCPDACSTKRDCVECLLLHSGKPDNQTCHSLCRDEVITWVDTIVKDDQEAVLCFYKTAKDCVMMFTYVELPSGKSNLTVLREPECGNTPNAMTILLAVVGSILLVGLALLAIWKLLVTIHDRREFAKFQSERSRARYEMASNPLYRKPISTHTVDFTFNKFNKSYNGTVD", "text": "FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor for adenovirus type C. FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the integrin beta chain family."}
+{"protein": "MTVPTDTVSRRLQSLAWSDIKQHAPWLPSSRTLVSGFLCLILLQILYSRGRKSDLRVYNPKKWWELTTMRAKREFDANAPAWIEAWFSKNDQPLRFIVDSGYCTILPSSMADEFRKMKELCMYKFLGTDFHSHLPGFDGFKEVTRDAHLITKVVMNQFQTQAAKYTKPLADEASATIADIFGDNKEWHTAPVYNECLDLVTRTVTFIMVGDKLAHNEEWLDIAKHHAVTMAIQARQLRLWPVILRPIVHWLEPQGAKLRAQVRRARQLLEPIIQERRAEKAKCLAQGIEPPRYVDSIQWFEDTAKGQWYDAAGAQLAMDFAGIYGTSDLMIGGLVDIVRHPHLIEPLRNEIRTVIGEEGWTPASLYKLKLLDSCLKESQRVKPVECATMRSYALQNVTFSNGTFVPKGELVAVAADRMSNPEVWPEPKKYDPYRYMRLREDPDKAFSAQLENTNGNHIGFGWHPRACPGRFFASKEIKIMLAFLLIRYDWKLVPNEPLQYYRHSFSVRIHPATKLMMRRRDEDL", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase (PubMed:18578535). Monakolin K biosynthesis is performed in two stages (PubMed:19693441). The first stage is catalyzed by the nonaketide synthase mokA, which belongs to type I polyketide synthases and catalyzes the iterative nine-step formation of the polyketide (PubMed:18578535, PubMed:19693441). This PKS stage is completed by the action of dehydrogenase mokE, which catalyzes the NADPH-dependent reduction of the unsaturated tetra-, penta- and heptaketide intermediates that arise during the mokA-mediated biosynthesis of the nonaketide chain and leads to dihydromonacolin L (PubMed:19693441). Covalently bound dihydromonacolin L is released from mokA by the mokD esterase (By similarity). Conversion of dihydromonacolin L into monacolin L and then monacolin J is subsequently performed with the participation of molecular oxygen and P450 monoogygenase mokC (PubMed:19693441). Finally, mokF performs the conversion of monacoline J to monacoline K through the addition of the side-chain diketide moiety (2R)-2-methylbutanoate produced by the diketide synthase mokB (PubMed:19693441). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MARPQRTPARSPDSIVEVKSKFDAEFRRFALPRTSVRGFQEFSRLLCVVHQIPGLDVLLGYTDAHGDLLPLTNDDSLHRALASGPPPLRLLVQKRAEGDSSGLAFASNSLQRRKKGLLLRPVAPLRTRPPLLISLPQDFRQVSSVIDVDLLPETHRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSDEILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQRNNVVRGASGRLTGPSSVGPGPTDPDSDDDNSDPVIENRHPPCSNGLSQGPLCWDLQPGCLHPSAGSSLPSLDSREQANSGWGNGMRGDVSGFSL", "text": "FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in the formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Regulates centrosome organization and function. Essential for the centrosomal recruitment of key proteins that control centrosomal microtubule organization. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Cell junction, tight junction Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Colocalizes with GTP-bound CDC42 or RAC1 at membrane ruffles and with PARD3 at epithelial tight junctions. Recruited to the centrosome by a microtubule and dynein- dynactin-dependent mechanism. SIMILARITY: Belongs to the PAR6 family."}
+{"protein": "MSRLQTEEQAVDSEGDSSLHRRNEEGTQSSHRMLGFSDALLSIIATVMILPVTHTEISPEQQFDKSIQKLLATRIAVYLMTFLIVTVAWTAHTRLFQVVGKIDDTLALLNLACMMTITLLPYTFSLMVTFPDVPLGIFLFCVCVIAIGSVQAMIVGYAFHFPHLLNPQIQCSTHRDLSRRHILHLVLRGPALCFVAAVFSLFFFPLSYLLMVTVIFLPHISKATTWCKDKLMGQRESPAHDMEPFSIDLHAPLSKERVEAFSDGVYAIVATLLILDICEDNVPDPKDVQEKFSGSLVAALGAYGPQFLAYFGSFATVGLLWFAHHSLFLHVRKATQTMGLLNILSLAFVGGLPLAYQQTSAFARQPHDELERVRVSCAIIFFASIFQFAIWTTALLHQTETLQPAVQFGGQEHAFMFAKLALYPCASLLAFAATCLLSRFSTAIFHLMQISVPFAFLLLRLLVRLALAGLQVLRGLWPHHPQQDQSEPEAQSQLLPDPC", "text": "FUNCTION: Proton-activated proton channel that catalyzes proton efflux from endosomes and lysosomes to maintain a steady-state pH (PubMed:35750034). Activated at low pH (under pH 4.6) by luminal side protons: selectively mediates lysosomal proton release from lysosomes, eliciting a proton leak that balances V-ATPase activity to maintain pH homeostasis (By similarity). Regulation of lumenal pH stability is required for autophagosome-lysosome fusion (PubMed:26317472). May also act as a potassium channel at higher pH, regulating potassium conductance in endosomes and lysosomes (PubMed:26317472, PubMed:33505021). The potassium channel activity is however unclear as it was tested in non-physiological conditions for a lysosomal channel (By similarity). Constitutes the pore-forming subunit of the lysoK(GF) complex, a complex activated by extracellular growth factors (PubMed:33505021). The lysoK(GF) complex is composed of TMEM175 and AKT (AKT1, AKT2 or AKT3), a major target of growth factor receptors: in the complex, TMEM175 channel is opened by conformational changes by AKT, leading to its activation (PubMed:33505021). The lysoK(GF) complex is required to protect neurons against stress-induced damage (PubMed:33505021). SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM175 family."}
+{"protein": "MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHYHLGQKDRETATIA", "text": "FUNCTION: Plays an important role in galactose metabolism. SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase type 1 family."}
+{"protein": "MSSTLGKDKDSKEREPKAEGKSKTKGKDAKDGKKDTSGASPAVAFTLDSTIKRPNPPPSTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHLLPSSIKELTQLTELYLYSNKLQSLPPEVGCLSGLVTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPAVVYRVSSLTTLYLRFNRITTVEKDIKNLSKLTMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNDLLDLPETIGNLASINRLGLRYNRLSAIPRSLAKCRELEELNLENNNISVLPEGLLSSLVNLTSLTLARNCFQSYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDICGLVSLEMLTLSNNLLKKLPYGIGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTYLGLGENLLQHLPEEIGTLENLEDLYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV", "text": "FUNCTION: Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of raf1 kinase and stimulate raf1 activity at specialized signaling complexes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SHOC2 family."}
+{"protein": "MSSDLRLTLLELVRRLNGNATIESGRLPGGRRRSPDTTTGTTGVTKTTEGPKECIDPTSRPAPEGPQEEPLHDLRPRPANRKGAAVE", "text": "FUNCTION: Plays an essential role in the inhibition of host apoptosis. Mediates host mitochondria-mediated apoptosis through interaction with the mitochondrial antiviral signaling protein/MAVS and thereby promotes viral persistence in host central nervous system. Within the host nucleus, regulates viral RNA synthesis and polymerase complex assembly. FUNCTION: Plays an essential role in the inhibition of host apoptosis. Mediates host mitochondria-mediated apoptosis through interaction with the mitochondrial antiviral signaling protein/MAVS and thereby promotes viral persistence in host central nervous system. Within the host nucleus, regulates viral RNA synthesis and polymerase complex assembly. SUBCELLULAR LOCATION: Host nucleus. Host mitochondrion. SUBCELLULAR LOCATION: Host nucleus. Host mitochondrion."}
+{"protein": "MQCNDVQATEPDIKVSLTRVGVTNLKKLVKLKRTNKRDIVLLPTFEVFVDLPSSQKGIHMSRSPEVIEEVVENILLEKEIYGVEDLSVEIVMKLFEKHEYATRAEIMLYSDYMMEEKSPVTQKDSQEIGKIIARAYGVKDENGKIHVKKMVGAEVVGITACPCAQNMLKENAVTSLKEKGFSNEEIEKILDSVTIATHNQRGIGTVMIEVPNGYTVGISKIIKIIKDSMSGEVYELLKRSDEAFVVETAHKNPKFVEDCAREMIKRVVDVFDYLPEDTQVLVRQVNKESIHRHDAFAERNSTLRELRDELKTLTN", "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": "MRVLSARFRVLLACLALVIPVSETNFLSKERASQVLVRKRRANTLFEETMKGNLERECIEELCNKEEAREVFENNPETDYFYPKYLGCLGAFRVGSFHAARQSANAYPDLRSCVKAISDQCDPIPCNEDGYLACQDGQAAFTCFCKPGWQGDRCQYDVNECKDPSNVNGGCSQICDNTPGSYHCSCKRGFAMLPNKKDCKDLDECALKPSVCGTAVCKNIPGDFECECPDGYRYDPSSKSCKDVDECSENMCAQLCVNFPGGYSCYCDGKKGFKLAQDQKSCEGIPVCLSLDLDKNYELLYLAEQFAGVVLYLKFRLPDITRFSAEFDFRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNINKLGSLFKPTDGFLDTKIYFAGLPRKVESALIKPINPRLDGCIRGWNLMKQGALGAKEIIEGKQNKHCFLNVEKGSYYPGSGIAQFSIDYNNVTNAEGWQMNVTLNIRPSTGTGVMLALVSGGTVPFALSLVDSRSGTSQDIVVFVENSVVARLEAVSLCSDQQSQLKCNVNRNGLELWTPLRKDVIYSKDLQRQLAVLDKAMKRTVATYLGGIPDISFSATPVNAFYSGCMEVNINGVQLDLDEAISKHKDIRAHSCPSVRKIQKNF", "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": "MMLASSAPTAPSLLPPSSQPSAATTRADDCSSSTSPTNTSASDASMEMLTSLMNGAVAAAAAPGNALVKQESPPLTTPPLFNPDLALLQFSQLFQAQQAMVQFHNQQKQQQQIIQQQQQQQQQQQQNQNPSQSQSSSSDRKRSYPCTFQYCVICQKDVHSSKLPCHIRQCHVAKPMFQCPACDFTSTYSKNNVKSHMVSLHGLAGDPISYMDKYAGQVEEFMKLCFPNVRGRGRPMQGRSSPKSPTSPTQPGRRGSQASSLPSRRNTVSQNDLLATLQQHQQQQAAFHPLRNLRFNPLQSIFPAVLANNNNNSVLATNKHVNNFLIKQEESEVPPITMPMQDLKTMLDANSSPSPISLSSSIIPIQPIKPGENAQPKYMKSLDWTILNDLQMKGTVFADCRSNMELYAENIARKIENTKAFQSFVLSDDMRTVVEEVRSRVSIQLFEVMFAIHRMDIKVLNQNLVDSLLQIAPTNSDAQLLRKMENLSDPNEEFLLGLTKIDHIEEKLETMKHMYRFPEQVELLKENIIKYEIAVKVLSESRALRNVMQLVLAILNIGFFDDRQCLSINGFSVSDISSILSTNTPSGQSVQSILVTILKDEINLDLDELFGLIDVLEKIENDDVNSVAQDLMVLDDKTVRAEKEMEHSGSNIPLSEFVENAKTISKERWEHFKSLKTSIERLTIYLGSPLPRHQNLDAHSPFNNVLQMLRSLKTAIELDDASDDHHINVSSP", "text": "FUNCTION: Acts redundantly with hlh-1 to promote body wall muscle cell and coelomocyte specification in postembryonic mesoderm progenitors, probably through suppression of sem-2. SIMILARITY: Belongs to the formin homology family."}
+{"protein": "MTVSTDNTSPVISRASSPTFGDHGKDFDNNKIIPISIEAPTSSAAAVGAKTAIEPEGRSPLLQRICYLVKIIAAIALFVVGIAALVCLYLGSVISTPSLILMLAIMLVSFVIVITAIRDGTPSQVVRHMKQQIQQFGEENTRLHTAVENLKAVNVELSEQINQLKQLHTRLSDFGDRLEANTGDFTALIADFQLSLEEFKSVGTKVETMLSPFEKLAQSLKETFSQEAVQAMMSSVTELRTNLNALKELITENKTVIEQLKADAQLREEQVRFLEKRKQELEEACSTLSHSIATLQESTTLLKDSTTNLHAVESRLIGVMVQDGAESSTVEEASQDDSAQPQDENQSDAGEHKDS", "text": "FUNCTION: Chlamydia replicate within a host intracellular vacuole, termed an inclusion, which is formed by fusion of many smaller inclusion bodies. IncA is probably involved in the homotypic fusion of inclusions. SUBCELLULAR LOCATION: Secreted Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane; Multi-pass membrane protein Note=Secreted, probably by a type III secretion system (By similarity). Localized in the inclusion membrane (Probable). In the inclusion, the C-terminus faces the host cytosol (Probable). SIMILARITY: Belongs to the IncA family."}
+{"protein": "MSSPRAVVQLGKAQPAGEELATANQTAQQPSSPAMRRLTVDDFEIGRPLGKGKFGNVYLARLKESHFIVALKVLFKSQIEKEGLEHQLRREIEIQAHLQHPNILRLYNYFHDARRVYLILEYAPRGELYKELQKSEKLDEQRTATIIEELADALTYCHDKKVIHRDIKPENLLLGFRGEVKIADFGWSVHTPSLRRKTMCGTLDYLPPEMIEGRTYDEKVDLWCIGVLCYELLVGYPPFESASHSETYRRILKVDVRFPLSMPLGARDLISRLLRYQPLERLPLAQILKHPWVQAHSRRVLPPCAQMAS", "text": "FUNCTION: Serine/threonine-protein kinase 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. Also plays a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'. SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere Cytoplasm, cytoskeleton, spindle Note=Distributes in the condensed chromosomes during prophase to metaphase. After entering anaphase, there is a dissociation from separated chromosomes and a redistribution to midzone microtubules, and finally remains in the midbody during cytokinesis. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily."}
+{"protein": "MALVVKGKVNINEFIDLTKMEKILPSMFTPVKSVMCSKVDKIMVHENESLSEVNLLKGVKLIDSGYVCLAGLVVTGEWNLPDNCRGGVSVCLVDKRMERADEATLGSYYTAAAKKRFQFKVVPNYAITTQDAMKNVWQVLVNIRNVKMSAGFCPLSLEFVSVCIVYRNNIKIGLREKITNVRDGGPMELTEEVVDEFMEDVPMSIRLAKFRSRTGKKSVVPKGNFSSRDRSQPNKNYGNAKDFGGMSFKKNNLIDDGSETSVAESDSF", "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. Forms a ribonucleoprotein complex with viral RNA. Binds microtubules and modulates microtubule stability. Can bind double- stranded DNA. Triggers host hypersensitive defense reaction in incompatible plants harboring resistance (R) proteins. SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton Host cell junction, host plasmodesma Note=Binds to the host cytoskeleton before being transported to the host plasmodesmata. Observed in virus replication complexes (VRCs) of tobamovirus infected host cells (By similarity). In resistant plants, targeted to the host plasma membrane via the interaction with host resistance (R) protein TM-2 (e.g. tomato ToMV resistance protein TM-2(2), AC Q71BG9) (By similarity). SIMILARITY: Belongs to the tobamovirus movement protein family."}
+{"protein": "MDHYLDIRLRPDPEFPPAQLMSVLFGKLHQALVAQGGDRIGVSFPDLDESRSRLGERLRIHASADDLRALLARPWLEGLRDHLQFGEPAVVPHPTPYRQVSRVQAKSNPERLRRRLMRRHDLSEEEARKRIPDTVARALDLPFVTLRSQSTGQHFRLFIRHGPLQVTAEEGGFTCYGLSKGGFVPWF", "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. Absolutely required for crRNA production or stability. Upon expression in E.coli endonucleolytically processes pre-crRNA, although disruption and reconstitution experiments indicate that in situ other genes are also required for processing. Yields 5'-hydroxy and 3'-phosphate groups. The Csy ribonucleoprotein complex binds target ssDNA with high affinity but target dsDNA with much lower affinity. SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas6 family. Cas6f/Csy4, subtype I-F/Ypest subfamily."}
+{"protein": "MSNENLSPNSSNPDLTKLNNGESGTIDTSKFSPNEMKLYKMYGKLPSKKDIFKHTMQKRKYFDSGDYALQKAGIQNNDPINYGKNNLPLTNPSKLREDIIKRRISTCPSTASTAGVVDNATLIQKEGSISSGPPSSNNGTIGGGSTSSTPVGNHSSSSSSLYTESPIR", "text": "FUNCTION: Required for TORC1 to properly control gene expression and chronological life span. Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway. SIMILARITY: Belongs to the endosulfine family."}
+{"protein": "MAFLKKSLFLVLFLGIVSLSICEEEKREGEEEEKQEEENEELSEEELRERRAWLDKLKSIGKVVGKVAIGVAKNLLNPQ", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
+{"protein": "MLKLASSLRTGLISRSIRTLAPTVNPAEQQQVQAVLPDKLYSSVEIEYRGHDKAVLKSYTSFLQQVCQHLEIPQGRLEVLPYIRWVQPALRSKFVHKKYKLHYETRTHISKLEILNVTGSTASTFLEYIQRNIPEGVGMRVGFTELQPLPLTIQKN", "text": "FUNCTION: Ribosomal protein required for normal mitochondrial function and normal larval development. Thought to have a role in insulin/IGF signaling. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS10 family."}
+{"protein": "MRFLSSLIILLIITIYSSVNGDIYMHSPPGSNNRNQEQGQNRDNNQRLFNSQNNDKGGYCRGEALEWYEKSYLPVEWTNQHGCGSGETECNIVIQYMCTDNAKAADTEYIRDGTVTTTISANDITQSSTKETNEYKFGMHESYHHYQNCTGRERNKGLFIANQNIGNNADRTRQSNNGNNYGYECQEERDYYPYWAPSPWKDVAIITDNRDLCKWYRSESQNVQPKYYCKAATTNNNQPRSIDPVICANQGGVWTKVDSHDIGAPECIKAEWTQVNTLGHVLEDGHNPMYNWSLPHSGMEPCIATGTCSCVLRVRYNISSSDLKGNGDEFTDYKSNGPKGATNVNDPNVVVAGQNVTLNINPNQYGRTFQDRSHVFSIIARPDSLKKAKIWNLLVKGKRGNIVQSHPAQEYQFVPKTLHIKVNEYIHYQWTGCDFNPQNYDGTGIKGSDRSNMCQIKTLNHNYPMTDDELNDDNALFADMETRLRFARLGQKSCLTYDELMTKNNNNKDAVEVDPQNCMVLNNAGTRFNGGVQKMSKTGSYYYMSTRNNNFSNRNQKGAIHVDPLLAGWQIGLIASGCSLFVIISATAGCVTFARFHPHSGMHRAVSKVPGLKRLV", "text": "FUNCTION: May participate in O-glycosylation. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
+{"protein": "MSIKGDSPSSTNASSSPKSTYSIQSDDKANLGSGNVDIRTDNSQQDSNNRRDIVVVTRVASEETLESQSSTSSMGIRPESSFNYEDASNQARVEMNNRVHGSNMNTINKYYPVRFPKNNERQLSDTNNLNEKVQGTHTVQSSTQEDKILDGDTSNSQVTPSLNIAEFPTDKLLKMLTALLTKIIKSNDRTAATNPSLTQEIENGRCLALSDNEKKYLSPVLGFRGKHVPQIGLDQYFQRIQKYCPTTNDVFLSLLVYFDRISKRCNSVTTTPKTNTAKHESPSNESSLDKANRGADKMSACNSNENNENDDSDDENTGVQRDSRAHPQMFVMDSHNIHRLIIAGITVSTKFLSDFFYSNSRYSRVGGISLQELNHLELQFLVLCDFELLISVNELQRYADLLYRFWNNAKAQSQALVTGM", "text": "FUNCTION: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL7, controls glycogen phosphorylase and glycogen synthase activities in response to nutrient availablility. The PCL6- PHO85 cyclin-CDK holoenzyme has GLC8 kinase activity and phosphorylates and inactivates the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates and activates glycogen phosphorylase. PCL6-PHO85 also phosphorylates YJL084C. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cyclin family. PHO80 subfamily."}
+{"protein": "MNIIEIKQLNRYFGEGENRVHVLKDISLSIERGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSSKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQSQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKRQVKSAVKNPSVFKGRFGFSKDQLMEAFRMSVSAIVAHKMRSLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGTNTMTIFNGNGFGDRRSRHIQNLKISDANTLSKQSYIQSVTPNTSSSGILVVGNKSFTSANLYGIGEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIFANENPLGKTVIFNKRPFRVIGVVSDQQLGGFPGNSLNLYSPYSTVLNKITGGSRIGSITVKISDDVNSTVAEKSLTELLKSLHGKKDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFNSFITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALAQE", "text": "FUNCTION: Part of the tripartite efflux system MacAB-TdeA. 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": "MAPAAASGGSTLPSGFSVFVTFPDLLFIFEFIFGGLVWILIASSLVPMPLVQGWVMFVSVFCFLATTSLMVMYIIGTHGGETSWITLDAAYHCVAALFYLSASVLEALATITMFDGFTYRHYHENIAAVVFAYVATLLYVIHAVFSLIRWKSS", "text": "FUNCTION: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Could be involved in myelin biogenesis and/or myelin function. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MAL family."}
+{"protein": "MAMSSGGSGGGVPEQEDSVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETSGKPKTTPKRKPAKKNKSQKKNTAAPLKQWKVGDKCSAIWSEDGCIYPATIASVDFKRETCVVVYTGYGNREEQNLSDLLSPISEVANNIEQNAQENENESQVSTDESENSRSPGSKSDNIKSKSAPWNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPPPPPPHLLSCWMPPFPSGPPIIPPPPPICPDSLDDADALGSMLISWYMSGYHTGYYMGFRQNQKEGRCSHSLN", "text": "FUNCTION: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre- mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R- loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). SUBCELLULAR LOCATION: Nucleus, gem Nucleus, Cajal body Cytoplasm Cytoplasmic granule Perikaryon Cell projection, neuron projection Cell projection, axon Cytoplasm, myofibril, sarcomere, Z line Note=Colocalizes with actin and at the Z-line of skeletal muscle (By similarity). Under stress conditions colocalizes with RPP20/POP7 in punctuated cytoplasmic granules. Colocalized and redistributed with ZPR1 from the cytoplasm to nuclear gems (Gemini of coiled bodies) and Cajal bodies. Colocalizes with FMR1 in cytoplasmic granules in the soma and neurite cell processes (By similarity). SIMILARITY: Belongs to the SMN family."}
+{"protein": "MEVVSKIDQENQAKIWKQIFGFAESLVLKCAVQLEIAETLHNNVKPMSLSELASKLPAQPVNEDRLYRILHFLVHMKLFNKDATTQKYSLAPPAKYLLKGWEKSMVPSILSVTDKDFTAPWNHLGDGLTGNCNAFEKALGKGIRVYMRENPEKDQLFNEGMACDTRLFASALVNECKSIFSDGINTLAGVGRGTGTAVKAISKAFPDIKCTIHDLPEVTSKNSKIPRDVFKSVPSADAIFMKSILHEWNDEECIQILKRCKEAIPKGGKVIIADVVIDMDSTHPYSKSRLAMDLAMMLHTGGKERTEEDWKKLIDAAGFASCKITKLSALQSVIEAYPH", "text": "FUNCTION: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:22535422, PubMed:29723437, PubMed:27378283, PubMed:29610307). Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
+{"protein": "MASALLRKATVGGSAAAAAARWASRGLASVGSGSDIVSAAPGVSLQKARSWDEGVATNFSTTPLKDIFHGKKVVIFGLPGAYTGVCSQAHVPSYKNNIDKLKAKGVDSVICVSVNDPYALNGWAEKLQAKDAIEFYGDFDGSFHKSLDLEVDLSAALLGRRSHRWSAFVDDGKIKAFNVEVAPSDFKVSGAEVILDQI", "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. Reduces preferentially hydrogen peroxide rather than alkyl peroxides. May be involved in mitochondrial redox homeostasis. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily."}
+{"protein": "MDEGVIAVSAMDAFEKLEKVGEGTYGKVYRAREKATGKIVALKKTRLHEDEEGVPSTTLREISILRMLARDPHVVRLMDVKQGLSKEGKTVLYLVFEYMDTDVKKFIRSFRSTGKNIPTQTIKSLMYQLCKGMAFCHGHGILHRDLKPHNLLMDPKTMRLKIADLGLARAFTLPMKKYTHEILTLWYRAPEVLLGATHYSTAVDMWSVGCIFAELVTNQAIFQGDSELQQLLHIFKLFGTPNEEMWPGVSTLKNWHEYPQWKPSTLSSAVPNLDEAGVDLLSKMLQYEPAKRISAKMAMEHPYFDDLPEKSSL", "text": "SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "MLRGEIWQVDLDPARGSAANMRRPAVIVSNDRANAAAIRLDRGVVPVVPVTSNTEKVPIPGVVAGSERWPGRRFEGAGPAGWIRRCATSPLPS", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system, its cognate antitoxin is MazE1 (Probable). Probably an endoribonuclease (By similarity). SIMILARITY: Belongs to the PemK/MazF family."}
+{"protein": "MHPSTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQSLCPAPPSSPGHVFPQSPCPTSYPHSPGSPSESDSPYQHSDFRPVCYEEPQHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKVFNNQLFAQLLAQSVHHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS", "text": "FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor- regulated SMAD (R-SMAD). Has been shown to be activated by activin type I receptor-like kinases (ALK-2, ALK-3, ALK-6) which stimulate heteromerization between SMAD9 and SMAD4. May play a role in osteoblast differentiation and maturation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. SIMILARITY: Belongs to the dwarfin/SMAD family."}
+{"protein": "MSRPSRVLGLPLLSLGLTLLVSTPLQAQEAQTFRAVKQDLVKLYQSHPSTFYCGCNIKFSGKKMAPDWESCGYLPRKQANRAARIEWEHVVPAWEFGHQLQCWQEGGRKNCGKSAEFNKMEGDMHNLFPAIGEVNGDRANYRFSDWNGKPNQYGKCQMLVDFKEQRVQPPKGPVRGQIARAYLYMGEQYGLRLAAQQRKLFEAWDRQYPADRWECERNRRIGKLQGNTNPFIEKQCQ", "text": "FUNCTION: Endonuclease which is capable of degrading plasmid DNA. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the EndA/NucM nuclease family."}
+{"protein": "MPALRPLLPLLLLLRLTSGAGLLPGLGSHPGVCPNQLSPNLWVDAQSTCERECSRDQDCAAAEKCCINVCGLHSCVAARFPGSPAAPTTAASCEGFVCPQQGSDCDIWDGQPVCRCRDRCEKEPSFTCASDGLTYYNRCYMDAEACLRGLHLHIVPCKHVLSWPPSSPGPPETTARPTPGAAPVPPALYSSPSPQAVQVGGTASLHCDVSGRPPPAVTWEKQSHQRENLIMRPDQMYGNVVVTSIGQLVLYNARPEDAGLYTCTARNAAGLLRADFPLSVVQREPARDAAPSIPAPAECLPDVQACTGPTSPHLVLWHYDPQRGGCMTFPARGCDGAARGFETYEACQQACARGPGDACVLPAVQGPCRGWEPRWAYSPLLQQCHPFVYGGCEGNGNNFHSRESCEDACPVPRTPPCRACRLRSKLALSLCRSDFAIVGRLTEVLEEPEAAGGIARVALEDVLKDDKMGLKFLGTKYLEVTLSGMDWACPCPNMTAGDGPLVIMGEVRDGVAVLDAGSYVRAASEKRVKKILELLEKQACELLNRFQD", "text": "FUNCTION: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease- inhibitor activity (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the WFIKKN family."}
+{"protein": "TQSTGTSQTVEVGLWGGPDN", "text": "FUNCTION: Alpha-methyl-D-mannoside and D-mannose specific lectin. Binds IgA. SIMILARITY: Belongs to the jacalin lectin family."}
+{"protein": "EFRYSQYKVQYDMPKEAYESKWTQCIKLIDQGGENLEERLNSQFKNWYRQKYLNLEEYRRLTVLNQIAWKALSNQIQYSCRKIMNSDISSFKHINELKSLEHRAAKAAEAEMKKRAQKPKKKKSRRGWLCCGGGDIETVEPQQEEPVQTVQEQQVNEYGDILPTLRASITNSAINYYDTVKDGVYLDHETSDALYTDEDLLFDLEKQKYMDMLDTSQEESVEENEEEHTVDDEHVEEHTADDEHVEEPTVADDEHVEEPTVADEHVEEPTVAEEHVEEPTVAEEHVEEPASDVQQTSEAAPTIEIPDTLYYDILGVGVNADMNEITERYFKLAENYYPYQRSGSTVFHNFRKVNEAYQVLGDIDKKRWYNKYGYDGIKQVNFMNPSIFYLLSSLEKFKDFTGTPQIVTLLRFFFEKRLSMNDLENKSEHLLKFMEQYQKEREAHVSEYLLNILQPCIAGDSKWNVPIITKLEGLKGSRFDIPILESLRWIFKHVAKTHLKKSSKSAKKLQQRTQANKQELANINNNLMSTLKEYLGSSEQMNSITYNFENINSNVDNGNQSKNISDLSYTDQKEILEKIVSYIVDISLYDIENTALNAAEQLLSDNSVDEKTLKKRAQSLKKLSSIMERYAGGKRNDKKAKKYDTQDVVGYIMHGISTINKEMKNQNENVPEHVQHNAEANVEHDAEENVEHDAEENAEENVEENVEEVEENVEENVEENVGEKKMRREEKKKRVQEPIKIDEIQVYDIIKNEKKKKTEF", "text": "FUNCTION: May disrupt the normal intermolecular interactions of the cytoplasmic domain of band 3 and thereby facilitate the invagination of the red cell membrane which is necessary for the formation of the parasitophorous vacuole. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Probably located on the cytoplasmic face of the membrane where it associates with components of the membrane skeleton."}
+{"protein": "MDIVNLILVAVLIALTAFFVASEFAIIRIRGSRIDQLIAEGNKAAIAVKKVTTHLDEYLSACQLGITLTSIGLGVLGESTIERLLHPLFVQMNVPGSLSHVISFIFAYAIITFLHVVVGELAPKTVAIQKAEAVSMLFAKPLIWFYRIAFPFIWLLNNSARLLTKAFGLETVSENELAHSEEELRIILSESYKSGEINQSEFKYVNKIFEFDDRLAKEIMIPRTEIVSLPHDIKISEMMDIIQIEKYTRYPVEEGDKDNIIGVINIKEVLTACISGEVSVDSTISQFVNPIIHVIESAPIQDLLVKMQKERVHMAILSDEYGGTAGLVTVEDIIEEIVGEIRDEFDIDEISEIRKIGEGHYILDGKVLIDQVNDLLGIHLENEEVDTIGGWFLTQKYDVEKDDSIIEEGCEFIINEIDGHHVAYIEVKKLQEEELLETANQQEA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0053 family."}
+{"protein": "MKHYSIQPANLEFNAEGTPVSRDFDDVYFSNDNGLEETRYVFLGGNQLEVRFPEHPHPLFVVAESGFGTGLNFLTLWQAFDQFREAHPQAQLQRLHFISFEKFPLTRADLALAHQHWPELAPWAEQLQAQWPMPLPGCHRLLLDEGRVTLDLWFGDINELTSQLDDSLNQKVDAWFLDGFAPAKNPDMWTQNLFNAMARLARPGGTLATFTSAGFVRRGLQDAGFTMQKRKGFGRKREMLCGVMEQTLPLPCSAPWFNRTGSSKREAAIIGGGIASALLSLALLRRGWQVTLYCADEAPALGASGNRQGALYPLLSKHDEALNRFFSNAFTFARRFYDQLPVKFDHDWCGVTQLGWDEKSQHKIAQMLSMDLPAELAVAVEANAVEQITGVATNCSGITYPQGGWLCPAELTRNVLELAQQQGLQIYYQYQLQNLSRKDDCWLLNFAGDQQATHSVVVLANGHQISRFSQTSTLPVYSVAGQVSHIPTTPELAELKQVLCYDGYLTPQNPANQHHCIGASYHRGSEDTAYSEDDQQQNRQRLIDCFPQAQWAKEVDVSDKEARCGVRCATRDHLPMVGNVPDYEATLVEYASLAEQKDEAVSAPVFDDLFMFAALGSRGLCSAPLCAEILAAQMSDEPIPMDASTLAALNPNRLWVRKLLKGKAVKAG", "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. 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. 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. SIMILARITY: In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family. SIMILARITY: In the C-terminal section; belongs to the DAO family."}
+{"protein": "MAGNNNTPLGSSSGLPFPTLKRSHILHCSYHYWHPKYRSVTPKARLIPLNDAFLNYLRADGIILPPQDENPPGADDDSGIYSLSDDSDPDDDDVDPSIQWQEIHAQIKATIEELGGKVAPKLNWSAPKDATWISATNDMQCRTPNDIYLLLKSSDFVTHDLEHAFDGCVSDTEEKSDGEVEVEVEEGKEKEQKQAEQSRIPYHLVLRKYITLNPSLEFRCFVRDRKLLCLCQRDLNHFNFLFGLRDNLRDKIQTFFDIRLRDTFPDPDFVFDVYVPPPHNRVWLIDINPFALRTDPLLFSWLEILNLKVPSCDDDGESDTVRVEMRRGGAERGTENGIGDEESEGGDEDDLDAATTFSFVPEFRLVEHDDPEAYGFATPRYSAHKLPRDVVDASRSGPGGMNEFLGQWQDILAKRIQEDEEGGA", "text": "FUNCTION: Regulates the cell cycle in a nutrient dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CDC123 family."}
+{"protein": "MEFVAKLFKFFKDLLGKFLGNN", "text": "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. 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). Showed the most pronounced pro-inflammatory and cytolytic activities in the host, thus contributing greatly to virulence and possibly to the development of disease. 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. SIMILARITY: Belongs to the phenol-soluble modulin alpha peptides family."}
+{"protein": "MRVLGLNGWPRDFHDASAALLVDGRIAAFAEEERFTRKKHGYNTAPVQAAAFCLAQAGLTVDDLDAVAFGWDLPAMYRERLGGWPHSDSEALDILLPRDVFPRRTDPPLHFVQHHLAHAASAYYFSGEDRGAVLIVDGQGEEECVTLAHAEGGKITVLDTVPGAWSLGFFYEHVSEYTGLGGDNPGKLMGLAAHGTTVDETLSAFAFDSDGYRLNLIDPQARDPEDWDEYSVTERAWFAHLERIYRLPPNEFVRRYDPAKGRVVRDTRRDPYEYRDLAATAQAALERAVFGLADSVLARTGERTLFVAGGVGLNATMNGKLLTRSTVDKMFVPPVASDIGVSLGAAAAVAVELGDRIAPMGDTAAWGPEFSPDQVRAALDRTGLAYREPANLEREVAALIASGKVVGWAQGRGEVGPRALGQRSLLGSAHSPTMRDHINLRVKDREWWRPFAPSMLRSVSDQVLEVDADFPYMIMTTKVRAAYAERLPSVVHEDWSTRPQTVTEASNPRYHRMLTELGDLVGDPVCLNTSFNDRGEPIVSSPADALLTFSRLPIDALAVGPYLVTKDLRH", "text": "FUNCTION: TobZ is involved in the biosynthesis of the 2- deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. Catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O- carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. SIMILARITY: Belongs to the NodU/CmcH family."}
+{"protein": "SSPEKKNDMSKPGRMRFDNKKEPRSSAKNSGNGYGCVDVNAGREPLTGPGKYPSSFLLLLEHRKPPDKDRDRWDNVKGCERKDGKSHWYDSMLKHRSPREKTLVGSGKDSTNFVYRLLTEPLLNERAGCKVVDMWYSLSYWMDVVNKRFGLCHYLGSMMDHGRWNDYSLCKDSYAGKHKPAGGPPTPRLKNREECKFYWCWSGSEERAGGMGREYVMHSGGLYGDLTDKRDDPEPNGNLEGGV", "text": "FUNCTION: Has potent hemolytic activity. Is lethal to crayfish. Causes cutaneous inflammation in humans. May act as a pore-forming toxin, disrupting normal transmembrane ion concentration gradients in susceptible cells. SUBCELLULAR LOCATION: Secreted Nematocyst Target cell membrane. Note=Forms a membrane channel in the prey. SIMILARITY: Belongs to the jellyfish toxin family."}
+{"protein": "MQTQIKVRGYHLDVYQHVNNARYLEFLEEARWDGLENSDSFQWMTAHNIAFVVVNININYRRPAVLSDLLTITSQLQQLNGKSGILSQVITLEPEGQVVADALITFVCIDLKTQKALALEGELREKLEQMVK", "text": "FUNCTION: Long-chain acyl-CoA thioesterase that could be involved in beta-oxidation of fatty acids (PubMed:18576672). Is most active with 3,5-tetradecadienoyl-CoA, a metabolite of oleic acid that is hydrolyzed during oleate beta-oxidation, but can also use other substrates such as 3,5-dodecadienoyl-CoA, 9-cis-octadecenoyl-CoA, octadecanoyl-CoA, hexadecanoyl-CoA, 3-hydroxytetradecanoyl-CoA and tetradecanoyl-CoA (PubMed:18576672). SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family."}
+{"protein": "MGARASVLTGGKLDQWEAIYLRPGGKKKYRLKHLVWASRELERFACNPGLMDTANGCAQLINQLEPALKTGSEGLRSLXNTLAVLYCVHSNIPVHNTQEALDKIKEKQEQHKSEPKKPEAGTAAAADSSISRNYPLVQNAQGQMVHQPLTPRTLNAWVKVIEEKAFNPEIIPMFMALSEGATPSDLNSMLNTVGGHQAAMQMLKEVINEEAAEWDRTHPAPVGPLPPGQMRDPRGSDIAGTTSTLAEQVAWMTSNPPIPVGDIYRRWIVLGLNRIVRMYSPVSILEIKQGPKEPFRDYVDRFYKTLRAEQATQDVKNWMTETLLVQNANPDCKQILKALGPGATLEEMMTACQGVGGPAHKARVLAEAMAQAQTATSVFVQRGNFKGIRKTIKCFNCGKEGHLARNCKAPRRRGCWKCGQEGHQMKDCKNEGXQANFLGKGWSPFKGRPGNFPQTTTRREPTAPPLESYGSQEEKSTQGKEMQENQEKTETSLYPPLTSLRSLFGNDLSSQ", "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": "MPEHLNARVEACYRQAEHFFQRSFPRPTVSFRLRGQKAGVAHLDENLLRFNPQLYRENREHFLEQTVAHEVAHLIAHQLFGPRIRPHGEEWQLIMRGIYGLPPDRCHTYAVKRRATTRYLYRCHCPEHNDFPFSPQRHTLVAKGRRYYCRRCKATLVFTGEVLRE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SprT family. SIMILARITY: Belongs to the SprT family."}
+{"protein": "MKSLQTICLLFIFIARGTSDKCEICHGFGDDCDGYQEECPSPEDRCGKILIDIALAPVSFRATHKNCFSSSICKLGRVDIHVWDGVYIRGRTNCCDNDQCEDQPLPGLPLSLQNGLYCPGAFGIFTEDSTEHEVKCRGTETMCLDLVGYRQESYAGNITYNIKGCVSSCPLVTLSERGHEGRKNDLKKVECREALKPASSD", "text": "FUNCTION: Inhibits the enzymatic activity of phospholipase A2 (PA2) (PubMed:10924158). Binds to the major PLA2 toxin of D.russelli siamensis (Daboiatoxin, AC Q7T2R1, and AC Q7T3T5) at 1-2-fold molar excess of inhibitor to toxin (PubMed:10924158). It exhibits broad spectra in neutralizing the toxicity of various snake venoms and toxins and inhibits the formation of edema in mice (PubMed:10924158). May bind to PLA2 through its proline-rich hydrophobic core region (Probable). SUBCELLULAR LOCATION: Secreted Note=Secreted in blood plasma. SIMILARITY: Belongs to the CNF-like-inhibitor family."}
+{"protein": "MKPNNRTCDVITNKDESLPALLLPALNSYTCDDSLLKGQISSNGRYQPFGFSDCSLLPKRLNIQAGQGSMPVSSIQCADHSYSNWQKESEKTKLPKLGCPTEYTEYYKTVSSGETTDSAVVSSIATNRLKRKRQRDGPSCDSCRIKKIKCNATIIIFLQDRNLISSISSNLHYTLSQDDINQFRMKFFRKLPDVMGTYEVIKHLDKIVLFKACTSCSRRNQKNGKCLFSRGFTKSDMNVFPKINSKLKDKSIFEMTVDDYVAAGFQTL", "text": "FUNCTION: Putative transcription factor involved in the regulation of the activity of the cAMP/protein kinase A pathway. Involved in sterol uptake. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SUT1 family."}
+{"protein": "GVPCRCDSDGPSVHGNTLSGTIWVGSCETGWHKCNTEHNLFHECCKQ", "text": "FUNCTION: Inhibits voltage-gated sodium channels (Nav). SUBCELLULAR LOCATION: Secreted. Nematocyst. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type I subfamily."}
+{"protein": "MKRYLSVALAALVLTGCITQPPVEPTTPPVTIEPVTPPVPETPPPVDNVPPPPKMEQSIDWAASVEPLVAQMVNSNDVANGSILLLDSVKNNTNGRLPTAKATSALHQVLSSNKKFVLISPQQLAVAKQTLGLSEEDSLGSRSKAIGLARYVSAQYVLYSDVSGDVKSPTIEMQLMQAQTGEIIWSGNGPVKR", "text": "FUNCTION: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the LpoB family."}
+{"protein": "MNLSDAINAVNRVKDIINSHNTWRRKETINLIPSENVMSPLAEYFYINDMMGRYAEGTIGNRYYQGVKYVDEIEAYLVDLMSKLFHASYVDVRPISGTVANMAVYLTLAKGGKIAAVPRQCGGHISHDEVGAPGAFGIKVIHLPCDEENFSINVDSAVKVIREEKPQLVILGASLYLFPHPVKELAQVAHENGAYLMHDSAHVLGLIAGGQFPNSLNEGADLMTSSTHKTFPGPQGGVIFTNNESIFKNIQRAVFPQLTSNYHLHRYASTAITAIEMMTFGESYAYQVRLNAKKLAEELSKYGIPVVAEARGFTETHQVVFDASKFGGGAKVAQLLEDGGIIVNKNMLPWDRSAVRPSGIRMGVQEMTRVGMGTQEMAEIAAFMKAILIDGKEPSSVKGEVKEFKAHYTEVKYGFKLSDVGIKCDCLPLNY", "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": "MEFSGTHQAFRNRWAKTDDEMCKHSMSFHLHKTLRKEFFASYLYLLEQIPLVKLYALTCEYIKGEKQFYYRAQNFYKDVPPSEEGMMGDFVEISDIDLEGSRQFLKKFVGPGKAGTKCALDCGCGIGRVSKGVLFPVFESMEMLDMMEEFILHAHECYLGDYADRVESYYLYNLQEFIPPRKKYDVIWMQWVACHLTDKDLMEFLMRAKESLRPNGVIIIKDNMARQGCKLDPIDSSIIRHLDIMNGIIQRAGLNILDVEKQEGFPEAIVPVWMIAMR", "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 monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-Lys motif. Predominantly functions as a mono-methyltransferase but is also able to di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA peptide (in vitro). May activate NTMT1 by priming its substrates for trimethylation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family."}
+{"protein": "MAILAWLEPRPLLAVLVLVLTMRMAQPAHLLTLLSSGQGALDRVALGGLLNTLAARVHCTSGPCGKCLSVDDLLALGRPEEPGHLARLSAAAALYLSDPEGTCEDIRAGRWASRADHLLALLEGPKALAPGLSRLLQRIQAQTTGQPSAGEACVDPPQLLREAGVAGAPGSPGPVLATLLEHVGRGSCFHTLPTPQYFVDFVFQQSHGNTPNISVAELAALMQRLGVGGVTETHSDHHHQEKRVNRQGPTPLTAPNSSSDTWDTVCLSARDVMAVYGLSEQTGVTPEAWAQLSPALLQQQLSGACSPQPSHPAQNQLSQAEKYLYGSLATLLICLCSTFGLLLLTCAACSTAAHYVIQTFLGMAVGALTGDALLHLTPKVLGLHQHGGDSEHRADSHGPQTTWRLVVALSGLYVFFLFEKLCDLLLPQDPEDRKGTPRSHSGHSHGMSLQLAPRELRPPKQPHEGSRADLVAEESPELLSPEPRRKSPELRLLPYMITLGDGLHNFADGLAVGAAFASSWKTGLATSLAVFCHEVPHELGDFAALLHAGLPVSRALLLNLASGLTAFAGLYVALALGVGEESESWTLAVAIGLFLYVALCDMLPAMLNVRDPRPWLLFLLHNVGLLGGWAVLLLLSLYEDSIAL", "text": "FUNCTION: Selective transporter that mediates the uptake of Zn(2+) (PubMed:27321477). Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability. Exhibits also polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(2+) but at higher concentrations (By similarity). 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 zinc availability. Translocates to the apical membrane during zinc deficiency. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
+{"protein": "MSPTPPETVTPLWQQFLRWAARVGLAKRLAFALSLAALVAGFATYTALTESAPFGETNPRTVTWLLTLDLALLLLLGVLIARRIVYLWIGRRRGLAGSQMHVRLVAVFSLLAVAPAIIMAIFSTVFFYVGVQSWFSERVRTAVNESLAVASAYLHEHQQNIRADALAMANDLNQEAARLASDPERFEQVVATQAMLRALSEAIVFNGTTGAIVARSGYTFALEFDPIPDDKLATARRGEVAMIVSENDDRVRALVRLDRFADTYLYVGRMVEPRVLSHMASAEGAVREFGALESQRGSLQITFTLIFLCVALLLLLAAVWAGLIFATRLVRPISALIGAADRVRAGDLTVRVTERPAEDDLALLSRAFNRMTTEIESQRHALLSANRLIDSRRRFTETVLSGVSAGRDGLDAEGRITLSKFSAARLLGVKDAESLIGMRLAELVPEMGGLLHEAPGRPGLVVQDQIKIRRDGTTPLTLLVRISTEGRGSGMMRGYVVTFDEHHRTWSPAQRKAAWARRRPIAASPTRVKNPLTPIQLSAEPCAASTLKEITSDTEVFTMCTDTIVRQVDDIRRMVDEFSAFARMPQPVMKPCNLNDLVRQAVFLQSSAHAGKIKFDMALPQGPLTVPCDSRQISQALTNLLQNAADAIEGRPPPAEGTELPPGHVAIRVEADAERIAMIIEDNGKGLPTEERDRLTEPYVTTRAKGTGLGLAIVKKIMEDHGGVLTLEDREGGGARVGLVIPQHIPPASGTAAGDAPGGVGTPAETGEEKRHAAHGA", "text": "FUNCTION: Member of the two-component regulatory system NtrY/NtrX involved in nitrogen level control. Probably activates NtrX by phosphorylation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
+{"protein": "MKDLRFGRLKCYSLHLGILPLTVLVLVFFCFVCLSLRSQEWGHPGAVNRKAYPQPRVLTPTRTDVLVLTPWLAPIIWEGTFDIDTLNEQFRLRNTTIGLTVFAVKKYVVFLKLFLETAEQHFMVGHKVIYYVFTDRPADVPQVPLGAGRRLVVLTVRNYTRWQDVSMHRMEVISHFSEQRFRHEVDYLVCADVDMKFRDHVGVEILSALFGTLHPGFYRSRRESFTYERRPQSQAYIPWDQGDFYYMGAFFGGSVVEVHHLTKACHQAMVEDQANGIEAVWHDESHLNKYLLYHKPTKVLSPEYMWDQQLLGWPSIMKKLRYVAVPKNHQAIRN", "text": "FUNCTION: Posseses strong B transferase activity and a weak A transferase 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 (By similarity). SIMILARITY: Belongs to the glycosyltransferase 6 family."}
+{"protein": "MEDPDIKRCKLSCVATVDDVIEQVMTYITDPKDRDSASLVCRRWFKIDSETREHVTMALCYTATPDRLSRRFPNLRSLKLKGKPRAAMFNLIPENWGGYVTPWVTEISNNLRQLKSVHFRRMIVSDLDLDRLAKARADDLETLKLDKCSGFTTDGLLSIVTHCRKIKTLLMEESSFSEKDGKWLHELAQHNTSLEVLNFYMTEFAKISPKDLETIARNCRSLVSVKVGDFEILELVGFFKAAANLEEFCGGSLNEDIGMPEKYMNLVFPRKLCRLGLSYMGPNEMPILFPFAAQIRKLDLLYALLETEDHCTLIQKCPNLEVLETRNVIGDRGLEVLAQYCKQLKRLRIERGADEQGMEDEEGLVSQRGLIALAQGCQELEYMAVYVSDITNESLESIGTYLKNLCDFRLVLLDREERITDLPLDNGVRSLLIGCKKLRRFAFYLRQGGLTDLGLSYIGQYSPNVRWMLLGYVGESDEGLMEFSRGCPNLQKLEMRGCCFSERAIAAAVTKLPSLRYLWVQGYRASMTGQDLMQMARPYWNIELIPSRRVPEVNQQGEIREMEHPAHILAYYSLAGQRTDCPTTVRVLKEPI", "text": "FUNCTION: Required for jasmonate-regulated plant fertility and defense processes, and for coronatine and/or other elicitors perceptions/responses. Seems to not be required for meiosis. Required for the regulation of some genes induced by wounding, but not for all. Component of SCF(COI1) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including the ribulose bisphosphate carboxylase small chain 1B RBCS-1B and the histone deacetylase HDA6). These SCF complexes play crucial roles in regulating response to jasmonate, and their interactions with the COP9 signalosome (CSN) appear to be important for their activity. Interacts with TIFY10A and inositol pentakisphosphate to form a high-affinity jasmonates coreceptor. Involved in the regulation of plant gene expression during plant- pathogen interactions with Pseudomonas syringae and Alternaria brassicicola."}
+{"protein": "MLVFKGKLKEHPRWEVENELYRFRNRVFSDRLGWDVESHRGLEQDSFDTPDTHWVLIEDEEGLCGCIRLLSCAKDYMLPSIFPTALAGEAPPRSNDVWELTRLAIDAERAPRLGNGISELTCIIFREVYAFAKAQGIRELVAVVSLPVERIFRRLGLPIERLGHRQAVDLGAVRGVGIRFHLDERFARAVGQPLQGAYDEARELVTE", "text": "FUNCTION: Required for the synthesis of N-butanoyl-L-homoserine lactone (BHL), an autoinducer molecule which binds to AhyR. SIMILARITY: Belongs to the autoinducer synthase family."}
+{"protein": "DHEIAAAAGVPIPTIFEMEGEQGFRSRETAILKKLIVLPHIVLSTGGGAVLKEENRALIRKSGTVVYLHAPPETLLERTRCDNSRPLLQVADPLAKLRELYAARDPVYRQTADFTVESANCRETVQTLLKRLSR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the shikimate kinase family."}
+{"protein": "MKTQFAVLIISMILMQMLVQTEAGFWGKLWEGVKSAIGKRSLRNQDQFDNMFDSDLSDADLKLLDDLFD", "text": "FUNCTION: Antimicrobial peptide that is rapidly bactericidal against Gram-positive bacteria. 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": "MGPLLQLAGTRLHIGIDDTDSIKGMCTTYLGFRLARLLQKEGAEFEDYPRLVRLNPNVPWKTRGNGAVGMTVNVSDPEAARKIAIDAVSLYSDLENGANPAAVFCEGGIPQPVRDLSREALHVMVEQERARGIIERHCSGLFYTGSGQGMVGAAAAIGYEFGDSTLELLSYRREENRGTPRPIWPEDVRGIQGAYPDTFNSYDEARGTSIIAPRGPDPVFYGIRGELASSLLGASEMVRTPERLEGYMIYRSNQGTADHLEYVIDAADPRPYSSGTISGVISTEPVVREGGHVFFEINAGGSMVPCAVYKESGMTDAAALLRGGDKVVVGGGIRRESGSHPKVLNVEFARVERLARIYRMANPYCTKCSKSMKSKGIGQGFKCTRCGAASIHRVEREIPRGISVGLYLPVASSQRHLARPYGRQGRTSRIQFDGASPWLGVFDSGE", "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": "MPVFYTPIPQNLRVGLANVSGSVFINNRTRDSADFKDHYLENEACAEVSSHLPLQMMLYFNMFFFPFWWISELLMLQLKFSYLPVYYQCLLVTGMVLISIFEVLRMYLGYAGNLKEKVPELAGFWLISFLFQLPILLFFITDPDIIILPLERAVHSLYLAFLLGELMASFLALRVMTRKLAQQFHMRQFGHVQGLHTAEALPMFGLPYGGRSVLPVQDI", "text": "FUNCTION: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity). SUBCELLULAR LOCATION: Cell projection, cilium membrane; Multi-pass membrane protein Note=Localizes to the transition zone of primary cilia. SIMILARITY: Belongs to the TMEM17 family."}
+{"protein": "MRPQVVGAILRSRAVVSRQPLSRTHIFAAVTVAKSSSPAQNSRRTFSSSFRRLYEPKAEITAEGLELSPPQAVTGGKRTVLPNFWLRDNCRCTKCVNQDTLQRNFNTFAIPSDIHPTKVEATKENVTVQWSDNHTSTYPWPFLSFYLTSNARGHENDQISLWGSEAGSRPPTVSFPRVMASDQGVADLTAMIKEFGFCFVKDTPHDDPDVTRQLLERIAFIRVTHYGGFYDFTPDLAMADTAYTNLALPAHTDTTYFTDPAGLQAFHLLEHKAAPSRPPPPPPPPPPPSEEKEAAGSAAGEAAAAAEGGKSLLVDGFNAARILKEEDPRAYEILSSVRLPWHASGNEGITIAPDKLYPVLELNEDTGELHRVRWNNDDRGVVPFGEKYSPSEWYEAARKWDGILRRKSSELWVQLEPGKPLIFDNWRVLHGRSAFSGIRRICGGYINRDDFISRWRNTNYPRSEVLPRVTG", "text": "FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the gamma-BBH/TMLD family."}
+{"protein": "VFTHVLQPYPEIRPRFPLVGGWKTHYXV", "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. SIMILARITY: Belongs to the OST1 family."}
+{"protein": "DCLGFMRKCIPDNDKCCRPNLVCSRTHKWCKYVF", "text": "FUNCTION: Potent voltage-gated sodium channel blocker (PubMed:25658507). Potently inhibits the voltage-gated sodium channels Nav1.7/SCN9A (IC(50)=0.58-10 nM) (PubMed:25658507, PubMed:26999206). Also shows a moderate activity on Nav1.1/SCN1A (IC(50)=6 nM), Nav1.2/SCN2A (IC(50)=5-128 nM), Nav1.3/SCN3A (IC(50)=20.3-170 nM), and Nav1.6/SCN8A (IC(50)=17-20.1 nM) (PubMed:25658507, PubMed:26999206). Shows an unclear inhibition of Nav1.4/SCN4A (IC(50)=200 nM to >10 uM), Nav1.5/SCN5A (IC(50)=140 nM to >10 uM) and Nav1.8/SCN10A (IC(50)=68- 12200 nM) (PubMed:25658507, PubMed:26999206). Weakly blocks the low voltage-gated calcium channels Cav3.1/CACNA1G (30% inhibition of the peak current at 9.8 nM) (By similarity). shows moderate affinity for lipid bilayers (By similarity). In vivo, when tested on the OD1-induced mouse model of Nav1.7/SCN9A-mediated pain, the toxin is effective when co-administered with OD1, but lacks efficacy when delivered systemically (PubMed:26999206). FUNCTION: Potent voltage-gated sodium channel blocker (PubMed:24211312). Potently inhibits the voltage-gated sodium channels Nav1.7/SCN9A (IC(50)=0.58-10 nM) (PubMed:24211312) (By similarity). Shows a moderate activity on Nav1.1/SCN1A (IC(50)=6 nM), Nav1.2/SCN2A (IC(50)=5-128 nM), Nav1.3/SCN3A (IC(50)=20.3-170 nM), and Nav1.6/SCN8A (IC(50)=17-20.1 nM) (PubMed:24211312) (By similarity). Shows an unclear inhibition of Nav1.4/SCN4A (IC(50)=200 nM to >10 uM), Nav1.5/SCN5A (IC(50)=140 nM to >10 uM) and Nav1.8/SCN10A (IC(50)=68-12200 nM) (PubMed:24211312) (By similarity). Weakly blocks the low voltage-gated calcium channels Cav3.1/CACNA1G (30% inhibition of the peak current by 9.8 nM of the toxin) (By similarity). It shows moderate affinity for lipid bilayers (By similarity). SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 08 (Gtx1-15) subfamily."}
+{"protein": "MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG", "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). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster (PubMed:18390544). It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b (COB) to cytochrome c1 (CYT1) (PubMed:1657998, PubMed:2538628) (Probable). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Rieske iron-sulfur protein family."}
+{"protein": "MKWDWIFFDADETLFTFDSFTGLQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGAITSLQLQHGRFESWAERLNVEPGKLNEAFINAMAEICTPLPGAVSLLNAIRGNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGNPDRSRVLMVGDTAESDILGGINAGLATCWLNAHHREQPEGIAPTWTVSSLHELEQLLCKH", "text": "FUNCTION: Nucleotidase that shows high phosphatase activity toward non- canonical pyrimidine nucleotides and three canonical nucleoside 5'- monophosphates (UMP, dUMP, and dTMP), and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Appears to function as a house-cleaning nucleotidase in vivo, since the general nucleotidase activity of YjjG allows it to protect cells against non- canonical pyrimidine derivatives such as 5-fluoro-2'-deoxyuridine, 5- fluorouridine, 5-fluoroorotate, 5-fluorouracil, and 5-aza-2'- deoxycytidine, and prevents the incorporation of potentially mutagenic nucleotides into DNA. Its dUMP phosphatase activity that catalyzes the hydrolysis of dUMP to deoxyuridine is necessary for thymine utilization via the thymine salvage pathway. Is strictly specific to substrates with 5'-phosphates and shows no activity against nucleoside 2'- or 3'- monophosphates. FUNCTION: Nucleotidase that shows high phosphatase activity toward non- canonical pyrimidine nucleotides and three canonical nucleoside 5'- monophosphates (UMP, dUMP, and dTMP), and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Appears to function as a house-cleaning nucleotidase in vivo, since the general nucleotidase activity of YjjG allows it to protect cells against non- canonical pyrimidine derivatives such as 5-fluoro-2'-deoxyuridine, 5- fluorouridine, 5-fluoroorotate, 5-fluorouracil, and 5-aza-2'- deoxycytidine, and prevents the incorporation of potentially mutagenic nucleotides into DNA. Its dUMP phosphatase activity that catalyzes the hydrolysis of dUMP to deoxyuridine is necessary for thymine utilization via the thymine salvage pathway. Is strictly specific to substrates with 5'-phosphates and shows no activity against nucleoside 2'- or 3'- monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. YjjG family."}
+{"protein": "MPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAIPFAITISTGFCAACHGCLFIACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTRAKGIIAICWVLSFAIGLTPMLGWNNCGQPKEGKNHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFLAARRQLKQMESQPLPGERARSTLQKEVHAAKSLAIIVGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHTNSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFKAAGTSARVLAAHGSDGEQVSLRLNGHPPGVWANGSAPHPERRPNGYALGLVSGGSAQESQGNTGLPDVELLSHELKGVCPEPPGLDDPLAQDGAGVS", "text": "FUNCTION: Receptor for adenosine (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 Note=Colocalizes with GAS2L2 at neuronal processes. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MKGYLTFVLHTHIPYVRKHGKWPFGEEWVFEAISETYIPLLMEFERLRDSGVKFGIVINVTPVLAEQLTDEYMKKAFEEYMERKLKAMEEDLKSGKYDEKAVSYMLNYFRKVYDYWKAINGDIIGKLRELQDQGYVEVITSAATHGYLPLLGRDEAIRAQIANGVATYEKHFGMKPKGIWLPECAYRPAGEWELPGGRKVKRQGIEKFLEEFGLRYFFVESRLIDEGPASNVYGEVLIADTEKTTLRPYWIKGSNVAVFARNRETGHQVWSAHYGYPGDFWYREFHKKAPKSGGQYWRITSKEVGLGEKEFYDPDKAMERVEEHARHFVSLVERLLREHEEKFGEKGIIVAPYDTELFGHWWFEGVKWLGRVLELLYQRGVETPTLSRFLEEYSGEKHEIELPEGSWGANSDHSTWWNEETEWTWPHIYRAEDRMVAIVSRFRGRDELTNRVIEQLARELLILEASDWQFLITTGQAKEYAKRRVLIHSRDFHRLANELVRYVKIGEFDVKLLEELEERDNPFRPVVVGPYVSENPPELEEYVEPPEVPPEKEETEEKPKVLTEKATSLALAVKKVKPVKEETREVKKKAVEASKRGKRKSSKSKRLPRKVSKKAPSKGPSDLLSIKGIGPKTFQKLKRAGVETIEDLKNANIEDLARKTGISTKRLKKFIAQVE", "text": "FUNCTION: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two local maxima at DP 6 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Does not display alpha-galactosidase or pullulanase activity, since melibiose and pullulan are not substrates. Is not able to catalyze the hydrolysis or transglycosylation of maltoheptaose, suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity. SIMILARITY: Belongs to the glycosyl hydrolase 57 family."}
+{"protein": "MWTLALWAFSFLCKFSLAVLPTKPENISCVFYFDRNLTCTWRPEKETNDTSYIVTLTYSYGKSNYSDNATEASYSFPRSCAMPPDICSVEVQAQNGDGKVKSDITYWHLISIAKTEPPIILSVNPICNRMFQIQWKPREKTRGFPLVCMLRFRTVNSSHWTEVNFENCKQVCNLTGLQAFTEYVLALRFRFNDSRYWSKWSKEETRVTMEEVPHVLDLWRILEPADMNGDRKVRLLWKKARGAPVLEKTFGYHIQYFAENSTNLTEINNITTQQYELLLMSQAHSVSVTSFNSLGKSQEAILRIPDVHEKTFQYIKSMKAYIAEPLLVVNWQSSIPAVDTWIVEWLPEAAMSKFPALSWESVSQVTNWTIEQDKLKPFTCYNISVYPVLGHRVGEPYSIQAYAKEGTPLKGPETRVENIGLRTATITWKEIPKSARNGFINNYTVFYQAEGGKELSKTVNSHALQCDLESLTRRTSYTVWVMASTRAGGTNGVRINFKTLSISVFEIVLLTSLVGGGLLLLSIKTVTFGLRKPNRLTPLCCPDVPNPAESSLATWLGDGFKKSNMKETGNSGDTEDVVLKPCPVPADLIDKLVVNFENFLEVVLTEEAGKGQASILGGEANEYVTSPSRPDGPPGKSFKEPSVLTEVASEDSHSTCSRMADEAYSELARQPSSSCQSPGLSPPREDQAQNPYLKNSVTTREFLVHENIPEHSKGEV", "text": "FUNCTION: Associates with OSMR to form the interleukin-31 receptor which activates STAT3 and to a lower extent STAT1 and STAT5. May function in skin immunity (PubMed:15184896). Mediates IL31-induced itch, probably in a manner dependent on cation channels TRPA1 and TRPV1 (PubMed:24373353). Positively regulates numbers and cycling status of immature subsets of myeloid progenitor cells in bone marrow in vivo and enhances myeloid progenitor cell survival in vitro (PubMed:17379091). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Presynaptic cell membrane Cell projection, axon. SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 subfamily."}
+{"protein": "MANPTTGKSSIRAKLSNSSLSNLFKKNKNKRQREETEEQDNEDKDESKNQDENKDTQLTPRKRRRLTKEFEEKEARYTNELPKELRKYRPKGFRFNLPPTDRPIRIYADGVFDLFHLGHMKQLEQCKKAFPNVTLIVGVPSDKITHKLKGLTVLTDKQRCETLTHCRWVDEVVPNAPWCVTPEFLLEHKIDYVAHDDIPYVSADSDDIYKPIKEMGKFLTTQRTNGVSTSDIITKIIRDYDKYLMRNFARGATRQELNVSWLKKNELEFKKHINEFRSYFKKNQTNLNNASRDLYFEVREILLKKTLGKKLYSKLIGNELKKQNQRQRKQNFLDDPFTRKLIREASPATEFANEFTGENSTAKSPDDNGNLFSQEDDEDTNSNNTNTNSDSDSNTNSTPPSEDDDDNDRLTLENLTQKKKQSAN", "text": "FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis. SUBCELLULAR LOCATION: Membrane. Note=Most of its activity is membrane- associated. SIMILARITY: Belongs to the cytidylyltransferase family."}
+{"protein": "MKNLCWVFLSLFWFGVFLIIRFAEGQNQEGFISLDCGLPLNEPPYIESETGIQFSSDENFIQSGKTGRIPKNLESENLKQYATLRYFPDGIRNCYDLRVEEGRNYLIRATFFYGNFDGLNVSPEFDMHIGPNKWTTIDLQIVPDGTVKEIIHIPRSNSLQICLVKTGATIPMISALELRPLANDTYIAKSGSLKYYFRMYLSNATVLLRYPKDVYDRSWVPYIQPEWNQISTTSNVSNKNHYDPPQVALKMAATPTNLDAALTMVWRLENPDDQIYLYMHFSEIQVLKANDTREFDIILNGETINTRGVTPKYLEIMTWLTTNPRQCNGGICRMQLTKTQKSTLPPLLNAFEVYSVLQLPQSQTNEIEVVAIKNIRTTYGLSRISWQGDPCVPKQFLWDGLNCNITDISAPPRIISLNLSSSGLSGTIVSNFQNLAHLESLDLSNNSLSGIVPEFLATMKSLLVINLSGNKLSGAIPQALRDREREGLKLNVLGNKELCLSSTCIDKPKKKVAVKVVAPVASIAAIVVVILLFVFKKKMSSRNKPEPWIKTKKKRFTYSEVMEMTKNLQRPLGEGGFGVVYHGDLNGSEQVAVKLLSQTSAQGYKEFKAEVELLLRVHHINLVNLVGYCDEQDHFALIYEYMSNGDLHQHLSGKHGGSVLNWGTRLQIAIEAALGLEYLHTGCKPAMVHRDVKSTNILLDEEFKAKIADFGLSRSFQVGGDQSQVSTVVAGTLGYLDPEYYLTSELSEKSDVYSFGILLLEIITNQRVIDQTRENPNIAEWVTFVIKKGDTSQIVDPKLHGNYDTHSVWRALEVAMSCANPSSVKRPNMSQVIINLKECLASENTRISRNNQNMDSGHSSDQLNVTVTFDTDVKPKAR", "text": "FUNCTION: Receptor-like serine/threonine-kinase required during the endosperm development in seeds. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MLYGKENRDEAEFLEPIFGSESEQVDLPKYKLAQQSIEPRVAYQLVQDEMLDEGNARLNLATFCQTYMEPEAVKLMSQTLEKNAIDKSEYPRTTEIENRCVNMIADLWNASEKEKFMGTSTIGSSEACMLGGMAMKFSWRKRAEKLGLDINAKKPNLVISSGYQVCWEKFCVYWDIEMREVPMDREHMSINLEKVMDYVDEYTIGVVGIMGITYTGRYDDIKALDNLIEEYNKQTDYKVYIHVDAASGGLYAPFVEPELEWDFRLKNVISINTSGHKYGLVYPGVGWVLWRDKKYLPEELIFKVSYLGGELPTMAINFSHSASQLIGQYYNFVRYGFDGYKAIHERTHKVAMYLAEEIEKTGMFEIMNDGAQLPIVCYKLKENSNRGWNLYDLADRLLMKGWQVPAYPLPKNLENEIIQRLVIRADFGMNMAFNYVQDMQEAIDALNKAHILFHQEPENKTYGFTH", "text": "FUNCTION: Converts internalized glutamate to GABA and increases the internal pH. Involved in glutamate-dependent acid resistance. SIMILARITY: Belongs to the group II decarboxylase family."}
+{"protein": "MLCCMRICVCGDEGTGKSSLITSLVKGVFVTNKIQPILPQITIPPTIGTPENVTTTTVVDTSAVPQERSNLAREIRKSNVILLVYSDHYSYERVALFWLPYFRSLGVNVPVVLCANKSDLAADHTETQVIEDEMLPLMSEFKEIDSCIRTSAREHRNVNEAFFLCQKAVTHPIAPLFDAKESALKPAAVAALQRIFYLSDKDRDGYLSDKEIKDFQMRCFEKPLSEEDLVHIKETIQKTHPDSVTPSGIDCRGFIHLNKMYAEKGRHETVWIILRAFQYTDSLSLQESYLHPKFEVPPFASAELSPEGYRFFVNLFLLSDKDNDGGLNDAELASLFAPTPGLPPSWADGSFPSCTVRNEAGHVTLQGWLAQWSMTTFTSPKTTLEYLAYLGFESSDRSNPSTTAALKVTRPRKRRKRPGRVGRNVVLGHIVGAPGSGKSALLDAFLSRGFSTTYHPTIQPRTAVNTVELPGGKQCYLIMDELGELEPAILENQAKLLDQCDVIVYTYDSSDPDSFAYIPALRAKYPHLEELPSVYIALKADLDRTTQRAEHQPHEYTALLNMPGPPLHVSVTWSSIQEVFVHIAEAAMEPSTAFPRSEEDVEGKWMSWGIALGAVVCAGAAAVMIWRRVSGSGV", "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": "MENYEACVGFDVCEIPLSAVAQKIMSAMRSGDFMDSRNEGESTNTSKVAKKSSVHYSVLAEHEETQSLGTKNPESLITQTPRGSIELCPQPSITKLTCQLSAGQVQNSISSLGLSSYLIPQCDQEASVLPNMEHKRQHFLKENIGKEDKDNSSLKRKYITCSKSSEKASKHTALEKDTDGTESWPNSRDTRALGERLCDVRYLGDLAKAQLMDALKQAAALVVTLMYKDGSTQLSAKEALTCTVKGIVVLLKSHVGNSTLTLPAHGGALEKDFISEDHCVYIHTEHSPFWDPKQEAHSLFVRNILFWTLRCKCPVVCFNAKDFVRTVLQLYGEDGSWKHVADFVGLDPRVAAWLIDPSDTAPSFEDLVAKHLEKSITVKPSSTFREASRNTLSQNVFMNLKILYDLTMDLCSKLKAYGLWQLFCTLELPLIPILAVMENHKIPVDKEEMERTSALLGARLKELEQEAHFVAGEQFLIMSNNQLREILFGKLKLHLLSQRKHLPRTGLQNQLSTSEAMLNSLQDLHPLPKLILEYRQVHKIKSTFIDGLLAYMKKGSISSTWNQTGTVTGRLSAKHPNIQGISKHPIKISKPWNFKGKEEETVTISPRTLFVSSEGHTFLAADFSQIELRILAHLSGDPELLKLFQESERDDVFSTLTSQWKDIPIERVTHMDREQTKKVVYSVVYGAGKERLAACLGVTVLEATHFLERFLQKYKKIKDFAQTVIGQCHSAGYVTSILGRRRPLPRICAQDQQLRAQAERQAVNFVVQGSAADLCKLAMIRISTAVATSPTLTARLVAQIHDELLFEVEDTQVPEFAALVRRIMESLQQVQTLELQLQVPLKVNLSVGRSWGHLTPLQEILGSA", "text": "FUNCTION: DNA polymerase with very low fidelity that catalyzes considerable misincorporation by inserting dTTP opposite a G template, and dGTP opposite a T template. Is the least accurate of the DNA polymerase A family (i.e. POLG, POLN and POLQ). Can perform accurate translesion DNA synthesis (TLS) past a 5S-thymine glycol. Can perform efficient strand displacement past a nick or a gap and gives rise to an amount of product similar to that on non-damaged template. Has no exonuclease activity. Error-prone DNA polymerase that preferentially misincorporates dT regardless of template sequence. May play a role in TLS during interstrand cross-link (ICL) repair. May be involved in TLS when genomic replication is blocked by extremely large major groove DNA lesions. May function in the bypass of some DNA-protein and DNA-DNA cross-links. May have a role in cellular tolerance to DNA cross-linking agents. Involved in the repair of DNA cross-links and double-strand break (DSB) resistance. Participates in FANCD2-mediated repair. Forms a complex with HELQ helicase that participates in homologous recombination (HR) repair and is essential for cellular protection against DNA cross-links. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA polymerase type-A family."}
+{"protein": "MDKQPATSWSIHTRPEIIAKYEIFERVGSGAYADVYRARRLSDGLIVALKEIFDYQSAFREIDALTILNGSPNVVVMHEYFWREEENAVLVLEFLRSDLAAVIRDGKRKKKVEGGDGFSVGEIKRWMIQILTGVDACHRNLIVHRDLKPGNMLISDDGVLKLADFGQARILMEHDIVASDENQQAYKLEDKDGETSEPPEVIPDYENSPRQGSDGQEREAMSKDEYFRQVEELKAKQVVRDDTDKDSNVHDGDISCLATCTVSEMDDDLGRNSFSYDADEAVDDTQGLMTSCVGTRWFRPPELLYGSTMYGLEVDLWSLGCVFAELLSLEPLFPGISDIDQISRVTNVLGNLNEEVWPGCVDLPDYKSISFAKVESPLGIEGCLPNHSGDVISLLKKLICYDPASRATTMEMLNDKYLSEEPLPVPVSELYVPPTMSGPDEDSPRKWNDYREMDSDSDFDGFGPMNVKPTSSGFTIEFP", "text": "FUNCTION: CDK-activating kinase that modulates CDKD-2 and CDKD-3 activities by phosphorylation of the T-loop. Activates CDKD-2 C- terminal domain (CTD) kinase activity. Activates CDKA-1 probably by phosphorylation. Posseses a CDK kinase activity independently of association with cyclin CYCH1-1. Phosphorylates the CTD of the large subunit of RNA polymerase II. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
+{"protein": "MKKVVSSLLIILGAAMLIFAIALPTYVVPKGKVLPKDIVSTTGTDPIKGNLLDASALAEGKPVSGKENLPECRGKDKQVSCFIWKDLELQSQRFTRAQEPTDDKVVTLEAGQTLFRTDRQEPKNLVNATVDRVTLDRKTQMPVADPVSTLDVNAPALNPNGEAAIGPFTRPGIQYQFPMGTDRRSYDYFDTQALKAQPIDYVGEEEQDGEKVYKFEQTVSPVELYPRLKEQLEADGDLSKADQSTLASLRLKFPAKVWGIEGADTKSAADSKDDKKKDGDKKDEKSPEVELSRYYTVKRTLWVQPDTGVIVNGKEDIWQFYAKDQDEADKMAQPENREKEMNNPKRTALYIPGAWNDESRAAQMDKAKEGLKTLKTMGTTVPWILGPLGLLLLLVGLVMALKRRRAERHANAL", "text": "FUNCTION: Forms water-filled channels that favor the permeation of cations. SUBCELLULAR LOCATION: Secreted, cell wall Note=Probably part of the corynemycolate layer which forms a structure similar to the outer membrane found in Gram-negative bacteria. SIMILARITY: Belongs to the PorA family."}
+{"protein": "MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHKKHRTSVGPSKPVSQPRRNIVGCRIQHGWREGNGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELNKDDRVSALEVLPDRVATSRISDAHLADTMIGKAVEHMFETEDGSKDEWRGMVLARAPVMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS", "text": "FUNCTION: Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway. Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes. May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus. SIMILARITY: Belongs to the SPIN/STSY family."}
+{"protein": "MNLEYVQVVQKFNQVLLELTKKVCTVVGGSKPTYWYHHIRRVCSECPSMPMSMIGPYLNVYKAQILTKDKNFFMNFDPAHNEYTFIIQKLKEAARNMPEDELEQYWVKLLFLLKSYIKCKPFIN", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the asfivirus H124R family."}
+{"protein": "MGSLEVPCIDLSENDTSIVVKELLDACKNWGFVSLKNHGIPLDEIDRTFKLADKFFDIPVEEKQKYLFKGGRLHSGYTGHFGEKLDMEHQSRGDLKESYDLAGFPDPKLENLCPFIAEHMDEFLQFQRHCYKLTLRLLDFFAIGFGIPPDFFSKSHSSEEDVLRLLKYSIPEGVERREDDEDAGAHSDYGSITLLFQRDAAGLEIRPPNFVKDMDWIKVNVQPDVVLVNIADMLQFWTSGKLRSTVHRVRIDPGVKTRQTIAYFVTPDPETPLSPLFEEKTGKDIETVTAGEWIDGRINFTYGYSAPPKGYLGSQNDGIVA", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the UPF0676 family."}
+{"protein": "MPSRIPLPAFCCFLLPWAFTSFHKALGNPAPHPGPHYLLPPIHEVIHSRRGATATLPCVLGTSPPSYKVRWSKVEPGELRETLILITNGLHARDYGLLGGRASLRRGHRLDASLIIKNVRLEDEGRYRCELINGIEDESVALTLRLEGVVFPYQPSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGHGRPGIRSYGPRDRSRDRYDAFCFTSALAGQVFFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPDPGVRSFGFPRPQQASYGTYCYAEK", "text": "FUNCTION: Mediates a firm binding of versican V2 to hyaluronic acid. May play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS) which facilitates neuronal conduction and general structural stabilization. Binds to hyaluronic acid. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the HAPLN family."}
+{"protein": "MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPQRADDARQLFALSCAAEEQGMLPEDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITQSPLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF", "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. SUBCELLULAR LOCATION: Cytoplasm Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Membrane; Lipid-anchor Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody (By similarity). SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily."}
+{"protein": "MNPVVCAFGVIFVVVTLELVVAHPGKDVLGCHNGTSITVDECCAIPMLANKTVIEKCKAAHPFKPPQNTDDKGPRGHPGECIAECIMKGMGALKNEKVDGPAFRKAIEPVVKANPAFAKLLDDTVKQCHESINVDSEFTRYVTKPVCKADAKAFINCVYGTLFEQCPTNVWTQKDGCTQLKDKIKKGCAYFALRKHGGRRMRPT", "text": "FUNCTION: Present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the PBP/GOBP family."}
+{"protein": "MADSSESFNIATSPRAGSRRDALTSSPGRDLPPFEDESEGMFGDGVVPEEEEDGEELIGDAMERDYRPISELDRYEVEGLDDEEDVEDLTASQREAAEQSMRMRDREMGRELGRMRRGLLYDSDEEEEDRPARKRRMAERAAEGAPEEDEEMIESIENLEDMKGHTVREWVSMAATRLEIYHRFKNFLRTHVDEHGHNVFKEKISDMCKENKESLPVNYEDLAAREHVLAYFLPEAPAEMLKIFDEAAKEVVLVMYPKYDRIAREIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTCCTGVLPQLSMVKYNCNKCNFILGPFFQSQNQEVRPGSCPECQSFGPFEINMEETVYQNYQRITIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTANGFPVFATVILANHITKKDDKVAVGELTDEDVKAIVALSKDERIGERIFASIAPSIYGHEDIKRGLALALFGGEAKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYVEKVASRAVFTTGQGASAVGLTAYVQRHPVTKEWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAASNPIGGRYDPSLTFSENVDLTEPIVSRFDILCVVRDTVDPVQDEMLARFVVSSHIKHHPSSKDIANGDAAEFALPNTFGVEALPQEVLKKYIMYAKEKIRPKLNQMDQDKVAKMYSDLRKESMATGSIPITVRHIESMIRMAEAHARMHLRDYVVEDDVNMAIRVMLESFIDTQKFSVMRSMRKTFARYLAFRRDNNELLLFVLKQLIAEQVTYQRNRYGAQQDTIEVPEKDLVDKARQINIHNLSAFYDSDLFKMNKFTHDVKKKLIIQQF", "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. Required for the entry in S phase and for cell division. 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": "MYAVFQSGGKQHRVSEGQTVRLEKLDIATGETVEFAEVLMIANGEEVKIGVPFVDGGVIKAEVVAHGRGEKVKIVKFRRRKHYRKQQGHRQWFTDVKITGISA", "text": "FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
+{"protein": "MSGNTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQGIPLITGRFDSLEQLNEFSRSF", "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": "MDPCKFRPSSSFDTKTTTTNAGAPVWNDNEALTVGPRGPILLEDYHLIEKVAHFARERIPERVVHARGASAKGFFECTHDVTDITCADFLRSPGAQTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHHPESLHTFFFLFDDVGIPTDYRHMDGFGVNTYTFVTRDAKARYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIAAGNFPEWKLFVQVIDPEEEERFDFDPLDDTKTWPEDEVPLRPVGRLVLNRNVDNFFNENEQLAFGPGLVVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCAHHNNHYDGAMNFMHRDEEVDYYPSRHAPLRHAPPTPITPRPVVGRRQKATIHKQNDFKQPGERYRSWAPDRQERFIRRFAGELAHPKVSPELRAIWVNYLSQCDESLGVKIANRLNVKPSM", "text": "FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity). Involved in environmental stress response. Promotes drought stress tolerance and recovery (Ref.10). FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. SUBCELLULAR LOCATION: Peroxisome Glyoxysome. SUBCELLULAR LOCATION: Cytoplasm Cell membrane. SIMILARITY: Belongs to the catalase family."}
+{"protein": "MSIPANTIQKDKMMHSDYYTQSQGPTVEQQPEWQASVQPYSDPHAYSPSFYMNMSQVPHFLPAQVDPFIYPNTLGSYGGDKQVQCLWETNGQVCMHVCQNSGELSTHISSNHITHDSKFVCLWKGCDREFKMFKAKYKLVNHMRVHTGERPFLCDVCNKVFARSENLKIHKRIHSGEKPFQCTHNGCTKLFANSSDRKKHMHVHSSHKPYSCMYPDCGKTYTHPSSLRKHTKVHENEKKSQLSPEHDESSDSGNASIGTPTTDESLTFSPENIKRDQHLHTMHTFMDRPNPFMQMYQNQFSNPTYHMFMAKPDSY", "text": "FUNCTION: Transcription factor (PubMed:26073017). Modulates expression of target genes by binding to regulatory elements (PubMed:26073017). Required for normal cell division timing and cell positioning in anterior lineages, acting in a cell-autonomous manner (PubMed:35660370). Required for development, fusion and fate of cells of the ventral epidermis, the Pn.p cells, during larval development; acts in concert with homeobox genes lin-39 and mab-5 (PubMed:12091304). Required for the specification of the AIY interneuron (PubMed:19386265). In complex with TCF transcription factor pop-1, positively modulates expression of LIM/homeobox protein ttx-3 in anterior daughter cells of the SMDD/AIY neuron lineage (PubMed:19386265, PubMed:26073017). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localized to nucleus during interphase in cells giving rise to SMDD/AIY neurons, then in cytoplasm just before cell cleavage."}
+{"protein": "MALSLFTVGQLIFLFWTLRITEANPDPAAKAAPAAVADPAAAAAAAVADTASDAAAAAAATAAAAAKAAADTAAAAAKAAADTAAAAAEAAAATARG", "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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-I AFP family."}
+{"protein": "MAEEKHHHHLFHHKKDDEPATGVDSYGEGVYTSETVTTEVVAGGQDEYERYKKEEKQHKHKQHLGEAGALAAGAFALYEKHEAKKDPENAHRHKITEEIAATAAVGAGGYAFHEHHEKKKDHKSAEESTGEKKHHLFG", "text": "FUNCTION: Involved in tolerance to aluminum. Regulates the expression of different genes that collectively contribute to the protection of the cell in response to aluminum stress. FUNCTION: May function in gibberellin signaling pathway downstream of GID1 and SLR1. May be involved in the regulation of plant growth in the basal region of leaf sheaths (Probable). Involved in tolerance to aluminum (PubMed:22676236, PubMed:24253199). Regulates the expression of different genes that collectively contribute to the protection of the cell in response to aluminum stress (PubMed:22676236, PubMed:24253199). Binds to the promoter and regulates the expression of target genes involved in aluminum stress response. Binds to the promoter of STAR1 gene, which encodes an ABC transporter required for aluminum tolerance (PubMed:24253199). Involved in drought tolerance. Plays a positive role in response to drought stress response by regulating abscisic acid (ABA) biosynthesis, promoting stomatal closure, and acting as chaperone-like protein that possibly prevents drought stress-related proteins from inactivation (PubMed:27420922). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the abscisic acid and water stress-induced protein family."}
+{"protein": "MNTSIKSIKKQDLKDRIVFTLFLIVMSRLGTFLPIPGVDHDAFYQSIISNPLVNFLNVFSGGGFASIGVFALGIVPYINASIIVQLATNSIPSLEKLQKEEGELGRQKIVQLTRYVALVWALIQSIGVSFWVRPYVFNWDLNFVFAMSLTLTIGSMLIMWFSEQITEKGIGNGPSLLIFINIISGLPKLLQSQIQSTRLNIQALDIFVLVFIFSVMIIGIIFIQEGIKRIPIISARQLGKGQMDNKTSYLPLKLNQSGVMPIIFASAVLVLPAYLAQLVSNEQLRTVLHLFDGTSNNKLLYLLFYFTLILFFSYFYTSLILNPNDVSKNLKKMESSIYGVRPGKATTEYLQKTLNRLTFLGALFLAFIAIVPNIIETLTNLSVFKGLGGTSLLIIVGVQVDTSKQIQTYLISKNYETIVR", "text": "FUNCTION: The central subunit of the protein translocation channel SecYE. 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 (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecY/SEC61-alpha family."}
+{"protein": "MDIENWDTIDQLMADSAQPDFEDWGDLGDLMPDVLPESNGSSSGTATDNDNRCWDHGCNGKKFLNHSNLVRHRRENGSARPRFTCPMCGAYFSRSTARNQHLEKKSCNRVRRYSNGRERPRPRVKD", "text": "FUNCTION: Transcription factor that probably regulates the expression 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). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family."}
+{"protein": "MSSASSSSAASLLLGREVDVFLSFCCQTSHGYFQNILIRNGIRTFLSYRCLEKRFGPIGQRTLKALEESRVAVVMTSTTKPCSVGFLEELLVILEFQEKGSLMVIPIFLTDLSFNVEEICRQHPEKAPSWRTALTKLTNLAAEYPLSQNLAGMDQSDLLNQIARDISLVVFYSGSNDSNALVAMDRHMKVVYDLLALEVNKEVRTIGIWGSAGVGKTTLARYIYAEIFVNFQTHVFLDNVENMKDKLLKFEGEEDPTVIISSYHDGHEITEARRKHRKILLIADDVNNMEQGKWIIEYANWFAPGSRVILISQNKNLLVDAGVMDVYEVRSLRYDEALQVFSHFAFKQPYPPSDFEELAVRAVHLAGFLPLGLRLLGSFLAGKGREEWVAALLKLKAKQGGHIMEVWKLMEATDDKGLEEWETAADIVERKESSQDKSQQESEVAADILIGKESSQDKQ", "text": "FUNCTION: Confers resistance to low temperatures by limiting chloroplast damage and cell death, thus maintaining growth homeostasis. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MSQVEISELAKEIRASLKQFPNFPSEGILFEDFLPVFTKPDLFQKLVRAFQLHVGEQKVDYVVGLESRGFLFGPTLALALGAGFVPVRKAGKLPGPVFTAEFQKEYGSDKFQIQKDVIEEGAKVLIVDDILATGGSASSAGELVKQTGGDIVEYLFVMELDFLNGRDKLDKPAFTLLSGQAEKLQN", "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": "SGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMKLNSRGKLVQVNSRFNAPTIHDLVYIDPSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQRERCHCKF", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. Required during embryogenesis for extension of the primary anterior-posterior axis. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
+{"protein": "MKFFAFSMLIGEASPIVLALRRTTLEVRQLDPIIRSELEQGSSSSCPKAILIFARGSTEIGNMGVSAGPAVASALEAYGADQIWVQGVGGPYTADLPSNFLPGGTSQSAINEAVRLFNEANTKCPSTPIVAGGYSQGTAVMAGAIPKLDAVRARVVGTVLFGYTQNQQNNKGIKDYPQEDLQVYCEVGDLVCDGTLIITVSHFLYLEEAAGPAPEFLKSKIGA", "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). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family."}
+{"protein": "MTKLEDHLEGIINIFHQYSVRTGHYDTLSKCELKKLITTELVNTIKNTKDQATVDRIFRDLDEDGDHQVDFKEFLSLLASVLVTAHENIHKE", "text": "FUNCTION: S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF- kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm Cytoplasm, cytoskeleton Cell membrane; Peripheral membrane protein Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation is secreted via a microtubule- mediated, alternative pathway (By similarity). SIMILARITY: Belongs to the S-100 family."}
+{"protein": "MALLLTLTSPDLEGTWDTRDKDGFKAQEGPPLAVPEFPVCGLYRIYGVCGSFSSFFIIRCSLCALETLKSPQHDPLEIPEQSLKLIPLVSGKRELTRGQKAGEKPLAAGPGEEELLRGSAPHAQDTQSEELPPSCTISGEKKPPAVSGEATGADAGRLCPPPRSRAPHKDRTLARSRPQTQGEDCSLPVGEVKIGKRSYSPAPGKQKKPNAMGLAPTSSPGAPNSARATHNPVPCGSGRGPCHLANLLSTLAQSNQNRDHKQGPPEVTCQIRKKTRTLYRSDQLEELEKIFQEDHYPDSDKRREIAQTVGVTPQRIMVKGAGSLVAGWSGGGPTIETLELQSERSAVAWVWFQNRRAKWRKMEKLNGKESKDNPAAPGPASSQCSSAAEILPAVPMEPKPDPFPQESPLDTFPEPPMLLTSDQTLAPTQPSEGAQRVVTPPLFSPPPVRRADLPFPLGPVHTPQLMPLLMDVAGSDSSHKDGPCGSWGTSITLPPPCSYLEELEPQDYQQSNQPGPFQFSQAPQPPLFQSPQPKLPYLPTFPFSMPSSLTLPPPEDSLFMFPCGPSGGTSQGYCPGASSGQILMQPPAGNIGTASWSDPCLPELPFPGPFCPQALGHPPGGDGYFPDLFPTPCPQALGRQPSSALSWMPEGARPGTGPLLSKAKEEPPAASLDQPSALEEARGDDKNSHVP", "text": "FUNCTION: Transcription factor which may play a role in oogenesis. Binds preferentially to the DNA sequences 5'-TAATTG-3', 5'-TAGTTG-3' and 5'-TAATTA-3'. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MKFKLNLITLALLANTGFAIAADGYGLANANTEKVKMSAWSCKGCVVETGTSGTVGVGVGYNSEEDIRSANAFGTSNEVAGKLDADVTFRGEKGYRASVEAYQLGMDGGRLEVNAGKQGQYNVNVNYRQIATYNSNSALTPYSGVGSDNLTLPDNWVTAGSSSQMPLLMDSLNSLELSLKRERTGLGFDYQGESLWSTHVSYMREEKTGLKKASGGFFNQSMMLAEPVDYTTDSIEAGIKLKGDNWFTALNYNGSIFKNEYNQLNFDSAFNPTFGAQTSGSIALDPDNQSHTVSLMGQYNDSTNVLSARLLTGQMSQDQALVTSGYGYQVPTEALDAKVDLIGLNLKVVSKVTNSLRLSGSYDYNDRDNNTQIEEWTQVSINNVNGKVAYNTPYDNTSQRFKVAADYRITRGMKLDGGYDFRRDERNYQDRETTDENTVWARFRVNSFETWDMWVKGSYGQRDGSEYQASEWTSSETNSLLRKYNLANRDRTQVEARVTHSPIESLTIDFGARYALDDYTDTVIGLTESKDTSYDANISYMITDDLLANAFYNYQIIESEQAGSSNYSTPTWTGFIEDKVDVVGAGISYNNLLENKLRMGLDYTYSDSNSNTQVRQGITGDYGDYFAKVHNINLYAQYQATEKMALRFDYKIENYKDNDAANDIAVNGIWNVVGFGDNSHDYTAQMIMLSMSYKI", "text": "SUBCELLULAR LOCATION: Cell outer membrane."}
+{"protein": "MSDNTLVSDYGMCEEEQVARIAWFYYHDGLTQSEISERLGLTRLKVSRLLEKGHQSGIIRVQINSRFEGCLEYENALRNHFALQNIRVLPALPDADIGLRLGIGAAHMLMESLRPQQLLAVGFGEATMTTLKRLSGFISAQQIRLVTLSGGVGPYMTGIGQLDAACSVSIMPAPLRASSQEIACTLRNENSVRDVMLTAQAADAAIVGIGAINQKDQASILKSGYITQGEQLMIGRKGAVGDILGYFFDAHGEIIPDIKIHNELIGLKLNSLSTIPTVIGVAGGEQKAEAIIAAMRGNYINALVTDQKTAGKIIQLIEK", "text": "FUNCTION: In the absence of autoinducer 2 (AI-2), represses transcription of the lsrACDBFGE operon and its own transcription. In the presence of AI-2, LsrR is inactivated by binding phospho-AI-2, leading to the transcription of the lsr genes (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SorC transcriptional regulatory family."}
+{"protein": "MQVDKTSFTPLYKQLFFIICQQIQNGSLPLGSQLPTQKEIARSYNVSLIVVKQAWSELINAGIISSQRGSGSVVCSVPEGVSYGHTFRGITRDLQDASVAIENRILEIAPRRARDAQADGLSLPAQHHYLYISRIRCLNNRPFNHEKIYLDLSFFPGLELTPQALEHTSLYSLLNVTSDSAIEKVEAILPSADLCEKLQIAANKPLLSVARQTFQAGKDSPFEYCRYYVLSEYFGEIHYH", "text": "FUNCTION: Represses the expression of the STM4065-STM4067 operon."}
+{"protein": "MKWGRLLAFLAMVVVVLGLTISTGPKIWKSIPLGLDLKGGVDLLYAVDTPKGHPLDSTGKAALVRAIEMRVNSLGVSSPIIQLEGRNQLGQDQIRVEVAGVKNQQEAVSVIGATAQLAIYGSAKIDPKTGKIVPVGPPLATGADLKSNAHWVVDQQTGQNAVAIEFKNASLWTSITKRYLQKPIYVFLNGQLLTNPVVEQVMYTGQSEISGGNLTTPQACIDLANELNAGALPYPLTLESETSVGPTLGATSLHRTLIAGVIAVVLIFAFMIAAYRMAGLIADIALVAYGYLTLLTFAGLHVVLTLSGLAALILGVGIAVDANIITYERIKDEVRNGRSLRSAVRIGNKNAFRTIVDSNATTFIAGLIMYIFGGEGDVRGFAVALMVGIIVSLLTAVLFARAMLLTFTAAQAVKNPWWYGAPRGVVKSREAKV", "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. SecD subfamily."}
+{"protein": "MKVDLGPDPSLVYRPDVDPEMAKSKGSFRNYTSGPLLDRVFTTYKLMHTHQTVDFVMRKRIQFGSFSYKKMTVMEAVDMLDDLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKILALWGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPRYSTELGMYQPHCGLENVLMSWGHDEYLYQMMKFNKFSLPSEAFYMVRFHSFYPWHTGGDYRQLCSQQDLDMLPWVQEFNKFDLYTKCPDLPEVKSLRPYYQGLIDKYCPGILSW", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the myo-inositol oxygenase family."}
+{"protein": "MKTVILFGFLLALLGYLEAEHAQSDPEFTAKARQMLAVFGNSEVDRYTKSRNLPALIEFYEKYSSRLPLTVQDRTYANNVIRRYRAHNNQQVDGVPAQGGVGVVFALLLPFAVSIVEGIAKAIRE", "text": "FUNCTION: A humoral factor that may play a role in stress tolerance. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Turandot family."}
+{"protein": "MIGNSVYISPSPSPSDHSLSPNPNLCISAMEEQLVVDDDDDDLAPPPIPDLDIDLEDDDDACCHGLLHIAPNHEEETGCDENAFANEKCLMAPPPTPGMEFESYDDAYSFYNSYARELGFAIRVKSSWTKRNSKEKRGAVLCCNCQGFKLLKDAHSRRKETRTGCQAMIRLRLIHFDRWKVDQVKLDHNHSFDPQRAHNSKSHKKSSSSASPATKTNPEPPPHVQVRTIKLYRTLALDTPPALGTSLSSGETSDLSLDHFQSSRRLELRGGFRALQDFFFQIQLSSPNFLYLMDLADDGSLRNVFWIDARARAAYSHFGDVLLFDTTCLSNAYELPLVAFVGINHHGDTILLGCGLLADQSFETYVWLFRAWLTCMLGRPPQIFITEQCKAMRTAVSEVFPRAHHRLSLTHVLHNICQSVVQLQDSDLFPMALNRVVYGCLKVEEFETAWEEMIIRFGMTNNETIRDMFQDRELWAPVYLKDTFLAGALTFPLGNVAAPFIFSGYVHENTSLREFLEGYESFLDKKYTREALCDSESLKLIPKLKTTHPYESQMAKVFTMEIFRRFQDEVSAMSSCFGVTQVHSNGSASSYVVKEREGDKVRDFEVIYETSAAAQVRCFCVCGGFSFNGYQCRHVLLLLSHNGLQEVPPQYILQRWRKDVKRLYVAEFGSGRVDIMNPDQWYEHLHRRAMQVVEQGMRSKEHCRAAWEAFRECANKVQFVTEKPS", "text": "FUNCTION: Putative transcription activator involved in regulating light control of development. May have a role in controlling flowering time. SUBCELLULAR LOCATION: Nucleus Note=The nuclear localization is independent of the light treatment. SIMILARITY: Belongs to the FHY3/FAR1 family."}
+{"protein": "MQDLQHVFPRLRSYILYLLALYVLGWGFTSYKAVFAGLILGTALSLYNLWNLVRKFEQFGQALDEGKKPRSIGTVVRFATAALAVVITISYPKTFHIISVVVGLMTYYVVIIIDLVVQNMRRR", "text": "FUNCTION: A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bacterial AtpI family."}
+{"protein": "MADAVNAQTPSLSEQYHLEKEVKQDTSAKPVEVKEVAPEVTTQAEEVKTEQAKEESPVEEAVSVVEEKSESAPESTEVASEAPAAAEDNAEETPAAAEENNDENASEEVAEETPDEIKLETAPADFRFPTTNQTRHCFTRYVEYHRCVAAKGDDAPECDKFAKFYRSLCPSEWVDRWNEQRENGTFPGPLP", "text": "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. This protein may be one of the heme-binding subunits of the oxidase. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B (TC 3.D.4.8) family."}
+{"protein": "MEMTEMTGVSLKRGALVVEDNDSGVPVEETKKQKLSECSLTKGQDGLQNDFLSISEDVPRPPDTVSTGKGGKNSEAQLEDEEEEEEDGLSEECEEEESESFADMMKHGLTEADVGITKFVSSHQGFSGILKERYSDFVVHEIGKDGRISHLNDLSIPVDEEDPSEDIFTVLTAEEKQRLEELQLFKNKETSVAIEVIEDTKEKRTIIHQAIKSLFPGLETKTEDREGKKYIVAYHAAGKKALANPRKHSWPKSRGSYCHFVLYKENKDTMDAINVLSKYLRVKPNIFSYMGTKDKRAITVQEIAVLKITAQRLAHLNKCLMNFKLGNFSYQKNPLKLGELQGNHFTVVLRNITGTDDQVQQAMNSLKEIGFINYYGMQRFGTTAVPTYQVGRAILQNSWTEVMDLILKPRSGAEKGYLVKCREEWAKTKDPTAALRKLPVKRCVEGQLLRGLSKYGMKNIVSAFGIIPRNNRLMYIHSYQSYVWNNMVSKRIEDYGLKPVPGDLVLKGATATYIEEDDVNNYSIHDVVMPLPGFDVIYPKHKIQEAYREMLTADNLDIDNMRHKIRDYSLSGAYRKIIIRPQNVSWEVVAYDDPKIPLFNTDVDNLEGKTPPVFASEGKYRALKMDFSLPPSTYATMAIREVLKMDTSIKNQTQLNTTWLR", "text": "FUNCTION: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs (PubMed:28073919, PubMed:29628141, PubMed:30778726, PubMed:31477916, PubMed:35051350, PubMed:34718722). Acts as a regulator of protein synthesis in embryonic stem cells by mediating pseudouridylation of RNA fragments derived from tRNAs (tRFs): pseudouridylated tRFs inhibit translation by targeting the translation initiation complex (PubMed:29628141). Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3' (PubMed:28073919, PubMed:31477916, PubMed:35051350). Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions (PubMed:35051350). Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing (PubMed:35051350). In addition to mRNAs and tRNAs, binds other types of RNAs, such as snRNAs, Y RNAs and vault RNAs, suggesting that it can catalyze pseudouridylation of many RNA types (PubMed:29628141). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the pseudouridine synthase TruD family."}
+{"protein": "MDKKVCVSILLAMLAIAALCRPMTELESARHGAQRKNSISDVSRRDLLASLTHEQKQLIMSQLLPELLSELSNAEDHLHPMRDRDYAGWMDFGRRSSEVTES", "text": "FUNCTION: May control digestion processes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family."}
+{"protein": "MRTLALLAAILLVALQAQAEHVSVSIDEVVDQQPPQAEDQDVAIYVKEHESSALEALGVKAGVVCACRRALCLPRERRAGFCRIRGRIHPLCCRR", "text": "FUNCTION: This peptide has antibiotic, anti-fungi and antiviral activity. It also inhibits corticotropin (ACTH) stimulated corticosterone production. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
+{"protein": "MRWLPLLLIFLLAYIEISIFIKVAAVLGVAVTLLLVVFSSCVGISLVRNQGMKTFVQMQQKLAAGESPAAEMVKSVSLVLAGFLLLIPGFFTDFLGLLLLLPPVQKSLTLKLMPHLSVYRPGGWTGGDAANGNTFDGEF", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0716 (FxsA) family."}
+{"protein": "MNRNDKQAYDRGTSLFSPDGRIYQVEYAREAVKRGAPVLGVRTADGVVLAALRSTPSELMEAESIEKLHKLDDALGAATAGHVADARKLVDFARTTAQREHLRYGEPIGVETLTKTITDNIQESTQSGGTRPYGASLLIGGVENGSGRLFATDPSGTPQEWKAVAIGGHREDVQAALEDGYAEDLSLEDGLALAVEALVAADEEIESDELNLVTVSEAGYEIVDEETIAELFADATADDESDETDEREE", "text": "FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta-alpha2 proteasome is able to cleave oligopeptides after Tyr and thus displays chymotrypsin-like activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase T1A family."}
+{"protein": "MASPGILEESSSGDVCSGGCPDQWEEKTEEELQCQFEQAAKHVQNVASVASTEQLLYLYARYKQVKVGRCNTPKPGFFDYEGKKKWEAWKALGDYSHQQAMTEYIETVKKLDPDWSPQALEEPYKEPKTTFGGPVVSCLYKVQETLREEDKDIFDYCRENNHSRVSHALSTGSVDVNVADDEGRSLLHWACDRGHTQLVSVILFHNAHINMQDSEGQTPLHYASACEFPDIVDLLLDHGADPSLVDNDGFQPHEVTDSKTIAAMLQQHASNGEHNKPPSLLLEMPQ", "text": "FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA. Does not bind fatty acids (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNESNKVNGN", "text": "FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the glycogen phosphorylase family."}
+{"protein": "MKRKTKLDKKSKWVLDMKFGVSSLVFLPESLTSSMEKIAEHNFDAWEIVCEGTHYLSPKNIKYLMELRDRYEVEIVVHAPFSDLNPASMNERVRKLTVECIRDAIEGAFELDSEVVVVHPGYIPELWSNYVSEILDNNFSTLSEIVEIAEDYGIKIGLENMPNFRGVLGITPESLLEIVKDIDSKNLGITFDIGHANTAGNPAEFVEKLQNIGIGIIHVHAHDNNGYDDEHLKIGEGNINFIEVLEKLKEIGYDGVISIENKNIRDAVKSKEILKEYLEIVNEKVAEKEKIEE", "text": "SIMILARITY: To M.jannaschii MJ1614 and MJ0008."}
+{"protein": "MTPRIESEESAPLVNKNNNNNNDNNNNNNVDEENPLIIESGIPIEDLEQKNKPYLIKVPNIDKPDSKWINFKTLWAFTGPGFLMSIAYLDPGNLESDIQAGAMAGYQLLWVLFWSTVIGFWLQMLASRLGVVTGKHLAEHCREQYPKTPRLLLWLMTELAIIGSDIQEVIGTAIALQILSNGHIPLWAGVLFTAADTFTFLFLEKYGIRKLEAFFCSLIAIMAISFGVEYIISKPDQIEVVKGVFIPLCSQNNISQAVGILGAVVMPHNIYLHSALVQSREIDRKSETQVKIANKYNRLESAFALIISFIINLLLVSVFAKGFYGETTEIGLSSAADFLMDKYGKVAKYIWAIGLFSAGQCSTMTGTYSGQFVMEGFLKLKIAPWKRLLITRCTAIVPAMVVAILSTSHLDSLDQWLNILQSIQLPFAVVPVLLFTSSEKIMGSKFKNHWLNNQFVRFLSLLIIAINIYLIITFSMQISESAWMISIVSISFFFYFIFIVYLSMGQENFNSMTKKIKNLFNNNSNQTYNNINY", "text": "FUNCTION: Depletes iron from the phagolysosome in an ATP-dependent process. May rather act as a symporter of protons and metal cations in an ATP-dependent process. Nramp1 overexpression protected cells from L.pneumophila infection. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Note=Located at vesicles of variable size, which are distributed all over the cytoplasm, in part clustered at a perinuclear site. Several tiny vesicles travel rapidly outward from and towards the perinuclear cluster. These vesicles are part of the endo- and phagolysosomal pathway. SIMILARITY: Belongs to the NRAMP family."}
+{"protein": "MNLVMLILALWAPVAGSMPELSLTLFDEPPPLVETEPLPPLSDVSEYRVEYSEARCVLRSGGRLEALWTLRGNLSVPTPTPRVYYQTLEGYADRVPTPVEDVSESLVAKRYWLRDYRVPQRTKLVLFYFSPCHQCQTYYVECEPRCLVPWVPLWSSLEDIERLLFEDRRLMAYYALTIKSAQYTLMMVAVIQVFWGLYVKGWLHRHFPWMFSDQW", "text": "FUNCTION: Participates in the inhibition of the host immune response. Redirects newly synthesized major histocompatibility complex (MHC) class I heavy chains via the SEC61 translocon to the cytosol where they undergo proteasome-dependent destruction. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes. SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the cytomegalovirus US6 family."}
+{"protein": "MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKVVCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGNEITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPLVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQGSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE", "text": "FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin- sensitive, G(i/o)-alpha family of G proteins but also to the Gq family (PubMed:12496283, PubMed:12711604, PubMed:23589301). Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine. May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake. Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes. In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines. May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils. In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin-8/IL-8 in response to the presence of microbes (PubMed:21037097). Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably acetate, propionate and butyrate (PubMed:12496283, PubMed:12711604). Exhibits a SCFA- independent constitutive G protein-coupled receptor activity (PubMed:23066016). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MPSFTYLTAALALTSSVVASPVEKRDAFEVKQVAHGLHRKNGPAQIAKTLRKYGKAVPAHIQAAADNNAVVQADANTGSDPAVPSDQYDSSYLSPVTVGTSTVHLDFDTGSADLWVFSDLQAKSSLSGHDYYKTDASKRKSGYTWKISYGDGSGASGQVYTDKVTVGQVTATAQAVEAATSVSAQFSQDVDTDGLLGLAMSSINTVKPQQQTTWFDTVKSQLAKPLFAVTLKYHAAGTYDFGYIDSAKYTGAITYVNADASQGFWGFTASGYSVGTGATVSSSISGILDTGTTLMYVPAATAKAYYAKVSGAKLDSTQGGYVFPCSATLPNFSITVAGVKQTVPGKYINYAPITDGSSTCFGGMQPDTDIGQSIFGDIFLKSKYIVHDMSNGTPRLGFAQQAGVSS", "text": "FUNCTION: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MHRASHHELRAMFRALLDSSRCYHTASVFDPMSARIAADLGFECGILGGSVASLQVLAAPDFALITLSEFVEQATRIGRVARLPVIADADHGYGNALNVMRTVVELERAGIAALTIEDTLLPAQFGRKSTDLICVEEGVGKIRAALEARVDPALTIIARTNAELIDVDAVIQRTLAYQEAGADGICLVGVRDFAHLEAIAEHLHIPLMLVTYGNPQLRDDARLARLGVRVVVNGHAAYFAAIKATYDCLREERGAVASDLTASELSKKYTFPEEYQAWARDYMEVKE", "text": "FUNCTION: Catalyzes the decarboxylation of oxaloacetate into pyruvate. Seems to play a role in maintaining cellular concentrations of bicarbonate and pyruvate. FUNCTION: Catalyzes the decarboxylation of oxaloacetate into pyruvate with high efficiency. Is also able to decarboxylate 3- methyloxaloacetate. Seems to play a role in maintaining cellular concentrations of bicarbonate and pyruvate. SIMILARITY: Belongs to the isocitrate lyase family. Oxaloacetate decarboxylase subfamily. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. Oxaloacetate decarboxylase family."}
+{"protein": "MPPQQGDPAFPGRCEAPPVPPRRERGVRGPGAPGGRGRAGGPEGHGVKCVLVGDGAVGKTSLVVSYTTNGYPTEYIPTAFDNFSAVVSVDGRPVKLQLCDTAGQDEFDKLRPLCYTNADIFLLCFSVVGPSSFQNVSEKWVPEIRCHCPKAPIILVGTQSDLREDVKVLIELDKCKEKPVPEEAARLCAEEIKATSYIECSALTQKNLKEVFDAAIVAGIQYSDSQQQPKKSKSRTPDKMKTLSKSWWKKYCCFV", "text": "FUNCTION: Acts upstream of PAK1 to regulate the actin cytoskeleton, adhesion turnover and increase cell migration. Stimulates quiescent cells to reenter the cell cycle. Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP-bound. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Golgi apparatus membrane; Lipid-anchor Cell junction, focal adhesion Cell projection, podosome Note=Localizes to podosomes in SRC- transformed cells. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
+{"protein": "MDTNSPKSIDKDANSTEVDAAEQDAASVKINSTRASPNGSDLLNDDSEAAKITTNEKQSSPVDSHNESPNDTTINKGEDGNENEVDNVNNNDKKEDEDNVEENEEEADANEEEEEDEEDDEEDEEDEDESGGGRRKRARHDRRNQFLDIEAEVDEDEEELEDEEDEIGREDGFIEEEVGADYVGDDRRHRELDRQRQELQSVDAERLAEEYREKYGRSQTVVGDTSNVPQRLLLPSVNDPNIWAVRCKIGKEKDIVFTIMRKAMDLQYTSSPLEIISAFQRDSLVGYIYVEARKQSHVLDALNGVLNVYTNNMILVPIKEMPDLLKVQKQVVELLPGAYVRIRRGKYAGDLAQVDNLSENGLTARVRIVPRIDYSDGLKRKNSATRPQARLFNESEAFKSNPSKFSKRGPRLFLFNNEEFEDGFLVKDIRISSLITEGVNPTLDEVSKFNPNNEDLDLSSLALSVKGGHAEFQPGDHVEVYVGEQTGVSGVVENVRGSVITMVSSDGLRLDVPSRGLRKRFRHGDYVKVIAGKYKDDTGMVVRISKDEVTFLSDTLMTELTVFSRDLGEASSAQAVNSAYELHDLVQLDVNTVACIFSVDRDTYKVIDQNGGVRTVLASQITMRHSNRRGVATDRNGAEIRIGDKVKEVGGEGKQGTILHIYRAFVFLHNRDIAENNGVFSARSRNVATIAAKGARISADLTKMNPALSNGPALPPVANLKRTIGRDKAIGATVRIRRGPMKGLLGVIKDTTDANARVELHTGNKMVTIPKENLLYTTKTGELISYTEFIERSRGIRPGSISTADGPNVPNWAQGARTPAVANGSRTPAWNTGSRTPAWNSGSKTPAWNSGSRTPAWNSGNKTPAWNAGSRTPAWNSGNKTPAWNVGNKTPAWNSGAKTPAWNAGNKTPSWNNGTKTPAWNANQTPMVANGTNTSWGQTPAYGGFSETNWDTEDNSKPYTAPTPGAWAAPTPGGWDDEEGDSPKYVPPSP", "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. SIMILARITY: Belongs to the SPT5 family."}
+{"protein": "MEIVQEGIAKIIVPEIPKTVSSDMPVFYNPRMRVNRDLAVLGLEYLCKKLGRPVKVADPLSASGIRAIRFLLETSCVEKAYANDISSKAIEIMKENFKLNNIPEDRYEIHGMEANFFLRKEWGFGFDYVDLDPFGTPVPFIESVALSMKRGGILSLTATDTAPLSGTYPKTCMRRYMARPLRNEFKHEVGIRILIKKVIELAAQYDIAMIPIFAYSHLHYFKLFFVKERGVEKVDKLIEQFGYIQYCFNCMNREVVTDLYKFKEKCPHCGSKFHIGGPLWIGKLWDEEFTNFLYEEAQKREEIEKETKRILKLIKEESQLQTVGFYVLSKLAEKVKLPAQPPIRIAVKFFNGVRTHFVGDGFRTNLSFEEVMKKMEELKEKQKEFLEKKKQG", "text": "FUNCTION: Dimethylates the guanine residues at position 26 and 27 of one or more 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": "MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARAGVYNLTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQKIPAKRIGVPEEVSSVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPDHDNWPKGAGDLSVVKKMKETFKEKAKL", "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": "MAGERRDSKAAAFFCLAWALCLALPGFPQHVGGREDRADWTQEKYSHRPTILNATSILQVTSQTNVNRMWQNDLHPILIERYPGSPGSYAVRQHIKHRLQGLQAGWLVEEDTFQSHTPYGYRTFSNIISTLNPLAKRHLVVACHYDSKYFLPQLDGKVFVGATDSAVPCAMMLELARSLDRQLSFLKQSSLPPKADLSLKLIFFDGEEAFVRWSPSDSLYGSRSLAQKMASTPHPPGARNTNQIQGIDLFVLLDLIGARNPVFPVYFLNTARWFGRLEAIEQSLHDLGLLNNYSSERQYFRSNLRRYPVEDDHIPFLRRGVPILHLIPSPFPRVWHTMEDNEENLDKPTIDNISKILQVFVLEYLNLG", "text": "FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N- terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glutaminyl-peptide cyclotransferase family."}
+{"protein": "MTSHPVFIDLSLDEQVQELRKYFKKLGAEISSEKSNKGVEDDLHKIIGVCDVCFKDGEPSQIDGILNSIVSIMITIPLDRGENIVLAYCEKMTKAPNLPLGKVCLQSLWRLFNNLDTASPLRYHVYYHLVQVAKQCEQVLEVFSGVDQLKSQFANCPPSSEQMQKLYRLLHDVTKDTNLELSSKVMIELLGTYTADNACVAREDAMKCIVTALADPNTFLLDPLLSLKPVRFLEGDLIHDLLSIFVSEKLPAYVQFYEDHREFVNSQGLNHEQNMKKMRLLTFMQLAESSPEMTFETLTKELQINEDEVEPFVIEVLKTKLVRARLDQANQKVHISSTMHRTFGAPQWEQLRDLLQAWKENLSTVREGLTSVSSAQLDLARSQKLIH", "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 (Potential). 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 Golgi apparatus. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus. SIMILARITY: Belongs to the eIF-3 subunit M family."}
+{"protein": "MFCCLGYEWLSGGCKTWHSAWVINTLADHHHRGTDFGGSPWLRIIIAFPRSYKVVLTLWTVYLWLSFLKTIFQSENGHDVSTDVQQRARRSNRRRQEGLRSICMHTKKRVSSFPGNKIGLKDVITLRRHVETKGRAKIRKMKVTTKINHHDKINGKRKTAKKQKLSVKECEHAEKERQVSEAEENGKLDMKEIHTYMKMFQRAQELRRRAEDYHKCKIPPSARKALCNWVRMAAAEHRHSSGLPYWPYLTAETLKNRMGHQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSADDNLKTPPECLLTPLPPSAPPSADDNLKTPPLATQEAEAEKPPKPKRWRAAEMESPPEPKRRRAAEVESPPEPKRRRAAEVEPSSPEPKRRRLSKLRTGHCTQA", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NPIP family."}
+{"protein": "MNVPWENAHGGALYCLIRGDEFSAWHRLLFQRPGCAESVLACRHFLDGSPVARCSYPEEYHPCVISRIALLCDSVGWTADVERISAWLNGLDRETYELVFAAIEVLEEEGPALGCPLVDTVRGSRHKNMKELRPGSQGRSEVRILFAFDPARQAIMLAAGNKAGRWTQWYDEKIKAADEMFAEHLAQFEDTKPKRRKRKKG", "text": "FUNCTION: Putative toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin would be HigA2. SIMILARITY: Belongs to the mycobacterial HigB family."}
+{"protein": "MERPLTVLQVSLYHPTQGPVAFAKVPLQLQHDASRLLVGRGQDTHLQLQLPQLSRHHLCLEPYLEKGSNLLAFCLKVLTRQSCVWVNGLPLRYLEQVPLHSVNRISFSGIQMLIRKEGGASLEAFVCYFHLSPSPLIYRPKAQETDE", "text": "FUNCTION: Inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA."}
+{"protein": "MQRDTERAAQLSPSSEDEALVLRQKPLEMPAQEEDSTTLQQWKARQLQRLAEELKAEWQEARLQQVRQAERLYLSHLLDEAAERSMGNDPSVHEQNQRRTAKHTRAKERNRAAFREERGRREEHPRQHPKSRKKAPCSERRSSAKARGPASGEKGKRRRVSSSKDHDGYQGPRVTRRVGVAKLNPFFDGDTDCMEDVQKEFFREGRRPSAKGTHNLRDQSLQGKTTALTQPLLHGPTCKQEAAAQEPPSKYNKNLWHKEIESTFEELFNMNRKLKKHLNLHLEQRLKADQNPDEQQSYSEIRSETFGTPREERTEEVETAEESGSPTEVETTEMWSKVNLKQILSDSEYPRYQQIAKYPLKSESLVPVKAGTSREQDDLLSLSPESGQEPPKSPLLEDESLKPYLQKQADSVASWMALRQKQKAELEQRRQKALLELTEHPNMSLEIHYKAELEEERRARRRMRLALLKSNSTGICALPPDRNNLSLDNGLLDEDKQNQMIRDLQQQILEQNKLHQEFLEKARKRLQEFQKSF", "text": "SUBCELLULAR LOCATION: Cell projection, cilium Note=Colocalizes to the motile cilium of mature spermatozoa."}
+{"protein": "MSLKDRFDRFIDYFTEDEDSSLPYEKRDEPVFTSVNSSQEPALPMNQPSQSAGTKENNITRLHARQQELANQSQRATDKVIIDVRYPRKYEDATEIVDLLAGNESILIDFQYMTEVQARRCLDYLDGACHVLAGNLKKVASTMYLLTPVNVIVNVEDIRLPDEDQQGEFGFDMKRNRVR", "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. 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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to the division site, in a FtsZ-dependent manner. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to the division site, in a FtsZ-dependent manner. SIMILARITY: Belongs to the SepF family. SIMILARITY: Belongs to the SepF family."}
+{"protein": "MEVKDANAALLSNYEVFQLLTDLKEQRKESGKNKHSAGQQNLNAITYETLKYISKTPCRNQSPAIVQEFLTAMKSHKLTKAEKLQLLNHRPMTAVEIQLMVEESEERLTEEQIEALLHTVTSILPAGPEDEQSKSTSNDVAMEEEEPA", "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. 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). FUNCTION: Accessory protein for the calcitonin gene-related peptide (CGRP) receptor. It modulates CGRP responsiveness in a variety of tissues. SUBCELLULAR LOCATION: Nucleus Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the eukaryotic RPC9 RNA polymerase subunit family."}
+{"protein": "MDYSSMHQNVMGVSSCSTQDYQNQKKPLSATRPAPPEQSLRCPRCDSTNTKFCYYNNYSLSQPRYFCKSCRRYWTKGGILRNIPIGGAYRKHKRSSSATKSLRTTPEPTMTHDGKSFPTASFGYNNNNISNEQMELGLAYALLNKQPLGVSSHLGFGSSQSPMAMDGVYGTTSHQMENTGYAFGNGGGGMEQMATSDPNRVLWGFPWQMNMGGGSGHGHGHVDQIDSGREIWSSTVNYINTGALL", "text": "FUNCTION: Transcription factor that negatively affects seed germination and opposes TCP14 function in the regulation of a specific set of abscisic acid-related genes (PubMed:22155632). 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": "QDWLTFQKKHITNTRDVDCDNIMSTNLFHCKDKNTFIYSRPEPVKAICKGIIASKNVLTTSEFYLSDCNVTSRPCKYKLKKSTNKFCVTCENQAPVHFVGVGSC", "text": "FUNCTION: Basic protein with antiproliferative/cytotoxic activity against several tumor cell lines in vitro, as well as antitumor in vivo. It exhibits a ribonuclease-like activity against high molecular weight ribosomal RNA. SIMILARITY: Belongs to the pancreatic ribonuclease family."}
+{"protein": "MGALAARRCVEWLLGLYFVSHIPITLFIDLQAVLPPELYPQEFSNLLRWYSKEFKDPLMQEPPVWFKSFLLCELVFQLPFFPIAAYAFFKGSCRWIRIPAIIYAAHTITTLIPILYTLLFEDFSKAVAFKGQRPESFRERLTLVGVYAPYLIIPLILLLFMLRNPYYKYEEKRKKK", "text": "FUNCTION: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein Rough endoplasmic reticulum membrane; Multi-pass membrane protein Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. SIMILARITY: Belongs to the TMEM97/sigma-2 receptor family."}
+{"protein": "MANPRVFFDMTVGGAPAGRIVMELYANEVPKTAENFRALCTGEKGVGKSGKPLHYKGSTFHRVIPEFMCQGGDFTRGNGTGGESIYGEKFPDEKFVRKQPAPGVLSMANAGPNTNGSQFFICTVATPWLDGKHVVFGQVVEGMDVVKAIEKVGTRNGSTSKVVKVADCGQLS", "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": "RWADIIVAARPGVGKALALDTPLPTPTGWTTTGDVAVGDELLGADGKPTRVVAATEVLLGRPCYEVEFSDGTVIVADAAHQWLTETRASRKSAQAAAAGYNRYKNQRTFAAVRTTAEIAGTLRCPTLDRRLNHSVVNARALDLPDREFLVPPYTLGAWLGDGTSAAAQITAADPEIIMRIEAEMSSTVGTLQARLRTIGVLGNKHIPTEYLRGSETQRRELLAGLLDTDGTVTAGGAVQFSVTNQRLACDVAELIVSLGYRCQTSTKRVRGRNESSSIAYTLTFSTEKKMFALERKAIHKERRAMAGTTRSGSRFIVDVRPVETVAVRCVEVDNGSHLYLASRAMVPTHNSTLGLDFLRSCSIKHRMASVIFSLEMSKSEIVMRLLSAEAKIKLADMRSGRMSDEDWTRLARRMSEISEAPLYIDDSPNLTMMEIRAKARRLRQKADLRLVVVDYLQLMSSGKKVESRQLEVSEFSRQLKLLAKELEVPVVAISQLNRGPEQRTDKKPMLSDLRESGSLEQDADMVILLNRPDAFERDDPRGGEADFILAKHRNGPTKTVTVAHQLHLSRFANMAR", "text": "FUNCTION: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. SIMILARITY: Belongs to the helicase family. DnaB subfamily."}
+{"protein": "MSNESIYSVLDLTQVIFEDRYLVKQKLGDGSFGTVYLAQRKEKNGLYETVAVKKLKNSSKPKPKHELLKLRESLALRKISKHPCLIDLLETFMDPYRNIFLVMEFMDCNLFQLFKRRQGRLFTKETAFNILLQIISGIEHIHKHGFMHRDIKPENILVKRISPKPISSRYSIKLGDFGLARPSVSSDPLTEYVSTRWYRAPELLLRSGSYNHSVDLYAFGCIVFEIYSLKPLFPGRNETDQLNRVCEILGNPGIDELDTLHYWSQAKELAKRLGFMLPPTKPYPIQKLLPQNCPEGHAKMIPCLLAWNPDVRPTAKYCKEVFFPLPPSASKSNSVPQKISNPKVEQNLGFPISREDKKSTRRVGWLKKNLSEFVSSVKSVFPDSHGSQPHVKTEKPINAKESTGHLANPIASSNVPAISLKPGELHESVFFSENEQIDYLLTSIDYLPSYKPPSNGSNIAINAFNETVGDRIPSSKDILITEKIPFKKENEIRDSIVPSCSQPDESNKEGVASCLLLQKSGMEMTSVLEYSTPNPAEVQNICNDHAKFETSKSLHLSSP", "text": "FUNCTION: Protein kinase which is essential for spore formation. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MDRLVKTEFNEVNLNFQKNQKCSSSFKLTNLMHTMSVAVSLTTTNPTTFSINKPLSVIPPLSSSTYTLHLTNLNQPPLSEPADVITVRTSMLPTGKATTDDLRRLFNKPGPHVFRDAVITVILVGPTVAEYVISNYETRNLFTKAISVCTKSNLTNLMKPAVESGKVEYVTDLITAGGDVNFRDSNGKSLIPFAIRTGKLAVLKLLVANGCRINDSVDFVLHEAAIIDRVDVVKFLFESFCDELDVNSVNREMMTPIHVSASEGHVSLIEFFVSIGGNANAVDSRRWTPLHHAASRNHLKAVEFLLENSDVKYARELNGKTAFEIASESGHTRLFGVLRWGDALLQAARVDDVHALKKCLGEGAEVNRKDQNGWTPLHWASFKGRIKSVKVLLEHGAEVDSVDDAGYTPLHCAAEAGHLQVALVLIAHGGCQTNLKSFQHVSPIATFQKHVSLHYSTKKSETFA", "text": "FUNCTION: May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi and in nitrogen-fixing rhizobial bacteria symbiosis leading to the formation of root nodules. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane; Peripheral membrane protein; Cytoplasmic side."}
+{"protein": "MASTSSLALSQALLARAISHHGSDQRGSLPAFSGLKSTGSRASASSRRRIAQSMTKNRSLRPLVRAAAVETVEPTTDSSIVDKSVNSIRFLAIDAVEKAKSGHPGLPMGCAPMAHILYDEVMRYNPKNPYWFNRDRFVLSAGHGCMLLYALLHLAGYDSVQEEDLKQFRQWGSKTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDAEVVDHYTYAILGDGCQMEGISNEACSLAGHWGLGKLIAFYDDNHISIDGDTEIAFTENVDQRFEALGWHVIWVKNGNTGYDEIRAAIKEAKTVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALGEKEVEATRNNLGWPYEPFQVPDDVKSHWSRHTPEGATLESDWSAKFAAYEKKYPEEASELKSIITGELPAGWEKALPTYTPESPGDATRNLSQQCLNALAKVVPGFLGGSADLASSNMTLLKAFGDFQKATPEERNLRFGVREHGMGAICNGIALHSPGLIPYCATFFVFTDYMRGAMRISALSEAGVIYVMTHDSIGLGEDGPTHQPIEHIASFRAMPNTLMFRPADGNETAGAYKIAVTKRKTPSILALSRQKLPHLPGTSIEGVEKGGYTISDDSSGNKPDVILIGTGSELEIAAQAAEVLRKDGKTVRVVSFVCWELFDEQSDEYKESVLPSDVSARVSIEAASTFGWGKIVGGKGKSIGINSFGASAPAPLLYKEFGITVEAVVDAAKSFF", "text": "FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose- 4-phosphate or ribose-5-phosphate, respectively (By similarity). Could act as a stress sensor involved in adaptation process. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the transketolase family."}
+{"protein": "MNIVSDVNYATSVAALRMLQASAVLDVTEEDFDFLTGDKIWIATDRNRARRCVEACVYGTLDFVGYPRFPAPVEFIAAVIAYYVHPVNVQTACLVMEGAEFSENIINGVERPVNAAELFAYTLRIKAGFKETVMDAEENARQKLRANGLK", "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. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the microvirus D protein family."}
+{"protein": "MASTFSKLLTGRNASLLFATLGTGALTTGYLLNKQNVCAAAREQHKLFPPSADYPDLRKHNNCMAECLTPAIYAKLRNKVTPSGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFADLFDPVIKLRHNGYDPRVMKHPTDLDASKITQGQFDERYVLSSRVRTGRSIRGLSLPPACSRAELREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDIKVPPPLPQFGKK", "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 (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the ATP:guanido phosphotransferase family."}
+{"protein": "MKSCEHELLKTRRGKSREVSSRFLSSPSASSSPNRRNSTSNSSRDDQNNNGVKGHLGLKKHDRMSDGTRVCFGLPNQSSIEVDTKENRMPSPWINDEDNVILPGRFSVDECALYRASSRRNSCSLLYESFNDETDSELSDVSCASSLSTNRSSWNHKPGIKVSSKYLHDLTAKPSKGNNKTKLRSQDDSQRTNSSKGIENRLQRNNSVSRYGSSMSQWALSPGRSLDTQAVTVPSSKLKPPRGKGVGKLINLGFDFFRSKNKSSPFTSPLKPKTCDTESAHQLKLMNNRLLQWRFVNARACDVNKNVASQEKNQLLCAWDTLIKLNNLVLQERIKLQKKNLEMKLNYVFLSQVKHLEAWEDMEIQHLSSLSIIRDSLHSVLSRLPLKEGAKVNLESAVSIIKNAEAVTDAIISTVDDYAPTMEGIVPLASQLAEVVVQEKLMLEKCHDLLRMISELEMQERSLKCCFLIQHKQTFDTNLLKH", "text": "SIMILARITY: Belongs to the QWRF family."}
+{"protein": "MNKFCLLPFHGKRIGVANIPFTILFKKGPYFLHSHITAVYYSTKGKNDSHEQSRVSKKSTFTPLETPWYLRIVDNEKELMEGKKNNHHTMNKELEIPKTSPNSLRKIADLLTGKLGLDDFLVFDLRKKSPNSVSAVNKLGDFMVICTARSTKHCHKSFLELNKFLKHEFCSSAYVEGNFNERQESRRKRRLARKSNLSKLLGRSSECSAKDLNSEAWYMIDCRVDGIFVNILTQRRRNELNLEELYAPENEKSKFQNIDSGNVPTISGVNEISSNNNILLGLRRLAQQRRRYSTINPNGLSNLRYFLQKEDFKGANKIIQSSSGTETHNIRTLEHVKNTLKDLVGQERKVDVVQWKSLFDEHSTFLTINQSAAYWPLRLEYAILLNKADPQFYSDRVFLKDYLLLKKSLGQELIREDLIALLEMVLKTQHSSHSYFNLVKQNRVIIRALNLFKGLQTEDDGSVVYDEVVISLLLNSMVADERVKLRSLYETIDHIFQTFGDKLTSGMIVSILQNLAKIKDWNKLLQVWEAITPTEGEGQDKRPWNEFINVINQSGDSHVISKIVNNGHLLWIRRLNVNVTPELCNSIKALLKTAGMENSTLEEFLVRGTNNQ", "text": "FUNCTION: mRNA stabilization factor specific for the 0.95 kb OLI1 mRNA. Also involved in OLI1 ring formation. FUNCTION: mRNA stabilization factor specific for the 0.95 kb OLI1 mRNA. Also involved in OLI1 ring formation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the ATP25 family."}
+{"protein": "MSFDSLSPQELAALHARHQQDYAALQGMKLALDLTRGKPSAEQLDLSNQLLSLPGDDYRDPEGTDTRNYGGQHGLPGLRAIFAELLGIAVPNLIAGNNSSLELMHDIVAFSMLYGGVDSPRPWIQEQDGIKFLCPVPGYDRHFAITETMGIEMIPIPMLQDGPDVDLIEELVAVDPAIKGMWTVPVFGNPSGVTYSWETVRRLVQMRTAAPDFRLFWDNAYAVHTLTLDFPRQVDVLGLAAKAGNPNRPYVFASTSKITFAGGGVSFFGGSLGNIAWYLQYAGKKSIGPDKVNQLRHLRFFGDADGVRLHMLRHQQILAPKFALVAEVLDQRLSESKIASWTEPKGGYFISLDVLPGTARRTVALAKDVGIAVTEAGASFPYRKDPDDKNIRIAPSFPSVPDLRNAVDGLATCALLAATETLLNQGLASSAPNVR", "text": "FUNCTION: Main aspartate aminotransferase that couples nitrogen assimilation to aspartate synthesis. Has a weak, but significant, side activity toward kynurenine (Kyn). Oxaloacetate and 2-oxoglutarate, but not pyruvate, serve as amino acceptors, while Asp, Glu and Kyn serve as the best amino donors. Essential for axenic growth and survival of M.tuberculosis in macrophages and in mice. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MNVFFMFSLLFLAALGSCADDRNPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYANLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIKNIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKVVEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLPTAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPSVTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSGTKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTNGVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLPKKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDPLTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLASENPSGIHLSNDNEL", "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:11248687, PubMed:8080286). Shows high affinity for L- Phe, L-Trp, L-Met, L-Leu, and L-Ile, moderate affinity for L-Arg, L- Asp, and L-His, and very low affinity for L-Gln, L-Lys, and L-Ala (PubMed:8080286). Also shows high activity on L-norleucine (L-2- aminohexanoate), and L-norvaline (L-2-aminopentanoate) and a weak activity on L-ornithine and L-aminobutyric acid (PubMed:8080286). Also 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 (By similarity). 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 (By similarity). A possible explanation of high efficacy it that LAAO may bind to target cells through its sialylated glycan moiety that would bind to sialic acid-binding lectins (siglec) on target cells (PubMed:11453999). This interaction may result in production of locally high concentrations of hydrogen peroxide in or near the binding interface, leading, in turn to oxidative damage of the siglec or another adjacent cell structural elements (PubMed:11453999). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
+{"protein": "MQIILPDILQTWAYARLLNPHYDGAKLESSLWIHPLVAKLFDQKGQKAFQNDYTSLLASLMYSHQGKVPSRRCDMMNLFFVYDEYTDVVSPEIAHRLSKIVVDAMKNSDEMSPCGEHPIGDKAKEFWRLATTLLPATGSNSDVCKSRFINLTEEYLNAVTVEARDRNEGTIHSVKEYLTMRRATSGAGLMLALIEFELDLPKAVLEHKFVQALEEIYTRTRVSSGQANHNLITVVMHENPGLSLQGAFDWLGSYAAGVVECFQTNVRNLPSFCDVEGPACESVDGTLQERVDKYISGLGQAVRAEDDWAFETTRYYGEDGPKVRETRVLVIRPVKRITRRHLLQSLEIKYSMVRG", "text": "SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MNARGLGSELKDSIPVAELSASGPFESHDLLRKGFSCVKNELLPSHPLELSEKNFQLNQDKMNFSTLRNIQGLFAPLKLQMEFKAVQQVHRLPFLPSSNLSLDILRGNDETIGFEDILNDPSQSELMGEPHVMVEHKLGLL", "text": "FUNCTION: Molecular chaperone essential for the assembly of standard proteasomes and immunoproteasomes. Degraded after completion of proteasome maturation (By similarity). Mediates the association of 20S preproteasome with the endoplasmic reticulum (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Microsome membrane. SIMILARITY: Belongs to the POMP/UMP1 family."}
+{"protein": "MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVIRLDGAIRMQP", "text": "FUNCTION: In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:24549042, PubMed:25925575, PubMed:26950678, PubMed:28888424). Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit (PubMed:23042678, PubMed:25925575, PubMed:28888424). 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 (PubMed:29040705). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly. FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (PubMed:9553139, PubMed:10600649, PubMed:12917011, PubMed:20077426, PubMed:18996107, PubMed:19706438, PubMed:25925575, PubMed:26950678, PubMed:28888424). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA (PubMed:9553139, PubMed:10600649, PubMed:12917011, PubMed:25925575, PubMed:26950678). Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2- methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway (PubMed:20077426, PubMed:18996107, PubMed:19706438). Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids (PubMed:10600649, PubMed:12917011). Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel (PubMed:19706438, PubMed:28888424). Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis (PubMed:26338420). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (PubMed:9338779). Essential for structural and functional integrity of mitochondria (PubMed:20077426). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MEIPPQEAPPGPGADGEAEEAPVEAPSPGPASPPADGRLKAAAKRVTFPSDEDIVSGAVEPKDPWRHAQNVTVDEIIGAYKQACQKLNCRQIPKLLRQLQEFTDLGHRIDCLDLKGEKLDYKTCEALEEVFKRLQFKVVDLEQTNLDEDGASALFDMIEYYESATHLNISFNKHIGTRGWQAAAHMMRKTSCLQYLDARNTPLLDHSAPFVARALRIRSSLAVLHLESSSLSGRPLMLLATALKMNMTLRELYLADNKLNGLQDSAQLGNLLKFNCSLQILDLRNNHVLDSGLAYICEGLKEQRKGLATLVLWNNQLTHTGMAFLGMTLPHTHSLETLNLGHNPIGNEGVRNLKNGLISNRSVLRLGLASTKLTCEGAVAVAEFIAESPRLLRLDLRENEIKTGGLMALSLALKVNHSLLRLDLDREPKKEAVKSFIETQKALLAEIQNGCKRNFVLVREREEKEQRLQLSASMPEITVTEPQPDDEPREEPAAEAQENGAPGPSPGPDSDSDSDSEGEDRDEADGERAEAPCPTLVPPTDSLGPGDRSPPGCPSSPAEQRISVSSPGWGHKVFVVTRVESPPERAEPPVPPAPPGPVSPPASASPPTSPFPTPTEAASTPDPGPPEPQPPLEPPQVGPPLPNGLKPEFALALSPEPPPGPEAKVGSCGLEHELSCSKNEKELEELLLEASQESGQETL", "text": "FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. SIMILARITY: Belongs to the PPP1R37 family."}
+{"protein": "MAAARRLRTLQSQPENKVCVDCSQKNPQWASISYGIFMCLECSGKHRGLGVHISFVRSVTMDSWSEIQIKKMDAGGNERLNNFLAQYGISKETDIISKYNSNAASVYRDRIQALAEGRQWRDPPIVKESVGGGLMNKKPPLSQGGGRDSGNGGWDNWDNDDSFRSTDMRRNQSAGDFRSSGGRGAPAKSKSSEDIYSRSQLEASAANKESFFAKRMAENESKPEGLPPSQGGKYVGFGSSPGPAPRSNQQSGGGDVFSVMSEGFGRLSLVAASAANVVQTGTMEFTSKVKEGGLDQTVSETVNVVASKTTEIGQRTWGIMKGVMAIASQKVEEFTKEEASTWNQQNKTEGNGYYQNSGIGNKTANSSFGGSQSSSSGHNNSYRNSNSWDDWGEENNSKKEAAPKVSTSNDDDDGGWAGWDDNDAKDDDFYYQPASDKKSVGHNGKSDTAWTGGGFL", "text": "FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor (ARF). Involved in protein trafficking by controlling ARF1 activity; may participate in COPI vesicle formation at the Golgi complex. SUBCELLULAR LOCATION: Golgi apparatus."}
+{"protein": "MLLLLLPLLLAAVLTRTQADPVPRATRLPVEAKDCHIAQFKSLSPKELQAFKKAKGAIEKRLLEKDMRCSSHLISRAWDLKQLQVQERPKALQAEVALTLKVWENINDSALTTILGQPLHTLSHIHSQLQTCTQLQATAEPKPPSRRLSRWLHRLQEAQSKETPGCLEDSVTSNLFQLLLRDLKCVASGDQCV", "text": "FUNCTION: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. 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. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the lambda interferon family."}
+{"protein": "MTALTQAHCEACRADAPHVSDEELPVLLRQIPDWNIEVRDGIMQLEKVYLFKNFKHALAFTNAVGEISEAEGHHPGLLTEWGKVTVTWWSHSIKGLHRNDFIMAARTDEVAKTAEGRK", "text": "FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. May also have a positive regulatory role in the expression of phhA. SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family. SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family."}
+{"protein": "MEGIPLIDIYGKQWKIDKLIGCGGFGCVYSTQCASNTRQAVIKVESLNNTTMVSEVLVYNNIYDKNRIALWKNYKNIDHLGIPMYYGCGSFKRNTMYYRFILLERLVENTKELLKRVKKPKPLIKNIMKDMLYTLEYIHEHGISHGDIKPENIMVDGRYRSYLIDYGIVSYFIVNGKHVKYYKESKNWHRGTLYYASLDAHNGTCVTRRGDLESLGYCMLKWAGIPLPWKVFGNNGNMVHVAKCDFIKRVHKNKVNIKSANKGIYDYIKCVTKLSYEEKPDYDLLRQLVNSL", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Poxviruses subfamily."}
+{"protein": "MPSAKQLADIGYKTFSASMMLLTVYGGYLCSVRAYHYLQLRSARRQAAEEQKTSGVL", "text": "FUNCTION: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. Requires for coordination of the early steps of cytochrome c oxidase assembly with the synthesis of MT-CO1. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein."}
+{"protein": "MKLPPVFVFELVENQGLANIALIRPRVIAPDNNLRPGGIVSGIAGLLTLGQENRNLISENRQVINNNTTAIGQNSDRIDANAKGVADNRAAIGQNSGRIDANAKGVADNKAAIGRNSGRIDANAKGVADNKTAIGRNSGRIDTNAKGVADNRAAISQNRGRINANAAGVASNRAAIRQNSAAISALGQRVDGLQGQINSARKEARAGAANAAALSGLRYDNRPGKVSIATGVGGFKGSTALAAGIGYTSKNENARYNVSVAYNEAGTSWNAGASFTLN", "text": "FUNCTION: Participates in bacterial attachment to several surfaces, including various extracellular matrix (ECM) components and a hydrophobic abiotic surface. Involved in adhesion to host epithelial cells and is required for full virulence in mice. Also implicated in the resistance to porcine serum. SUBCELLULAR LOCATION: Cell surface Cell outer membrane Note=The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface (By similarity). Localizes at the new cell pole generated after cell division (PubMed:24236157). SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family."}
+{"protein": "MRKLTKMSAMLLASGLILTGCGGNKGLEEKKENKQLTYTTVKDIGDMNPHVYGGSMSAESMIYEPLVRNTKDGIKPLLAKKWDVSEDGKTYTFHLRDDVKFHDGTPFDADAVKKNIDAVQENKKLHSWLKISTLIDNVKVKDKYTVELNLKEAYQPALAELAMPRPYVFVSPKDFKNGTTKDGVKKFDGTGPFKLGEHKKDESADFNKNDQYWGEKSKLNKVQAKVMPAGETAFLSMKKGETNFAFTDDRGTDSLDKDSLKQLKDTGDYQVKRSQPMNTKMLVVNSGKKDNAVSDKTVRQAIGHMVNRDKIAKEILDGQEKPATQLFAKNVTDINFDMPTRKYDLKKAESLLDEAGWKKGKDSDVRQKDGKNLEMAMYYDKGSSSQKEQAEYLQAEFKKMGIKLNINGETSDKIAERRTSGDYDLMFNQTWGLLYDPQSTIAAFKEKNGYESATSGIENKDKIYNSIDDAFKIQNGKERSDAYKNILKQIDDEGIFIPISHGSMTVVAPKDLEKVSFTQSQYELPFNEMQYK", "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. Binds the metal via the metallophore StP, and transfers the StP-metal complex to the membrane-bound permease (PubMed:23279021, PubMed:29581261). Binds one molecule of StP/metal. Binds StP/Co(2+) and StP/Ni(2+) tighter than StP/Zn(2+) (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; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family."}
+{"protein": "MHEISLSDVSSLVGQELGTSKWITIDQAMINLFADATHDHQFIHVDPNRAAAESPFGGAIAHGFLTLALLSVMNFSGMPKFREQTMGINYGFDRVRFISPVRTGSRVHGRFVLSDCRLRRASILMTAYNVTVEIENENKPALTANWIAIAQFNPKDRPKAG", "text": "FUNCTION: Involved in the production of the root hair deformation (HAD) factor specifically on medicago. SIMILARITY: To the R.leguminosarum biovar viciae counterpart."}
+{"protein": "MLSMLRTMTRLCFLLFFSVATSGCSAAAASSLEMLSREFETCAFSFSSLPRSCKEIKERCHSAGDGLYFLRTKNGVVYQTFCDMTSGGGGWTLVASVHENDMRGKCTVGDRWSSQQGNKADYPEGDGNWANYNTFGSAEAATSDDYKNPGYYDIQAKDLGIWHVPNKSPMQHWRNSALLRYRTNTGFLQRLGHNLFGIYQKYPVKYRSGKCWNDNGPAIPVVYDFGDAKKTASYYSPYGQREFVAGFVQFRVFNNERAANALCAGIKVTGCNTEHHCIGGGGFFPQGKPRQCGDFSAFDWDGYGTHVKSSCSREITEAAVLLFYR", "text": "FUNCTION: May play a role in the defense system against pathogens. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MNSTKSPASHHTERECFKNSQVLSWTMAGASILFLSVCFITRCVVTYHSFQIYGQKKLQPHKTIKELSCYLEASGSVKNCCPLNWKHFQSSCYFFSTTTLSWLSSLKNCSDMGAHLVVINTWEEQEFLFRTKPRKKEFYIGLTDQVVEGQWRWVDDTPFTESLSFWDAGEPNNIVFVEDCATMRDSSNPRKNWNDVSCFFSMPWICEMPEISPLD", "text": "FUNCTION: Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: recognizes damage- associated molecular patterns (DAMPs) of abnormal self and pathogen- associated molecular patterns (PAMPs) of bacteria and fungi. The PAMPs notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant immunomodulatory functions. Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, 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 (Th1) and T-helper 17 (Th17) cell subtypes. Also recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia and mediates macrophage activation. Through recognition of DAMPs released upon nonhomeostatic cell death, enables immune sensing of damaged self and promotes inflammatory cell infiltration into the damaged tissue. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Cell projection, phagocytic cup."}
+{"protein": "MGGRVSKAVACCCCRSQHHGVVVESSEKTAEEDHGESYELPAFQEFSFEQLRLATSGFAVENIVSEHGEKAPNVVYKGKLDAQRRIAVKRFNRSAWPDPRQFLEEAKSVGQLRSKRLANLLGCCCEGDERLLVAEYMPNDTLAKHLFHWEAQAMKWPMRLRVVLYLAEALEYCTSKGRALYHDLNAYRVLFDDDCNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYMRTGRITPESVIYSFGTLLLDVLSGKHIPPSHALDLIRDRNFNMLTDSCLEGQFSNEEGTELVRLASRCLHYEPRERPNVRSLVQALAPLQKDLETPSYELMDIPRGGATSVQSLLLSPLAEACSRKDLTAIHEILEKTGYKDDEGTANELSFQMWTNQMQDTLNSKKKGDNAFRQKDFSSAIDCYSQFIEVGTMVSPTIYARRCLSYLMNDKAEQALSDAMQALVISPTWPTAFYLQAAALLSLGMENEAQEAIKDGCAHETSSSSGH", "text": "FUNCTION: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of BRI1. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Note=Plasma membrane localization is required for its function in the regulation of brassinosteroid signaling."}
+{"protein": "MAFSTQDSDEVLSEINVTPLVDVMLVLLVVFIVTAPLLTNSIPINLPKTESVAPPEQKDPLVVSIDGAGKLFVNKDEIQPELLESNLAAAKAKDAEVRVQLQADEGVNYGQVAKAMASIERAGITRLAVITAR", "text": "FUNCTION: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the ExbD/TolR family."}
+{"protein": "MRHCAFLFRLFLIGYSCSVYFSACTQASSLKEPADELPRAEQWDSDGKRILQADDPEHIPTEERGITQNLSPAVESVGKVKASKMAVPKSVISKLNPVNWVKGTWAALKKGFKALQLG", "text": "FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host cell membrane. SIMILARITY: Belongs to the RxLR effector family."}
+{"protein": "MACGATLKRPMEFEAALLSPGSPKRRRCAPLPGPTPGLRPPDAEPPPPFQTQTPPQSLQQPAPPGSERRLPTPEQIFQNIKQEYSRYQRWRHLEVVLNQSEACASESQPHSSALTAPSSPGSSWMKKDQPTFTLRQVGIICERLLKDYEDKIREEYEQILNTKLAEQYESFVKFTHDQIMRRYGTRPTSYVS", "text": "FUNCTION: Molecular adapter that acts as a bridge between proteins, and which is involved skeletal muscle development (By similarity). Functions as signal transducer for MSTN during skeletal muscle regeneration and myogenesis (By similarity). May regulate chemotaxis of both macrophages and myoblasts by reorganising actin cytoskeleton, leading to more efficient lamellipodia formation via a PI3 kinase dependent pathway (By similarity). In contrast to AKIRIN2, not involved in nuclear import of proteasomes (PubMed:34711951). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the akirin family."}
+{"protein": "MAKRRSWFGWMKRLFICEAKARAEKKPRRLRWVFKRLKLRPQLATCGQETRTLNEATQDQRKHAMNVAIATAAAAEAAVAAAKAAAEVVRMAGNAFTSQHFVKKLAPNVAAIKIQSAFRASLARKALRALKALVRLQAIVRGRAVRRKVSALLKSSHSNKASTSNIIQRQTERKHWSNTKSEIKEELQVSNHSLCNSKVKCNGWDSSALTKEDIKAIWLRKQEGVIKRDRMLKYSRSQRERRSPHMLVESLYAKDMGMRSCRLEHWGESKSAKSINSFLIPSEMLVPTKVKLRSLQRQDSGDGQDSPFSFPRRSFSRLEQSILEDESWFQRSNGFQPYMSVTESAREKMRSLSTPRQRVGIMDSLFDNYKKDGDKVSLWSTFVCENSKINNAKKSSLTTYQHNC", "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 Cell membrane Note=Recruits calmodulin (CaM2) at plasma membrane subdomains. SIMILARITY: Belongs to the IQD family."}
+{"protein": "TERGFLDCTSPPVTGPCRAGFKRYNYNTRTKQCEPFKYGGCKGNGNRYKSEQDCLDACSGF", "text": "FUNCTION: Inhibitor of trypsin and chymotrypsin. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MITIACAEGGSTIYSLKKAIEDLGEKCNILLLSSDNLLVDTDFNIKTDLIHSRCGIGDYLDRLTLFSWQVLKNLESEGHYFINPLETIYNSSDKFKTTKILSKNGLKTPKTALIRDYADAKHFLDTKNMNYPVILKNSFSKCGMKVQKANSDDELKKLSKNSIWESKLIQEYVDFKNGDTYKDMRILVIDGEVVGGYRRVSNNFITNLYVGGQIEPLNVSSELEEIALKCSECMNGYIMGIDILPKDGEYYVVEVNTAPGTKGFRSLGIDVDKRIAECLIKYKKS", "text": "FUNCTION: Catalyzes the ATP-dependent addition of one alpha-linked L- glutamate molecule to coenzyme gamma-F420-2, producing coenzyme alpha- F420-3. Thus, caps the gamma-polyglutamate tail of coenzyme F420 with a terminal alpha-linked glutamate (By similarity). SIMILARITY: Belongs to the RimK family. CofF subfamily."}
+{"protein": "MKRQALAAMIASLFALAACGGEQAAQAPAETPAASAEAASSAAQATAETPAGELPVIDAVTTHAPEVPPAIDRDYPAKVRVKMETVEKTMKMDDGVEYRYWTFDGDVPGRMIRVREGDTVEVEFSNNPSSTVPHNVDFHAATGQGGGAAATFTAPGRTSTFSFKALQPGLYIYHCAVAPVGMHIANGMYGLILVEPKEGLPKVDKEFYIVQGDFYTKGKKGAQGLQPFDMDKAVAEQPEYVVFNGHVGSIAGDNALKAKAGETVRMYVGNGGPNLVSSFHVIGEIFDKVYVEGGKLINENVQSTIVPAGGSAIVEFKVDIPGSYTLVDHSIFRAFNKGALGQLKVEGAENPEIMTQKLSDTAYAGSGAASAPAASAPAASAPAASASEKSVY", "text": "FUNCTION: Catalyzes the reduction of nitrite to nitric oxide (NO), probably with azurin as electron donor. Essential for growth and survival in oxygen-depleted environments. Can also provide protection against killing by normal human sera. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the multicopper oxidase family."}
+{"protein": "MASSLLILCLVLVSLASSALCAAPRRPVDVPFGRNYIPTWAFDHIKYFNGGSEIQLHLDKYTGTGFQTKGSYLFGHFSMNIKMVPGDSAGTVTAFCLSSQNAEHDEIDFEFLGNRTGQPYILQTNVFTGGKGDREQRIYLWFDPTKAYHRYSVLWNMYQIVFLVDNIPIRVFKNLKELGVKFPFNQPMKVYNSLWNADDWATRGGLEKTDWSKAPFVAEYKGFHVDGCEASVNSRFCATQGKRWWDQTEFRDLDSFQWRRLKWVRQKFTIYNYCTDRTRYPQLPPECRRNRDI", "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 (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1 subfamily."}
+{"protein": "MTLFKKIQWFCNLIRLRSYYKFLLLIAYTAFGAWLFRTYELQADIKRRSVFGNTTNLVRRQLAERWIEMHKDAVLRNDSALRFRRAAEAVEWLLDELNLSDHIRDLSEETPWTWTGAMFYAGQLYTTIGYGYPTTKTDEGRICTIFYALFGIPCFLMYLKIENAIEWKKDKQLGKRALKMHGLINDSFQSIGKTLSKKMKKYYKKLRRSRVGRILLPTRVTAMKDGFEDPEAAEERKKKPFPIPIAIIMLIIWICFSASMFCIWEDTWVFSSAVYFFIVSISTVGLGDMLFRTPDMMVFNFLLILVGLALLSMCFELITDRVAKWKQKRFDEHIKKVQKMAFQVFEKDPFIEEAPPLGIRMAPNLMQIAATHVSEEKRGFFAEFKDWFAGKVTDNVIQSKLEDSDDESDSEEALEEFDSPQIATVTANDLIVCSNGAATRRVSKQSYALSDISNLSNSKILPGNNYGQLLDRIKAMEKFKPKKNDLDSRMFAKFLENKKLAKILEQTELRELATVSCQTDLSGLVVQRRNPKGRHARIGSCSSQSTMSTLLPNKMHAPDEDSVMSFTFGDLKFDYKTEPFIDEYYIRESNHSIFDFDEDETVRIPQKMLISRPGMPPPPPSRPLNLASPLRTLLEKEQKYDEDPEIQLTPRRLNSLSDIQARKVKLGVDENLQHARLVCGLLPQDFDSPSTSTSTSMIDSGYELSKRDASTMA", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the two pore domain potassium channel (TC 1.A.1.8) family."}
+{"protein": "MAQRMTTQLLLLLVWVAVVGEAQTRIAWARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTVLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMSGAGPWAAWPFLLSLALMLLWLLS", "text": "FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells (PubMed:23851396, PubMed:23934049, PubMed:2527252, PubMed:8033114, PubMed:8567728, PubMed:19074442). Has high affinity for folate and folic acid analogs at neutral pH (PubMed:23851396, PubMed:23934049, PubMed:2527252, PubMed:8033114, PubMed:8567728). Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release (PubMed:8567728). Required for normal embryonic development and normal cell proliferation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Apical cell membrane; Lipid-anchor, GPI- anchor Basolateral cell membrane; Lipid-anchor, GPI-like-anchor Secreted Cytoplasmic vesicle Cytoplasmic vesicle, clathrin-coated vesicle Endosome Note=Endocytosed into cytoplasmic vesicles and then recycled to the cell membrane. SIMILARITY: Belongs to the folate receptor family."}
+{"protein": "MFDLDEWIATVRKCKYLPEHQLKRLCEMVKVILMEESNIQPVRTPVTVCGDIHGQFYDLLELFRVGGELPSTNYIFMGDFVDRGYFSLETFTLFMLLKARYPDKITLLRGNHESRQITQVYGFYDECQTKYGNANVWKYCCQVFDFLTLAAVIDNKILCVHGGLSPEVRTLDQIRILARAQEIPHEGSFCDLMWSDPEDIESWTVSPRGAGWLFGSKVTTEFSQINDLTLIARAHQLVQEGYKYHFADKNLVTVWSAPNYCYRCGNVASVMKVDESLEPEFRIFSAVADEDRTVPPSRKRSEYFI", "text": "FUNCTION: Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. Negatively regulates mis12. SUBCELLULAR LOCATION: Nucleus Note=Associated with chromatin. SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily."}
+{"protein": "MAALPRGSRGLPLLPLLLLLPPLGGPRGADGYFPEERWSPESPLQAPRVLIALLARNAAPALPATLGALEQLRHPRERTALWVATDHNTDNTSAILREWLVAVKGLYHSVEWRPAEEPSSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFMDIDNLITNPDTLSLLIAENKTVVAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPTHPDYTWSFDDIIVFAFSCKQAEVQMYVCNKEVYGFLPVPLRAHSSLQDEAESFMHVQLEVMVKHPPVQLSRFISAPRKTSDKMGFDEVFMINLKRRRDRRERMLRALHEQEIDCQLVEAVDGKAMNTSQVEAMGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRGLQKSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPHVRNLVEADYSYWTLAYVISLQGAQKLLAAKPLAKMLPVDEFLPVMFDKHPMSEYKSHFSPRNLRAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEQVKTDWDRAKSQKMREQQALSREAKNSDVLQSPLDSTARDEL", "text": "FUNCTION: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. By acting on collagen glycosylation, facilitates the formation of collagen triple helix. Also involved in the biosynthesis of collagen type IV. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Note=Colocalized with PLOD3 and mannose binding lectin. SIMILARITY: Belongs to the glycosyltransferase 25 family."}
+{"protein": "MAEVKKSIPKRRFVGKKNRKENNLDGSNRDVENAALVTINSKRSAGRVATQIPEDILNDKAINEAIKLLPQNYNFEIHKTIWHIRLRKAKRVALQLPEGLLMFGCILSDIFEQFCQVETIVMGDVTYGACCIDDFTARALDCDFLVHYGHSCLIPVDQTPIKVLYVFVDIKIDLQHVVSSLKHNLPSNSRLALVGTIQFVGSLNSIKDALQIQDEDGKGGFYVVIPQAKPLSPGEALGCTSPYIEKGSVDALIYIGDGRFHLESVMIANPDLPAYRYDPYSHKLSIESYAHEEMKSIRYSAVEKARTAKKFGLIQGTLGRQGSPKVLENLKNTLRKNNKDFVCVLMSEIFPSRLGQFSDIDAWIQVACPRLSIDWGYAFPAPLLTPYEASAAFNVVPWKEVYPMDFYATNSLGNWTPNNPENRPLPNRKKTGPVSS", "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": "MGRRRGVELYRAPFPLYALRIDPKTGLLIAAGGGGAAKTGIKNGVHFLQLELINGCLSASLLHSHDTETRATMNLALAGDILAAGQDAQCQLLRFQVHQQKGSKAEKSGSKEQGPRQRKGAPPAEKKSGAQVHPEGVELKVKNLEAVQTDFSNEPLQKVVCFNHDNTLLATGGTDGHVRVWKVPSLEKVLEFKAHEGEIGDLTLGPDGKLVTVGWDFKASVWQKDQLVTQLQWQENGPASSNTPYRYQACRFGQVPDQLGGLRLFTVQIPHKRLRQPPPCYLTAWDSSTFLPLRTRSCGHEVISCLSVSDSGTFLGLGTVTGSVAIYIAFSLQRLYYVKEAHGIVVTDVTFLPEKGCGPKLLGPHETALFSVAVDSRCQLHLLPSRRSVPVWLLLLLCVGLIIVTILLLQTAFPGFL", "text": "FUNCTION: Was first identified based on its probable role in the regulation of pituitary gene transcription. Binds to the prolactin gene (PRL) promoter and seems to activate transcription. FUNCTION: Guanine nucleotide exchange factor that specifically activates the small GTPase SAR1B. Mediates the recruitment of SAR1B and other COPII coat components to endoplasmic reticulum membranes and is therefore required for the formation of COPII transport vesicles from the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus Note=Concentrates at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER)."}
+{"protein": "MEKKQDNEVELYSIDLKNRNESAKIKLAYAKALEESILCETRKIEQEIKDQVVQKENKTYFNNKFDNRYKLRDLEKNLAEEEVRITEMLTIQRQDIAIERRKNTNCFSESSQVDQYSVTETNLQYATNIGLNLLQQLRYLRLQLSEKEDLHKKLSVDNAHLIKQLDLLSSNMKTLMKEKTKVQGQRDLLEQRLQGLMKKLTEVESLTVSLNDEKNKLTLELTNLRICLHELQLNAEKGETIDESEDSKNTLVTEDENDDSVFLESSSDKYFDSSSFDAEQEEKHDFPIDPFLSLESNVQTSVSQSSAVLKSINLAKQELVSVNHLVADDTKTPSPNLSSEIIENTKADIKKSIRSLNKAVSPENSIDIEDETDRDDEFICFLLSYQQLQKALKSNLGLFQLSCLYPLSLNHLIQSFFQSLTSQISIKDIDSKNKQVIKLFKPTKSSDRQEIFELAQFEPRQKFPIDTNSSKCDMSASTEMHLKDTEKFANFKLKENILNHSSIYERDVSYLPALNKGGRENYLNNRVSSYRLVKPILNSYGNHVLNRIQHDILENHFCCLKNVKDFVCGANTISMQWNLQKNMEFISSVFSLIKNEVNDTSANSVILRTDALSNVATTRLKRKLTSAIIDCSIPRRRLRHYSNPEIAEFKNFRLSTDISHSNVRNSKKLCSNGSMNCMRQGKAVFPRKIPYQEHDWEQWEKIAQSSMFKNRSIASRQSLETSDVTLDINMSSRHSNGTSSMLFKDFTKHNNWEASTYPSAPKNTRTYPTAEVEKTRHDSSQSARQLKARSTATTISISLSTVSDVFTLPRNNLKSKTNTKKCRDNLNLSGLSSSTCNANSVNKLMKHVMMGNEMMKYPRSESFKMFKKSHWRYFWINPHCEMLCWSKTNPFIEKGRKNQVKSVKIKGMTIIKAPDALKNANLHNEVIVMQTTDKPIVLKAKSKKIHNIWVQAIKQINHKAIFDTKPGI", "text": "FUNCTION: Involved in chromosome segregation. Facilitates nuclear oscillation during meiotic prophase I, the 'horsetail' phase, by acting as a dynein anchor. Essential for anchoring dhc1 to the cortex. Required for proper sliding of the microtubules along the cell cortex, which leads to the proper U-turn movement of the nucleus. SUBCELLULAR LOCATION: Cytoplasm, cell cortex Note=Localizes to the cell cortex during the 'horsetail' phase of mitosis."}
+{"protein": "MERDGDQAGHGPRHGSAGNGRELESPAAASLLAPMDLGEEPLEKAERARPAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFSNCRCDAACVSLGNCCLDFQETCVEPTHIWTCNKFRCGEKRLSRFVCSCADDCKTHNDCCINYSSVCQDKKSWVEETCESIDTPECPAEFESPPTLLFSLDGFRAEYLHTWGGLLPVISKLKNCGTYTKNMRPMYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPLWYKGQPIWVTANHQEVKSGTYFWPGSDVEIDGILPDIYKVYNGSVPFEERILAVLEWLQLPSHERPHFYTLYLEEPDSSGHSHGPVSSEVIKALQKVDRLVGMLMDGLKDLGLDKCLNLILISDHGMEQGSCKKYVYLNKYLGDVNNVKVVYGPAARLRPTDVPETYYSFNYEALAKNLSCREPNQHFRPYLKPFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNLFSNMQALFIGYGPAFKHGAEVDSFENIEVYNLMCDLLGLIPAPNNGSHGSLNHLLKKPIYNPSHPKEEGFLSQCPIKSTSNDLGCTCDPWIVPIKDFEKQLNLTTEDVDDIYHMTVPYGRPRILLKQHHVCLLQQQQFLTGYSLDLLMPLWASYTFLRNDQFSRDDFSNCLYQDLRIPLSPVHKCSYYKSNSKLSYGFLTPPRLNRVSNHIYSEALLTSNIVPMYQSFQVIWHYLHDTLLQRYAHERNGINVVSGPVFDFDYDGRYDSLEILKQNSRVIRSQEILIPTHFFIVLTSCKQLSETPLECSALESSAYILPHRPDNIESCTHGKRESSWVEELLTLHRARVTDVELITGLSFYQDRQESVSELLRLKTHLPIFSQED", "text": "FUNCTION: Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (PubMed:9662402, PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:22510396, PubMed:25260930). PPi inhibits bone mineralization and soft tissue calcification by binding to nascent hydroxyapatite crystals, thereby preventing further growth of these crystals (PubMed:9662402, PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:19419305, PubMed:22510396, PubMed:25260930, PubMed:25479107, PubMed:26910915, PubMed:30111653). Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP and UTP to their corresponding monophosphates with release of pyrophosphate, as well as diadenosine polyphosphates, and also 3',5'-cAMP to AMP (PubMed:11027689, PubMed:1647027, PubMed:23027977, PubMed:8223581). May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling (PubMed:1647027). Inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling; it is however unclear whether hedgehog inhibition is direct or indirect (PubMed:30111653). Appears to modulate insulin sensitivity (By similarity). Also involved in melanogenesis (By similarity). Also able to hydrolyze 2',3'-cGAMP (cyclic GMP-AMP), a second messenger that activates TMEM173/STING and triggers type-I interferon production (PubMed:25344812). 2',3'-cGAMP degradation takes place in the lumen or extracellular space, and not in the cytosol where it is produced; the role of 2',3'-cGAMP hydrolysis is therefore unclear (By similarity). Not able to hydrolyze the 2',3'-cGAMP linkage isomer 3',3'-cGAMP (By similarity). SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase family member 1]: Cell membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Note=Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, secreted form]: Secreted Note=Secreted following proteolytic cleavage. SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase family."}
+{"protein": "MKTPITEAIATADNQGRFLSNSELHASFGRFQRAASALEAARSLTSNSQKLIDGAAAAVYQKFPYTTQTFGPQYASTAEGKAKCTRDIGYYLRIVTYALVAGGTGPLDEYLVAGLEEMNRAFDLSPSWYVEALKYIKANHGLSGQAATEANGYFDYVINALS", "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: Plastid, cyanelle thylakoid membrane; Peripheral membrane protein; Stromal side Note=Part of the phycobilisome rod. SIMILARITY: Belongs to the phycobiliprotein family."}
+{"protein": "MSVQFTSEHVCYVNCNYCNTILVVNVPNNCSYNIVTVRCGHCTMVLSMDLAPFHQARTVQDHQVQNRGFQGNNFGSYDIASRNQRTSTAMYPMPTSQQQVSPIRPPEKRQRVPSAYNRFIKEEIQRIKTSNPEISHREAFSAAAKNWAHLPRLHFGLSVADGGGGGGSN", "text": "FUNCTION: May play a role in floral meristem development and maintenance of stamens, rather than in determining polarity in floral organs. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the YABBY family."}
+{"protein": "MSVCMPQKRYYRQRAHSNPMADHTFQYPVCPEQMDWSPLYPQYFPQQEEAGGAQVEFADIGCGYGGLLVQLSLLFPQQLILGLEIRVKVSDYVQDRIRSLRVAEPGRYQNIACLRSNAMKYLPNFFRKGQLSKMFFLFPDPHFKKTKHKWRIISPTLLAEYAYTLRIGGLVYTNTDVEEVHEWIVQHFSDHPLFSRVTEEQLADDIIVGHLGTCTEEGKKVQRNGGKNFLAVFRRVEDPQT", "text": "FUNCTION: Catalytic component of METTL1-WDR4 methyltransferase complex that mediates the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable loop. M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA tertiary structure and protect tRNAs from decay. Also acts as a methyltransferase for a subset of internal N(7)-methylguanine in mRNAs. Internal N(7)-methylguanine methylation of mRNAs regulates translation. Also methylates a specific subset of miRNAs. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family."}
+{"protein": "MQAQQYQQQRRKFAAAFLAFIFILAAVDTAEAGKKEKPEKKVKKSDCGEWQWSVCVPTSGDCGLGTREGTRTGAECKQTMKTQRCKIPCNWKKQFGAECKYQFQAWGECDLNTALKTRTGSLKRALHNAECQKTVTISKPCGKLTKPKPQAESKKKKKEGKKQEKMLD", "text": "FUNCTION: Secreted growth factor that mediates its signal through cell- surface proteoglycan and non-proteoglycan receptors (PubMed:16814777, PubMed:11278720, PubMed:19141530). Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups (PubMed:26896299, PubMed:27445335). Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration in several tissues namely neuron and bone (PubMed:1733956, PubMed:1768439, PubMed:11278720, PubMed:19141530, PubMed:27445335, PubMed:30667096, PubMed:19442624). Also plays a role in synaptic plasticity and learning-related behavior by inhibiting long-term synaptic potentiation (By similarity). Binds PTPRZ1, leading to neutralization of the negative charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby causing the dimerization and inactivation of its phosphatase activity leading to increased tyrosine phosphorylation of each of the PTPRZ1 substrates like ALK, CTNNB1 or AFAP1L2 in order to activate the PI3K-AKT pathway (PubMed:17681947, PubMed:27445335, PubMed:30667096, PubMed:16814777, PubMed:10706604). Through PTPRZ1 binding controls oligodendrocyte precursor cell differentiation by enhancing the phosphorylation of AFAP1L2 in order to activate the PI3K-AKT pathway (PubMed:27445335, PubMed:30667096). Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration through SRC dephosphorylation and activation that consequently leads to ITGB3 'Tyr-773' phosphorylation (PubMed:19141530). In adult hippocampus promotes dendritic arborization, spine development, and functional integration and connectivity of newborn granule neurons through ALK by activating AKT signaling pathway (By similarity). Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs) at the neuron surface, leading to abrogation of binding between PTPRS and CSPGs and neurite outgrowth promotion (By similarity). Binds SDC3 and mediates bone formation by recruiting and attaching osteoblasts/osteoblast precursors to the sites for new bone deposition (By similarity). Binds ALK and promotes cell survival and cell proliferation through MAPK pathway activation (PubMed:11278720). Inhibits proliferation and enhances differentiation of neural stem cells by inhibiting FGF2-induced fibroblast growth factor receptor signaling pathway (By similarity). Mediates regulatory mechanisms in normal hemostasis and in hematopoietic regeneration and in maintaining the balance of myeloid and lymphoid regeneration (By similarity). In addition may play a role in the female reproductive system, auditory response and the progesterone-induced decidualization pathway (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pleiotrophin family."}
+{"protein": "MGQPLPPVALLLLVSASSRAADVPKALVLLDPPWASVLKDDHVTLKCQGLHPAGDNTTQWLHNGSLLSSQAPAYTITAARAEDGGEYRCQTGLSSLSDPVQLRVHLGWLVLQAPRWVFQEGEPIQLRCHSWKNNKLHKVTYLQNGRGLRYFHQNSDLHIPEATRNHSGSYFCRGLIRHHNVSSETVTITVQGPANPVVSSSVLPWHQIAFCLVMGLLLAADTGLYFSVQRDLRSSQRARKEHTLGWSLGSQDK", "text": "FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (By similarity). 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. 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 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 (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
+{"protein": "MASQWQGMRTSVRRRSLLKEEQLEKKEVTRSAGGHPETGPLGSLCRQFQRRLPLRAVSLNLGNGPSWKRLESPEPEQQGLQAAARSAKSALGAMSQRIQESCQSGTKWLMETQVKVRRKRGAQKDRGSPPPSLSQKNTRLCRANRDARVGGHLRLSGQMGPHAHRRQRLRRESALRSPCSSTEPLCSPSESDSDLEPVGAGIQHLQKLSQRLDRAIKAEESGDMTVSLIRE", "text": "FUNCTION: During mitosis, may play a role in the metaphase-to-anaphase transition. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Note=Partially localizes to the nucleolus."}
+{"protein": "MKASIVLVSFLGLVSGMVLPGHRLSPSGAKLQPRSLFKREANLDYRYAPEPCRAILTTCRVTSDCCSGMKCVSADGESVCTPSD", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the UPF0499 family."}
+{"protein": "MSNEVETSATNGQPDQQAAPKAPSKKEKKKGPEKTDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNVKKKEEEKKKIEEASKAVENGSEALMILDDQTNKLKSGVDQMDLFGDMSTPPDLNSPTESKDILLVDLNSEIDTNQNSLRENPFLTNGITSCSLPRPTPQASFLPENAFSANLNFFPTPNPDPFRDDPFTQPDQSTPSSFDSLKSPDQKKENSSSSSTPLSNGPLNGDVDYFGQQFDQISNRTGKQEAQAGPWPFSSSQTQPAVRTQNGVSEREQNGFSVKSSPNPFVGSPPKGLSIQNGVKQDLESSVQSSPHDSIAIIPPPQSTKPGRGRRTAKSSANDLLASDIFAPPVSEPSGQASPTGQPTALQPNPLDLFKTSAPAPVGPLVGLGGVTVTLPQAGPWNTASLVFNQSPSMAPGAMMGGQPSGFSQPVIFGTSPAVSGWNQPSPFAASTPPPVPVVWGPSASVAPNAWSTTSPLGNPFQSNIFPAPAVSTQPPSMHSSLLVTPPQPPPRAGPPKDISSDAFTALDPLGDKEIKDVKEMFKDFQLRQPPAVPARKGEQTSSGTLSAFASYFNSKVGIPQENADHDDFDANQLLNKINEPPKPAPRQVSLPVTKSTDNAFENPFFKDSFGSSQASVASSQPVSSEMYRDPFGNPFA", "text": "FUNCTION: Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Note=Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane and translocated to the cytoplasm."}
+{"protein": "MANRKLEKMASIDVHLRQLVPGKVSEDDKLVEYDALLLDRFLDILQDLHGEDLRETVQELYEHSAEYEGKHEPKKLEELGSVLTSLDPGDSIVIAKAFSHMLNLANLAEEVQIAYRRRIKKLKKGDFVDESSATTESDLEETFKKLVGDLNKSPEEIFDALKNQTVDLVLTAHPTQSVRRSLLQKHGRIRDCLAQLYAKDITPDDKQELDEALQREIQAAFRTDEIKRTPPTPQDEMRAGMSYFHETIWKGVPKFLRRVDTALKNIGIEERVPYNAPLIQFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAATMYFNQIEDLMFEMSMWRCNDELRARADEVHANSRKDAAKHYIEFWKSIPTTEPYRVILGDVRDKLYHTRERAHQLLSNGHSDVPVEATFINLEQFLEPLELCYRSLCSCGDRPIADGSLLDFLRQVSTFGLSLVRLDIRQESDRHTDVLDAITTHLDIGSYREWSEERRQEWLLSELSGKRPLFGSDLPKTEEIADVLDTFHVIAELPADSFGAYIISMATAPSDVLAVELLQRECRVKQPLRVVPLFEKLADLEAAPAAVARLFSVDWYKNRINGKQEVMIGYSDSGKDAGRLSAAWQLYKAQEELVKVAKEYGVKLTMFHGRGGTVGRGGGPTHLAILSQPPDTINGSLRVTVQGEVIEQSFGEEHLCFRTLQRFTAATLEHGMRPPISPKPEWRALLDEMAVVATEEYRSVVFQEPRFVEYFRLATPELEYGRMNIGSRPSKRKPSGGIESLRAIPWIFAWTQTRFHLPVWLGFGSAIRHVIEKDVRNLHMLQDMYQHWPFFRVTIDLIEMVFAKGDPGIAALYDKLLVSEELWPFGEKLRANFEETKKLILQTAGHKDLLEGDPYLKQRLRLRDSYITTLNVCQAYTLKRIRDPSYHVTLRPHISKEIAESSKPAKELIELNPTSEYAPGLEDTLILTMKGIAAGLQNTG", "text": "FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. Contributes probably to the adaptation to inorganic phosphate (Pi) deprivation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PEPCase type 1 family."}
+{"protein": "MSTKREDHLRKGADVTPTEALVAGSIAGAISRAFTAPLDTIKIRLQLQPKGFKHRKSVVTIVKNLLENEGIIALWKGNVPAEILYILYGGVQFGSYSIISKSVSKLENNYRINLSSANHSLIVGIGSGIVSTLVTYPFDLLRTRLIANKNRGLLSMTGTIKDIIKLEGIRGIYAGIRPAMLSVSSTTGLMFWSYELARELSNNYQRVPFIEAICGFIAGATSKGITFPLDTLRKRCQMCSVVHGRPYTASHIFVTILKNEGVFGLYKGFGISVLKTAPTSAISLFMYEYSLSFIRKIRVIE", "text": "FUNCTION: Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "ASMLPLDKCFKASFCGDDSLIYLPKGLEYPDIQATANLVWNFEAKLFRKKYGYFCGKYIIHHANGCIVYPDPLKLISKLGNKSLVGYEHVEEFRISLLDVAHSLFNGAYFHLLDDAIHELFPNAGGCSFVINCLCKYLSDKRLFRSLYIDVSK", "text": "FUNCTION: The replicase large subunit is an RNA-dependent RNA polymerase active in viral RNA replication. SIMILARITY: Belongs to the tobamovirus RNA-directed RNA polymerase family."}
+{"protein": "MTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSISSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKGS", "text": "FUNCTION: Adapter protein able to interact with different proteins and involved in different biological processes (PubMed:11459825, PubMed:11459826, PubMed:17719540, PubMed:17296730, PubMed:19443654, PubMed:29656893). Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis (PubMed:20164194). Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions (PubMed:20164194). Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs) (PubMed:29656893). 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 (PubMed:29656893). Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres (PubMed:29656893). May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1 (PubMed:17296730). Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle (PubMed:11459825, PubMed:17719540). Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (PubMed:19443654). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle Cytoplasm Chromosome Note=Recruited to sites of chromosomal double-stranded breaks during G1 and S phase of the cell cycle."}
+{"protein": "MLVYIAGSGAMGCRFGYQISKTNNDVILLDNWEDHINAIKENGLVVTGDVEETVKLPIMKPTEATQEADLIILFTKAMQLPQMLQDIKGIIGKETKVLCLLNGLGHEDVIRQYIPEHNILMGVTVWTAGLEGPGRAHLQGVGALNLQSMDPNNQDAGHQVADLLNKANLNATYDENVVPNIWRKACVNGTMNSTCALLDCTIGELFASEDGLKMVKEIIHEFVIVGQAEGVELNEEEITQYVMDTSVRAAHHYPSMHQDLVQNHRLTEIDFINGAVNTKGEKLGINTPYCRMITELVHAKEAVLNIQ", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ketopantoate reductase family."}
+{"protein": "MPVDLSKWSGPLSLQEVDERPQHPLQVKYGGAEVDELGKVLTPTQVKNRPTSITWDGLDPGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNNISSGTVLSDYVGSGPPKGTGLHRYVWLVYEQEGPLKCDEPILSNRSGDHRGKFKVASFRKKYELGAPVAGTCYQAEWDDYVPKLYEQLSGK", "text": "FUNCTION: HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity). FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family."}
+{"protein": "SYGISSGCFGLKLDRIGTMSGLGCWRLLQDSP", "text": "FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasorelaxant effects. Produces a dose-dependent hypotension in rats, followed by significant increases in concentrations of markers of nitric oxide (NO) formation measured in the plasma and vasorelaxation in a thoracic aortic ring bath. The peptide may exert its hypotensive action, at least in part, through stimulation of NO production. The vasorelaxant effect is endothelium-dependent and does not appear to be mediated by the natriuretic peptide receptor-A, as its action is not modified by isatin (a potent NPR1 antagonist). May act by activating the natriuretic peptide receptor-B (NPR2). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family. Snake NP subfamily."}
+{"protein": "MFKPKKKLGQCFLIDKNFVNKAVESANLTKDDVVLEIGLGKGILTEELAKNAKKVYVIEIDKSLEPYANKLKELYNNIEIIWGDALKVDLNKLDFNKVVANLPYQISSPITFKLIKRGFDLAVLMYQYEFAKRMVAKEGTKDYGRLSVAVQSRADVEIVAKVPPSAFYPKPKVYSAIVKIKPNKGKYHIENENFFDDFLRAIFQHRNKSVRKALIDSSKELNYNKDEMKKILEDFLNTNSEIKNLINEKVFKLSVKDIVNLSNEFYRFLQNRGRL", "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": "MRLALFALFALMTVATALPAHAEKLTLEAITGSAPLSGPTLTKPQIAPDGSRVTFLRGKDRDRNRLDLWEYDIASGQTRLLVDSSVVLPGEEVLSDEEKARRERQRIAALSGIVDYQWSPDGKALLFPLGGELYFYDLTKSGRDAVRKLTNGGGFATDPKISPKGGFVSFIRDRNLWAIDLASGKEVQLTRDGSDTIGNGVAEFVADEEMDRHTGYWWAPDDAAIAFARIDETPVPVQKRYEVYPDRTEVVEQRYPAAGDHNVRVQLGVIAPKTGARPRWIDLGKDPDIYLARVDWRDPQRLTFQRQSRDQKKIELIETTLTNGTQRTLVTETSTTWVPLHNDLRFLKDGRFLWSSERSGFEHLYVASEDGSTLTALTQGEWVVDSLLAIDEAAGLAYVSGTRDGATEAHVYAVPLSGGEPRRLTQAPGMHAATFARNASVFVDSWSSDTTLPQIELFKADGTKLATLLVNDVSDATHPYAKYRAAHQPTAYGTLTAADGTTPLHYSLIKPAGFDPKKQYPVVVFVYGGPAAQTVTRAWPGRSDSFFNQYLAQQGYVVFTLDNRGTPRRGAAFGGALYGKQGTVEVDDQLRGIEWLKSQAFVDPARIGVYGWSNGGYMTLMLLAKHDEAYACGVAGAPVTDWALYDTHYTERYMDLPKANEAGYREASVFTHVDGIGAGKLLLIHGMADDNVLFTNSTKLMSELQKRGTPFELMTYPGAKHGLRGSDLLHRYRLTEDFFARCLKP", "text": "FUNCTION: Catalyzes the sequential release of Tyr-Pro, Phe-Pro and Gly- Pro from the N-terminus of peptides and proteins. Is able to cleaves bioactive peptide beta-casomorphin. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 1]: Periplasm. SIMILARITY: Belongs to the peptidase S9B family."}
+{"protein": "SPAFNSWG", "text": "FUNCTION: Mediates visceral muscle contractile activity (myotropic activity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kinin family."}
+{"protein": "MNEPAKHRLGCTRTPEPDIRLRKGHQLDDTRGSNNDNYQGDLEPSLETPVCSSYYENSPEEPECHDDNSQEDEGFMGMSPLLQAHHAMERMEEFVCKVWEGRWRVIPHDVLPDWLKDNDFLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGCVFFLCLGIFYMFRPNISFVAPLQEKVVFGLFFLGAILCLSFSWLFHTVYCHSEGVSRLFSKLDYSGIALLIMGSFVPWLYYSFYCNPQPCFIYLIVICVLGIAAIIVSQWDMFATPQYRGVRAGVFVGLGLSGIIPTLHYVISEGFLKAATIGQIGWLMLMASLYITGAALYAARIPERFFPGKCDIWFHSHQLFHIFVVAGAFVHFHGVSNLQEFRFMIGGGCTEEDAL", "text": "FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:17327425, PubMed:17068142, PubMed:17268472, PubMed:24742672). Required for normal body fat and glucose homeostasis (PubMed:17327425, PubMed:17068142, PubMed:17268472, PubMed:24742672). ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake (PubMed:12802337, PubMed:17268472, PubMed:24742672). Has intermediate affinity for globular and full-length adiponectin (PubMed:12802337). Required for normal revascularization after chronic ischemia caused by severing of blood vessels (PubMed:24742672). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localized to the cell membrane and intracellular organelles. SIMILARITY: Belongs to the ADIPOR family."}
+{"protein": "MSQPAGGRRKPRTLGPPVCSIRPFKSSEQYLEAMKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTDAALAFLAEAPAQAQKIPMPRVGVSCNGAAQPGTFQARDNVSNFIQWCRKEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRAWRFGVAAPTLVQLEEEIEEEVRRELALPPPDPSPPAPPRRQPCHFRNLDQMVQSLVSHCTCPVQFSMVKVSEGKYRVGDSNTLIFIRILRNHVMVRVGGGWDTLGHYLDKHDPCRCTSLSHKPGSFLKPPAPPVQHEVRVQDGPSQTQPTMTISRSQSPPPPVDWKTYTSSDRRLRPPTPSSPRPRRERGAGTGASREMAPFLRCQERSLIPSWRQPTAGDSPPSPQSSSTQKGRDPQCTSSGKREERYPPELPRGRIPTSWVHEETDSWGTDAGNPTPQRLRAIEATTKGISARGPSPLPRSFGPAECLGLRLPLRDEAKGAFFQFREPESVRSPTPVQGLTKIPIRLPPARPPTPGRSFPGATSGSPRTELGRDPIPLRAVTVDLAGSTHGDCSVEVRQEDQQLDIQVMAEARESWDLGLQEQEGRYTPLPLGGNKEQAIYCSLEEEILGNMKLLEVRSACPQGTRSGVIPRSGVYIPRLAGQWPEPGGPYDKAIQELAQGSPSLLKVDLEAWKAAPTGSPKPAVTPGPGSLKGKLGARQSGPRTKASLSAKGTHMRKVPPQGGQDCSASTVSASPEAPTPSPLDPNSDKAKACLSKGRRTLRKPKRVPSIYKLKLRPRIRPRRDHRPEKQPSRIPRPLAYVFLGPARQPPKDRLLRAVLGSKGGEASRVDGASVGEEEEEGKEEKEPAAPLESSPQPPEGLQPHWLNQAPLPPEEESWV", "text": "FUNCTION: Involved in the cross-linking of microtubules and microfilaments (PubMed:12584248, PubMed:24706950). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (PubMed:24706950). Enhances ADORA2- mediated adenylyl cyclase activation by acting as a scaffold to recruit trimeric G-protein complexes to ADORA2A (By similarity). Regulates ciliary orientation and performance in cells located in the airway (PubMed:30665704). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell membrane Cytoplasm, cytoskeleton, stress fiber Cytoplasm, cytoskeleton, cilium basal body Note=Colocalizes with ADORA2A at neuronal processes (By similarity). Colocalizes with and tracks the tips of microtubule plus ends (PubMed:24706950). SIMILARITY: Belongs to the GAS2 family."}
+{"protein": "XIFPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNL", "text": "FUNCTION: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down- regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity). Interacts with DDX3X; this interaction enhances CSNK1D kinase activity in vitro, but it is unclear whether this interaction is physiologically relevant (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily."}
+{"protein": "MKKFQLFSILSYFVALFLLPMAFASGDDNSTESYGTVIGIDLGTTYSCVAVMKNGRVEIIANDQGNRITPSYVAFTEDERLVGEAAKNQAPSNPENTIFDIKRLIGRKFDEKTMAKDIKSFPFHIVNDKNRPLVEVNVGGKKKKFTPEEISAMILSKMKQTAEAYLGKPVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVIRIVNEPTAAAIAYGLDKTDTEKHIVVYDLGGGTFDVSLLSIDNGVFEVLATSGDTHLGGEDFDNRVINYLARTYNRKNNVDVTKDLKAMGKLKREVEKAKRTLSSQKSVRIEIESFFNGQDFSETLSRAKFEEINMDLFKKTLKPVEQVLKDSNLKKSEIDDIVLVGGSTRIPKVQELLESFFGKKASKGINPDEAVAYGAAVQAGVLSGEEGSDNIVLLDVIPLTLGIETTGGVMTKLIGRNTPIPTRKSQIFSTAVDNQNTVLIQVYEGERTLTKDNNLLGKFDLRGIPPAPRGVPQIEVTFEVDANGVLTVSAVDKSGKGKPEKLVIKNDKGRLSEEDIERMVKEAEEFAEEDKILKERIEARNTLENYAYSLKGQFDDDEQLGGKVDPEDKQAVLDAVEDVAEWLEIHGEDASKEEFEDQRQKLDAVVHPITQKLYSEGAGDADEEDDDYFDDEADEL", "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."}
+{"protein": "SRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPSVDVWLDAIYQESPAKTREYCLHAKLSETKVAARCPTMGPAVLTEEHQIGTVCKRDQSDRGWGNHCGLFGKGSIVACVKAACEAKKKATGYVYDANKIVYTVKVEPHTGDYVAANETHKGRKTTTFTVSSEKTILTLGEYGDVSLLCRVASGVNLAQTIILELDKTAEHLPTAWQVHRDWFNDLALPWKHDGNPHWNNAERLVEFGVPHAVKMDVYNLGDQTGVLLKALAGVPVAHIEGNKYHLKSGHVTCEVGLENLKMKGLTYTMCDKSKFTWKRTPTDSGHDTVVMEVTFSGSKPCRIPVRAVAHGSPDVNVAMLITPNPTIENDGGGFIEMQLPPGDNIIYVGELSHQWFQTGSSIGRVFQTTRKGIERLTVIGEHAWDFGSAGGFFSSIGKAVHTVLGGAFNSIFGGVGFLPKLLMGVALAWLGLNTRNPTMSMSFLLAGGLVLAMTLGVGA", "text": "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 ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane; Multi-pass membrane protein Host endoplasmic reticulum membrane; Multi-pass membrane protein."}
+{"protein": "MLNILNNVSNSSLYSAASNATAQTGSNLINDLVPETLTASGISIAISVFSVIGTIVIALSVLPQTIKTLREKDTASLSLLLFLLNGIATAFLTLYGIGLVTVHPNSFSFLVDIKNGMFIYNREEWVAGYLICGIFLIMGEALCSVTSFIVLFCKVNNMIKAKKMGMSEEEYYEKQIKPFLKVKGAN", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To U.parvum UU008, UU041 and UU042."}
+{"protein": "MVSISASGGYAMPCCCESQELQSSDMETPAVGTPEFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKAMFTCPFSGDCKITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKESLKPKLSEEQQKVINILLEAHHKTFDTTYSDFNKFRPPVRSKFSSSTATHSSSVVSQDFSSEDSNDVFGSDAFGAFPEPMEPQMFSNLDLSEESDESPSMNIELPHLPMLPHLADLVSYSIQKVIGFAKMIPGFRDLTAEDQIALLKSSAIEVIMLRSNQSFTMEDMSWTCGSNDFKYKVSDVTQAGHSMDLLEPLVKFQVGLKKLNLHEEEHVLLMAICILSPDRPGVQDTSLVESIQDRLSDTLQTYIRCRHPPPGSRLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPEHSMQLTPLVLEVFGNEIS", "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": "MSPDRKLITIFGGTGKQGGSVAHSLLQNPDFRVRVITRNAQSDASRKLAALGADIAQGDGFSGDEMLSAFSGSWGAFVNINSDDKIFTTEGGPTEFDMGKIIVDSAVQAGVKHLVFSSGPPCTEMTNGRVRMKAMDMKNKIEQYARSLGSFETFTPIGAGWFLENFLGKEVAPVFGGFPYFPDDQGYLTFRVPYWGGDEHVPWLSISDDFGDIVQGIFLDPGRWNGHFVHGVSDIRSFEQVVADFAAVTGNKARFQPILPTWEAFDTHGIQELEDVKLMFGFTQLTGGRYFGPEDTEVDTARQLKQITGLKLGRPEGQHKLTSARDWFAARFAN", "text": "FUNCTION: NmrA-like family domain-containing oxidoreductase; part of the lna gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine (PubMed:23281040). The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure (PubMed:23281040). One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine (PubMed:23281040). The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines (PubMed:23281040). SIMILARITY: Belongs to the NmrA-type oxidoreductase family."}
+{"protein": "MSVKRRDHILIPKNPDAPLPSLKIEEVGECTIDNIYASPEPFVNGMTMKLSAVKNHGIERDSGEVELAGPMEKIFYNPETTKVAIVTCGGLCPGLNNVIRGLVLNLYNRYHVNNIFGLRWGYEGLVPELSEVQRLTPEIVSDIHQKGGSILGTSRGAQSPEVMAQFLIDNNFNILFTLGGDGTLRGANAINKELRRRKVPITVVGIPKTIDNDICYTDSTFGFQTAVGLSQEAINAVHSEAKSAKNGIGIVRLMGRDAGFIALYASLANGDANLVLIPEIDIPITQICEFVGKRIMSKGHVVIVVAEGALQNQKPKDLDLGTDKSGNILHWDSINYLRDSITKYLKSIGIEEHTIKFVDPSYMIRSAPCSAADAHFCMCLANAAVHVAMAGKTGLVICHHHNNFVSVPIDRTSYYIKRVNTDGPLYTMMTAIEKPK", "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. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily."}
+{"protein": "MADESSDAAGEPQPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQEMEREAEERRGEKGRVLRTRCQPLELDGLGFEELQDLCRQLHARVDKVDEERYDVEAKVTKNITEIADLTQKIYDLRGKFKRPTLRRVRISADAMMQALLGTRAKESLDLRAHLKQVKKEDIEKENREVGDWRKNIDALSGMEGRKKKFEG", "text": "FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. SIMILARITY: Belongs to the troponin I family."}
+{"protein": "MSEEEAAQIPRSSVWEQDQQNVVQRVVALPLVRATCTAVCDVYSAAKDRHPLLGSACRLAENCVCGLTTRALDHAQPLLEHLQPQLATMNSLACRGLDKLEEKLPFLQQPSETVVTSAKDVVASSVTGVVDLARRGRRWSVELKRSVSHAVDVVLEKSEELVDHFLPMTEEELAALAAEAEGPEVGSVEDQRRQQGYFVRLGSLSARIRHLAYEHSVGKLRQSKHRAQDTLAQLQETLELIDHMQCGVTPTAPACPGKVHELWGEWGQRPPESRRRSQAELETLVLSRSLTQELQGTVEALESSVRGLPAGAQEKVAEVRRSVDALQTAFADARCFRDVPAAALAEGRGRVAHAHACVDELLELVVQAVPLPWLVGPFAPILVERPEPLPDLADLVDEVIGGPDPRWAHLDWPAQQRAWEAEHRDGSGNGDGDRMGVAGDICEQEPETPSCPVKHTLMPELDF", "text": "FUNCTION: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE (By similarity). SUBCELLULAR LOCATION: Lipid droplet Cytoplasm Mitochondrion Note=Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm. SIMILARITY: Belongs to the perilipin family."}
+{"protein": "MRLRFWLLIWLLLGFISHQPTPVINSLAVYRHRETDFGVGVRDHPGQHGKTPSPQKLDNLIIIIIGFLRRYTFNVLFCTSCLCVSFLKTIFWSRNGHDGSMDVQQRAWRSNRSRQKGLRSICMHTKKRVSSFRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKPLCNWVRMAAAEHCHSSGLPYWLYLTAETLKNRMGRQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSVDDNIKECPLAPLPPSPLPPSVDDNLKECLFVPLPPSPLPPSVDDNLKECLFVPLPPSPLPPSVDDNLKTPPLATQEAEVEKPPKPKRWRVDEVEQSPKPKRQREAEAQQLPKPKRRRLSKLRTRHCTQAWAIRINP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPIP family."}
+{"protein": "MVSEIKTLVTFFGGTGDLAKRKLYPSVFNLYKKGYLQKHFAIVGTARQALNDDEFKQLVRDSIKDFTDDQAQAEAFIEHFSYRAHDVTDAASYAVLKEAIEEAADKFDIDGNRIFYMSVAPRFFGTIAKYLKSEGLLADTGYNRLMIEKPFGTSYDTAAELQNDLENAFDDNQLFRIDHYLGKEMVQNIAALRFGNPIFDAAWNKDYIKNVQVTLSEVLGVEERAGYYDTAGALLDMIQNHTMQIVGWLAMEKPESFTDKDIRAAKNAAFNALKIYDEAEVNKYFVRAQYGAGDSADFKPYLEELDVPADSKNNTFIAGELQFDLPRWEGVPFYVRSGKRLAAKQTRVDIVFKAGTFNFGSEQEAQEAVLSIIIDPKGAIELKLNAKSVEDAFNTRTIDLGWTVSDEDKKNTPEPYERMIHDTMNGDGSNFADWNGVSIAWKFVDAISAVYTADKAPLETYKSGSMGPEASDKLLAANGDAWVFKG", "text": "FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone. Can utilize either NADP(+) or NAD(+). SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family."}
+{"protein": "MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR", "text": "FUNCTION: Involved in UV protection and mutation. Essential for induced (or SOS) mutagenesis. May modify the DNA replication machinery to allow bypass synthesis across a damaged template (By similarity). FUNCTION: Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair (PubMed:10801133). Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB) (PubMed:10801133). RecA and to a lesser extent the beta clamp-complex may target Pol V to replication complexes stalled at DNA template lesions (PubMed:10801133). SIMILARITY: Belongs to the peptidase S24 family."}
+{"protein": "MTRTKYQQLQPEERMRIEIWKAEDVSLRAMARRLGRAPSTLMRELRRNATARGGYGAMSAQACRTQRLKASRPVAKLAPDGVLWGVVRHFLDQKWSPQEISATLKRAFPDQPDLNVSHETIYNAIYAYPRGELRRQLIACLRQARTKRLPRSRGTDRRGQIPDMVSIHVRPPEVNDRLMPGHWEGDLIKGAGNQSAVGVLVERMSRAVLLVKMPDATAASALAGFTGKLQSLVAPLRQTLTYDQGREMARHAELSAATGVRVYFCDPHSPWQRGTCENTNGLLRQYLPKGTDLSVYSQEELDAIADSLNGRPRKTLNWHSPLQVLAQVLANPTDRLPVQ", "text": "FUNCTION: Required for the transposition of the insertion element. SIMILARITY: Belongs to the transposase IS30 family."}
+{"protein": "MGPQRRLSPAGAALLWGFLLQLTAAQEAILHASGNGTTKDYCMLYNPYWTALPSTLENATSISLMNLTSTPLCNLSDIPPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSVLFPPSGNRSEFPDVKILIAFISYKDFRDMNQTLGDNITVKMYSPSWPNFDYTMVVIFVIAVFTVALGGYWSGLVELENLKAVTTEDREMRKKKEEYLTFSPLTVVIFVVICCVMMVLLYFFYKWLVYVMIAIFCIASAMSLYNCLAALIHKIPYGQCTIACRGKNMEVRLIFLSGLCIAVAVVWAVFRNEDRWAWILQDILGIAFCLNLIKTLKLPNFKSCVILLGLLLLYDVFFVFITPFITKNGESIMVELAAGPFGNNEKLPVVIRVPKLIYFSVMSVCLMPVSILGFGDIIVPGLLIAYCRRFDVQTGSSYIYYVSSTVAYAIGMILTFVVLVLMKKGQPALLYLVPCTLITASVVAWRRKEMKKFWKGNSYQMMDHLDCATNEENPVISGEQIVQQ", "text": "FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in FASLG, ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17557115, PubMed:17965014). 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). Also responsible for the intramembrane cleavage of Fas antigen ligand FASLG, which promotes the release of the intracellular FasL domain (FasL ICD) (PubMed:17557115). Essential for degradation of the invariant chain CD74 that plays a central role in the function of antigen-presenting cells in the immune system (By similarity). Plays a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus envelope glycoprotein gp130 independently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Membrane; Multi-pass membrane protein; Lumenal side Note=Colocalizes with palmitoylated and myristoylated proteins at the plasma membrane. SIMILARITY: Belongs to the peptidase A22B family."}
+{"protein": "MASKDFAIGMILSQIMVGFLGNFFLLYHYSFLHFTRGMLQSTDLTLKHLTIANSLVILSKGIPQTMAAFGLKDSLSDIGCKFVFYVHRVGRAVCTGNACLLSVFQVITISSSEFRWAELKLHAHKYIRSFILVLCWILNTLVNITVPLHVTGKWNSINSTKTNDYGYCSGGSRSRIPHSLHIVLLSSLDVLCLGLMTLASGSMVFILHRLKQQVQHIHGTNLSPRSSPESRVTQSILVLVSTLCYFTRSPPSLHMSLFPNPSWWPLNASALITACFPTVSPFVLMSRHPRIPRLGSACCGRNPQFPKLVR", "text": "FUNCTION: Putative pheromone receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MSSSGMPDLPAPLTNIKIQHTKLFINNEWHDSVSGKTFPVFNPATEEKICEVEEADKEDVDKAVKAAREAFQMGSPWRTMDASERGQLIYKLADLIERDRLLLATLESINAGKIFASAYLMDLDYCIKVLRYCAGWADKIQGRTIPVDGEFFSYTRHEPIGVCGQIFPWNAPMILLACKIGPALCCGNTVIVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKMIQEAAAKSNLKRVTLELGAKNPCIVFADADLDSAVEFAHQGVFTNQGQSCIAASKLFVEETIYDEFVQRSVERAKKYVFGNPLTPGVNHGPQINKAQHNKIMELIESGKKEGAKLECGGGPWGNKGYFIQPTIFSNVTDDMRIAKEEIFGPVQQIMKFKSLDEVIKRANNTYYGLVAGVFTKDLDKAVTVSSALQAGTVWVNCYLAASAQSPAGGFKMSGHGREMGEYGIHEYTEVKTVTMKISEKNS", "text": "FUNCTION: Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class- 1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
+{"protein": "MSNLATVTPIKPHLEVVEHRVAELDDGYTRTANTLLEAVMLSGLTQHQLLIVMAVWRKTYGYNKKIDWIGNEQFAELTGMAPTKCSTAKNELIRMGVLTQVGRQVGMNKNISEWKTKVNGFGKTFTRSVKLTFTKSVKTNLPNQSNTKDNIQKTINTNTPLPPKGGCDEGSKPEKRKPTKINYSEYLAAYNEIVGDRLPHAVEVNSERQRKLKKLIDSLATKNIDGFRAYVKAFMAAARPFHFGDNDRDWVANFDYLLRPKVLIAIREGTL", "text": "SIMILARITY: Belongs to the phage O protein family."}
+{"protein": "MFYFRGCGRWVAVSFTKQQFPLARLSSDSAAPRTPHFDVIVIGGGHAGTEAATAAARCGSRTLLLTHRVDTIGQMSCNPSFGGIGKGHLMREVDALDGLCSRICDQSGVHYKVLNRRKGPAVWGLRAQIDRKLYKQNMQKEILNTPLLTVQEGAVEDLILTEPEPEHTGKCRVSGVVLVDGSTVYAESVILTTGTFLRGMIVIGLETHPAGRLGDQPSIGLAQTLEKLGFVVGRLKTGTPPRIAKESINFSILNKHIPDNPSIPFSFTNETVWIKPEDQLPCYLTHTNPRVDEIVLKNLHLNSHVKETTRGPRYCPSIESKVLRFPNRLHQVWLEPEGMDSDLIYPQGLSMTLPAELQEKMITCIRGLEKAKVIQPDGVLLLLPRMECNGAISAHHNLPLPGYGVQYDYLDPRQITPSLETHLVQRLFFAGQINGTTGYEEAAAQGVIAGINASLRVSRKPPFVVSRTEGYIGVLIDDLTTLGTSEPYRMFTSRVEFRLSLRPDNADSRLTLRGYKDAGCVSQQRYERACWMKSSLEEGISVLKSIEFLSSKWKKLIPEASISTSRSLPVRALDVLKYEEVDMDSLAKAVPEPLKKYTKCRELAERLKIEATYESVLFHQLQEIKGVQQDEALQLPKDLDYLTIRDVSLSHEVREKLHFSRPQTIGAASRIPGVTPAAIINLLRFVKTTQRRQSAMNESSKTDQYLCDADRLQEREL", "text": "FUNCTION: Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the MnmG family."}
+{"protein": "MTAIFNFESLLFVILLTICTCTYLHRQFPALLEKRKEGVTMVFWKCARIGERASPYISLFCVFMALRFIFGSS", "text": "FUNCTION: Involved in the early part of the secretory pathway. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the KISH family."}
+{"protein": "MSEKYVVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVIDIPQNTWIEQPWDMGVVFVPPISGR", "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. FUNCTION: Acts on guanine, xanthine and to a lesser extent hypoxanthine. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily."}
+{"protein": "MTNMKSVEAYQQLDNQNLKKVVGGKYYGNGVHCTKSGCSVNWGEAASAGIHRLANGGNGFW", "text": "FUNCTION: Bacteriocin active against Listeria monocytogenes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family."}
+{"protein": "MDDFERRRELRRQKREEMRLEAERIAYQRNDDDEEEAARERRRRARQERLRQKQEEESLGQVTDQVEVNAQNSVPDEEAKTTTTNTQVEGDDEAAFLERLARREERRQKRLQEALERQKEFDPTITDASLSLPSRRMQNDTAENETTEKEEKSESRQERYEIEETETVTKSYQKNDWRDAEENKKEDKEKEEEEEEKPKRGSIGENQVEVMVEEKTTESQEETVVMSLKNGQISSEEPKQEEEREQGSDEISHHEKMEEEDKERAEAERARLEAEERERIKAEQDKKIADERARIEAEEKAAAQERERREAEERERMREEEKRAAEERQRIKEEEKRAAEERQRIKEEEKRAAEERQRIKEEEKRAAEERQRARAEEEEKAKVEEQKRNKQLEEKKHAMQETKIKGEKVEQKIEGKWVNEKKAQEDKLQTAVLKKQGEEKGTKVQAKREKLQEDKPTFKKEEIKDEKIKKDKEPKEEVKSFMDRKKGFTEVKSQNGEFMTHKLKHTENTFSRPGGRASVDTKEAEGAPQVEAGKRLEELRRRRGETESEEFEKLKQKQQEAALELEELKKKREERRKVLEEEEQRRKQEEADRKLREEEEKRRLKEEIERRRAEAAEKRQKMPEDGLSDDKKPFKCFTPKGSSLKIEERAEFLNKSVQKSSGVKSTHQAAIVSKIDSRLEQYTSAIEGTKSAKPTKPAASDLPVPAEGVRNIKSMWEKGNVFSSPTAAGTPNKETAGLKVGVSSRINEWLTKTPDGNKSPAPKPSDLRPGDVSSKRNLWEKQSVDKVTSPTKV", "text": "FUNCTION: Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, myofibril Cytoplasm, cytoskeleton, stress fiber Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). SIMILARITY: Belongs to the caldesmon family."}
+{"protein": "MFKWAQAALANVAGTKEPIYGPEAIRSVAEEAKTTPYTETTKDDLKWQAMESTCVETQCFYFMTDSGQLAFAQVIYSNVAGIRTTCQFNCKVFSLDGSKPHLWCSTPLNNHEFSEDKTSFYATDCAVELSEDGNSYTIKSLNDERSIVNVTIKRTAPGFKIGTSGTTLFGTDLANPWGSMRHVFWPRCVAEGTIATPDGPVDCKGRAMFVHALQGMKPHHAAAKWNFCNFQGPNYSAVLMQYTTPPSYGSTVVNVGGIVKDNEIIFAGAEGAVTHVAIKGDTENDWPEPTAIKFEWKGTTKDGKQADAVLEGELEDKLDRIDVMAEVPGFVKQIVAGAVGTKPYIYQYAPQKKKLTLKLKLGEEEISEEGYLFSEATFISA", "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": "MGVNDLWQILEPVKQHIPLRNLGGKTIAVDLSLWVCEAQTVKKMMGSVMKPHLRNLFFRISYLTQMDVKLVFVMEGEPPKLKADVISKRNQSRYGSSGKSWSQKTGRSHFKSVLRECLHMLECLGIPWVQAAGEAEAMCAYLNAGGHVDGCLTNDGDTFLYGAQTVYRNFTMNTKDPHVDCYTMSSIKSKLGLDRDALVGLAILLGCDYLPKGVPGVGKEQALKLIQILKGQSLLQRFNRWNETSCNSSPQLLVTKKLAHCSVCSHPGSPKDHERNGCRLCKSDKYCEPHDYEYCCPCEWHRTEHDRQLSEVENNIKKKACCCEGFPFHEVIQEFLLNKDKLVKVIRYQRPDLLLFQRFTLEKMEWPNHYACEKLLVLLTHYDMIERKLGSRNSNQLQPIRIVKTRIRNGVHCFEIEWEKPEHYAMEDKQHGEFALLTIEEESLFEAAYPEIVAVYQKQKLEIKGKKQKRIKPKENNLPEPDEVMSFQSHMTLKPTCEIFHKQNSKLNSGISPDPTLPQESISASLNSLLLPKNTPCLNAQEQFMSSLRPLAIQQIKAVSKSLISESSQPNTSSHNISVIADLHLSTIDWEGTSFSNSPAIQRNTFSHDLKSEVESELSAIPDGFENIPEQLSCESERYTANIKKVLDEDSDGISPEEHLLSGITDLCLQDLPLKERIFTKLSYPQDNLQPDVNLKTLSILSVKESCIANSGSDCTSHLSKDLPGIPLQNESRDSKILKGDQLLQEDYKVNTSVPYSVSNTVVKTCNVRPPNTALDHSRKVDMQTTRKILMKKSVCLDRHSSDEQSAPVFGKAKYTTQRMKHSSQKHNSSHFKESGHNKLSSPKIHIKETEQCVRSYETAENEESCFPDSTKSSLSSLQCHKKENNSGTCLDSPLPLRQRLKLRFQST", "text": "FUNCTION: Endonuclease which resolves Holliday junctions (HJs) by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated. Four-way DNA intermediates, also known as Holliday junctions, are formed during homologous recombination and DNA repair, and their resolution is necessary for proper chromosome segregation (PubMed:19020614, PubMed:26682650). Cleaves HJs by a nick and counter- nick mechanism involving dual coordinated incisions that lead to the formation of ligatable nicked duplex products. Cleavage of the first strand is rate limiting, while second strand cleavage is rapid. Largely monomeric, dimerizes on the HJ and the first nick occurs upon dimerization at the junction (PubMed:26578604). Efficiently cleaves both single and double HJs contained within large recombination intermediates. Exhibits a weak sequence preference for incision between two G residues that reside in a T-rich region of DNA (PubMed:28049850). Has also endonuclease activity on 5'-flap and replication fork (RF) DNA substrates (PubMed:26578604). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. GEN subfamily."}
+{"protein": "MKAVLALATLIGSTLASSCSSTALSCSNSANSDTCCSPEYGLVVLNMQWAPGYGPDNAFTLHGLWPDKCSGAYAPSGGCDSNRASSSIASVIKSKDSSLYNSMLTYWPSNQGNNNVFWSHEWSKHGTCVSTYDPDCYDNYEEGEDIVDYFQKAMDLRSQYNVYKAFSSNGITPGGTYTATEMQSAIESYFGAKAKIDCSSGTLSDVALYFYVRGRDTYVITDALSTGSCSGDVEYPTK", "text": "FUNCTION: This is a base non-specific ribonuclease. SIMILARITY: Belongs to the RNase T2 family."}
+{"protein": "YFAADGSVVPSISDWNLWVPLGILGIPTIWIALTYR", "text": "FUNCTION: One of the components of the bacteriochlorophyll-protein complex in the chromatophore membrane."}
+{"protein": "GLVSSIGRALGGLLADVVKSKEQPA", "text": "FUNCTION: Antimicrobial 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": "MYTPPRWNNKALKWFDERLPVLTVAHKELVVYPAPRNLNYFWNFGSLAGIAMIIMIATGIFLAMSYTAHVDHAFDSVERIMRDVNYGWLMRYMHANGASMFFIVVYVHMFRGLYYGSYKPPREVLWWLGLVILLLMMATAFMGYVLPWGQMSFWGATVITNLFSAIPVVGDDIVTLLWGGFSVDNPTLNRFFSLHYLFPMLLFAVVFLHMWALHVKKSNNPLGIDAKGPFDTIPFHPYYTVKDAFGLGIFLMVFCFFVFFAPNFFGEPDNYIPANPMVTPTHIVPEWYFLPFYAILRAVPDKLGGVLAMFGAILILFVLPWLDTSKVRSATFRPVFKGFFWVFLADCLLLGYLGAMPAEEPYVTITQLATIYYFLHFLVITPLVGWFEKPKPLPVSISSPVTTQA", "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": "MELYLDTANVAEVERLARIFPIAGVTTNPSIVAASKESIWDVLPRLQNAIGEEGTLFAQTMSRDAKGMVEEAKRLNNAIPGIVVKIPVTAEGLAAINLLKKEGIVTLGTAVYSASQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQTLLEHHAPDSMVLAASFKTPRQALDCLLAGCQAITLPLDVAQQMLNTPAVESAIERFEQDWKNAFGNLNL", "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": "MREFIPPASRFIELPDGFAMRRGGALYGARIAYETFGSLNAARDNAVLVLTGLSPDAHAASRPDDPTPGWWEAMVGPGKPVDTDLWHVICVNSLGSCKGSTGPASTDPRTGEPYRLSFPELSIEDIADAAAHTVRALGISRLACVVGASMGGMSALALLARHPELARTHISLSGAVHALPFSIAVRSLQREAIRSDPGWLQGHYDEGEGPRRGMLTARKLGMMTYRSAQEWDCRFGRTRIGERRRADQGRFGPEFEVESYLDFHAQRFADRFDPNSYLYLSHAMDQFDLGDGGGGGGGAPGALSRMRVERALVMGARTDILFPLSQQQEIADGLSAGGADVSFLPVDTPAGHDAFLVDIERFGPPVAKFLAIVA", "text": "FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-serine to yield the activated serine, O-acetyl-L-serine. It prefers L-serine over L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family."}
+{"protein": "MIASLDELYHSELFFLPVMDENARLVGLEIIATFAAEDGAVRMPTELVAPRLSVEEQYCLFVEKLALLETCQHFFIQHKLIAWLNLPPAISDLLLLDSELFSRAARFPFLELAINENYPGLNQGKNNETLANLAMHFPLMLANFGAGEASTKAIFDGLFKRVMLDKNFIQQRAEMISFEPFMHAIVAQISSSCESLMIAGIDTEAMFARAAPLGFSAFQGGLWPPVPVSQLIKLVQR", "text": "FUNCTION: Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD, decreasing its ability to bind DNA, and thus negatively regulates expression of flagellar class II operons, decreasing motility in nutrient-poor medium. Required for resistance to host phagocyte oxidase. Suppresses killing of macrophages, while promoting resistance to hydrogen peroxide. Data regarding c-di-GMP is controversial; suppresses bacterial c-di-GMP levels (PubMed:15882417) but neither synthesizes nor degrades c-di-GMP (PubMed:19376870). FUNCTION: Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD, decreasing its ability to bind DNA, and thus negatively regulates expression of flagellar class II operons, decreasing motility in nutrient-poor medium. Positively regulates expression of the multicellular rdar morphotype behavior, its major regulator CsgD and suppresses motility. Regulates the rdar morphotype and motility indirectly by affecting the expression of the c-di-GMP-dependent phosphodiesterases YciZ and YhjH. Required for resistance to host phagocyte oxidase. Suppresses killing of macrophages, while promoting resistance to hydrogen peroxide. Data regarding c-di-GMP is controversial; suppresses bacterial c-di-GMP levels (PubMed:15882417) but neither synthesizes nor degrades c-di-GMP (PubMed:19376870). FUNCTION: Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD, decreasing its ability to bind DNA, and thus negatively regulates expression of flagellar class II operons, decreasing motility in nutrient-poor medium. Required for resistance to host phagocyte oxidase (By similarity). SIMILARITY: Belongs to the YdiV family."}
+{"protein": "MLHILCQGTPFEIGYEHGSAAKAVIARSIDFAVDLIRGKTKKTDEELKQVLSQLGRVIEERWPKYYEEIRGIAKGAERDVSEIVMLNTRTEFAYGLKAARDGCTTAYCQLPNGALQGQNWDFFSATKENLIRLTIRQAGLPTIKFITEAGIIGKVGFNSAGVAVNYNALHLQGLRPTGVPSHIALRIALESTSPSQAYDRIVEQGGMAASAFIMVGNGHEAFGLEFSPTSIRKQVLDANGRMVHTNHCLLQHGKNEKELDPLPDSWNRHQRMEFLLDGFDGTKQAFAQLWADEDNYPFSICRAYEEGKSRGATLFNIIYDHARREATVRLGRPTNPDEMFVMRFDEEDERSALNARL", "text": "FUNCTION: Isopenicillin-N N-acyltransferase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:2120195, PubMed:2110531, PubMed:1368505). AatA catalyzes the exchange of the alpha-aminoadipyl side chain of isopenicillin N for phenylacetic acid to yield penicillin (PubMed:2120195, PubMed:2110531, PubMed:1368505). This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively (PubMed:23053082). The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin in the peroxisomal matrix (PubMed:1368505) (Probable). FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:1368505, PubMed:2120195, PubMed:2110531). The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine (PubMed:9266851, PubMed:9355751, PubMed:19686863, PubMed:21889568). The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV (PubMed:8416970, PubMed:22777282). Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates (PubMed:9266851, PubMed:21889568). The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus (PubMed:1368505, PubMed:1369045, PubMed:1588566). Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin (PubMed:2120195, PubMed:2110531, PubMed:1368505). This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively (PubMed:23053082). SUBCELLULAR LOCATION: Peroxisome matrix Note=The unprocessed preprotein is translocated inside peroxisomes and regulates its self-processing. SIMILARITY: Belongs to the peptidase C45 family."}
+{"protein": "MYRTHYSSEITEELNGQKVKVAGWVWEVKDLGGIKFLWIRDRDGIVQITAPKKKVDPELFKLIPKLRSEDVVAVEGVVNFTPKAKLGFEILPEKIVVLNRAETPLPLDPTGKVKAELDTRLDNRFMDLRRPEVMAIFKIRSSVFKAVRDFFHENGFIEIHTPKIIATATEGGTELFPMKYFEEDAFLAQSPQLYKQIMMASGLDRVYEIAPIFRAEEHNTTRHLNEAWSIDSEMAFIEDEEEVMSFLERLVAHAINYVREHNAKELDILNFELEEPKLPFPRVSYDKALEILGDLGKEIPWGEDIDTEGERLLGKYMMENENAPLYFLYQYPSEAKPFYIMKYDNKPEICRAFDLEYRGVEISSGGQREHRHDILVEQIKEKGLNPESFEFYLKAFRYGMPPHGGFGLGAERLIKQMLDLPNIREVILFPRDRRRLTP", "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). Is specific for tRNA(Asp) since it aspartylates tRNA(Asn) 3 orders of magnitude less efficiently than tRNA(Asp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily."}
+{"protein": "MDGSSENLPEVEEKGRESSCCSSETTRQEEEEQSPSCTEDFTASPVSSRWSVKNIDGEKKKIRSDSRVSEVEMMKERFSKLLLGEDMSGSGNGVCTALAISNAITNLCATLFGQLWRLEPLPTEKKEMWRREMEWLLCVSDHIVEMTPTWQTFPDGTKLEIMTCRPRSDLYVNLPALRKLDNMLLEILDSFEETEFWYVDQGIMAHESAADGSSSFRKSFQRQEDKWWLPVPRVSPGGLQENSRKQLQHKRDCTNQILKAAMAINSITLADMEIPESYLESLPRKGRSCLGDLIYRYISSDQFSPECLLDCLDLSSEHQAIEIANRVESSIYLWHKRTNSKPATNTKTSWEMVKELMVDADKLELMADRAESLLLSLKQRFPGLPQTALDMSKIQYNKDIGKSILESYSRVLESLAFNIVARIDDLLFVDDLTRHSSDQIPTTLGNNGNDAPKSIAVPVSNYTTPSYSPSKQELRSSITVPPSPSRFKIPHSSSVKRVLTAYVTKNEPRLKNLPLERSSRSSSSERLSLEKCMKESLNVSNLDPGI", "text": "FUNCTION: Guanine-nucleotide exchange factor (GEF) that acts as an activator of Rop (Rho of plants) GTPases by promoting the exchange of GDP for GTP. In postembryonic roots, modulates root stem cell maintenance by regulating the expression of PLT1 and PLT2, which are key transcription factors that mediate the patterning of the root stem cell niche. May connect RopGEF-regulated Rac/Rop signaling and auxin- dependent PLT-regulated root pattern formation. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Interacts with ARAC1/ROP3 on plasma membrane."}
+{"protein": "MNANIRLLKYIVGVSSALFLIFSLISLFETIQNEKLYERDICFDSQCLKFFAEKTSGIVMYFQAFGWLITTFVTVFGVMIALMTYNAGVKNNNNSNYTSHLTMFREFASAELTKRSSIYPEKVNFFRWYRVMFPEAQGGDISVSRDYLEIISRIKCVIEEANAHITEENKDYKYKTHQRKMMAVLDEIGISISNGPKNIFIEVESQILDYIDTINLSFCHSSSVIELSRVKRKYI", "text": "FUNCTION: Membrane component of antiviral defense system Retron Ec48, composed of a non-coding RNA (ncRNA), a reverse transcriptase (RT) and this membrane protein. Expression of this retron confers protection against bacteriophages lambda, T2, T4, T5 and T7. At multiplicity of infection (MOI) of 0.02 cultures grow normally when infected with lambda without collapsing, at MOI 2 cultures enter growth stasis. At MOI 3 cell membranes are permeabilized within 15 minutes of infection but do not lyse, suggesting the phage are not able to finish a replication cycle. Antiviral defense is suppressed by mutations that knockout the lambda gam expression or phage T7 gp5.9 expression; both viral genes inhibit host RecBCD (PubMed:33157039). The Ec48 retron may sense the integrity of the RecBCD enzyme; when RecBCD is perturbed by viral proteins the Ec48 effector (the membrane protein) is activated, leading to abortive infection and bacterial growth arrest (Probable). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
+{"protein": "NLVQFSNMIQCANHGSRPSLAYADYGCYCSAGGSGTPVDELDRCCKTHDDCYARATKSYSCTPYWTLYSWQCIEKTPTCDSKTGCQRFVCDCDATAAKCFAKAPYNKENYNIDPKKRCQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
+{"protein": "MASILHYFLALSLSCSFLFFLSDSVTPTKPINLVVLPVQNDGSTGLHWANLQKRTPLMQVPVLVDLNGNHLWVNCEQQYSSKTYQAPFCHSTQCSRANTHQCLSCPAASRPGCHKNTCGLMSTNPITQQTGLGELGEDVLAIHATQGSTQQLGPLVTVPQFLFSCAPSFLVQKGLPRNTQGVAGLGHAPISLPNQLASHFGLQRQFTTCLSRYPTSKGAIIFGDAPNNMRQFQNQDIFHDLAFTPLTITLQGEYNVRVNSIRINQHSVFPLNKISSTIVGSTSGGTMISTSTPHMVLQQSVYQAFTQVFAQQLPKQAQVKSVAPFGLCFNSNKINAYPSVDLVMDKPNGPVWRISGEDLMVQAQPGVTCLGVMNGGMQPRAEITLGARQLEENLVVFDLARSRVGFSTSSLHSHGVKCADLFNFANA", "text": "FUNCTION: Seed storage protein. Has a protein kinase activity. Binds leginsulin. SIMILARITY: Belongs to the peptidase A1 family."}
+{"protein": "MKGSPVLAVCAAALTLIPSVVALPMIDKDLPSSISQSSDKTSQERAEAVKAAFRFAWEGYLEHAFPNDELHPVSNTPGNSRNGWGASAVDALSTAIIMDMPDVVEKILDHISNIDYSQTDTMCSLFETTIRYLGGMISAYDLLKGPGSHLVSDPAKVDVLLAQSLKLADVLKFAFDTKTGIPANELNITDKSTDGSTTNGLATTGTLVLEWTRLSDITGDPEYGRLAQKGESYLLNPQPSSSEPFPGLVGRTIDIETGLFRDDYVSWGGGSDSFYEYLIKMYVYDKGRFGKYKDRWVTAAESTIEHLKSSPSTRKDLTFVATYSGGRLGLNSGHLTCFDGGNFLLGGQILNRDDFTKFGLELVEGCYATYAATATKIGPEGFGWDATKVPEAQAEFYKEAGFYITTSYYNLRPEVIESIYYAYRMTKDPKYQEWAWDAFVAINATTRTSTGFTAIGDVNTPDGGRKYDNQESFLFAEVMKYSYLIHSPEADWQVAGPGGTNAYVFNTEAHPVKVFSRGC", "text": "FUNCTION: Alpha-mannosidase 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). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 47 family."}
+{"protein": "MSVSQTIVGNGRKIVSFNLQGIDKVLPYIAKRIAWAAKLSGIKTVGPLPLPSTSRQWTVNKSPHTDKHSRDQYEMKVNKRLVQIDAPVQTADMFVKFVQTKLPPISATVDIKIEERVYLPTEDFYSDKRIA", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS10 family."}
+{"protein": "MDLFPILVVVLMTDTVLGKFQIVFPDQNELEWRPVVGDSRHCPQSSEMQFDGSRSQTILTGKAPVGITPSKSDGFICHAAKWVTTCDFRWYGPKYITHSIHHLRPTTSDCETALQRYKDGSLINLGFPPESCGYATVTDSEAMLVQVTPHHVGVDDYRGHWIDPLFPGGECSTNFCDTVHNSSVWIPKSQKTDICAQSFKNIKMTASYPSEGALVSDRFAFHSAYHPNMPGSTVCIMDFCEQKGLRFTNGEWMGLNVEQSIREKKISAIFPNCVAGTEIRATLESEGARTLTWETQRMLDYSLCQNTWDKVSRKEPLSPLDLSYLSPRAPGKGMAYTVINGTLHSAHAKYIRTWIDYGEMKEIKGGRGEYSKAPELLWSQWFDFGPFKIGPNGLLHTGKTFKFPLYLIGAGIIDEDLHELDEAAPIDHPQMPDAKSVLPEDEEIFFGDTGVSKNPIELIQGWFSNWRESVMAIVGIVLLIVVTFLAIKTVRVLNCLWRPRKKRIVRQEVDVESRLNHFEMRGFPEYVKR", "text": "FUNCTION: Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the vesiculovirus glycoprotein family."}
+{"protein": "MEVHPISEFASPFEVFKCIERDFKVAGLLESIGGPQYKARYSVIAWSTNGYLKIHDDPVNILNGYLKDLKLADIPGLFKGGMIGYISYDAVRFWEKIRDLKPAAEDWPYAEFFTPDNIIIYDHNEGKVYVNADLSSVGGCGDIGEFKVSFYDESLNKNSYERIVSESLEYIRSGYIFQVVLSRFYRYIFSGDPLRIYYNLRRINPSPYMFYLKFDEKYLIGSSPELLFRVQDNIVETYPIAGTRPRGADQEEDLKLELELMNSEKDKAEHLMLVDLARNDLGKVCVPGTVKVPELMYVEKYSHVQHIVSKVIGTLKKKYNALNVLSATFPAGTVSGAPKPMAMNIIETLEEYKRGPYAGAVGFISADGNAEFAIAIRTAFLNKELLRIHAGAGIVYDSNPESEYFETEHKLKALKTAIGVR", "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. SIMILARITY: Belongs to the anthranilate synthase component I family."}
+{"protein": "MKWVTFVSLLFLFSSAYSRGVLRRDTHKSEIAHRFNDLGEKHFKGLVLVAFSQYLQQCPFEDHVKLVNEVTEFAKKCAADESAENCDKSLHTLFGDKLCTVATLRATYGELADCCEKQEPERNECFLTHKDDHPNLPKLKPEPDAQCAAFQEDPDKFLGKYLYEVARRHPYFYGPELLFHAEEYKADFTECCPADDKLACLIPKLDALKERILLSSAKERLKCSSFQNFGERAVKAWSVARLSQKFPKADFAEVSKIVTDLTKVHKECCHGDLLECADDRADLAKYICEHQDSISGKLKACCDKPLLQKSHCIAEVKEDDLPSDLPALAADFAEDKEICKHYKDAKDVFLGTFLYEYSRRHPDYSVSLLLRIAKTYEATLEKCCAEADPPACYRTVFDQFTPLVEEPKSLVKKNCDLFEEVGEYDFQNALIVRYTKKAPQVSTPTLVEIGRTLGKVGSRCCKLPESERLPCSENHLALALNRLCVLHEKTPVSEKITKCCTDSLAERRPCFSALELDEGYVPKEFKAETFTFHADICTLPEDEKQIKKQSALAELVKHKPKATKEQLKTVLGNFSAFVAKCCGREDKEACFAEEGPKLVASSQLALA", "text": "FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ALB/AFP/VDB family."}
+{"protein": "MKIFFAILLILAVCSMAIWTVNGTPFAIRCKTDSDCSYKCPGNPPCRNGFCKCT", "text": "FUNCTION: Inhibits potassium channels. May be active towards small conductance calcium-activated potassium channels (KCNN, SK), and less active towards voltage-gated potassium channels (Kv/KCN). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 14 subfamily."}
+{"protein": "MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVSRSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS", "text": "FUNCTION: [Isoform Crk-II]: Regulates cell adhesion, spreading and migration (PubMed:31311869). Mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4 (PubMed:19004829). May regulate the EFNA5-EPHA3 signaling (By similarity). FUNCTION: Involved in cell branching and adhesion mediated by BCAR1- CRK-RAPGEF1 signaling and activation of RAP1. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Translocated to the plasma membrane upon cell adhesion. SIMILARITY: Belongs to the CRK family."}
+{"protein": "MSGPAMVHQEPYSVQATAAIASAITFLILFTIFGNALVILAVLTSRSLRAPQNLFLVSLAAADILVATLIIPFSLANELLGYWYFWRAWCEVYLALDVLFCTSSIVHLCAISLDRYWAVSRALEYNSKRTPRRIKCIILTVWLIAAVISLPPLIYKGDQRPEPHGLPQCELNQEAWYILASSIGSFFAPCLIMILVYLRIYVIAKRSHCRGLGAKRGSGEGESKKPHPAAGGVPASAKVPTLVSPLSSVGEANGHPKPPREKEEGETPEDPEARALPPNWSALPRSVQDQKKGTSGATAEKGAEEDEEEVEECEPQTLPASPASVFNPPLQQPQTSRVLATLRGQVLLSKNVGVASGQWWRRRTQLSREKRFTFVLAVVIGVFVVCWFPFFFSYSLGAICPQHCKVPHGLFQFFFWIGYCNSSLNPVIYTIFNQDFRRAFRRILCRQWTQTGW", "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 Note=Interaction with RAB26, GGA1, GGA2 and GGA3 mediates transport from the Golgi to the cell membrane. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2B sub-subfamily."}
+{"protein": "MAESCEALGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITELLKVRADAEKLKVTDTNRRFQDAGKEVIIQTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSMKRYYSALKTMEQLENVYFPRVSQYRFCQLMMETLPKLREDMMNYCMSDLTYGLESIRKHSDKIGEAAMKQAQQQKSFSVALQKQNNMRFGKNMHVNNDRILEEKSDVIPKHALEEEAENDEEVLTVQDLVDFSPVYRCLHIYSALGDEETFENYYRKQRKKQARLVLQPQSSVHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRVYTEELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFADTLQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGIFRDIFEEDNYSPIPIGSEEEYKVVISRFPFQDPDLEKQSFPKKFPMSQSVPLIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRILSSCLLNLIRKPHIGLTELVQIIINTTHLEQACKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMAESDGRASGYLMDLINFLRSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLRQLLDLFMVWDWSTYLADYGQPASKYLRVNPHAALTLLEKMKDTSKKNNIFAQFRKNDRDRQKLIETVVRQLRGLVTGMSQHT", "text": "FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Cell projection, growth cone Midbody, Midbody ring Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). SIMILARITY: Belongs to the SEC15 family."}
+{"protein": "MDGSMNLGNEPPGDGGGGGGLTRQGSIYSLTFDEFQSSVGKDFGSMNMDELLKNIWSAEETQAMASGVVPVLGGGQEGLQLQRQGSLTLPRTLSQKTVDQVWKDLSKVGSSGVGGSNLSQVAQAQSQSQSQRQQTLGEVTLEEFLVRAGVVREEAQVAARAQIAENNKGGYFGNDANTGFSVEFQQPSPRVVAAGVMGNLGAETANSLQVQGSSLPLNVNGARTTYQQSQQQQPIMPKQPGFGYGTQMGQLNSPGIRGGGLVGLGDQSLTNNVGFVQGASAAIPGALGVGAVSPVTPLSSEGIGKSNGDSSSLSPSPYMFNGGVRGRKSGTVEKVVERRQRRMIKNRESAARSRARKQAYTVELEAEVAKLKEENDELQRKQARIMEMQKNQETEMRNLLQGGPKKKLRRTESGPW", "text": "FUNCTION: Involved in ABA and stress responses and acts as a positive component of glucose signal transduction. Functions as transcriptional activator in the ABA-inducible expression of rd29B. Binds specifically to the ABA-responsive element (ABRE) of the rd29B gene promoter. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. ABI5 subfamily."}
+{"protein": "MSINPITRNKIKDYLNGFIDQQLAVYSQRNLREFHDVDSYLAAISSDGDLKPFHASIIPSAIMRLNRFERSLSTGLGSTFEECARVIALDHHAVAIRSYDIHTSLDQAVWASIDLLISNIDRNNQRQIPSITEMLEKLQSIALTGIAENHVVRADLYVQRHDGSELFFEIKSPKPNKGQCLEVMQRLLRIYAIKQNSTLPTHAFYAMAYNPWGANRASYTYSIVKKYTDFTNAVVIGQEFWSLIGESSTYTELLEIYREVGLSKSSEITKKLL", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGWCC-3' and cleaves after G-1. SIMILARITY: Belongs to the TdeIII type II restriction endonuclease family."}
+{"protein": "MNGDLEVDMSRGDFNPSFFLGKLKDDEFESRSLSDDSFDAMSGDEDKQEQRPKKKKRKTKYHRHTSYQIQELESFFKECPHPNEKQRLELGKKLTLESKQIKFWFQNRRTQMKTQLERHENVILKQENEKLRLENSFLKESMRGSLCIDCGGAVIPGEVSFEQHQLRIENAKLKEELDRICALANRFIGGSISLEQPSNGGIGSQHLPIGHCVSGGTSLMFMDLAMEAMDELLKLAELETSLWSSKSEKGSMNHFPGSRETGLVLINSLALVETLMDTNKWAEMFECIVAVASTLEVISNGSDGSRNGSILLMQAEFQVMSPLVPIKQKKFLRYCKQHGDGLWAVVDVSYDINRGNENLKSYGGSKMFPSGCIIQDIGNGCSKVTWIEHSEYEESHTHSLYQPLLSSSVGLGATKWLATLQRQCESFTMLLSSEDHTGLSHAGTKSILKLAQRMKLNFYSGITASCIHKWEKLLAENVGQDTRILTRKSLEPSGIVLSAATSLWLPVTQQRLFEFLCDGKCRNQWDILSNGASMENTLLVPKGQQEGSCVSLLRAAGNDQNESSMLILQETWNDVSGALVVYAPVDIPSMNTVMSGGDSAYVALLPSGFSILPDGSSSSSDQFDTDGGLVNQESKGCLLTVGFQILVNSLPTAKLNVESVETVNNLIACTIHKIRAALRIPA", "text": "FUNCTION: Probable transcription factor that binds to the DNA sequence 5'-GCATTAAATGC-3' (PubMed:16778018). Seems to promote cell differentiation (PubMed:25564655). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class IV subfamily."}
+{"protein": "MNLIKHAAFAASFQGETDCTSHASARKFSTSGSSPLLDSTEGNGFKGHSMLAPFTAGWHSTDLEPLIIERSEGSYVYDSKGNKYLDTLAGLWCTALGGSEPRLVKAATDQLNKLPFYHSFWNSTAKPPLDLAEELISMFTAKEMGKVFFTNSGSEANDSQVKLVWYYNNALGRPNKKKIIAQSQAYHGSTLISASLSGLPAMHLKFDLPAPFVLHTDCPHYWRFGLPGEAEEEFATRLADNLENLILKEGPETVAAFIAEPVIGAGGVIPPPKTYFEKIQAVLQKYDVLFIADEVITGFGRLGTMFGSDLYNIKPDLVSLAKALSSAYVPIGATLVSPEISDVVHSQSNKIGFFAHGFTYSGHPVSCAVALEALKIYRERNIPAHVKQISPRFQEGIKAFAGSSIIGETRGVGLLLATEFANNKSPNDPFPVEWGVAQIFGAECKKRGMLVKVVGDEIAMSPPLIMSQREVDGLVSIYGEALKATEERVAELRSKKK", "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": "MVGTTTLNTGASLELVGYGTWQAAPGEVGQGVKVAIETGYRHLDLAKVYSNQPEVGAAIKEAGVKREDLFITSKLWNNSHRPEQVEPALDDTLKELGLEYLDLYLIHWPVAFPPEGDITQNLFPKANDKEVKLDLEVSLVDTWKAMVKLLDTGKVKAIGVSNFDAKMVDAIIEATGVTPSVNQIERHPLLLQPELIAHHKAKNIHITAYSPLGNNTVGAPLLVQHPEIKRIAEKNGCTPAQVLIAWAIVGGHSVIPKSVTPSRIGENFKQVSLSQEDVDAVSKLGEGSGRRRYNIPCTYSPKWDINVFGEEDEKSCKNAVKIK", "text": "FUNCTION: Catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. Reduces ethyl 4-chloro-3- oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. SIMILARITY: Belongs to the aldo/keto reductase family."}
+{"protein": "MATGQLFSRNTQALFYNYKQLPIQRMLDFDFLCGRETPSVAGIINPGSEGFQKLFFGQEEIAIPVHAAIEAACAAHPTADVFINFASFRSAAASSMAALKQPTIKVVAIIAEGVPESDTKQLIAYARANNKVIIGPATVGGVQAGAFKIGDTAGTIDNIIQCKLYRPGSVGFVSKSGGMSNEMYNTIARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMVVVLGELGGRDEYSLVEAMKQGKVTKPVVAWVSGTCARLFKSEVQFGHAGAKSGGEMESAQAKNQALQDAGATVPTSFEALEVAIKETFDKLVEEGKVSPIKEVTPPQIPEDLSSAIKSGKVRAPTHIISTISDDRGEEPCYAGVPMSSIIEQGYGVGDVISLLWFKRSLPRYCTKFIEICIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDACDRNLTPYEFVEGMKKKGIRVPGIGHRIKSRDNRDKRVELLQKFARSNFPAVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDEIVQIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYTK", "text": "FUNCTION: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. In contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family."}
+{"protein": "MSPKVQALIFIVGLITLLAAHAQEELSDNIESERGCSGAYKRCSSSQRCCEGRPCVCSAINSNCKCRKTYTELFKEYFGK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family. 05 (U19- lycotoxin) subfamily."}
+{"protein": "MTTMDHRFPSRIFVNERTSITREQLNSLLETYNVFYENQKNLHILYGQTEDGQLIVEGMLDIFWGVKRPIQLKIQDEKQISSFDLLKSPETFSSKGRMTRWGEFDDLYRISEMDKTQALAPEARHTPEDYLSCYSVLKQCADEEPESPLLYRTVSEAALVRKRMRAPEMYRKDRMGTLAKHRASINGHVYDHETSIFTPTFGSETKVRANSIMKTEEVIKQLLQKFKIENSPRDFALYIIFGTGEKRKLKKTDVPLLQRLIQGPSKSNARIFLMDKDAEEISSDVAPYINFHFSFLKSILQRLDEEEKMEIERIMAKFNTERAFILKCLQSKRAAKTETTV", "text": "FUNCTION: Involved in the induction of apoptosis. May act as a Ras effector protein. May suppress the serum-induced basal levels of NF- kappa-B."}
+{"protein": "MEFKYSTLIDPEMYETEGLCDGIPVRYHNNPELEEIDCLRCHEHWRENVGPLGVYKGGLADQWNGISIAIPEALPDRLGVVSYASEFAFVHDDVIDIAQHGNEQNDDLRVGFEQMIDAGAIKYSTSGKRALQSYIAKRMLSIDRERAIISLRAWLEFIEKTGRQEERRFNNEKEFLKYRIYDVGMLFWYGLLTFAQKITIPENELTTCHELAIPAYRHMALLNDLVSWEKERASSIALGKDYCINFIFVAMEESGISEDEAKERCREEIKLATVDYLRVFDEAKDRIDLSHDTMLYLESLLYSMSGNVVWGLQSPRYYTDAKFSQRQLDWIKNGLPLEVRLEDRVFGLSPSEDRVTHQAVIENGLPESGLGKNGNSSNGVDVNKALLSAVLHEHLKGHAVFKMSDHEVKVKASNGRSLDTKVLQAPYEYITGLPSKRLREQAIDAMNVWFRVPAEKLDLIKSITTILHNASLMLDDVEDGSELRRGNPSTHTIFGLSQTINSANYQLVRALERVQKLEDSESLLVFTEELRNLYIGQSMDLYWTGNLICPTMNEYFHMVECKTGGLFRLFTRLMSLHSTSAVKVDPTTLSTRLGIYFQTRDDYKNLVSTEYTKQKGYCEDLEEGKFSLPLIHLIQAMPDNHVLRNILTQWRVTRKVTLAQKQVVLGLMEKSGSLKFTRETLASLYSGLEKSFTELEEKFGTENFQLKLILQFLRTE", "text": "FUNCTION: Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into astellifadiene (PubMed:27038368). The C-terminal prenyltransferase (PT) domain of EvAS catalyzes formation of geranylfarnesyl pyrophosphate (GFPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP to astellifadiene (PubMed:27038368). 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": "MNGSADAGPRPRKYVFITGGVVSSLGKGILTSSLGALLRARGYRVTAIKIDPYVNVDAGTMRPYEHGEVFVTADGAETDLDIGHYERFLDMDLSRGNNLTTGQVYLSVIQKERRGEYLSQTVQVIPHITDEIKERIRKVAEEQKAEIVVVEVGGTVGDIESLPFLEAIRQFRFDEGEGNTLYLHLTLVPYLETSEEFKTKPTQHSVATLRGVGIQPDILVLRSARPVPEEVRRKVALFTNVRPGHVFSSPTVEHLYEVPLLLEEQGLGRAVERALGLEAVIPNLSFWQEAVRVLKHPERTVKIAIAGKYVKMPDAYLSLLEALRHAGIKNRARVEVKWVDAESLEAADLDEAFRDVSGILVPGGFGVRGIEGKVRAAQYARERKIPYLGICLGLQIAVIEFARNVAGLKGANSTEFDPHTPHPVIDLMPEQLEVEGLGGTMRLGDWPMRIKPGTLLHRLYGKEEVLERHRHRYEVNPLYVDGLERAGLVVSATTPGMRGRGAGLVEAIELKDHPFFLGLQSHPEFKSRPMRPSPPFVGFVEAALAYQERA", "text": "FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (PubMed:15296735). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity). SIMILARITY: Belongs to the CTP synthase family."}
+{"protein": "MKIYYIGILRIGGEKALELTSARDLSQFSFFERNGVSQFMTFFSETVSQRTQAGQRQSIEEGNYIGHTYTRSEGLACVIITDKEYPVRPAYTLINKILEEYLSLHPQKDWANISATNASFNYDNLEHYIKKYQDPSQADSIMKVQQELDETKIVLHKTIESVLQRGEKLDSLVDKSEALSSSSRMFYKQAKKTNSCCIIM", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the synaptobrevin family."}
+{"protein": "ATQRLPPLSTEPNR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid."}
+{"protein": "MAVAVASGFWIWAAVLLVPAAAVYEDQVGKFDWRQQYVGKIKFASLEFSPGSKKLVVATEKNVIAALNSRTGEILWRHVDKGTAEGAVDAMLVHGQDAITVSNGGRLMRSWETNIGGLNWEITLDTGSFQALGLVGLQESVRYIAVLKKTTLTLHHLSSGHLKWVEHLPESDSILYQMVYSYGSGVVWALGIVPFSHVNIVKFNVEDGEIVQQVRVWTPWLQHLTGACGVVDEAVLVCPDPSSHSLHTLALETEWELRQIPLQSPDLEFGSGFQPQVLPTQPSPVAPSRAQFFLQLSPSHYALLHYHHGAVTLLKNFPQATLVSFATTGEKTVAAVMTCRTEVQKPVSAGDGSVASFPETSGAQDSLACFNQTYTINLYLVETGRRLLDTSISFSLEQKGTRPEQLYIQVFLKKDDSVGYRALVQTQDHLQLFLQQLAGKVVLWSREESLAEVVCLEMVDLPLTGAQAELEGEFGKKAAIQDGLLGMFLKRLSSQLILLQAWTSHLWKMFYDARKPRSQIKNEINIDTLARDEFNLQKMMVTVTASGKLFGIESSSGTILWKQYLPNVKPDSSFKLMVQRTTAHFPHPPQCTLLVKDKETGMSSLFVFNPIFGKWSQVAPPVLKRPILQSLLLPVMDQDYAKVLLLVDDEYKVTAFPATRNVLRQLHELAPSIFFYLVDAEQGRLSGYQLRKDLTTELSWELTIPPEVQRVVKVKGKRSSEHVHSQGRVMGDRSVLYKSLNPNLLAVVTESTDVHHERTFIGIFLIDGVTGRIIHSSVQKKARGPVHLVHSENWVVYQYWNSKARRNELTALELYEGTEQYNATAFSSLDRPQLPQVLQQSYIFPSSISAMEATITERGITSRHLLIGLPSGAILSLPKALLDPRRPEIPTEQSREENLIPYSPDVQVHAERFINYNQTVSRMRGIYTAPSGLESTCLVVAYGLDIYQTRVYPSKQFDVLKDDYDYVLISSVLFGLVFATMITKRLAQVKLLNRAWR", "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": "MEPYDVVVNQPVVIDNGSGVIKAGFAGEHIPKCRFPNYIGRPKHVRVMAGALEGDIFVGPKAEEHRGLLSIRYPMEHGIVTDWNDMERIWSYIYSKEQLATFTEDHPVLLTEAPLNPRRNREKAAEFFFEGINAPALFVSMQAVLSLYATGRVTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVTRYLKTLIRREGFNFRSTAEFEIVRSIKEKVCYLATNPQKEETVETEKFAYKLPDGKIFEIGPARFRAPEVLFRPDLLGEECEGIHDVLMYSIEKSDMDLRKMLYQNIVLSGGSTLFKGFGDRLLSELKKHSAKDLKIRIAAPQERLYSTWMGGSILASLDTFKKMWISKREYEEEGQKAVHRKTF", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family. ARP1 subfamily."}
+{"protein": "MGYWNSKVVPKFKKLFEKNSAKKAAAAEATKTFDESKETINKEIEEKKTELQPKVVETYEATSAEVKALVRDPKVAGLKKNSAAVQKYLEELVKIEFPGSKAVSEASSSFGAGYVAGPVTFIFEKVSVFLPEEVKTKEIPVEEVKAEEPAKTEEPAKTEGTSGEKEEIVEETKKGETPETAVVEEKKPEVEEKKEEATPAPAVVETPVKEPETTTTAPVAEPPKP", "text": "FUNCTION: May be involved in intracellular signaling through interaction with PtdInsPs and calmodulin (CaM); may keep PtdInsPs attached to the plasma membrane until Ca(2+)-CaM reaches a competitive concentration subsequent to an increase triggered by a stimulus, thus leading to PtdInsPs release and subsequent activation of InsPs- dependent signaling cascade. Interacts competitively at the N-terminus with calcium ions and CaM (in a calcium-dependent manner), and with the phosphatidylinositol phosphates PtdIns(3,4,5)P(3), PtdIns(3,4)P(2), PtdIns(4,5)P(2) and PtdIns(3,5)P(2). Binds also weakly to PtdIns(3)P, PtdIns(4)P and PtdIns(5)P. Negative regulator of hypocotyl cell elongation by destabilizing cortical microtubules in a calcium- dependent manner. Binds directly to and destabilized microtubules to enhance microtubule depolymerization when cytoplasmic calcium increases. In case of Turnip mosaic virus (TuMV) infection, confers sensitivity by promoting viral cell-to-cell movement through interaction with viral P3N-PIPO. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, plasmodesma. Note=Shuttles from plasma membrane to cytoplasm (e.g. colocalizes with cortical microtubules) upon calcium levels increase. Co-localizes with Turnip mosaic virus (TuMV) P3N-PIPO at the plasmodesmata. SIMILARITY: Belongs to the DREPP family."}
+{"protein": "MSYPADDYESEAAYDPYAYPGDYDMHTGDPKQDLAYERQYEQQTYQVIPEVIKNFIQYFHKTVSDLIDQKVYELQASRVSSDVIDQKVYEIQDIYENSWTKLTERFFKNTPWPEAETIAPQVGNDAVFLILYKELYYRHIYAKVSGGPSLEQRFESYYNYCNLFNYILNADGPAPLELPNQWLWDIIDEFIYQFQSFSQYRCKTAKKSEEEIDFLRSNPKIWNVHSVLNVLHSLVDKSNINRQLEVYTSGGDPESVAGEYGRHSLYKMLGYFSLVGLLRLHSLLGDYYQAIKVLENIELNKKSMYSRVPECQVTTYYYVGFAYLMMRRYQDAIRVFANILLYIQRTKSMFQRTTYKYEMINKQNEQMHALLAIALTMYPMRIDESIHLQLREKYGDKMLRMQKGDPQVYEELFSYSCPKFLSPVVPNYDNVHPNYHKEPFLQQLKVFSDEVQQQAQLSTIRSFLKLYTTMPVAKLAGFLDLTEQEFRIQLLVFKHKMKNLVWTSGISALDGEFQSASEVDFYIDKDMIHIADTKVARRYGDFFIRQIHKFEELNRTLKKMGQRP", "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. 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit L family."}
+{"protein": "MQKDASSSGFLPSFQHFATQAIHVGPEPEQWSSRAVVLPISLATTFKQDSPGQSSGFVYSRSGNPTRNCLEKAVAALDGAKHCLTFARGLAATTTITHLLKAGDEVICMDEVYGGTNRYFRRVASEFGLKISFVDCSKTKLLEAAITPQTKLVWIETPTNPTLKLADIKACAQIVHKHKDIILVVDNTFMSAYFQRPLALGADICMCSATKYMNGHSDVVMGLVSVTSDDLNERLRFLQNSLGAVPSPFDCYLCCRGLKTLQIRMEKHFRNGMAVARFLESNPRVEKVIYPGLPSHPQHELAKRQCTGCPGMVSFYIKGTLQHAQVFLKNIKLFALAESLGGYESLAELPAIMTHASVPEKDRATLGISDTLIRLSVGLEDEKDLLEDLGQALKAAHP", "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 (Probable) (PubMed:13525371). 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. 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. By generating the gasotransmitter H2S, it participates in a number of physiological processes such as vasodilation, bone protection, and inflammation (By similarity). Plays an essential role in myogenesis by contributing to the biogenesis of H2S in skeletal muscle tissue (By similarity). Can also accept homoserine as substrate (PubMed:13525371). Catalyzes the elimination of selenocystathionine (which can be derived from the diet) to yield selenocysteine, ammonia and 2-oxobutanoate (Probable). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
+{"protein": "MDLFFAYMFVASATPLFLWLEHRKIALASIPFIIVMWVLALAHIFDGFLFDLHHSAFVTAFLINVFIAHFAALVLYVYPHLRSKSRRFTQSTE", "text": "FUNCTION: Required for proper spore morphogenesis. Important for spore germination (By similarity). SUBCELLULAR LOCATION: Spore membrane; Multi-pass membrane protein Spore outer membrane; Multi-pass membrane protein Cell membrane. SIMILARITY: Belongs to the YwcE family."}
+{"protein": "MDQEESRVISIFETLGAYFINIFYNFLYKNALYKKHSIVTEYQYQVKGYILGVKQNKKLYEKMLDSFYKYFCNITQINSKTLNFSNFVSTIVDSFIPKEYSQSISLEKKESILELLLCDYISNLGTFITTEKMLPFIIKNRKENYHKVTKEMQDYSLTFLLKKRMELYNKFLRKQAYVEPETELEETYARLSSYNRSLLHQIEELTSENKSLLADLSTLRKKYEKRQSEYRRLVQLLYQQIQRSSTSKSSYPLTKFIETLPSEHFSNEEYQKETPADQKEVVETELLRKQELLTSQELTSKSPNNYPVPHSRTIVSKPSDNYPVPRSRTTKIDFDNSLQNQELHTKNGFSEKDIVEFSQDKPEEENILAIKQDNPEEEDILAIKQDNPEEEDILEFNQDKPEFNQDKPEFKEAVLDIKENILEEENQDEPIVQNPFLENFWKPEQKTFNQSGLFEESSNFSNDWSGGDVTLNFS", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the asfivirus B475L family."}
+{"protein": "MKEKILLGGYTKRVSKGVYSVLLDSKKAELSALTEVAAVQNPTYITLDQKGHLYTCAADGNGGGIAAFDFDGQNTTHLGNVTSTGAPLCYVAVDEARQLVYGANYHLGEVRVYKIQADGSLRLTDTVKHNGSGPRPEQASSHVHYSDLTPDGRLVTCDLGTDEVTVYDVIGEGKLNIVTIYRAEKGMGARHISFHPNGKIAYLVGELNSTIEVLSYNEEKGRFARLQTISTLPEDYHGANGVAAIRISSDGKFLYASNRGHDSLAIYKVSPLGTKLESIGWTKTEGHIPRDFNFNKTEDYIIVAHQESDNLTLFLRDKNTGSLTLEQKDFYAPEITCVLPL", "text": "SIMILARITY: Belongs to the cycloisomerase 2 family."}
+{"protein": "MLSGDIPPNQTVYLRNLNEKVKKEELKRSLYALCSQYGRILDVVALKTPKLRGQAWVVFSEITAATNAFRGLQEFDFYGKRMRVQYAKTRSDCLATEDGSTAPKEKRKKQEEKAAEKKRRAEEAQQSGPNAAAQSNGTGYQASRLGKTSQEPPAPPNNILFIQNLPAETTSMMLQILFQQYPGFREVRMIEAKPGIAFVEYEDDSQSMVAMQALQGFKITPYNPMAISYAKK", "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. Also detected in central nucleolar vacuole. SIMILARITY: Belongs to the RRM U1 A/B'' family."}
+{"protein": "MGYDEAIIHLGDFGRYQKIIYFLICLTSIPVAFHKLAGVFLLAKPDFRCALPFENGSSYDLPTHLWNLSYPENERCSYYDVDYTEEYLNGSIPRSSNETKTCSSYVYDRSKYLNSAVTEWNLVCGRDFMAATSDSLFMLGVLLGSIVFGQLSDKYGRKPILFASLVIQVLFGVLAGVAPEYFTYTFARLMVGATTSGVFLVAYVVAMEMVGPDKRLYAGIFVMMFFSVGFMLTAVFAYFVHDWRWLQIALTLPGLIFMFYYWIIPESARWLLLKGRKDCAIANMQKAARFNKVEISDEALSELLDEGENSEEKAKQKLEDQELDEGPPPSVWDLFCYPNLRRKTLLIFLDWLVTSGVYYGLSWNTSNLGGNVLLNFVISGAVEIPAYIFLLLTLNRWGRRSILCGCLVMAGLSLLATVIIPQRMHTLIVACAMLGKLAITASYGTVYIFSAEQFPTVVRNVALGAASMVARISGMMAPFLNFLATIWKPLPLLICGSLTLVAGLLSLLLPETHNKPMLETIADGERFGKKTKADVYLETGQELRAPEAQPLKGSGETNGSTIANGHK", "text": "FUNCTION: Probably transports organic cations. SUBCELLULAR LOCATION: 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": "MFGAAGRQPIGAPAAGNSWHFSRTMEELVHDLVSALEESSEQARGGFAETGDHSRSISCPLKRQARKRRGRKRRSYNVHHPWETGHCLSEGSDSSLEEPSKDYRENHNNNKKDHSDSDDQMLVAKRRPSSNLNNNVRGKRPLWHESDFAVDNVGNRTLRRRRKVKRMAVDLPQDISNKRTMTQPPEGCRDQDMDSDRAYQYQEFTKNKVKKRKLKIIRQGPKIQDEGVVLESEETNQTNKDKMECEEQKVSDELMSESDSSSLSSTDAGLFTNDEGRQGDDEQSDWFYEKESGGACGITGVVPWWEKEDPTELDKNVPDPVFESILTGSFPLMSHPSRRGFQARLSRLHGMSSKNIKKSGGTPTSMVPIPGPVGNKRMVHFSPDSHHHDHWFSPGARTEHDQHQLLRDNRAERGHKKNCSVRTASRQTSMHLGSLCTGDIKRRRKAAPLPGPTTAGFVGENAQPILENNIGNRMLQNMGWTPGSGLGRDGKGISEPIQAMQRPKGLGLGFPLPKSTSATTTPNAGKSA", "text": "FUNCTION: Enhances the ATPase activity of DHX15 in vitro. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, nucleolus."}
+{"protein": "MNEKKKDSLSVLDSNEFFGETTMVSPSIDVSSSPRPNVERFSPCSTKKDLLEGNNIMTRIPEELSRVSLQFDSKGSQQSMIFTNNRCLSDKENLENLQNLLYLHCDLNRPHLSCELPSEHREKCLKRRNSSLSSNLHANKRFLFNSQSDGNKKNETFPSTNYSNVFYPNNCDSKEVASETTFSLDAPNNSVNYSYFSPNLLGNDSKTRQSFPPHSSSSSHNSLHEPVIYDFSSENPSIHPSNHLSSQKNAVLKLAQLISSFEKLPESVRQYLLFHLLSRCGKHAVQNIHKILLPIFQKNFLTGFPAEITNLVLTHLDAPSLCAVSQVSHHWYKLVSSNEELWKSLFLKDGFFWDSIDSKIRTMCLEQSLSACAIMKRVYFRHFNLRERWLHAPEKIKRCSFPIHGVRLITKLQFDDDKIIVSTCSPRINIYDTKTGVLIRSLEEHEGDVWTFEYVGDTLVTGSTDRTVRVWDLRTGECKQVFYGHTSTIRCIKIVQGNQSTTDTDDVEKENRPASNDANSMPPYIISSSRDCTIRLWSLPCLDDPPFVNVNENPDQNNDFTSATTNPFYIRTLRGHTDSVREVACLGDLIVSASYDGTLRVWKASTGVCLHVLRGHVGRVYSVTINPSRQQCISAGTDAKIRIWNLESGELLQTLHGHSNLVSQVTFNQNILVSASAPPDTSLRVWDLNTGSCRDILKCPLGHIFFQHDESKVVSGSHSTLQLWDIRSGKLVRDLLTDLDIIWQVAYNENVCVAAVLRNNRFWIEVLEFGSTKSS", "text": "FUNCTION: Involved in maintenance of ploidy through proteasome dependent degradation of CDK inhibitor rum1 and S-phase initiator cdc18. Functions as a recognition factor for rum1 and cdc18, which are subsequently ubiquitinated and targeted to the 26S proteasome for degradation. Together with pop2, required for cig2 instability during G2 and M phase and cig2 degradation in exponentially growing cells. Regulates cell-cycle progression under starvation through the rum1 protein. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MPLLPAALTSSMLYFQMVIMAGTVMLAYYFEYTDTFTVNVQGFFCHDSAYRKPYPGPEDSSAVPPVLLYSLAAGVPVLVIIVGETAVFCLQLATRDFENQEKTILTGDCCYINPLVRRTVRFLGIYTFGLFATDIFVNAGQVVTGNLAPHFLALCKPNYTALGCQQYTQFISGEEACTGNPDLIMRARKTFPSKEAALSVYAAMYLTMYITNTIKAKGTRLAKPVLCLGLMCLAFLTGLNRVAEYRNHWSDVIAGFLVGISIAVFLVVCVVNNFKGRQAENEHIHMDNLAQMPMISIPRVESPLEKVTSVQNHITAFAEVT", "text": "FUNCTION: Induces filopodia formation and promotes neurite growth in a CDC42-independent manner; impedes neurite growth inhibitory-mediated axonal retraction. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family."}
+{"protein": "MIGYQIYVRSFRDGNFDGVGDFKGLKGAISYLKELGVDFVWLMPVFSSISFHGYDVVDFYSFKAEYGDEKDFREMIEAFHDNGIKVVLDLPIHHTGFLHTWFQKALKGDPHYRDYYVWASEKTDLDERREWDNERIWHPLEDGRFYRGLFGPLSPDLNYDNPQVFEEMKKVVYHLLEMGVDGFRFDAAKHMRDTLEQNVRFWRYFLSDIEGIFLAEIWAESKVVDEHGRIFGYMLNFDTSHCIKEAVWKENFKVLIESIERALVGKDYLPVNFTSNHDMSRLASFEGGLSEEKVKLSLSILFTLPGVPLIFYGDELGMKGIYRKPNTEVVLDPFPWSENISLEGQTFWKWPAYNSPFSGVSVEYQKKKRDSILLHIMKWTGFRKENHWLDRANIEFLCKEEKLLHVYRLVDEGRSLKVIHNLSNGEMVFEGVRVQPYSTEVI", "text": "FUNCTION: Hydrolyzes the 1,4-alpha-glycoside bonds in oligomeric and polymeric 1,4-alpha-glucans and transfers oligosaccharides (maltotriose being the shortest one) to acceptor maltodextrins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
+{"protein": "MMQPSIKPADEHSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQDQMEKSAKALTQRWDDWFADPIDLADARELVTDTRQFLADVPAHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQESRPKRENQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF", "text": "FUNCTION: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). FUNCTION: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Note=Colocalizes with CheA chemoreceptor patches near the cell poles, which requires CheA(short). SIMILARITY: Belongs to the CheZ family."}
+{"protein": "HRVYVEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSNIDNKISTFWNESPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRSGFYLAFQDYGACMSLLSVRVFFKKCPSVVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGKCTCKAGYEPENHVVCKACPAAMFKANQGMGICAQCPANSRSTSEASPICICRNGYYRADFDTPEAPCTSVPSGPRNVISIVNETAITLEWHPPRETGGRDDVNYNIICKKCQSDRRGCSHCDDNVDFVPRQLGLTDTRVFISNLWVHTPYTFEIQAVNGVTNKSPFPPQHVSVNITTNQAAPSSVPIMHQVKATMKSITLSWPQPEQPNGIILDYEIRYYEKDHHEFNSSLARSQTNTASIEGLRPGVVYVVQVRARTVAGYGKFSSKMCFQTLTEEDYKSELREQLPLIAGSAAAGVVFIVSLVAISIVCSRKRTYSKEAVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPSKREISVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIRYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFGEIVNTLDKMIRNPASLKTVATIPAVPSQPLLDRSIPDISAFTSVDDWLSAIKMGQYRDNFLSSGFTSLHVVAQMTSEDLLRIGITLAGHQKKILNSIQSMRVQISQSPTSIA", "text": "FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B 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. May play a role in axon guidance during nervous system development. May also play an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. More generally, may play a role in targeted cell migration and adhesion. Upon activation by ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Early endosome membrane; Single-pass type I membrane protein Cell projection, dendrite. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily."}
+{"protein": "MLTPRVLRALGWTGLFFLLLSPSNVLGASLSRDLETPPFLSFDPSNISINGAPLTEVPHAPSTESVSTNSESTNEHTITETTGKNAYIHNNASTDKQNANDTHKMPNILCDTEEVFVFLNETGRFVCTLKVDPPSDSEWSNFVLDLIFNPIEYHANEKNVEAARIAGLYGVPGSDYAYPRQSELISSIRRDPQGTFWTSPSPHGNKYFIWINKTTNTMGVEIRNVDYADNGYMQVIMRDHFNRPLIDKHIYIRVCQRPASVDVLAPPVLSGENYKASCIVRHFYPPGSVYVSWRQNGNIATPRKDRDGSFWWFESGRGATLVSTITLGNSGIDFPPKISCLVAWKQGDMISTTNATAIPTVYHHPRLSLAFKDGYAICTIECVPSEITVRWLVHDEAQPNTTYNTVVTGLCRTIDRHRNLLSRIPVWDNWTKTKYTCRLIGYPFDEDKFQDSEYYDATPSARGTPMVITVTAVLGLAVILGMGIIMTALCLYNSTRKNIRL", "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": "MCKKRNAEINAEFDIIKKYCIYIGNIPFFASKNDVVVKFAEYGETCNIYMQSNKPHCDVKPAIVRYRSRKSVDKSLCLNNSKFGNTILIVLPLSLPYSRYLLTYDTCIVVYINDKNSCKTSMAELYDEFQKIGDIQNMFKTTNNMIYINFESEKSMQLSLATKPFLINNNIFKIKKVERNINMCGLNSESQDFSTNLKKKLLYNRSIGIFGLPSNATEERIAQIFSRFGDIQKITLICDVVGNSKQYGFIYYKKRTSANAAKVIMDGENFEGNKISVRFVPEKKVFKN", "text": "FUNCTION: Male determiner protein (M-factor) that controls male somatic sexual differentiation. Acts as a dominant factor that regulates the mRNA splicing of doublesex (dsx) or fruitless (fru) transcripts and promotes expression of male splice forms of dsx and fru."}
+{"protein": "MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD", "text": "FUNCTION: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR) (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). 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 (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). Recruited to resolve stalled replication forks during replication stress (PubMed:27797818, PubMed:31844045). Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR (PubMed:24141787, PubMed:12442171). Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3 (PubMed:20413593). Also involved in interstrand cross-link repair (PubMed:26253028). 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 (PubMed:20154705). DNA damage induces an increase in nuclear levels (PubMed:20154705). Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment (PubMed:23754376). Accumulated at sites of DNA damage in a SPIDR- dependent manner (PubMed:23509288). Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner (PubMed:23401855). Colocalizes with ERCC5/XPG to nuclear foci in S phase (PubMed:26833090). Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner (PubMed:27797818, PubMed:31844045). SIMILARITY: Belongs to the RecA family. RAD51 subfamily."}
+{"protein": "MFSSFETLILSFVSLFFMMIFIHSKWISSYSKMAKNLPPSPFGLPIIGNLHQLGMTPYNSLRTLAHKYGSLMLIHLGSVPVIVASSAEAAQEIMKTHDQIFSTRPKMNIASIVSFDAKIVAFSPYGEHWRQSKSVYLLNLLSTKRVQSFRHVREDETNLMLDVIENSCGSEIDLSNMIMSLTNDVVCRIAYGRKYYEDWFKELMKEVMDVLGVFSVGNYVPSLSWIDRLSGLEGRAYKAAKQLDAFLEGVVKQHETKSNESMRDQDVVDILLETQREQASAGTPFHRDTLKALMQEMFIAGTDTTSTAIEWEISEVIKHPRVMKKLQQELDEIAQGRQRITEEDLEDTQHPYLEAILKESMRLHIPVPLLLPREATHDVKVMGYDIAAGTQVLINAWMIARDPTIWEDADEFKPERFLDTNIDYKGLNFELLPFGAGRRGCPGIQFAMSVNKLALANLVYKFDFKLPNGLRLEQLDMTDSTGITVRRKYPLLVIPTARF", "text": "FUNCTION: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones (PubMed:30468448). Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti- cancer drugs highly active against colon cancer cells (PubMed:30468448). Catalyzes the conversion of costunolide and parthenolide to 3-beta-hydroxycostunolide and 3-beta- hydroxyparthenolide, respectively (PubMed:24704560). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "MDADDTPPNLQISPTAGPLRSHHNTDGHEPNATAADQQERESTNPTHGCVNHPWANPSTATCMESPERSQQTSLFLLKHGLTRDPIHQRERVDVFPQFNKPPWVFRISKLSRLIVPIFTLNEQLCFSKLQIRDRPRFAGRGTYGRVHIYPSSKIAVKTMDSRVFNRELINAILASEGSIRAGERLGISSIVCLLGFSLQTKQLLFPAYDMDMDEYIVRLSRRLTIPDHIDRKIAHVFLDLAQALTFLNRTCGLTHLDVKCGNIFLNVDNFASLEITTAVIGDYSLVTLNTYSLCTRAIFEVGNPSHPEHVLRVPRDASQMSFRLVLSHGTNQPPEILLDYINGTGLTKYTGTLPQRVGLAIDLYALGQALLEVILLGRLPGQLPISVHRTPHYHYYGHKLSPDLALDTLAYRCVLAPYILPSDIPGDLNYNPFIHAGELNTRISRNSLRRIFQCHAVRYGVTHSKLFEGIRIPASLYPATVVTSLLCHDNSEIRSDHPLLWHDRDWIGST", "text": "FUNCTION: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factor proteins 24 and 27, by phosphorylating the protein kinase ORF66, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI) (By similarity). Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator IE63. FUNCTION: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factor proteins 24 and 27, by phosphorylating the protein kinase ORF66, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI). Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator IE63 (By similarity). SUBCELLULAR LOCATION: Virion tegument Host nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
+{"protein": "MAEKPKRPLSAYMLWLNSARESIKKENPDFKVTEIAKKGGELWRGMKDKSEWEAKAAKMKEEYEKAMKEFERNGGDKSSGASTKKRGKAAEKKKPAKKSKKKDSEDDEEEDESD", "text": "FUNCTION: Found in condensed chromomeres. Binds preferentially to AT- rich DNA. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the HMGB family."}
+{"protein": "MDLWQLLLTLAVAGSSDAFSGSEATPAVLVRASQSLQRVHPGLETNSSGKPKFTKCRSPELETFSCHWTDGVRHGLQSPGSIQLFYIRRSTQEWTQEWKECPDYVSAGENSCYFNSSYTSIWIPYCIKLTSNGGTVDQKCFSVEEIVQPDPPIGLNWTLLNISLTGIHADIQVRWEPPPNADVQKGWIVLEYELQYKEVNETQWKMMDPVLSTSVPVYSLRLDKEYEVRVRSRQRNSEKYGEFSEVLYVTLPQMSPFACEEDFRFPWFLIIIFGIFGLTVILFLLIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDNYKHEFYSDDSWVEFIELDIDDPDEKTEGSDTDRLLNNDHEKSLTILGAKEDDSGRTSCYEPDILETDFNANDVCDGTAEVAQPQRLKGEADLLCLDQKNQNNSPSNDAAPATQQPSVILAEENKPRPLIISGTDSTHQTAHTQLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKNKAGISQCDMHLEVVSPCPANFIMDNAYFCEADAKKCIAMAPHVEVESRLAPSFNQEDIYITTESLTTTAGRSATAECAPSSEMPVPDYTSIHIVQSPQGLVLNATALPLPDKEFLSSCGYVSTDQLNKIMP", "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: 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. SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted Note=Complexed to a substantial fraction of circulating GH. SIMILARITY: Belongs to the type I cytokine receptor family. Type 1 subfamily."}
+{"protein": "MDEVYLYSDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTSHIVFVVHGIGQKMDQGRIIKNTAMMREAARKMEEKHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLRDMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPDFEEKGGKVSIVSHSLGCVITYDIMMGWNPGGLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLREIEDRLHGLKAPSISQTPALKFKVENFFCMGSPLAVFLALRGIRPGNSGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEHMKPNFLNPAKEPTSVSDSENIAAIPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSASQPSEPSKDSLEDDKKPSASPSTTTVATQTLPHSGSGFLDSAYFRLQESFFYLPQLLFPENVMQSKDDSLVELEHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDTEAKPSLGSL", "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:30221923). 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:30221923) (By similarity). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system (PubMed:30221923). Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (PubMed:30221923). 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": "MNPSLCIAVAFACPLSALAASGAPGVGFNEKPSFLGEIVQRSVDGVSDDLLTAGLGRDGIQSATPPLVSASPTATELRRLAIYNNYRALVDTTSGGGFGSLFGPLIAVDAGGRVSAPGDGKIAGTEYLAYAIDRGDDSKVTLMVQVPAHFNPKAPCIVTGTSSGSRGIYGAIGTSGEWGLQKGCAVAYADKGTGNGMHDLDTNTVGLIDGTRADAVAAGVASHFTADLTEAERTQFLASWPHRVAVKHAHSRANPEAHWGQDTLDAVRFAFFVLNETYGRRTPRGIVRTILPPNTVVIASSVSNGGGAALAAAEQDDERLIDGVAVGEPQIQLRENDAVRVVRGSQVRTGTGRPLYDYTTFANLLQPCAVLSPRAAGSPGEAFIPAALAANRCEALAAHEFITGNTPAERGDSALDALVAYGWEPESTPLTASHYAFAVPPIALTYANAYGRFGVEERVCNYSFAATDAAGTPIAWPAASAATSFGTGNGIPPAAGLQIINDASLGGPRRDGASISPSTGKLDFNVDGALCLRQLWTGGGASAREVHESVDEVQVSAQLQGRPAIIVHGRADALVPVGFTSRPYLGLNSLAEHGRSRLRYVEVTNAQHFDAFIGTATLPGYDTRFVPLHVYFRQALDLMYSHLTARTPLPPSQLVRTTPRAGTPGAAVAITAANVPPIRMKPAAADLITVRRGEVVVPD", "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": "MAGPGEYFAIGAYVSCRTCQETRLQGEVVAFDYPSKMLALKCPSSSGKANHADILLLNLDYVSDVEVINERTQTPPPLASLNITKLASRARLEKEEKLSQAYAISAGVSLDGQQLFQTIHKTIKDCKWQEKNIVVMDEVVISPPYQVENCKGKEGRALTHVCKIVEKHFRDVENQKGVQRNPVAQSQKETSTSS", "text": "FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP) binding protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LSM12 family."}
+{"protein": "MPGAAAKGSELSERIESFVETLKRGGGRRTSEDMARETLGLLRRLITDHHWNNAGDLMDLIRREGRRMTAAHPPETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLSEDFSFHYAPLKSNIIEAINELLVELEGTTENIAAQALEHIHSNEVIMTIGFSRTVEAFLREAAQKRKFHVIAAECAPFCQGHEMAVNLSEAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGSLRAVAGTHTLALAAKHHSTPLIVCAPMFKLSPQFPSEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPDLITLFISNIGGNAPSYVYRLMSELYHPDDHVL", "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": "MQTPKRRRGAQGCPRSSPSPPLLLLVGAVWFCAALSVAAGSFELTILHTNDVHARVEQTSRDSGKCTGQDCYGGVARRATKIRELRANHSHVLLLDAGDQYQGTIWFSFFKGREVVKFMNSLGYDAMALGNHEFDNGLAGLLDPLLKHANFPILSANIRPKGSIASNISGYILPYKIINVGSEKVGIIGYTTKETPVLSNPGPYLEFRDEVEELQKHANKLTTLGVNKIIALGHSGFFEDQRIARKVKGVDVVVGGHTNTFLYTGSPPSTEVAAGNYPFMVKSDDGRQVPVVQAYAFGKYLGYLNVIFDDKGNVIKSSGNPILLNKNISEDQDVKAEVNKMKIQLHNYSSQEIGKTIVYLNGTTQACRFHECNLGNLICDAVIYNNVRHPDYNEWNHVSMCIVNGGGIRSPIDERANNGTITLEELTAVLPFGGTFDLLQIKGCALKQAFEHSVHRHGQGMGELLQVSGIKVVYDLSRKPGSRVVSLNVLCTECRVPTYVPLEKEKTYKLLLPSFLAGGGDGYHMLKGDSSNHSSGNLDISIVGDYIKRMGKVFPAVEGRVIFSAGTLFQAQLFLTWGLCISLLYFIL", "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": "MADKTKILIIGGTGYIGKFIVEASAKSEHPTFALARESTISDPVKGKIIQGFKNSGVTILTGDLYDHESLVKAIKQVDVVISTVGQLQLADQVKIIAAIKEAGNVKRFFPSDFGTDVDRCHAVEPAKSSFEIKSQIRRAIEAEGIPYTFVSANYFAGYSLPTLVQPEVTAPPRDKVIILGDGNAKAVFNEENDIGTYTIKAVDDARTLNKILYIKPPKNIYSFNELVALWEKKIGKTLEKIYVPEEQVLKQIQESPFPINIVMAINHSAFVKGDLTNFKIEPSFGVEASELYPDVKYTTVEEYLDQFV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily."}
+{"protein": "MMVKLRNLVLFFMLLTVVAHILLYTDPAASFKTPFSKRDFLEDVTALTFNSDENRLNLLPRESPAVLRGGLVGAVYSDKNSRRLDQLSARVLSATDDDTHSHTDISIKQVTHDAASDSHINRENMHVQLTQQTSEKVDEQPEPNAFGAKKDTGNVLMPDAQVRHLKDQLIRAKVYLSLPSAKANAHFVRELRLRIKEVQRALADASKDSDLPKTAIEKLKAMEQTLAKGKQIQDDCSTVVKKLRAMLHSADEQLRVHKKQTMFLTQLTAKTIPKGLHCLPLRLTTDYYALNSSEQQFPNQEKLEDTQLYHYALFSDNVLATSVVVNSTITNAKHPLKHVFHIVTDRLNYAAMRMWFLDNPPGKATIQVQNVEEFTWLNSSYSPVLKQLSSRSMIDYYFRAHHTNSDTNLKFRNPKYLSILNHLRFYLPEIFPKLSKVLFLDDDIVVQKDLSGLWSVDLKGNVNGAVETCGESFHRFDRYLNFSNPLISKNFDPRACGWAYGMNVFDLDEWKRQNITEVYHRWQDLNQDRELWKLGTLPPGLITFWRRTYPLDRKWHILGLGYNPSVNQRDIERAAVIHYNGNLKPWLEIGIPRYRGFWSKHVDYEHVYLRECNINP", "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": "MSIAEFAYKEKPETLVLFDVDGTLTPARLTVSEEVRKTLAKLRNKCCIGFVGGSDLSKQLEQLGPNVLDEFDYSFSENGLTAYRLGKELASQSFINWLGEEKYNKLAVFILRYLSEIDLPKRRGTFLEFRNGMINVSPIGRNASTEERNEFERYDKEHQIRAKFVEALKKEFPDYGLTFSIGGQISFDVFPAGWDKTYCLQHVEKDGFKEIHFFGDKTMVGGNDYEIFVDERTIGHSVQSPDDTVKILTELFNL", "text": "FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol- phosphate-mannose required for a number of critical mannosyl transfer reactions such as folding and glycosylation of secretory proteins in the ER lumen. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic PMM family."}
+{"protein": "MVKKAIVTAMAVISLFTLMGCNNRAEVDTLSPAQAAELKPMPQSWRGVLPCADCEGIETSLFLEKDGTWVMNERYLGAREEPSSFASYGTWARTADKLVLTDSKGEKSYYRAKGDALEMLDREGNPIESQFNYTLEAAQSSLPMTPMTLRGMYFYMADAATFTDCATGKRFMVANNAELERSYLAARGHSEKPVLLSVEGHFTLEGNPDTGAPTKVLAPDTAGKFYPNQDCSSLGQ", "text": "FUNCTION: Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes (PubMed:7635807). Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation (PubMed:11830644). Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR (PubMed:7635808, PubMed:15252048). DegP induction seems to require membrane anchoring of this protein (PubMed:15252048). Structural changes and/or interaction of the CXXC motif with its environment may lead to activation of the Cpx stress response (PubMed:17698001). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor."}
+{"protein": "MATVPVGAGSAPGPEPADLHSVPMVALNYGVRRRLGLYLNPRAATAADWTALAEKLGHDYLEIRRLEALPDPTAALLEEWQSRCPGGATVGQLLELLRQLGRHDVLLELGGSVEEDCKKYLRRKQQEAEQPLQVPAVDSSVPKTSELMGITTRDDPYGHGTEMFDAFICYCQKDLQFVQEMIRELEQTEFKLKLCVFDRDVLPGTCVWSISGELIERRCRRMVVVISDDYLESDECDFQTKFALSLSPGARLKRLIPVKCKTMKNEFPSILRFITICDYTNPCTKKWFWTRLAKSLLLP", "text": "FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic, with some expression in the nucleus."}
+{"protein": "MGNSIYRFLCGLCSPSPEYQPHGAHPAVAALGRDIQQFEATSQVPDGLSRHVVSSKKAQANWYKKLIVTWKKARPTPRTPEEAARLVVTTLKNHQKADVEGFLVFYGLPIPNAAASTPAPHTAHVPKPQGCKFELHTLPVDAKAVADGDTITVYIDTADPRESGNVPREIQKAAAERTRARAARDYQKADGLQKMIADAGYRQVPNARGEEVLAKKYRIRLRGIDAPESAMPYGKEAKEALLKMVQGKSLKVYVYDEDRYGRCVGDIYCDGVFVQEQMLKKGCAWHYTAYDQRPELAKWEKQAQSGRKGLWAASRPQKPWEWRRDKRNGTA", "text": "FUNCTION: Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the thermonuclease family."}
+{"protein": "MNNAIFPNKFKAALAAQQVQIGCWSALASPITTEVLGLAGFDWLVLDGEHAPNDVTTLIPQLMALKGSASAPVVRVPTNEPVIIKRMLDIGFYNFLIPFVETQEEAARAVASTRYPPEGIRGVSVSHRANMFGTVPDYFAQSNKNITIIVQIESQLGVDNVDAIAATEGVDGIFVGPSDLAAALGHLGNASHPDVQQTIQHIFARAKAHGKSCGILAPVEADARRYLEWGATFVAVGSDLGAFRASTQKLADTFKK", "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": "MLTLIQGKKIVNDLRSRLAFEYNGQLIKILSKNIVAVGSLRREEKMLNDVDLLIIVPEKKLLKHVLPNIRIKDFSFSIKVCGERKCVLFIEWKKNTYQLDLFTALAEEKPYAVLHFTGPVSYLIRIRAALKKKNYKLNQYGLFKNQTLVPLKITTEKELIKELGFTYRIPKKRL", "text": "FUNCTION: Error-prone polymerase lacking a proofreading 3'-5' exonuclease which catalyzes the gap-filling reaction during the DNA repair process (By similarity). Specifically binds intermediates in the single-nucleotide base-excision repair process (By similarity). Also catalyzes DNA polymerization with low nucleotide-insertion fidelity (By similarity). Probably acts as a strategic DNA mutase, which gives rise to a rapid emergence of variants (By similarity). Generates mismatched G-G pairs, in that case, the polymerase first binds the deoxynucleotide followed by mismatch formation (By similarity). Together with the viral DNA ligase, fills the single nucleotide gaps generated by the AP endonuclease (Probable). Binds DNA with high affinity via the helix alphaE (By similarity). SUBCELLULAR LOCATION: Virion Note=Found in association with viral nucleoid. SIMILARITY: Belongs to the DNA polymerase type-X family."}
+{"protein": "MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQEPCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAWEKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQFITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMFVSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQQIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK", "text": "FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (PubMed:11714285). Plays a role in the synthesis of ribosomal RNA in the nucleolus (PubMed:10791971). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus, nucleolus Note=Localizes to the nucleolus in proliferative cells but disappears in quiescent cells. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
+{"protein": "MLEANVYDNFNPNYYNVSDFSMPNGKKEKRGLPIPKARCQVINYELWETGYLYTSSATLTVSVEVGDIVQILFPEVVPIEEALGKKKKLNLDMVYLVTDVDESNKATLKNYFWAMIESLDVPNAITKTTNFAIIDYLIDPSKNNLMSYGYFFNSSIFAGKATINRKAETSSAHDVAKRIFSKVQFQPTTTIQHAPSETDPRNLLFINFASRNWNRKRITTRVDIKQSVTMDTETIVERSAYNFAVVFVKNKATDDYTDPPKMYIAKNNGDVIDYSTYHGDGTDLPDVRTAKTLFYDRDDHGNPPALSTIKVEISPSTIVTRLIFNQNELLPLYVNDLVDIWYEGKLYSGYIADRVKTEFNDRLIFVESGDKPNVI", "text": "FUNCTION: Forms a dome thereby closing the central channel at the end of the baseplate. Changes its conformation upon activation by calcium allowing the channel to open at the bottom of the baseplate for DNA ejection. SUBCELLULAR LOCATION: Virion Note=Part of the baseplate. SIMILARITY: Belongs to the skunalikevirus baseplate protein gp16 family."}
+{"protein": "MDVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA", "text": "FUNCTION: The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. FUNCTION: The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. SIMILARITY: Belongs to the shikimate dehydrogenase family."}
+{"protein": "MSIYTRPVMLLLCGLLLLTLAIAVLNTLVPLWLAQANLPTWQVGMVSSSYFTGNLVGTLFTGYLIKRIGFNRSYYLASLIFAAGCVGLGVMVGFWSWMSWRFIAGIGCAMIWVVVESALMCSGTSHNRGRLLAAYMMVYYMGTFLGQLLVSKVSGELLHVLPWVTGMILAGILPLLFTRIVNQQTQARHSSSISAMLKLRQARLGVNGCIISGIVLGSLYGLMPLYLKHQGMANASIGFWMAVLVSAGILGQWPMGRLADKFGRLLVLRVQVFVVILGSIAMLTQAAMAPALFILGAAGFTLYPVAMAWACEKVEHHQLVAMNQALLLSYTVGSLLGPSFAAMLMQNYSDNLLFIMIASVSFIYLLMLLRNVGQTPNPVAHI", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. YcaD (TC 2.A.1.26) family."}
+{"protein": "MALNLKALLGMLFVFIGCCSNVVFLELIIQIDPGAGNLITFAQFLFIALEGLVFTSKFFTVRPKIALKDYVILVALFFGANVCNNYAFNFNIPMPLHMIFRSGSLMANMIMGIVLLKKRYNLRQYSSVAMITAGIILCTLVSSGDVKDNTHHSLKVDTSYSDFFWWTVGIGLLTIALLVTAYMGIYQEVIYKKYGKHPSEALFFTHMLPLPGFLIMAGNIVQHFGIAWSSEPVAVPLLGAIGLEWKFPLMLFYLLCNVVTQYVCISAVYVLTTECASLTVTLVVTLRKFVSLLFSIIYFRNPFTLNHWVGTILVFFGTILFANVINQVRDAYRARSSRKTHFDTAPLAKKVE", "text": "FUNCTION: Sugar transporter that specifically mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc), GDP-fucose and UDP-xylose. Functions redundantly with nac in the O-fucosylation of Notch, positively regulating Notch signaling. Involved in the biosynthesis of heparan sulfate-glycosaminoglycan (HS-GAG) and in Dpp signaling in the wing imaginal disk. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily."}
+{"protein": "MTTNLPFSSPSKQLNRFSFWQSISIPWVVTIIYLLLILVLPIAALLVKSASLGLEGFWQIATTPIAISTYNVTFITALAAGLVNGVMGTLVAWVLVRCQFPGKKIVDAMVDLPFALPTSVAGLVLATLYSQTGWVGRFFAPFGIQIAFSRLGVFVAMVFISLPFIVRTLQPVLQELEEEAEEAAWSLGATEFQTFWRVIFPPLIPPILTGIALGFSRAVGEYGSVVLIASNIPFKDLIAPVLVFERLEQYDYPAATVIGAVLLSVSLILLLIINLLQQWGRRYAND", "text": "FUNCTION: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate 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. CysTW subfamily."}
+{"protein": "MAGVKLLLLSLCVGYTAYHFYSSESMNPESVRGKRVLITGSSTGIGEQIAYEFARMGAHIMVTARRLQRLQEVANECLKLGAASAHYVASDMGNLTSAQYVAQEAVNKLGGLDYLVLNHIGGSASFGFFKGEMDPVVGSIYINFLSYVQLTSAALKALQESQGSIVVMSSMSGRIGAPFTTSYCASKFALEGFYSSLRREFALQNSNMSVTVAVLGYIDTENAVKKVGNKVSMSASSKEDCAREVVKAAVLKQPELFYPYWGIKPFVLLRDWFPGLVAKILDNFYILENIQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MKTLLLLAVIMAIGLLQVHGDLLNFRKMIKLTTGKEPATRYSFYGCYCGMSGRGTPKDATDWCCRAHDCCYKNLESRGCRTKFLKYNVTYQEDQIVCEDADDCKSQVCQCDKIAANCFAANLKTYNKKLRFYNKFRCRGAAPAC", "text": "FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (By similarity). 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). Contributes 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. Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (By similarity). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin- dependent manner (By similarity). SUBCELLULAR LOCATION: Secreted Cell membrane; Peripheral membrane protein Mitochondrion outer membrane; Peripheral membrane protein. SIMILARITY: Belongs to the phospholipase A2 family."}
+{"protein": "MATIKDVAGAAGVSVATVSRNLNDNGYVHEETRTRVIAAMAKLNYYPNEVARSLYKRESRLIGLLLPDITNPFFPQLARGAEDELNREGYRLIFGNSDEELKKELEYLQTFKQNHVAGIIAATNYPDLEEYSGMNYPVVFLDRTLEGAPSVSSDGYTGVKLAAQAIIHGKSQRITLLRGPAHLPTAQDRFNGALEILKQAEVDFQVIETASFSIKDAQSMAKELFASYPATDGVIASNDIQAAAVLHEALRRGKNVPEDIQIIGYDDIPQSGLLFPPLSTIKQPAYDMGKEAAKLLLGIIKKQPLAETAIQMPVTYIGRKTTRKED", "text": "FUNCTION: Transcriptional repressor for the ribose rbsDACBK operon."}
+{"protein": "MWRPHLVDTARLKYLGIVDALEADIRAGRVTPGERLPPQRAIAEALGVDLTTVTRALNEAQRRGLVSAQVGRGTFVRDEPAGDEGGGTPLDLSMNIPPQPAEPDLRRILPQGIASILTSPRGTLAMHYQESTGAPADRTAAASWLAGRVAGASADRIVVTSGAQAALFALCALLLGRGDVVAAGAVTYPGLKAVAAQQHLELAPVAMDEQGILPEAFEAVCRERAPKLLYLIPSIDNPTTATLPADRRREVAAVARRHGVLLIEDDPYAPLRSERLPALAELAPELTWHIATLSKCSTPALRIAYVLAPNAAAAVRLATVLRSSVLMAPPIFAALATRWITDGTLTALASAIRAENRQRQSSAASIFSGLDFAADPDGHHLWLHLPQRWRAAEFADHAERAGLAIVPASAFAVSPHPAEAVRISLGIAPDRGMLEEGLTQLSGLLTQPAVGSRAVV", "text": "SIMILARITY: In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
+{"protein": "MATTRGGSGPDPGSRGLLLLSFSVVLAGLCGGNSVERKIYIPLNKTAPCVRLLNATHQIGCQSSISGDTGVIHVVEKEEDLKWVLTDGPNPPYMVLLEGKLFTRDVMEKLKGTTSRIAGLAVTLAKPNSTSSFSPSVQCPNDGFGIYSNSYGPEFAHCKKTLWNELGNGLAYEDFSFPIFLLEDENETKVIKQCYQDHNLGQNGSAPSFPLCAMQLFSHMHAVISTATCMRRSFIQSTFSINPEIVCDPLSDYNVWSMLKPINTSVGLEPDVRVVVAATRLDSRSFFWNVAPGAESAVASFVTQLAAAEALHKAPDVTTLSRNVMFVFFQGETFDYIGSSRMVYDMENGKFPVRLENIDSFVELGQVALRTSLDLWMHTDPMSQKNESVKNQVEDLLATLEKSGAGVPEVVLRRLAQSQALPPSSLQRFLRARNISGVVLADHSGSFHNRYYQSIYDTAENINVTYPEWQSPEEDLNFVTDTAKALANVATVLARALYELAGGTNFSSSIQADPQTVTRLLYGFLVRANNSWFQSILKHDLRSYLDDRPLQHYIAVSSPTNTTYVVQYALANLTGKATNLTREQCQDPSKVPNESKDLYEYSWVQGPWNSNRTERLPQCVRSTVRLARALSPAFELSQWSSTEYSTWAESRWKDIQARIFLIASKELEFITLIVGFSTLVFSLIVTYCINAKADVLFVAPREPGAVSY", "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). 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": "MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGQNMALLLITYVINILCAVCWKSLFIKYQWKIYNKTTYYFIIQNILNTKQLNNFVLKFNWTKQYNKMNIVSDLFNPNRVKYYYKEDNQQVTNMNSSNTHLTSNKKNLLVDTSETTRTTKNKFNYLLNIFNMKKMNQIITKRHYSIYKDSNIRFNQWLAGLIDGDGYFCITKNKYASCEITVELKDEKMLRQIQDKFGGSVKLRSGVKAIRYRLQNKEGMIKLINAVNGNIRNSKRLVQFNKVCILLNIDFKEPIKLTKDNAWFMGFFDADGTINYYYSGKLKIRPQLTISVTNKYLHDVEYYREVFGGNIYFDKAKNGYFKWSINNKELHNIFYTYNKSCPSKSNKGKRLFLIDKFYYLYDLLAFKAPHNTALYKAWLKFNEKWNNN", "text": "FUNCTION: Mitochondrial mRNA maturase required for splicing of intron 4 of the cytochrome b (COB) gene, containing its own coding sequence, and intron 4 in COX1, coding for the related homing endonuclease aI4. In vivo splicing requires in addition the imported mitochondrial leucyl- tRNA synthetase NAM2. Both proteins seem to stimulate the intrinsic ribozyme activity of intron bI4 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: In the C-terminal section; belongs to the LAGLIDADG endonuclease family."}
+{"protein": "MAVSSTPWALVALFLMASSTVMAIPPRKAIDVPFGRNYVPTWAFDHQKQLNGGSELQLILDKYTGTGFQSKGSYLFGHFSMHIKLPAGDTAGVVTAFYLSSTNNEHDEIDFEFLGNRTGQPVILQTNVFTGGKGNREQRIYLWFDPSKAYHTYSVLWNLYQIVFFVDNIPIRVFKNAKDLGVRFPFNQPMKLYSSLWNADDWATRGGLEKTNWANAPFIASYRGFHIDGCQASVEAKYCATQGRMWWDQNEFRDLDAEQYRRLKWVRMKWTIYNYCTDRTRFPVMPAECRRDRDV", "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. SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1 subfamily."}
+{"protein": "MDSTLISTRPDEGTLSLSRARRAALGSFAGAVVDWYDFLLYGITAALVFNREFFPQVSPAMGTLAAFATFGVGFLFRPLGGVIFGHFGDRLGRKRMLMLTVWMMGIATALIGILPSFSTIGWWAPILLVTLRAIQGFAVGGEWGGAALLSVESAPKNKKAFYSSGVQVGYGVGLLLSTGLVSLISMMTTDEQFLSWGWRIPFLFSIVLVLGALWVRNGMEESAEFEQQQHYQAAAKKRIPVIEALLRHPGAFLKIIALRLCELLTMYIVTAFALNYSTQNMGLPRELFLNIGLLVGGLSCLTIPCFAWLADRFGRRRVYITGTLIGTLSAFPFFMALEAQSIFWIVFFSIMLANIAHDMVVCVQQPMFTEMFGASYRYSGAGVGYQVASVVGGGFTPFIAAALITYFAGNWHSVAIYLLAGCLISAMTALLMKDSQRA", "text": "FUNCTION: Involved in the uptake of shikimate, an intermediate in the aromatic amino acid biosynthetic pathway. 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": "MIVIYHNPDCGTSRNVLQLIEAAGYLPQVIEYVKEGWTKPQLLGLFAAADLTPRSALRTTKSPAAELNLLEETVTDAQILDAMVEYPILVNRPIVCTPKGVRLCRPSEVVLDLLDHWPSGPFAKEDGELIIDERGNRVYT", "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": "MLANYAFIGVFFIGAIIFPIIPLAAAYFLGPKRPTPIKLDTYECGLEAIGDIRVQFKIQYYLYALAFVIFDIEVVFLYPWAVAYGQLGLFAFIAMAIFLIILIGGLVYEWKKGALEWV", "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 3 family."}
+{"protein": "MGRKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSFQVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAVLVTWDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRLYYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPRVKVDFALSCHEDLLAPISEPIEWKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGVDSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQISYTPQDPRDLCGRILTTCYMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLALQNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCIQRFQLPALQSILLAPATAELEPLADGQVSQTDEEDMGMTYAELSVYGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFSKYSMNRHKMTTLTPAYHAENYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEPQSLDGVD", "text": "FUNCTION: Catalyzes the final step of the nicotinamide adenine dinucleotide (NAD) de novo synthesis pathway, the ATP-dependent amidation of deamido-NAD using L-glutamine as a nitrogen source. SIMILARITY: In the C-terminal section; belongs to the NAD synthetase family."}
+{"protein": "MADSTPVRMPRAPKLRASCDECGAAKLKCDRGHPSCGRCISLGLKCVYGVSRKAGKPRRDAQSATRPPPTPGDSGPPLDYNSFGPTSPPSSVGDGATLASGLLPGAADLSPLDWGPGSSSSYRAVVDLCSRYAKEPMRMDDTAMSSVWDGFLEPSLFATYGSPVQVARLAGGSVPFSAAPVRDLPI", "text": "FUNCTION: Transcription factor that specifically regulates the expression of the pgm gene cluster that mediates the biosynthesis of cryptic naphthoquinones derived pigments responsible for the coloration of the fruiting bodies. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MCSPGRAPPGPAPAGDLPPEWETDDERMAFLFSAFKQSREVNSTEWDSKMAFWVGLVLARGRRRGVVRTCLRELQNGFERRGSVPLGLGTVLRELLRRGKMQRESDFMASVDSSWISWGVGVFILKPLKWTLSSVLGDSKVPEEEEVLIYVELLQEKAEEVYRLYQNSVLSSHPVVALSELRSLCAGVCPDERTFYLLLLQLQKEKKVTILEQNGEKIVKFARGLHAKVSPMNDVDIGVYQLMQSEQLLSQKVESLSQEAEKCKDDARSACRAGKKQLALRCLKSKRRTERRIEELHSKLDAVQGILDRIYASQTDQMVFNAYQAGVGALKLSMKDVTVEKAENLVDQIQELCDTQDEVAQTLAGAGVNGLEMDSEELEKELDSLLQDSAKEPVHLHPVPQKDSGFAGAISDAELEAELEKLSVCDGDLAQKTPSASSEPQTALGLNL", "text": "FUNCTION: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope (NE) during late anaphase (By similarity). Together with SPAST, the ESCRT-III complex promotes NE sealing and mitotic spindle disassembly during late anaphase (By similarity). Recruited to the reforming NE during anaphase by LEMD2 (By similarity). Plays a role in the endosomal sorting pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus envelope Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. SIMILARITY: Belongs to the SNF7 family."}
+{"protein": "MPHSSDSSDSSFSRSPPPGKQDSSDDVRRVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLNSHEPLCSVLAASTPSPPEVVYSAHAFHQPHVSSPRFQP", "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). 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": "MTENAPTELAITGMTCDGCAAHVRKALEGVPGVREAQVSYPDATARVVLEGEVPMQRLIKAVVASGYGVHPRSDGASSTNDGQELHIAVIGSGGAAMACALKAVERGARVTLIERSTIGGTCVNIGCVPSKIMIRAAHIAHLRRESPFDGGIQAVAPTIQRTALLVQQQARVDELRHAKYEGILDGNPAITVLRGEARFKDSRSVVVHLNDGGERVVMFDRCLVATGASPAVPPIPGLKDTPYWTSTEGLVSESIPERLAVIGSSVVALELAQAFARLGSHVTILARGTLFLREDPAIGEAITAAFRAEGIEVLEHTQASQVAYADGEFVLATGHGELRADKLLVATGRAPNTRRLNLEAAGVAINAQGAIVIDQGMRTNSPNIYAAGDCTDQPQFVYVAAAAGTRAAINMMGGSAALDLTAMPAVVFTDPQVATVGYSGAEAHRDGIETDSRTLTLDNVPRALANFNTRGFIKLVAEVGSGRLIGVQVVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFTRDVKQLSCCAG", "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": "MTVKTEAARSTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKLANNSYACKHPEVQSYLKISQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEAFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHIFFSLINWDDLINKKITPPFNPNVSGPSDLRHFDPEFTEEPVPSSIGRSPDSILVTASVKEAAEAFLGFSYAPPMDSFL", "text": "FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis (By similarity). Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. May also play an important role in the development of particular groups of neurons in the postnatal brain. SUBCELLULAR LOCATION: Cytoplasm Nucleus Endoplasmic reticulum membrane Cell membrane Mitochondrion Note=The subcellular localization is controlled by the cell cycle, as well as by exposure to specific hormones and environmental stress stimuli. In proliferating cells, it shuttles between the nucleus and cytoplasm in synchrony with the cell cycle, and in serum/growth factor-stimulated cells it resides in the nucleus. In contrast, after exposure to environmental stress or treatment with glucocorticoids, it is detected in the cytoplasm and with certain stress conditions is associated with the mitochondria. In osmoregulation through the epithelial sodium channel, it can be localized to the cytoplasmic surface of the cell membrane. Nuclear, upon phosphorylation (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family."}
+{"protein": "MTEYTPKERLYRALRKQPVDRMPAVCFTQTGTVEQMEASGAFWPEAHADAEKMAKLAEAGHTVIGFEAVRVPFDITAEAELFGCGIKAGDLKQQPSVIKHSVKNLEDLDKIKNYSLDTGRIGTILKAVKILSEKYGKELPVIGSMIGPFSLAQHINGDAWFGNLFTGEDIVPALLDFCADFNIAYAKAMVENGADTIAIIDPTASYELIGGEFYEKYALPYQKKIVDAMKELDVATVLHICGNTTNGLAIMDRTGVNAISVDQRVDIKTATGNVENAIIVGNLDPVAVLWNGTPEDVEAASKKVLDAGVGILTVGCGIVSMTPSANLQKMVECAKNYRY", "text": "FUNCTION: Methyltransferase involved in methanogenesis from methylamines methanol pathway. Catalyzes the transfer of the methyl group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) to coenzyme M, forming the substrate for coenzyme-B sulfoethylthiotransferase. SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family. MtbA/MtaA subfamily."}
+{"protein": "MDFFSTHNILIHIPIGAGGYDLSWIEAVGTIAGLLCIWLASLEKISNYFFGLVNVTLFAIIFFQIQLYASLLLQLFFFAANIYGWYAWSRQTKDNQAELKIRWLPLPKAMAWLAICVIAIGLMTRYIDPVFAVLTRVAVAIMQMLGLQVTMPVLQPDAFPFWDSCMMVLSIVAMILMTRKYVENWLLWVIINVISVVIFALQGVYAMSLEYLILTFIAVNGSRLWINSARERGSRALSR", "text": "FUNCTION: Required for nicotinamide riboside transport across the inner membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake permease (TC 4.B.1) family."}
+{"protein": "MMIKIAVVLCAVMATSMVFANDVKEQELADLLDLLISEEVSSPDDAVAESWGHKLRSSWNKVKHAVKKGAGYASGACRVLGHSPQEARAKVLEAFPEMKESDLDEEQVGKYCAVAHAIHGR", "text": "FUNCTION: [Centrocin 2, heavy chain]: Has antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and against fungi with minimum inhibitory concentration (MIC) between 0.78 uM and 50 uM. Shows little hemolytic activity at concentrations up to 12.5 uM but >50% lysis at 100 uM."}
+{"protein": "MASENQKLSSVALTPVEATDYAENTATYKANKRPFLSFMSGISAGACIALAFVFYTTTQTASAGAPWGLTKLVGGLVFSLGVIMVVILGSELFTSSTLTLVARVGGRITTTQMIRNWIVVYLGNFVGGLFIAAVIWFSGQTMAANGQWGLTILATAQHKIHHTWFEAFNLGILCNIMVCVAVWMSYSGKTVTDKAFIMIMPIGLFVASGFEHCVANMFMIPMGIITAHFSTPEFWQQIGVDPMKYADLDLYHFIVKNLIPVTLGNIVGGAICIGVFQRYLTKTH", "text": "FUNCTION: Involved in the bidirectional transport of formate during mixed-acid fermentation. Functions to maintain relatively constant intracellular formate levels during growth, using different mechanisms for efflux and uptake of the anion. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FNT transporter (TC 2.A.44) family."}
+{"protein": "MSADEPSPEDEKYLESLRDLLKISQEFDASNAKQNDEPEKTAVEVESAETRTDESEKSIDIPREQQLLPSERVEPLKSMVEPEYVKKVIRQMDTMTAEQLKQALMKIKVSTGGNKKTLRKRVAQYYRKENALLNRKMEPNADKTARFFDYLIAIDFECTCVEIIYDYPHEIIELPAVLIDVREMKIISEFRTYVRPVRNPKLSEFCMQFTKIAQETVDAAPYFREALQRLYTWMRKFNLGQKNSRFAFVTDGPHDMWKFMQFQCLLSNIRMPHMFRSFINIKKTFKEKFNGLIKGNGKSGIENMLERLDLSFVGNKHSGLDDATNIAAIAIQMMKLKIELRINQKCSYKENQRSAARKDEERELEDAANVDLTSVDISRRDFQLWMRRLPLKLSSVTRREFINEEYLDCDSCDDLTDDKNDEAAFQEKMAIREYLENKQTEDFAKIAAERGIFKIGEIKSYQTARPIIEDDDVDVESEEEDYGTEFEMLEVVERMPPVSSTLHTEVDLDAVWERDGGSDSERENLSNAPSLHEFPSSSTSSPHATSEHVTSSSPLHIDDDVDRVLNAPPKNSLASSSNRSSF", "text": "FUNCTION: RNA exonuclease that acts as a negative regulator of RNA interference (RNAi) (PubMed:14961122). Probably acts by degrading the 3'-overhangs of short interfering RNAs (siRNAs) (PubMed:14961122). Component of the ERI/DICER complex which is involved in processing amplified double-stranded RNA (dsRNA) intermediates during small-RNA- mediated gene-silencing or RNA interference (RNAi) (Probable). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MKPNLKQWKQFMLFGICAWGLLFLVIFVYFTDSNSVEPVPSAFSYVESKKHFPLQGKQRAIMGAHQDQLFSYAIDDQDLLKEGILDSFIVGPGSMKKMAGADNYFESEQEFIMSKKTQKSTSNNHEDDDDEIYLHKNIDSVSGKKAPAYGKRYYHDTQRQHKKIRRNMQRKKQHMIEDSYDWNGFSSSMSKSFLQKLWKGNVSSKMLTPRLQKARREYLRANKLGVNFNGKQNSRKLNPQELLCVLKDRAQVKTLDGKDAPFSSLGWEKYFPKIALNKLYPHGFSTCAVVSSAGAILNSSLGAEIDSHDAVLRFNSAPTRNYEKDVGNKTTLRIINSQILTNPNHHFTDSSLYKDVTLIAWDPSPYYADLHMWYHKPDYNLFPPYEKHRKRNPDQPFYILHPKFTWELWKIIQENSNEKIQPNPPSSGFIGILIMMSMCRTVHVYEYIPSYRQTDLCHYHEQYYDAACTLGAYHPLLYEKMLIQRINQGTEDNLLRKGKVILPGFSSIHCPIKDHIT", "text": "FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
+{"protein": "MRLAVVCFCLFGLASCLPVKVAEFGSSEEKAHYSKHSDAVATWLKPDPSQKQNLLAPQNSVSSEETDDFKQETLPSNSNESHDHMDDDDDDDDDGDHAESEDSVNSDESDESHHSDESDESFTASTQADVLTPIAPTVDVPDGRGDSLAYGLRSKSRSFPVSDEQYPDATDEDLTSRMKSQESDEAIKVIPVAQRLSVPSDQDSNGKTSHESSQLDEPSVETHSLEQSKEYKQRASHESTEQSDAIDSAEKPDAIDSAERSDAIDSQASSKASLEHQSHEFHSHEDKLVLDPKSKEDDRYLKFRISHELESSSSEVN", "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": "MREPALAASAMAYHPFHAPRPADFPMSAFLAAAQPSFFPALALPPGALGKPLPDPGLAGAAAAAAAAAAAAEAGLHVSALGPHPPAAHLRSLKSLEPEDEVEDDPKVTLEAKELWDQFHKLGTEMVITKSGRRMFPPFKVRVSGLDKKAKYILLMDIVAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMAKPVAFHKLKLTNNISDKHGFTILNSMHKYQPRFHIVRANDILKLPYSTFRTYVFPETDFIAVTAYQNDKITQLKIDNNPFAKGFRDTGNGRREKRKQLTLPTLRLYEEHCKPERDGAESDASSCDPPPAREPPPSPSAAPSPLRLHRARAEEKPGAADSDPEPERTGEERSAAPLGRSPSRDASPARLTEPERSRERRSPERCSKEPTEGGGDGPFSLRSLEKERPEARRKDEGRKDVGEGKEPSLAPLVVQTDSASPLGAGHLPGLAFSSHLHGQQFFGPLGAGQPLFLHPGQFAMGPGAFSAMGMGHLLASVAGGSGSSGGAGPGTAAGLDAGGLGPAASAASTAAPFPFHLSQHMLASQGIPMPTFGGLFPYPYTYMAAAAAAASALPATSAAAAAAAAAGSLSRSPFLGSARPRLRFSPYQIPVTIPPSTSLLTTGLAAEGSKGGNSREPSPLPELALRKVGGPSRGALSPSGSAKEAASELQSIQRLVSGLESQRALSPGRESPK", "text": "FUNCTION: Transcription factor which acts as a transcriptional repressor (PubMed:22186728, PubMed:11867218, PubMed:18025091, PubMed:12023302). May also function as a transcriptional activator (PubMed:26486273, PubMed:22186728, PubMed:11867218). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half- site, which are present in the regulatory region of several genes (PubMed:9710594, PubMed:26971330, PubMed:12023302, PubMed:33731112, PubMed:27720610). Required for cardiac atrioventricular canal formation (PubMed:15459098). May cooperate with NKX2.5 to negatively modulate expression of NPPA/ANF in the atrioventricular canal (PubMed:12023302). May play a role as a positive regulator of TGFB2 expression, perhaps acting in concert with GATA4 in the developing outflow tract myocardium (PubMed:22186728). Plays a role in limb pattern formation (PubMed:15459098). Acts as a transcriptional repressor of ADAM10 gene expression, perhaps in concert with histone deacetylase HDAC1 as cofactor (PubMed:30599067). Involved in branching morphogenesis in both developing lungs and adult mammary glands, via negative modulation of target genes; acting redundantly with TBX3 (PubMed:27720610, PubMed:16222716). Required, together with TBX3, to maintain cell proliferation in the embryonic lung mesenchyme; perhaps acting downstream of SHH, BMP and TGFbeta signaling (PubMed:27720610). Involved in modulating early inner ear development, acting independently of, and also redundantly with TBX3, in different subregions of the developing ear (PubMed:33795231). Acts as a negative regulator of PML function in cellular senescence (By similarity). Acts as a negative regulator of expression of CDKN1A/p21, IL33 and CCN4; repression of CDKN1A is enhanced in response to UV-induced stress, perhaps as a result of phosphorylation by p38 MAPK (PubMed:18025091, PubMed:33731112). Negatively modulates expression of CDKN2A/p19ARF and CDH1/E-cadherin (By similarity). Plays a role in induction of the epithelial-mesenchymal transition (EMT) (By similarity). Plays a role in melanocyte proliferation, perhaps via regulation of cyclin CCND1 (PubMed:26486273). Involved in melanogenesis, acting via negative modulation of expression of DHICA oxidase/TYRP1 and P protein/OCA2 (PubMed:26971330, PubMed:9710594). Involved in regulating retinal pigment epithelium (RPE) cell proliferation, perhaps via negatively modulating transcription of the transcription factor CEBPD (PubMed:28910203). SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MDLVRGLWRKHRRKILVTTTCLGSGYLLYKLYNAHTRKLADLERELANERENDEIIKTQMKAHFDNIQMIADTTTLPHAIHHLSSRVVEEIDVSSIMDKLSKGKGILIPSEKLQLWNELKILSFTRMVLSLWSVTMLSLYIRVQVNILGRHLYIDTARGLGSSHLLDELDLIERDDEQKFLTSADFLATSGMPSLISNMQNAVKEVLKGKQLKDVLTTSALRETVMRILDVFMSTGSPHHWVDYLMMSQDATTDVSSSDATVTKFHLLITETREVLTSNDFSNVAEISLKCCAVALVEEMETQTGLATGMQLAKLLPQIEKTMPEISAEPEKNRFLQLIRDLPEVKLFFTLLYANMPQ", "text": "FUNCTION: Involved in morphology determination of peroxisomes, but not in import of peroxisomal matrix proteins. May act as a docking factor for PEX19 and be necessary for the import of peroxisomal membrane proteins in the peroxisomes. SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peroxin-3 family."}
+{"protein": "MVGEEKMSLRNRLSKSGENPEQDEAQRSVSDTQSNGRITMKQLIAKKRQLAAEAEELKPLFLKEVGCHFDDFVTNLIEKSASLDNGGCALTTFSILEEMKNNHRAKDLRAPPEKGKIFISRRSLLDELFEVDHIRTIYHMFIGLLILFILSTLVVDYIDEGRLVLEFNLLGYAFGKLPTVIWTWWAMFLSTLSIPYFLFQRWAHGYSKTSHPLIYSLSHGFFFLVFQLGILGFVPTYVVLAYTLPPASRFIVILEQIRMVMKAHSFVRENVPRVLNAAKEKSSTVPVPTVNQYLYFLFAPTLIYRDSYPRTPTVRWGYVAVQFLQVFGCLFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLMLFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYAYKDLLWFFSKRFKSAAMLAVFALSAVVHEYALAVCLSYFYPVLFVLFMFFGMAFNFIVNDSRKRPIWNIMVWASLFLGHGVILCFYSQEWYARQHCPLKNPTFLDYVRPRSWTCQYVF", "text": "FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. 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. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily."}
+{"protein": "MAVVPIRIVGDPVLHTATTPVTVAADGSLPADLAQLIATMYDTMDAANGVGLAANQIGCSLRLFVYDCAADRAMTARRRGVVINPVLETSEIPETMPDPDTDDEGCLSVPGESFPTGRAKWARVTGLDADGSPVSIEGTGLFARMLQHETGHLDGFLYLDRLIGRYARNAKRAVKSHGWGVPGLSWLPGEDPDPFGH", "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. 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. SIMILARITY: Belongs to the polypeptide deformylase family."}
+{"protein": "MSAQIAPAEQVCYVHCNFCNTILAVSVPGNSMLNIVTVRCGHCTNLLSVNLRGLMHSAPALQDHHHHHLQESGLSGCFRDQSGYPEFGFSAASSSSKLRLPPAAAAMVSYSQQNQQLEQALHARPPEKRQRVPSAYNRFIKEEIRRIKANNPDISHREAFSTAAKNWAHYPNIHFGLSPGHEGGKKLVDVDPIPTAPSSKKIQGFYS", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the YABBY family."}
+{"protein": "MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDNLPEDMGRLHLDDGKSPNHGEIAKVGEGKYREDFQMDEGEDPSFLFQSYLENVGVQIVRQMRSGERFLKIWSQTVEEIISYVAVNFPNPPGKSSEDKSTQTTGRELKKETTPTPSQRESQSSKARMAAQIASGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGILLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKLPLRCVLGWVALANSKKFQLLVESDKLSKIMQDDLNRYTSC", "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. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body (By similarity). Inhibits interferon induction pathways by interacting with host TBK1 and preventing the formation of dynamic cytoplasmic condensates that have liquid properties and that are essential for interferon production (PubMed:36640307). SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus. SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm. SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm. SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus. SIMILARITY: Belongs to the lyssavirus protein P family."}
+{"protein": "MGVEVCVKAAVGHPDTLGDCPFSQRVLLTLEEKKVPYEMKLIDVQNKPDWFLKISPEGKVPVFNGGDGKWIPDSDVITQVIEEKYPTPSLVTPPEYASVGSKIFSCFTTFLKSKDPNDGSEKALLTELQALEEHLKAHGPFINGQNISAADLSLAPKLYHLQVALEHFKGWKIPEDLTNVHAYTEALFSRESFIKTKAAKEHLIAGWAPKVNA", "text": "FUNCTION: Involved in ascorbate homeostasis. Maintains redox pools of ascorbate by recycling dihydroascorbate (DHA) to ascorbate (Probable). Involved in scavenging reactive oxygen species (ROS) under oxidative stresses. Possesses dehydroascorbate reductase (DHAR) activity in vitro (PubMed:19011360). May function via a ping-pong reaction mechanism with an electron transfer at the active site (PubMed:26775680). Possesses chaperone-like activity in vitro (PubMed:26775680). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. DHAR family."}
+{"protein": "MSLPDISRRRSPVPQEDWPLTPNALRPSPFPNPVLQALYSLSRVLLFPTYWSLDQLLGCWAPSVRSKSLGWFKVLAGSGVLLPLVVVGLPLALVGLALWLPLQVWRRPFCYQPPPACWVWPQPWHPPAERRRCFVFLTANLCLLPHGLAHFNNLSHSLQRAEAVGAALLDSLQSSQYRVSECSQPPPRVPGGELKATLPMGLDFVCLQEVFDLRAARRLVRVLVPNLGPVIYDVGTFGLMAGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASKGLLSVQAQLGIVDGHPIVGYLHCTHLHAPVEDGHIRCKQLTLLLEWVEEFEAENRQSDEAVAFSVLLGDLNFDNCSQDHAKEQGHKLFSCFQDPCRLGVCQEQPWALGTILNSSMLRHSIACSPEMLRRALRQEKGRRLYLSGPLHGSYPAQSWKGRRLDYITYRRVPGSRLSPEAEQVTFSTAFAGLTDHLAMGLKLQVVCS", "text": "FUNCTION: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass type II membrane protein; Intermembrane side Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the neutral sphingomyelinase family."}
+{"protein": "MASGSDTKSDDLSTAILKQKSRPNRLIVDESINEDNSMVSLSQAKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRVHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDSTGRLEILQIHTKNMKLSDDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSIKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRMAILKANLRKSPVAKDVDVDFLAKMTNGFSGADLTEICQRACKLAIRESIENEIRRERDRQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPAGGQSGAGPSPGAGGGSGGGHFTEEDDDLYG", "text": "FUNCTION: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. Involved in 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. Plays a role in the regulation of stress granules (SGs) clearance process upon arsenite-induced response (By similarity). Also involved in DNA damage response: recruited to double- strand breaks (DSBs) sites and promotes the recruitment of tp53bp1 at DNA damage sites (By similarity). Together with sprtn metalloprotease, involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis (By similarity). Involved in interstrand cross- link repair in response to replication stress by mediating unloading of the ubiquitinated CMG helicase complex (PubMed:30979826, PubMed:30849395, PubMed:30842657). Enhances cell cycle progression and inhibits apoptosis at low temperatures (By similarity). Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy (By similarity). Acts as a negative regulator of type I interferon production by promoting ubiquitination of rigi (By similarity). May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation (By similarity). May more particularly play a role in caveolins sorting in cells (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Endoplasmic reticulum Nucleus Cytoplasm, Stress granule. SIMILARITY: Belongs to the AAA ATPase family."}
+{"protein": "MIQITVVQIDNYGPWTVTPNPRRESDLQALQSRLYCDMNLQFGAHKGLAFYTRFDNIIAITNGIDLETHKRIQNSVKNRYPFTVSMAVASAETAYEAQKLATKTIQEYGSAQDDVRKEVLDVANEFVSNGYVQLAHVDINDITGKLTDLETAYDTYLSVQKTKLKLMEELKKYDSLGFFIGGDNFMCPCNGMNEKDFLCMFEDIKDSCGIELKAGIGIGKTAEDASNLADIGLEVIREGKTDSQVYTLKQEIDEQKNVPYNYMCPI", "text": "FUNCTION: Catalyzes the formation of 2-amino-5-formylamino-6- ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and inorganic phosphate from GTP. Also has an independent pyrophosphate phosphohydrolase activity. SIMILARITY: Belongs to the archaeal-type GTP cyclohydrolase family."}
+{"protein": "MSKGPGLFADIGKYAKDLLTRDYSTDQKFSISTNSVSGVALTSTALKNGVLHAANVATQYKYRNTFFDVKIDTDFNVKSLVYPMNKFVSIDHNTLTGYDTTSRTFTKYNVGVSVTKPDQCVSIILGDKGDSIKASYVYYLDESTRSATVGEVIRKISTNETTVTVGGLYAVDHLTNVKAKLNSNGKFGALLQHEGLPKSIVTISGEIDTKTLDKYPRLGLSLSLKP", "text": "FUNCTION: Putative channel that allows diffusion of small hydrophilic molecules through membranes. SUBCELLULAR LOCATION: Mitochondrion outer membrane. SIMILARITY: Belongs to the eukaryotic mitochondrial porin (TC 1.B.8.1) family."}
+{"protein": "MQHKRSRALASPRSPFLFALLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDELFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKASAVQGGNPLGAYAQTFQRLFGTPAAELLQPRNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQIQVSNGQQVSADTKLGVYASNINTALCEGGSSTGPHLHFSLLYNGAFVSLQGASFGPYRINVGTSNYDNDCRRYYFYNQSAGTTHCAFRPLYNPGLAL", "text": "FUNCTION: Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidogylcan), preferring Gly- Gly-|-X substrates where X is Ala or Gly. Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases. Degradation of elastin is likely to contribute to the pathogenicity of P.aeruginosa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M23A family."}
+{"protein": "MSTVEEDSDTVTVETVNSVTLTQDTEGNLILHCPQNEADEIDSEDSIEPPHKRLCLSSEDDQSIDDSTPCISVVALPLSENDQSFEVTMTATTEVADDEVTEGTVTQIQILQNEQLDEISPLGNEEVSAVSQAWFTTKEDKDSLTNKGHKWKQGMWSKEEIDILMNNIERYLKARGIKDATEIIFEMSKDERKDFYRTIAWGLNRPLFAVYRRVLRMYDDRNHVGKYTPEEIEKLKELRIKHGNDWATIGAALGRSASSVKDRCRLMKDTCNTGKWTEEEEKRLAEVVHELTSTEPGDIVTQGVSWAAVAERVGTRSEKQCRSKWLNYLNWKQSGGTEWTKEDEINLILRIAELDVADENDINWDLLAEGWSSVRSPQWLRSKWWTIKRQIANHKDVSFPVLIKGLKQLHENQKNNPTLLENKSGSGVPNSNTNSSVQHVQIRVARLEDNTAISSSPMAALQIPVQITHVSSADSPATVDSETITLNSGTLQTFEILPSFHLQPTGTPGTYLLQTSSSQGLPLTLTASPTVTLTAAAPASPEQIIVHALSPEHLLNTSDNVTVQCHTPRVIIQTVATEDITSSISQAELTVDSDIQSSDFPEPPDALEADTFPDEIHHPKMTVEPSFNDAHVSKFSDQNSTELMNSVMVRTEEEISDTDLKQEESPSDLASAYVTEGLESPTIEEQVDQTIDDETILIVPSPHGFIQASDVIDTESVLPLTTLTDPILQHHQEESNIIGSSLGSPVSEDSKDVEDLVNCH", "text": "FUNCTION: Transcriptional activator which activates the CDKN2A/ARF locus in response to Ras-Raf signaling, thereby promoting p53/TP53- dependent growth arrest (By similarity). Binds to the consensus sequence 5'-CCCG[GT]ATGT-3' (By similarity). Isoform 1 may cooperate with MYB to activate transcription of the ANPEP gene. Isoform 2 may antagonize transcriptional activation by isoform 1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DMTF1 family."}
+{"protein": "MSRVASSRVLKDSNGDIGEHLRNHIHLTNCIHLKNHMHNNNKQSPVLTDRSLLMRDLVVLQRSRSLRDPSASPNLKEDHQDSREGRRRSGLRLSGSSPIVSFGTSKVTPSDEKFDRSSRKSYRVEEVNEVYSVPSVKSVSKDRINKKVNEAIVKTLSDQLNEVGGDSDDLVSCNVRPRGDGCRRRKFRGTRRAGRAVNVRDNAAGNESEMSIASNSVPRGEKYEGEEGGGGRDREQNMSCGIPFNWSRIHHRGKTFLDIAGRSLSCGISDSKGRKGEAGTPMFSDSSSSDREALPLLVDSADNEEWVHDYSGELGIFADNLLKNGKDSVIGKKSSRKNTRWHQSFTQKYAPRTFRDLLGQNLVVQALSNAIAKRRVGLLYVFHGPNGTGKTSCARVFARALNCHSTEQSKPCGVCSSCVSYDDGKNRYIREMGPVKSFDFENLLDKTNIRQQQKQQLVLIFDDCDTMSTDCWNTLSKIVDRAPRRVVFVLVCSSLDVLPHIIVSRCQKFFFPKLKDVDIIDSLQLIASKEEIDIDKDALKLVASRSDGSLRDAEMTLEQLSLLGTRISVPLVQEMVGLISDEKLVDLLDLALSADTVNTVKNLRIIMETGLEPLALMSQLATVITDILAGSYDFTKDQCKRKFFRRQPLSKEDMEKLKQALKTLSESEKQLRVSNDKLTWLTAALLQLAPDKQYLLPHSSSADASFNHTPLTDSDPSNHVVAGTRRDDSKQGFSCKNRPSVEDIWLAVIENVRVNGLREFLYKEGKIFSISIGSAPMVQLMFNSPIAKSTAENFEEHILKAFEAVLGSPVTLEMRTESKKDLGFSSLQGLSNGERFRESGRSEIVEVADSESPMTRVRRKHLEASQNQNQNQNQSIVRGKVSLAQVIKQAEGNSWSKHKAVEIANKLEQENLKLEPRSRSLICWKASRSTRRKLSRLKVRTRKLRLHSLLKLVSCGKCLSTRSPPR", "text": "SIMILARITY: Belongs to the DnaX/STICHEL family."}
+{"protein": "MREIVTITASHRANHLITQFFNGQERALHERDEQAGSDPSVFLHGTIDADGRTMSYEPRAVLWDAKGGSGALGRFQYWSQDDYADEEEPPRAAPGIEVVQTAARVRRSAYQRALDAGEAPPALTAAGARYWSDYGRMIYGQDSVQELAHWHHDVAAPSAPDFEALGQRRFDRYENGYEVFTEECARDFFDISLHRQLEQCDTLQGFNLVTETDNGWGGFMAALQEQLREEVPKVCYFGWGLNVDESGPRHPPRAGFQRQSNKLRATLAMLEQSDLYFPIRSEAADSLWEAGGWACHVLDSVNSAMCLEKSRTLRFMNQLADRLHSGDEQRNVVSLMSSGQRSYSYFADAPRHRSSRGDPHTFSRCRLLRGSHSPPETTLSVENLELIRTYAWRPADTIPETARNLHHIDLGVTEKCRDVFKNWYEMVAKQFRYDPDREELKERLGTLGAAYECGWYSDDDSGDDT", "text": "FUNCTION: Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the misato family."}
+{"protein": "MDTPTSSSLPAIERQHLPALFAARPTDAHKGSCGTLGVIGGGPGMVGAALLAARAGLKVGAGKVLVGLVADTPPLPCDPMQPELMLRDFRGLLEAGLGIDAWTAGCGCGMDALAANALSELFQLRGDAALVLDADGLNLLAAGAVQARWGDAPVVLTPHPAEAGRLLGLSTEAVQADRPGAARALAARYGAWIVLKGAGSIVCDPAGACRINRTGNPGLATAGTGDVLAGILGSLLAQRIAPEQAVPGAVWLHGAAADALVTHGVGPIGLTAGELADSARRLRNSRA", "text": "FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. 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": "MAKINELLRESTTTNSNSIGRPNLVALTRATTKLIYSDIVATQRTNQPVAAFYGIKYLNPDNEFTFKTGATYAGEAGYVDREQITELTEESKLTLNKGDLFKYNNIVYKVLEDTPFATIEESDLELALQIAIVLLKVRLFSDAASTSKFESSDSEIADARFQINKWQTAVKSRKLKTGITVELAQDLEANGFDAPNFLEDLLATEMADEINKDILQSLITVSKRYKVTGITDSGFIDLSYASAPEAGRSLYRMVCEMVSHIQKESTYTATFCVASARAAAILAASGWLKHKPEDDKYLSQNAYGFLANGLPLYCDTNSPLDYVIVGVVENIGEKEIVGSIFYAPYTEGLDLDDPEHVGAFKVVVDPESLQPSIGLLVRYALSANPYTVAKDEKEARIIDGGDMDKMAGRSDLSVLLGVKLPKIIIDE", "text": "FUNCTION: Capsid protein that self-associates to form pentons, building the capsid in association with hexamers of the major capsid protein and one dodecamer of the portal protein. The capsid vertex protein self- associates to form 11 pentons, building the T=13 laevo capsid in association with 160 hexamers of the major capsid protein. SUBCELLULAR LOCATION: [Mature capsid vertex protein]: Virion. Note=Part of the capsid icosahedric shell of the mature virion. The capsid contains 55 copies. SUBCELLULAR LOCATION: [Capsid vertex protein]: Virion. Note=Part of the capsid icosahedric shell of the immature virion. The capsid contains 55 copies. SIMILARITY: Belongs to the Tevenvirinae capsid vertex family."}
+{"protein": "MGEIPPTDSGYPTPRDEIPSTSRPNSPNNAQLYPLTSTPIRGNKSRSMKENFATFRNDLSIIESTGSDTIENDSHFVLDGVKSLLEASKELKKKDRANSLLRDQNESLRGENESLREENCSLREESRRMDLVDKENVIPVIPRLVFDEKPDLDPITVKSSEQIKKELLSFIKNDEDRTIMEAKMENMLISDSKPPAKVFTATATIQVDTEKMDANIQTDKDDHVNVVNANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHETFEINARNQFYAVTGQMHEDIESYKQRLLELEPYPGKIISGSFRDFPSQTDPSPATTDAWMQTDVEEQLMVSPEVSLVSEAPSSLQDSRRSSHLDEKLRRTIEKIGELLAEHESFQESLRDPEFHTAEAFRKISQLLKSILSGANSEEMLERIWTWLTLKTKALVEQQDEQMKKVQKAGEMLLSQLREKESDNEVLTKKSLEMEAAAEEFRTYYNDMLTENDELRHRIVQLDEIREVESSNSTKIEKGLREQLEQAQHELEKKKREYMWKLQQKDEFYEIMDRNVKETEKENKRLLRKRTEDKERMDDFMLNIRKAQEQWKYLRMRNCQRHTSMMNMLESVKKKKHESRDMNWLLQRFEDSIRKYGVAELTTEEILEPEGSRSSSSRTLSNH", "text": "FUNCTION: Plays a role in centriole duplication in meiosis and mitosis (PubMed:28092264). Required for daughter centrioles to acquire duplication competence and become mother centrioles, and for mother centrioles to maintain duplication competence (PubMed:28092264). Regulates spd-2 centriolar localization and affects the recruitment and incorporation of downstream core components (PubMed:28092264). Also required for the assembly of a peripheral centriole structure called the paddlewheel, for centriole elongation and for pericentriolar material assembly (PubMed:28092264). Required to maintain pcmd-1 at the centrosome in early embryos (PubMed:34545391). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localizes to centrioles independently of spd-2."}
+{"protein": "MNSYFEQASGFYGHPHQATGMAMGSGGHHDQTASAAAAAYRGFPLSLGMSPYANHHLQRTTQDSPYDASITAACNKIYGDGASAYKQDCLNIKADAVNGYKDIWNTGGSNGGGTGGGGGGGGAGGNASNGSNAGNAANGQNNAAGGMPVRPSACTPDSRVGGYLDTSGGSPVSHRGGSAGGNVSAGGGGQSGQSGAPGVGVGVGVGVGAGAGTAWNANCTISGAAAAQTAAASSLHQASNHTFYPWMAIAGKIRSDLTQYGGISTDMGKRYSESLAGSLLPDWLGTNGLRRRGRQTYTRYQTLELEKEFHTNHYLTRRRRIEMAHALCLTERQIKIWFQNRRMKLKKEIQAIKELNEQEKQAQAQKAAAAAAAAAAVQGGHLDQN", "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. Binds the consensus region 5'-TTAAT[GT][GA]-3'. This homeotic protein controls development of the cells in the posterior thoracic and first abdominal segments. It activates the synthesis of the decapentaplegic (DPP) growth factor (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family."}
+{"protein": "MLGTKRHWPPGPSLSLELPLALTLLALRAGWAQEGTEPVLLEGECLVVCEPGRAAAGGPGGAALGEAPPGRVAFAAVRSHHHEPAGEIGNGTSGAIYFDQVLVNEGGGFDRTSGSFVAPVRGVYSFRFHVVKVYNRQTVQVSLMLNTWPVVSAFANDPDVTREAATSSVLLPLDPGDRVSLRLRRGNLLGGWKYSSFSGFLIFPL", "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": "MTAGAAPRILKHQVVRAELDRMLDGMRIGDPFPAEREIAEQFEVARETVRQALRELLIDGRVERRGRTTVVARPKIRQPLGMGSYTEAAKAQGLSAGRILVAWSDLTADEVLAGVLGVDVGAPVLQLERVLTTDGVRVGLETTKLPAQRYPGLRETFDHEASLYAEIRSRGIAFTRTVDTIDTALPDAREAALLGADARTPMFLLNRVSYDQDDVAIEQRRSLYRGDRMTFTAVMHAKNSAIVS", "text": "FUNCTION: Represses the phnDCE operon, involved in the uptake of phosphate, under conditions of phosphate availability in the cell. SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MSSATSGEYWLISVPGEKGANDAWDKLNRSTGNTSTNSKYLIPDLKVGTLDQLVGLSDDLSKLDTSAEAVIRKLVQYFTEVLEEDKSKIAENLVIGNKDMKTYVTKFQWEGAKYPLKQSLKVLSEIIGKQISQIDNDLKVKSLTYNNLKNALASMDRKTVGSLLTKDLADLVKADDFVLNSEYLQTVIVVVPKISVKEWEQKYATLSSMVVPGSSKLLTEEGEHALYTVTLFKKVIDEFKNTARENKFIVRDFVYDEETLKAGRTERDKLMAEKQRQYAPLIRWLKINFGEIFAAYIHIKALRVFVESVLRYGLPVNFQAAVIEPAKGQQKKLRQELHKLYIHLDGSAAGPIDTLEDSPALMSLGVNEYYPYVFFKLNIDFLNK", "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 (Probable). 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 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 (By similarity). Has roles in embryogenesis and ovulation (PubMed:10846178). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Note=In embryonic cells, detected in dot-like structures in the cytoplasm around the nuclei. SIMILARITY: Belongs to the V-ATPase C subunit family."}
+{"protein": "MTAEFLSLLCLGLCLGYEDEKKNEKPPKPSLHAWPSSVVEAESNVTLKCQAHSQNVTFVLRKVNDSGYKQEQSSAENEAEFPFTDLKPKDAGRYFCAYKTTASHEWSESSEHLQLVVTDKHDELEAPSMKTDTRTIFVAIFSCISILLLFLSVFIIYRCSQHSSSSEESTKRTSHSKLPEQEAAEADLSNMERVSLSTADPQGVTYAELSTSALSEAASDTTQEPPGSHEYAALKV", "text": "FUNCTION: [Isoform 2]: Behaves as a cytokine, promoting IL17A secretion by CD4+ T-cells, and differentiation and activation of IL17 producing helper T-cells (TH17). FUNCTION: [Isoform 1]: Inhibitory immune receptor involved in the regulation of phagocytes. SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Secreted."}
+{"protein": "MDTFPSIFPPGGDSRLNPEPEFQSMLIDERVRCEHHKHNYQALKIEHKRLQEEYVKSQNELKRVLNEKQTNQEKFQLLLEELRGELVEKVKDMEAMKLQILTPQKLELVKAQLQQELEAPMRERFRTLDEEVERYRAEYNKLRYEHTFLKSEFEHQKEELTRISEEEKMKYKSEVARLEKDKEELHNQLLSVDPTRDSKRVEQLVREKTHLLQKLKSLEAEVAELRAEKENSGAQVENVQRIQVRQLAEMQATLRSLEAEKQSAKLQAERLEKELQSSNEQNTCLISKLHKADREISTLTSQVKELKHANKLEITDVKLEAARAKSELERERNKIQSELDGLQSDNEILKSTVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLSDLEKMKVEHDVWRQSEKDQCEEKLRASQAAEEAARRELQSIRLKLQQQIVNTEKAEKEKLENSELKQQISHLQIQVTSLTQSENDLLNSNQMLKDMVERLKQECRHLRSQAEKVQLEVEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAATAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEEYTRLQKRLKDIQRRHNEFRSLILVPNMPPAASVNPANFQSSAIVPGVELSFPPHLQEEQHQRELSLLRKRLEELETTQRKQLEELGSPGE", "text": "FUNCTION: Component of the distal appendage region of the centriole involved in the initiation of primary cilium assembly. May collaborate with IFT20 in the trafficking of ciliary membrane proteins from the Golgi complex to the cilium during the initiation of primary cilium assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localizes specifically to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. Localizes to centrioles at all stages of the cell cycle, including mitosis (By similarity). SIMILARITY: Belongs to the CEP83 family."}
+{"protein": "MSSCNFTHATFVLIGIPGLEKAHFWVGFPLLSMYVVAMFGNCIVVFIVRTERSLHAPMYLFLCMLAAIDLALSTSTMPKILALFWFDSREISFEACLTQMFFIHALSAIESTILLAMAFDRYVAICHPLRHAAVLNNTVTAQIGIVAVVRGSLFFFPLPLLIKRLAFCHSNVLSHSYCVHQDVMKLAYADTLPNVVYGLTAILLVMGVDVMFISLSYFLIIRTVLQLPSKSERAKAFGTCVSHIGVVLAFYVPLIGLSVVHRFGNSLHPIVRVVMGDIYLLLPPVINPIIYGAKTKQIRTRVLAMFKISCDKDLQAVGGK", "text": "FUNCTION: Olfactory receptor (PubMed:29249973, PubMed:27226631). Activated by the odorant, beta-ionone, a synthetic terpenoid (PubMed:29249973, PubMed:27226631, PubMed:19389702). The activity of this receptor is probably mediated by G-proteins leading to the elevation of intracellular Ca(2+), cAMP and activation of the protein kinases PKA and MAPK3/MAPK1 (PubMed:27226631, PubMed:29249973). Stimulation of OR51E2 by beta-ionone affects melanocyte proliferation, differentiation, and melanogenesis (PubMed:27226631). Activation of OR51E2 by beta-ionone increases proliferation and migration of primary retinal pigment epithelial (RPE) cells (PubMed:29249973). Activated also by the short-chain fatty acids (SCFA) acetate and propionate. In response to SCFA, may positively regulate renin secretion and increase blood pressure (PubMed:23401498). May also be activated by steroid hormones and regulate cell proliferation (PubMed:19389702). Activated by L-lactate in glomus cells (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MQALLFLMALLLPSGAGAEEIIGGVEARPHSRPYMAHLKIITDRGSEDRCGGFLIAPQFVLTAAHCKGREITVTLGAHDVSKSESTQQRIKVEKQIIHKNYNVSFNLYDIMLLKLEEKAELTPTVDVIPLPGPSDFIDPGKMCWTAGWGKTGEKEPTSETLREVELRIMDKEACKMYKHYDYNFQVCVGSSTKLKTAYMGDSGGPLLCAGVAHGIVSYGDSHGKPPAVFTRISAYVPWIKTVINGK", "text": "FUNCTION: Has a chymotrypsin-like activity. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory granules. SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily."}
+{"protein": "IDCCEICCNPACFGCLNDANGLINGDRPIRAQHVC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the heat-stable enterotoxin family."}
+{"protein": "MKLRWFAFLIVLLAGCSSKHDYTNPPWNAKVPVQRAMQWMPISQKAGAAWGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTSGRDVYRRMGWSGEPTTSELKNPERNISMGAAYLNILETGPLAGIEDPKVLQYALVVSYANGAGALLRTFSSDRKKAISKINDLDADEFLDHVARNHPAPQAPRYIYKLEQALDAM", "text": "FUNCTION: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Preferentially cleaves at a distance of more than two disaccharide units from the ends of the glycan chain. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the transglycosylase Slt family."}
+{"protein": "MAHSDRQCTNAAQTALSDAVESARKHNNGFVDPAHLALVLFKNEDGLASRVLRKLNAGTVLEPLAARVGALPEQRPRPRSITFSSDGGCAQHRRAEANRVGDSLIAVDHLLIGLFECKEVEAIMKAAHASKKAVEGALLELRKGKKVTSEFQEENYQALEKYATDLCKLAEEGKLDPVIGRTDEVLRTIRVLSRRTKNNPILIGEPGVGKTAIAEGIAQRIVRGDVPDTLLNTRLFSLDLGALIAGSSLRGEFEERLKSVLNEVKESSNGVILFIDEIHLVLGAGKSGGSMDAANLLKPMLARGELRTIGATTLEEYRTYVEKDAAFERRFMPVYVTEPSVEECISILRGLKDRYEAHHGVQITDNAVVVAAQLANRYITNRFMPDKAIDLIDEACANVRVQLSSRPEAIDILERKKRQLEIEAKALERDKEAASRERLKLVKADIQRVEEELQPLVSKYNDERQRIDELQEMQSRLDEKKKLERAVRDGKMDLAADLQYNVIPLIQDRIRSLKEDIERQKATLVQEKVTEGDVAAVVARWTGIPVVKLSQTDRERLLNLSMHLHRRVKGQDEAVERVADAIIRARAGLSRPNSPTASFLFLGPTGVGKTELVKAVAAELFDDEKHMVRIDMSEYMEQHSVSRLIGAPPGYIGHDEGGQLTEPVRRRPHAVVLFDEVEKAHPNVYNVLLQVLDDGRLTDSRGRTVDFSNTIIVMTSNLGSEHLLNPEETNESYEVLRENVLAAVRSYFRPELINRLDDIVVFRRLRTEDLRGVVDNLIAGVNERLKSSGFSVLLDDGVKDFILEHGHDANMGARPLRRWIEKNIVTEIGRMLIAKELPPNSTLRVSLPEGGNKLTFGVKRGLTSDEWE", "text": "SIMILARITY: Belongs to the ClpA/ClpB family."}
+{"protein": "MVTNKKDTDENRDVQGSIVTKTSAIFPVLVGFRVINSLLTRTYFQADEFWQSLEPAHYKAFGYGELTWEWKVGLRSYAFPMLFEIIYRLVKLLAIASKEALSIICSIGAGLMLLCFPQSKLATEVARDLLTIPNEYSETVEYYGVIYAPKLFMALLAATGEYFTIKLIQKVYLKTVSKNDDQLPKLSNITKIALLLTLTNFFNCFFITRTFINSFEMILTSIALYNWDWSGGIEINTRSFTKSLFFAMFACIQRPSNAIIWIVLGFFLTINLLLRRDYTLIGRLYAKILVVFTITMLVNVVIDFYFYNQIIFPVFKFINFNFTSILSEFYGVAPWHFHLLQSLPIMLGYSLPLFIYGLFSNDSTTKNNIRFGALRQIKFVLILNIIFYSYLKHKEFRFIYPLQPLFCLLSALGALKLAGKVQNYRYLKEYVWIIPLMSMIVSIFITTFQESGVIQVMKDLHNEKDIDSVGFVMPCHSTPWQSYLHRNDIRQLWAISCEPPLHLLGKNNASIELQTYMDESDYLYENISGFIKKNFPKFTNSMDMENVNNNASMPQFPHEWPQFLIIFEQLDNEFMSRYLLDSGYVKYNKIFNSYSHWDSRRNGDLIIYYKNN", "text": "FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB subfamily."}
+{"protein": "MATAAMLCAARALRPRSWIPGTCQAQVRHTHQRASLLSFWELIPMRAEPLRKKKKVDPRKDQAAKDRLKKRIRKLERASQELVPIEDFITPVRFLDKSRQRPQEEHSFEESERRALLLKRWALYKQQEHEMERDAIRAMLEAQQEALEQLKLESTELYAEAIKRDTSLFPFEKEGPHYTPPVPNYQAPEGRYNDITKVYTQVEFKR", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL40 family."}
+{"protein": "MAGKRSGWSRAALLQLLLGANLMVMPPTQARSLRFVTLLYRHGDRSPVKTYPKDPYQEEEWPQGFGQLTKEGMLQHWELGQALRQRYHGFLNTSYHRQEVYVRSTDFDRTLMSAEANLAGLFPPNGMQRFNPNISWQPIPVHTVPITEDRLLKFPLGPCPRYEQLQNETRKTPEYQNESSRNAQFLDMVANETGLTDLTLETVWNVYDTLFCEQTHGLHLPPWASPQTMQRLSRLKDFSFRFLFGIYQQAEKARLQGGVLLAQIRRNLTLMATTSQLPKLLVYSAHDTTLVALQMALDVYNGEQAPYASCHIFELYQEDSGNFSVEMYFRNESDKAPWPLSLPGCPHRCPLQDFLHLTEPVVPKDWQQECQLASGPADTEVIVALAVCGSILFLLIVLLLTVLFRMQAQPPGYRHVADGEDHA", "text": "SUBCELLULAR LOCATION: Lysosome membrane; Single-pass membrane protein; Lumenal side Lysosome lumen Note=The soluble form arises by proteolytic processing of the membrane-bound form. SIMILARITY: Belongs to the histidine acid phosphatase family."}
+{"protein": "MKAYPFTSTTATTMRQNCGGSLMFNMYLSDPTENLLKESKSPSWTPINTGVQKGSGQIQLWQFLLELLSDSANMTCIAWEGTNGEFKLIDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFNGLAQVCQPSSTEQAIYKFQSNFAPIQFSGISKLNLVAPGVGPSGFSYWPGSPPTLYHSHNLQPPGPFGAVSASHLSCVNNINSLNNLNNINNHYN", "text": "FUNCTION: Functions as a transcriptional regulator. Functions in the differentiation and the maintenance of the central serotonergic neurons. May play a role in cell growth (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family."}
+{"protein": "MGIISKRKRHVEDSNSSSDDDDGFDITSNIGLNTADSSDESESSGDDEEEVQDIVDFSDEEDTKKKPKSSNKTLTDNNSFPSLEISDDEDSNNKGDHEDDDDDLNDYFSINNSEKSKHKKGSFPSFGFSKLILSNVHKKGFRQPTPIQRKTIPLILQKRDIVGMARTGSGKTAAFVLPMIEKLKSHSSKIGARAVILSPSRELALQTHRVFKEFSKGTHLRSVLLTGGDSLEDQFSMMMSNPDVIVATPGRFLHLKVEMSLDLKTVEYVVFDEADRLFEMGFQEQLNELLAALPMNRQTLLFSATLPSSLVDFAKAGLTNPVLVRLDAETKISENLEILFLSTKNEERENNLLYLLQDVIKIPLGTDDQIKKLSDFNKSLSDSDSEDEDNKGKQNSRKSKKGKFQKLKVSASNELPTEKSTIVFAPTRHHVEYITQLLKDSGFLVSYLYGTLDQHARKRQLLNFRAGLTSILVVTDVAARGVDIPMLANVINYSLPASSKIFIHRVGRTARAGNRGWAYSIVSETELPYMLDLELFLGKKILLTSMYEASCKLMKSKWIADGNTESSFEDPKISYTNRLVLGSAPRYDIESVGDLYKNIIESNFDLQMAKKVSLKAEKLYCRTRTAASPESIKRSKEVIASGWDEQNIRFGRNLEKEKLNFLAKFQNRRNKETVFEFGKNPNDDTAILMQKRRKQIAPIQRKARKRQELLDKERVAGLTHKIEDEILKGEDHEAGYSVPEEALKSFEDADKILEEQESSRKKKSKTFRDPNFFISHYAPAGDIQDKQLQITSGFTNDAAQAAYDLNDDDKVQVHKQTATVKWDKKRKKYVNMQGIDNKKYIIGESGQKIPASFKSGKFAEWSKSRNIKGIKTGARETSIPTNLLSDPTTDSGSQRGPGGRFKHKQNKAPRLPDKFRDDYQSQKKKVQSAIERGVSVKGFGGSSGNTELKTTAQIRKERMAKEKKRQKNARPTKKRKF", "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. DDX54/DBP10 subfamily."}
+{"protein": "MSPEKSQEESPEEDTERTERKPMVKDAFKDISIYFTKEEWAEMGDWEKTRYRNVKRNYNALITIGLRATRPAFMCHRRQAIKLQVDDTEDSDEEWTPRQQVKPPWMALRVEQRKHQKGMPKASFSNESSLKELSRTANLLNASGSEQAQKPVSPSGEASTSGQHSRLKLELRKKETERKMYSLRERKGHAYKEVSEPQDDDYLYCEMCQNFFIDSCAAHGPPTFVKDSAVDKGHPNRSALSLPPGLRIGPSGIPQAGLGVWNEASDLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYEYVDGKDKSWANWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELGIKWGSKWKKELMAGREPKPEIHPCPSCCLAFSSQKFLSQHVERNHSSQNFPGPSARKLLQPENPCPGDQNQEQQYPDPHSRNDKTKGQEIKERSKLLNKRTWQREISRAFSSPPKGQMGSCRVGKRIMEEESRTGQKVNPGNTGKLFVGVGISRIAKVKYGECGQGFSVKSDVITHQRTHTGEKLYVCRECGRGFSWKSHLLIHQRIHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEKPYVCRECGRGFSRQSVLLTHQRRHTGEKPYVCRECGRGFSRQSVLLTHQRRHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEKPYVCRECGRGFSNKSHLLRHQRTHTGEKPYVCRECGRGFRDKSHLLRHQRTHTGEKPYVCRECGRGFRDKSNLLSHQRTHTGEKPYVCRECGRGFSNKSHLLRHQRTHTGEKPYVCRECGRGFRNKSHLLRHQRTHTGEKPYVCRECGRGFSDRSSLCYHQRTHTGEKPYVCREDE", "text": "FUNCTION: Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localization thereby promoting meiotic recombination (PubMed:24634223, PubMed:24095733, PubMed:26833727, PubMed:27129774). Can also methylate all four core histones with H3 being the best substrate and the most highly modified (PubMed:24095733, PubMed:24634223, PubMed:26833727). Is also able, on one hand, to mono and di-methylate H4K20 and on other hand to trimethylate H3K9 with the di-methylated H3K9 as the best substrate (By similarity). During meiotic prophase, binds specific DNA sequences through its zinc finger domains thereby determining hotspot localization where it promotes local H3K4me3 and H3K36me3 enrichment on the same nucleosomes through its histone methyltransferase activity (PubMed:26833727). Thereby promotes double-stranded breaks (DSB) formation, at this subset of PRDM9-binding sites, that initiates meiotic recombination for the proper meiotic progression (By similarity). During meiotic progression hotspot-bound PRDM9 interacts with several complexes; in early leptonema binds CDYL and EHMT2 followed by EWSR1 and CXXC1 by the end of leptonema. EWSR1 joins PRDM9 with the chromosomal axis through REC8 (By similarity). In this way, controls the DSB repair pathway, pairing of homologous chromosomes and sex body formation (By similarity). Moreover plays a central role in the transcriptional activation of genes during early meiotic prophase thanks to H3K4me3 and H3K36me3 enrichment that represents a specific tag for epigenetic transcriptional activation (By similarity). In addition performs automethylation (By similarity). Acetylation and phosphorylation of histone H3 attenuate or prevent histone H3 methylation (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes in nuclei of pre-leptotene, leptotene, and early to mid-zygotene spermatocytes. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
+{"protein": "MTHLELVPVPPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWMPQGLGKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFINLLPQAQRQAHQAVVIPPYQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGAASLEEAFIAYLQEAAGQSNEAEAPPVVHDTTHAPRQGFSLRRLFSYSRREALELRRDPVRSTLALMGTVILMLIMGYGISMDVENLRFAVLDRDQTVSSQAWTLNLSGSRYFIEQPPLTSYDELDRRMRAGDITVAIEIPPNFGRDIARGTPVELGVWIDGAMPSRAETVKGYVQAMHQSWLQDVASRQSTPASQSGLMNIETRYRYNPDVKSLPAIVPAVIPLLLMMIPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIALGMLNFFLLCGLSVFVFGVPHKGSFLTLTLAALLYIIIATGMGLLISTFMKSQIAAIFGTAIITLIPATQFSGMIDPVASLEGPGRWIGEVYPTSHFLTIARGTFSKALDLTDLWQLFIPLLIAIPLVMGLSILLLKKQEG", "text": "FUNCTION: Exhibits an intrinsic ATPase activity that is stimulated by both 70S ribosomes and 30S ribosomal subunits. Could be involved in protein-chain elongation and in release of deacyl-tRNA from ribosomes after peptide bond synthesis. Stimulates the synthesis of polyphenylalanine in vitro. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. SIMILARITY: In the C-terminal section; belongs to the ABC-2 integral membrane protein family."}
+{"protein": "METDQDMHDQAMAGEETDLDEKYPNRPQNKAPTLPFHDLYETLFRPLREIKKKPVGPAGNRRKAGPHGLSAANLNPIERRRDIIERFISRWRKEVGDDIYPAFRLILPDKDRDRAMYGMKEKIIGKMLVNIMKIDKNSEDGFNLLNWKLPGQSATSSMAGDFAGRCYDVVSKRPMRTEFGNMLIEEVNEKLDQLSSASKEEEQLPILAEFYRRMNPEELAWLIRIILRQMKLGATERTFFDVWHPDAENLYSISSSLRRVCWELHDPNIRLDAEDRGVSLMQCFQPQLAQFQMQSLDRMIARMRPTEDDPVFWIEEKLDGERMQLHMVSDASAPGGRRFRFWSRKAKDYTYLYGNGIYDEAGSLTRHLKDAFADGVDNLILDGEMITWNTEQDAPEPFGTLKTAALSEQRNPFRQGIHPLFRVFDILYLNGRDLTRYTLRDRRNALQKVIKPVHRRFEVHSYEEATTKAEVEASLRKAVAEASEGLVLKNPRSPYRLNERHDDWMKVKPEYMTEFGESLDLVVIGGYYGSGHRGGKLSSFLCGLRVDEGQSSQGSNPTKCYSFCKVGGGFTAADYANIRHHTDGKWVEWNPKKPPTTYIELAGGDSQYERPDMWIKPEDSVVICVKAASVSVSDQFRIGLTLRFPRFKRLRMDKDWKSALSVQEFLDLKSHAEQEHREKEFNVENFRKKRVKKTTKKPLAIAGYDENAEVQYAGPSGHIFDGLNFFILTDSNAPVKKSKAELENLVKANGGRIFQTNDAVPDTICIADRRTVKAASLQKKGDIDIIRPSWILDCIKQSEIDAGLPDLLLPLEPGHMFFMTKDKEEIVAGSLDQFNDSYARDITVEELRNLLDQMAKDGKTDSFCSPEAIQKVTEHIQEKVDSGWTMPCGWLFKGLVLCFPENENDSASEGPEPKQSQRIHLAQNTAKFAGASVTTSLKDTSITHVVVDPDFTSSELPKLRRTLSTRRKLPHIVKVNWIEDSWKENTLLDEEQHMPVYMRRYPNIQLMKV", "text": "FUNCTION: Involved in ds DNA break repair. Has a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologous end-joining. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
+{"protein": "MVKLTTWLKKIGWGETITQRIFCFYIYCILFGSLLLFLPIALQDNYQKVVSYGIDWQGKRFEQKTDYNFLDALFLSTSAFSDTGLSTVVVSKTYSIFGQIVLAVLLQLGGIGFVVIAFLAWRLFNFHKKEQYSFYEKLMLQSERGGSKLGNTSEMILVSIIFLFIVELIYGFLYGILFYFIPGFEPANLFADHAKVSTQLKALVVDSNQTIAAFNDINKAFQAGFFHSLSAVNNAGIDLIGGSSFVPYRNGLGIIIQWLTISQIIFGGIGYPCLFDGFEAIKKKIKYGRHTKHQFSLFTKLTVITNIVVILLFFTLLLMVEFIASDSLTNTIVNFSDEKKSLINTQLQSQSNQAIHASVFGNNPNASRVMQLFFMVISSRSAGFSVFPVASEIQTTKIIIALAMFIGASPSSTAGGIRTTTLAVIFLALVAKFKGQKEVKAFKRSIDQTTVIDAFLVLIISLIAVLLTAVLLPLSMEQPVSFIDALFETTSAFGTVGLSSGATVNIALDPNRNTFNFLALCLLMVMGQVGVSSSVLTFVRKHPKANSYSYPKEAVKIG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TrkH potassium transport family."}
+{"protein": "MLNKAEQISEKSESAYVERFVNAGGVETRYLEAGKGQPVILIHGGGAGAESEGNWRNVIPILARHYRVIAMDMLGFGKTAKPDIEYTQDRRIRHLHDFIKAMNFDGKVSIVGNSMGGATGLGVSVLHSELVNALVLMGSAGLVVEIHEDLRPIINYDFTREGMVHLVKALTNDGFKIDDAMINSRYTYATDEATRKAYVATMQWIREQGGLFYDPEFIRKVPVPTLVVHGKDDKVVPVETAYKFLDLIDDSWGYIIPHCGHWAMIEHPEDFANATLSFLSRRADITRAAA", "text": "FUNCTION: Involved in the degradation of carbazole, a toxic N- heterocyclic aromatic compound containing dibenzopyrrole system. Catalyzes the hydrolytic cleavage of a carbon-carbon bond of 2-hydroxy- 6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid (HOPDA) to yield anthranilate. CarC is specific for 2-hydroxy-6-oxo-6-phenylhexa-2,4- dienoic acid (6-phenyl-HODA), and has little activity toward 2-hydroxy- 6-oxohepta-2,4-dienoic acid and 2-hydroxymuconic semialdehyde. The effect of the presence of an amino group or hydroxyl group at the 2'- position of phenyl moiety of 6-phenyl-HODA on the enzyme activity is found to be small. SIMILARITY: Belongs to the DmpD/TodF/XylF esterase family."}
+{"protein": "MENYLEEELIIGGIEINYLYVCKTKLWYFVRGITMEQESDFVDLGKFLHEKSYFGEEKEVQIGSIKIDFIKKRDVIEIHEVKRGKQMEKAHIMQVLYYIYYLNSLGIKSKAILHYPKLKEIKEIELKENNKEEIKRAIKEIEYIKSLKEPPEPIYQKICKNCAYYELCFI", "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). This protein may be a 5' to 3' ssDNA exonuclease. SIMILARITY: Belongs to the CRISPR-associated exonuclease Cas4 family."}
+{"protein": "MYEDCVKSTEDYYLFCDNEGPWAIVLESLAVIGIVVTILLLLAFLFLMRKVQDCSQWNVLPTQFLFLLAVLGLFGLTFAFIIQLNHQTAPVRYFLFGVLFAICFSCLLAHASNLVKLVRGRVSFCWTTILFIAIGVSLLQTIIAIEYVTLIMTRGLMFEHMTPYQLNVDFVCLLIYVLFLMALTFFVSKATFCGPCENWKQHGRLIFATVLVSIIIWVVWISMLLRGNPQLQRQPHWDDAVICIGLVTNAWVFLLIYIIPELSILYRSCRQECPTQGNVCQVPVYQRSFRMDTQEPTRARDSDGAQEDVALTAYGTPIQLQSADPSREYLIPSATLSPQQDAGL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 3 family."}
+{"protein": "MPYKTAIDCIEELATQCFLSKLTDDDVSTFRRVCSKENDIIKLALRIPRTIDYTSILRLLYDTLPLRSLSFNEALPLFCYSIDPAQQRQCDLRFYLRDVVKLARPRKRLEMQKALLQWLPSLLSDVTLQLLNDIRIRFEEIQPNIRQTVLQIYDRTCYPSLNFEHPNLGVFPETDSIFEPV", "text": "FUNCTION: Plays a role in 2-micron plasmid partitioning. Antagonizes transcriptional repression of recombinase FLP by REP1-REP2 (PubMed:2832156). Regulates both stability and copy number of the plasmid by blocking the formation of the REP1-REP2 repressor complex (PubMed:28472368)."}
+{"protein": "MAPETNEKCKACGGFNFSMIDGFKYCDRCGTLLENFEELEAEEGGIQQTRGAGKIKIKKKGGDDGEKKTTNLVSTNESNVQIMRKALEKRSDFFSRQALKNDELAFPHESTPDYLYRLGLRLAAFTQVLAKVGHVLVKELNFEPRVLPTILATFQRYLAHCHVAFCHSEQCGSDEQLRFVAMMENLEFEQQEREEKRRKKLARRGKGVKALSKSAAAWTLLTQGNITENLDLDSEEDEEEEENPNLNKSMENLEFEDTQNDETVAVNDTTVGFVRKITTALSTEALRRARQMILNLEILVAIIHSALMSCGYRNVLASDVVRWIREDRFRISLRSIRLMRHSAKEQETKEAMTKVDYAEPYLRFPLYEITRTSTLFHQSLNLNEKLVSLNFETLAARLCDNLNLPVEFLSRVLLLESMIPCDVNPSLRKQADVSMGHNCEQLAAIQPKLYNSGFLSCFGRKERTWREADNCDESVKLALLRIQCICRVLLSPDTKLMAYILLVFRLTFDIDNATCSPDSKDALKFDIDTWIHQLEMRLKCWQEHDMSMVLRSSCPVPDIQISTPFGPNYSYYDKKGNPWVHRLRRQVGFAKCIPSEMSFNSTSSLPTVFDIRQNRFKTERRQLEAVMSPLKFQRVILRKEMERDPEKYRNIVDPDSEKTFFKDFTVRKVLENTQKIAETSNSFDEYFPCASRYTIYKRPDWIQNCTARSKQLSPKIGPYRFYISNQACDDLLGVATSSFSPRFKFLLDSLALIIGEDPKALYTAFVMLEMHLTSSDTLETIRESLLRSKPITVKCQKFRKTMWHVECLRRVVTEHPVGKIEDLKYFIVASTRESQEELAESSEAYLMHFRNHEIREDLTSLEAEKVQNRVLKLAYDFETFFGILAVKMW", "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": "YIYTQ", "text": "FUNCTION: In presence of 2,4-D, stimulates proliferation of the cells, but does not stimulate differentiation into the somatic embryos. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phytosulfokine family."}
+{"protein": "IQPPKTFSSLLFSSLLFSSAAQAASEDGSRSPYYVQADLAYAAERITHNYPEPTGADKDKISTVSDYFRNIRAHSIHPRVSVGYDFGGWRIAADYASYRKWKESNFSTKKVTEEIKDNYKETKTEHQGNGSFHATSSLGLSAIYDFKLNDKFKPYIGARVAYGHVKHQVHSVETKTTTVTSKPKGGTPAGGPVIKTDPSKPPYHESHSISSLGLGVIAGVGFDITPKLTLDTGYRYHNWGRLENTRFKTHEASLGMRYRF", "text": "SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the opacity porin family."}
+{"protein": "MRLLFSALLALLSSIILLFVLLPVAATVTLQLFNFDEFLKAASDPAVWKVVLTTYYAALISTLIAVIFGTPLAYILARKSFPGKSVVEGIVDLPVVIPHTVAGIALLVVFGSSGLIGSFSPLKFVDALPGIVVAMLFVSVPIYINQAKEGFASVDVRLEHVARTLGSSPLRVFFTVSLPLSVRHIVAGAIMSWARGISEFGAVVVIAYYPMIAPTLIYERYLSEGLSAAMPVAAILILLSLAVFVALRIIVGREDVSEGQG", "text": "FUNCTION: Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Probably 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": "AYTLATHTAGVIPAGKLERVDPTTVRQEGPWADPAQAVVQTGPNQYTVYVLAFAFGYQPNPIEVPQGAEIVFKITSPDVIHGFHVEGTNINVEVLPGEVSTVRYTFKRPGEYRIICNQYCGLGHQNMFGTIVVKE", "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; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
+{"protein": "MNPVPAQREYFLDSIRAWLMLLGIPFHISLIYSSHTWHVNSAEPSLWLTLFNDFIHSFRMQVFFVISGYFSYMLFLRYPLKKWWKVRVERVGIPMLTAIPLLTLPQFIMLQYVKGKAESWPGLSLYDKYNTLAWELISHLWFLLVLVVMTTLCVWIFKRIRNNLENSDKTNKKFSMVKLSVIFLCLGIGYAVIRRTIFIVYPPILSNGTFNFIVMQTLFYLPFFILGALAFIFPHLKALFTTPSRGCTLAAALAFVAYLLNQRYGSGDAWMYETESVITMVLGLWMVNVVFSFGHRLLNFQSARVTYFVNASLFIYLVHHPLTLFFGAYITPHITSNWLGFLCGLIFVVGIAIILYEIHLRIPLLKFLFSGKPVVKRENDKAPAR", "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": "MNARLTGLGLNLLSFAVGIGGWYLLTATGAVVLPGPVDVLERAVTLLLNGQLVGDIFASLRRVLSGFVLGVALAIPVGFLMGWYRIARSLIEPWVQFFRMIPPLAVIPLAIVTLGIDESPKIFVIFLASFLSSVVATYQGVISVDRTLINAARVLGAKDATIFARVIVPASVPFILVGVRIGLGSAWATVVAAELIAAQSGLGYRMQQAQLYYDLPTIFVSLVTIGILGLFMDRLLQAADRRLTQWQERA", "text": "FUNCTION: Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane (Probable). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family."}
+{"protein": "MSIAGVAAQEIRVPLKTGFLHNGRAMGNMRKTYWSSRSEFKNNFLNIDPITMAYSLNSSAQERLIPLGHASKSAPMNGHCFAENGPSQKSSLPPLLIPPSENLGPHEEDQVVCGFKKLTVNGVCASTPPLTPIKNSPSLFPCAPLCERGSRPLPPLPISEALSLDDTDCEVEFLTSSDTDFLLEDSTLSDFKYDVPGRRSFRGCGQINYAYFDTPAVSAADLSYVSDQNGGVPDPNPPPPQTHRRLRRSHSGPAGSFNKPAIRISNCCIHRASPNSDEDKPEVPPRVPIPPRPVKPDYRRWSAEVTSSTYSDEDRPPKVPPREPLSPSNSRTPSPKSLPSYLNGVMPPTQSFAPDPKYVSSKALQRQNSEGSASKVPCILPIIENGKKVSSTHYYLLPERPPYLDKYEKFFREAEETNGGAQIQPLPADCGISSATEKPDSKTKMDLGGHVKRKHLSYVVSP", "text": "FUNCTION: Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Nucleus Note=Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes (By similarity). SIMILARITY: Belongs to the MIG6 family."}
+{"protein": "MKLSCGTSFAFLLLFLLAAQSVHVYAGSFHKDVQIHWGDGRGKIHDRDGKLLSLSLDKSSGSGFQSNQEFLYGKAEVQMKLVPGNSAGTVTTFYLKSPGTTWDEIDFEFLGNISGHPYTLHTNVYTKGTGDKEQQFHLWFDPTVNFHTYCITWNPQRIIFTVDGIPIREFKNPEAIGVPFPTRQPMRLYASLWEAEHWATRGGLEKTDWSKAPFTAFYRNYNVDGCVWANGKSSCSANSPWFTQKLDSNGQTRMKGVQSKYMIYNYCTDKRRFPRGVPAECT", "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. SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast Cell membrane. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 2 subfamily."}
+{"protein": "MLDYDEVTAFLGEWGTFQRLIFFLLSASIIPNGFTGLSAVFLTAIPEHRCRIPDTVNLSSAWRNHSIPMETKDGPEVPQKCRRYRLATIANFSELGLEPGRDVDLEQLEQENCLDGWEYDKDIFLSTIVTEWDLVCKDDWKAPLTTSFFYVGVLLGSFISGQLSDRFGRKNILFLTMAMHTGFSFIQVFSVNFEMFTLLYTLVGMGHISNYVAAFVLGTEMLSKSVRIIFATLGVCIFFAFGFMVLPLFAYFIREWRRLLLAITLPGVLCGALWWFIPESPRWLISQGRIKEAEVIIRKAAKINGIVAPSTIFDPSETNKLQDDSSKKPQSHHIYDLVRTPNIRILTIMSIILWLTISVGYFGLSLDTPNLNGNIYVNCFLLAAVEVPAYVLAWLLLQHVSRRYSMAGSLFLGGSVLLLVQLVPSDLHYLSTTLVMVGKFGITSAYSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRRLPYILMGSLTILTAIITLFFPESSGVSLPETIDEMQKVKKLKQRQSLSKKGSPKESKGNVSRTSRTSEPKGF", "text": "FUNCTION: Sodium-ion independent, medium affinity carnitine transporter. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 746. SUBCELLULAR LOCATION: Peroxisome 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": "MRHSKRTYCPDWDDKDWDYGKWRSSSSHKRRKRSHSSAQENKRCKYNHSKMCDSHYLESRSINEKDYHSRRYIDEYRNDYTQGCEPGHRQRDHESRYQNHSSKSSGRSGRSSYKSKHRIHHSTSHRRSHGKSHRRKRTRSVEDDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITLREALKHPFFDLLKKSI", "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 and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily."}
+{"protein": "MDTLPDLYGTVGDSLDYFLEHSLQPQRDWKEEGKDAWERIERFFREKCFCDELLLDQEVRVLKVVKGGSSGKGTALNHRSDQDMILFLSCFSSFKQQARDRKAVIDFIKSKLIHCRKSLAYNITVRQHKEGKRTPRSLTLEIQSRKSNDIICMDILPAYNALGSFSRDCKPEPEIYENLIRCKGYPGDFSPSFAELQRHFVKSRPVKLKNLLRLVKFWHLKYLRHKYRRAVLPSKYALELLTIYAWEMGTDSSDNFNLDEGFVAVMELLRDYQDICIYWTKYYDFQNEVVRNFLKEQLKGDRPIILDPADPTNNLGRRGKWELVAKEATYCLLQLCCVTADRWNVQVSIAHYLRGARDVQVTVKQTGREEWILLTNPHSPIRKLKAKIKKRMNLCGELRISFQEPGGERQPLSGRKTLSDYGIFSKVNIRVMETFPPEIQVFVRYPGGQNKPFAIDPDATILSLWEKIEEDGGPCTEDWVLLFEGEELDDDDNLAELQIKDCDTIQLSRVS", "text": "FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Synthesizes oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L (By similarity). SIMILARITY: Belongs to the 2-5A synthase family."}
+{"protein": "MSVLAAIAVLAVLILVHELGHFVAARSQGIHVNRFSLGFGPVLWKYQGAETEYAIRAFPLGGFVGFPDDDPDSDIPPNDPNLLRNRPILDRAIVISAGVIANLIFAYMLLLAQVGFVGIGQASQPGVSIQQLAPEVSAVATNAGLKPGDVILSANQKEFGTSLQEIEALRDIIKNSPGKSIQLTVARGDERLSVNVIPEAKPAGGSIGIGLAPNGKVERRPVSLSKAFSVGASEFQRIVVMTFKGFGQLVTNFGETASQVAGPIKIVEIGANIAQNDTGSLFFFAALISINLAVINILPLPALDGGQLAFLLIEGLRGKPLPNRIQEGVMQTGLVLLLGLGIFLIVKETTQLTTQLEWVQKLFQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family."}
+{"protein": "MPDNPSSFEDEFMKSNHLSVASESIPNESQRQSPTRLRVGTSKTDDIYRQKRQTKHIISQNEVFLQPKFFDNQNFDAQSYLNDVLQDLSEDEFVSLYNKLLRIHMGVRKNLEKNFYKNLNEYVFISGEVESMTSDFKKFQSLLKTLETDIEGLNLVDHTHDPSDESIKQTVQRLRSSIEGLDEAFWEAPQRQLICEQYNWMLINIDNQRPKLLVNMLLFNDRLLVTTSHMKEVDFPAKQQVLYNWNLTEISISSIETYGPAGAEMLQKEKEVSLYKLSINHNNKTTLLAVHNSEERDYMVRQARHHQLQELENWSRKHDEDLEFSRELEYHTKSEQADMCSYTSFQVLCKNLDTQDILQAYAKQRNMVKEISMQFDHLDIQISLQEFTDAIRNLALIQNKLERGNLNELFAEFFADKLHNRKRKVTEILLHQLGFKGISLSHGKEIVRYLRSLGHEKEGQGVFMKSRTLLIKEKCLNVQLEKDTPNFIDACAFIVFRCLAQTTSSYLQLFELKKLDPAYRNWIFQQIEALVDLIENQYKHLAHDRSYTDAVSKIMTYNTELKEAKIDAMPILQRLFDVHSKDLK", "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": "MATVTSSAAVAIPSFAGLKASSTTRAATVKVAVATPRMSIKASLKDVGVVVAATAAAGILAGNAMAAEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNVVFDEDEVPAGVDVTKISMPEEDLLNAPGEEYSVTLTEKGTYKFYCAPHAGAGMVGKVTVN", "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:10220581). SIMILARITY: Belongs to the plastocyanin family."}
+{"protein": "MVMILRRSLINQGADSGAHRTFIPELHTPKMSQGPTLLSCGIMENDRWRDLDRKCPLQIDQPSASIWECLPEKCQDGSLWHQEAVTACAVTSLIKDLNINDHNGNPSAPPSKRQCRSLSFSDEMSSCRTSWRPLGSKVWTPVEKRRCYSGGSVQRYSNGVSPMQRSSSFSLPARANGLSSPCHQSSLHHRFGGQPCQGAPGSAPCGQAGDSWSPDPHPVGGGRLDLQRSLSCSHEQFSFPEYCPPSANSTPASTPELARRSSGLARSRSQPCVLNDKKIGVKRRRPDEVQEQRPSLDLAKMAQNCQTFSSLSCLNMGVDDHSSQSPFALVSSTRSWTALLSASSPGGRTPAGTPVPEPVPHSFDDQFTCQEDLSCDESDGCSLDEDCCRKGDPATSWRDRGACTNSLCSLDGELDIEQIENN", "text": "FUNCTION: Acts as a regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) nuclear localization. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FAM53 family."}
+{"protein": "MEAALEQHLEDTMKNPSIVGVLCTDSQGLSLGCCGSLSDKHAGVISILPQYAAKLTSDPTDVPVVCLESDNGIVMIQKHDHLTVAVHKVTS", "text": "FUNCTION: Regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, may activate the TOR signaling cascade in response to amino acids (By similarity). SUBCELLULAR LOCATION: Cytoplasm Lysosome. SIMILARITY: Belongs to the LAMTOR5 family."}
+{"protein": "MAVIQDIIAALWQHDFAALANPHVVSVVYFVMFATLFLENGLLPASFLPGDSLLLLAGALIAQDVMHFLPTIGILTAAASLGCWLSYIQGRWLGNTRTVKGWLAQLPAKYHQRATCMFDRHGLLALLAGRFLAFVRTLLPTMAGISGLSNRRFQFFNWLSGLLWVTVVTSFGYALSMIPFVKRHEDQVMTFLMILPVALLVAGLLGTLVVVIKKKYCNA", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DedA family."}
+{"protein": "MGSPPCALGLFCCCSSCFCLCCPRHRPVSRLAAVVGGAAAVPAVVSGVTGLILSPSQSPIFIQPTPLPQTLPLRPGLDLAFANQPGHLAPLGEIRPSAPPLPPVADLPQPGLRR", "text": "FUNCTION: Small multifunctional phosphoprotein involved in virion morphogenesis, egress and counteracting host innate immunity. 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. Acts also as a viroporin and forms ion conductive pores allowing viral particle release. Impairs the generation of type I interferon by down- regulating host TLR3 and TLR7 as well as their downstream signaling pathways. Down-regulates the phosphorylation of host IRF3 via the interaction with host SIRP-alpha, thereby inhibiting IFN-I expression. Interacts with host microtubules. SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Lipid-anchor Host cytoplasm, host cytoskeleton Virion Host cell membrane; Lipid-anchor Note=The N-terminal region seems to associate with the cytoskeleton probably via one of its hydrophobic regions. Present on the surface of the membrane-wrapped virions. SIMILARITY: Belongs to the hepevirus ORF3 protein family."}
+{"protein": "STAADAEEKLMNHLLSPDRYNKLIRPAVNSSQLVSIELQVSLAQLISVNEREQIMTTNVWLNQEWIDYRLAWKPSDYEGINMLRIPAKHIWLPDIVLYNNADGTYEVSLYTNAIVQNNGSIRWLPPAIYKSACKIEVKHFPFDQQNCTLKFRSWTYDHTEIDMVLKTSMASMDDFTPSGEWDIVALPGRRTENPLDPNYVDVTYDFIIKRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMPPWVKLVFLERLPAYLFMKRPENNSPRQKPANCKKTRAENLCMDPADFYKNSTYFVNTASAKKYDMKITDTLDNVSSHQDFRLRTGTKFSPEVQEAIDGVSFIAEHMKSDDNDQSVIEDWKYVAMVVDRLFLWIFVLVCVLGTVGLFLQPLFQNHIAATNP", "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": "MASSSSSLLILAVACFVSLISPAISQQACKSQNLNSAGPFDSCEDLPVLNSYLHYTYNSSNSSLSVAFVATPSQANGGWVAWAINPTGTKMAGSQAFLAYRSGGGAAPVVKTYNISSYSSLVEGKLAFDFWNLRAESLSGGRIAIFTTVKVPAGADSVNQVWQIGGNVTNGRPGVHPFGPDNLGSHRVLSFTEDAAPGSAPSPGSAPAPGTSGSTTPGTAAGGPGNAGSLTRNVNFGVNLGILVLLGSIFIF", "text": "FUNCTION: One-heme-containing cytochrome. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor."}
+{"protein": "MLEVVLQVLSISAITTTIALFFCGIPICMQIRRQGAVGDISGVPFLMGVLGGSFWLRYGLLKMDYVMIIVNVVGVACMAFYCVFFLIYSLPKKTFTCQLILVTSTIGGMVLWIALKPNLDYLGVICMTFNIMNFGAPLAGLGVVLKNREVSTLPLPMCVANFLVSSQWCLYGNLVSDIYIIIPNGIGMFLAIVQLALFVVLPIRENEKSPLEKLASWFTGRDSKVKDLERGDCIVSSPPSSPQKVPNETRSDVEDKFDKLMAETSSTIPSDSRRGSMGSPPSYKSRSSSDPDLSSIQSP", "text": "FUNCTION: Mediates both low-affinity uptake and efflux of sugar across the membrane. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SWEET sugar transporter family."}
+{"protein": "MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIYLEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEWVRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNLSTSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRLFKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQNLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVLNIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPMLMGPPPRSTNFFGFLS", "text": "FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:2175712, PubMed:15544348). 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 (PubMed:2175712, PubMed:15544348). Also plays an important role in the biosynthesis of complex lipids (Probable). Can also phosphorylate 1-alkyl-2- acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group (PubMed:15544348). Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol (PubMed:22627129). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family."}
+{"protein": "MEYWKHTNHRKDAGNELETSMATHGNKLTNKITYILWTIILVLLSIVLIIVLINSIKSEKAHESLLQDINNEFMEITEKIQMASDNTNDLIQSGVNTRLLTIQSHVQNYIPISLTQQMSDLRKFISEIIIRNDNQEVPPQRITHDVGIKPLNPDDFWRCTSGLPSLMKTPKIRLMPGPGLLTMPTTVDGCVRTPSLVINDLIYAYTSNLITRGCQDIGKSYQVLQIGIITVNSDLVPDLNPRISHTFNINDNRKSCSLALLNTDVYQLCSTPKVDERSDYASSGIEDIVLDIVNYDGSISTTRFKNNNISFDQPYAALYPSVGPGIYYKGKIIFLGYGGLEHPINENVICNTTGCPGKTQRDCNQASHSPWFSDRRMVNSIIVVDKGLNSIPKLKVWTISMRQNYWGSEGRLLLLGNKIYIYTRSTSWHSKLQLGIIDITDYSDIRIKWTWHNVLSRPGNNECPWGHSCPDGCITGVYTDAYPLNPTGSIVSSVILDSQKSRVNPVITYSTATERVNELAIRNKTLSAGYTTTSCITHYNKGYCFHIVEINHKSLDTFQPMLFKTEVPKSCS", "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": "MSKDFDLIIRNAYLSEKDSVYDIGIVGDRIIKIEAKIEGTVKDEIDAKGNLVSPGFVDAHTHMDKSFTSTGERLPKFWSRPYTRDAAIEDGLKYYKNATHEEIKRHVIEHAHMQVLHGTLYTRTHVDVDSVAKTKAVEAVLEAKEELKDLIDIQVVAFAQSGFFVDLESESLIRKSLDMGCDLVGGVDPATRENNVEGSLDLCFKLAKEYDVDIDYHIHDIGTVGVYSINRLAQKTIENGYKGRVTTSHAWCFADAPSEWLDEAIPLYKDSGMKFVTCFSSTPPTMPVIKLLEAGINLGCASDNIRDFWVPFGNGDMVQGALIETQRLELKTNRDLGLIWKMITSEGARVLGIEKNYGIEVGKKADLVVLNSLSPQWAIIDQAKRLCVIKNGRIIVKDEVIVA", "text": "FUNCTION: Transforms N-isopropylammelide to cyanuric acid and isopropylamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. N- acyl-D-amino-acid deacylase family."}
+{"protein": "MNKKTLLVIFFITMLIVDEVNSFKIGGFIKKLWRSKLAKKLRAKGRELLKDYANRVINGGPEEEAAVPAERRR", "text": "FUNCTION: Amphipathic peptide that displays potent antimicrobial activities against a range of Gram-positive and Gram-negative planktonic bacteria with MIC values in the range 5 uM to 10 uM (Ref.2). In more details, it is active on Listeria ivanovii (MIC=5 uM), Staphylococcus epidermidis (MIC=10 uM), Salmonella enterica (MIC=5 uM), Pseudomonas aeruginosa (ATCC 27853) (MIC=5 uM), Acinetobacter baumannii (MIC=5 uM), Klebsiella pneumoniae (MIC=5 uM), Escherichia coli (MIC=7.5 uM), Salmonella typhimurium (MIC=7.5 uM), Pseudomonas aeruginosa (ATCC 9027) (MIC=10 uM) (Ref.2). Is also able to prevent P.aeruginosa biofilm formation while showing weak hemolytic activity towards human erythrocytes (Ref.2). Probably induces bacterial cell death through membrane permeabilization (Ref.2). Moreover, shows DNA-binding activities (Ref.2). Also exerts potent selective cytotoxic and antiproliferative activity against three different prostate cancer cell lines (IC(50)=4.4-7.8 uM), compared to non-tumorigenic cell lines (IC(50)=59.7 uM in Vero and 62.5 uM in HUVEC cells) (Ref.1). This peptide possibly exerts its cytotoxic activity through a necrotic mode of cell death (Ref.1). 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. Long chain multifunctional peptide (group 2) family."}
+{"protein": "MFYAHAFGGYDENLHAFPGISSTVANDVRKYSVVSVYNKKYNIVKNKYMWCNSQVNKRYIGALLPMFECNEYLQIGDPIHDLEGNQISIVTYRHKNYYALSGIGYESLDLCLEGVGIHHHVLETGNAVYGKVQHEYSTIKEKAKEMNALKPGPIIDYHVWIGDCVCQVTTVDVHGKEIMRMRFKRGAVLPIPNLVKVKVGEENDTINLSTSISALLNSGGGTIEVTSKEERVDYVLMKRLESIHHLWSVVYDHLNVVNGEERCYVHMHSSHQSPMLSTVKTNLYMKTMGACLQMDSMEALEYLSELKESGGRSPRPELQKFEYPDGVKDTESIERLAEEFFNRSELQAGESVKFGNSINVKHTSVSAKQLRTRIRQQLPSILSSFANTKGGYLFIGVDNNTHKVIGFTVGHDYLKLVESDIEKYIQKLPVVHFCKKKEDIKYACRFIKVYKPGDETTSTYVCAIKVERCCCAVFADWPESWYMDTSGSMKKYSPDEWVSHIKF", "text": "FUNCTION: Nuclease that is responsible for viral evasion of host cGAS- STING innate immunity. Cleaves 2',3'-cGAMP which is produced by host cGAS following recognition of cytosolic DNA and blocks the subsequent 2',3'-cGAMP-mediated activation of TMEM173/STING, which normally spreads to adjacent cells and activates the interferon and NF-kappa-B immune responses. SIMILARITY: In the C-terminal section; belongs to the Schlafen protein family. Subgroup poxviridae B3 subfamily. SIMILARITY: In the N-terminal section; belongs to the poxin family."}
+{"protein": "MANRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFSRAKNWVKELQRQASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTPMNVNEIFMAIAKKLPKNEPQNPGANSARGRGVDLTEPAQPARSQCCSN", "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 to regulate cellular responses such as of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Active GTP-bound form is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan. Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Early endosome membrane; Lipid-anchor Melanosome Cytoplasmic vesicle Cell projection, ruffle Membrane Cytoplasm, cytosol Cytoplasmic vesicle, phagosome membrane Endosome membrane Note=Enriched in stage I melanosomes. Alternates between membrane-bound and cytosolic forms. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MAPFSAETNSTDLLSQPWNESPVILSMVILSLTFLLGLPGNGLVLWVAGLKMQRTVNTVWFLHLTLADLLCCLSLPFSLAHLALQGQWPYGRFLCKLIPSIIVLNMFASVFLLTAITLDRCLVVFKPIWCQNHRNVGTACTICGCIWVVAFVMCIPVFVYREIFTTDNHSKCGYKFDLSGSLDYLDFYGNPLENRSLENIFQLPGEMNDRLDPSSFQANDHPWTVTTAFHTQTFQRPSADSLPKDSASHSPYSNVFKPAGVASPKIPSGFPIEGHKTSPLDDSDAFLSTHLKLFPSAASNSLYEYELPQDFQDYYSLGQFTYDNQVSTPLVAITITRLVVGFLLPSVIMIACYSFIVLRMQRGRFAKSQGKTLRVAVVVVTVFLVCWAPYHISGVLSLFTDPETPLGKTLMSWDHVFTALASANSCFNPFLYALLGKDFRKKARQSIQSILEAAFSEELTHSTHCSSNNVFSERNSISTTV", "text": "FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
+{"protein": "MAIIMAESSYERRVKALYEKQIRMETLEGKFIKKVFKFNSILLDVKEAAARHQRKVEKMQKVVIERREELEKRVSFMGQLAQEVEATKLRNLAMKDRIKQQKMLARERNNEIMERIHTLSKTTGTYVNQEALPARVKGVTVLRGDKRDQLIPFDLNATDAEGLNSLCQHLESLNVDVSQWQQLVSLVMDVTMEARAPTTPPKEAANCKSIIEIDLTSPTS", "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": "MLLLKKQTEDISSVYEIREKLGSGAFSEVMLAQERGSAHLVALKCIPKKALRGKEALVENEIAVLRRISHPNIVALEDVHESPSHLYLAMELVTGGELFDRIMERGSYTEKDASHLVGQVLGAVSYLHSLGIVHRDLKPENLLYATPFEDSKIMVSDFGLSKIQAGNMLGTACGTPGYVAPELLEQKPYGKAVDVWALGVISYILLCGYPPFYDESDPELFSQILRASYEFDSPFWDDISESAKDFIRHLLERDPQKRFTCQQALQHLWISGDAALDRDILGSVSEQIQKNFARTHWKRAFNATSFLRHIRKLGQSPEGEEASRQGMTRHSHPGLGTSQSPKW", "text": "FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro, isoform 1 and isoform 2 phosphorylate CREB1, SYN1/synapsin I. Phosphorylates and activates CAMK1. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily."}
+{"protein": "MYDKLNVALSKDLRKKYGIRSFPIVKGDVVKVVSGARKGEGGKVAEVDHHSGLVIVEGITIAKIDGKQKGFGISPEKLQITHLDLSRSERFQKIKELANIKHITIQEEPIQEEQQKTEETKQEIAPEEVEAKEAQDKQEVKENDQ", "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": "MNGDNASSAADRAGGPAATPVPIPIGWQRCVREGAVYYISPSGTELSSLEQTRSYLLSDGTCKCGLECPLNVPKVFNFDPLAPVTPGGAGVGPASEEDMTKLCNHRRKAVAMATLYRSMETTCSHSSPGEGASPQMFHTVSPGPPSVRPPCRAPPTTPLNGGPGSIPQDPPSVPQAFPPLTGPAGLFPPPRLPDPVPSAGSSSPCFLPRGNAPSPAPPPPPAISLNAPSYNWGASLRSNLVPSDLGSPPAPHASSSPPSDSPLFHCSDALTSPPLPPSNNPPGPPGPPGPATQPPVSSATMHLPLVLGSLGGAPAVEGPGAPPFLASSLLSAAAKAQLPPPSTLQGRRPRAQAPSAAHASPRPSQRRPRRPPTVLRLLEGGGPQTPRRTRPRAPAPVPQPFPLPEPSQPILPSVLSLLGLPTPGPSHSDGSFNLLGSDAHLPPPPALSSGSPPQPRHPIQPSLPGTTSGSLSSVPGAPAPPAASKAPVVPSPVLQSPSDGLGMGAGPACPLPPLAGGEAFPFPSPEQGLALSGAGFPGMLGALPLPLSLGQPPPSPFLSHSLFGVLAGGGQPPPEPLLPPPGGPGPPSAPGEPEGPSLLVASLLSPPPSDLLPPPSAPPSNLLASFLPLLALGPTAGDGEGSAEGAGGPNGEPFSGLGDLPPLLFPPLSAPPTLIALNSALLAASLDPPSGTPPQPCVLSAPQPGPPTSSVTTATTDPGASSLGKAPSNSGRPQLLSPLLSASLLGDLSSLASSPGALPSLLQPPGPLLSSQLGLQLLPGGGAPPALSEASSPLACLLQSLQIPPEQPDAPCLPPESPASALEPEPARPPLSALAPPHASPDPPVPELLTGRGSGKRGRRGGGGLRGINGETRPGRGRKPGSRREPGRLALKWGTRGGFNGQMERSPRRTHHWQHNGELAEGGAEPKDPPLPGTHSEDLKVPPGIVRKSRRGRRRKYNPARNSSSSRQDVTLEPSPTTRAAVPLPPRARPGRPAKNKRRKLAP", "text": "FUNCTION: Binds to heterochromatin. Does not interact with either methylated or unmethylated DNA (in vitro) (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Associated with pericentric heterochromatin in about 25% of the cells."}
+{"protein": "MRPLSRLHFPRGSLPLCPYSGSSAEAEAYQRLRGVRAASELWCELHDLAEHLLPIVSKRGRRPDDEAGRSLMLRNAADRLRASFVRAVELSKPSADAQDKGRSDGAGDKQKGGDAARDGGEMAGLSQLLFLPSPALHRPPIRVGPTEDCLNSDMTSSDAAVPHAYGSSSSSSDEAGVPGRRRSRRRRCVHAWRKENVEARARAQSNNLRAAVSAVLLDRWLPIGDARNTCTPPGELEERLLAAVLAAAHWCCLWHDSPCGAGSLYADIYAEDIFATGAPQR", "text": "SUBCELLULAR LOCATION: Virion tegument. Host nucleus matrix. SIMILARITY: Belongs to the herpesviridae US10 family."}
+{"protein": "MGNSSSSGSHRPPRPASSESALPPAAAAAEELSSYEAACRSDPELRTFDTTLQRRTSRAISTLAVGVEVRSLSLESLREVTGCLLDMNQEVVRVILDCKKDIWKSPELFDLVEDYFESSLHTLDFCTALDKCLKRARDSQLLLHVALQRFDDEEDNDAAAAGQEDAAPSARYARTLHELRQFKAAGDPFTEEFFSAFQAVYRQQLTMLEKLQQRKHRLDKKVRAIKAWRRVSSIIFATTFAAVLICSVVAAAIAAPPVAAALAAAASIPVGSMGKWIDSLLKGYQDALRGQKEVVSAMQVGTFIAIKDLDSIRVLINRVELEISSMIDCVEFAERDEEAVKFGVEEIKKKLEVFMKSVEDLGEQADRCSRDIRRARTVVLQRIIRHPS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0496 family."}
+{"protein": "MSDAGGDVQVAPAAVAQGPMDKEGALRAVLRAAHHADGLAKGLHETCKALDKREAHFCVLAENCDEPQYVKLVETLCAEHQIPLIKVADKKIIGEYCGLCKYDKEGKARKVVGCSSAVVTNWGNEEQGRAILTDYFASKN", "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 (By similarity). Subunit of the 40S ribosomal complex (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS12 family."}
+{"protein": "MAEKFDHLEEHLEKFVENIRQLGIIVSDFQPSSQAGLNQKLNFIVTGLQDIDKCRQQLHDITVPLEVFEYIDQGRNPQLYTKECLERALAKNEQVKGKIDTMKKFKSLLIQELSKVFPEDMAKYRSIRGEDHPPS", "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. 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 10 family."}
+{"protein": "MEYRLKAYYREGEKPSALRRAGKLPGLMYNRHLNRKVYVDLVEFDKVFRQASIHHVIVLELPDGQSLPTLVRQVNLDKRRRRPEHVDFFVLSDEPVEMYVPLRFVGTPAGVRAGGVLQEIHRDILVKVSPRNIPEFIEVDVSGLEIGDSLHASDLKLPPGVELAVSPEETIAAVVPPEDVEKLAEEAAAEVAEPEVIKKGKEEEEE", "text": "FUNCTION: This is one of 3 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit. SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily."}
+{"protein": "MTGRYSRQELFAPIGPSGQKKLKEARAVIIGAGALGTASAEMLVRAGVGSVKIADRDYVEWSNLQRQQLYTEDDVKKEMPKAAAAERRLRSINSDVDVTGLVMDVTAENIFELIRDASIIVDAADNFETRLIVNDAAVKEGIPFLYGACVGSYGLTFTVVPGSTPCLHCLLDALPIGGATCDTAGIISPAVLQVAVFQVTDALKLLTGEECEPVLRSFDLWKNERSEVRAASLKHDACPSCGTKDFPFLSYENQTKAAVLCGRNTVQIRSSITKEADLEALAGQLRQAGLEVAANPYLISCRSDDMKMVLFRDGRALIHGTNDIARAKSIYHKWIG", "text": "FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS. SIMILARITY: Belongs to the HesA/MoeB/ThiF family."}
+{"protein": "MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS", "text": "FUNCTION: Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (PubMed:26246606, PubMed:12390251, PubMed:18615013, PubMed:11039908, PubMed:17125279, PubMed:17360485). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (PubMed:26246606, PubMed:14523000). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426). Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:18056443, PubMed:15128871, PubMed:14702041, PubMed:11551964, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18615013). Regulates KIF2A tubulin depolymerase activity (PubMed:19351716). Important for microtubule formation and/or stabilization (PubMed:18056443). Required for normal axon formation (PubMed:19812038). Plays a role in microtubule remodeling during neurite extension (PubMed:19668197). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint- response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (PubMed:14702041). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723, PubMed:20643351). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cell projection, neuron projection Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Basolateral cell membrane Note=Detected at the neurite hillock in developing neurons (By similarity). Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase (PubMed:9606188, PubMed:17229885, PubMed:21225229). Colocalized with SIRT2 at centrosome (PubMed:22014574). Moves to the midbody during both telophase and cytokinesis (PubMed:17726514). Associates with both the pericentriolar material (PCM) and centrioles (PubMed:22014574). The localization to the spindle poles is regulated by AAAS (PubMed:26246606). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily."}
+{"protein": "MALKELLGSDAPLEKVCSALLEYESKRKSSENIDSESKKTNLLEDEQDDIEPVWLQLATLKFIGNNRKLIPYKIAIKNPVIPSSSEACLIVKDPQRVYKDLVNEAGLSKVVTRVIGLSKLKAKWNSYEQKRQLRDQFDIFLADDRVIPMLPRILGKTFYQKSKVPVPVKISKGTAEQLKREVVSAYGATYFNSAPCSSFMIKCGHVSNTSTELAENVESILQFVSKHIVPDGAKGIASIHLKTSQSIAIPLWNNPNLKELIASSRKVVTKETASSKRKSDEESLPSQKKQKKVEVAKESKDSKQQNVSDKKQVTVKEVPKKLSVKNAAKTTNRDEDSKGKKAKASPKVSQSSLKANGTTAIKKVKAGKNKVKH", "text": "FUNCTION: Involved in rRNA-processing and ribosome biosynthesis. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the universal ribosomal protein uL1 family. Highly divergent."}
+{"protein": "MAAEACVPAEFSKDEKNGSILSAFCSDIPDITSSTESPADSFLKVELELNLKLSNLVFQDPVQYVYNPLVYAWAPHENYVQTYCKSKKEVLFLGMNPGPFGMAQTGVPFGEVNHVRDWLQIEGPVSKPEVEHPKRRIRGFECPQSEVSGARFWSLFKSLCGQPETFFKHCFVHNHCPLIFMNHSGKNLTPTDLPKAQRDTLLEICDEALCQAVRVLGVKLVIGVGRFSEQRARKALMAEGIDVTVKGIMHPSPRNPQANKGWEGIVRGQLLELGVLSLLTG", "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. Does not exhibit any enzymatic activity towards G/T mismatches. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. SMUG1 family."}
+{"protein": "MSLGTTDIASETGDDSLSAITFESDIESKTKRKSFHKPPSTSPKSPYYSKPRKVTSWRSLKTAGSMPLSSRMSLTPQKLWLGSSKQGSVAQPPSPTLTSEHAWTHPPSCTPDYLTEAVRAKRADLRRSGSHGHVSGTSVYREKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGWVITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPCSEERREAAIRTLQAQWKAHRRKKREAALDEAATVLQAAFRGHLARSKLVRSKVPDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQARFIASCCREIAASSQRETVSLTPSGSASPPSLRASPGVIRKELCASEELRETSASEPAPSVPYSAQGGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSPF", "text": "FUNCTION: Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling (PubMed:24582806). Required for proper limb morphogenesis (By similarity). SUBCELLULAR LOCATION: Cell projection, cilium membrane; Peripheral membrane protein; Cytoplasmic side Note=The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner (PubMed:24582806)."}
+{"protein": "MGVEPFAHDPAPSELIHSVPACGSPERRVMRPMVREGWLADRQHSDRRGRGRERFLPVSWDAALDLVAGEIRRVSADHGNAAIFAGSYGWTSCGRFHHASTLLKRMLNLVGGFTGHVDTYSIAAGPVILRHTLGDDRACGGQANTLDSIAEHSQTLVVFGAMSPRTAQSEAGGIGAHHLETYLRRIVERGVRVILVSPLKDDLPDWVAAEWWPIRPNTDTALMLGLAGEIVRSGRQDSDFLARCTSGSELYLAYLRGEGDGRPKDAEWASTITGLPAEAIRALAGDLPRTRSMLTVSWSLQRAHHGEQPFWAALGLAAVIGQIGRPGGGVGYGYGSLGGVGAPFTIGKSPAMSQLSKPINSFIPVARISDMLLNPGGPYSYEGEDRRYPDIRLVYWSGGNPFHHHQDLNRLSEAWTRPETIIVQDPMFTATAKRADIVLPASTSIERNDLAGNKRSDFILAMGQAIAPLGEARSDFDIFNALSGKLGVAAAFNEGRDEMGWIRHLYEESRNHAQRHHHFEMPDFETFWAQGHAPCPVQRDHTYLAAFREDPGAHPLDTESGLIVLGSATLARLGYADCGPHPAWIEPAEWLGKAQAGELHLISHQPKGRLHSQLETAEASLAGKREGRDEVMLHPDDASVRGIADGQTVRLWNARGACLATAQVTDSVAAGVAILPTGAWFTPAEAEGPELSGNPNVLTLDIGSSAFGQGCSAHTCLVRIEAHAGDAGDAVRIYDAHLAAILPT", "text": "FUNCTION: This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin (By similarity). SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family."}
+{"protein": "RNGLPGPIGPAG", "text": "FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the fibrillar collagen family."}
+{"protein": "MGSLSTANVEFCLDVFKELNSNNIGDNIFFSSLSLLYALSMVLLGARGETAEQLEKVLHFSHTVDSLKPGFKDSPKCSQAGRIHSEFGVEFSQINQPDSNCTLSIANRLYGTKTMAFHQQYLSCSEKWYQARLQTVDFEQSTEETRKMINAWVENKTNGKVANLFGKSTIDPSSVMVLVNIIYFKGQRQNKFQVRETVKSPFQLSEGKNVTVEMMYQIGTFKLAFVKEPQMQVLELPYVNNKLSMIILLPVGIANLKQIEKQLNSGTFHEWTSSSNMMEREVEVHLPRFKLEIKYELNSLLKPLGVTDLFNQVKADLSGMSPTKGLYLSKAIHKSYLDVSEEGTEAAAATGDSIAVKSLPMRAQFKANHPFLFFIRHTHTNTILFCGKLASP", "text": "FUNCTION: Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily."}
+{"protein": "MEFPEHGVRLLGRLRQQRELGFLCDCTVLVGDARFPAHRAVLAACSVYFHLFYRDQPASSRDTVRLNGDIVTVPAFSRLLDFMYEGRLDLHNLPVEDVLAAASYLHMYDIVKVCKGRLRKKDPDLETRTLGTELPGQPPHPLPSWSPAFCQAAPKAKHPSLGVKATHPLPTFGPPSWQVAEQSSGALDLSLKPSPRPEQVHPPCRLQTSLCSSVQQVAQPLVKAEQDSFSEQDSSSPQSADRSPPPVCASAAQGLAVDLEPLHIEGTGSQQLGLPAEPVLDSEELGPSRHLCICPLCCKLFPSTHALQLHLSAHFRERDSVRARLSPEGSVPTCPLCSKTFSCTYTLKRHERTHSGEKPYTCVQCGKSFQYSHNLSRHAVVHTREKPHACRWCERRFTQSGDLYRHVRKFHYGLVKPLLV", "text": "FUNCTION: Transcriptional repressor. Specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Note=In skeletal myofibers, highly enriched in subsynaptic nuclei at the neuromuscular junctions. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family. ZBTB18 subfamily."}
+{"protein": "MASNNPHDNLSDQTPSDDFFEQILGLPNFSASSAAGLSGVDGGLGGGAPPMMLQLGSGEEGSHMGGLGGSGPTGFHNQMFPLGLSLDQGKGPGFLRPEGGHGSGKRFSDDVVDNRCSSMKPVFHGQPMQQPPPSAPHQPTSIRPRVRARRGQATDPHSIAERLRRERIAERIRALQELVPTVNKTDRAAMIDEIVDYVKFLRLQVKVLSMSRLGGAGAVAPLVTDMPLSSSVEDETGEGGRTPQPAWEKWSNDGTERQVAKLMEENVGAAMQLLQSKALCMMPISLAMAIYHSQPPDTSSVVKPENNPPQ", "text": "FUNCTION: Required for ovule fertilization. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLSRILGVRNHSFRAFSTIGVCYNKSNTSPKKYLSPNEFASQKQVDEIEEQAYKQNLLNEEYKYDPKYLSENELNPISKRPIPLNVELLKYKPVQLPPTHGHEVAKIEFKGYDKDDLIRASEFAARAAFYLGIPCSKVQSLKTEKRLYTVIKSPFAQAKSKENFKRTTYGRKVYAYDATPEVVDLWLSFINKHAIEGVKYNALIHTRESLDFCEKLDALSADDMHMPDAYKGSDDPIANKVEELLKSDTFKKYFDEANIAESPKESK", "text": "FUNCTION: Involved in mitochondrial genome encoded proteins translation. Involved in the binding of tRNA to the ribosomes (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS10 family."}
+{"protein": "IPRITSDRLLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHESTKEELEALVRDKGVNSFLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYITKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPINPDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGINGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGMPTVVISQGRVVLEDGNLLVTPGAGRFIPRKTFPDFVYKRIKARNRLAEIHGVPRGLYDGPVHEVMLPAKPGSGTQARASCPGKISVPPVRNLHQSGFSLSGSQADDHIARRTAQKIMAPPGGRSNITSLS", "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. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family."}
+{"protein": "MGLLSILRKLKSAPDQEVRILLLGLDNAGKTTLLKQLASEDISHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWKNYFENTDILIYVIDSADRKRFEETGQELAELLEEEKLSCVPVLIFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALTGEGVQDGMNWVCKNVNAKKK", "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) (PubMed:16525022, PubMed:18588884). Required for normal cytokinesis and cilia signaling (PubMed:22085962). Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for targeting proteins to the cilium, including myristoylated NPHP3 and prenylated INPP5E (PubMed:30269812). Targets NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium (PubMed:22085962). Required for PKD1:PKD2 complex targeting from the trans-Golgi network to the cilium (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm. Cell projection, cilium Note=Detected predominantly in the photoreceptor connecting cilium. Present on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
+{"protein": "MANSGEEKLKLYSYWRSSCAHRVRIALALKGLDYEYIPVNLLKGDQFDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDEKYPEPPLLPRDLHKRAVNYQAMSIVLSGIQPHQNLAVIRYIEEKINVEEKTAWVNNAITKGFTALEKLLVNCAGKHATGDEIYLADLFLAPQIHGAINRFQINMEPYPTLAKCYESYNELPAFQNALPEKQPDAPSSTI", "text": "FUNCTION: Acts a maleylacetone isomerase. Also catalyzes the glutathione-dependent dehalogenation of dichloroacetic acid to glyoxylic acid. In vitro, possesses glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. Zeta family."}
+{"protein": "MSELSQMTLKILYTLDNGSNGSYLARSRAPKQVRVANIPSPFPTDSNEQTELRIGAIHLKTILHEIYLNSPEVLDHDTLKDGYDYNLYYRDICEVDEPLVSLGLLSGLRKKFHKNSPYQYTENNIGEEESEERDEVTEEEYEDESFIVTGRVCSNVSALLRRSYSNISNKKGRVVNNQIPEETLEVKLRFTKVITNLRTSGNNTTNSRISCLQMPSSLPSATLPFTPKSQSLFKTNQIKNSRNARTTITINNTNSGTVGRRQTNPMPAPKAVRTQSLPIWNLKPNIANTGFPRNSIAHKIYLADRKTEANQQNNQHQNIAYEINTLQNDNTIQRTKIDDSVSKRFDFMLNKRKSTKKVSPGIATIAKKPASININPKQPPKTSGEKKANDKQTIVKVKNSNSKNSAKSTQAGCRRSSVIEHLNDHDDSILSDILSEPGIEGQKLQQKQKGRKISLTSENDKENIPPQSITSKENKLEGDLDFNAEFPMSDFSDVVFKDEMGWFSNFNCNFFESPTSASASQLNQQNLKPSITLNDPNTCNTIALENEDVSELETAQNNKISLPSDVDKTSPIDSLSIPLIELTHSSSTTNMQRISIKEGSTLNITDSNNATPCDNDIKDRKASVIDSDNTKPQAGLINFSTPADQPASDNNVTASKKLTSMLETQQSKRSHEEVLDEEEEEEALKKQKAIPSSPCGMFNYHQPMELSEDIVEEEQGHNIGDDNESDKTNDLFSTFIHSGIRVSQVVTSPIGEFQSIKH", "text": "FUNCTION: Required for normal transcription at a number of loci in yeast."}
+{"protein": "MDVDLPPPGPLTSGGLRVTALGGINEIGRNMTVFEHLGRLLIIDCGVLFPGHDEPGVDLILPDMRHVEDRLDDIEALVLTHGHEDHIGAIPFLLKLRPDIPVVGSKFTLALVAEKCREYRITPVFVEVREGQSTRHGVFECEYFAVNHSTPDALAIAVYTGAGTILHTGDIKFDQLPPDGRPTDLPGMSRLGDTGVDLLLCDSTNAEIPGVGPSESEVGPTLHRLIRGADGRVIVACFASNVDRVQQIIDAAVALGRRVSFVGRSMVRNMRVARQLGFLRVADSDLIDIAAAETMAPDQVVLITTGTQGEPMSALSRMSRGEHRSITLTAGDLIVLSSSLIPGNEEAVFGVIDALSKIGARVVTNAQARVHVSGHAYAGELLFLYNGVRPRNVMPVHGTWRMLRANAKLAASTGVPQESILLAENGVSVDLVAGKASISGAVPVGKMFVDGLIAGDVGDITLGERLILSSGFVAVTVVVRRGTGQPLAAPHLHSRGFSEDPKALEPAVRKVEAELESLVAANVTDPIRIAQGVRRTVGKWVGETYRRQPMIVPTVIEV", "text": "FUNCTION: An RNase that has 5'-3' exonuclease and possibly endoonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay (By similarity). FUNCTION: An RNase that has 5'-3' exonuclease and possible endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay (By similarity). Has both beta-lactamase and RNase activity, but the physiological relevance of the beta- lactamase activity, i.e. whether it confers antibiotic resistance, has not been shown (PubMed:21568871). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily."}
+{"protein": "MWSILWVVTTLISIVAADPNMKELAGTWTSKSNTVFTGPGFYDPVDELLIQPDLPGISYSFTEDGHYEEALYRVTSNSQNHSCATAVLIYQHGTYEILNNGSLVMTPIAVDGRQLLSDPCGYSETESQYTRYVQPTWFKAYYVQVDSYSGKMKLQIYQFDGSLMQPLYLAYSPPLMLPTKALNPTDKASETKSSLRRKVKRSLENQYRTTAVKSFNYEKYDKYWWAAVGVIGIASASVFLH", "text": "FUNCTION: Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the ROT1 family."}
+{"protein": "MSLPLTEEQRKKIEENRQKALARRAEKLLAEQHQRTSSGTSIAGNPFQAKQGPSQNFPRESCKPVSHGVIFKQQNLSSSSNADQRPHDSHSFQAKGIWKKPEEMPTACPGHSPRSQMALTGISPPLAQSPPEVPKQQLLSYELGQGHAQASPEIRFTPFANPTHKPLAKPKSSQETPAHSSGQPPRDAKLEAKTAKASPSGQNISYIHSSSESVTPRTEGRLQQKSGSSVQKGVNSQKGKCVRNGDRFQVLIGYNAELIAVFKTLPSKNYDPDTKTWNFSMNDYSALMKAAQSLPTVNLQPLEWAYGSSESPSTSSEGQAGLPSAPSLSFVKGRCMLISRAYFEADISYSQDLIALFKQMDSRRYDVKTRKWSFLLEEHSKLIAKVRCLPQVQLDPLPTTLTLAFASQLKKTSLSLTPDVPEADLSEVDPKLVSNLMPFQRAGVNFAIAKGGRLLLADDMGLGKTIQAICIAAFYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLSPDCINVVVTGKDRLTAGLINIVSFDLLSKLEKQLKTPFKVVIIDESHFLKNSRTARCRAAMPVLKVAKRVILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAKRMPWGWDYSGSSNLGELKLLLEEAVMLRRLKSDVLSQLPAKQRKIVVIAPGRINARTRAALDAAAKEMTTKDKTKQQQKDALILFFNRTAEAKIPSVIEYILDLLESGREKFLVFAHHKVVLDAITQELERKHVQHIRIDGSTSSAEREDLCQQFQLSERHAVAVLSITAANMGLTFSSADLVVFAELFWNPGVLIQAEDRVHRIGQTSSVGIHYLVAKGTADDYLWPLIQEKIKVLAEAGLSETNFSEMTESTDYLYKDPKQQKIYDLFQKSFEKEGSDMELLEAAESFDPGSASGTSGSSSQNMGDTLDESSLTASPQKKRRFEFFDNWDSFTSPL", "text": "FUNCTION: ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks. SUBCELLULAR LOCATION: Nucleus Note=Recruited to damaged DNA regions. SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SMARCAL1 subfamily."}
+{"protein": "DAGNRIAAPACVHFTADWRYTFVTNDCSIDYSVTVAYGDGTDVPCRSANPGDILTFPGYGTRGNEVLGAVLCATDGSA", "text": "FUNCTION: Inhibits mammalian alpha-amylases specifically but has no action on plant and microbial alpha-amylases."}
+{"protein": "MREDLLRNSVEFLREKTVLDAPDVKKIEFLKSKGLTAEEIQEAFKLAKNPLFPSYPRFENTSNFVSRDWRDWFIMGVISTGFAWSAYSLVKKYIAPMFRAPSQNAYEADKNALDAKFLEAHKILENLDEQTRKLSERTEKQQDELDIALDDLEETLNTLKRTSENRDREIARISQDVYTMSTITLPQSLEQIKKSQEEALQNLSREISSLRCLQTDSKKDDTFATTSNSSIPVLENPLDTSEGFQTKKVGTASLPDWQISMHNEASKNIDFNDIDPAESYVAEDAY", "text": "FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 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. SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the peroxin-14 family."}
+{"protein": "MTSQIQDLLATDQDLLLMQEGTMMRKVRTKSWKKLRYFRLQNDGMTVWHGSQPESMPKPTFSISDVERIRKGQDSELLRYLVEEFPLEQGFTVVFHGRRPNLDLVANSVEEAQIWMRGLQLLVDLVASMDHQEQMDQMLNEWFQQADRNQDGRMSFREAQRLLLLMNVEMDEEYAFSLFQEADVTQSDDLGSEEFVQFYKALTKRTEIEEIFEDFSSDKQKLTLLEFVDFLRKEQKEKDHAPDLALELIDRYEPSENGRLLHVLSKDGFLKYLCSKDGNIFNSDCLPIYQDMTQPLSHYYINSSHNTYLVGDQLCGQSSVEGYIRALKRGCRCVEVDTWDGPDGEPVVYHGHTLTSRILFKDVLATLAQYAFQSSDYPLILSLENHCTWEQQRTMAHHLTEILGEQLLRNTLEGLLVDSMPSPEQLRGKILVKGKKLRTIEVDKEEEEEEEEEELEKDEGPDLDPASPELDTQPQPETQGQAAGNKKERKKKVMKCPMSCLLICGHVMAQAPSSIPESILLSKQFLLLSSTTIMCPDLSALVVYLRTVPFCSFTHSKENYHIYDISSFSESKAKNLIKEAGNEFVQHNARQLCRVYPSGLRTDSSNFNPQEHWNVGCQMVAMNMQTAGSAMDICDGLFRQNGGSGYVLKPEFLRDTQSSFNPERPISLYKAQILVVQVISGQQLPKVDKTKETTVVDPLVKVELYGVPEDTKEQETSHVENNGINPYWGETFYFRLQVPELAMLRFVVKDYSRKSRNNFIGQYTLPWTCMKQGYRHVSLLSRDGTSLNPASIFVYTCMQEDLDMDEP", "text": "FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca(2+) mobilization in the zona pellucida-induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression up-regulates the Erk signaling pathway and proliferation. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Nucleus Cytoplasm Endoplasmic reticulum Note=Localizes primarily to intracellular membranes mostly to the endoplasmic reticulum."}
+{"protein": "MAGTVRTACLLVAMLLGLGCLGQAQPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASMELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQMMNPGLPESVLDINECLRGARRDLKVFGSFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNGGKLTTTIGKLCAHSQQRQYRSAYYPEDLFIDKKVLKVARVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSVPKGKVVDKSLDEEGLESGDCGDDEDECIGSSGDGMMKVKNQLRFLAELAYDLDVDDAPGNKQHGNQKDNEITTSHSVGNMPSPLKILISVAIYVACFFSWCTDLPCPCLCCPAAPCGPPT", "text": "FUNCTION: Cell surface proteoglycan (By similarity). Negatively regulates the hedgehog signaling pathway when attached via the GPI- anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (By similarity). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands (By similarity). Positively regulates the non- canonical Wnt signaling pathway (By similarity). Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (By similarity). Inhibits the dipeptidyl peptidase activity of DPP4 (By similarity). Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4 (By similarity). Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis (By similarity). Required for coronary vascular development (By similarity). Plays a role in regulating cell movements during gastrulation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. SIMILARITY: Belongs to the glypican family."}
+{"protein": "MSEAEASSGMAHNAGPDEKTLQVLRDMANRLRIRSIKATNSSTTSYLIPCSNAEIMSVLFFYTMRYKQEDPENPDNDRCILSKGLPFVNVATGWPGQGLGAACGMAYTGKYFDQASYRVFCLLGDEESTEGSVWEAFAFASYYNLDNLMAIFDVNRIGHSSSMSVEHCIAIYQKRCEAFGWNTYVVDGRDVKTLCHVFSQAAQVRGKPTAVVAKTFKARGMPNVEDAESWYGRPMPKERADAIVKLIESQIQTNKILVPSPPIEDSPQINIMNICMTSPPVYVADDKVSTQRACGLALAKLGHENDRVIVLGSDTKNCNFSDIFKKEHPERFIQCCIAEQNMVNVALGCSTRDRTIVFAYSFAAFFTRAFDQIRLGAISQININLIGCHCGVSTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAANTKEMCFIRTSQAETAIIYTTQETFQIGQAKVVRHSDNDKVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKATGGRIITVEDHYPEGGIGGAVCAAVSMEPNIVVHNLAVMDVPRSGRCNEALDFSGISSRHIIVAVKCILMT", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transketolase family."}
+{"protein": "MATATVATTPEGIPVIILKEGSSRTYGKEALRANIAAVKAIEEALKSTYGPRGMDKMLVDSLGDITITNDGATILDKMDLQHPTGKLLVQIAKGQDEETADGTKTAVILAGELAKKAEDLLYKEIHPTIIVSGYKKAEEIALKTIQEIAQPVTINDTDVLRKVALTSLGSKAVAGAREYLADLVVKAVAQVAELRGDKWYVDLDNVQIVKKHGGSVNDTQLVYGIVVDKEVVHPGMPKRIENAKIALLDASLEVEKPELDAEIRINDPTQMHKFLEEEENILKEKVDKIAATGANVVICQKGIDEVAQHYLAKKGILAVRRAKKSDLEKLARATGGRVISNIDELTSQDLGYAALVEERKVGEDKMVFVEGAKNPKSVSILIRGGLERVVDETERALRDALGTVADVIRDGRAVAGGGAVEIEIAKRLRKYAPQVGGKEQLAIEAYANAIEGLIMILAENAGLDPIDKLMQLRSLHENETNKWYGLNLFTGNPEDMWKLGVIEPALVKMNAVKAATEAVTLVLRIDDIVAAGKKSGSEPSGKKEKDKEEKSSED", "text": "FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
+{"protein": "MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWDNTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAVQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLATASGNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHAELWPAKQYPLVTPNEERNVMEEAKGFQPSRSTAQQELDGKPASPTPVIVASHTANKEEKSLLELEVDLDNLELVDIDTTDINLDEDILDD", "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": "MINNYIDITVRLLENILDNEADYVKEAGAKVAESIENDGVIHLFGCGHSHILTEEVFYRAGGLAAIHPILHEPLMLHEGAAASSVLERKNDYAKTFMAEEDIRPGDIMIVLSTSGRNPVPIDVAEIAREKGAFVIVITSLQYSASQKSRHTSGKRLSDAGDIVIDNGAVKGDAVLKSANFDIAFAPTSTVTGAVILQSIFAEAIETMVNDNFTPPVFISGNVENADAHNQALVDKYNERIPLLGMNL", "text": "SIMILARITY: Belongs to the UPF0309 family."}
+{"protein": "MDIQLDPARDDLPLMANTSHILVKHYVLDLDVDFESQVIEGTIVLFLEDGNRFKKQNSSIEEACQSESNKACKFGMPEPCHIPVTNARTFSSEMEYNDFAICSKGEKDTSDKDGNHDNQEHASGISSSKYCCDTGNHGSEDFLLVLDCCDLSVLKVEEVDVAAVPGLEKFTRSPELTVVSEEFRNQIVRELVTLPANRWREQLDYYARCSQAPGCGELLFDTDTWSLQIRKTGAQTATDFPHAIRIWYKTKPEGRSVTWTSDQSGRPCVYTVGSPINNRALFPCQEPPVAMSTWQATVRAAASFVVLMSGENSAKPTQLWEECSSWYYYVTMPMPASTFTIAVGCWTEMKMETWSSNDLATERPFSPSEANFRHVGVCSHMEYPCRFQNASATTQEIIPHRVFAPVCLTGACQETLLRLIPPCLSAAHSVLGAHPFSRLDVLIVPANFPSLGMASPHIMFLSQSILTGGNHLCGTRLCHEIAHAWFGLAIGARDWTEEWLSEGFATHLEDVFWATAQQLAPYEAREQQELRACLRWRRLQDEMQCSPEEMQVLRPSKDKTGHTSDSGASVIKHGLNPEKIFMQVHYLKGYFLLRFLAKRLGDETYFSFLRKFVHTFHGQLILSQDFLQMLLENIPEEKRLELSVENIYQDWLESSGIPKPLQRERRAGAECGLARQVRAEVTKWIGVNRRPRKRKRREKEEVFEKLLPDQLVLLLEHLLEQKTLSPRTLQSLQRTYHLQDQDAEVRHRWCELIVKHKFTKAYKSVERFLQEDQAMGVYLYGELMVSEDARQQQLARRCFERTKEQMDRSSAQVVAEMLF", "text": "FUNCTION: Aminopeptidase which catalyzes the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the peptidase M1 family."}
+{"protein": "MRSHFCTEISEKDVGKIVKVAGWCNTYRDHGGVVFIDLRDKSGLVQLVCDPSSKAYEKALEVRSEFVLVAKGKVRLRGAGLENPKLKTGKIEIVLEELIIENKSATPPIEIGNKHVNEDLRLKYRYLDLRSPNSYEIFKLRSEVALITRNTLAQKGFLEIETPILSKTTPEGARDYLVPSRVHEGEFFALPQSPQLFKQLLMVGGMDRYFQIARCFRDEDLRADRQPEFTQIDAEMSFCDENDVMGVVEDLLQEIFKAVGHTISKPFKRMPYKEAMENYGSDKPDLRFELPLIEVGDCFRDSSNAIFSNTAKDPKNKRIKALNVKGADALFSRSVLKELEEFVRQFGAKGLAYLQIKEDEIKGPLVKFLSEKGLKNILERTDAQVGDIVFFGAGDKKIVLDYMGRLRLKVAETLDLIDKDALNFLWVVNFPMFEKTENGYHAAHHPFTMPKNIECEDIEEVEAHAYDVVLNGVELGGGSIRIHKEEMQKKVFEKINIHEEEAQKKFGFLLEALKFGAPPHGGFAIGFDRLIMLMTKSHSIRDVIAFPKTQKASCLLTNAPSPINEEQLRELHIRLRK", "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). Is 1.7 times more efficient at aminoacylating tRNA(Asp) over 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": "MNPDLRRERDAASFDAEKLTYILDGGSERTRRRREIENLILNDPDFKHEDLNFLTRSERYEIAVRKSATMVKKMRDFGIADPEEIMWFKKPQLINFVEPVGLTYSMFIPTLLDQGTTAQQQKWLPPTQGLQIIGTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLYTKGECYGLHAFIVPIREMGTHKPFPGIIVGDIGPKFGYDEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARSLSKACTIAIRYSLIRHQSEIRPGDPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINVDINQGNLNELPELHALTAGLKAFTSWTTNSGIEACRMACGGHGYSHCSGLPNIYVTFTPTCTFEGENTVMMLQTARFLMKSYDQVHSGKLVGGMVSYLNDLPSQRIQPQQVAAWPAMVDINNPDSLTEAYKHRAARLVEAAARNLQAEMKHRKSKEIAWNFTSVDLVRASEAHCHYVVVKLFSGNLSKIDDKPIQAVLTNLCLLYALYGISQNSGDFLQGGILTESQLTQVNQRVKELLTLIRPESAALVDAFDFQDVSLGSVLGRYDGNIYENMFEWAKKSPLNKSEVHESYHKHLKPLQSKL", "text": "FUNCTION: Involved in the initial and rate-limiting step of peroxisomal beta-oxidation of straight-chain saturated and unsaturated very-long- chain fatty acids (PubMed:12758125). Catalyzes the desaturation of fatty acyl-CoAs such as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans- enoyl-CoAs ((2E)-enoyl-CoAs) such as (2E)-hexadecenoyl-CoA, and donates electrons directly to molecular oxygen (O(2)), thereby producing hydrogen peroxide (H(2)O(2)) (PubMed:12758125). Isoform 2 shows higher activity with hexadecanoyl-CoA as substrate than isoform 1 (PubMed:12758125). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the acyl-CoA oxidase family."}
+{"protein": "MSGDDDWWTSSNEALLVSLVTPSDTGVKTLDTFHPEYTNNIFGEKEQIFGYKGLRINLQYNASDMLPNLKVSYKKKYQPTADEEALDINEVLSEFLPEIAFQKQSDFETRLKSIPDNWTPPGTLVTSFTNKDGEYEVYSGKITDPAVKQLLNRIQILVPFFVDGGTPIDMEDPDVDRWTIYFLYNKRPLLNQPDKFSYHFAGYSTLYRYYAFQPPAESESKTPTDTPTFSVDGDFDLDTLPCRTRISQFIIIPPFQQKGLGSRLYSIIYQQYLKHEPTIELTVEDPNEAFDDMRDLADLAFLSKQPEFQALKIDTSVEIPEEGKAPSNIVDQAAWEACRKKFKIVPRQFARVLEMYLMSQLPESVRPGLGAPEDEDYEEQSGRSKSKGHEKALPKPTPEDEHTYRLWMMLVKRRLYVHNRDALGQLELKERREELAKVFAGVEFDYARLLIKAEEQGKLAQADGETAGDQVPATPSAANGKRKLDEVEQAEGTAAASSKKAKVESGHA", "text": "FUNCTION: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which 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": "MGIYSFWIFDRHCNCIFDREWTLASNSASGTINSKQNEEDAKLLYGMIFSLRSITQKLSKGSVKNDIRSISTGKYRVHTYCTASGLWFVLLSDFKQQSYTQVLQYIYSHIYVKYVSNNLLSPYDFAENENEMRGQGTRKITNRNFISVLESFLAPMVNQ", "text": "FUNCTION: Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation. Required for sporulation. Has a role late in meiosis following DNA replication. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network. Endoplasmic reticulum. Preautophagosomal structure. SIMILARITY: Belongs to the TRAPP small subunits family. BET5 subfamily."}
+{"protein": "MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPTEGSFKPGNIDPCLCTHLIYAFAGMKNNEITYLSEQDLRDYEALNGLKDRNTELKTLLAIGGWKFGPAPFSSMVSTPQNRQTFIKSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVQEMRKAFEEESTLNHIPRLLLTSTGAGFIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKNGYTGENSPLYKSPYDIGKSADLNVDSIITYWKDHGAASEKLIVGFPAYGHTFILSDPSKNGIGDPTVSAGPPGKYTNEQGLLAYFEICTFLNEGATEIFDATQEVPYAYLGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSGSFCHQGRFPLTTTLKRDLNVHSASCKASYRGEL", "text": "FUNCTION: Has low chemotactic activity for eosinophils. May play a role in inflammation and allergy. Has no chitinase activity. SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Detected in the cytoplasm of keratinocytes. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily."}
+{"protein": "MGRYTTDQVQVYVLVIVLCTFFSTLQARSLRDHPLIHKNIDSRSLLQKLRIHISNHKQVRDISGDRLSPAGPDPQHNGRSPPRK", "text": "FUNCTION: [CLE13p]: Signaling peptide involved in the regulation of nodulation (PubMed:20348212). Moves from root to shoot to function with the receptor kinase SUNN, in a signaling pathway that plays roles during cellular differentiation, both at the onset of nodulation, and later during nodule meristem development and subsequent homeostasis (PubMed:20348212). Interacts with SUNN signaling to control nodule numbers (PubMed:22168914). SUNN is 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 (Probable). SUBCELLULAR LOCATION: [CLE13p]: Secreted, extracellular space. SIMILARITY: Belongs to the CLV3/ESR signal peptide family."}
+{"protein": "MTEITQLFQYNTLGALMAGLYEGTMTIGELLKHGDLGIGTLDSVDGELIVLDGKAYQAKGDKTIVELTDDIKVPYAAVVPHQAEVVFKQKFTASDKELEDRIESYFDGQNLFRSIKITGEFPKMHVRMIPRAKSGTRFVEVSQNQPEYTEENVKGTIVGIWTPEMFHGVSVAGYHLHFISEDFTFGGHVLDFIIDNGTVEIGAIDQLNQSFPVQDRKFLFADLDIEALKKDIDVAE", "text": "FUNCTION: Converts acetolactate into acetoin. SIMILARITY: Belongs to the alpha-acetolactate decarboxylase family."}
+{"protein": "MKTNREQEIYVERSFKPNNSTIQNLMDIERFILPHTSTSGVARLKMRVISWVGLQFYNY", "text": "FUNCTION: Involved in regulating carbon and nitrogen allocation to starch and protein (PubMed:25146936). SUBCELLULAR LOCATION: Cytoplasm."}
+{"protein": "MEFISFVYTLIAFSSLLYFYLIWSESAKPKTTTHKAPPEASGAWPVIGHLRIMSGHPSAGIPHVNLGMLADKHGPIFSIRLGVHRVVVVSSPEVIKELFTTNDVAVSSRPSVKAGKHLAYDNAMLGFASYGAYWRQLRKIVSLELLSNRRLELQSHVSMSETGQFVKELYKLWEKKKSDGSGTEVGEGVVVDMKRWLGELNMNVVMRMVAGKRFGSGDNAEETKRCRRVMGDFFYLAGFFVPADALPYLGWLDLGGHEKRMKKAAKELDEVVGEWLAEHREREFSGEGKAQDFMDVMISVVKGADLQCEFDVDTIIKATCGTLIAGGTDTTAVVFVWALSLLLNHSHVLKKAQQELDKHVGKDRRVKESDLNNLIYLQAIVKETLRLYPPGPLAGTRRFTEDCVVGGYYIPKDTWLIVNLWKLQRDPRVWSDPLEFRPERFLAGDKTFDVKGQDFELIPFGAGRRICPGLSFGLQMLHLVLASLLQAFDMSTVSDEAVDMSESAGLTNMKATPLDVVVTPRLPPRLYNEIVEIY", "text": "FUNCTION: Hydroxylase 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:23184958). Catalyzes the 6-hydroxylation of 7-O-methylated precursors such as the conversion of genkwanin (GENK) to scutellarein- 7-methyl ether (SCU7Me) (PubMed:23184958). Can also use, with a lower efficiency, apigenin-7,4'-dimethyl ether (AdM), naringenin-7-methyl ether (SAK) and naringenin-7,4'-dimethyl ether (NdM) as substrates (PubMed:23184958). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
+{"protein": "LKCNRLIPPFWKTCPEGKNLCYKMTMRLAPKVPVKRGCIDVCPKSSLLIKYMCCNTNKCN", "text": "FUNCTION: Shows cytolytic activity on many different cells by forming pore in lipid membranes (PubMed:8182052). 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": "MDEWYGQVAPREKLLKYGAAVLTDAELLAIFLRTGIPGMHVMKMAEYLIETFGSLHGLISADYQTLCAHKGIGASKYSQIQAIGELACRCFSSHLMRESVLLNPGITQKFLQNILSHREREIFLVVFLDNQHRVIRHEEMFTGTISSVEVHPREIVREALKVNAAALILAHNHPSGKAEPSQADRLITTQVIKACSLLDIRVLDHLVVGRGECVSFAERGWL", "text": "SIMILARITY: Belongs to the UPF0758 family. YicR subfamily."}
+{"protein": "DYDWSLRGPPKCATYGQKCRTWSPPNCCWNLRCKAFRCRPR", "text": "FUNCTION: Binds to chitin. Shows strong activity against E.coli (IC(50) is 1.2 ug/ml). Is also very active against S.aureus (IC(50) is 0.8 ug/ml), C.albicans (IC(50) is 0.9 ug/ml) and P.pastoris (IC(50) is 0.3 ug/ml). Binds to chitin (5.2 uM are required to obtain 50% of binding). Causes hemolysis on sheep erythrocytes, probably by forming ion- permeable pores. SUBCELLULAR LOCATION: Secreted."}
+{"protein": "MKIPLLGLLLLISLVGSPTRAEEGPVCPKTETLSRASFPEGFMFGTATAAFQVEGAVNEGCRGPSLWDIYTKKFPHRVKNHNADEAVDFYHRYKEDIQLMKKLNTDGFRLSISWPRIFPHGRMEKGISKEGVQFYHDLIDELLKNDITPLVTVFHWDTPADLEDEYGGFLSERIVPDFVEYANFTFHEYGDKVKNWITFNEPWVFSRSGYDVGKKAPGRCSPYVKEFGKLCQDGRSGFEPYVVSHNLLVGHAEAVDAFRKCEKCKGGKIGIAHSPAWFEPEDVEGGQATVNRVLDFVIGWHLDPTTFGDYPQSMKDAVGSRLPRFTKAQKAKLKDSTDFVGINYYTSFFAKADQKVDSRNPTWATDALVEFEPKTVDGSIKIGSQPNTAKMAVYAKGLRKLMKYIKDRYNSPEIIITENGYGEDLGDKDTDLSVALNDHNRKYYLQRHLLALNEAICEDKVNVTSYFLWSLMDNFEWQDGYTARFGVYYIDFKNNLTRMEKESAKWLSEFLKPGLKPSKSSKLHEEL", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
+{"protein": "MFPKPLVILAHEIYGVNSHMKKMGRLIKMAGYDVLTPNLLGEDEVYTLKEEKTAYEQFTKHERLKTGETIIQNVIRQNAGRHIFVIGFSVGATIAWKCSSMPEVSGSVCYYGSRIRDSLHHMPACPVLLFFPNYEPSFDVALLIKKLREKQHTHLEIYQFDALHGFANPDSVYFNRALFFKTLSIIKNGAESRLRTVSSSFF", "text": "SIMILARITY: Belongs to the dienelactone hydrolase family."}
+{"protein": "MIQNVGNHLRRGLASVFSNRTSRKSALRAGNDSAMADGEGYRNPTEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQVASEDLCSEKQWNVCKALATFVARREITKVKLKQITPRTEEEKMEHSVAAERRRMRLVYADTIKDLLANCAIQGDLESRDCSRMVPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEAYRQEAETHRRHINSAFMTFVVLDADDQPQLLPWIRPQPGDGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKFLSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRKPCDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKCCWVRVSLTELVSASGFYSWGLESRSKGRRSDGWNGKLAGGHLSTLKAIPVAKINSRFGYLQDT", "text": "FUNCTION: Has an acyl-CoA thioesterase activity with a preference for the long chain fatty acyl-CoA thioesters hexadecanoyl-CoA/palmitoyl-CoA and tetradecanoyl-CoA/myristoyl-CoA which are the main substrates in the mitochondrial beta-oxidation pathway. SUBCELLULAR LOCATION: Mitochondrion matrix Cytoplasm."}
+{"protein": "MSTAWDTVWHACSVIEHALQASHLTYSEFSGVPDGLLRLVVELPGERRLKTNAILSIGEHSVHVEAFVCRKPDENHEGVYRFLLKRNRRLFCVSYTLDNVGDIYLVGRMSLASVDTDEIDRVLGQVLEAVESDFNTLLELGFRSSIQKEWDWRISRGESLNNLQAFAHLIDDEGDGDASIYARP", "text": "SIMILARITY: To M.tuberculosis Rv0487."}
+{"protein": "MERFRWQVAAVAAVGLALALEALPSVLCWLRAGRRQQQRPPRRQVLFFPSQVTCTEALLQAPGEAPSGPPAGCRCSLPHGESSLSRLLRALLAARASLELCLFAFSSPQLGRAVQLLHQRGVRVRVITDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVDKKVLITGSLNWTTQAIQNNRENVLIMEDEEYVRLFLEEFERIWEEFNPTKYTFFPQKKTGTSLPPQVSCFGQLVSCHSKCSHHLSQV", "text": "FUNCTION: Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholipase activity. In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3- phosphate), a second messenger signaling lipid. Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission. Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (By similarity). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation. Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation. The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis. Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins. Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA- mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation. PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs. Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Nucleus membrane Cell membrane Golgi apparatus Note=Localization in the mitochondrial outer membrane is found in different cell types where phospholipase was the predominant activity, however, in pachytene spermatocytes and spermatids of mouse testes where nuclease activity is predominant, localization is restricted to the Golgi, suggesting this enzyme is localized in different subcellular compartments depending on the role (phospholipase or nuclease) it needs to play in each cell type and developmental stage. SIMILARITY: Belongs to the phospholipase D family. MitoPLD/Zucchini subfamily."}
+{"protein": "MPPKAGQTKKAKMEAANKGAKKTTKKWSKGQSREALQNAVMFDKETYDKLRSEVPKYKLITPSIISDRLKIAVSIAAAGLKQLCREKLIRLVSCSSKTRVYTRIVQAAPAEAAAAAPAAE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS25 family."}
+{"protein": "MGTLPVMVLFGLSFPPAFFALLAALPLFWLLRRLLQPSGLYDMIWHPALFNCALYGCLFYLVSWLFI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AaeX family."}
+{"protein": "MEHTLFGCLRSPHATSQGLHPFAQSSLALHGRSDHMSYPDLSSSSSSCILTGYPNEESMFGSQHHRGHHHHHHHHHQQQQHQTLQSNWHIPQMSSPPASTRHSLCLQQDSGPPDLSGSPSILCSNTSSLGTNNSTGAACVTGDYGRQSLSPAEAEKRTGKRKSDSSDSQEGSYKSDVNSKPRKERTAFTKEQIRELEAEFAHHNYLTRLRRYEIAVNLDLTERQVKVWFQNRRMKWKRVKGGQQGAAAREKELVNVKKGTLLPSELSGIRSNSLQHTADSLTNDDSHDSSQSSEHAHL", "text": "FUNCTION: Mesodermal transcription factor that plays a key role in somitogenesis and somitogenesis and limb muscle differentiation. Required during limb development for normal appendicular muscle formation and for the normal regulation of myogenic genes. Also acts as a negative regulator of angiogenesis. SUBCELLULAR LOCATION: Nucleus Nucleus speckle."}
+{"protein": "MESVLKSLFVLLVATSFTLAKEIPAKVSKPQTLSRGWGDNLEWVQTYEEGLYKAKAENKPLMLINHRNDCPHSLALKKAFAEHQGIQKLAEEFILLNVVYDPTDKNLQLDGQYVPKIIFVDPSLVVRADLPGKYSNHQYTYEPADIDHLFENMKKALVLLKTEL", "text": "SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum. SIMILARITY: Belongs to the AGR family."}
+{"protein": "MDLISTFLLHFLLLACSLPPGAVSLRTALRKSGKVGPPLDIKLGALNCTAFSIQWKTPKRSGSSIVGYTVFYSELGSDKSLREQSHNVPVGQDTLITEEVIGDLKPGTEYRVSIAAYSQTGKGRLSFPRHVTTLSQDSCLPPEAPHQPHVLVVSDSEVALSWRPGENEGSAPIQSYSVEFIRPDFDKSWTIIQERLQMDSMVIKGLDPDTNYQFAVRAMNAYGFSLRSQPSNTIRTLGPGEAGSGRYGPGYITDTGVSEDDDASEDELDLDVSFEEVKPLPATKVGNKKSKKTSVSNSEMDSRLAQPTSASLPETTVAVPPTPAQRKGKNSVAVMSRLFDMSCDETLCSADSFCVNDYAWGGSRCHCNLGKGGEACSEDIFIQYPQFFGHSYVTFEPLKNSYQAFQITLEFRAEAEDGLLLYCGESEHGRGDFMSLALIRRSLHFRFNCGTGMAIIISETKIKLGAWHSVTLYRDGLNGLLQLNNGTPVTGQSQGQYSKITFRTPLYLGGAPSAYWLVRATGTNRGFQGCVQSLAVNGKKIDMRPWPLGKALNGADVGECSSGICDEASCINGGTCAAIKADSYICLCPLGFRGRHCEDAFTLTIPQFRESLRSYAATPWPLEPQHYLSFTEFEITFRPDSGDGVLLYSYDTSSKDFLSIIMAAGHVEFRFDCGSGTGVLRSEDTLTLGQWHDLRVSRTAKNGILQVDKQKVVEGMAEGGFTQIKCNTDIFIGGVPNYDDVKKNSGILHPFSGSIQKIILNDRTIHVRHDFTSGVNVENAAHPCVGAPCAHGGSCRPRKEGYECDCPLGFEGLNCQKAITEAIEIPQFIGRSYLTYDNPNILKRVSGSRSNAFMRFKTTAKDGLLLWRGDSPMRPNSDFISLGLRDGALVFSYNLGSGVASIMVNGSFSDGRWHRVKAVRDGQSGKITVDDYGARTGKSPGMMRQLNINGALYVGGMKEIALRTNRQYMRGLVGCISHFTLSTDYHISLVEDAVDGKNINTCGAK", "text": "FUNCTION: Involved in both the normal 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. Colocalizes with BSN, CTBP2 and DAG1 in photoreceptor synaptic terminals."}
+{"protein": "MGTPWRKRKGIAGPGLPDLSCALVLQPRAQVGTMSPAIALAFLPLVVTLLVRYRHYFRLLVRTVLLRSLRDCLSGLRIEERAFSYVLTHALPGDPGHILTTLDHWSSRCEYLSHMGPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEHMVELIVGSSEDVIPCLRTQYQLSRADLVLLAHRPRCYLRDLQLLEAHALLPAGATVLADHVLFPGAPRFLQYAKSCGRYRCRLHHTGLPDFPAIKDGIAQLTYAGPG", "text": "FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function (PubMed:18794526). Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity (By similarity). SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Endoplasmic reticulum Note=Localized to the cell body of the cochlear hair cells, but is not present in the stereocilia (PubMed:28504928). Present but not restricted to the apical cistern, Hensen's body and the subsurface cistern (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family."}
+{"protein": "MAARQQQKGTGFGVQYEDFVPKSEWKDQPEATILNIDLTGFAKEQMKVTYVHSSKMIRVTGERPLANRKWSRFNEVFTVPQNCLVDKIHGSFKNNVLTITMPKETITKVAYLPETSRTEAAALEKAAKLEEKRLLEESRRKEKEEEEAKQMKKQLLEEKEALIRKLQEEAKAKEEAEMRKLQEEAKAKEEAAAKKLQEEIEAKEKLEERKLEERRLEERKLEDMKLAEEAKLKKIQERKSVDESGEKEKILKPEVVYTKSGHVATPKPESGSGLKSGFGGVGEVVKSAEEKLGNLVEKEKKMGKGIMEKIRRKEITSEEKKLMMNVGVAALVIFALGAYVSYTFCSSSSSSSSSSPSSSSSSTKPE", "text": "FUNCTION: Required for the restriction of long-distance movement of the pathogenic tobacco etch virus (TEV) without causing a hypersensitive response or inducing systemic acquired resistance. Seems to not be involved in heat resistance. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Present in sieve elements. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
+{"protein": "MKYTDFLAHPDEIIPTIRMMYADYRLKNMEIKDPSVRFCYNMLNRVSRSFAMVIQQLPVELRDATCVFYLILRALDTVEDDMAIPKEVKIPMLRTFHEHLSDRSWKIKCGYGPYVDLMDNYPLVTDVYLRFDEGTKAVIKDITRRMGNGMADFIDLDEVLTIPQYDLYCHYVAGLCGIGMCKLFVDSGLEKEDLVAEEDLANQMGLFLQKNNIVRDYLEDINELPAPRMFWPKEIWGNYAKQLDEFKDPKNLDKAMLCLNHMVTDALRHCEVGLRSLSLLHNPNILRAVLIPQVMGVRTLTLVYNNPEVFRGVVKMRRGETAKIFVTTTSKLSFFRTYLQFANEMEQKCLTEAKNDPMVALTLKRVQGVQAACRAAIVKAEIAEGAKGPSTAMVLAGALLIAALAYFAYVYSAGGTSLKALPLFGVVIILAIGLFGRNLALKTV", "text": "FUNCTION: Converts the C20 geranylgeranyl diphosphate (GGPP) to the C40 lycopaoctaene, the first committed intermediate in the production of lycopadiene (PubMed:27050299, PubMed:28813599). Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes (PubMed:27050299, PubMed:28813599). Converts with low efficiency the C20 phytyl diphosphate (PPP) to the C40 lycopadiene in vitro. This reaction may not have biological significance in vivo (PubMed:27050299). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phytoene/squalene synthase family."}
+{"protein": "METAICGRLALAPSSLFNSKSGDKHLVSKGPCVNRSILMTLSTSAALGKGGGVLDKPIIEKTTPGRESEFDLRKSKKIAPPYRVILHNDNFNKREYVVQVLMKVIPGMTVDNAVNIMQEAHINGLAVVIVCAQADAEQHCMQLRGNGLLSSVEPDGGGC", "text": "FUNCTION: Small adapter protein that modulate the activity of CLPC (By similarity). Involved in plastid biogenesis in particular when chloroplast protein synthesis capacity is a limiting factor (PubMed:23898032). Probably involved in substrate selection for plastid Clp protease system (PubMed:23898032). Recruitment to ClpC chaperones is facilitated by CLPF thus forming a binary adapter for selective substrate recognition and delivery to plastid Clp protease system (CLPC) (PubMed:26419670). SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the ClpS family."}
+{"protein": "MKKASELIFIPIPGIGHIVSTVEIAKLLLCRDDNLFITILIMKFPFTADGSDVYIKSLAVDPSLKTQRIRFVNLPQEHFQGTGATGFFTFIDSHKSHVKDAVTRLMETKSETTRIAGFVIDMFCTGMIDLANEFGLPSYVFYTSGAADLGLMFHLQALRDEENKDCTEFKDSDAELVVSSFVNPLPAARVLPSVVFEKEGGNFFLNFAKRYRETKGILVNTFLELEPHAIQSLSSDGKILPVYPVGPILNVKSEGNQVSSEKSKQKSDILEWLDDQPPSSVVFLCFGSMGCFGEDQVKEIAHALEQGGIRFLWSLRQPSKEKIGFPSDYTDYKAVLPEGFLDRTTDLGKVIGWAPQLAILAHPAVGGFVSHCGWNSTLESIWYGVPIATWPFYAEQQVNAFELVKELKLAVEIDMGYRKDSGVIVSRENIEKGIKEVMEQESELRKRVKEMSQMSRKALEEDGSSYSSLGRFLDQIQTS", "text": "FUNCTION: Broad spectrum multifunctional glucosyltransferase. Catalyzes the formation of flavonol 3-O-glucosides during fruit ripening. Accepted substrates include several flavonoids, hydroxycoumarins and beta-naphthols. Uses UDP-Glc as a sugar donor, but not UDP-Gal or UDP- GlcUA. May also be involved in detoxification of xenobiotics. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
+{"protein": "GLFDIIKKIAESF", "text": "FUNCTION: Antimicrobial activity against B.cereus, L.lactis, L.innocua, M.luteus, P.multocida, S.aureus, S.epidermidis and S.uberis. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Aurein subfamily."}
+{"protein": "MNKLVDAHCHVITDPDNTFCGDDGGSQGTLRCVMSSNPYDWNNLKKLAGRSTSKNDICVGFGVHPWYSHLFYVGSRRDKVSHYQDVLEYKNEEQFDSLVQVLPEPLDLEEYIKREFNDTLVSVIGEIGLDKLFRLPANGFYMQNEKARLTTVKVKLSHQETVFRRFCRLARHTSKPISIHDVKCHGKLNDICNEELLTYHSVKICLHSYTGSKETLLGQWLKKFPPDRIFVSLSKWINFKDPEEGDALVRSLPSTCILTETDYPIDNPDPSYQKALTEQLQYLNAQIARAWDETLDASQAALRVYENFQKFIK", "text": "FUNCTION: Putative deoxyribonuclease. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family."}
+{"protein": "MSEYWYPILGGILLGLSTVMLLLLNGRIAGISGIVGRLLQGGNPAQNIPFVVGLVLGPLLFTVIFDRFPSVTVAATWPTIIVAGLLVGLGTRMGAGCTSGHGIVGIARHSPRSIVATAIFLISGMATATFMGVYQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0394 family."}
+{"protein": "MADDELETYRLWRIRKTVLQMVHDRGYLVAQEELDQPLETFKETFGDRPSEKKPARSDLTILVAHNDDPADQMFVFFPEDTKIGIKTIKAICQQMQEQNISRAIIVVQTGMTPSAKQSIGDMAPKYMLEHFLEAELMVNITEHELVPEHVVMTAEEKAELLARYKLKDSQLPRIQQCDPVARYFGLRRGQVVKIIRPSETAGRYITYRLVV", "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 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, 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 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family."}
+{"protein": "MSAGGDFGNPLRKFKLVFLGEQSVAKTSLITRFRYDSFDNTYQAIIGIDFLSKTMYLEDGTIGLRLWDTAGQERLRSLIPRYIRDSAAAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIITLVGNRTDLADKRQVSVEEGERKAKGLNVTFIETRAKAGYNVKQLFRRVAAALPGMESTQDGSREDMSDIKLEKPQEQTVSEGGCSCYSPMSSSTLPQKPPYSFIDCSVNIGLNLFPSLITFCNSSLLPVSWR", "text": "FUNCTION: May be involved in the regulation of centrosome duplication and cell cycle progression. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
+{"protein": "MISSDSRSSPGLARWAESYEAKCERRQETRENRRRRRNETTCRQPGKVLRTQHKERLQGARQLQFLKRRNLEEEKKGQAREQGPSSKTDGGTGQVSILKESLPGANKASFPGQQETGISSEVFPALHHSSSGIQRDLGGHHASHGRAFPPQDSDIKKPHRQHRGTQTKAEEALPTIKNDASQQTNCGVAVLDKDIIQLSEYLKEALHRELILKKKMVILQDLLPALIRASDSSWKGQLNEDKLKGKLRSLENQLYTCLQKHSPWGMKKVLLEMEDQRSSYEQKAKASLQKVLEEKMCAEQQLQRAQLSLALAEQKCQEWKSQYEALKEDWRTLGDQHRELESQLHVLQSKLQGADSRDSQMSQALQLLENEHQELQTKLESLQGDGEQQSSETQDLQDQLKKSEEEKQALVSKVQQLQSLLQNQSLQLQEQEKLLKKDQGLPVWNPKLSLDEVKPEGTRKEKEEELRDQLQKETFQLQVKENELQCGQWLPVLMVVIATALAVFLANKGNLVI", "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:30115741). In response to viral infection, facilitates the recruitment of TRAF3 to MAVS within mitochondria leading to IRF3 activation and interferon production (PubMed:30115741). However, participates in the maintenance of immune homeostasis and the prevention of overzealous innate immunity by promoting 'Lys-48'- dependent ubiquitination of TBK1 (By similarity). 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": "MEDDCDIIIIGAGIAGTACALRCARAGLSVLLLERAEIPGSKNLSGGRLYTHALAELLPQFHLTAPLERRITHESLSLLTPDGVTTFSSLQPGGESWSVLRARFDPWLVAEAEKEGVECIPGATVDALYEENGRVCGVICGDDILRARYVVLAEGANSVLAERHGLVTRPAGEAMALGIKEVLSLETSAIEERFHLENNEGAALLFSGRICDDLPGGAFLYTNQQTLSLGIVCPLSSLTQSRVPASELLTRFKAHPAVRPLIKNTESLEYGAHLVPEGGLHSMPVQYAGNGWLLVGDALRSCVNTGISVRGMDMALTGAQAAAQTLISACQHREPQNLFPLYHHNVERSLLWDVLQRYQHVPALLQRPGWYRTWPALMQDISRDLWDQGDKPVPPLRQLFWHHLRRHGLWHLAGDVIRSLRCL", "text": "FUNCTION: Probably accepts electrons from YgcQ/YgcR and reduces a quinone. SIMILARITY: Belongs to the ETF-QO/FixC family."}
+{"protein": "DVCDSLVDGRCIHNGCFCEESKPNGNCCDSGGCVWWWCPGTKWD", "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": "MNKQSGMTLLEVLLAMSIFTAVALTLMSSMQGQRNAIERMRNETLALWIADNQLQSQDSFGEENTSSSGKELINGEEWNWRSDIHSSKDGTLLERTITVTLPSGQTTSLTRYQSIDNKSGQAQDD", "text": "FUNCTION: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP I family."}
+{"protein": "MEYVYAALILNEADEEINEDNLTDVLDAAGVDVEESRVKALVAALEDVDIEEAVDQAAAAPVPASGGAAAPAEGDADEADEADEEAEEEAADDGGDDDDDEDDEASGEGLGELFG", "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 eukaryotic ribosomal protein P1/P2 family."}
+{"protein": "MTVKDILDAIQSKDATSADFAALQLPESYRAITVHKDETEMFAGLETRDKDPRKSIHLDEVPVPELGPGEALVAVMASSVNYNSVWTSIFEPVSTFAFLERYGKLSPLTKRHDLPYHIIGSDLAGVVLRTGPGVNAWQPGDEVVAHCLSVELESPDGHDDTMLDPEQRIWGFETNFGGLAEIALVKTNQLMPKPKHLTWEEAAAPGLVNSTAYRQLVSRNGAAMKQGDNVLIWGASGGLGSYATQFALAGGANPICVVSSPQKAEICRSMGAEAIIDRNAEGYKFWKDEHTQDPKEWKRFGKRIRELTGGEDIDIVFEHPGRETFGASVYVTRKGGTITTCASTSGYMHEYDNRYLWMSLKRIIGSHFANYREAYEANRLIAKGKIHPTLSKTYSLEETGQAAYDVHRNLHQGKVGVLCLAPEEGLGVRDAEMRAQHIDAINRFRNV", "text": "FUNCTION: May play a role in supplying butyryl-CoA for straight-chain fatty acid biosynthesis. Catalyzes the conversion of crotonyl-CoA to butyryl-CoA. It shows a high substrate specificity for crotonyl-CoA, a short-chain-length (C4), but no measurable activity is observed with shorter (C3) or longer-chain-length enoyl-CoA thioesters. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Crotonyl-CoA carboxylase/reductase subfamily."}
+{"protein": "MVDNRRTFTAPQSLLETNLTFPNDEPSLTTITVTRERCVDPSLIDSFLRFLRHGSDDIIRQKLNNYRKGSINGKNKCKEFLKQELYPNWQIRNNIISFCEKEAAEMKNETDQQCGNNKKTTAEPLIDARIDPYAARERAEKQEAQYKDWTKVTEWVANNRKIEQILTSTTEGILRQNCEQNNDYLKEFTQFCKDNS", "text": "FUNCTION: Regulator of the mitochondrial protein import machinery that is localized in the mitochondrial intermembrane space (IMS) and facilitates the transport of proteins from the cytosol into the mitochondrial matrix (PubMed:32826315). Not essential for mitochondrial protein import but induced and required when mitochondrial import is compromised (PubMed:32826315). Stimulates or stabilizes the translocation into the mitochondria of proteins such as OXA1, ATP1 and COX12 (PubMed:32826315). SUBCELLULAR LOCATION: Mitochondrion intermembrane space Note=Imported into the mitochondria via the mitochondrial MIA40-ERV1 machinery. SIMILARITY: Belongs to the MIX23 family."}
+{"protein": "MADSSEGPRAGPGEVAELPGDESGTPGGEAFPLSSLANLFEGEDGSLSPSPADASRPAGPGDGRPNLRMKFQGAFRKGVPNPIDLLESTLYESSVVPGPKKAPMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPPPILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDLSSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYPYRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDRWSSVVPRVVELNKNSNPDEVVVPLDSMGNPRCDGHQQGYPRKWRTDDAPL", "text": "FUNCTION: [Isoform 2]: Lacks channel activity, due to impaired oligomerization and intracellular retention. FUNCTION: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:18826956, PubMed:18695040, PubMed:29899501). Also activated by heat, low pH, citrate and phorbol esters (PubMed:16293632, PubMed:18826956, PubMed:18695040, PubMed:25256292, PubMed:20037586, PubMed:21964574). Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin- dependent mechanism with a negative feedback mechanism (PubMed:12724311, PubMed:18826956). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (By similarity). Acts as a regulator of intracellular Ca(2+) in synoviocytes (PubMed:19759329). Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4- alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (PubMed:19759329). Together with PKD2, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (By similarity). Regulates expression of chemokines and cytokines related to pro-inflammatory pathway in adipocytes (By similarity). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (By similarity). Required for normal development and maintenance of bone and cartilage (PubMed:26249260). In its inactive state, may sequester DDX3X at the plasma membrane. When activated, the interaction between both proteins is affected and DDX3X relocalizes to the nucleus (PubMed:29899501). FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication, possibly through its action on DDX3X. FUNCTION: [Isoform 6]: Lacks channel activity, due to impaired oligomerization and intracellular retention. FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication, possibly through its action on DDX3X. FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication, possibly through its action on DDX3X. FUNCTION: [Isoform 4]: Lacks channel activity, due to impaired oligomerization and intracellular retention. FUNCTION: [Isoform 5]: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by phorbol esters. Has the same channel activity as isoform 1, and is activated by the same stimuli. SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum. SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum. SUBCELLULAR LOCATION: Cell membrane Apical cell membrane; Multi-pass membrane protein Cell junction, adherens junction Cell projection, cilium Note=Assembly of the putative homotetramer occurs primarily in the endoplasmic reticulum. SUBCELLULAR LOCATION: [Isoform 6]: Endoplasmic reticulum. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane. SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane. SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV4 sub-subfamily."}
+{"protein": "MMGGGLVMDQGMMFPGVHNFVDLLQQNGGDKNLGFGALVPQTSSGEQCVMGEGDLVDPPPESFPDAGEDDSDDDVEDIEELERRMWRDRMKLKRLKELQLSRGKDPAGGVVGDPSKPRQSQEQARRKKMSRAQDGILKYMLKMMEVCRAQGFVYGIIPEKGKPVSGASDNLRGWWKEKVRFDRNGPAAIAKYQADNAVPGFESELASGTGSPHSLQELQDTTLGSLLSALMQHCDPPQRRYPLEKGVPPPWWPTGDEEWWPELGIPKDQGPPPYKKPHDLKKAWKVSVLTAVIKHMSPDIEKIRRLVRQSKCLQDKMTAKEISTWLAVVKQEEELYLKLNPGARPPAPTGGITSAISFNASSSEYDVDVVDDCKGDEAGNQKAVVVADPTAFNLGAAMLNDKFLMPASMKEEATDVEFIQKRSASGAEPELMLNNRVYTCHNVQCPHSDYGYGFLDRNARNSHQYTCKYNDPLQQSTENKPSPPAIFPATYNTPNQALNNLDFGLPMDGQRSITELMNMYDNNFVANKNLSNDNATIMERPNAVNPRIQIEEGFFGQGSGIGGSNGGVFEDVNGMMQQPQQTTPAQQQFFIRDDTPFGNQMGDINGASEFRFGSGFNMSGAVEYPGAMQGQQKNDGASEFEELE", "text": "FUNCTION: Transcription factor acting as a positive regulator in the ethylene response pathway (PubMed:19798512). Involved in wound signaling by binding specifically to the DNA sequence 5'-ATGTACCT-3' found in the promoter of some wound-inducible genes (PubMed:19798512). Binds directly to the DNA sequence 5'-TGTTACAAATACC-3' in the promoter of the GA20OX2 gene to activate its expression at the transcriptional level during ethylene signaling (PubMed:30002253). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EIN3 family."}
+{"protein": "MSTQPTKTSSTKLRIFKWLFIISTLVAIAIPITRLLMHLYGKIDEKMYARIFMSYRVNSADSFMINGRYKAIKAKAYPTSEERNKFNSIAQEGDKAVLLKYPYPEHFSLEPEWHYTLCDDVFYNLWKIRVNVCEYYKNNKQEDIAGLVTPPKEAKVDRFFRQDPKISDDDYKKLFTGTDENGKGWSSAAVQFIDILLNLINKPEECKLKDGKLNEKFQKDLESLVSQLGYSTEDMKNIANEIPNFFIQFGKAFPTVIHSTVYSRFYYFFLFLTINGNFDFSEVEKTDGMKIEEFNKQTMKVMASVFAQIFAKVYEESYNYEIKDAGFMDKVRAYFSVSDNIDNVKDQTKNINTVKEVLIKNKELLSK", "text": "FUNCTION: Involved in adherence of spores to the host cell surface and in infection efficiency. SUBCELLULAR LOCATION: Cytoplasm Spore wall Spore polar tube Note=Localized to the cytoplasm of sporonts, to the cytoplasm and surface coat of sporoblasts and to the spore wall and polar tube of mature spores."}
+{"protein": "MEQRLAEFRAARKRAGLAAQPPAASQGAQTPGEKAEAAATLKAAPGWLKRFLVWKPRPASARAQPGLVQEAAQPQGSTSETPWNTAIPLPSCWDQSFLTNITFLKVLLWLVLLGLFVELEFGLAYFVLSLFYWMYVGTRGPEEKKEGEKSAYSVFNPGCEAIQGTLTAEQLERELQLRPLAGR", "text": "SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass membrane protein."}
+{"protein": "MHRALLNASRRVATVRSMASTVEGDAFRLSEYSSKYLGHRKAAFTEKLEIVNADDTPALPIYRVTNAVGDVIDKSQDPNFDEQTSLKMYKTMTQLNIMDRILYDSQRQGRISFYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYGNADDLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNNRIAVVYFGDGAASEGDAHAAFNFAATLKCPIIFFCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRVALTNRPVLIEAMTYRLGHHSTSDDSTAYRSSDEVQTWGDKDHPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFAAAEKRKKAHYHDLFEDVYDELPLRLRRQRDELDAHVAEYKEHYPMLETLQSKP", "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). Required for the production of the monomethyl branched-chain fatty acids (mmBCFAs) isopentadecanoate (C15iso) and isoheptadecanoate (C17iso) (PubMed:15340492). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the BCKDHA family."}
+{"protein": "MNVPLTHLQRLEAESIHIFREVAAAFTKPVMLYSVGKDSSVLMHLAMKAFYPAKPPFPFLHVDTTWKFREMIAFRDQMAQKRGFDLLVHFNEDGVRDNINPFDHGSNTHTHVMKTVALRQALDKYGFDAAFGGARRDEEKSRAKERIFSFRNAQHVWDPKNQRPEMWKIFNTRIASGESIRVFPLSNWTELDIWQYILQENIPIVPLYFAKQRPVVERDGMLILRDDERMKLRPGETVENRLVRFRTLGCYPLTGAIESDADTLEAIVGEMLTARTSERQGRLIDRDEAGSMEKKKREGYF", "text": "FUNCTION: Proposed to provide activated sulfate for transfer to nod factor. SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily."}
+{"protein": "MAENGKNCDQRRIAMSKDQHNGSLTDPSSVHEKKRRDREERQNIVLWRQPLITLQYFSLETLVVLKEWTSKLWHRQSIVVSFLLLLAALVATYYVEGAHQQYVQRIEKQFLLYAYWIGLGILSSVGLGTGLHTFLLYLGPHIASVTLAAYECNSVNFPEPPYPDQIICPEEEGAEGAISLWSIISKVRIEACMWGIGTAIGELPPYFMARAARLSGAEPDDEEYQEFEEMLEHAEAAQDFASRAKLAVQKLVQKVGFFGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIVTFSKHIVEQMVTFIGAVPGIGPSLQKPFQEYLEAQRQKLHHRSEAGTPQGENWLSWMFEKLVVAMVCYFVLSIINSMAQNYAKRIQQRLNSEEKTK", "text": "FUNCTION: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes (By similarity). Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine (By similarity). Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by ATG2 (ATG2A or ATG2B) to mediate autophagosome assembly (PubMed:17940279, PubMed:28890335). Regulates ATP2A2 activity to control ER-isolation membrane contacts for autophagosome formation (By similarity). In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required (By similarity). Modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity). Plays an essential role in formation of cell junctions (PubMed:31526472). Upon stress such as bacterial and viral infection, promotes formation of cytoplasmic vacuoles followed by cell death (By similarity). Involved in the cytoplasmic vacuolization of acinar cells during the early stage of acute pancreatitis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Vacuole membrane; Multi- pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the VMP1 family."}
+{"protein": "MHRDAWLPRPAFSLTGLSLFFSLVPPGRSMEVTVPATLNVLNGSDARLPCTFNSCYTVNHKQFSLNWTYQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQVLXEEPPERDSTVAVIVGASVGGFLAVVILVLMVVKCVRRKKEQKLSTDDLKTEEEGKTDGEGNPDDGAK", "text": "FUNCTION: Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-2 causes an increase in the plasma membrane surface area and in its folding into microvilli. Interacts with TNR may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN2B (TC 8.A.17) family."}
+{"protein": "METVLEQLAGLESFPSPYFDEDDFFTDHSSRDALDADDFLEDDVDFLAGQIQDYYRDSRVLHTDDDYCDAGNFSFSSSSSGGFPYECGDGGCDLSPGMKGGSLVMKRRRRLRSDAEMQQLRQAANVRERRRMQSINDAFEGLRSHIPTLPYEKRLSKVDTLRLAIGYINFLSEMVQSDLPLRNPNSDSGNQPKKVIICHRGTRSPSPSDPDYGLPPLAGHSLSWTDEKQLRDQNVVRTAKVWTPEDPRKLNKSPFSNIENEPPLTLCLDM", "text": "FUNCTION: Transcription factor implicated in the cell fate determination in various organs. Binds to the E-box consensus sequence 5'-CANNTG-3'. Acts together with pdx1 to induce the pancreatic lineage within the endoderm. Plays a central role in directing the differentiation of retinal progenitors towards horizontal and amacrine fates. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MASATLTAWIKMPSFLKKILKLRGRRQEDESRSRMLSDSSMLSCRVNQLTSEGTEAGSTTPSTLPKDQALLIEPKVRAKEKSQHRRPKIIDQVRRVESLGEQASQRQKHMLETLINKIYTGPLGEELVQTLYLRIWAMEETPESLKILQMREDIRDQVLKMKTERWLRTLIRGEKTKLKDFQKRYEEVHPYLMKEKVEQVIMEEAWSLAAHIVQE", "text": "FUNCTION: The different isoforms prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. They inhibit IFN-alpha/beta induced tyrosine phosphorylation of STAT1 and STAT2. Blocking the IFN- alpha/beta pathway requires binding to STAT1 in the cytoplasm. They inhibit IFN-gamma induced serine phosphorylation of STAT1. Block the IFN-gamma pathway by binding to and stabilizing the parallel form of the STAT1 dimer, further inducing high-molecular-weight complex (HMWC) formation and inhibition of transcription by IFN-gamma. May also have a role in preventing the cell to enter apoptosis. Modulate regulation of viral transcription and replication. Overexpression inhibits the viral RNA polymerase. The absence of all C', C, Y1 and Y2 proteins leads to viral delayed growth. Plays an important role in virion particles release. Modulates virion shape. SUBCELLULAR LOCATION: [Isoform C' protein]: Host cytoplasm Note=Protein C' seems to localize around the Golgi. SUBCELLULAR LOCATION: [Isoform C protein]: Host cytoplasm Virion. Note=The C protein is found in virion at a ratio of approximately 40 molecules per virion, presumably associated with the nucleocapsid. SIMILARITY: Belongs to the respirovirus protein C family."}
+{"protein": "MEAFHTHSGIGVPLRRSNVDTDQIIPAVFLKRVTRTGFEDGLFAGWRSDPAFVLNLSPFDRGSVLVAGPDFGTGSSREHAVWALMDYGFRVVISSRFGDIFRGNAGKAGLLAAEVAQDDVELLWKLIEQSPGLEITANLQDRIITAATVVLPFKIDDHSAWRLLEGLDDIALTLRKLDEIEAFEGACAYWKPRTLPAP", "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": "MDPVNFIKTYAPRGSIIFINYTMSLTSHLNPSIEKHVGIYYGTLLSEHLVVESTYRKGVQIVPLDSFFEGYLSAKVYMLENIQVMKIAADTSLTLLGIPYGFGHNRMYCFKLVAECYKNAGINTSSKRILGKDIFLSQNFTDDNRWIKIYDSNNLTFWQIDYLKG", "text": "FUNCTION: Contributes to virulence in host but not to replication in cell culture. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Localized to the interior of virions, primarily between the membrane and core. SIMILARITY: Belongs to the orthopoxvirus OPG091 family."}
+{"protein": "MRLRTSLGVASACASVASAALKVTEDNSTITLANDRLTSTFAKDKGRVSELFLDGQDLLGPISGNTGVGPYLDCYCIPSGFYTAGSTDPRLEVVQGTDSTGTKYAGVILNDTYTPTGQQFQQYWFLRDGETGLHTFSRLAYYNETTPFLRNLQEFRTLFRPNTELWTHLTSSEAQTAPLPSKEAIANEVVVQDATWRFNNTPNDAYYTQFSEYFTKYTFSNCMGLFKTYWYAASANLQ", "text": "FUNCTION: Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 4 family."}
+{"protein": "MTKLKDQTRAILLATLMVTSVFAGAIAFTGSAAAERGNLDADSESFNKTIQSGDRVFLGEEISTDAGLGASNPLLTGTAGNSEGVSLDLSSPIPQTTENQPLGTYDVDGSGSATTPNVTLLAPRITDSEILTSSGGDVTGSAISSSDAGNLYVNADYNYESAEKVEVTVEDPSGTDITNEVLSGTDTFVDDGSIGSTSSTGGGVGIDMSDQDAGEYTIILEGAEDLDFGDATETMTLTISSQDEIGIELDSESVTQGTDVQYTVTNGIDGNEHVVAMDLSDLQNDATTEQAKEVFRNIGDTSEVGIANSSATNTSGSSTGPTVETADIAYAVVEIDGASAVGGIETQYLDDSEVDLEVYDAGVSATAAVGQDATNDITLTIEEGGTTLSSPTGQYVVGSEVDINGTATSSDSVAIYVRDDGDWQLLEIGGDNEISVDSDDTFEEEDIALSGLSGDGSSILSLTGTYRIGVIDASDADVGGDGSVDDSLTTSEFTSGVSSSNSIRVTDQALTGQFTTINGQVAPVETGTVDINGTASGANSVLVIFVDERGNVNYQEVSVDSDGTYDEDDITVGLTQGRVTAHILSVGRDSAIGDGSLPSGPSNGATLNDLTGYLDTLDQNNNNGEQINELIASETVDETASDDLIVTETFRLAESSTSIDSIYPDAAEAAGINPVATGETMVIAGSTNLKPDDNTISIEVTNEDGTSVALEDTDEWNNDGQWMVEIDTTDFETGTFTVEADDGDNTDTVNVEVVSEREDTTTSSDNATDTTTTTDGPTETTTTAEPTETTEEPTEETTTSSNTPGFGIAVALVALVGAALLALRREN", "text": "FUNCTION: S-layer protein. The S-layer is a paracrystalline mono- layered assembly of proteins which coat the surface of the cell. SUBCELLULAR LOCATION: Secreted, cell wall, S-layer Cell membrane Note=This archaeon is covered by an S-layer with hexagonal symmetry. S-layer glycoproteins are anchored to the plasma membrane as well as being surface-exposed (PubMed:2123862, PubMed:1569073). Bound to the membrane via a covalent lipid-mediated ArtA-dependent anchoring mechanism (PubMed:26712937). SIMILARITY: Belongs to the halobacterial S-layer protein family."}
+{"protein": "MSKSYNQRQRKKLHLAEFQELGFLVNFQFAEGTAIETVDETVDRFINEVIQPNGLAYEGSGYLHWEGLVCLEKIGKCDESHRETVKKWLETNGLQQIEVSELFDIWWEYPTKVE", "text": "SIMILARITY: To E.coli YggL."}
+{"protein": "MAVPKKRTSIYKKRIRKNIWKKKGYWAALKAFSLAKSLSTGNSKSFFVRKISNQTLE", "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 bacterial ribosomal protein bL32 family."}
+{"protein": "MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTASSLANQYHIDSEQARRVLDTTMQMYEQWREQQPKLAHPQLEALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQEQQLMMATLVRYHRKAIKLDDLPRFTLFKKKQFLPLIQLLRLGVLLNNQRQATTTPPTLTLITDDSHWTLRFPHDWFSQNALVLLDLEKEQEYWEGVAGWRLKIEEESTPEIAA", "text": "FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. Has a strong preference for long-chain polyphosphates and has only weak affinity for smaller size polyP of about 15 residues. FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the GppA/Ppx family."}
+{"protein": "MNLNKHSERKFDLITVGRACIDLNAVEYNRPMEETMTFSKYVGGSPANIAIGTAKLGLKVGFIGKISADQHGRFIEKYMRDLSINTDGMVKDTEGRKVGLAFTEIKSPDECSILMYRENVADLYLTPEEISEDYIKEARVLLISGTALAQSPSREAVLKAVSLARKNDVAVAFELDYRPYTWTNTEETAVYYSLVAEQADVIIGTRDEFDMMENQVGGKNEATKAHLFQHQAEIVVIKHGVEGSFAYTKAGETFQAKAYKTKVLKTFGAGDSYASAFLYGLFSGESIETALKYGSAAASIVVSKHSSSDAMPTADEIKALIAQAE", "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": "MAAAGPAAGPTGPEPMPSYAQLVQRGWGSALAAARGCTDCGWGLARRGLAEHAHLAPPELLLLALGALGWTALRSAATARLFRPLAKRCCLQPRDAAKMPESAWKFLFYLGSWSYSAYLLFGTDYPFFHDPPSVFYDWTPGMAVPRDIAAAYLLQGSFYGHSIYATLYMDTWRKDSVVMLLHHVVTLILIVSSYAFRYHNVGILVLFLHDISDVQLEFTKLNIYFKSRGGSYHRLHALAADLGCLSFGFSWFWFRLYWFPLKVLYATSHCSLRTVPDIPFYFFFNALLLLLTLMNLYWFLYIVAFAAKVLTGQVHELKDLREYDTAEAQSLKPSKAEKPLRNGLVKDKRF", "text": "FUNCTION: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward stearoyl-CoA (octadecanoyl-CoA; C18:0-CoA) (PubMed:17977534, PubMed:23530041, PubMed:26887952, PubMed:31916624). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively (PubMed:17977534, PubMed:23530041, PubMed:26887952, PubMed:31916624, PubMed:24782409). Plays a predominant role in skeletal muscle in regulating C18 ceramide and dihydroceramide levels with an impact on whole-body glucose metabolism and insulin sensitivity. Protects from diet-induced obesity by suppressing the uptake of glucose in multiple organs in a FGF21-dependent way (By similarity). Generates C18 ceramides in the brain, playing a critical role in cerebellar development and Purkinje cell function (By similarity). In response to cellular stress mediates mitophagy, a known defense mechanism against cell transformation and aging. Upon mitochondria fission, generates C18 ceramides that anchor lipidated MAP1LC3B/LC3B-II autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria (PubMed:22922758). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
+{"protein": "MSLVSISEGVRAGLVLKRHVVCFTGTSNDQGLKSISDLLSHMDNPAVPSPQSCSIDSLPDTETQNGISCYLVPYSGTAEIDYELQNRFALWLHKSTVPVILVLQDNPLMIPYLRHQFWFACGEDMGQWQDSVVAESIVDSVYMHHSIRRYILDLIVHLRMHRLSKPSQGGGAHSRSLSDMTLLCKWIALTSGSSFITPDMVQTACERYFPWHLQLIESSKEDPSVMYGSQEELVDELINRFDTFAIKMAQEYKNPLFKQLCIVQSVMKDIIPAT", "text": "FUNCTION: May be involved in telomere capping. SIMILARITY: Belongs to the MTC2 family."}
+{"protein": "MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLCGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPSEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHAEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPAQ", "text": "FUNCTION: Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (By similarity). Phosphorylates ceramide but not sphingosine (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (By similarity). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (By similarity). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (By similarity). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein Mitochondrion intermembrane space Note=Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it. SIMILARITY: Belongs to the AGK family."}
+{"protein": "MDVVEVAGSWWAQEREDIIMKYEKGHRAGLPEDKGPKPFRSYNNNVDHLGIVHETELPPLTAREAKQIRREISRKSKWVDMLGDWEKYKSSRKLIDQAYKGMPMNIRGPMWSVLLNTEEMKLKNPGRYQIMKEKGKKSSEHIQRIDRDVSGTLRKHIFFRDRYGTKQRELLHILLAYEEYNPEVGYCRDLSHIAALFLLYLPEEDAFWALVQLLASERHSLQGFHSPNGGTVQGLQDQQEHVVATSQPKTMGHQDKKDLCGQCSPLGCLIRILIDGISLGLTLRLWDVYLVEGEQALMPITRIAFKVQQKRLTKTSRCGPWARFCNRFVDTWARDEDTVLKHLRASMKKLTRKKGDLPPPAKPEQGSSASRPVPASRGGKTLCKGDRQAPPGPPARFPRPIWSASPPRAPRSSTPCPGGAVREDTYPVGTQGVPSPALAQGGPQGSWRFLQWNSMPRLPTDLDVEGPWFRHYDFRQSCWVRAISQEDQLAPCWQAEHPAERVRSAFAAPSTDSDQGTPFRARDEQQCAPTSGPCLCGLHLESSQFPPGF", "text": "FUNCTION: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Note=Associated with lipid rafts."}
+{"protein": "MSKRTFKIVILPGDGIGPEVVAEATRVLEVVSASSSDVEIKLETHDFGGCSIDKHGEPLTAATLEACKLADAILLGAIGGPKWGVNSKVRPEQALLALRKALGLYANIRPANFASDSLLAYSPLKPSVARGVDIIVIRELIGGAYFGERKELGARAQEDAAWDTMIYSVPEVQRITRSRRQVASPDPPLPVHSIDKANVLASSRLWRKVATETIQNEFPQLKLDHHLVDSASMLIVANPKKLNGVILTENLFGDILSDESSVIPGSLGLLPSASLAARPLWPNTAHRRSSPRRVYEPIHGSAPDIAGQGIANPIGTILSAAMLCGTRSVWRSPAKAIEAAVEGARRQGDRREGLRTADLGGSSKTKDIGHKVVEILKATL", "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."}
+{"protein": "MTKIENCKSCLPTENEVEEEALSGVTFLGRVFKVARCERPVFTYMSIILFLVSYIYSVSRDMKDAIIIERLDPASIPYLKVLVVLPVNICIVFSIQKILINTSVSKVFSIMCVMFGIYFCLYGTVLMSFRHIFELNEFLIRDWFADDKMVFMGLQWTIALALPVNSWTSSLMYLSAEIWGTVVFQFLFFALSNEIYTQKQSLRFIPLFLVFGNVALIVSGFSMKFIKYVSEQGSYEFTLFFRKLVFVLMGICSFVIYLIHRYFEDNIAHKPLFVTSEASYKQKTKSKIGFMEAMQTMASSRLVLAISFVVIAYSVSVNMVEASFKTCMSQYALQKGAQADFHVMGVQSDIQLAVGALSIILLLSSFPALIRDKGFLYVAFVPPIFCIFGMASVFGMAALNNSARGNRTLLGFVSIGENLWLEQLLGAIIVTGFKILKYSAVDVSKEALSMRINPAYRARFKGIYDGVCGKLGKAIGSGITNMQNVFYNSSDVRKAAISSLTIVTVITACWGFAVRYLAGKYDKSTHSNTDIDIDLINVDPMEKDADDL", "text": "FUNCTION: ATP transporter involved in the uptake of ATP from the host cell cytoplasm. Provides the microsporidian cell with host ATP in exchange for ADP. This is an obligate exchange system. This energy acquiring activity is an important component of microsporidian parasitism (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ADP/ATP translocase tlc family."}
+{"protein": "MLPNNQWQIPINNGLTHQENMAAHAAVMKLRVHDLQSIISQLSLRKPRPQKSEHQKVVVESLRDPHHARQIYQMASNFPNGNYEMQKRPATTSQVRSHPYVLPSRSGASNHLVNHHYQQQQQQQPQPHNLLHQQMMASHHSHLQQQHHPSTVRWLTPELLEEQLRGSMRYGAPAAAAATNAPLHSSFPNHGRSSQQSLQKSEKSNRPKKMYADNFEPLPLPFYDVISVLLKPVELHSSDSPTLKQTKQLQFPFLLTAEHISKISYRADVTPLPRYELQLRFFNLTEPVQGPQKDDFPLNCYARVDDSVVQLPNVIPTNKTNAEPKRPSRPVNITSNMNRYKKEHTVAVEWLADKRVWAAGVYFVHRVNSDILFKRLNQNVSRHRSLEVTKQEVIKKLSGGEDDIAMDRLNISLLDPLCKTRMTTPSRCQDCTHLQCFDLLSYLMMNEKKPTWQCPVCSSNCPYDRLIVDDYFLDMLAKVDKNTTEVELKEDGSYDVIKEEAFCISDDDDDDVVPATVNGTASCSSTNGNGLANEAAKKKPADDDIITLSDDDDEELNRGIMNSLNDSFSPGRHTASAELAAQKTPPQQKKKTKDDDIEIITLDDTPPRPVAASANLPMRQMSQQNQMPVGSSPSGMASTQMGMNEGASKTIRDALNKIGEQSANSSTQSSPLVQLHHTTHPLNFAQSSYMNPSSGSQTPTSQYGYSPMINQAPHFQMQNGLIGRNNQMVHMQQHHLQQQQQQQQSPQIMSPSFYAQQQMSNGGAFAYYPPQYPQQQYRQN", "text": "FUNCTION: Functions as an E3-type smo-1 ligase (PubMed:15654100, PubMed:16701625, PubMed:16549501, PubMed:25475837). Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment (PubMed:25475837). In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation (PubMed:15654100). In embryos, plays a role in determining telomere localization in the nucleus (PubMed:24297748). SIMILARITY: Belongs to the PIAS family."}
+{"protein": "MSKFSLLDHELIPHHEIMDEDDLKTVLTHYNVEREQLPKLKVTDPIALEIGAEPGDVVKVIRKSQTAGEALYYRYVIG", "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": "MNHKSKKRIKEAKRSARPELKDSQDWCRHNYCEVFSLNPSTVRDNVERADDAHLSIEEFIDRYEKPYKPVVIVNATADWPAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIDYMEGTRDDSPLYIFDSSYGEHPKRKKLLEDYEVPKYFRDDLFQFAGEKRRPPYRWFVMGPARSGTGIHIDPLGTSAWNSLVHGHKRWCLFPTNTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQLPSWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTAIAVTQNFASCSNFPVVWHKTVRGRPKLSRKWYRILKQERPELAALADTVDLQEATGIASDSSSDSSSSSSSSSSESCSEDDLSSGAEMMSHRKKKRKICSVMENGDSTTQDDCVSKERSSSR", "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. SIMILARITY: Belongs to the JMJD6 family."}
+{"protein": "MDTEYEQVNKPWNELYKETTLGNKLTVNVGMEDQEVPLLPSNFLTKVRVGLSGGYITMRRIRIKIIPLVSRKAGVSGKLYLRDISDTTGRKLHCTESLDLGQEIRLTMQHLDFSVSTRSDVPIVFGFEELVSPFLEGRELFSISVRWQFGLSKNCYSLPQSKWKVMYQEDALKVLKPSKKKASKTDSSV", "text": "FUNCTION: Cell-to-cell movement. Displays RNA-binding activity (By similarity). SUBCELLULAR LOCATION: Host membrane. SIMILARITY: Belongs to the tombusvirus/aureusvirus movement protein p22 family."}
+{"protein": "NLIDFKNMIKCTTKRSVLDFADYGCYCGSGGSGTPVDDLDRCCKVHDDCYGEAEKVHGCWPKWTLYSYDCSNGQLTCKDNNTKCKDFVCNCDRTAAICFAKAPYDDNNFMINNPRCQ", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that shows strong myotoxicity and induces edema in mice. Shows no cytotoxicity in vitro. Has a strong anticoagulant effect in vitro. 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": "MGASIDDYSLVHKNILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSSALVPADEGLFLSMLLKLMNAKRTIEIGVYTGYSLLTTALALPEDGKITAIDVNKSYYEIGLPFIQKAGVEHKINFIESEALPVLDQMLEEMKEEDLYDYAFVDADKSNYANYHERLVKLVRIGGAILYDNTLWYGSVAYPEYPGLHPEEEVARLSFRNLNTFLAADPRVEISQVSIGDGVTICRRLY", "text": "FUNCTION: 4'-O-methyltransferase converting norbelladine to 4'-O- methylnorbelladine. 4'-O-methylnorbelladine is a precursor to all Amaryllidaceae alkaloids such as galanthamine, lycorine and haemanthamine, and including haemanthamine- and crinamine-type alkaloids, promising anticancer agents. Can use norbelladine, N- methylnorbelladine and dopamine as substrate, but not caffeic acid, vanillin, 3,4-dihydroxybenzaldehyde and tyramine. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family."}
+{"protein": "MVPLVAVVSGPRAQLFACLLRLGTQQVGPLQLHTGASHAARNHYEVLVLGGGSGGITMAARMKRKVGAENVAIVEPSERHFYQPIWTLVGAGAKQLSSSGRPTASVIPSGVEWIKARVTELNPDKNCIHTDDDEKISYRYLIIALGIQLDYEKIKGLPEGFAHPKIGSNYSVKTVEKTWKALQDFKEGNAIFTFPNTPVKCAGAPQKIMYLSEAYFRKTGKRSKANIIFNTSLGAIFGVKKYADALQEIIQERNLTVNYKKNLIEVRADKQEAVFENLDKPGETQVISYEMLHVTPPMSPPDVLKTSPVADAAGWVDVDKETLQHRRYPNVFGIGDCTNLPTSKTAAAVAAQSGILDRTISVIMKNQTPTKKYDGYTSCPLVTGYNRVILAEFDYKAEPLETFPFDQSKERLSMYLMKADLMPFLYWNMMLRGYWGGPAFLRKLFHLGMS", "text": "FUNCTION: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone-10, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro) (PubMed:22852582). It is believed the in vivo electron acceptor is glutathione (PubMed:25225291, PubMed:29715001). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the SQRD family."}
+{"protein": "MKPTRPNTDIPAWLQTTTTTPTPAIKAKFWQRNQRHLRQLLSRLAQPAPVTATSHWRVAPQFKLIQLLLLVILIALSNNLILLWSLALLVGCQLLWLPPRQLRRFMGSWLISVGMAMLFVLPSYWLAGPTTLLFFGLKTSLMLANAQYYRLTTPFQDLLAGLKALHCPDLLIMTLAIAITYLRMLGQHLLLTMEALELRTVAPTAHPYRLIGALFGNLYLKSYTYALELYAAMEARGFNGHYVRSTGRRTHWRDYLALSPAIIVWILFIFWRH", "text": "FUNCTION: Probable transmembrane component of the energy-coupling factor (ECF) transporter complex LarMNQO involved in nickel import. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiQ family."}
+{"protein": "GWKDWLKTAGGWLKKKGPSILKAVVGAATQ", "text": "FUNCTION: Has activity against some Gram-positive bacteria and S.cerevisiae. Has a non-hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ponericin-G family."}
+{"protein": "MDEYEDSQSPAPSYQYPKETLRKRQNSVQNSGGSVSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNISIPNVLRWLIMEKNHSGVPGSKEELDKELPVLKPYFVSDPEDAGVREAGLRVTWLGHATLMVEMDELIFLTDPMFSSRASPSQYMGPKRFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWSRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHADPEDAVRIHIDLQTKRSVAIHWGTFALANEHYLEPPVKLNEALERYGLSCEDFFILKHGESRYLNTDDRAFEET", "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:14634025, PubMed:15760304, PubMed:17655883, PubMed:21801852). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (PubMed:21801852, PubMed:16605240). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (PubMed:31685899). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose (PubMed:25757720). Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (PubMed:14634025). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein Early endosome membrane; Peripheral membrane protein Nucleus envelope Nucleus, nucleoplasm Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. SIMILARITY: Belongs to the NAPE-PLD family."}
+{"protein": "MSSIEIESSDVIRLIEQFLKESNLHRTLAILQEETNVSLNTVDSIDGFCNEITSGNWDNVLKTVQSLKLPAKKLIDLYEHVIIELVELRELATARLVARQTDPMILLKQIDPDRFARLESLINRPYFDGQEVYGDVSKEKRRSVIAQTLSSEVHVVAPSRLLSLLGQSLKWQLHQGLLPPGTAIDLFRGKAAQKEQIEERYPTMMARSIKFSTKSYPESAVFSPDANYLVSGSKDGFIEVWNYMNGKLRKDLKYQAQDNLMMMDAAVRCISFSRDSEMLATGSIDGKIKVWKVETGDCLRRFDRAHTKGVCAVRFSKDNSHILSGGNDHVVRVHGMKSGKCLKEMRGHSSYITDVRYSDEGNHIISCSTDGSIRVWHGKSGECLSTFRVGSEDYPILNVIPIPKSDPPQMIVCNRSNTLYVVNISGQVVRTMTSGKREKGDFINCILSPKGEWAYAIAEDGVMYCFMVLSGTLETTLPVTERLPIGLAHHPHQNLIASYAEDGLLKLWTD", "text": "FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome (By similarity). Selectively regulates alternative splicing of unc-52 exon 17 (PubMed:11438655, PubMed:15254247). Thus, smu-1 mutants selectively suppress the effects of unc-52 nonsense mutations in exon 17 by promoting the accumulation of unc-52 isoforms that lack exon 17 and enhance the effects of unc-52 mutations that affect the exon 16 splice donor site (PubMed:11438655, PubMed:15254247). In contrast, smu-1 mutants do not suppress unc-52 nonsense mutations in exon 18 (PubMed:11438655). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat SMU1 family."}
+{"protein": "MPVFTKEALERLPIQLGNFFKKFPPENPNAWTTNPNRQNPFLATRNPQNGLVINPYYSNRRQAEIYKEARLQNLDNLLPQQMSWQKDSTRHILKGLLNPKGKISERKRDEILENRRLKLSESLKKTSKFKNERQKASKIAKPSPF", "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 mL59 family."}
+{"protein": "MAIVKVTDSNFDENIQSGVKLVDFWATWCGPCKMIAPVLEELAGDYDGKADILKLDVDENPSTAAKFEVMSIPTLIVFKDGEPVDKVVGFQPKENLAEVLDKHL", "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": "MALTKAEMSEYLFDKLGLSKRDAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENASPKEE", "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. FUNCTION: IHF also plays a crucial role in the lysogenic life cycle of bacteriophage lambda, as it is required not only in the recombination reaction, which inserts lambda DNA into the E.coli chromosome, but also for the synthesis of int and cI repressor, two phage proteins necessary for DNA insertion and repression, respectively. The synthesis of int and cI proteins is regulated indirectly by IHF via translational control of the lambda cII protein (By similarity). 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: IHF also plays a crucial role in the lysogenic life cycle of bacteriophage lambda, as it is required not only in the recombination reaction, which inserts lambda DNA into the E.coli chromosome, but also for the synthesis of int and cI repressor, two phage proteins necessary for DNA insertion and repression, respectively. The synthesis of int and cI proteins is regulated indirectly by IHF via translational control of the lambda cII protein. SIMILARITY: Belongs to the bacterial histone-like protein family. SIMILARITY: Belongs to the bacterial histone-like protein family."}
+{"protein": "MNSTQGTVGSDPVILATAGYDHTVRFWQAHSGICTRTVQHQDSQVNSLEVTPDRSMIAAAGYQHIRMYDLNSNNPNPVINYDGVSKNITSVGFHEDGRWMYTGGEDCMARIWDLRSRNLQCQRIFQVNAPINCVFLHPNQAELIVGDQSGAIHIWDLKTDQNEQLIPETDVSINSVHIDPDASYMAAVNSSGNCFVWNLTGGLGEDLTQLIPKTKIPAHKRCALKCKFSPDSTLLATCSADQTCKIWRTSNFSLMTELSIKSNNPGETSRGWMWDCAFSGDSQYIVTASSDNLARLWCVETGEIKREYSGHQKAVVCLAFNDSVLG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the WD repeat LST8 family."}
+{"protein": "MSGSVSGCGSGGCSIVWFRRDLRVEDNPALAAAVRAGPVIALFVWAPEEEGHYHPGRVSRWWLKNSLAQLDSSLRSLGTCLITKRSTDSVASLLDVVKSTGASQIFFNHLYDPLSLVRDHRAKDVLTAQGIAVRSFNADLLYEPWEVTDELGRPFSMFAAFWERCLSMPYDPESPLLPPKKIISGDVSKCVADPLVFEDDSEKGSNALLARAWSPGWSNGDKALTTFINGPLLEYSKNRRKADSATTSFLSPHLHFGEVSVRKVFHLVRIKQVAWANEGNEAGEESVNLFLKSIGLREYSRYISFNHPYSHERPLLGHLKFFPWAVDENYFKAWRQGRTGYPLVDAGMRELWATGWLHDRIRVVVSSFFVKVLQLPWRWGMKYFWDTLLDADLESDALGWQYITGTLPDSREFDRIDNPQFEGYKFDPNGEYVRRWLPELSRLPTDWIHHPWNAPESVLQAAGIELGSNYPLPIVGLDEAKARLHEALSQMWQLEAASRAAIENGSEEGLGDSAEVEEAPIEFPRDITMEETEPTRLNPNRRYEDQMVPSITSSLIRPEEDEESSLNLRNSVGDSRAEVPRNMVNTNQAQQRRAEPASNQVTAMIPEFNIRIVAESTEDSTAESSSSGRRERSGGIVPEWSPGYSEQFPSEENGIGGGSTTSSYLQNHHEILNWRRLSQTG", "text": "FUNCTION: Implicated in promoting R protein-mediated resistance to Pseudomonas syringae pv. tomato (Pst.) DC3000 under continuous light conditions. Promotes systemic acquired resistance (SAR) and PR gene expression triggered by P. syringae. FUNCTION: Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation, and regulates other light responses, including circadian rhythms, tropic growth, stomata opening, guard cell development, root development, bacterial and viral pathogen responses, abiotic stress responses, cell cycles, programmed cell death, apical dominance, fruit and ovule development, seed dormancy, and magnetoreception. Photoexcited cryptochromes interact with signaling partner proteins to alter gene expression at both transcriptional and post-translational levels and, consequently, regulate the corresponding metabolic and developmental programs (PubMed:21841916). Blue-light absorbing flavoprotein that activates reversible flavin photoreduction via an electron transport chain comprising a tryptophan triad (W-324, W-377 and W-400), accompanied by a large conformational change upon photoexcitation, or via an alternative electron transport that involves small metabolites, including NADPH, NADH, and ATP. The half-life of the activated signaling state is about 5 minutes (PubMed:26313597, PubMed:25157750, PubMed:23398192, PubMed:21875594, PubMed:21467031). Also involved in the detection of blue/green ratio in light (shade under leaf canopies) and subsequent adaptations on plant growth and development (PubMed:20668058). In darkness, the dark reoxidation of flavin occurs and leads to inactivated state (PubMed:21467031, PubMed:23398192). Perceives low blue light (LBL) and responds by directly contacting two bHLH transcription factors, PIF4 and PIF5, at chromatin on E-box variant 5'-CA[CT]GTG-3' to promote their activity and stimulate specific gene expression to adapt global physiology (e.g. hypocotyl elongation and hyponastic growth in low blue light) (PubMed:26724867, PubMed:19558423). When activated by high-intensity blue light, catalyzes direct enzymatic conversion of molecular oxygen O(2) to reactive oxygen species (ROS) and hydrogen peroxide H(2)O(2) in vitro. ROS accumulation upon activation by blue light leads to cell death in protoplasts (PubMed:25728686). Seems essential for blue-light- triggered and singlet oxygen-mediated programmed cell death (PCD) (PubMed:17075038). Required for the induction of nuclear genes encoding photoprotective components by GATA24 and GATA28 in extreme light intensities that exceed the electron utilization capacity of the chloroplast (PubMed:22786870). Involved in shortening the circadian clock period, especially at 27 degrees Celsius, in blue light (BL) and required to maintain clock genes expression rhythm (PubMed:23511208). Mediates blue light-induced gene expression and hypocotyl elongation through the inhibition of COP1-mediated degradation of the transcription factors BIT1 and HY5 and via the activation of anion channels at the plasma membrane, probably via auxin signaling (PubMed:21511872, PubMed:21511871, PubMed:16093319, PubMed:18397371, PubMed:12324610, PubMed:8528277, PubMed:9765547, PubMed:25721730). Required for the hypocotyl hook formation in darkness (PubMed:22855128). Involved in blue light-dependent stomatal opening, CHS gene expression, transpiration, inhibition of stem growth and increase of root growth, probably by regulating abscisic acid (ABA) (PubMed:22147516, PubMed:16093319, PubMed:16703358, PubMed:7756321, PubMed:9565033). Prevents lateral roots growth by inhibiting auxin transport (PubMed:20133010). Necessary for shade avoidance syndrome (SAS), characterized by leaf hyponasty and reduced lamina/petiole ratio, when exposed to blue light attenuation (PubMed:21457375). Together with phototropins, involved in phototropism regulation by various blue light fluence; blue light attenuates phototropism in high fluence rates (100 umol.m-2.s-1) but enhances phototropism in low fluence rates (<1.0 umol.m-2.s-1) (PubMed:12857830). Required for blue/UV-A wavelengths-mediated inhibition of explants shoot regeneration in vitro (e.g. new shoot apical meristems regeneration from excised cotyledons) (PubMed:22681544). Modulates anthocyanin accumulation in a PHYA-dependent manner in far-red-light. Acts as a PHYA/PHYB-dependent modulator of chlorophyll accumulation in red light. Contributes to most blue light deetiolation responses (PubMed:9733523, PubMed:8528277). May act as a chemical magnetoreceptor, via magnetically sensitive kinetics and quantum yields of photo-induced flavin / tryptophan radical pairs (PubMed:22421133). The effect of near-null magnetic field on flowering is altered by changes of blue light cycle and intensity in a CRY1/CRY2-dependent manner (PubMed:26095447). Involved in the strigolactone signaling that regulates hypocotyl growth in response to blue light (PubMed:24126495). Modulates temperature-dependent growth and physiology maintenance, especially at warm ambient temperatures, via HFR1-dependent activity (PubMed:21265897). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, PML body Note=The nuclear pool is involved in hypocotyl and petiole growth inhibition and anthocyanin production, while the cytoplasmic pool is involved in root growth and cotyledon expansion (PubMed:18003924). Present in nuclear bodies (NBs) (PubMed:21511872, PubMed:21765176). SIMILARITY: Belongs to the DNA photolyase class-1 family."}
+{"protein": "MKFGKELSSQMVQEWQQAYVNYDYLKTLLKEIIKLKEKTNPPPPPHHAVPGEGISRKMTLYRAFSGLVQTPGKKRQSSRQSNYSSEIDIEEGKAPILVSKSTHGLETTFLMTAEEGGEYELVFFRRLDDEFNRVEKFYKEKVEEVMKDAIMLNKQMDALIAFRVKVENPVGWGWEERTVEMTRLASDIATSTAAIAASTPARTRTMNPRAQAHMEAIQEGSFSRENEDEDHGSVRGATGDVKTSSLNTMRGARPAPIEVLDHIKINNTKATPRSTIKGVLNSSSQNEIIFNRQNLNEVEEKLKFAFVEFYQKLRLLKSYSFLNVLAFSKILKKYDKITSRNASKSYMKMVDNSYLGSSDELMKLIQRVESTFIKHFANGHRRKGMNILRPQMKREKHRVTFSTGFSAGCIFSLIVALVAIIRTRKTMPEAEHNTYMNTMFPLYSLFGFIVLHITMYAIDIYYWKRYRVNYAFIFGCKQGTELGYRQVLFLGFTIGTFALLCVLGNLDMEVNPKTKNFKPLTELLPLFLLVALFVVLIMPFHFLYRSTRFFFLTCLLHCLAAPLYKVTLPDFFLGDQLTSQVQALRSINFYICYYGWGDFKKRQNTCEASEIYIYSLYIVASLPYLSRLLQCMRRMIEERSLDQGYNGVKYLLTVIAVSLRTAYGYEVKNTKNPTSHLKVLAGSSSILAAVFCTYWDFVHDWGLLNKTSKNRWLRDKLLIPQKKVYFIAMILNVVLRFAWLQTILNFEFEFLHKQTTLAVVASLEIMRRGMWNFFRVENEHLNNVGKFRAFKSVPLPFNYDEDDEKDD", "text": "FUNCTION: May transport inorganic phosphate (Pi). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family."}
+{"protein": "MVEENSRVLIVLPYTPPSATLQRIIGQTIPFLRECQSQLDIVIVPEFKTSFQLDSALGKMYSITRDVLLGYGMINSGINIIFNNIHFVESNLQWKVVLLPQESTFETWKLELGQGQYHSIEHYALHDNIMEEIEGPKDANKFHVTALGGTFDHIHDGHKILLSVSTFITSQRLICGITCDELLQNKKYKELIEPYDTRCRHVHQFIKLLKPDLSVELVPLRDVCGPTGKVPEIECLVVSRETVSGAETVNKTRIEKGMSPLAVHVVNVLGGREEDGWSEKLSSTEIRRLLKSSASPTCTPQNPCV", "text": "FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity). Plays a role in the physiological regulation of the intracellular CoA concentration. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the eukaryotic CoaD family."}
+{"protein": "QGGLPRPGPEIPP", "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": "MGSLSSRVLRQPRPALAQQAQGARAGGSARRPDTGDDAAGHGFCYCAGSHKRKRSSGSFCYCHPDSETDEDEEEGDEQQRLLNTPRRKKLKSTSKYIYQTLFLNGENSDIKICALGEEWSLHKIYLCQSGYFSSMFSGSWKESSMNIIELEIPDQNIDVEALQVAFGSLYRDDVLIKPSRVVAILAAACLLQLDGLIQQCGETMKETVNVKTVCGYYTSAGTYGLDSVKKKCLEWLLNNLMTHQNVELFKELSINVMKQLIGSSNLFVMQVEMDIYTALKKWMFLQLVPSWNGSLKQLLTETDVWFSKQRKDFEGMAFLETEQGKPFVSVFRHLRLQYIISDLASARIIEQDAVVPSEWLSSVYKQQWFAMLRAEQDSEVGPQEINKEELEGNSMRCGRKLAKDGEYCWRWTGFNFGFDLLVTYTNRYIIFKRNTLNQPCSGSVSLQPRRSIAFRLRLASFDSSGKLICSRTTGYQILTLEKDQEQVVMNLDSRLLIFPLYICCNFLYISPEKKN", "text": "FUNCTION: Possible function in spermatogenesis. Enhances the degradation of MDM2 and increases the amount of p53 probably by modulating the nucleocytoplasmic transport (By similarity). SUBCELLULAR LOCATION: Nucleus matrix."}
+{"protein": "MRYDVQELLLHQSAEDPFARFANGMAYHPFLQLTQRPTDFSVSSLLTAGSNNNNSGNTNSGNNNSNSNNNTNSNTNNTNNLVAVSPTGGGAQLSPQSNHSSSNTTTTSNTNNSSSNNNNNNSTHNNNNNHTNNNNNNNNNTSQKQGHHLSTTEEPPSPAGTPPPTIVGLPPIPPPNNNSSSSSSNNSASAAAHPSHHPTAAHHSPSTGAAAPPAGPTGLPPPTPPHHLQQQQQQQQHPAPPPPPYFPAAALAALAGSPAGPHPGLYPGGGLRFPPHHPGAHPHAHHLGSAYTTAEDVVLASAVAHQLHPAMRPLRALQPEDDGVVDDPKVTLEGKDLWEKFHKLGTEMVITKSGRQMFPQMKFRVSGLDAKAKYILLLDIVAADDYRYKFHNSRWMVAGKADPEMPKRMYIHPDSPTTGEQWMQKVVSFHKLKLTNNISDKHGFVSTTILNSMHKYQPRFHLVRANDILKLPYSTFRTYVFKETEFIAVTAYQNEKITQLKIDNNPFAKGFRDTGAGKREKKQALMSNRGSDSDKLNPTHVSSSRAPLHLGHAGRPPHLHPHAALLDNQQDDDDKLLDVVGPPQSPLLPLSHSLQQMHAHQHSAALAAWFNHLAGAGAGASEHAAAAAANASAEDALRRRLQADADVERDGSDSSCSESVGGSTGGAFRPTSTGSPKEAVGAAAAAAAAGLNPGGGSYPSPNISVGPPIHPSPHLLPYLYPHGLYPPPHLGLLHNPAAAAAMSPAGLNPGLLFNAQLALAAQHPALFGHAYAAAGHTPVSPLQGLKSHRFSPYSLPGSLGSAFDAVTPGSNANRSGDPPGGGGGGLGGGVVENGPRSLSSSPRPRPASHSPPTRPISMSPTTPPSLMKQPRGGGAGAGVAQSQHSPSELKSMEKMVNGLEVQHNGSAAAAAAALQLAEEAAQHHHHTQAHHQQQQHQSHHQQQHHQQPAQPHPHHQTHLHSHHGATTGGTDQ", "text": "FUNCTION: Essential protein that may function as a transcription regulator. Vital for pupal development. Required for proper development of the optic lobes and wings, and abdominal pigmentation. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MFFYKIIYFIGFPYIVLRLIVSIILPIASLYFIYCNFIAPKLREKPESSYKNKVVIITGASSGIGAELAKKYARLGCKVTIVARRLDQLEKVKSSFLKDYSRVNDDDILVIKGDLTLIDDCKNMVEKVIEKWSKIDICVWNAGSGSLIEFSKLQGDISIYRDNMELNYFSLVNCTHLVYKYLEQSHGSIIVISSLAGKFGTALRTSYSSSKHAVMGFFNSLRNETKNIQITIVCPGFILTEFHDNLKTLDGKQVERNKGNFMTASQCANEIILAERQGIRELIQTAKGRVGNYLQAIFPELIEFLTHKFASSSVKK", "text": "FUNCTION: Putative oxidoreductase. SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
+{"protein": "MANEIPTKGILKSEALKQYIMETSAYPREHELLKELRKATVQKYGNLSEMEVPVDEGHFLSMLVKIMNAKNTIEIGVFTGYSLLTTALALPEDGRITAIDIDKEAYEVGLEFIKKAGVDHKINFIHSDGLKALDQLVNDKCEFDFAFADADKSSYVNFHERLLKLVKVGGIIAFDNTLWFGFVAEDEDGVPEHMREYRAALIEFNKKLALDPRVEVSQISIGDGITLCRRLV", "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 (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily."}
+{"protein": "MIELDRLDLGGGRRLVITSEPDAAVPQVRDADGHWRRAGPGDGVAEAMLDALNQNPGTTKHGNFTLLSWASQTARGERPITVDQTNESVIVGDAAVVKWATHLQEGPHPAPARIKALRGNGFRGMPMPWGLVTWQTADHPETLVVTVDEYLPDAVDGWTWAVALVTDAAQDRAAVPALVDAVTAVGCVVAELHAAQADTARPATAADARSWREAALETVETAATLGTSVSGELLRARREDVEAVVGTLGDLAGIPVLAGHGDLHVGQVLRAGGRYVVTDFDGNPVLPAEARVKPVPAALDVAGMAQSLAHVAIVACKYTELAPAALADVDRLARTTFVGAYTDRLETLGHRSVYDPAPLRALRLQQVLREIIYAARHLPRWMYVPDAALPALLDEGTST", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-glucosamine (GlcN) to D-glucosamine 6-phosphate. May be involved in the phosphorylation of acquired extracellular GlcN derived from the hydrolysis of chitosan, i.e., in the incorporation of exogenous GlcN into the bacterial GlcNAc metabolism. Is unable to phosphorylate maltose. SIMILARITY: Belongs to the actinobacterial glucosamine kinase family."}
+{"protein": "MSLSDEQVQAEMHKMVSFIKQEALEKAKEIHTLSEEEFQVEKAKIVREQCDAIDQTYDMKLKRASMAQKIAKSNVLNKSRLEILNSKQKVIDDIFSRVEKKLDGIEQKKDAYTKFMADLIVQAMELLGEPVGIVYSRQRDAEIVKAAIPKATEVLKSKNGSIDYELDAETDDFLNDSVLGGVVLVGLGGKIRVDNTLRARLEIVKEEALPEIRRLLFGENPNRKFDN", "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": "MEELSMANTMFALNLLKQIEQSNSTQNIFISPWSISSTLAIVFLGAQANTEEQMAKVLNFDKIGSYDLTPGNPENFHGCDFAQHIQRDNYPVAILQAQARDKIHSAFSSLSSTINTPRLGDYLLESANKLFGEKSARFKEEYIQRCKKYYSTEPEAVDFLECANEARKKINSWVKTQTKGEIPNLLPEGSVDEDTKMVLVNTIYFKGRWKTPFQKRLNGLYPFRVNLNESKPVQMMYLREKLNIGYIKDLKTQILELPYIGNISMFLLLPDEIEDSSTGLEMLEREINFDNFNKWISKETLDEDDVLVYIPKFKLAQNYELKPILQRMGMEDAFNKGKADFSGMSESNDLFLSEVFHQATVDVNEEGTVAAGGTGAVMTGRTGHGGPQFVADHPFLFFIMNNITRTILFVGRFSSP", "text": "FUNCTION: Inhibits urokinase-type plasminogen activator. SUBCELLULAR LOCATION: Cytoplasm Secreted, extracellular space. SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily."}
+{"protein": "MTTKQICFADRCFNFAFGEHVLESVESYIPRDEFDQYIMISDSGVPDSIVHYAAEYFGKLAPVHILRFQGGEEYKTLSTVTNLQERAIALGANRRTAIVAVGGGLTGNVAGVAAGMMFRGIALIHVPTTFLAASDSVLSIKQAVNLTSGKNLVGFYYPPRFVFADTRILSESPPRQVKAGMCELVKNMLILENDNKEFTEDDLNSANVYSPKQLETFINFCISAKMSVLSEDIYEKKKGLIFEYGHTIGHAIELAEQGGITHGEAIAVGMIYAAKIANRMNLMPEHDVSAHYWLLNKIGALQDIPLKSDPDSIFHYLIHDNKRGYIKLDEDNLGMILLSGVGKPAMYNQTLLTPVRKTLIKEVIREGL", "text": "FUNCTION: Catalyzes the intramolecular carbocycle formation from D- glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI). SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI synthase family."}
+{"protein": "MAAEARVSRWYFGGLASCGAACCTHPLDLLKVHLQTQQEVKLRMTGMALRVVRTDGILALYSGLSASLCRQMTYSLTRFAIYETVRDRVAKGSQGPLPFHEKVLLGSVSGLAGGFVGTPADLVNVRMQNDVKLPQGQRRNYAHALDGLYRVAREEGLRRLFSGATMASSRGALVTVGQLSCYDQAKQLVLSTGYLSDNIFTHFVASFIAGGCATFLCQPLDVLKTRLMNSKGEYQGVFHCAVETAKLGPLAFYKGLVPAGIRLIPHTVLTFVFLEQLRKNFGIKVPS", "text": "FUNCTION: Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane (PubMed:29211846). Plays an important role in gluconeogenesis, fatty acid metabolism, urea synthesis, and sulfur metabolism, particularly in liver, by supplying the substrates for the different metabolic processes. Regulates fatty acid release from adipocytes, and contributes to systemic insulin sensitivity (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
+{"protein": "MAFTRIHSFLASAGNTSMYKRVWRFWYPLMTHKLGTDEIMFINWAYEEDPPMALPLEASDEPNRAHINLYHRTATQVNLSGKRILEVSCGHGGGASYLTRALHPASYTGLDLNPAGIKLCQKRHQLPGLEFVRGDAENLPFDNESFDVVINIEASHCYPHFPRFLAEVVRVLRPGGHLAYADLRPSNKVGEWEVDFANSRLQQLSQREINAEVLRGIASNSQKSRDLVDRHLPAFLRFAGREFIGVQGTQLSRYLEGGELSYRMYSFAKD", "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": "MSAQHLHSCKFYRLPLEIIPLICRFLSVQDIQSFIRVFPSFQTILDSSNDLFWKKKNYELRIRRNRLLRGSYAAGVSSSAMNGFVNGTQISSTPAEREYYSKSDEIKNICGLPPGPMKVEQIGHAIDHLVSETHTVDHLGSSIKASFFHIDDVPLEWISSICMQVQSFFSPAAREAISSLKSRTTTSNLLLSLFVGILFEDDLWYFFNTLYMLSSTSAIEFAYFLDSIFTVVRTDYEHYRDPLSQTLITSCTRIHNIVAVIESPYDEPNTKGLTSEQKMIVECQLNPGEVLKVKAFAGTGKTKALLEFAKSRPKDKILYVAFNKAAKEDAELRFPFNVKCSTMHGLAYGAILAQADLPQAKLERQLSNSTIASLLSLQVAFPKANRKNNPGTPSASLVASHIMFTLNRFMHSTDWQLGFRHISKRSLEVTKLSKEKLLAYTKKLWSLIVNFEYTHAPLIPDAYMKLLHLYEFPNIFSKYDYILFDEAQDFTPCMVDLIYRQKHARIVIVGDAHQCIYGFRGANACAFNENLYPSTKQLCLTKSFRFGNSVAKYANFLLSLKGENVKLKGVQNDHAYWSSASNPNNVSGAFRFFPHTIIFRTNKELILQSIRLSVSLPKEIPIAILGSMRKKAFQLLRSGSELAHGQRPSHPKLKDFSSWGEFEVHVKNSAEEDAELALVYDMADELFSESFLSRLDNCEKRLMDSKDDGDNGIILATAHQSKGLEWDNVQLGNDFRPKFDSVSFSRIGSSRYLQEEINILYVALTRAKKRLILNDTITKLYALECGLVRFAGGILTEDQLQPGKVALFVDWQIDKFSFFYETPAEGYNLLVEANEKSVWDIFFGVLSGAWQNYIANTSERLKRSMLFIENQLFAVHDQ", "text": "FUNCTION: Involved in ATP-dependent DNA-unwinding in a 3' to 5' direction, and ATP-ase activities stimulated by the single-stranded DNA-binding protein ssb1. Essential for viability and normal growth of stationary phase cells and in the absence of either srs2 or rqh1 DNA helicase (PubMed:16135799, PubMed:9228070). Involved in DNA recombination repair of strand breaks and stalled or collapsed replication forks, on the rhp51-dependent pathway: promotes rhp51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination (PubMed:16135800, PubMed:19546232). Ubiquitination and DNA helicase activities are essential for controlling rhp51-dependent recombination in the absence of rad22. Plays a role in the processing of toxic recombination intermediates. Promotes proper chromosome segregation (PubMed:16135799, PubMed:16135800, PubMed:9228070, PubMed:19546232). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Becomes localized at discrete nuclear foci together with rhp51, in response to DNA strand breakage. SIMILARITY: Belongs to the helicase family. UvrD subfamily."}
+{"protein": "MANDITAHWKDLLRKRLASLKPDGRTEEEKKAEESELFSKYYTEWKGGEKGEDDSFKHIPRFYYRLPAEDEVLMQKLREESRAVFLQRKSRELLDNEELQNLWFLLDKHQVPPTTGDEAMISYESFLKVGEKAGTKCKLFFTARVYAKLLHNDPYGRISIMQFFNYVMRKVWLHQTRIGLSLYDVAGQGYLRESDLENYILELIPTLPQLDGLEKSFYSFYVCTAVRKFFFFLDPLHTGKIKIQDILACSFLDDLLELRDEELSKESQESNWFSAPSALRVYGQYLNLDKDHNGMLSKEELSRYGTGTLTSVFLDRVYQACLTYDGEMDYKTYLDFVLALENRKEPAALQYIFKLLDMENKGYLNVFALNYFFRAIQEQMKIHGQEPVSFQDVKDEIFDMVKPKDPYKITLQDLVNSGQGDTVSSILIDLNGFWTYENREVLVANDTDSNAADLDDT", "text": "FUNCTION: Possible role in the regulation of cell death. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
+{"protein": "MKRNQKEWESVSKKGLMKPGGTSIVKAAGCMGCWASKSIAMTRVCALPHPAMRAI", "text": "FUNCTION: Produces a 26-residue extracellular sporulation filling factor (SKF) that induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, providing a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation (PubMed:12817086, PubMed:20805502). Can also inhibit growth of other bacteria at high concentrations (PubMed:11851812). Addition of SKF to solid cultures induces killing, but it is much less effective than SDP (AC O34344) (PubMed:20805502). Has a role in protecting the secreted lipase LipA against proteolysis, either by modulating its folding or by acting as a protease inhibitor (PubMed:15812018). SUBCELLULAR LOCATION: Secreted Note=Probably secreted by the ABC transporter SkfEF."}
+{"protein": "MRCAPPGLLLAQLHACIFWSGLWPAGCQSPPAAWRQRIQWENNGQVYSLLSQGAQYQPPRRRQGAEPASSPVLLLRGNGSVPRAAAAAAARPQPEPQPQAQPQPRPRSSRRQPLGRRHWFQAGYRAPSGSARPAPRRRPRGRRSRRRERAERRRAAAPSGLRPGREDVMVGDDPYSPYKYTDDNPYYNYYDTYERPRQGSRYRPGYGTGYFQYGLPDLVPDPYYIQASTYVQRMSMYNLRCAAEENCLASSAYRADVRDYDNRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDASSHRKVAEGHKASFCLEDTSCDYGYYRRYACTAHTQGLSPGCYDTYNADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYSNNIVRCDIRYTGHHAYASGCTISPY", "text": "FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. FUNCTION: In addition to cross linking of extracellular matrix proteins, it may have a direct role in tumor suppression. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the lysyl oxidase family."}
+{"protein": "MNKAIASKILITLGFLFLYRVLAYIPIPGVDLAAIKAFFDSNSNNALGLFNMFSGNAVSRLSIISLGIMPYITSSIIMELLSATFPNLAKMKKERDGMQKYMQIVRYLTILITLIQAVSVSVGLRSISGGANGAIMIDMQVFMIVSAFSMLTGTMLLMWIGEQITQRGVGNGISLIIFAGIVSGIPSAISGTFNLVNTGVINILMLIGIVLIVLATIFAIIYVELAERRIPISYARKVVMQNQNKRIMNYIPIKLNLSGVIPPIFASALLVFPSTILQQATSNKTLQAVADFLSPQGYAYNILMFLLIIFFAYFYSSIVFNSKDIADNLRRNGGYIPGLRPGEGTSSFLNSVASKLTLWGSLYLALISTVPWILVKAMGVPFYFGGTAVLIVVQVAIDTMKKIEAQIYMSKYKTLSAVGF", "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 inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecY/SEC61-alpha family."}
+{"protein": "MAETAVINHKKRKNSPRIVQSNDLTEAAYSLSRDQKRMLYLFVDQIRKSDGTLQEHDGICEIHVAKYAEIFGLTSAEASKDIRQALKSFAGKEVVFYRPEEDAGDEKGYESFPWFIKRAHSPSRGLYSVHINPYLIPFFIGLQNRFTQFRLSETKEITNPYAMRLYESLCQYRKPDGSGIVSLKIDWIIERYQLPQSYQRMPDFRRRFLQVCVNEINSRTPMRLSYIEKKKGRQTTHIVFSFRDITSMTTG", "text": "FUNCTION: Replication initiator in the monomeric form, and autogenous repressor in the dimeric form. SIMILARITY: Belongs to the initiator RepB protein family."}
+{"protein": "MSTAFVDQDKQMANRLNLSPLERSKIEKQYGGATTLAFISNKQNELAQILSRADILKIASYDCAAHALQAVLDCGPMLGKRGFSQSDIVKIAGNIGGAQALQAVLDLESMLGKRGFSRDDIAKMAGNIGGAQTLQAVLDLESAFRERGFSQADIVKIAGNNGGAQALYSVLDVEPTLGKRGFSRADIVKIAGNTGGAQALHTVLDLEPALGKRGFSRIDIVKIAANNGGAQALHAVLDLGPTLRECGFSQATIAKIAGNIGGAQALQMVLDLGPALGKRGFSQATIAKIAGNIGGAQALQTVLDLEPALCERGFSQATIAKMAGNNGGAQALQTVLDLEPALRKRDFRQADIIKIAGNDGGAQALQAVIEHGPTLRQHGFNLADIVKMAGNIGGAQALQAVLDLKPVLDEHGFSQPDIVKMAGNIGGAQALQAVLSLGPALRERGFSQPDIVKIAGNTGGAQALQAVLDLELTLVEHGFSQPDIVRITGNRGGAQALQAVLALELTLRERGFSQPDIVKIAGNSGGAQALQAVLDLELTFRERGFSQADIVKIAGNDGGTQALHAVLDLERMLGERGFSRADIVNVAGNNGGAQALKAVLEHEATLNERGFSRADIVKIAGNGGGAQALKAVLEHEATLDERGFSRADIVRIAGNGGGAQALKAVLEHGPTLNERGFNLTDIVEMAANSGGAQALKAVLEHGPTLRQRGLSLIDIVEIASNGGAQALKAVLKYGPVLMQAGRSNEEIVHVAARRGGAGRIRKMVAPLLERQ", "text": "FUNCTION: Binds to dsDNA in a sequence-specific manner. Also binds a DNA/RNA duplex when the recognized sequence is in the DNA strand. Each tandem core repeat recognizes a single nucleotide in the target DNA via its base-specifying residue (BSR, residue 13 of each repeat); altering this amino acid changes sequence specificity. SIMILARITY: Belongs to the transcription activator-like effector (TALE) family. Bat subfamily."}
+{"protein": "MVTSNVVLVSGEGERFTVDKKIAERSLLLKNYLNDMHDSNLQNNSDSESDSDSETNHKSKDNNNGDDDDEDDDEIVMPVPNVRSSVLQKVIEWAEHHRDSNFPDEDDDDSRKSAPVDSWDREFLKVDQEMLYEIILAANYLNIKPLLDAGCKVVAEMIRGRSPEEIRRTFNIVNDFTPEEEAAIRRENEWAEDR", "text": "FUNCTION: Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory 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 centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins into the kinetochore thus providing cell cycle-regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52. SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the SKP1 family."}
+{"protein": "MMQFQRDLEASLEAVSANAQELLKSLKSRKDVQDLNASLPKDPLDNCDAQTQAARAQLAEAATRILRLSIRPQEYLEHLQNGYQHLTCFRWLVELNILDHLPHSGTISYTDLARKASVPPMQLRSICRMAICNGFLEEPEANQVRHSRISALFARDESYLGWARWMVNYSVPAAYKLSDATRSWGETVAKDQTAFNLGMDVKVPFFDHLRQTPAMKDAFAAYMRNVTSNATWGLQHAVTGFDWASLPRGAKVVDVGGSLGHGSIAIAKEHTHLTFVIQDLPETVAGARKEMAQNDKIEASVKSRITFQEHDFFGPQTVKDADVYFLRMICHDWPDNEAKVILSQIRAALKPGAQIVIMDTILPQPGTTSVLQEQQLRIRDLTMMEVFNAKERELEDWSSLMQSAGLEISRVNQPLNSVMGLLTVRSAGQTALSGTNTLTPELVTAVSASTGSADSRPVLIAGAGIAGLCLAQALKKAGIDFRVFERDSHIDARPQGYRLKFEADAAQSLKNILPDDVYEAFELSNAVTAVGETDFNPFNGNIIHSRTGGGLSGKKGLYATFTVDRKAFRTQLMTGIEDKISFGKEIAYYKTDDSASTVTAEFKDGTHVTGSFLAGTDGLHSVVRKTCVPDHRIVDTGAACIYGKTVMTPEFLARFPEKGLRFMTVVSDIAPMLQSCLIGDSPVTLLLEPIRFSEASRARYPELPADYVYWALIGPKERFGSQEVTSMKNFVSLDQAAEQAAKLSLAVTEEWHPSLRALFELQDTKQASLIRVASTIPDIPSWESHSNVTVLGDSIHPMSPCGGVGANTAIVDADALAKVLVEHGTKPPVNAIAEFEAAMRTRAKRNIWRSEVGSKRMFGQKNLVDCSEFVF", "text": "FUNCTION: Dual O-methyltransferase/FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin (By similarity). 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 (By similarity). 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 (By similarity). The bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (By similarity). 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 (By similarity). 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 (By similarity). 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: In the N-terminal section; belongs to the class I-like SAM- binding methyltransferase superfamily. Cation-independent O- methyltransferase family. COMT subfamily. SIMILARITY: In the C-terminal section; belongs to the paxM FAD- dependent monooxygenase family."}
+{"protein": "MRDYIPKYLNAFLLAFATFAVGFAIFIAKDSNSSSHLYFSTSSSLWTSSFSPAFITVSIFLTVHRFREKRKRNGSNPGSGYWKRDGKVEAELATARVLIREAQLNYSSTTSSPLGDEDYVPHGDIYRNPYAFHRSYLLMEKMFKIYVYEEGDPPIFHYGLCKDIYSMEGLFLNFMENDVLKYRTRDPDKAHVYFLPFSVVMILHHLFDPVVRDKAVLERVIADYVQIISKKYPYWNTSDGFDHFMLSCHDWGHRATWYVKKLFFNSIRVLCNANISEYFNPEKDAPFPEINLLTGDINNLTGGLDPISRTTLAFFAGKSHGKIRPVLLNHWKEKDKDILVYENLPDGLDYTEMMRKSRFCICPSGHEVASPRVPEAIYSGCVPVLISENYVLPFSDVLNWEKFSVSVSVKEIPELKRILMDIPEERYMRLYEGVKKVKRHILVNDPPKRYDVFNMIIHSIWLRRLNVKLL", "text": "FUNCTION: May be involved in cell wall biosynthesis. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 47 family."}
+{"protein": "MNIRMGTKGKRPLRSLTPRDKIHAIQRIHDGESKASVARDIGVPESTLRGWCKNEDKLRFMSRQSATDNLCADALGDKMDGGGGGGGGAGGGGLLGPPEKRQRLDGALPLNFSNKLKFDELAFKRSPLNGLDYSTNKNLADLGYNGLPVDYAAFNGGVKAKVFGADINRPAADPSLNAISPLSSLTHLSGLTGISQSPLAISFNELTTNLNLLAQLNPGLAAMSGLNSFPAGAGNLRTPKPSGQTPLQVQSPRSDSGDRSAQGLSVKNWAKQKPGEGQGSLNLSIKNEGKGGDIKSPSPSIAPSQMGGPMTLSNLAEDPLLYWLKSQQTMLGLNPLYPPTIPMGVTSPPIRSSTPQHMSQLAQTPPIPSAPLTPSSTPSGSLDEKNAAWYNWCKAFGASLHTLNPNAATLAALQANQLQQQVATTAAEGGSMGDPSNILYSHLTKETETPSVRSLSSNEQNPEADEATETDLDGEVEPEASGKPEDLSAAGKVMTPSQSPIAHSSGSRSPEPKAKTKTPETTNSTSECKKILDNMLFKMGGMEATGPLMPEQGSSESEGSFQDTSNPHTNNNDVSASNNNNNNNSNKTDEEEKAKYLDCTADEDIEAIRHGEKFLQWLENCSNPRVTAVQLMQLRFLIAAIKSGNETPMIEKSALPEDSEEHAAEEEGSGRGKSRRRK", "text": "FUNCTION: Probable transcription factor with a role in the retinal determination (RD) network. Regulates ato expression and is required for normal R8 induction and differentiation. Danr appears to repress Dan expression, but Dan is required for Danr expression anterior to the morphogenetic furrow (MF). Dan and Danr lie downstream of so and require dac function for highest levels of expression. Contributes to differentiation of antenna-specific characteristics; effector gene that acts downstream of homothorax (hth), Distal-less (Dll), cut (ct) and spineless (ss) genes to control differentiation of distal antennal structures. SUBCELLULAR LOCATION: Nucleus."}
+{"protein": "MLVDRVENNEKQQQQMASSSDAMSDSSLSDDEIIEHVVHGKEPKSTYELSWVSNAIAWSGALVWPLMLTVPLLLSSMYSPISYRQVFPESWYVYDTLSNCAPKPLGLVLGILAVAVGQVFVWIFFYLFKFGYLGTDPRSIQSKGAREYIFREGLLTHIGQPEGFVLLIGYLAITWMLKLMPQSYYSFEGTIQYKELFMCLVLQDGIQYTMHVLEHIVSPAFYQMSHKPHHRFTNPRLFDAFNGSLMDTFCMIIIPLFVTANLVRHCNVWTYMAFGSSYACWLTLIHSEYVFPWDGIFRKLGLGTPADHHVHHKFFKFNYGHLFMWFDQLGGTYRDPSGFAPRVFRENV", "text": "FUNCTION: Catalyzes the stereospecific epoxidation of squalene at the terminal double bond to form (S)-2,3-epoxysqualene, the first oxygenation step in sterol biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Detected in the outer envelope of chloroplasts, which is termed the chloroplast endoplasmic reticulum and is continuous with the nuclear envelope. SIMILARITY: Belongs to the sterol desaturase family."}
+{"protein": "MWRETKLLLIDDNLDRSRDLAVILNFLGEDQLTCNSEDWREVAAGLSNSREALCVLLGSVESKGGAVELLKQLASWDEYLPILLIGEPAPADWPEELRRRVLASLEMPPSYNKLLDSLHRAQVYREMYDQARERGRSREPNLFRSLVGTSRAIQQVRQMMQQVADTDASVLILGESGTGKEVVARNLHYHSKRREGPFVPVNCGAIPAELLESELFGHEKGAFTGAITSRAGRFELANGGTLFLDEIGDMPLPMQVKLLRVLQERTFERVGSNKTQNVDVRIIAATHKNLEKMIEDGTFREDLYYRLNVFPIEMAPLRERVEDIALLLNELISRMEHEKRGSIRFNSAAIMSLCRHDWPGNVRELANLVERLAIMHPYGVIGVGELPKKFRHVDDEDEQLASSLREELEERAAINAGLPGMDAPAMLPAEGLDLKDYLANLEQGLIQQALDDAGGVVARAAERLRIRRTTLVEKMRKYGMSRRDDDLSDD", "text": "FUNCTION: AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression (PubMed:9287015, PubMed:11673434, PubMed:26362077). In addition to flagella genes, regulates also expression of biofilm-related genes (PubMed:22581773). Functions as a transcriptional repressor in the absence of c-di-GMP and as an activator when c-di-GMP is present (PubMed:22581773)."}
+{"protein": "MSILIDEKTPILVQGITGDKGTFHAKEMIAYGSNVVGGVTPGKGGKTHCGVPVFNTVKEAVEATGATTSITFVAPPFAADAIMEAADAGLKLVCSITDGIPAQDMMRVKRYLRRYPKEKRTMVVGPNCAGIISPGKSMLGIMPGHIYLPGKVGVISRSGTLGYEAAAQMKELGIGISTSVGIGGDPINGSSFLDHLALFEQDPETEAVLMIGEIGGPQEAEASAWIKENFSKPVIGFVAGLTAPKGRRMGHAGAIISATGDSAAEKAEIMRSYGLTVAPDPGSFGSTVADVLARAA", "text": "SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family."}
+{"protein": "MMPLILLPAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVGKLDVQVELSGGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVQIIDGEHRLRGRGWETDGGDLWDVLERLDSEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLTHRGVEGAIVGKALYARRFTLPQALAAVRD", "text": "FUNCTION: Involved in both the histidine and tryptophan biosynthetic pathways. FUNCTION: Involved in both the histidine and tryptophan biosynthetic pathways. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family. SIMILARITY: Belongs to the HisA/HisF family."}
+{"protein": "MVTRRRLHHPEVEQVSKRQKVDKAESKNKKHADVAAERGEQSTEDHEDESQDKKDKKVVGDNRDEDEEVSPNGQEAAEDNDDRKDKDAKEKDTETNDEGTEKSHTDVNDDDDDVDESKEEDAAAAVDITKEKKDEQESDNKTEEKKVQENEEEEEEDENKNDEDVEELGSTEPVDDEKKGLVKFEFDGVEYKFKERASVIEENEGKIEFRVVSNDNTRENMMVLTGLKNIFQKQLPKMPKEYIARLVYDRSHLSMAVIRKPLTVVGGITYKPFNKRQFAEIVFCAISSTEQVRGYGAHLMNHLKDYVRNTSDIRYFLTYADNYAIGYFKKQGFTKDITLDKKVWMGYIKDYEGGTLMQCSMLPRIRYLDAAKILLLQEAALRRKIRTISKSHVVHPGLECFNDIENIKPIDPMSIPGLKEAGWTPEMDELAQRPKRGPHYAAIQNILVELQNHAAAWPFLRPVNKEEVPDYYEFIKEPMDLSTMELKLENNKYEKMEEFIYDARLVCNNCRLYNGENTSYYKYANRLEKFFNNKVKEIPEYSHLID", "text": "FUNCTION: Histone acetyltransferase that acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, with a lower preference histone H4 to form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. In addition to histone acetyltransferase, can use different acyl-CoA substrates, such as (2E)- butenoyl-CoA (crotonyl-CoA) and is able to mediate histone crotonylation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily."}
+{"protein": "MGPGIQPTSARPCSRTKHSRFALLAAALTARRVKQFTKQFRSRRMAEDILKLWQRQYHLPREDSDKRTLRERVHLYRPPRSDLGGIAVAVTVIALWATLFVYGLWFVKLPWALKVGETATSWATIAAVFFSLEFLYTGLFITTHDAMHGTIALRNRRLNDFLGQLAISLYAWFDYSVLHRKHWEHHNHTGEPRVDPDFHRGNPNLAVWFAQFMVSYMTLSQFLKIAVWSNLLLLAGAPLANQLLFMTAAPILSAFRLFYYGTYVPHHPEKGHTGAMPWQVSRTSSASRLQSFLTCYHFDLHWEHHRWPYAPWWELPKCRQIARGAALAPGPLPVPAAAAATAATAAAAAAATGSPAPASRAGSASSASAAASGFGSGHSGSVAAQPLSSLPLLSEGVKGLVEGAMELVAGGSSSGGGGEGGKPGAGEHGLLQRQRQLAPVGVMA", "text": "FUNCTION: Involved in the biosynthesis of ketocarotenoids which are powerful anti-oxidative molecules (PubMed:21398427, PubMed:22526507). Catalyzes the conversion of zeaxanthin to astaxanthin via adonixanthin (PubMed:21398427, PubMed:22526507). Catalyzes the conversion of beta- carotene to canthaxanthin via echinenone (PubMed:21398427, PubMed:22526507)."}
+{"protein": "MQQTIQTTLLIIGGGPGGYVAAIRAGQLGIPTVLVEGQALGGTCLNIGCIPSKALIHVAEQFHQASRFTEPSPLGISVASPRLDIGQSVAWKDGIVDRLTTGVAALLKKHGVKVVHGWAKVLDGKQVEVDGQRIQCEHLLLATGSSSVELPMLPLGGPVISSTEALAPKALPQHLVVVGGGYIGLELGIAYRKLGAQVSVVEARERILPTYDSELTAPVAESLKKLGIALHLGHSVEGYENGCLLANDGKGGQLRLEADRVLVAVGRRPRTKGFNLECLDLKMNGAAIAIDERCQTSMHNVWAIGDVAGEPMLAHRAMAQGEMVAEIIAGKARRFEPAAIAAVCFTDPEVVVVGKTPEQASQQGLDCIVAQFPFAANGRAMSLESKSGFVRVVARRDNHLILGWQAVGVAVSELSTAFAQSLEMGACLEDVAGTIHAHPTLGEAVQEAALRALGHALHI", "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 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
+{"protein": "MVPSRRTWNLGATPSLRGLWRVGRAPEPEPGMARPAPAPASPAARPFPHTGPGRLRTGRGKDTPVCGDEDSSARSAARPALAQCRALSVDWAGPGSPHGLYLTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVRPVTKEDGEGPEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSVELGPGLRRAELGSWSSQEHLEWEPACQTPQPSARAHSAPSSGTSSRPGSIRRKLQPSGKSRPLPV", "text": "FUNCTION: Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance. SUBCELLULAR LOCATION: Cell junction, adherens junction Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasmic vesicle membrane; Peripheral membrane protein Note=Apical cell membrane. On membrane organelles immediately beneath the apical plasma membrane of renal tubular epithelial cells. Localized in the distal tubules and loops of Henle in the kidney, but not in the proximal tubules or the glomeruli, with stronger staining in the apical area of these epithelial cells (By similarity). Localizes along zonula adherens only at mature cell-cell contacts. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family."}
+{"protein": "MKDSAILNQLKVVLPPHIMEIIYFRYNQIDTYLKPYNLPIKTDVLLLALFTLIFIIIISKLFGSSGNKTRSVGGRTSNDKKVKRGVNIAILGLSNAGKTALLLNLTNVDKKISTHTSITTNNGVYITENKKKLPIIDVPGNGKAKASLPKILSNSACIIYVIDGTTFIDNSTQEAQYLYDILTNESVYQKKIPVLVFNNKMDLDSTIDTEQVKNILERELDDLRRTRGATPIVLGQEEDKKDIYLGIEGTPFQFDHLPNDVQFSNGSASPSNGELKEIDDIKNFIQTTTL", "text": "FUNCTION: Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SRP receptor beta subunit family."}
+{"protein": "MSAAPGLLHQELSCPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQAPTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGEAGVALRRELGSLNSYLEQLRQMEKVLEEVADKPQTEFLMKYCLVTSRLQKILAESPPPARLDIQLPIISDDFKFQVWRKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSEQKAPPAGEDPRQFDKAVAVVAHQQLSEGEHYWEVDVGDKPRWALGVIAAEAPRRGRLHAVPSQGLWLLGLREGKILEAHVEAKEPRALRSPERRPTRIGLYLSFGDGVLSFYDASDADALVPLFAFHERLPRPVYPFFDVCWHDKGKNAQPLLLVGPEGAEA", "text": "FUNCTION: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)- dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). SUBCELLULAR LOCATION: Cell membrane, sarcolemma Cytoplasmic vesicle membrane Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. SIMILARITY: Belongs to the TRIM/RBCC family."}
+{"protein": "MNPIVEFCISNLAKGGDYVYNQLENDPGIDVLEYGCLQNCGICSSGLYALVNGDIVEGESPDDLLQKIYAHIEETWIF", "text": "SIMILARITY: Belongs to the UPF0349 family."}
+{"protein": "MSLAFNPAATAFSGNGARSRRENFPVKHVTVRGFPMITNKSSFAVKCNLTTTDLMGKIAEKFKGEDSNFPAAAAVQPAADMPSNLCIIDTLQRLGVDRYFRSEIDTILEDTYRLWQRKERAIFSDTAIHAMAFRLLRVKGYEVSSEELAPYADQEHVDLQTIEVATVIELYRAAQERTGEDESSLKKLHAWTTTFLKQKLLTNSIPDKKLHKLVEYYLKNXHGILDRMGVRQNLDLYDISYYRTSKAANRFSNLCSEDFLAFARQDFNICQAQHQKELQQLQRWYADCKLDTLKYGRDVVRVANFLTSAIIGDPELSDVRIVFAQHIVLVTRIDDFFDHRGSREESYKILELIKEWKEKPAAEYGSEEVEILFTAVYNTVNELAERAHVEQGRSVKDFLIKLWVQILSIFKRELDTWSDDTALTLDDYLSASWVSIGCRICILMSMQFIGIKLSDEMLLSEECIDLCRHVSMVDRLLNDVQTFEKERKENTGNSVTLLLAANKDDSSFTEEEAIRIAKEMAECNRRQLMQIVYKTGTIFPRQCKDMFLKVCRIGCYLYASGDEFTSPQQMMEDMKSLVYEPLTIHPLVANNVRGK", "text": "FUNCTION: Involved in tanshinone biosynthesis in hairy roots (PubMed:19905026, PubMed:21082262). Catalyzes the conversion of copalyl diphosphate (CPP) to miltiradiene (PubMed:19905026, PubMed:21082262). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
+{"protein": "MAPRGRKRKAEAAVVAVAEKREKLANGGEGMEEATVVIEHCTSURVYGRNAAALSQALRLEAPELPVKVNPTKPRRGSFEVTLLRPDGSSAELWTGIKKGPPRKLKFPEPQEVVEELKKYLS", "text": "FUNCTION: May be involved in a redox-related process. SIMILARITY: Belongs to the SelWTH family."}
+{"protein": "MKFVPCLLLVTLSCLGTLGQAPRQKQGSTGEEFHFQTGGRDSCTMRPSSLGQGAGEVWLRVDCRNTDQTYWCEYRGQPSMCQAFAADPKPYWNQALQELRRLHHACQGAPVLRPSVCREAGPQAHMQQVTSSLKGSPEPNQQPEAGTPSLRPKATVKLTEATQLGKDSMEELGKAKPTTRPTAKPTQPGPRPGGNEEAKKKAWEHCWKPFQALCAFLISFFRG", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the fibroblast growth factor-binding protein family."}
+{"protein": "MEPGRSEVEGHQRNALYLLSALCMVFMTLVVAIQPLFLRNVLNIPFETAGAVNANVQVVTEVLDLFIFAYLGYLSDRIGRVRIIVAGFLVAAVGAVIAPLSPWVGGASIGALVVYYVSRVIMSAGSGAVWPQLSALAGDFSDDSNRARLLSNTAFMMAFGVTLVYAVLMQIPGHAGITVTMLLTAAISVAGAWLARKFLVDVAPRTVETSVPWRAVWDLVKAEPRLRLAFASSLFARSDMVFVGLFLMLWFIYFADLVKVGQAEAAARAGMLIGLMGAVVMLSIPVWRSFIERFGRIQAVLLGMMLSALGFIMLGFVVNPFDGFIVFPILLVSAGQAGCFVAPQILTVDHAPKDLLGSVLGAFNVIGCLGIIFFVQIGGFLFDYIGPPAPFIFTGVGNLIISAYALRLVKSEARGVGGGNTPGDDEVA", "text": "FUNCTION: Required for correct biomineralization of the magnetosome; probably transports some form of iron. Partially functionally redundant with MamZ. SUBCELLULAR LOCATION: Magnetosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
+{"protein": "MPSESSVKATAAPPPFPLPPDGGWGWVVVCASFISIGFSYAFPKAVTVFFNDIKDIFKTTSSQIAWISSIMLAVMYAGGPISSVLVNNYGSRPVVIVGGLLCCTGMILASFSSSVIELYLTVGFIGGLGLAFNLQPALTIIGKYFYRKRPLANGFAMAGSPVFLSTLAPFNQFLFNSYGWKGSFLILGAIFLHSCVAGCLMRPVGPSPRAAKSKSKVGSRQDSSTKRLSKVSTAEKINRFLDFGLFTHRGFLIYLSGNVVLFLGMFAPIIFLAPYAKDKGVDDYNSAFLLSVMAFTDMFARPSVGLIANTSLIRPRIQYLFSVAIMFTGICHLLCPLAHSYTALVVYVIFFGIGFGSISSLLFECLMDQVGASRFSSAVGLVTIVECCPVLFGPPLAGKLLDITGQYKYLYIASGIVVLSSGIYLLICNAINYRLLEKERKREKARRKKSASQASKEMEALSRSKQDDVTVKVSNTHNPPSDRDKESSI", "text": "FUNCTION: Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L- lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate (PubMed:10417314, PubMed:20695846). Dimerization is functionally required and both subunits work cooperatively in transporting substrate (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Cytoplasm Note=Requires the ancillary protein, EMB for plasma membrane localization (PubMed:15917240, PubMed:20695846). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (By similarity). SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
+{"protein": "MVPLTFLRTKASRSLPIMLAALIFAGCGTQAPDQTAAHMQGSAQADSGFYLQQMSQSSNDTKTNWQLLAIRALLNEGKTQQAVDLYNQLPQELNNTQRGEQSLLAAELKIAQKEYPAAKKLLADIDTKALENNQQARYWQAVIAAEQGRPSLPLLRALIAQEPLLSGADKQKNIDTTWQALSSMTPEQSQALVINADENVLQGWLDLQQMWFNNRSDPKMLKAGITDWQTRYPQNPGAKMLPTQLVNVQNFQPASVSKIALLLPLNGQAAVFGRTIQQGFEAAKNGTTAVAGNAVPAQAAQAANVNDVISPSAVETSDLTSAQAPAQGTMQNPVTAPTTPPATTQAPAETAAPAEAQTPVVPQAAPATDAATAQPQTTTPDQQPAAQPQAVAATTANPGAELKIYDTSSQPLDQVLAQVQKDGASIVVGPLLKNNVEELMKSNTSLNVLALNQPEQVQNRANICYFALSPEDEARDAARHIHEQGKQAPLLLTPRSALGDRVATAFAQEWQQLGGNIVLQQKFGSTSELRAGVNGGSGIALTGSPVSASLPQQQGVTIGGLTIPAPPTDAQISGGGKVDAAYIVATPEEIAFIKPMIAMRNGSQSGVTLYASSRSAQGTAGPDFRLEMDGLQYSEIPMLAGSNPALMQQALSSVRNDYSLARLYAMGVDAWALANHFTQMRQVPGFELNGNTGDLTATQDCVINRKLSWLKYQQGQIVPAS", "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": "MWALRGCRSGSRWGQGAALLLLLLGVPPRGLALPPLRYSHAGICPNDMNPNLWVDAQSTCKRECETDQECETYEKCCPNVCGTKSCVAARYMDVKGKKGPVGMPKEATCDHFMCLQQGSECDIWDGQPVCKCRDRCEKEPSFTCASDGLTYYNRCYMDAEACSKGITLAVVTCRYHFTWPNTSPSPPETTVHPTTAPPETPGLDATAPALLNHPAHQSVTVGETVSFLCDVVGRPRPEITWEKQLEDRENVVMRPNHVRGNVVVTNIAQLVIYNAQPQDAGIYTCTARNAAGVLRADFPLSVVSGGQASATAESSPNGTALPAAECLKPPDSDDCGEEQTRWYFDAQANNCLTFTFGHCHRNRNHFETYEACMLACMSGSLAMCSLPALQGPCKAYVPRWAYNSQTGQCQSFVYGGCEGNGNNFESREDCEESCPFPRGNQRCRACKPRQKLVTSFCRSDFVILGRISELTEEPDSGRALVTVDEVLKDEKMGLKFLGQEPLEVTLLHMDWTCPCPNVTVGEAPLIIMGEVDGGMAVLRPDSFVGASSTRRARKLREVMHKKTCDVLKDFPGLQ", "text": "FUNCTION: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease- inhibitor activity. Inhibits the biological activity of mature myostatin, but not activin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the WFIKKN family."}
+{"protein": "MRVLVWIAGLAPLAVAVPSSSYRVAVAARADNTSASVAPSQNVSGAAPPELVVYTLPCEDGNSTARTAEIRLKQATLLYGPSLLGNASYFPGGPLGDAISLRDQTVWEGAAVVQSLRAFTDAAKVAANIKQNGGLNSLDDFKVLYQDGWKGSVPQGIARGQSENYTSDLLFSMERLSVNPYILKRLHPTEDALPFQVDRATVKQLTKTSLKALHAAGRLFVADHSYQRNYTRLANRYSAACTALFYLDPRSNQFLPLAIKTNVGADLTYTPLDTDNNNWLLAKIMFNNNDLFHGQIFHVAYPHAIAEIVHLAALRTMSARHPVLALMERLMYQAYAVRPLGERVLFNKGGLFEQNFAYPQDMVYKFVGDSYPTTGRWRAGYLDTDVRARGLVDADYGPELPHFPFYEDGSRLVEVIRRFVRSFVDATYHESDEMVAKDAELQAWVAEANGPAGVEDFEPGPLDTRERLVEVLTHMAWLTGCAHHVLNQGEPVTASGVLPMHPTALYAPVPTSKANTTADLLGYLPSAQKSVDQVTLLARFNRPDVVPTNQTLRYMFAAPQLLLGNGEAYRRANQRFVRAMGRISDEVKARRFDDRGLSQGMPFIWQALDPGNIPFYLSV", "text": "FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate product 11S-HPODE from linoleic acid is then transformed into 9S-HPODE and 13R-HPODE as the final products. The intermediate product 11R-HPOTrE from alpha-linolenic acid is transformed into 9S-HPOTrE and 13R-HPOTrE as the final products. 9S- HPOTrE is further oxidized by the enzyme to 9S,16S-DiHPOTrE as the end product. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the lipoxygenase family. Manganese lipoxygenase subfamily."}